ID D5X2A9_THIK1 Unreviewed; 1037 AA.
AC D5X2A9;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 72.
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 OrderedLocusNames=Tint_1890 {ECO:0000313|EMBL:ADG31255.1};
OS Thiomonas intermedia (strain K12) (Thiobacillus intermedius).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Thiomonas.
OX NCBI_TaxID=75379 {ECO:0000313|EMBL:ADG31255.1};
RN [1] {ECO:0000313|EMBL:ADG31255.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 {ECO:0000313|EMBL:ADG31255.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ovchinnikova G., Kerfeld C.A., Cannon G.C.,
RA Heinhorst S., Woyke T.;
RT "Complete sequence of Thiomonas intermedia K12.";
RL Submitted (APR-2010) 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; CP002021; ADG31255.1; -; Genomic_DNA.
DR AlphaFoldDB; D5X2A9; -.
DR STRING; 75379.Tint_1890; -.
DR KEGG; tin:Tint_1890; -.
DR eggNOG; COG0587; Bacteria.
DR HOGENOM; CLU_001600_4_0_4; -.
DR BioCyc; TINT75379:TINT_RS09480-MONOMER; -.
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};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01902}.
FT DOMAIN 8..75
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1037 AA; 115743 MW; 0030D3003BEC26A7 CRC64;
MDPLPDYVEL HCRSNFSFLT GASHPEELVE RAHELHYAGL ALTDECSLAG IVRAHGAAKA
AGLPLLVGVQ FAVEGDEKTR TPPFTLVVLA CNLNGYGNLC EFITRLRRAS PKGSYRLDRQ
SITGETLADC VVLAVPSRQA TDAGLLELGA WLLARFTGRV WLAVELHRRL DDERWLERLQ
DLAEATAIPL VAAGDVHMHR RSRKPLQDTL TAIRLGRPIA DCGHALQPNA ERHLRSRLRL
ALTYPAELLA ETLRVAARCR FSLDELRYRY PKEVIPAGET ADGYLRRRVY EGAGRRWPDG
LHAKVQDLLE HELALIAELG YAHYFLTVDD IVAFARSRHI LCQGRGSAAN SAVCYALGIT
EVDPEQQQVL FERFISKERN EPPDIDVDFE HERREEVIQY LYAKYGRDRA ALTAAVIRYR
PKSALRDVGK ALGFDLETVD RLARNVHWWD GREVARERLE EVGLDPDALG VQQWMALVRQ
LLGFPRHLSQ HTGGFVLTEG PLSRLVPIEN ASMPERTVIE WDKDDLDAAG LLKVDILALG
MLTAIRKALD AIGQSLGQTF AMQDIPREDP QTYDMLCQAD SVGVFQVESR AQQGMLPRLQ
PRCFYDLVIE TAIVRPGPIQ GGMVHPYLNR RQGKEVVVYP SKDLESVLQR TLGVPVFQEQ
VMQIAMVAAG FSAGEADGLR RAMAAWRRTG SLEKYRDRLI AGMTERGYSA DFAQSIYEQV
QGFSEYGFPE SHAASFALLV YASAWIKRHH PAEFLMALLN SQPMGFYTPS QLVQDAKRHG
VTVRPVDVLH SDWDCTLEEA VPYPAVRLGL RLVKGLGREA GLRIAAARMS RPPVDAEDLA
KRAQLDTMAL RQLAAADALR SLSGHRRQQV WEATAVERMP ALLDDAAPQE DWLELPAPPE
GEDIVFDYAT TGLSLRRHPL ALLRPLLAKR RLQTAAELAQ APDGRIVRAC GIVTLRQQPE
TAKGTTFVSL EDETGTVQVI CWKSLRQRQR TVLLRSRLLA VAGTWQREGD TASLIAGHLE
DWTPLLGGLA TRGREFR
//
