ID A0A367Z1L9_9ACTN Unreviewed; 1148 AA.
AC A0A367Z1L9;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-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=DT076_01230 {ECO:0000313|EMBL:RCK71121.1};
OS Desertihabitans brevis.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Desertihabitans.
OX NCBI_TaxID=2268447 {ECO:0000313|EMBL:RCK71121.1, ECO:0000313|Proteomes:UP000252770};
RN [1] {ECO:0000313|EMBL:RCK71121.1, ECO:0000313|Proteomes:UP000252770}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=16Sb5-5 {ECO:0000313|EMBL:RCK71121.1,
RC ECO:0000313|Proteomes:UP000252770};
RA Liu S.;
RT "Desertimonas flava gen. nov. sp. nov.";
RL Submitted (JUL-2018) 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:RCK71121.1}.
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DR EMBL; QOUI01000001; RCK71121.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A367Z1L9; -.
DR Proteomes; UP000252770; 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 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}; Reference proteome {ECO:0000313|Proteomes:UP000252770};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01902}.
FT DOMAIN 63..130
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
FT REGION 19..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 864..904
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..49
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1148 AA; 125866 MW; 91E2C4F53D2CE926 CRC64;
MGYFNPDVRW AELERRLSGR RRRGSEAKPW ERDGDGAPGW ERRPRYEASP RVTRPSGATV
PYAELHAHSD FSFLDGASDP ERLVEEAVGL GLTALALTDH DGFYGAARFA EAAQEYDLRT
IYGAELSLGL RTPQNGVADP EGEHLLVLAE GVTGYHRLAG AITDAQLRGD EKGRPLYRLD
ELAEQGAGHW TVLTGCRKGA VRRALETGGP EAAGRELGRL VELFGRDHVV VELTDSGLPT
DSVQHDALAA LASRHGLPLV ATNNVHYARP DDYRLASAMA AVRARRSLTE MDGWLPPPTA
HLRSGEEMAW LFRRFPAAVP ATVELAGRLA FDLRAASPRL PQLDVPEGHT PLSYLRELAE
RGADRLYPGS ARAGAQARLD KELAVIGAKD FPGYFLIVRD MVAFAKERGI LCQGRGSAAN
SVVCYTLGIT AVDPIKFDLP FERFLATTRD EEPDIDVDFD SERREEVIQE VYRRYGRRNA
AQVANVIAYR PKSAVRDMAK ALGYSTGQQD AWSKQIDSWG AVAVEGQEHD IPAEVVALAD
QLLKAPRHLG IHSGGMVLTE QPVGEICPIE RGRMDDRTVL QWDKDSCAWM GLVKFDFLGL
GILNAIQQTF DLAEQWLGER WGLETLPKEE AGVYDMVCRA DSVGLFQVES RAQIGTLPRL
LPRRFYDLVI EVALIRPGPI QGGAVHPYIR RSTGREPVSY PHPALEPVLE RTLGVPLFQE
QLMQIAMAVG GCTGDDADLL RRAMGSKRGV EKIERLRARL FEGMAEHGIT GDLADDIYDQ
IQAFANFGFA ESHACSFALL VYASAWLKLH YPAAYLAGLL RAQPMGFYSP QSLTADARRH
GVVVRRPDIS RSGAEAGLEL LEDDADPATP AGRAVPTGRD ACLERDQPPV PPFVRGTPDP
TPAHRRDGAC AVRLGLTSVQ GIGPELARRV VAERRRAPFT SVTDVVRRTG LTTAQAEALA
TAGAFDCFGL TRRQALWSAG YTDNPDLLEG TAIDAPPPEL PGMSSIETTL ADLWATRISP
DDHPLQHLRP AFDDHGILPV SRLGPEVHGR RVHVAGLVTH RQRPGTAAGV TFLNLEDETG
MLNVVCSPGL WQRFRRVARG TNAQLVRGTI EHRDGVTNLV ADRLEPLVNA FPETAAMLPR
RHVSRDFR
//
