ID A0A1I1B080_9ACTN Unreviewed; 1131 AA.
AC A0A1I1B080;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Error-prone DNA polymerase {ECO:0000256|HAMAP-Rule:MF_01902};
DE EC=2.7.7.7 {ECO:0000256|HAMAP-Rule:MF_01902};
GN Name=dnaE2 {ECO:0000256|HAMAP-Rule:MF_01902};
GN ORFNames=SAMN05192575_11138 {ECO:0000313|EMBL:SFB42020.1};
OS Nocardioides alpinus.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=748909 {ECO:0000313|EMBL:SFB42020.1, ECO:0000313|Proteomes:UP000199113};
RN [1] {ECO:0000313|EMBL:SFB42020.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10697 {ECO:0000313|EMBL:SFB42020.1};
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|HAMAP-Rule:MF_01902}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-C family. DnaE2
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01902}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FOKC01000011; SFB42020.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1B080; -.
DR STRING; 748909.SAMN05192575_11138; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000199113; 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: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; cd07431; PHP_PolIIIA; 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; 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 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 51..118
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1131 AA; 122543 MW; F42C5EC0E8ADF9CC CRC64;
MGWNNPAMHW KELERRLSGL PGADDAPVSR RKRGATEART IERPAVVTPY AELHCHSHFS
FLDGASSPAA LVEEAVRLGL HALAITDHDG FYAAPMLAEA AAVYDLPTVF GAELSLGLSS
PQNGVPDPEG SHLLVLARGV EGYHRLAAAM TDAHLRGDEK GRPVYDLDEL GERGRGHWAV
LTGCRKGAVR QALATGGEAA AAEALDRLTS LFGIEHVLVE LSPRPGSDGT NTSLARLAAV
HGLDVVAAGN VHHATPQQHR LASAMAAVRA RRSLTDLDGW LDLSGSAHLR SGAETASALT
AYDGAVARSV SLADELAFDL HKASPALPKR QIPEGHTADS WLRVLAERGF AERYAGVPHE
QQARERLEHE LRVVSEKDFA GYFVIVHDIV AFARSRGILC QGRGSAASSA VCYALGITAV
DAVFYRLPFE RFISAHRDEE PDIDVDFDSD RREEVIQWVY DTYGRRNAAQ VANVISYRPR
MAVRDAAKAL GFSQGQQDAW SKQIDGWQSV VSGDAGDPTA HDVPPTVVAL AEELMGAPRH
LGIHSGGMVL TERPIGEVCP IERGRMDRRT VLQWDKDACE SMGLVKFDLL GLGMLGALDH
MMRLVADHLG ERWDLATMPK EEPAVYDMLC RADSIGVFQV ESRAQIGTLP RLRPREFYDL
AIEIALIRPG PMQGGAVHPY VRRATGKEPV TYDHPELIPV LERTKGVPLF QEQLMAMAVT
LGDCSRDDAD LLRRAMGSKR GVERIESVKQ KLYAGMARRG ITGDLADSIY VKILSFANFG
FAESHALSFA LLVYASSWFK LHYPAAFLAG LLRNQPMGFY SPQSLVGDAR RHGVDVRRPD
VTRSAAQAEL EAVVLGPVAA TGLDACCQPR FDRVEWVPGT PDPVPAHRRD AALAVRLGLD
SVRGIGLEVA RRIVAARDEA PFTGVTDLSR RADLTSAQLE SLATAGAFDA WGLDRREALW
AAGFAEGAGH LPGTTPSPAA PALPGMSEPE ITLADLWATG ISPERHPVEH LRDELRRAGV
RSVAELADTE HGRRVHVGGL ITHRQRPGTA MGVTFLNLED ETGMLNVVCS IGVMKAHRHA
ARNRVAVVIR GRLERNEGVT NLLADRVEAI DVVVPGAGAV LQARASSRDF R
//