ID A0A1B9R1H6_9VIBR Unreviewed; 1033 AA.
AC A0A1B9R1H6;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
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=A6E14_06495 {ECO:0000313|EMBL:OCH78041.1};
OS Vibrio genomosp. F10.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=723171 {ECO:0000313|EMBL:OCH78041.1, ECO:0000313|Proteomes:UP000093173};
RN [1] {ECO:0000313|Proteomes:UP000093173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=9CSC122 {ECO:0000313|Proteomes:UP000093173};
RA Hehemann J.-H., Arevalo P., Datta M.S., Polz M.F.;
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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:OCH78041.1}.
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DR EMBL; MAJZ01000317; OCH78041.1; -; Genomic_DNA.
DR RefSeq; WP_065576489.1; NZ_MAJZ01000317.1.
DR AlphaFoldDB; A0A1B9R1H6; -.
DR Proteomes; UP000093173; 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 Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 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; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004365; NA-bd_OB_tRNA.
DR InterPro; IPR004013; PHP_dom.
DR InterPro; IPR003141; Pol/His_phosphatase_N.
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.
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:UP000093173};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01902}.
FT DOMAIN 4..73
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1033 AA; 117490 MW; DFA250E0144F718D CRC64;
MKYAELFCQS NFSFLTGASH AEELVIQADF LRYQAIAITD ECSVAGVVRA HTAIKDHHLA
IKQIIGSMFW LNAECQLVLL CPNRQAYAEL CRIITNARRR ANKGEYQLSE WDIMSVQHCL
IIWLPCHHSI DRHWGKWLNQ HHADRLWLGL QRHLNGNDKE YTAHCQTLAT EFQLPITACG
GVLMHTATRL PLQHTLTAIK HGSTLDAIGE HMLTNTERAL RSQEKLARIF KPEWLAETEH
IAQRCQFDLA SLRYEYPSEL IPNQMTPIGY LRQLTAQGKH LRFPNGVPDS IDQIIEKELT
LIEQLDYAFF FLTIHDIVMF AKRQGILYQG RGSAANSVVC YCLEITSVDP RQVSVLFERF
ISKERAEPPD IDVDFEHERR EEVIQYIYKK YGRERAALAA SVISYRLKSA IRDIGKTLGI
NDTQLDFFIK NINRRDHQLG WQAQLIELGL KPDSLKGEHF ITLVNDIIGF PRHLSQHVGG
FVISSGPLYE LVPIENAAMD QRTVIQWDKD DLESLGLLKV DVLALGMLTA IRKCFSLIQQ
YHGQSLSIAD ITRKEDDPNV YGMIQRADTV GVFQIESRAQ MSMLPRLKPK CYYDLVIQIA
IVRPGPIQGD MVHPFLKRRD GIERTSYPSE EVKEVLSRTM GVPIFQEQVI KLAMVAAGFS
GGEADKLRRA MASWKKNGEL FKFKTKLIDG MLARGYELDF AERIFDQICG FGEYGFPESH
SASFAVLAYC SAWLKYYYPE AFYTSLLNSL PMGFYTASQL IQDAKRHHIT VLPVCINHSD
YDHLVVAHSS VLAIRLGLRQ IKGVTQDGMQ QLIKARPPQG YQSPSQLQHI GINKRDIELL
ASANAMHSFA HNRYQARWSM MDSITDLPLF QHEVETEDDK MQNHPIQNHR LETPSDMQTL
MEDLSSTGVS LDLHPITLLD NARQLSPFTR MTNLMNKDHQ SMVTVVGLVT GRQSPGTAAG
VTFFTLEDDT GNINVVVWKA TARAQKQAYL TAKILMVKGI LEKEGNVTHI IAGRLIDLTQ
HFEHLDTRSR DFH
//
