Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 95 (11 Dec 2019)
Sequence version 1 (09 Jan 2007)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

RecBCD enzyme subunit RecB

Gene

recB

Organism
Francisella tularensis subsp. novicida (strain U112)
Status
Unreviewed-Annotation score:

Annotation score:3 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>
-Protein inferred from homologyi <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 highly rapid and processive ATP-dependent bidirectional helicase activity. Unwinds dsDNA until it encounters a Chi (crossover hotspot instigator) sequence from the 3' direction. Cuts ssDNA a few nucleotides 3' to the Chi site. The properties and activities of the enzyme are changed at Chi. The Chi-altered holoenzyme produces a long 3'-ssDNA overhang and facilitates RecA-binding to the ssDNA for homologous DNA recombination and repair. Holoenzyme degrades any linearized DNA that is unable to undergo homologous recombination. In the holoenzyme this subunit contributes ATPase, 3'-5' helicase, exonuclease activity and loads RecA onto ssDNA.UniRule annotation

<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 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

Mg2+UniRule annotationNote: Binds 1 Mg2+ ion per subunit.UniRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi944Magnesium; via tele nitrogenUniRule annotation1
Metal bindingi1108MagnesiumUniRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei1121For nuclease activityUniRule annotation1
Metal bindingi1121MagnesiumUniRule annotation1

<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 functionDNA-bindingUniRule annotationSAAS annotation, ExonucleaseUniRule annotationSAAS annotationImported, HelicaseUniRule annotationSAAS annotation, Hydrolase, Nuclease
Biological processDNA damage, DNA repairUniRule annotationSAAS annotation
LigandATP-binding, MagnesiumUniRule annotation, Metal-bindingUniRule annotation, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
FTUL401614:G1G75-1402-MONOMER

<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 RecBUniRule annotation (EC:3.1.11.5UniRule annotation)
Alternative name(s):
Exonuclease V subunit RecBUniRule annotation
Short name:
ExoV subunit RecBUniRule annotation
Helicase/nuclease RecBCD subunit RecBUniRule 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:recBUniRule annotationImported
Ordered Locus Names:FTN_1357Imported
<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>OrganismiFrancisella tularensis subsp. novicida (strain U112)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 identifieri401614 [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 lineageiBacteriaProteobacteriaGammaproteobacteriaThiotrichalesFrancisellaceaeFrancisella
<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
  • UP000000762 <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 describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
A0Q7L7

<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 RecA.

UniRule annotation

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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini1 – 447UvrD-like helicase ATP-bindingInterPro annotationAdd BLAST447
Domaini481 – 735UvrD-like helicase C-terminalInterPro annotationAdd BLAST255

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>Regioni1 – 852DNA-binding and helicase activity, interacts with RecCUniRule annotationAdd BLAST852
Regioni889 – 1216Nuclease activity, interacts with RecD and RecAUniRule annotationAdd BLAST328

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and domains’ section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili898 – 925Sequence analysisAdd BLAST28

<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 C-terminal domain has nuclease activity and interacts with RecD. It interacts with RecA, facilitating its loading onto ssDNA.UniRule annotation
The N-terminal DNA-binding domain is a ssDNA-dependent ATPase and has ATP-dependent 3'-5' helicase function. This domain interacts with RecC.UniRule annotation

<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 helicase family. UvrD subfamily.UniRule annotationSAAS annotation

Keywords - Domaini

Coiled coilSequence analysis

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000066038

KEGG Orthology (KO)

More...
KOi
K03582

Identification of Orthologs from Complete Genome Data

More...
OMAi
KQSIYRW

Database of Orthologous Groups

More...
OrthoDBi
137860at2

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.90.320.10, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_01485 RecB, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR014017 DNA_helicase_UvrD-like_C
IPR000212 DNA_helicase_UvrD/REP
IPR011604 Exonuc_phg/RecB_C
IPR027417 P-loop_NTPase
IPR038726 PDDEXK_AddAB-type
IPR004586 RecB
IPR011335 Restrct_endonuc-II-like
IPR014016 UvrD-like_ATP-bd
IPR034739 UvrD/AddA_N

The PANTHER Classification System

More...
PANTHERi
PTHR11070 PTHR11070, 1 hit
PTHR11070:SF23 PTHR11070:SF23, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF12705 PDDEXK_1, 1 hit
PF00580 UvrD-helicase, 1 hit
PF13361 UvrD_C, 1 hit

Superfamily database of structural and functional annotation

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

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00609 recB, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51198 UVRD_HELICASE_ATP_BIND, 1 hit
PS51217 UVRD_HELICASE_CTER, 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.

A0Q7L7-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKNLNANTIT LQGRHIIEAS AGTGKTFNIT KLYIRLLLEK KLLPSNILVM
60 70 80 90 100
TFTKDATQEI IGRVEKEIRD VLASYTDEKK ESDKENYKHL KRSLLEIDEA
110 120 130 140 150
AIFTIHGFCK KVLSEQAFAS GMEMDVSMEV DTSDILQKVV EDFFRKHINK
160 170 180 190 200
SETNFEHLQA YKLHTPDMFL DKLRNVVRSS HELLTKQAIS LDEFKILKKQ
210 220 230 240 250
QLELFINNHD IVDDFLSKLG KGEPQGKRVD EYHRVLEWLK LDNQTLFPEN
260 270 280 290 300
ISIITDGRKI SAKLIKPIFI GVKELRDLQQ EIKQAQAAQF IRKACLQIRE
310 320 330 340 350
SFAKAKEQKG VLDFDDLITK LCQSVKKSPD LVKTLQKQYP VALIDEFQDT
360 370 380 390 400
DAEQYEILDT IYPLKNSSHS HEGGNLLTNG LNLKDTRLRE YDSSSDQNDS
410 420 430 440 450
NLLLLMIGDP KQAIYGFRGG DIFTYLKAKD SCPEENRWSM DTNWRSTGEM
460 470 480 490 500
IKAYNRLFYK QDYQPEEEGQ IGTNIFSDGI GYQLVKASPD ADKKTKDFDD
510 520 530 540 550
NFKPINYFYY EVAEDDNKSD IDTNLSLWTV NEITRLLNTQ KVAENDIAIL
560 570 580 590 600
VENGKQAKII QQALQAKNLS SVYLSQRDNV YHSQEAKEIL ALMEGINDLE
610 620 630 640 650
NKSMLKRALS TSLLGGRADK FISYIDENDV SAWDDEIEKA KSLRQQWHKY
660 670 680 690 700
GFMAFIMQII HENFTQRADS KERIITNILH LAELIKVAEN KYKHPNQLIK
710 720 730 740 750
WYRHQLNNTA TSEGELRLES DDNLIKIITI HGSKGLEYSV VFIPFACYAS
760 770 780 790 800
TKKFETSNFT KYYDSDLKQT VYKIGKDDSV KQQADKEVIE ELMRLFYVAV
810 820 830 840 850
TRAKHRCYIG VAKYNNSEKS PLARFLGYQK DDDWLEKIQS ITANPANQSL
860 870 880 890 900
LINIADMREF SLKNLSSKDK NSDYDTLKAN YISKLENDSW EMLSFSKISK
910 920 930 940 950
SKVQNTALEK EIDEAEDDKT QASDRKLAFR FTASKGADMG NILHNVLEHT
960 970 980 990 1000
DFSLGEIDGN LLKEQMDRYK VVAAEDFDNL KLWLEECLEA HIPYIDTSFS
1010 1020 1030 1040 1050
SSNESIQYGL FDIKDKGFCL KTIPNSKTLK EAEFYFPVKN ENLYKTNILE
1060 1070 1080 1090 1100
ILQEYRELTK LKTYSHSYVG GNLSTNYQDL RDICLREYDN FTNFSNQKIF
1110 1120 1130 1140 1150
GMLHGFIDLI FEYEGKFYVA DYKSNYLGDT LEDYNQQAMQ EKNQSSFYDL
1160 1170 1180 1190 1200
QYLIYSVALD KYLRQNIESY NYEKHFGGVY YFYLRGMKDG YGVYQARPTL
1210
EIINKLASLF NGDDNV
Length:1,216
Mass (Da):140,720
Last modified:January 9, 2007 - 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:i6D4FB8FACDF77D9B
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
CP000439 Genomic DNA Translation: ABK90232.1

NCBI Reference Sequences

More...
RefSeqi
WP_003040212.1, NZ_CP009633.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
ABK90232; ABK90232; FTN_1357

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ftn:FTN_1357
ftx:AW25_646

<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
CP000439 Genomic DNA Translation: ABK90232.1
RefSeqiWP_003040212.1, NZ_CP009633.1

3D structure databases

Database of comparative protein structure models

More...
ModBasei
Search...

SWISS-MODEL Interactive Workspace

More...
SWISS-MODEL-Workspacei
Submit a new modelling project...

Proteomic databases

PRIDEiA0Q7L7

Genome annotation databases

EnsemblBacteriaiABK90232; ABK90232; FTN_1357
KEGGiftn:FTN_1357
ftx:AW25_646

Phylogenomic databases

HOGENOMiHOG000066038
KOiK03582
OMAiKQSIYRW
OrthoDBi137860at2

Enzyme and pathway databases

BioCyciFTUL401614:G1G75-1402-MONOMER

Family and domain databases

Gene3Di3.90.320.10, 1 hit
HAMAPiMF_01485 RecB, 1 hit
InterProiView protein in InterPro
IPR014017 DNA_helicase_UvrD-like_C
IPR000212 DNA_helicase_UvrD/REP
IPR011604 Exonuc_phg/RecB_C
IPR027417 P-loop_NTPase
IPR038726 PDDEXK_AddAB-type
IPR004586 RecB
IPR011335 Restrct_endonuc-II-like
IPR014016 UvrD-like_ATP-bd
IPR034739 UvrD/AddA_N
PANTHERiPTHR11070 PTHR11070, 1 hit
PTHR11070:SF23 PTHR11070:SF23, 1 hit
PfamiView protein in Pfam
PF12705 PDDEXK_1, 1 hit
PF00580 UvrD-helicase, 1 hit
PF13361 UvrD_C, 1 hit
SUPFAMiSSF52540 SSF52540, 1 hit
SSF52980 SSF52980, 1 hit
TIGRFAMsiTIGR00609 recB, 1 hit
PROSITEiView protein in PROSITE
PS51198 UVRD_HELICASE_ATP_BIND, 1 hit
PS51217 UVRD_HELICASE_CTER, 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 nameiA0Q7L7_FRATN
<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: A0Q7L7
<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/TrEMBL: January 9, 2007
Last sequence update: January 9, 2007
Last modified: December 11, 2019
This is version 95 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 statusiUnreviewed (UniProtKB/TrEMBL)
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