GenomeNet

Database: UniProt
Entry: A0A1I1B080_9ACTN
LinkDB: A0A1I1B080_9ACTN
Original site: A0A1I1B080_9ACTN 
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
//
DBGET integrated database retrieval system