| Tag | Content |
|---|
| CPLM ID | CPLM-002648 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Exodeoxyribonuclease V beta chain |
Protein Synonyms/Alias | Exodeoxyribonuclease V 135 kDa polypeptide |
Gene Name | recB |
Gene Synonyms/Alias | rorA; b2820; JW2788 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 268 | NQAKWIDKISAWAEE | acetylation | [1] | | 288 | QLPESLEKFSQRFLE | acetylation | [1] |
|
Reference | [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli. Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C. Mol Cell. 2013 Jul 25;51(2):265-72. [ PMID: 23830618] |
Functional Description | Required for efficient DNA repair; it catalyzes the unwinding of double-stranded DNA and the cleavage of single- stranded DNA and it stimulates local genetic recombination. All of these activities require concomitant hydrolysis of ATP. |
Sequence Annotation | DOMAIN 2 450 UvrD-like helicase ATP-binding.
DOMAIN 480 746 UvrD-like helicase C-terminal.
NP_BIND 23 30 ATP. |
Keyword | 3D-structure; ATP-binding; Complete proteome; DNA damage; DNA repair; Endonuclease; Exonuclease; Helicase; Hydrolase; Nuclease; Nucleotide-binding; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 1180 AA |
Protein Sequence | MSDVAETLDP LRLPLQGERL IEASAGTGKT FTIAALYLRL LLGLGGSAAF PRPLTVEELL 60
VVTFTEAATA ELRGRIRSNI HELRIACLRE TTDNPLYERL LEEIDDKAQA AQWLLLAERQ 120
MDEAAVFTIH GFCQRMLNLN AFESGMLFEQ QLIEDESLLR YQACADFWRR HCYPLPREIA 180
QVVFETWKGP QALLRDINRY LQGEAPVIKA PPPDDETLAS RHAQIVARID TVKQQWRDAV 240
GELDALIESS GIDRRKFNRS NQAKWIDKIS AWAEEETNSY QLPESLEKFS QRFLEDRTKA 300
GGETPRHPLF EAIDQLLAEP LSIRDLVITR ALAEIRETVA REKRRRGELG FDDMLSRLDS 360
ALRSESGEVL AAAIRTRFPV AMIDEFQDTD PQQYRIFRRI WHHQPETALL LIGDPKQAIY 420
AFRGADIFTY MKARSEVHAH YTLDTNWRSA PGMVNSVNKL FSQTDDAFMF REIPFIPVKS 480
AGKNQALRFV FKGETQPAMK MWLMEGESCG VGDYQSTMAQ VCAAQIRDWL QAGQRGEALL 540
MNGDDARPVR ASDISVLVRS RQEAAQVRDA LTLLEIPSVY LSNRDSVFET LEAQEMLWLL 600
QAVMTPEREN TLRSALATSM MGLNALDIET LNNDEHAWDV VVEEFDGYRQ IWRKRGVMPM 660
LRALMSARNI AENLLATAGG ERRLTDILHI SELLQEAGTQ LESEHALVRW LSQHILEPDS 720
NASSQQMRLE SDKHLVQIVT IHKSKGLEYP LVWLPFITNF RVQEQAFYHD RHSFEAVLDL 780
NAAPESVDLA EAERLAEDLR LLYVALTRSV WHCSLGVAPL VRRRGDKKGD TDVHQSALGR 840
LLQKGEPQDA AGLRTCIEAL CDDDIAWQTA QTGDNQPWQV NDVSTAELNA KTLQRLPGDN 900
WRVTSYSGLQ QRGHGIAQDL MPRLDVDAAG VASVVEEPTL TPHQFPRGAS PGTFLHSLFE 960
DLDFTQPVDP NWVREKLELG GFESQWEPVL TEWITAVLQA PLNETGVSLS QLSARNKQVE 1020
MEFYLPISEP LIASQLDTLI RQFDPLSAGC PPLEFMQVRG MLKGFIDLVF RHEGRYYLLD 1080
YKSNWLGEDS SAYTQQAMAA AMQAHRYDLQ YQLYTLALHR YLRHRIADYD YEHHFGGVIY 1140
LFLRGVDKEH PQQGIYTTRP NAGLIALMDE MFAGMTLEEA 1180 |
Gene Ontology | GO:0009338; C:exodeoxyribonuclease V complex; IDA:EcoCyc. GO:0005524; F:ATP binding; IDA:EcoliWiki. GO:0004003; F:ATP-dependent DNA helicase activity; IDA:EcoCyc. GO:0003677; F:DNA binding; IEA:InterPro. GO:0004519; F:endonuclease activity; IMP:EcoCyc. GO:0008854; F:exodeoxyribonuclease V activity; IMP:EcoCyc. GO:0006310; P:DNA recombination; IMP:EcoCyc. GO:0006302; P:double-strand break repair; IDA:EcoCyc. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |