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Entry version 50 (18 Sep 2019)
Sequence version 1 (06 Mar 2013)
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Protein

Cytochrome c-552

Gene

nir

Organism
Thioalkalivibrio nitratireducens (strain DSM 14787 / UNIQEM 213 / ALEN2)
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

Catalyzes the reduction of nitrite to ammonia, consuming six electrons in the process (PubMed:16500161, PubMed:22281743). Has very low activity toward hydroxylamine (PubMed:16500161). Has even lower activity toward sulfite (PubMed:16500161, PubMed:22281743). Sulfite reductase activity is maximal at neutral pH (PubMed:20944237).3 Publications

<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

Inhibited by azide and cyanide. Subject to competitive inhibition by sulfite.1 Publication

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=16700 µM for nitrite1 Publication
  2. KM=16400 µM for hydroxylamine1 Publication
  1. Vmax=4080 µmol/min/mg enzyme toward nitrite1 Publication
  2. Vmax=45 µmol/min/mg enzyme toward hydroxylamine1 Publication

pH dependencei

Optimum pH is 7-10 for nitrite reduction, and the optimum pH is 7 for sulfite reduction with only 20% residual activity at pH 7.8.2 Publications

Temperature dependencei

Optimum temperature is 80 degrees Celsius.1 Publication

<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: nitrate reduction (assimilation)

This protein is involved in the pathway nitrate reduction (assimilation), which is part of Nitrogen metabolism.
View all proteins of this organism that are known to be involved in the pathway nitrate reduction (assimilation) and in Nitrogen metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 sitei42Heme 1 (covalent)Combined sources3 Publications1
Binding sitei45Heme 1 (covalent)Combined sources3 Publications1
<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 bindingi46Iron (heme 1 axial ligand); via tele nitrogenCombined sources3 Publications1
Metal bindingi58Iron (heme 3 axial ligand); via tele nitrogenCombined sources3 Publications1
Binding sitei63Heme 2 (covalent)Combined sources3 Publications1
Binding sitei66Heme 2 (covalent)Combined sources3 Publications1
Metal bindingi67Iron (heme 2 axial ligand); via tele nitrogenCombined sources3 Publications1
Metal bindingi72Iron (heme 1 axial ligand); via tele nitrogenCombined sources3 Publications1
Binding sitei94Heme 3 (covalent)Combined sources3 Publications1
Binding sitei97Heme 3 (covalent)Combined sources3 Publications1
Metal bindingi98Iron (heme 3 axial ligand); via tele nitrogenCombined sources3 Publications1
Metal bindingi147Iron (heme 5 axial ligand); via tele nitrogenCombined sources3 Publications1
Binding sitei212Heme 6 (covalent)Combined sources3 Publications1
Binding sitei215Heme 6 (covalent)Combined sources3 Publications1
Metal bindingi216Iron (heme 6 axial ligand)Combined sources3 Publications1
Binding sitei255Heme 4 (covalent)Combined sources3 Publications1
Binding sitei258Heme 4 (covalent)Combined sources3 Publications1
Metal bindingi259Iron (heme 4 axial ligand); via tele nitrogen3 Publications1
Metal bindingi262Iron (heme 2 axial ligand); via tele nitrogenCombined sources3 Publications1
Binding sitei324Heme 5 (covalent)Combined sources3 Publications1
Binding sitei327Heme 5 (covalent)Combined sources3 Publications1
Metal bindingi328Iron (heme 5 axial ligand); via tele nitrogenCombined sources3 Publications1
Metal bindingi330CalciumCombined sources3 Publications1
Metal bindingi331Calcium; via carbonyl oxygenCombined sources3 Publications1
Metal bindingi386Calcium; via carbonyl oxygenCombined sources3 Publications1
Metal bindingi388CalciumCombined sources3 Publications1
Metal bindingi400Iron (heme 7 axial ligand); via tele nitrogenCombined sources3 Publications1
Binding sitei407Heme 8 (covalent)Combined sources3 Publications1
Binding sitei410Heme 8 (covalent)Combined sources3 Publications1
Metal bindingi411Iron (heme 8 axial ligand); via tele nitrogenCombined sources3 Publications1
Metal bindingi426Iron (heme 4 axial ligand); via tele nitrogenCombined sources3 Publications1
Binding sitei439Heme 7 (covalent)Combined sources3 Publications1
Binding sitei442Heme 7 (covalent)Combined sources3 Publications1
Metal bindingi443Iron (heme 7 axial ligand); via tele nitrogenCombined sources3 Publications1
Metal bindingi519Iron (heme 8 axial ligand); via tele nitrogenCombined sources3 Publications1

<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 functionOxidoreductase
Biological processElectron transport, Transport
LigandCalcium, Heme, Iron, Metal-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
TNIT1255043:G1HDO-251-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.7.2.2 9096

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

More...
UniPathwayi
UPA00653

<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:
Cytochrome c-552 (EC:1.7.2.22 Publications)
Alternative name(s):
Cytochrome c nitrite reductase2 Publications
TvNiR1 Publication
<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:nirImported
Ordered Locus Names:TVNIR_0259Imported
<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>OrganismiThioalkalivibrio nitratireducens (strain DSM 14787 / UNIQEM 213 / ALEN2)Imported
<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 identifieri1255043 [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 lineageiBacteriaProteobacteriaGammaproteobacteriaChromatialesEctothiorhodospiraceaeThioalkalivibrio
<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
  • UP000010809 <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

<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

GO - Cellular componenti

Keywords - Cellular componenti

Periplasm

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Chemistry databases

Drug and drug target database

More...
DrugBanki
DB02580 Pentaglyme

<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 denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 281 PublicationAdd BLAST28
<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_500108921429 – 553Cytochrome c-552Add BLAST525

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki331 ↔ 3333'-(S-cysteinyl)-tyrosine (Tyr-Cys)2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

The thioether cross-link between Tyr-331 and Cys-333 may play a structural role in the active site cavity (PubMed:19393666). Besides, it may lower the pKa of the Tyr hydroxyl group (PubMed:19393666). An additional covalent bond between Tyr-331 and Gln-388 has been observed in some protein crystals, but this may be an artifact that is due to the formation of tyrosyl radicals when the protein is exposed to oxygen (PubMed:22281743).2 Publications

Keywords - PTMi

Thioether bond

<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

Homohexamer. Dimer of trimers.

2 Publications2 Publications

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
1255043.TVNIR_0259

<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

Secondary structure

1553
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...
SMRi
L0DSL2

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
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

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the cytochrome c-552 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

KEGG Orthology (KO)

More...
KOi
K03385

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR003321 Cyt_c552
IPR011031 Multihaem_cyt
IPR036280 Multihaem_cyt_sf

The PANTHER Classification System

More...
PANTHERi
PTHR30633 PTHR30633, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF02335 Cytochrom_C552, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF000243 Cyt_c552, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF48695 SSF48695, 2 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51008 MULTIHEME_CYTC, 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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

L0DSL2-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MNDLNRLGRV GRWIAGAACL FLASAAHAEP GENLKPVDAM QCFDCHTQIE
60 70 80 90 100
DMHTVGKHAT VNCVHCHDAT EHVETASSRR MGERPVTRMD LEACATCHTA
110 120 130 140 150
QFNSFVEVRH ESHPRLEKAT PTSRSPMFDK LIAGHGFAFE HAEPRSHAFM
160 170 180 190 200
LVDHFVVDRA YGGRFQFKNW QKVTDGMGAV RGAWTVLTDA DPESSDQRRF
210 220 230 240 250
LSQTATAANP VCLNCKTQDH ILDWAYMGDE HEAAKWSRTS EVVEFARDLN
260 270 280 290 300
HPLNCFMCHD PHSAGPRVVR DGLINAVVDR GLGTYPHDPV KSEQQGMTKV
310 320 330 340 350
TFQRGREDFR AIGLLDTADS NVMCAQCHVE YNCNPGYQLS DGSRVGMDDR
360 370 380 390 400
RANHFFWANV FDYKEAAQEI DFFDFRHATT GAALPKLQHP EAETFWGSVH
410 420 430 440 450
ERNGVACADC HMPKVQLENG KVYTSHSQRT PRDMMGQACL NCHAEWTEDQ
460 470 480 490 500
ALYAIDYIKN YTHGKIVKSE YWLAKMIDLF PVAKRAGVSE DVLNQARELH
510 520 530 540 550
YDAHLYWEWW TAENSVGFHN PDQARESLMT SISKSKEAVS LLNDAIDAQV

ASR
Length:553
Mass (Da):62,345
Last modified:March 6, 2013 - v1
<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:iA9757797240FCCA7
GO

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
AJ880678 Genomic DNA Translation: CAI56199.2
CP003989 Genomic DNA Translation: AGA31970.1

NCBI Reference Sequences

More...
RefSeqi
WP_015257125.1, NC_019902.2

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AGA31970; AGA31970; TVNIR_0259

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
tni:TVNIR_0259

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1255043.3.peg.260

<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
AJ880678 Genomic DNA Translation: CAI56199.2
CP003989 Genomic DNA Translation: AGA31970.1
RefSeqiWP_015257125.1, NC_019902.2

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2OT4X-ray1.50A/B29-553[»]
2ZO5X-ray1.70A/B29-553[»]
3D1IX-ray1.80A/B29-553[»]
3F29X-ray2.00A/B29-553[»]
3FO3X-ray1.40A/B29-553[»]
3GM6X-ray1.80A/B29-553[»]
3LG1X-ray1.95A/B29-553[»]
3LGQX-ray1.80A/B29-553[»]
3MMOX-ray1.55A/B29-553[»]
3OWMX-ray1.65A/B33-551[»]
3RKHX-ray1.83A/B33-551[»]
3S7WX-ray1.79A/B33-551[»]
3SCEX-ray1.45A/B33-551[»]
3UU9X-ray2.20A/B33-552[»]
4L38X-ray1.80A/B33-551[»]
4L3XX-ray1.85A/B33-551[»]
4L3YX-ray1.95A/B33-551[»]
4L3ZX-ray1.85A/B33-551[»]
4Q0TX-ray1.70A/B30-553[»]
4Q17X-ray1.75A/B29-553[»]
4Q1OX-ray1.75A/B29-553[»]
4Q4UX-ray1.62A/B33-553[»]
4Q5BX-ray1.80A/B33-553[»]
4Q5CX-ray1.62A/B33-553[»]
SMRiL0DSL2
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi1255043.TVNIR_0259

Chemistry databases

DrugBankiDB02580 Pentaglyme

Genome annotation databases

EnsemblBacteriaiAGA31970; AGA31970; TVNIR_0259
KEGGitni:TVNIR_0259
PATRICifig|1255043.3.peg.260

Phylogenomic databases

KOiK03385

Enzyme and pathway databases

UniPathwayiUPA00653
BioCyciTNIT1255043:G1HDO-251-MONOMER
BRENDAi1.7.2.2 9096

Family and domain databases

InterProiView protein in InterPro
IPR003321 Cyt_c552
IPR011031 Multihaem_cyt
IPR036280 Multihaem_cyt_sf
PANTHERiPTHR30633 PTHR30633, 1 hit
PfamiView protein in Pfam
PF02335 Cytochrom_C552, 1 hit
PIRSFiPIRSF000243 Cyt_c552, 1 hit
SUPFAMiSSF48695 SSF48695, 2 hits
PROSITEiView protein in PROSITE
PS51008 MULTIHEME_CYTC, 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 nameiNIR_THIND
<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: L0DSL2
Secondary accession number(s): Q5F2I3
<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: April 29, 2015
Last sequence update: March 6, 2013
Last modified: September 18, 2019
This is version 50 of the entry and version 1 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 programProkaryotic 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
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