ID A0A1F1UZS3_9CORY Unreviewed; 1053 AA.
AC A0A1F1UZS3;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=HMPREF3171_01760 {ECO:0000313|EMBL:OFT31600.1};
OS Corynebacterium sp. HMSC08F01.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1581139 {ECO:0000313|EMBL:OFT31600.1, ECO:0000313|Proteomes:UP000176366};
RN [1] {ECO:0000313|EMBL:OFT31600.1, ECO:0000313|Proteomes:UP000176366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMSC08F01 {ECO:0000313|EMBL:OFT31600.1,
RC ECO:0000313|Proteomes:UP000176366};
RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA Babar A., Rosenke K.;
RL Submitted (APR-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}.
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:OFT31600.1}.
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DR EMBL; LWNT01000028; OFT31600.1; -; Genomic_DNA.
DR RefSeq; WP_070482419.1; NZ_KV789284.1.
DR AlphaFoldDB; A0A1F1UZS3; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000176366; 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; 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; 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 PANTHER; PTHR32294; DNA POLYMERASE III SUBUNIT ALPHA; 1.
DR PANTHER; PTHR32294:SF4; ERROR-PRONE DNA POLYMERASE; 1.
DR Pfam; PF07733; DNA_pol3_alpha; 2.
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 60..127
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
FT REGION 20..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1053 AA; 114459 MW; C0DA7C57B30BFC6F CRC64;
MRFNGGAPLS WSRLERILSG RPGPEPVPVG HTGTPAGAAY GKAEPAPPPQ KQCLSTTPFA
ELHTVSSYSF LGGASEPEDL VARAVELGLS AVGLLDRDGF YGAVKFAEAA AAAGLDTVFG
AELTLGDTVL PVIARGPDGY KRLSHLMADA HMATREKDKV AYPPLELIGD QLGGTCVVLA
GWQWVGEIDH LVETFGQDNV VREYEVSMTP EDADRHAMLD RFDHLPAIVT AIPAAATREQ
ARLAAAKRAL ARREALAQAH GDLHPMGANW LRSGEQLERM LPGCKHMLDY SVELAKQCAF
TLNLVAPELP RYPTPSGRGE MDHLRDLTLA SAQFRYATRS ADVRNQAMKQ IRYELSVIEE
LNFPGYFLII YDLVDFCAKQ NILCQGRGSA ANSAVCFALG ITNVEPIEAG LLFERFLSPD
RDGPPDIDLD IESGRREEVI QYVYDTYGRD NAAQVANVIT YRTKGAVRDA ARALGYAQGA
ADSWSKGLSD PPEAVEQLAA QFKGQPRHLG IHSGGMVICD RPIADVVPVE WARMADRSVV
QWDKDDCASA GLVKFDLLGL GMLEALHHMV DLVEETTGRK VHLWELSLDD DAVYDMLCRA
DSVGVFQVES RAQMGTLPRL KPRRFFDLVV QVALIRPGPI QGGSVHPYLR RRDGLEPVVY
DHPVLERSLG KTLGIPLFQE QLMQICVDAA GFSGREADAL RRAMGSKRSP AKMAALRARF
FEGCWATNQI SEEVAERLWQ KIVAFAAYGF PESHSQSFAS LVYFSAWFKC HYPAQFCVGL
LRAQPMGFYS PQSLVQDARR HGVEVLPVSV NASGREARCI DSSTIRMGLG LVRGLGADAA
DRIEAAAPFT DIADLSRRAD LSVDHVEALA RAGALDCFEV SRRQALWQAG IAATERHGML
PGLSAISAPA LPGMNSFELM VADIAATGVT PGLMPVEMVR ESLEERGVVP VSQLLHGVED
GTRVRIAGVV THRQHPVTAG GVTFLGMEDE TGLVNVVISV GLWKKQRVLA RTAKALVVRG
IVQNASGAVS VVADRFEPLE VGELLSRGSR DFR
//
