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UniProtKB - P30131 (HYPF_ECOLI)

Entry version 168 (02 Jun 2021)
Sequence version 2 (01 Nov 1997)
Previous versions | rss
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Protein

Carbamoyltransferase HypF

Gene

hypF

Organism
Escherichia coli (strain K12)
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

Involved in the maturation of [NiFe] hydrogenases (PubMed:8661925, PubMed:12377778, PubMed:12586941).

Along with HypE, it catalyzes the synthesis of the CN ligands of the active site iron of [NiFe]-hydrogenases (PubMed:12586941).

HypF functions as a carbamoyl transferase using carbamoylphosphate as a substrate and transferring the carboxamido moiety in an ATP-dependent reaction to the thiolate of the C-terminal cysteine of HypE yielding a protein-S-carboxamide (PubMed:12586941, PubMed:15291820).

In the absence of any other substrate, displays carbamoyl-phosphate phosphatase activity (PubMed:12377778).

4 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: [NiFe] hydrogenase maturation

This protein is involved in the pathway [NiFe] hydrogenase maturation, which is part of Protein modification.Curated
View all proteins of this organism that are known to be involved in the pathway [NiFe] hydrogenase maturation and in Protein modification.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri109 – 134C4-type1 PublicationAdd BLAST26
Zinc fingeri159 – 184C4-type1 PublicationAdd BLAST26

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

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 functionLigase
LigandMetal-binding, Zinc

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		EcoCyc:EG11551-MONOMER
MetaCyc:EG11551-MONOMER

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

More...UniPathwayi		UPA00335

<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%5Fand%5Ftaxonomy%5Fsection">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:
Carbamoyltransferase HypFCurated (EC:6.2.-.-2 Publications)
Alternative name(s):
Carbamoyl phosphate-converting enzyme HypF
[NiFe]-hydrogenase maturation factor HypF
Short name:
Hydrogenase maturation protein HypF
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:hypF1 Publication
Synonyms:hydA1 Publication
Ordered Locus Names:b2712, JW5433
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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>OrganismiEscherichia coli (strain K12)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri83333 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
  • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">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
  • UP000000625 Componenti: Chromosome

<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

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Deletion of the gene results in the loss of hydrogenase activity and in the synthesis of the large subunits of the hydrogenase 1, 2 and 3 in the inactive precursor form.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi23R → E or H: Loss of activity. 2 Publications1
Mutagenesisi23R → Q: Diminishes activity. 2 Publications1
Mutagenesisi109C → A: Loss of activity. 1 Publication1
Mutagenesisi159C → A: Loss of activity. 1 Publication1
Mutagenesisi475H → A: No change in activity. 1 Publication1
Mutagenesisi476H → A: Carbamoyl phosphate-dependent ATP hydrolysis activity diminished in vitro but sufficient for wild-type-like phenotype. 2 Publications1
Mutagenesisi479H → A: No change in activity. 1 Publication1

<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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000716141 – 750Carbamoyltransferase HypFAdd BLAST750

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P30131

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

More...PaxDbi		P30131

PRoteomics IDEntifications database

More...PRIDEi		P30131

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer (PubMed:12377778).

Forms a complex with HypE (PubMed:15291820, PubMed:18065529).

3 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		4259427, 14 interactors
849360, 8 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-5281, HypEF Ni-hydrogenase maturation complex

Database of interacting proteins

More...DIPi		DIP-10000N

Protein interaction database and analysis system

More...IntActi		P30131, 8 interactors

STRING: functional protein association networks

More...STRINGi		511145.b2712

<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

1750
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		P30131

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P30131

<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%5Fand%5Fdomains%5Fsection">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>Domaini8 – 92Acylphosphatase-likePROSITE-ProRule annotationAdd BLAST85
Domaini200 – 376YrdC-likePROSITE-ProRule annotationAdd BLAST177

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>Regioni19 – 23Substrate binding1 Publication5

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

Contains a version of the YrdC-like domain which probably has a different function than that of some proteins where it has been implicated in RNA binding.
Contains a unique C-terminal domain with an O-carbamoyltransferase motif.

<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 carbamoyltransferase HypF family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri109 – 134C4-type1 PublicationAdd BLAST26
Zinc fingeri159 – 184C4-type1 PublicationAdd BLAST26

Keywords - Domaini

Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		COG0068, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_009164_0_0_6

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P30131

Database for complete collections of gene phylogenies

More...PhylomeDBi		P30131

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR001792, Acylphosphatase-like_dom
IPR036046, Acylphosphatase-like_dom_sf
IPR017968, Acylphosphatase_CS
IPR004421, Carbamoyltransferase_HypF
IPR017945, DHBP_synth_RibB-like_a/b_dom
IPR041440, HypF_C
IPR006070, YrdC-like_dom
IPR011125, Znf_HypF

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00708, Acylphosphatase, 1 hit
PF17788, HypF_C, 1 hit
PF01300, Sua5_yciO_yrdC, 1 hit
PF07503, zf-HYPF, 2 hits

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF006256, CMPcnvr_hdrg_mat, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF54975, SSF54975, 1 hit
SSF55821, SSF55821, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR00143, hypF, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00150, ACYLPHOSPHATASE_1, 1 hit
PS51160, ACYLPHOSPHATASE_3, 1 hit
PS51163, YRDC, 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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

P30131-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAKNTSCGVQ LRIRGKVQGV GFRPFVWQLA QQLNLHGDVC NDGDGVEVRL 
        60         70         80         90        100
REDPETFLVQ LYQHCPPLAR IDSVEREPFI WSQLPTEFTI RQSTGGTMNT 
       110        120        130        140        150
QIVPDAATCP ACLAEMNTPG ERRYRYPFIN CTHCGPRFTI IRAMPYDRPF 
       160        170        180        190        200
TVMAAFPLCP ACDKEYRDPL DRRFHAQPVA CPECGPHLEW VSHGEHAEQE 
       210        220        230        240        250
AALQAAIAQL KMGKIVAIKG IGGFHLACDA RNSNAVATLR ARKHRPAKPL 
       260        270        280        290        300
AVMLPVADGL PDAARQLLTT PAAPIVLVDK KYVPELCDDI APDLNEVGVM 
       310        320        330        340        350
LPANPLQHLL LQELQCPLVM TSGNLSGKPP AISNEQALAD LQGIADGFLI 
       360        370        380        390        400
HNRDIVQRMD DSVVRESGEM LRRSRGYVPD ALALPPGFKN VPPVLCLGAD 
       410        420        430        440        450
LKNTFCLVRG EQAVLSQHLG DLSDDGIQMQ WREALRLMQN IYDFTPQYVV 
       460        470        480        490        500
HDAHPGYVSS QWAREMNLPT QTVLHHHAHA AACLAEHQWP LDGGDVIALT 
       510        520        530        540        550
LDGIGMGENG ALWGGECLRV NYRECEHLGG LPAVALPGGD LAAKQPWRNL 
       560        570        580        590        600
LAQCLRFVPE WQNYSETASV QQQNWSVLAR AIERGINAPL ASSCGRFFDA 
       610        620        630        640        650
VAAALGCAPA TLSYEGEAAC ALEALAASCH GVTHPVTMPR VDNQLDLATF 
       660        670        680        690        700
WQQWLNWQAP VNQRAWAFHD ALAQGFAALM REQATMRGIT TLVFSGGVIH 
       710        720        730        740        750
NRLLRARLAH YLADFTLLFP QSLPAGDGGL SLGQGVIAAA RWLAGEVQNG
Length:750
Mass (Da):82,066
Last modified:November 1, 1997 - 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:i8BB245F80349A91E
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 conflicti31 – 32QQ → RE in BAA03315 (Ref. 1) Curated2
Sequence conflicti367 – 386SGEML…LALPP → RRNAAPFAGVCAGCAGFAS in BAA03315 (Ref. 1) CuratedAdd BLAST20
Sequence conflicti431 – 432WR → CA in BAA03315 (Ref. 1) Curated2
Sequence conflicti435L → S in BAA03315 (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
D14422 Genomic DNA Translation: BAA03315.1
U29579 Genomic DNA Translation: AAA69222.1
U00096 Genomic DNA Translation: AAC75754.1
AP009048 Genomic DNA Translation: BAE76789.1

Protein sequence database of the Protein Information Resource

More...PIRi		D65051

NCBI Reference Sequences

More...RefSeqi		NP_417192.1, NC_000913.3
WP_001107704.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAC75754; AAC75754; b2712
BAE76789; BAE76789; BAE76789

Database of genes from NCBI RefSeq genomes

More...GeneIDi		944963

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ecj:JW5433
eco:b2712

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|1411691.4.peg.4030

<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
D14422 Genomic DNA Translation: BAA03315.1
U29579 Genomic DNA Translation: AAA69222.1
U00096 Genomic DNA Translation: AAC75754.1
AP009048 Genomic DNA Translation: BAE76789.1
PIRiD65051
RefSeqiNP_417192.1, NC_000913.3
WP_001107704.1, NZ_LN832404.1

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
1GXTX-ray1.30A1-91[»]
1GXUX-ray1.27A1-91[»]
SMRiP30131
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4259427, 14 interactors
849360, 8 interactors
ComplexPortaliCPX-5281, HypEF Ni-hydrogenase maturation complex
DIPiDIP-10000N
IntActiP30131, 8 interactors
STRINGi511145.b2712

Proteomic databases

jPOSTiP30131
PaxDbiP30131
PRIDEiP30131

Genome annotation databases

EnsemblBacteriaiAAC75754; AAC75754; b2712
BAE76789; BAE76789; BAE76789
GeneIDi944963
KEGGiecj:JW5433
eco:b2712
PATRICifig|1411691.4.peg.4030

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

More...EchoBASEi		EB1512

Phylogenomic databases

eggNOGiCOG0068, Bacteria
HOGENOMiCLU_009164_0_0_6
InParanoidiP30131
PhylomeDBiP30131

Enzyme and pathway databases

UniPathwayiUPA00335
BioCyciEcoCyc:EG11551-MONOMER
MetaCyc:EG11551-MONOMER

Miscellaneous databases

EvolutionaryTraceiP30131

Protein Ontology

More...PROi		PR:P30131

Family and domain databases

InterProiView protein in InterPro
IPR001792, Acylphosphatase-like_dom
IPR036046, Acylphosphatase-like_dom_sf
IPR017968, Acylphosphatase_CS
IPR004421, Carbamoyltransferase_HypF
IPR017945, DHBP_synth_RibB-like_a/b_dom
IPR041440, HypF_C
IPR006070, YrdC-like_dom
IPR011125, Znf_HypF
PfamiView protein in Pfam
PF00708, Acylphosphatase, 1 hit
PF17788, HypF_C, 1 hit
PF01300, Sua5_yciO_yrdC, 1 hit
PF07503, zf-HYPF, 2 hits
PIRSFiPIRSF006256, CMPcnvr_hdrg_mat, 1 hit
SUPFAMiSSF54975, SSF54975, 1 hit
SSF55821, SSF55821, 1 hit
TIGRFAMsiTIGR00143, hypF, 1 hit
PROSITEiView protein in PROSITE
PS00150, ACYLPHOSPHATASE_1, 1 hit
PS51160, ACYLPHOSPHATASE_3, 1 hit
PS51163, YRDC, 1 hit

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 nameiHYPF_ECOLI
<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: P30131
Secondary accession number(s): Q2MAB7, Q46878
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: November 1, 1997
Last modified: June 2, 2021
This is version 168 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, Reference proteome

Documents

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