ID A0A1Y5EAG8_9PROT Unreviewed; 1083 AA.
AC A0A1Y5EAG8;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-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=A9Q83_04750 {ECO:0000313|EMBL:OUR79703.1};
OS Alphaproteobacteria bacterium 46_93_T64.
OC Bacteria; Pseudomonadota; Alphaproteobacteria.
OX NCBI_TaxID=1856292 {ECO:0000313|EMBL:OUR79703.1, ECO:0000313|Proteomes:UP000196525};
RN [1] {ECO:0000313|Proteomes:UP000196525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Hu P., Dubinsky E.A., Probst A.J., Wang J., Sieber C.M.K., Tom L.M.,
RA Gardinali P., Banfield J.F., Atlas R.M., Andersen G.L.;
RT "Simulation of Deepwater Horizon oil plume reveals substrate specialization
RT within a complex community of hydrocarbon-degraders.";
RL Proc. Natl. Acad. Sci. U.S.A. 0:0-0(2017).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OUR79703.1}.
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DR EMBL; MAAN01000011; OUR79703.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y5EAG8; -.
DR Proteomes; UP000196525; 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 Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 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; IPR012340; NA-bd_OB-fold.
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 13..80
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
FT REGION 1054..1083
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1083 AA; 120702 MW; 1CFAA1EF856399B1 CRC64;
MTRKILQKTP VYAELAVTSN FSFLRGASHP DEMVLVAAAL GYGAIGIADR NTLAGVVRAH
KAAKDVRIKL VVGVRLVLVN GFECLCFPTD KAAYSRLTQL LSCGNLRAKK GDCHLTVEDV
EKFGEGQIFI AMPPYDISTE FEKQLSRFAE AFQKTCYLSL SAYLGGDDLP RLDRLSVLAQ
RLDLLPVVTN DALYHIPNRR PLQDVLTCIR THTTLQDAGF KLLANAERHL KSPTEMTRLF
PGFKGAVQRS QQIAEQCHFS LDELAYQYPD EPSGKSATPQ IELDRLTWIG AADRYPDGVP
EKVRKILAHE LKLIGELNYA PYFLTVYDIV RFARSLDPPI LCQGRGSAAN SAVCYCLGVT
SVNPSEINLL FERFVSAERD EPPDIDVDFE HERREEVIQY IYAKYGRHRA GLAATVVTYR
TRSSLREVGK AMGLSEDVVS ALASNVWGHS STGLDWEEAA RIGIGPADMT IRQVLRLSRD
LIGFPRHLSQ HVGGFVITRD PLIELSPISN AAMDNRTIVE WDKDDLDTLG ILKIDVLSLG
MLTCIRKAFD LLEEHYGVPM SLAAVPRDDP ATYEMIQKAD TVGVFQIESR AQMSMLPRLR
PANFYDLVIQ IAIVRPGPIQ GDMVHPYLRR RQGLETVEYP SEELRSVLEK TKGVPLFQEQ
AMQIAMVGAG FTAGEADGLR RAMATFKRTG DIGNFKERFL SGMRERGYTA DFSEKCFRQI
EGFSDYGFPE SHSASFALLA YASAWLKYHY PDVFVAAILN SQPMGFYSAA SLVRDFREHG
GDVLPVDINK SNWDYLLEPI DVQRRSTALR IGFRQVRGVK KANALQLIER RGDGYDSVRD
LYFRSGIDMK TLEELANADA FRSIGLDRRA ALWAVQGLAG HGGKRGAVEE LPLFSKAAAE
DELLQKEAEM ELPSMPLGQH VVEDYHSLRL SLKAHPISFL RPSLSMSAVL GSADLKSQKS
GSRIKVAGLV LARQRPGTAA GVIFMTLEDE TGTANIIVWP KKFEIYRRTV LSARVICIEG
ELQKEQDVIH VIAHHLEDLS DLLVNEMEEG TSIPTITKPS LGKPNLWKHP RTTSVMPKGR
NFH
//
