ID A0A1G6X694_9GAMM Unreviewed; 1063 AA.
AC A0A1G6X694;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=SAMN04488509_10661 {ECO:0000313|EMBL:SDD73681.1};
OS Aquimonas voraii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Aquimonas.
OX NCBI_TaxID=265719 {ECO:0000313|EMBL:SDD73681.1, ECO:0000313|Proteomes:UP000199603};
RN [1] {ECO:0000313|EMBL:SDD73681.1, ECO:0000313|Proteomes:UP000199603}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16957 {ECO:0000313|EMBL:SDD73681.1,
RC ECO:0000313|Proteomes:UP000199603};
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; FNAG01000006; SDD73681.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G6X694; -.
DR STRING; 265719.SAMN04488509_10661; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000199603; 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:UP000199603};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01902}.
FT DOMAIN 40..107
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1063 AA; 118122 MW; 611A213E8D96BEA8 CRC64;
MAATDNLVPL PRTPSRDSTR GEAPPRPSPK RPRSTTPPYA ELHCLSNFSF GRGASSAMEL
FERARAQGYS ALAITDECSL AGIVRAYEAA KATDLKLIVG AEFSTRDRAF KCVLLVEDSS
GYTALCELIT RARRRSEKGE YRFERADLEP APPGLLLLWI PQALAEAELV AQGQALAQQW
RDRCWLAVEL HRGPDDEAHK RQRLDLAARC GLPAVACGDA HMHIRARRPL QDCLTALRHR
LSVVQARGLL FPNGERHLRT RRALLAIYGD GLMAETLAIA ERCCFSLGEI RYRYPREVVP
EGHTPDSWLR ALTEQGARWR WPQGVPDTVQ AQIEKELAII AELDYAAYFL TVHDIVRFAR
ERGILCQGRG SAANSAVCFA LGVTEVDPAH SQLLFERFLS KERNEPPDID IDFEHQRREE
VIQYLYTRYG RERAALAATV ICYRSRSALR DAARALGLSA DQLEQLSAAS ARGQSAVPIE
ERLAERGFDL DSPVVRRLLQ IASELKGFPR HLSQHVGGFV ISDAPLSTLV PVENAAMPER
TIIQWDKDDL DTLGLLKVDC LALGMLSCVR RCLDLLREAR GIELTPATIP AEDAATYAMI
QRADTVGVFQ IESRAQMAML PRLKPRTFYD LVIEVAIVRP GPIQGRMVHP YLRRRQGLEP
VTYPSADLKQ VFERTLGVPL FQEQVMQLAI VAAGYTPGEA DELRRSMAAW KRRGGLEHHR
ARILEGMAAR GYPPEFAEQV FEQIKGFGSY GFPESHAASF ALITYVSCWL KCHHPDAFAC
ALLNAQPLGF YSTAQIVADA RRHGVRVHPV DVRYSAFDSH LEAGGATARG PIRLGLREVR
GLKSEAAQRI VLARAQRDFR DVEDLAHRAQ LDRGDLGLLA EAGALRGLAG HRHRARWAVA
GVETPLPLFE DLPTPEVQVS LPPPSAAENL LADYARTGLS LGPHPLALLR PQLNALRCKR
SRELAQMRNR SHVRYAGLVS LRQQPSTASG VTFVTLEDED GMVNLVVWQR VAIRDRRALL
ESRLLLVEGH LESADGVRHL IAGRLTDVSN LLGALDARSR DFH
//
