| Tag | Content |
|---|
| CPLM ID | CPLM-004121 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Nuclease SbcCD subunit C |
Protein Synonyms/Alias | |
Gene Name | sbcC |
Gene Synonyms/Alias | rmuA; b0397; JW0387 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 165 | FAAFLNAKPKERAEL | acetylation | [1] | | 1040 | INGLGYSKLESTFAV | 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 | SbcCD cleaves DNA hairpin structures. These structures can inhibit DNA replication and are intermediates in certain DNA recombination reactions. The complex acts as a 3'->5' double strand exonuclease that can open hairpins. It also has a 5' single-strand endonuclease activity. |
Sequence Annotation | NP_BIND 37 44 ATP (Potential). |
Keyword | ATP-binding; Coiled coil; Complete proteome; DNA recombination; DNA replication; Endonuclease; Exonuclease; Hydrolase; Nuclease; Nucleotide-binding; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 1048 AA |
Protein Sequence | MKILSLRLKN LNSLKGEWKI DFTREPFASN GLFAITGPTG AGKTTLLDAI CLALYHETPR 60
LSNVSQSQND LMTRDTAECL AEVEFEVKGE AYRAFWSQNR ARNQPDGNLQ VPRVELARCA 120
DGKILADKVK DKLELTATLT GLDYGRFTRS MLLSQGQFAA FLNAKPKERA ELLEELTGTE 180
IYGQISAMVF EQHKSARTEL EKLQAQASGV TLLTPEQVQS LTASLQVLTD EEKQLITAQQ 240
QEQQSLNWLT RQDELQQEAS RRQQALQQAL AEEEKAQPQL AALSLAQPAR NLRPHWERIA 300
EHSAALAHIR QQIEEVNTRL QSTMALRASI RHHAAKQSAE LQQQQQSLNT WLQEHDRFRQ 360
WNNEPAGWRA QFSQQTSDRE HLRQWQQQLT HAEQKLNALA AITLTLTADE VATALAQHAE 420
QRPLRQHLVA LHGQIVPQQK RLAQLQVAIQ NVTQEQTQRN AALNEMRQRY KEKTQQLADV 480
KTICEQEARI KTLEAQRAQL QAGQPCPLCG STSHPAVEAY QALEPGVNQS RLLALENEVK 540
KLGEEGATLR GQLDAITKQL QRDENEAQSL RQDEQALTQQ WQAVTASLNI TLQPLDDIQP 600
WLDAQDEHER QLRLLSQRHE LQGQIAAHNQ QIIQYQQQIE QRQQLLLTTL TGYALTLPQE 660
DEEESWLATR QQEAQSWQQR QNELTALQNR IQQLTPILET LPQSDELPHC EETVVLENWR 720
QVHEQCLALH SQQQTLQQQD VLAAQSLQKA QAQFDTALQA SVFDDQQAFL AALMDEQTLT 780
QLEQLKQNLE NQRRQAQTLV TQTAETLAQH QQHRPDDGLA LTVTVEQIQQ ELAQTHQKLR 840
ENTTSQGEIR QQLKQDADNR QQQQTLMQQI AQMTQQVEDW GYLNSLIGSK EGDKFRKFAQ 900
GLTLDNLVHL ANQQLTRLHG RYLLQRKASE ALEVEVVDTW QADAVRDTRT LSGGESFLVS 960
LALALALSDL VSHKTRIDSL FLDEGFGTLD SETLDTALDA LDALNASGKT IGVISHVEAM 1020
KERIPVQIKV KKINGLGYSK LESTFAVK 1048 |
Gene Ontology | GO:0008296; F:3'-5'-exodeoxyribonuclease activity; IDA:EcoCyc. GO:0005524; F:ATP binding; IEA:UniProtKB-KW. GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW. GO:0006260; P:DNA replication; IEA:UniProtKB-KW. GO:0000725; P:recombinational repair; IDA:EcoCyc. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |