ID A0A1G5PQG7_9RHOB Unreviewed; 1127 AA.
AC A0A1G5PQG7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=SAMN04488118_101476 {ECO:0000313|EMBL:SCZ51420.1};
OS Epibacterium ulvae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Epibacterium.
OX NCBI_TaxID=1156985 {ECO:0000313|EMBL:SCZ51420.1, ECO:0000313|Proteomes:UP000198767};
RN [1] {ECO:0000313|EMBL:SCZ51420.1, ECO:0000313|Proteomes:UP000198767}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=U95 {ECO:0000313|EMBL:SCZ51420.1,
RC ECO:0000313|Proteomes:UP000198767};
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; FMWG01000001; SCZ51420.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G5PQG7; -.
DR STRING; 1156985.SAMN04488118_101476; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000198767; 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:UP000198767};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01902}.
FT DOMAIN 29..133
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
FT REGION 1086..1127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1091..1127
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1127 AA; 126615 MW; A1765CACF81C0FCD CRC64;
MIEVNRTHRP VEAFQRDILD TRMQGQDYAE LCVTTNFTFL TGASHPEELV VRAAELGLSA
IAITDQNSLA GVVRAWSALK ELKHETKEIV EIRSQQRTDS SSRQQIGHNT PIAKPGAISL
PKLIVGCRLV LQDSPVDWIT LPRDRAAYKR LTRLLTLGKR RTKKGECLLY IKDMMAACKG
MILIALPQRS LDEAIPDIRK LRQQFPNHVF LGAAPCYDGS DQTYLNSCAQ AAQRTSAPMV
AVGDVLMHRA NRRQLADVLT CMREHITIDQ IGTRALPNGE RRLKAGADMA HLFRNHPAAL
RRTLEIADGC SFDLEELSYE YPHEETQGET PQDRLERLAT EGLKRRYPDA PPTRALDLMQ
KELTVVKELN FPAYFLTVHD IVQFAKSQGI LCQGRGSAAN SILCFLLGIT DVSPDMITMV
FERFVSKHRG EPPDIDVDFE HERREEVIQW IYEKYGRHRA GLCATVIHFR TRAAIREVGK
VMGLSQDVTA GLSSQIWGMT NGGVNLDRIR ELGLDPNDRR LMQTIRLIGE IIGFPRHLSQ
HVGGFIITRG RLDELAPIEN AAMEDRTVIC WDKDDIDALG ILKVDVLGLG MLSCIRKAFA
LMQEHDNITH SIASVPQGDE ATYDMLCQAD AIGVFQVESR AQMNFLPRMR PREFYDLVIE
VAIVRPGPIQ GDMVQPYIRR RNGLEEIEPF GPALEEVTRR TLGVPLFQEQ ALQIAVVGAG
FSAEEADHLR RSLASFRRMG TIGKYRDKFI AGMLRNGYAP DVAERCFGQI EGFADYGFPE
SHAAAFAMLA YVSAWLKRHH PAIFACALLN SQPMGFYAPA QIVRDVREHG VETRPICVNH
SDWDNTLERR PDGTLALRLG FRQIKGLKEE DAGWIVAARG NGYPDPEALW LRAGLHPDVL
TRLAEADAFS DMGLTRRDAL WQVKAIQSPK PLPLFNDPID GENIHEPQVA LPIMQLGEEV
VEDYVSTRLT LRAHPMELLR PTLSGLVTHA SLQNIALGRY SVCGLVITRQ RPGTASGVIF
LTLEDETGVS NVVVWRNVYE RFRRIVMGGR LLRVTGYLQR EGIVIHLIAQ DIQDMSHKLF
ELGHPEPEAL TTEGPRADDT PKQSRYPTRA MHPRDQAKRL FPSRDFH
//
