Tag | Content |
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CPLM ID | CPLM-001797 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | DNA polymerase I |
Protein Synonyms/Alias | POL I |
Gene Name | polA |
Gene Synonyms/Alias | resA; b3863; JW3835 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
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54 | RSLIMQYKPTHAAVV | acetylation | [1] | 65 | AAVVFDAKGKTFRDE | acetylation | [1] | 67 | VVFDAKGKTFRDELF | acetylation | [1] | 127 | TLAREAEKAGRPVLI | acetylation | [1] | 139 | VLISTGDKDMAQLVT | acetylation | [1] | 230 | GLSFRGAKTMAAKLE | acetylation | [1] | 235 | GAKTMAAKLEQNKEV | acetylation | [1] | 240 | AAKLEQNKEVAYLSY | acetylation | [1] | 295 | TADVEAGKWLQAKGA | acetylation | [1] | 345 | TLKAWIAKLEKAPVF | acetylation | [1] | 406 | ERALELLKPLLEDEK | acetylation | [1] | 413 | KPLLEDEKALKVGQN | acetylation | [1] | 422 | LKVGQNLKYDRGILA | acetylation | [1] | 481 | EEIAGKGKNQLTFNQ | acetylation | [1] | 518 | KMWPDLQKHKGPLNV | acetylation | [1] | 520 | WPDLQKHKGPLNVFE | acetylation | [1] | 546 | RIERNGVKIDPKVLH | acetylation | [1] | 550 | NGVKIDPKVLHNHSE | acetylation | [1] | 568 | LRLAELEKKAHEIAG | acetylation | [1] | 593 | LQTILFEKQGIKPLK | acetylation | [1] | 643 | LKSTYTDKLPLMINP | acetylation | [1] | 721 | MAHLSRDKGLLTAFA | acetylation | [1] | 731 | LTAFAEGKDIHRATA | acetylation | [1] | 786 | IPRKEAQKYMDLYFE | acetylation | [1] | 810 | ERTRAQAKEQGYVET | acetylation | [1] | 829 | RLYLPDIKSSNGARR | acetylation | [1] |
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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 | In addition to polymerase activity, this DNA polymerase exhibits 3' to 5' and 5' to 3' exonuclease activity. It is able to utilize nicked circular duplex DNA as a template and can unwind the parental DNA strand from its template. |
Sequence Annotation | DOMAIN 1 323 5'-3' exonuclease. DOMAIN 324 517 3'-5' exonuclease. REGION 324 928 Klenow fragment. REGION 521 928 Polymerase. |
Keyword | 3D-structure; Complete proteome; Direct protein sequencing; DNA damage; DNA repair; DNA replication; DNA-binding; DNA-directed DNA polymerase; Exonuclease; Hydrolase; Nuclease; Nucleotidyltransferase; Reference proteome; Transferase. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 928 AA |
Protein Sequence | MVQIPQNPLI LVDGSSYLYR AYHAFPPLTN SAGEPTGAMY GVLNMLRSLI MQYKPTHAAV 60 VFDAKGKTFR DELFEHYKSH RPPMPDDLRA QIEPLHAMVK AMGLPLLAVS GVEADDVIGT 120 LAREAEKAGR PVLISTGDKD MAQLVTPNIT LINTMTNTIL GPEEVVNKYG VPPELIIDFL 180 ALMGDSSDNI PGVPGVGEKT AQALLQGLGG LDTLYAEPEK IAGLSFRGAK TMAAKLEQNK 240 EVAYLSYQLA TIKTDVELEL TCEQLEVQQP AAEELLGLFK KYEFKRWTAD VEAGKWLQAK 300 GAKPAAKPQE TSVADEAPEV TATVISYDNY VTILDEETLK AWIAKLEKAP VFAFDTETDS 360 LDNISANLVG LSFAIEPGVA AYIPVAHDYL DAPDQISRER ALELLKPLLE DEKALKVGQN 420 LKYDRGILAN YGIELRGIAF DTMLESYILN SVAGRHDMDS LAERWLKHKT ITFEEIAGKG 480 KNQLTFNQIA LEEAGRYAAE DADVTLQLHL KMWPDLQKHK GPLNVFENIE MPLVPVLSRI 540 ERNGVKIDPK VLHNHSEELT LRLAELEKKA HEIAGEEFNL SSTKQLQTIL FEKQGIKPLK 600 KTPGGAPSTS EEVLEELALD YPLPKVILEY RGLAKLKSTY TDKLPLMINP KTGRVHTSYH 660 QAVTATGRLS STDPNLQNIP VRNEEGRRIR QAFIAPEDYV IVSADYSQIE LRIMAHLSRD 720 KGLLTAFAEG KDIHRATAAE VFGLPLETVT SEQRRSAKAI NFGLIYGMSA FGLARQLNIP 780 RKEAQKYMDL YFERYPGVLE YMERTRAQAK EQGYVETLDG RRLYLPDIKS SNGARRAAAE 840 RAAINAPMQG TAADIIKRAM IAVDAWLQAE QPRVRMIMQV HDELVFEVHK DDVDAVAKQI 900 HQLMENCTRL DVPLLVEVGS GENWDQAH 928 |
Gene Ontology | |
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