ID A0A1I6HRP9_9GAMM Unreviewed; 1038 AA.
AC A0A1I6HRP9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-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=SAMN04488070_2062 {ECO:0000313|EMBL:SFR56940.1};
OS Pseudidiomarina maritima.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Idiomarinaceae; Pseudidiomarina.
OX NCBI_TaxID=519453 {ECO:0000313|EMBL:SFR56940.1, ECO:0000313|Proteomes:UP000199424};
RN [1] {ECO:0000313|Proteomes:UP000199424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.7285 {ECO:0000313|Proteomes:UP000199424};
RA Varghese N., Submissions S.;
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; FOYU01000003; SFR56940.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I6HRP9; -.
DR Proteomes; UP000199424; 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 9..76
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1038 AA; 117490 MW; 0A019FA6DBA78642 CRC64;
MAGSVKRPAA LHCLTNFSFL RGGSHPHELV QRAVSCGYQA LAITDECSVA GVVRAYVAAR
EQPLRLIIGS EFQLENVGTL IVLVRNRQGY AQLCQLITTA RNRSKKGSYQ VFLDDFMGTL
NDCLLLWRPQ FKVPSANVER ETITVTAQQL KQQFGGALWL AYGRHYEADD AQRYSDYKQL
SVAHDIPVAA VCEVCYHEPQ RQLLHDVLVA IRRRQPLETQ VGQLKPNQDY CLRTPEQLQQ
CYPSAWLAQS VVIAKQCCFC LSELRYEYPA ELVPAGKTAS EHLRELTYLG AQQRFPHGLR
ADVKEKLEKE LKLIAQLRYE YFFLTIHDLV QFAQQRGILY QGRGSAANSV VCYCLQITAV
NPDQIDVLFE RFISAERDEP PDIDVDFEHE RREEVIQYIY QKYGRHRAAL AATVIRYRLR
SALRDVGKAL GFHEQELRHY LRQIDRRDQQ SDWQQQLLEK IPGLGQTHRG RCLFALTDAI
LGFPRHLSQH VGGFVIASTQ LSDLVPVENA SMPERTVIQW DKDDLETLRL IKVDVLALGM
LTALRKMLRL IQQHHQRELG LADIPQEDAK VYQMLQRADS IGVFQIESRA QMNMLPRLRP
QTFYDLVVQI AIVRPGPIQG DMVHPYLRRR AGLEPITFPS EAVKEVLERT LGVPIFQEQV
IKLAMVAAGF SGGEADQLRR AMANWKSSGE LRQFESKLIK GMRARGYSEE FAQRIFQQIC
GFGEYGFPES HSASFANLAY ASAWLKCYYP AAFYCALLNS LPMGFYSANQ LIQDARRHHI
TILPADIQHS NWDHQLEAGG RGMQLRLGLR LIKGLSQSHM QALLEQRPAQ GFQSLQQLRD
YGLSGADLHK LASADVLGAL AGHRYQSQWQ SLALQAEQLP LFAELTAVPT TQLAAPAEFQ
DIAVDYRTTG VSIRRHPLAL LREQQQLKGY KLASELAHCR HKQHVRVAGL VTCRQRPGTA
SGVTFVTLED ESGLINIVIW QKTARAFRQA YLTAQLLKIK GIVEIHGEVI HVIAGQLEDG
TEQLAQLGVS ANRSRDFH
//
