| Tag | Content |
|---|
| CPLM ID | CPLM-002519 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Exodeoxyribonuclease V gamma chain |
Protein Synonyms/Alias | Exodeoxyribonuclease V 125 kDa polypeptide |
Gene Name | recC |
Gene Synonyms/Alias | b2822; JW2790 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 252 | RYYWGDIKDPAYLAK | acetylation | [1] | | 1070 | TLQKARTKFLQAYEG | 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 | Exhibits a wide variety of catalytic activities including ATP-dependent exonuclease, ATP-stimulated endonuclease, ATP-dependent helicase and DNA-dependent ATPase activities. |
Sequence Annotation | |
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 | 1122 AA |
Protein Sequence | MLRVYHSNRL DVLEALMEFI VERERLDDPF EPEMILVQST GMAQWLQMTL SQKFGIAANI 60
DFPLPASFIW DMFVRVLPEI PKESAFNKQS MSWKLMTLLP QLLEREDFTL LRHYLTDDSD 120
KRKLFQLSSK AADLFDQYLV YRPDWLAQWE TGHLVEGLGE AQAWQAPLWK ALVEYTHQLG 180
QPRWHRANLY QRFIETLESA TTCPPGLPSR VFICGISALP PVYLQALQAL GKHIEIHLLF 240
TNPCRYYWGD IKDPAYLAKL LTRQRRHSFE DRELPLFRDS ENAGQLFNSD GEQDVGNPLL 300
ASWGKLGRDY IYLLSDLESS QELDAFVDVT PDNLLHNIQS DILELENRAV AGVNIEEFSR 360
SDNKRPLDPL DSSITFHVCH SPQREVEVLH DRLLAMLEED PTLTPRDIIV MVADIDSYSP 420
FIQAVFGSAP ADRYLPYAIS DRRARQSHPV LEAFISLLSL PDSRFVSEDV LALLDVPVLA 480
ARFDITEEGL RYLRQWVNES GIRWGIDDDN VRELELPATG QHTWRFGLTR MLLGYAMESA 540
QGEWQSVLPY DESSGLIAEL VGHLASLLMQ LNIWRRGLAQ ERPLEEWLPV CRDMLNAFFL 600
PDAETEAAMT LIEQQWQAII AEGLGAQYGD AVPLSLLRDE LAQRLDQERI SQRFLAGPVN 660
ICTLMPMRSI PFKVVCLLGM NDGVYPRQLA PLGFDLMSQK PKRGDRSRRD DDRYLFLEAL 720
ISAQQKLYIS YIGRSIQDNS ERFPSVLVQE LIDYIGQSHY LPGDEALNCD ESEARVKAHL 780
TCLHTRMPFD PQNYQPGERQ SYAREWLPAA SQAGKAHSEF VQPLPFTLPE TVPLETLQRF 840
WAHPVRAFFQ MRLQVNFRTE DSEIPDTEPF ILEGLSRYQI NQQLLNALVE QDDAERLFRR 900
FRAAGDLPYG AFGEIFWETQ CQEMQQLADR VIACRQPGQS MEIDLACNGV QITGWLPQVQ 960
PDGLLRWRPS LLSVAQGMQL WLEHLVYCAS GGNGESRLFL RKDGEWRFPP LAAEQALHYL 1020
SQLIEGYREG MSAPLLVLPE SGGAWLKTCY DAQNDAMLDD DSTLQKARTK FLQAYEGNMM 1080
VRGEGDDIWY QRLWRQLTPE TMEAIVEQSQ RFLLPLFRFN QS 1122 |
Gene Ontology | GO:0009338; C:exodeoxyribonuclease V complex; IDA:EcoCyc. GO:0005524; F:ATP binding; IEA:UniProtKB-KW. GO:0004003; F:ATP-dependent DNA helicase activity; IDA:EcoCyc. GO:0004519; F:endonuclease activity; IDA:EcoCyc. GO:0008854; F:exodeoxyribonuclease V activity; IDA:EcoCyc. GO:0006310; P:DNA recombination; IMP:EcoCyc. GO:0006302; P:double-strand break repair; IDA:EcoCyc. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |