ID A4G2X2_HERAR Unreviewed; 1045 AA.
AC A4G2X2;
DT 17-APR-2007, integrated into UniProtKB/TrEMBL.
DT 17-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 104.
DE RecName: Full=Error-prone DNA polymerase {ECO:0000256|HAMAP-Rule:MF_01902};
DE EC=2.7.7.7 {ECO:0000256|HAMAP-Rule:MF_01902};
GN Name=dnaE2 {ECO:0000256|HAMAP-Rule:MF_01902,
GN ECO:0000313|EMBL:CAL60859.1};
GN OrderedLocusNames=HEAR0663 {ECO:0000313|EMBL:CAL60859.1};
OS Herminiimonas arsenicoxydans.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Herminiimonas.
OX NCBI_TaxID=204773 {ECO:0000313|EMBL:CAL60859.1, ECO:0000313|Proteomes:UP000006697};
RN [1] {ECO:0000313|EMBL:CAL60859.1, ECO:0000313|Proteomes:UP000006697}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ULPAs1 {ECO:0000313|Proteomes:UP000006697};
RX PubMed=17432936; DOI=10.1371/journal.pgen.0030053;
RA Muller D., Medigue C., Koechler S., Barbe V., Barakat M., Talla E.,
RA Bonnefoy V., Krin E., Arsene-Ploetze F., Carapito C., Chandler M.,
RA Cournoyer B., Cruveiller S., Dossat C., Duval S., Heymann M., Leize E.,
RA Lieutaud A., Lievremont D., Makita Y., Mangenot S., Nitschke W., Ortet P.,
RA Perdrial N., Schoepp B., Siguier N., Simeonova D.D., Rouy Z., Segurens B.,
RA Turlin E., Vallenet D., Van Dorsselaer A., Weiss S., Weissenbach J.,
RA Lett M.C., Danchin A., Bertin P.N.;
RT "A tale of two oxidation states: bacterial colonization of arsenic-rich
RT environments.";
RL PLoS Genet. 3:518-530(2007).
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|HAMAP-Rule:MF_01902}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-C family. DnaE2
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01902}.
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DR EMBL; CU207211; CAL60859.1; -; Genomic_DNA.
DR AlphaFoldDB; A4G2X2; -.
DR STRING; 204773.HEAR0663; -.
DR KEGG; har:HEAR0663; -.
DR eggNOG; COG0587; Bacteria.
DR HOGENOM; CLU_001600_4_0_4; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000006697; Chromosome.
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: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; 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 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:UP000006697};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01902}.
FT DOMAIN 9..76
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1045 AA; 117821 MW; 1AF303E397DF06A2 CRC64;
MPPFLPAYAE LHCRSNFTFL QGASHPEELV QRACDLGYDS LAITDECSLA GVVRAYVEAK
KHNLHLIIGS DITLSCGTRL VFLATNRNGY GNLSELITLG RRRADKGFYT LHRSDLDPDE
RQEPNSIHLA QLPDCLAILI PKCCCSREEI ARQAAWLART FVGRAWVAAE LLHWSDDEYW
LDLLTGIAAE MDLPLVATGD VLMHVRSRKP LQDTLTAVRL GKSVAECGMD LQPNAEQHLR
SRLRLAQLYS PELLQETLTL AKLCTFSLDE LRYQYPEEIV PAGETLSSYL RRLTYEGATQ
RRFRQGIPAN IRQQIEHELV LITELNYEPF FLTVYDIVKF ARSKGILCQG RGSAANSVVC
YCLGITEVDP ARSSVLFERF ISRERNEPPD IDVDFEHQRR EEVIQYIYNK YGRHRAALTA
ALITYRPRSA MKDVGKALGL DFEQVNRLSQ SHKWWDGREI SDERLQEGGF DPQAPIVQKL
VELTKTLIGF PRHLSQHTGG FVIARDSLAR LVPIENASMK DRSVIEWDKD DLDALGLLKV
DVLALGMLSA IQRALEMIST RRGRMVEMQD IPSEDPLTYE MISAADTIGV FQIESRAQMS
MLPRLRPQKY YDLVVQVAIV RPGPIQGGMV HPYLKQRHMH PDDIVYPGPE IKEALSRTFG
VPIFQEQVMQ IAVLAAGYTP GEADELRRSM AAWKRKGNLE KHGDKLKKGL AKNGYDPEFA
NRLFEQIKGF GEYGFPESHA ASFALLVYVS AWIKRHEPAA FLAALLNSQP MGFYSASQLV
QDAKRHGVPV RPIDVLISEL ESTMEDIHER YPAVRLGLHM VKGLSLDGAK RIIEARAHQS
FKDVDDLARR AELDQHELGA LARANALLPL SGHRRQAKWE VAAMMSAPML LRDAPIREEP
LLLPAASEGQ EIVADYASTG LTLNRHPLAL LRPRLKKMNL STALEMKGFA DRKIARTTGI
VTMRQRPPTA KGTMFVTLED ETGITNVIIW PALVEKQRKE ILNSQLMTVY GIWQCKEEVR
HLVAKRIVDH SELLGDLSVS SRDFQ
//
