Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 175 (16 Oct 2019)
Sequence version 2 (11 Jan 2001)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Acetyl-CoA carboxylase

Gene

cut6

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Carries out three functions: biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

By phosphorylation.By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: malonyl-CoA biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes malonyl-CoA from acetyl-CoA.
Proteins known to be involved in this subpathway in this organism are:
  1. Acetyl-CoA carboxylase (cut6)
This subpathway is part of the pathway malonyl-CoA biosynthesis, which is itself part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes malonyl-CoA from acetyl-CoA, the pathway malonyl-CoA biosynthesis and in Lipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi375Manganese 1By similarity1
Metal bindingi389Manganese 1By similarity1
Metal bindingi389Manganese 2By similarity1
Metal bindingi391Manganese 2By similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei393By similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei1772Coenzyme ABy similarity1
Binding sitei2074Coenzyme ABy similarity1
Binding sitei2076Coenzyme ABy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi266 – 271ATPPROSITE-ProRule annotation6

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionLigase, Multifunctional enzyme
Biological processFatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism
LigandATP-binding, Biotin, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-SPO-163765 ChREBP activates metabolic gene expression
R-SPO-196780 Biotin transport and metabolism
R-SPO-200425 Import of palmitoyl-CoA into the mitochondrial matrix
R-SPO-75105 Fatty acyl-CoA biosynthesis

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00655;UER00711

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Acetyl-CoA carboxylase (EC:6.4.1.2)
Short name:
ACC
Alternative name(s):
Cell untimely torn protein 6
Including the following 1 domains:
Biotin carboxylase (EC:6.3.4.14)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:cut6
ORF Names:SPAC56E4.04c
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri284812 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002485 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome I

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
FungiDB:SPAC56E4.04c

Schizosaccharomyces pombe database

More...
PomBasei
SPAC56E4.04c cut6

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001467691 – 2280Acetyl-CoA carboxylaseAdd BLAST2280

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei745N6-biotinyllysinePROSITE-ProRule annotationBy similarity1
Modified residuei1179Phosphoserine1 Publication1
Modified residuei1181Phosphoserine1 Publication1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P78820

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P78820

PRoteomics IDEntifications database

More...
PRIDEi
P78820

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P78820

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts with sad1.

1 Publication

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
279766, 7 interactors

Protein interaction database and analysis system

More...
IntActi
P78820, 1 interactor

STRING: functional protein association networks

More...
STRINGi
4896.SPAC56E4.04c.1

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P78820

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini68 – 577Biotin carboxylationAdd BLAST510
Domaini226 – 418ATP-graspPROSITE-ProRule annotationAdd BLAST193
Domaini704 – 778Biotinyl-bindingPROSITE-ProRule annotationAdd BLAST75
Domaini1524 – 1863CoA carboxyltransferase N-terminalPROSITE-ProRule annotationAdd BLAST340
Domaini1867 – 2181CoA carboxyltransferase C-terminalPROSITE-ProRule annotationAdd BLAST315

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1524 – 2181CarboxyltransferasePROSITE-ProRule annotationAdd BLAST658

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000214115

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P78820

KEGG Orthology (KO)

More...
KOi
K11262

Identification of Orthologs from Complete Genome Data

More...
OMAi
LPYGEWN

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P78820

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.30.1490.20, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR034733 AcCoA_carboxyl
IPR013537 AcCoA_COase_cen
IPR011761 ATP-grasp
IPR013815 ATP_grasp_subdomain_1
IPR005481 BC-like_N
IPR001882 Biotin_BS
IPR011764 Biotin_carboxylation_dom
IPR005482 Biotin_COase_C
IPR000089 Biotin_lipoyl
IPR005479 CbamoylP_synth_lsu-like_ATP-bd
IPR029045 ClpP/crotonase-like_dom_sf
IPR011763 COA_CT_C
IPR011762 COA_CT_N
IPR016185 PreATP-grasp_dom_sf
IPR011054 Rudment_hybrid_motif
IPR011053 Single_hybrid_motif

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF08326 ACC_central, 1 hit
PF02785 Biotin_carb_C, 1 hit
PF00289 Biotin_carb_N, 1 hit
PF00364 Biotin_lipoyl, 1 hit
PF01039 Carboxyl_trans, 1 hit
PF02786 CPSase_L_D2, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00878 Biotin_carb_C, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51230 SSF51230, 1 hit
SSF51246 SSF51246, 1 hit
SSF52096 SSF52096, 2 hits
SSF52440 SSF52440, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50975 ATP_GRASP, 1 hit
PS50979 BC, 1 hit
PS00188 BIOTIN, 1 hit
PS50968 BIOTINYL_LIPOYL, 1 hit
PS50989 COA_CT_CTER, 1 hit
PS50980 COA_CT_NTER, 1 hit
PS00866 CPSASE_1, 1 hit
PS00867 CPSASE_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

P78820-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MRQSVTSSSS CSKLYAIKAT ISLPRLFYRR LRTMAPRVAS HFLGGNSLDK
60 70 80 90 100
APAGKVKDYI ASHGGHTVIT SILIANNGIA AVKEIRSIRK WAYETFNNER
110 120 130 140 150
AIKFTVMATP DDLKVNADYI RMADQYVEVP GGSNNNNYAN VELIVDIAER
160 170 180 190 200
MNVHAVWAGW GHASENPKLP EMLSASSKKI VFIGPPGSAM RSLGDKISST
210 220 230 240 250
IVAQSARVPC MSWSGNELDQ VRIDEETNIV TVDDDVYQKA CIRSAEEGIA
260 270 280 290 300
VAEKIGYPVM IKASEGGGGK GIRQVTSTEK FAQAFQQVLD ELPGSPVFVM
310 320 330 340 350
KLAGQARHLE VQILADQYGN NISLFGRDCS VQRRHQKIIE EAPVTIAPAA
360 370 380 390 400
TFHEMERAAV RLGELVGYAS AGTIEYLYEP ENDRFYFLEL NPRLQVEHPT
410 420 430 440 450
TEMVSGVNLP AAQLQVAMGL PLSRIPHIRE LYGLPRDGDS EIDFFFQNPE
460 470 480 490 500
SFKVQKVPTP KGHCVACRIT SEDPGEGFKP SSGMIKDLNF RSSSNVWGYF
510 520 530 540 550
SVGTAGGIHE FADSQFGHIF SFAESRESSR KSMVVALKEL SIRGDFRTTV
560 570 580 590 600
EYLVRLLETK EFSENEFTTG WLDRLIAQKV TSARPDKMLA VVCGALVRAH
610 620 630 640 650
ATADTQYRAF KSYLERGQVP SREFLKNVYD IEFIYDNTRY RFTASRSSPG
660 670 680 690 700
SYHLFLNGSR CTAGVRSLTD GGLLVLLNGH SYTVYYRDEV TGTRISIDNL
710 720 730 740 750
SCMLEQENDP TQLRTPSPGK LVRFLVETGE HIKAGEAYAE VEVMKMIMPL
760 770 780 790 800
VATEDGVVQL IKQPGASLDA GDILGILTLD DPSRVTHALP FDGQLPNWGE
810 820 830 840 850
PQIAGNKPCQ RYHALLCILL DILKGYDNQI ILNSTYNEFV EVLRNHELPY
860 870 880 890 900
SEWSAHYSAL VNRISPVLDK LFVSIIEKAR SRKAEFPAKQ LEVAIQTYCD
910 920 930 940 950
GQNLATTQQL KVQIAPLLKI ISDYKDGLKV HEYNVIKGLL EEYYNVEKLF
960 970 980 990 1000
SGINKREEDV ILRLRDENKD DVDKVIALAL SHSRIGSKNN LLITILDLMK
1010 1020 1030 1040 1050
SEPSTFVSLY FNDILRKLTD LDSRVTSKVS LKARELLITC AMPSLNERFS
1060 1070 1080 1090 1100
QMEHILKSSV VESHYGDAKF SHRTPSLDIL KELIDSKYTV FDVLPAFFCH
1110 1120 1130 1140 1150
TDPWVSLAAL EVYVRRAYRA YSVLEINYHT EAGTPYVLTW RFQLHSSGAP
1160 1170 1180 1190 1200
GLGANSTNGS NFPASTTPSY ENSNRRLQSV SDLSWYVNKT DSEPFRFGTM
1210 1220 1230 1240 1250
IAAETFDELE NNLALAIDRL PLSRNYFNAG LTLDGNSSSA NDNTQELTNV
1260 1270 1280 1290 1300
VNVALTSTGD LDDSAIVSKL NQILSDFRDD LLEHNVRRVT IVGGRINKSA
1310 1320 1330 1340 1350
YPSYYTYRVS AEQKDGNLVH YNEDERIRHI EPALAFQLEL GRLSNFNIEP
1360 1370 1380 1390 1400
VFTDNHNIHV YRATAKNMDT DKRFFTRALV RPGRLRDEIP TAEYLISETH
1410 1420 1430 1440 1450
RLINDILDAL EVIGHEQTDL NHIFINFTPA FGLAPKQVEA ALGGFLERFG
1460 1470 1480 1490 1500
RRLWRLRVTA AEIRIICTDP STNTLFPLRV IISNVSGFVV NVEIYAEVKT
1510 1520 1530 1540 1550
ENNSWIFKSI GQPGSMHLRP ISTPYPTKEW LQPRRYKAQL MGTTFVYDFP
1560 1570 1580 1590 1600
ELFRRAFTDS WKKVPNGRSK VTIPQNMFEC KELVADEHGV LQEVNREPGT
1610 1620 1630 1640 1650
NSCGMVAWCI TVKTPEYPNG RKIIVVANDI TFQIGSFGPQ EDEYFYKVTQ
1660 1670 1680 1690 1700
LARQRGIPRI YLAANSGARI GVADEIVPLF NIAWVDPDSP EKGFDYIYLT
1710 1720 1730 1740 1750
PEAYERLQKE NPNILTTEEV VTETGELRHK ITTIIGSSEG LGVECLRGSG
1760 1770 1780 1790 1800
LIAGVTSRAY NDIFTCTLVT CRAVGIGAYL VRLGQRAVQI EGQPIILTGA
1810 1820 1830 1840 1850
PALNKVLGRE VYTSNLQLGG TQVMHRNGIS HLTSQDDFDG ISKIVNWISY
1860 1870 1880 1890 1900
IPDKRNNPVP ISPSSDTWDR DVEFYPSQNG YDPRWLIAGK EDEDSFLYGL
1910 1920 1930 1940 1950
FDKGSFQETL NGWAKTVVVG RARMGGIPTG VIAVETRTIE NTVPADPANP
1960 1970 1980 1990 2000
DSTEQVLMEA GQVWYPNSAF KTAQAINDFN HGEQLPLFIL ANWRGFSGGQ
2010 2020 2030 2040 2050
RDMFNEVLKY GSYIVDALAS YKQPVFVYIP PFSELRGGSW VVVDPTINED
2060 2070 2080 2090 2100
QMEMYADEES RAGVLEPEGM VSIKFRREKL LSLMRRCDHK YASLCNELKR
2110 2120 2130 2140 2150
DDLSADDLST IKVKLMEREQ KLMPIYQQIS IHFADLHDRV GRMVAKKVVR
2160 2170 2180 2190 2200
KPLKWTEARR FFYWRLRRRL NEHYALQKIT QLIPSLTIRE SREYLQKWYE
2210 2220 2230 2240 2250
EWCGKQDWDE SDKSVVCWIE EHNDDLSKRT QELKSTYYSE RLSKLLRSDR
2260 2270 2280
KGMIDSLAQV LTELDENEKK ELAGKLASVN
Length:2,280
Mass (Da):256,843
Last modified:January 11, 2001 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i8262C9A1A5C8E891
GO

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence BAA11916 differs from that shown. Reason: Frameshift.Curated
The sequence BAA11917 differs from that shown. Reason: Frameshift.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti14 – 42LYAIK…VASHF → RFIFIDVLLISQLSISSFSF FILYFINHI in BAA11914 (PubMed:8769419).CuratedAdd BLAST29
Sequence conflicti258P → S in BAA11238 (Ref. 1) Curated1
Sequence conflicti339 – 340IE → L in BAA11238 (Ref. 1) Curated2
Sequence conflicti512A → S in BAA11238 (Ref. 1) Curated1
Sequence conflicti523A → T in BAA11238 (Ref. 1) Curated1
Sequence conflicti636 – 639DNTR → YRIP in BAA11915 (PubMed:8769419).Curated4
Sequence conflicti1017K → N in BAA11917 (PubMed:8769419).Curated1
Sequence conflicti1073R → H in BAA11917 (PubMed:8769419).Curated1
Sequence conflicti1098F → L in BAA11917 (PubMed:8769419).Curated1
Sequence conflicti1105V → Y in BAA11238 (Ref. 1) Curated1
Sequence conflicti1362R → S in BAA11238 (Ref. 1) Curated1
Sequence conflicti1427F → Y in BAA11916 (PubMed:8769419).Curated1
Sequence conflicti1444G → E in BAA11238 (Ref. 1) Curated1
Sequence conflicti1445F → C in BAA11916 (PubMed:8769419).Curated1
Sequence conflicti1449F → L in BAA11916 (PubMed:8769419).Curated1
Sequence conflicti1451R → S in BAA11238 (Ref. 1) Curated1
Sequence conflicti1465I → F in BAA11916 (PubMed:8769419).Curated1
Sequence conflicti1480V → L in BAA11916 (PubMed:8769419).Curated1
Sequence conflicti1485V → L in BAA11916 (PubMed:8769419).Curated1
Sequence conflicti1496A → S in BAA11238 (Ref. 1) Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
D78169 Genomic DNA Translation: BAA11238.1
CU329670 Genomic DNA Translation: CAB16395.1
D83413 Genomic DNA Translation: BAA11914.1
D83414 Genomic DNA Translation: BAA11915.1
D83416 Genomic DNA Translation: BAA11917.1 Frameshift.
D83415 Genomic DNA Translation: BAA11916.1 Frameshift.

Protein sequence database of the Protein Information Resource

More...
PIRi
T38906
T42531

NCBI Reference Sequences

More...
RefSeqi
NP_593271.1, NM_001018668.2

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
SPAC56E4.04c.1; SPAC56E4.04c.1:pep; SPAC56E4.04c

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
2543344

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
spo:SPAC56E4.04c

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D78169 Genomic DNA Translation: BAA11238.1
CU329670 Genomic DNA Translation: CAB16395.1
D83413 Genomic DNA Translation: BAA11914.1
D83414 Genomic DNA Translation: BAA11915.1
D83416 Genomic DNA Translation: BAA11917.1 Frameshift.
D83415 Genomic DNA Translation: BAA11916.1 Frameshift.
PIRiT38906
T42531
RefSeqiNP_593271.1, NM_001018668.2

3D structure databases

SMRiP78820
ModBaseiSearch...

Protein-protein interaction databases

BioGridi279766, 7 interactors
IntActiP78820, 1 interactor
STRINGi4896.SPAC56E4.04c.1

PTM databases

iPTMnetiP78820

Proteomic databases

MaxQBiP78820
PaxDbiP78820
PRIDEiP78820

Genome annotation databases

EnsemblFungiiSPAC56E4.04c.1; SPAC56E4.04c.1:pep; SPAC56E4.04c
GeneIDi2543344
KEGGispo:SPAC56E4.04c

Organism-specific databases

EuPathDBiFungiDB:SPAC56E4.04c
PomBaseiSPAC56E4.04c cut6

Phylogenomic databases

HOGENOMiHOG000214115
InParanoidiP78820
KOiK11262
OMAiLPYGEWN
PhylomeDBiP78820

Enzyme and pathway databases

UniPathwayiUPA00655;UER00711
ReactomeiR-SPO-163765 ChREBP activates metabolic gene expression
R-SPO-196780 Biotin transport and metabolism
R-SPO-200425 Import of palmitoyl-CoA into the mitochondrial matrix
R-SPO-75105 Fatty acyl-CoA biosynthesis

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P78820

Family and domain databases

Gene3Di3.30.1490.20, 1 hit
InterProiView protein in InterPro
IPR034733 AcCoA_carboxyl
IPR013537 AcCoA_COase_cen
IPR011761 ATP-grasp
IPR013815 ATP_grasp_subdomain_1
IPR005481 BC-like_N
IPR001882 Biotin_BS
IPR011764 Biotin_carboxylation_dom
IPR005482 Biotin_COase_C
IPR000089 Biotin_lipoyl
IPR005479 CbamoylP_synth_lsu-like_ATP-bd
IPR029045 ClpP/crotonase-like_dom_sf
IPR011763 COA_CT_C
IPR011762 COA_CT_N
IPR016185 PreATP-grasp_dom_sf
IPR011054 Rudment_hybrid_motif
IPR011053 Single_hybrid_motif
PfamiView protein in Pfam
PF08326 ACC_central, 1 hit
PF02785 Biotin_carb_C, 1 hit
PF00289 Biotin_carb_N, 1 hit
PF00364 Biotin_lipoyl, 1 hit
PF01039 Carboxyl_trans, 1 hit
PF02786 CPSase_L_D2, 1 hit
SMARTiView protein in SMART
SM00878 Biotin_carb_C, 1 hit
SUPFAMiSSF51230 SSF51230, 1 hit
SSF51246 SSF51246, 1 hit
SSF52096 SSF52096, 2 hits
SSF52440 SSF52440, 1 hit
PROSITEiView protein in PROSITE
PS50975 ATP_GRASP, 1 hit
PS50979 BC, 1 hit
PS00188 BIOTIN, 1 hit
PS50968 BIOTINYL_LIPOYL, 1 hit
PS50989 COA_CT_CTER, 1 hit
PS50980 COA_CT_NTER, 1 hit
PS00866 CPSASE_1, 1 hit
PS00867 CPSASE_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiACAC_SCHPO
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P78820
Secondary accession number(s): O94557
, Q09447, Q09576, Q09616, Q09667
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 11, 2001
Last modified: October 16, 2019
This is version 175 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again