ID A0A1H8RZ23_9GAMM Unreviewed; 1021 AA.
AC A0A1H8RZ23;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
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=SAMN04488052_102349 {ECO:0000313|EMBL:SEO71526.1};
OS Aquisalimonas asiatica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Aquisalimonas.
OX NCBI_TaxID=406100 {ECO:0000313|EMBL:SEO71526.1, ECO:0000313|Proteomes:UP000199657};
RN [1] {ECO:0000313|EMBL:SEO71526.1, ECO:0000313|Proteomes:UP000199657}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.6291 {ECO:0000313|EMBL:SEO71526.1,
RC ECO:0000313|Proteomes:UP000199657};
RA de Groot N.N.;
RL Submitted (OCT-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}.
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DR EMBL; FOEG01000002; SEO71526.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H8RZ23; -.
DR STRING; 406100.SAMN04488052_102349; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000199657; 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:UP000199657};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01902}.
FT DOMAIN 4..71
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1021 AA; 112704 MW; 11F692418478EACB CRC64;
MAYTELHCIT NFTFLRGASH PEELVARAAE LGYDGLAITD ECSVAGAVRA HGAARGHGLQ
LIIGSEIRLA DGPVVVLIAP HRQAYSQLSA LISLGRTSAP KGSYRLHRSD LEQSVPDCLA
LLIPETPATP EHAAWFGAHF RGRGWIAVHL HNGPDDAARL AELNHLATCS GLPLVAAGGV
HMHRRGRRAL QDTLTAIRHN RPVQELGYAL MSNGERHLRP LRRLQRLYPD ALLAETHHIA
AQCTFSLDEL RYEYPEELVP PGSTPAAHLR ALVTDGARRR WPGGTPAHVD ALLERELALI
AELRYEAYFL TVHDVVAFAR SRGILCQGRG SAANSAVCFA LGVTEVDPAD SQLLFERFIS
RDRGEPPDID VDFEHERREE VIQYIYRKYG RHRAALAATV ISYRPRSALR DVGRALGLEP
DQTERLAGAV QWWDGSDIAP DRIREAGFDP DNPVIHRVLT LTRELLGFPR HLSQHVGGFV
ISRGPLAELV PTENAAMEGR SVIQWDKDDL ESLGLLKVDV LALGMLSAIR RAFHLLEHHY
GITRTMADIP RNDDPYFAML QRGDSMGVFQ VESRAQMAML PRLKPECFYD LVIEVAIVRP
GPIQGDMVHP YLQRRDAPEQ ANYPSPEVED VLKRTLGVPI FQEQVMKLAE VAAGFTPDEA
DQLRRSMAAW RKRGGLGHFE QRLHDGMRAN GYSDAFAARI FRQIQGFGEY GFPESHAASF
ALLVCVSAWL KCHYPAVFTC ALLNSQPMGF YAPAQLVRDA REHGVAVRPV DVTTSQWDCT
LEPTAGDQAL RLGLRMVKGL SRDGADRLIA ARDTAALRTV EDLAHRAELG QRDLSALANA
GALEPLSGHR RNAWWQVLGV DREHPLVARA GHGDDTPPLE RPSTGEDLIA DYGSTGLTLG
PHPVALLREQ LQRRRFRSAA DLNTLDNAPV ARAAGIVTNR QRPGSAGGVT FVTLEDETGT
INVVVWRRLA EAQRRVLLGA RLLGVVGQWE RRNGVCHLIA GRLEDHSALL GGLQTRSRDF
H
//
