ID A0A2W2E3B6_9ACTN Unreviewed; 1088 AA.
AC A0A2W2E3B6;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
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=C1I95_16890 {ECO:0000313|EMBL:PZG16771.1};
OS Micromonospora craterilacus.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=1655439 {ECO:0000313|EMBL:PZG16771.1, ECO:0000313|Proteomes:UP000248924};
RN [1] {ECO:0000313|EMBL:PZG16771.1, ECO:0000313|Proteomes:UP000248924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA12 {ECO:0000313|EMBL:PZG16771.1,
RC ECO:0000313|Proteomes:UP000248924};
RA Sahin N., Ay H., Saygin H.;
RT "Draft genome sequence of Jishengella sp. NA12.";
RL Submitted (JAN-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:PZG16771.1}.
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DR EMBL; POTY01000099; PZG16771.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2W2E3B6; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000248924; 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 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:UP000248924};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01902}.
FT DOMAIN 39..106
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 823..853
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1088 AA; 118631 MW; 9B173BED64EF50CA CRC64;
MVDPLAVDAD GGDSPAWSRR REHYQPPELT RPDGVVPYAE LHAHTNFSFL DGASHPEELA
EEAVRLGLTA LAVTDHDGFY GVVRFAEAAR TLGLPTIFGA ELSLGLPGPQ NGVPDPHGNH
LLVLAHGHEG YARLAATIAR AQLRGGEKGR PVYGELEEVA DALRDHVLVL TGCRKGHVPA
ALLTEGVDAA ARELDRLTAL FGAETVAVEL TDHGHPVDGD RNDALAELAA AAGLPTVATN
NVHYATPGRR RLATTLAAVR ARRSLDEIDG WLPAAGTAHL RSGAEMAARF AGYPGAVARA
AEFGAELAFD LQLVAPQLPA YPVPPGHSEM SWLRHLTEQG ARDRYGPREA HPQAYAQLDH
ELNMIEELGF PGYFLVVYDI VDFCRQEDIY CQGRGSAANS AVCYALRITN VDAVRHRLLF
ERFLAPERDG PPDIDVDIES DRREEVIQHV YTRYGREHTA QVANVISYRP RSAVRDVAKA
FGFSPGQQDA WSKQIDRWGD VATVDVPEIP EQVIEYANHL QTFPRHLGIH SGGMVICDRP
VIEVCPVEWG RMPGRSVLQW DKDDCAAVGL VKFDLLGLGM LSALHYGYDM IGMSLDLGDM
TLDDPEVYDM LCRADSVGVF QVESRAQMAT LPRLKPRTFY DLVVEVALIR PGPIQGGSVH
PYIRRKSEQE EVTFPHPLMR NALEKTLGVP LFQEQLMQLA IDLAGFDAAE ADQLRRAMGA
KRSVERMAKI ADRLYSGMAE RGITGELADD VYRKLTAFAS YGFPESHAMS FAYLVYASSW
LKRYHPGPFL AALLSAQPMG FYSPQTLVDD ARRHGVEVRR PDVNASGAKP VLESTPDTRW
GSQPGEPPHA WGLGGPAVRL GLSSVRTLGD EVAERIEAER AANGPYRDMP DLARRVGLTA
AQLEALATAD AFACFGLTRR QALWAAGAAA QDRPGRLPGT VTGAAAPTLP GMEAVDRLVA
DVWATGLSPE NHPARFVRPQ LDGMGAVPID RLGRVEPGRR IRVGGIVTHR QRPATAGGVT
FLNLEDETGM LNVTCSPGLW QRYRRVARTS AALVVRGRLQ RHEGVVNLVA DRLDAIEPPV
SPASRDFR
//
