Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

RecBCD enzyme subunit RecC

Gene

recC

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

A helicase/nuclease that prepares dsDNA breaks (DSB) for recombinational DNA repair. Binds to DSBs and unwinds DNA via a rapid (>1 kb/second) and highly processive (>30 kb) ATP-dependent bidirectional helicase. Unwinds dsDNA until it encounters a Chi (crossover hotspot instigator, 5'-GCTGGTGG-3') sequence from the 3' direction. Cuts ssDNA a few nucleotides 3' to Chi site, by nicking one strand or switching the strand degraded (depending on the reaction conditions). The properties and activities of the enzyme are changed at Chi. The Chi-altered holoenzyme produces a long 3'-ssDNA overhang which facilitates RecA-binding to the ssDNA for homologous DNA recombination and repair. Holoenzyme degrades any linearized DNA that is unable to undergo homologous recombination (PubMed:4562392, PubMed:4552016, PubMed:123277). In the holoenzyme this subunit almost certainly recognizes the wild-type Chi sequence, when added to isolated RecB increases its ATP-dependent helicase processivity. The RecBC complex requires the RecD subunit for nuclease activity, but can translocate along ssDNA in both directions.18 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

  • Exonucleolytic cleavage (in the presence of ATP) in either 5'- to 3'- or 3'- to 5'-direction to yield 5'-phosphooligonucleotides.UniRule annotation EC:3.1.11.5

<p>This subsection of the ‘Function’ 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

After reacting with DNA bearing a Chi site the holoenzyme is disassembled and loses exonuclease activity, DNA unwinding and Chi-directed DNA cleavage; RecB remains complexed with ssDNA, which may prevent holoenzyme reassembly (PubMed:10197988). High levels of Mg2+ (13 mM MgCl2+) or incubation with DNase allow holoenyzme reassembly, suggesting it is DNA bound to RecB that prevents reassembly (PubMed:10197988).2 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section specifies the position and type of each DNA-binding domain present within the protein.<p><a href='/help/dna_bind' target='_top'>More...</a></p>DNA bindingi9711
DNA bindingi10011
DNA bindingi1078 – 10814

<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

  • ATP binding Source: UniProtKB-UniRule
  • ATP-dependent DNA helicase activity Source: UniProtKB-UniRule
  • DNA binding Source: UniProtKB-UniRule
  • exodeoxyribonuclease V activity Source: EcoCyc

GO - Biological processi

  • clearance of foreign intracellular DNA Source: UniProtKB
  • DNA recombination Source: EcoCyc
  • double-strand break repair via homologous recombination Source: EcoCyc
  • response to radiation Source: EcoCyc

<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 functionDNA-binding, Exonuclease, Helicase, Hydrolase, Nuclease
Biological processDNA damage, DNA repair
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:EG10825-MONOMER
MetaCyc:EG10825-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.1.11.5 2026

<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:
RecBCD enzyme subunit RecCUniRule annotation (EC:3.1.11.5UniRule annotation)
Alternative name(s):
Exodeoxyribonuclease V 125 kDa polypeptide
Exodeoxyribonuclease V gamma chain
Exonuclease V subunit RecCUniRule annotation
Short name:
ExoV subunit RecCUniRule annotation
<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:recCUniRule annotation
Ordered Locus Names:b2822, JW2790
<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>OrganismiEscherichia coli (strain K12)
<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 identifieri83333 [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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<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
  • UP000000318 <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
  • UP000000625 Componenti: Chromosome

Organism-specific databases

Escherichia coli strain K12 genome database

More...
EcoGenei
EG10825 recC

<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

<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

Decreased degradation of DNA with free ends that is unable to undergo homologous recombination, which can fortuitously lead to more efficient viral infection (PubMed:4562392, PubMed:123277). Cells are deficient in DNA recombination repair and have increased sensitivity to UV light. The cultures have many inviable cells.3 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'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>Mutagenesisi38Q → A: Acts at variant Chi sequences. 1 Publication1
Mutagenesisi64L → A: Does not act at Chi. 1 Publication1
Mutagenesisi70W → A: Does not act at Chi. 1 Publication1
Mutagenesisi133D → A: Does not act at Chi. 1 Publication1
Mutagenesisi134L → A: Acts at variant Chi sequences. 1 Publication1
Mutagenesisi136D → A: Does not act at Chi. 1 Publication1
Mutagenesisi137Q → A: Acts at variant Chi sequences. 1 Publication1
Mutagenesisi142R → A: Acts at variant Chi sequences. 1 Publication1
Mutagenesisi186R → A, C or H: Does not act at Chi. 1 Publication1
Mutagenesisi705D → A or H: Acts at variant Chi sequences. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL2095232

<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_00000871201 – 1122RecBCD enzyme subunit RecCAdd BLAST1122

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P07648

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

More...
PaxDbi
P07648

PRoteomics IDEntifications database

More...
PRIDEi
P07648

<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

Heterotrimer of RecB, RecC and RecD. All subunits contribute to DNA-binding. Interacts with YgbT (Cas1) (PubMed:21219465).UniRule annotation7 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
4261821, 369 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-2197 Exodeoxyribonuclease V complex

Database of interacting proteins

More...
DIPi
DIP-10650N

Protein interaction database and analysis system

More...
IntActi
P07648, 3 interactors

Molecular INTeraction database

More...
MINTi
P07648

STRING: functional protein association networks

More...
STRINGi
316385.ECDH10B_2992

<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

11122
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
1W36X-ray3.10C/F1-1122[»]
3K70X-ray3.59C/F1-1122[»]
5LD2electron microscopy3.83C1-1122[»]
5MBVelectron microscopy3.80C1-1122[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P07648

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

More...
SMRi
P07648

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
P07648

<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 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

The holoenzyme may undergo conformational shifts upon DNA binding: the nuclease domain of RecB may swing away from the DNA exit tunnel in RecC. When Chi DNA binds to the RecC tunnel, the nuclease domain may then swing back to its original position (that seen in crystal structures), allowing it to nick the DNA 3' of the Chi site and then rotate to load RecA. At high Mg2+ the nuclease domain may swing back more frequently, explaining differences seen in assays performed at high Mg2+.1 Publication

<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 RecC family.UniRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105DSY Bacteria
COG1330 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000258319

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P07648

KEGG Orthology (KO)

More...
KOi
K03583

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P07648

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.10.160, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_01486 RecC, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR013986 DExx_box_DNA_helicase_dom_sf
IPR027417 P-loop_NTPase
IPR006697 RecC
IPR011335 Restrct_endonuc-II-like

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF000980 RecC, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52540 SSF52540, 2 hits
SSF52980 SSF52980, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR01450 recC, 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.

P07648-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MLRVYHSNRL DVLEALMEFI VERERLDDPF EPEMILVQST GMAQWLQMTL
60 70 80 90 100
SQKFGIAANI DFPLPASFIW DMFVRVLPEI PKESAFNKQS MSWKLMTLLP
110 120 130 140 150
QLLEREDFTL LRHYLTDDSD KRKLFQLSSK AADLFDQYLV YRPDWLAQWE
160 170 180 190 200
TGHLVEGLGE AQAWQAPLWK ALVEYTHQLG QPRWHRANLY QRFIETLESA
210 220 230 240 250
TTCPPGLPSR VFICGISALP PVYLQALQAL GKHIEIHLLF TNPCRYYWGD
260 270 280 290 300
IKDPAYLAKL LTRQRRHSFE DRELPLFRDS ENAGQLFNSD GEQDVGNPLL
310 320 330 340 350
ASWGKLGRDY IYLLSDLESS QELDAFVDVT PDNLLHNIQS DILELENRAV
360 370 380 390 400
AGVNIEEFSR SDNKRPLDPL DSSITFHVCH SPQREVEVLH DRLLAMLEED
410 420 430 440 450
PTLTPRDIIV MVADIDSYSP FIQAVFGSAP ADRYLPYAIS DRRARQSHPV
460 470 480 490 500
LEAFISLLSL PDSRFVSEDV LALLDVPVLA ARFDITEEGL RYLRQWVNES
510 520 530 540 550
GIRWGIDDDN VRELELPATG QHTWRFGLTR MLLGYAMESA QGEWQSVLPY
560 570 580 590 600
DESSGLIAEL VGHLASLLMQ LNIWRRGLAQ ERPLEEWLPV CRDMLNAFFL
610 620 630 640 650
PDAETEAAMT LIEQQWQAII AEGLGAQYGD AVPLSLLRDE LAQRLDQERI
660 670 680 690 700
SQRFLAGPVN ICTLMPMRSI PFKVVCLLGM NDGVYPRQLA PLGFDLMSQK
710 720 730 740 750
PKRGDRSRRD DDRYLFLEAL ISAQQKLYIS YIGRSIQDNS ERFPSVLVQE
760 770 780 790 800
LIDYIGQSHY LPGDEALNCD ESEARVKAHL TCLHTRMPFD PQNYQPGERQ
810 820 830 840 850
SYAREWLPAA SQAGKAHSEF VQPLPFTLPE TVPLETLQRF WAHPVRAFFQ
860 870 880 890 900
MRLQVNFRTE DSEIPDTEPF ILEGLSRYQI NQQLLNALVE QDDAERLFRR
910 920 930 940 950
FRAAGDLPYG AFGEIFWETQ CQEMQQLADR VIACRQPGQS MEIDLACNGV
960 970 980 990 1000
QITGWLPQVQ PDGLLRWRPS LLSVAQGMQL WLEHLVYCAS GGNGESRLFL
1010 1020 1030 1040 1050
RKDGEWRFPP LAAEQALHYL SQLIEGYREG MSAPLLVLPE SGGAWLKTCY
1060 1070 1080 1090 1100
DAQNDAMLDD DSTLQKARTK FLQAYEGNMM VRGEGDDIWY QRLWRQLTPE
1110 1120
TMEAIVEQSQ RFLLPLFRFN QS
Length:1,122
Mass (Da):128,848
Last modified:April 1, 1988 - 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:i48B90092DFC1BD21
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti647 – 655QERISQRFL → KNVSASVF in recC-1004; holoenzyme prefers an altered Chi over wild-type Chi sequence. Pseudorevertant of a frameshift mutation at aa 647. 9

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
X03966 Genomic DNA Translation: CAA27604.1
U29581 Genomic DNA Translation: AAB40469.1
U00096 Genomic DNA Translation: AAC75861.1
AP009048 Genomic DNA Translation: BAE76891.1
AF176618 Genomic DNA Translation: AAD54314.1
X06227 Genomic DNA Translation: CAA29575.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A24137 NCECXV

NCBI Reference Sequences

More...
RefSeqi
NP_417299.1, NC_000913.3
WP_000946938.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC75861; AAC75861; b2822
BAE76891; BAE76891; BAE76891

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
947294

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW2790
eco:b2822

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.3914

<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
X03966 Genomic DNA Translation: CAA27604.1
U29581 Genomic DNA Translation: AAB40469.1
U00096 Genomic DNA Translation: AAC75861.1
AP009048 Genomic DNA Translation: BAE76891.1
AF176618 Genomic DNA Translation: AAD54314.1
X06227 Genomic DNA Translation: CAA29575.1
PIRiA24137 NCECXV
RefSeqiNP_417299.1, NC_000913.3
WP_000946938.1, NZ_LN832404.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1W36X-ray3.10C/F1-1122[»]
3K70X-ray3.59C/F1-1122[»]
5LD2electron microscopy3.83C1-1122[»]
5MBVelectron microscopy3.80C1-1122[»]
ProteinModelPortaliP07648
SMRiP07648
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261821, 369 interactors
ComplexPortaliCPX-2197 Exodeoxyribonuclease V complex
DIPiDIP-10650N
IntActiP07648, 3 interactors
MINTiP07648
STRINGi316385.ECDH10B_2992

Chemistry databases

ChEMBLiCHEMBL2095232

Proteomic databases

jPOSTiP07648
PaxDbiP07648
PRIDEiP07648

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75861; AAC75861; b2822
BAE76891; BAE76891; BAE76891
GeneIDi947294
KEGGiecj:JW2790
eco:b2822
PATRICifig|1411691.4.peg.3914

Organism-specific databases

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

More...
EchoBASEi
EB0818
EcoGeneiEG10825 recC

Phylogenomic databases

eggNOGiENOG4105DSY Bacteria
COG1330 LUCA
HOGENOMiHOG000258319
InParanoidiP07648
KOiK03583
PhylomeDBiP07648

Enzyme and pathway databases

BioCyciEcoCyc:EG10825-MONOMER
MetaCyc:EG10825-MONOMER
BRENDAi3.1.11.5 2026

Miscellaneous databases

EvolutionaryTraceiP07648

Protein Ontology

More...
PROi
PR:P07648

Family and domain databases

Gene3Di1.10.10.160, 1 hit
HAMAPiMF_01486 RecC, 1 hit
InterProiView protein in InterPro
IPR013986 DExx_box_DNA_helicase_dom_sf
IPR027417 P-loop_NTPase
IPR006697 RecC
IPR011335 Restrct_endonuc-II-like
PIRSFiPIRSF000980 RecC, 1 hit
SUPFAMiSSF52540 SSF52540, 2 hits
SSF52980 SSF52980, 1 hit
TIGRFAMsiTIGR01450 recC, 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 nameiRECC_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: P07648
Secondary accession number(s): Q2MA15, Q9RNX9
<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 1, 1988
Last sequence update: April 1, 1988
Last modified: January 16, 2019
This is version 156 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. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
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