ID A0A432ZF07_9GAMM Unreviewed; 1036 AA.
AC A0A432ZF07;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=Error-prone DNA polymerase {ECO:0000256|ARBA:ARBA00017273, ECO:0000256|HAMAP-Rule:MF_01902};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417, ECO:0000256|HAMAP-Rule:MF_01902};
GN Name=dnaE2 {ECO:0000256|HAMAP-Rule:MF_01902};
GN ORFNames=CWI83_09210 {ECO:0000313|EMBL:RUO76523.1};
OS Pseudidiomarina taiwanensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Idiomarinaceae; Pseudidiomarina.
OX NCBI_TaxID=337250 {ECO:0000313|EMBL:RUO76523.1, ECO:0000313|Proteomes:UP000288279};
RN [1] {ECO:0000313|EMBL:RUO76523.1, ECO:0000313|Proteomes:UP000288279}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PIT1 {ECO:0000313|EMBL:RUO76523.1,
RC ECO:0000313|Proteomes:UP000288279};
RX PubMed=30364313; DOI=.3389/fmicb.2018.02453;
RA Liu Y., Lai Q., Shao Z.;
RT "Genome-Based Analysis Reveals the Taxonomy and Diversity of the Family
RT Idiomarinaceae.";
RL Front. Microbiol. 9:2453-2453(2018).
CC -!- FUNCTION: DNA polymerase involved in damage-induced mutagenesis and
CC translesion synthesis (TLS). It is not the major replicative DNA
CC polymerase. {ECO:0000256|HAMAP-Rule:MF_01902}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC ChEBI:CHEBI:173112; EC=2.7.7.7;
CC Evidence={ECO:0000256|ARBA:ARBA00024632, ECO:0000256|HAMAP-
CC Rule:MF_01902};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_01902}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-C family. DnaE2
CC subfamily. {ECO:0000256|ARBA:ARBA00007391, ECO:0000256|HAMAP-
CC Rule:MF_01902}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RUO76523.1}.
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DR EMBL; PIQG01000004; RUO76523.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A432ZF07; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000288279; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd04485; DnaE_OBF; 1.
DR CDD; cd07434; PHP_PolIIIA_DnaE2; 1.
DR Gene3D; 1.10.150.870; -; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR HAMAP; MF_01902; DNApol_error_prone; 1.
DR InterPro; IPR011708; DNA_pol3_alpha_NTPase_dom.
DR InterPro; IPR040982; DNA_pol3_finger.
DR InterPro; IPR023073; DnaE2.
DR InterPro; IPR004805; DnaE2/DnaE/PolC.
DR InterPro; IPR029460; DNAPol_HHH.
DR InterPro; IPR004365; NA-bd_OB_tRNA.
DR InterPro; IPR004013; PHP_dom.
DR InterPro; IPR003141; Pol/His_phosphatase_N.
DR InterPro; IPR016195; Pol/histidinol_Pase-like.
DR NCBIfam; TIGR00594; polc; 1.
DR PANTHER; PTHR32294; DNA POLYMERASE III SUBUNIT ALPHA; 1.
DR PANTHER; PTHR32294:SF4; ERROR-PRONE DNA POLYMERASE; 1.
DR Pfam; PF07733; DNA_pol3_alpha; 1.
DR Pfam; PF17657; DNA_pol3_finger; 1.
DR Pfam; PF14579; HHH_6; 1.
DR Pfam; PF02811; PHP; 1.
DR Pfam; PF01336; tRNA_anti-codon; 1.
DR SMART; SM00481; POLIIIAc; 1.
DR SUPFAM; SSF89550; PHP domain-like; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01902};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW Rule:MF_01902};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW Rule:MF_01902};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|HAMAP-
KW Rule:MF_01902};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW ECO:0000256|HAMAP-Rule:MF_01902};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW Rule:MF_01902}; Reference proteome {ECO:0000313|Proteomes:UP000288279};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01902}.
FT DOMAIN 8..77
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1036 AA; 117696 MW; 62F75DB0A89F873D CRC64;
MAGSVNPVAL NCLSYYSFLR GASSPAELIE QAAELGYQAL AITDECSLAG VVRAYVANQQ
LPSPLQLLIG SSFDLAEQGR WVVLVRDHQG YTQLCELITK ARSRCSKGAY QLGLDDLAEL
DPNHVILLWR PELTGAMATV TQHLLPRFEG ALYLAFSRHY HSDDAARYRA YQHYHQVTGL
PIVAACEVLY HQRQQQPLFD VMQAIRERQA VTQIVEHLPA NHEYCLRSVA ELQQCYPHAW
LEQAGFIAQK CHFCLSELRY QYPSELVPEG QTATAYLREL TYAGAKRRFP DGLSADVQAK
LEKELGLIEQ LEYEYFFLTI YDIVQFAQQR GILYQGRGSA ANSVVCYCLE ITAVNPAQID
VLFERFISAE RDEPPDIDVD FEHQRREEVI QYIYQKYGRK RAALAATVVR YRLKSAFRDV
GKALGFREQA LRHYLQRIDR RDREYHWREQ LLEQVPELVQ TQRGRWLLDL TQALIGTPRH
LSQHVGGFVI ASRSLAELVP VENASMPERT VIQWDKDDIE ALRLIKVDIL ALGMLSALQK
MLTYVRGYGQ TAAEQQLSLA TIPTEDPKVY QMLQQADSIG IFQIESRAQM NMLPRLKPAT
FYDLVVQIAI VRPGPIQGDM VHPYLRRRAG LEPIEYPSAA VKQVLERTLG VPIFQEQVIK
LAMVAAGFSG GEADQLRRAM ANWQRSGKLK KFERKLIEGM RARGYSDDFA KRIYQQILGF
GEYGFPESHS ASFANLAYAS AWMKYHHPAA FYCALLNSLP MGFYSADQLL QDAKRHHVPL
LPVDIQFSQW DHQLVELTER RSLRLGLRLI KGLSRQRIEA LIAQRPPQGF QSLQQLQHCG
ARRHELQALA AADALAGVSG HRYQSQWQSL AVQEQPPLFA ELLDDLNDEQ VAAPTEIEDI
RADYQHLGLS LRRHPLAILR EQGKLRGYKT AAELSTCRSG QFVQISGLVT CRQRPGTSSG
VTFITLEDET GQANIVIWLA TARQFRQAYL RARLLKVKGV VEIHAGVVHV IAGQLFDESE
HLRPFQLDRK RSRDFH
//
