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UniProtKB - P02945 (BACR_HALSA)

Protein

Bacteriorhodopsin

Gene

bop

Organism
Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1) (Halobacterium halobium)
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

Light-driven proton pump.3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei98Primary proton acceptor3 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

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

<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 functionPhotoreceptor protein, Receptor, Retinal protein
Biological processHydrogen ion transport, Ion transport, Transport
LigandChromophore

Protein family/group databases

Transport Classification Database

More...TCDBi		3.E.1.1.1 the ion-translocating microbial rhodopsin (mr) family

<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:
Bacteriorhodopsin
Short name:
BR
Alternative name(s):
Bacterioopsin
Short name:
BO
<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:bop
Ordered Locus Names:VNG_1467G
<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>OrganismiHalobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1) (Halobacterium halobium)
<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 identifieri64091 [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 lineageiArchaea › Euryarchaeota › Stenosarchaea group › Halobacteria › Halobacteriales › Halobacteriaceae › Halobacterium ›
<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
  • UP000000554 <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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini14 – 22ExtracellularCombined sources2 Publications9
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei23 – 42Helical; Name=Helix ACombined sources2 PublicationsAdd BLAST20
Topological domaini43 – 56CytoplasmicCombined sources2 PublicationsAdd BLAST14
Transmembranei57 – 75Helical; Name=Helix BCombined sources2 PublicationsAdd BLAST19
Topological domaini76 – 92ExtracellularCombined sources2 PublicationsAdd BLAST17
Transmembranei93 – 109Helical; Name=Helix CCombined sources2 PublicationsAdd BLAST17
Topological domaini110 – 120CytoplasmicCombined sources2 PublicationsAdd BLAST11
Transmembranei121 – 140Helical; Name=Helix DCombined sources2 PublicationsAdd BLAST20
Topological domaini141 – 147ExtracellularCombined sources2 Publications7
Transmembranei148 – 167Helical; Name=Helix ECombined sources2 PublicationsAdd BLAST20
Topological domaini168 – 185CytoplasmicCombined sources2 PublicationsAdd BLAST18
Transmembranei186 – 204Helical; Name=Helix FCombined sources2 PublicationsAdd BLAST19
Topological domaini205 – 216ExtracellularCombined sources2 PublicationsAdd BLAST12
Transmembranei217 – 236Helical; Name=Helix GCombined sources2 PublicationsAdd BLAST20
Topological domaini237 – 262CytoplasmicCombined sources2 PublicationsAdd BLAST26

GO - Cellular componenti

View the complete GO annotation on QuickGO ...

Keywords - Cellular componenti

Cell membrane, Membrane

<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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_00000202461 – 133 PublicationsAdd BLAST13
<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_000002024714 – 262Bacteriorhodopsin2 PublicationsAdd BLAST249

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 residuei14Pyrrolidone carboxylic acid1 Publication1
Modified residuei229N6-(retinylidene)lysineCombined sources12 Publications1

<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 covalent binding of retinal to the apoprotein, bacterioopsin, generates bacteriorhodopsin.13 Publications

Keywords - PTMi

Pyrrolidone carboxylic acid

Proteomic databases

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

More...PaxDbi		P02945

<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

Homotrimer.5 Publications

Protein-protein interaction databases

Database of interacting proteins

More...DIPi		DIP-59007N

STRING: functional protein association networks

More...STRINGi		64091.VNG1467G

<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

1262
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

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
1AP9X-ray2.35A14-261[»]
1AT9X-ray3.00A15-261[»]
1BACmodel-A14-261[»]
1BADmodel-A14-261[»]
1BCTNMR-A176-244[»]
1BHANMR-A14-84[»]
1BHBNMR-A14-84[»]
1BM1X-ray3.50A15-261[»]
1BRDelectron microscopy-A15-261[»]
1BRRX-ray2.90A/B/C15-261[»]
1BRXX-ray2.30A15-261[»]
1C3WX-ray1.55A18-244[»]
1C8RX-ray1.80A14-262[»]
1C8SX-ray2.00A18-235[»]
1CWQX-ray2.25A/B14-261[»]
1DZEX-ray2.50A14-261[»]
1E0PX-ray2.10A18-245[»]
1F4ZX-ray1.80A18-244[»]
1F50X-ray1.70A18-244[»]
1FBBX-ray3.20A14-261[»]
1FBKX-ray3.20A14-261[»]
1IW6X-ray2.30A14-261[»]
1IW9X-ray2.50A14-261[»]
1IXFX-ray2.60A14-261[»]
1JV6X-ray2.00A14-262[»]
1JV7X-ray2.25A14-262[»]
1KG8X-ray2.00A14-244[»]
1KG9X-ray1.81A14-244[»]
1KGBX-ray1.65A14-244[»]
1KMEX-ray2.00A/B14-244[»]
1L0MNMR-A20-231[»]
1M0KX-ray1.43A1-262[»]
1M0LX-ray1.47A1-262[»]
1M0MX-ray1.43A1-262[»]
1MGYX-ray2.00A14-262[»]
1O0AX-ray1.62A14-262[»]
1P8HX-ray1.52A14-262[»]
1P8IX-ray1.86A14-262[»]
1P8UX-ray1.62A14-262[»]
1PXRX-ray1.70A/B14-262[»]
1PXSX-ray2.20A/B14-262[»]
1PY6X-ray1.80A/B14-262[»]
1Q5IX-ray2.30A/B14-262[»]
1Q5JX-ray2.10A/B14-262[»]
1QHJX-ray1.90A14-261[»]
1QKOX-ray2.10A14-261[»]
1QKPX-ray2.10A14-261[»]
1QM8X-ray2.50A14-261[»]
1R2NNMR-A14-262[»]
1R84NMR-A14-245[»]
1S51X-ray2.00A/B18-244[»]
1S52X-ray2.30A/B18-244[»]
1S53X-ray2.00A/B18-244[»]
1S54X-ray2.20A/B18-244[»]
1S8JX-ray2.30A14-262[»]
1S8LX-ray2.30A14-262[»]
1TN0X-ray2.50A/B14-262[»]
1TN5X-ray2.20A/B14-262[»]
1UCQX-ray2.40A14-262[»]
1VJMX-ray2.30A14-262[»]
1X0IX-ray2.30114-261[»]
1X0KX-ray2.60114-261[»]
1X0SX-ray2.50A14-261[»]
1XJIX-ray2.20A15-261[»]
2AT9electron microscopy3.00A15-261[»]
2BRDX-ray3.50A15-261[»]
2I1XX-ray2.00A14-262[»]
2I20X-ray2.08A14-262[»]
2I21X-ray1.84A14-262[»]
2NTUX-ray1.53A14-262[»]
2NTWX-ray1.53A14-262[»]
2WJKX-ray2.30A14-262[»]
2WJLX-ray2.15A14-262[»]
2ZFEX-ray2.50A1-262[»]
2ZZLX-ray2.03A1-262[»]
3COCX-ray2.31A/B14-262[»]
3CODX-ray2.70A/B14-262[»]
3HANX-ray2.75A14-262[»]
3HAOX-ray2.49A/B14-262[»]
3HAPX-ray1.60A14-262[»]
3HAQX-ray2.30A14-262[»]
3HARX-ray1.70A14-262[»]
3HASX-ray1.90A14-262[»]
3MBVX-ray2.00A14-261[»]
3NS0X-ray1.78A14-261[»]
3NSBX-ray1.78A14-261[»]
3T45X-ray3.01A/B/C20-244[»]
3UTVX-ray2.06A14-262[»]
3UTWX-ray2.40A14-262[»]
3UTXX-ray2.47A/B14-262[»]
3UTYX-ray2.37A/B14-262[»]
3VHZX-ray2.30A1-262[»]
3VI0X-ray2.30A1-262[»]
4FPDX-ray2.65A1-262[»]
4HWLX-ray2.00A/B1-262[»]
4HYXX-ray1.99A/B1-262[»]
4MD1X-ray1.73A14-261[»]
4MD2X-ray1.73A14-261[»]
4OV0X-ray2.00A14-262[»]
4X31X-ray2.40A18-246[»]
4X32X-ray1.90A18-245[»]
4XXJX-ray1.90A/B/C14-262[»]
5A44X-ray2.29A14-261[»]
5A45X-ray2.57A14-261[»]
5B34X-ray2.10A14-262[»]
5B35X-ray2.35A14-262[»]
5B6VX-ray2.00A14-261[»]
5B6WX-ray2.10A14-261[»]
5B6XX-ray2.10A14-261[»]
5B6YX-ray2.10A14-261[»]
5B6ZX-ray2.10A14-261[»]
5BR2X-ray1.80A14-262[»]
5BR5X-ray2.00A14-262[»]
5H2HX-ray2.10A14-261[»]
5H2IX-ray2.10A14-261[»]
5H2JX-ray2.10A14-261[»]
5H2KX-ray2.10A14-261[»]
5H2LX-ray2.10A14-261[»]
5H2MX-ray2.10A14-261[»]
5H2NX-ray2.10A14-261[»]
5H2OX-ray2.10A14-261[»]
5H2PX-ray2.10A14-261[»]
5J7AX-ray2.30A18-244[»]
5VN7X-ray2.70A/B1-262[»]
5VN9X-ray2.59A/B1-262[»]
5ZILX-ray1.29A18-246[»]
5ZIMX-ray1.25A18-245[»]
5ZINX-ray1.27A18-245[»]
6G7HX-ray1.50A14-261[»]
6G7IX-ray1.90A1-262[»]
6G7JX-ray1.90A1-262[»]
6G7KX-ray1.90A1-262[»]
6G7LX-ray1.90A1-262[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		P02945

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

More...SMRi		P02945

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P02945

<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 archaeal/bacterial/fungal opsin family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		arCOG02812 Archaea
COG5524 LUCA

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P02945

KEGG Orthology (KO)

More...KOi		K04641

Identification of Orthologs from Complete Genome Data

More...OMAi		QVYWARY

Database for complete collections of gene phylogenies

More...PhylomeDBi		P02945

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR001425 Arc/bac/fun_rhodopsins
IPR018229 Rhodopsin_retinal_BS

The PANTHER Classification System

More...PANTHERi		PTHR28286 PTHR28286, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF01036 Bac_rhodopsin, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00251 BACTRLOPSIN

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM01021 Bac_rhodopsin, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00950 BACTERIAL_OPSIN_1, 1 hit
PS00327 BACTERIAL_OPSIN_RET, 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>.<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.

P02945-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MLELLPTAVE GVSQAQITGR PEWIWLALGT ALMGLGTLYF LVKGMGVSDP 
        60         70         80         90        100
DAKKFYAITT LVPAIAFTMY LSMLLGYGLT MVPFGGEQNP IYWARYADWL 
       110        120        130        140        150
FTTPLLLLDL ALLVDADQGT ILALVGADGI MIGTGLVGAL TKVYSYRFVW 
       160        170        180        190        200
WAISTAAMLY ILYVLFFGFT SKAESMRPEV ASTFKVLRNV TVVLWSAYPV 
       210        220        230        240        250
VWLIGSEGAG IVPLNIETLL FMVLDVSAKV GFGLILLRSR AIFGEAEAPE 
       260 
PSAGDGAAAT SD
Length:262
Mass (Da):28,256
Last modified:July 1, 1989 - 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:i38AC8A364C8C7F21
GO

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 conflicti118Q → E AA sequence (Ref. 6) Curated1
Sequence conflicti124L → I AA sequence (Ref. 6) Curated1
Sequence conflicti130I → L AA sequence (Ref. 6) Curated1
Sequence conflicti151Missing AA sequence (Ref. 6) Curated1
Sequence conflicti159L → S AA sequence (Ref. 6) Curated1
Sequence conflicti219L → A AA sequence (Ref. 6) Curated1

<p>This subsection of the ‘Sequence’ section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>Mass spectrometryi

Molecular mass is 27052.5±2.7 Da from positions 14 - 261. Determined by ESI. 1 Publication

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
V00474 Genomic DNA Translation: CAA23744.1
M11720 Genomic DNA Translation: AAA72504.1
X70293 Genomic DNA Translation: CAA49774.1
AE004437 Genomic DNA Translation: AAG19772.1

Protein sequence database of the Protein Information Resource

More...PIRi		A93898 RAHSB
H84300

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAG19772; AAG19772; VNG_1467G

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hal:VNG_1467G

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|64091.14.peg.1122

<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
V00474 Genomic DNA Translation: CAA23744.1
M11720 Genomic DNA Translation: AAA72504.1
X70293 Genomic DNA Translation: CAA49774.1
AE004437 Genomic DNA Translation: AAG19772.1
PIRiA93898 RAHSB
H84300

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AP9X-ray2.35A14-261[»]
1AT9X-ray3.00A15-261[»]
1BACmodel-A14-261[»]
1BADmodel-A14-261[»]
1BCTNMR-A176-244[»]
1BHANMR-A14-84[»]
1BHBNMR-A14-84[»]
1BM1X-ray3.50A15-261[»]
1BRDelectron microscopy-A15-261[»]
1BRRX-ray2.90A/B/C15-261[»]
1BRXX-ray2.30A15-261[»]
1C3WX-ray1.55A18-244[»]
1C8RX-ray1.80A14-262[»]
1C8SX-ray2.00A18-235[»]
1CWQX-ray2.25A/B14-261[»]
1DZEX-ray2.50A14-261[»]
1E0PX-ray2.10A18-245[»]
1F4ZX-ray1.80A18-244[»]
1F50X-ray1.70A18-244[»]
1FBBX-ray3.20A14-261[»]
1FBKX-ray3.20A14-261[»]
1IW6X-ray2.30A14-261[»]
1IW9X-ray2.50A14-261[»]
1IXFX-ray2.60A14-261[»]
1JV6X-ray2.00A14-262[»]
1JV7X-ray2.25A14-262[»]
1KG8X-ray2.00A14-244[»]
1KG9X-ray1.81A14-244[»]
1KGBX-ray1.65A14-244[»]
1KMEX-ray2.00A/B14-244[»]
1L0MNMR-A20-231[»]
1M0KX-ray1.43A1-262[»]
1M0LX-ray1.47A1-262[»]
1M0MX-ray1.43A1-262[»]
1MGYX-ray2.00A14-262[»]
1O0AX-ray1.62A14-262[»]
1P8HX-ray1.52A14-262[»]
1P8IX-ray1.86A14-262[»]
1P8UX-ray1.62A14-262[»]
1PXRX-ray1.70A/B14-262[»]
1PXSX-ray2.20A/B14-262[»]
1PY6X-ray1.80A/B14-262[»]
1Q5IX-ray2.30A/B14-262[»]
1Q5JX-ray2.10A/B14-262[»]
1QHJX-ray1.90A14-261[»]
1QKOX-ray2.10A14-261[»]
1QKPX-ray2.10A14-261[»]
1QM8X-ray2.50A14-261[»]
1R2NNMR-A14-262[»]
1R84NMR-A14-245[»]
1S51X-ray2.00A/B18-244[»]
1S52X-ray2.30A/B18-244[»]
1S53X-ray2.00A/B18-244[»]
1S54X-ray2.20A/B18-244[»]
1S8JX-ray2.30A14-262[»]
1S8LX-ray2.30A14-262[»]
1TN0X-ray2.50A/B14-262[»]
1TN5X-ray2.20A/B14-262[»]
1UCQX-ray2.40A14-262[»]
1VJMX-ray2.30A14-262[»]
1X0IX-ray2.30114-261[»]
1X0KX-ray2.60114-261[»]
1X0SX-ray2.50A14-261[»]
1XJIX-ray2.20A15-261[»]
2AT9electron microscopy3.00A15-261[»]
2BRDX-ray3.50A15-261[»]
2I1XX-ray2.00A14-262[»]
2I20X-ray2.08A14-262[»]
2I21X-ray1.84A14-262[»]
2NTUX-ray1.53A14-262[»]
2NTWX-ray1.53A14-262[»]
2WJKX-ray2.30A14-262[»]
2WJLX-ray2.15A14-262[»]
2ZFEX-ray2.50A1-262[»]
2ZZLX-ray2.03A1-262[»]
3COCX-ray2.31A/B14-262[»]
3CODX-ray2.70A/B14-262[»]
3HANX-ray2.75A14-262[»]
3HAOX-ray2.49A/B14-262[»]
3HAPX-ray1.60A14-262[»]
3HAQX-ray2.30A14-262[»]
3HARX-ray1.70A14-262[»]
3HASX-ray1.90A14-262[»]
3MBVX-ray2.00A14-261[»]
3NS0X-ray1.78A14-261[»]
3NSBX-ray1.78A14-261[»]
3T45X-ray3.01A/B/C20-244[»]
3UTVX-ray2.06A14-262[»]
3UTWX-ray2.40A14-262[»]
3UTXX-ray2.47A/B14-262[»]
3UTYX-ray2.37A/B14-262[»]
3VHZX-ray2.30A1-262[»]
3VI0X-ray2.30A1-262[»]
4FPDX-ray2.65A1-262[»]
4HWLX-ray2.00A/B1-262[»]
4HYXX-ray1.99A/B1-262[»]
4MD1X-ray1.73A14-261[»]
4MD2X-ray1.73A14-261[»]
4OV0X-ray2.00A14-262[»]
4X31X-ray2.40A18-246[»]
4X32X-ray1.90A18-245[»]
4XXJX-ray1.90A/B/C14-262[»]
5A44X-ray2.29A14-261[»]
5A45X-ray2.57A14-261[»]
5B34X-ray2.10A14-262[»]
5B35X-ray2.35A14-262[»]
5B6VX-ray2.00A14-261[»]
5B6WX-ray2.10A14-261[»]
5B6XX-ray2.10A14-261[»]
5B6YX-ray2.10A14-261[»]
5B6ZX-ray2.10A14-261[»]
5BR2X-ray1.80A14-262[»]
5BR5X-ray2.00A14-262[»]
5H2HX-ray2.10A14-261[»]
5H2IX-ray2.10A14-261[»]
5H2JX-ray2.10A14-261[»]
5H2KX-ray2.10A14-261[»]
5H2LX-ray2.10A14-261[»]
5H2MX-ray2.10A14-261[»]
5H2NX-ray2.10A14-261[»]
5H2OX-ray2.10A14-261[»]
5H2PX-ray2.10A14-261[»]
5J7AX-ray2.30A18-244[»]
5VN7X-ray2.70A/B1-262[»]
5VN9X-ray2.59A/B1-262[»]
5ZILX-ray1.29A18-246[»]
5ZIMX-ray1.25A18-245[»]
5ZINX-ray1.27A18-245[»]
6G7HX-ray1.50A14-261[»]
6G7IX-ray1.90A1-262[»]
6G7JX-ray1.90A1-262[»]
6G7KX-ray1.90A1-262[»]
6G7LX-ray1.90A1-262[»]
ProteinModelPortaliP02945
SMRiP02945
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-59007N
STRINGi64091.VNG1467G

Protein family/group databases

TCDBi3.E.1.1.1 the ion-translocating microbial rhodopsin (mr) family

Proteomic databases

PaxDbiP02945

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAG19772; AAG19772; VNG_1467G
KEGGihal:VNG_1467G
PATRICifig|64091.14.peg.1122

Phylogenomic databases

eggNOGiarCOG02812 Archaea
COG5524 LUCA
InParanoidiP02945
KOiK04641
OMAiQVYWARY
PhylomeDBiP02945

Miscellaneous databases

EvolutionaryTraceiP02945

Family and domain databases

InterProiView protein in InterPro
IPR001425 Arc/bac/fun_rhodopsins
IPR018229 Rhodopsin_retinal_BS
PANTHERiPTHR28286 PTHR28286, 1 hit
PfamiView protein in Pfam
PF01036 Bac_rhodopsin, 1 hit
PRINTSiPR00251 BACTRLOPSIN
SMARTiView protein in SMART
SM01021 Bac_rhodopsin, 1 hit
PROSITEiView protein in PROSITE
PS00950 BACTERIAL_OPSIN_1, 1 hit
PS00327 BACTERIAL_OPSIN_RET, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		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 nameiBACR_HALSA
<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: P02945
Secondary accession number(s): Q9HPU5
<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 21, 1986
Last sequence update: July 1, 1989
Last modified: January 16, 2019
This is version 183 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 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. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
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