ID A0A2P8AM60_9ACTN Unreviewed; 1125 AA.
AC A0A2P8AM60;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 24-JAN-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 ECO:0000313|EMBL:PSK61511.1};
GN ORFNames=B0E53_06590 {ECO:0000313|EMBL:PSK61511.1};
OS Micromonospora sp. MH33.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=1945509 {ECO:0000313|EMBL:PSK61511.1, ECO:0000313|Proteomes:UP000240342};
RN [1] {ECO:0000313|EMBL:PSK61511.1, ECO:0000313|Proteomes:UP000240342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MH33 {ECO:0000313|EMBL:PSK61511.1,
RC ECO:0000313|Proteomes:UP000240342};
RA Thatcher L.F., Myers C.A., O'Sullivan C.A., Roper M.;
RT "Draft genome sequences of Micromonospora sp. MH33 and MH99.";
RL Submitted (FEB-2017) 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:PSK61511.1}.
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DR EMBL; MUYZ01000421; PSK61511.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P8AM60; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000240342; 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:UP000240342};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01902}.
FT DOMAIN 76..143
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..41
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1125 AA; 122485 MW; D61B14E05C205D02 CRC64;
MSFHNPKMPW SELEQVLSGR SDGRSGKGRP RGERHLHVVD PLAVDADGGD SPAWSRKRQE
YAPPELSRPD DAVPYAELHA HSNFSFLDGA SHPEELAEEA ARLGLTALAV TDHDGFYGVV
RFAEAARALH LPTVFGAELS LGLPGPQNGE PDPHGAHLLV LAHGHEGYAR LATTIARAQL
RGGEKGRPVY GELAEVAAEL RDHVLVLTGC RKGYVPAALL TEGVDAAARE LDRLTALFGA
ETVAVELTDH GHPLDADRND ALAELAAAAG LPTVATNNVH YATPGRRRLA TTVAAVRARR
SLDEIDGWLP AAATAHLRSG AEMAARFAAY PGAVARAAEF GAELAFDLQL VAPQLPAYPV
PPGHTEMSWL RHLTMAGARE RYGPPEAHPE AYAQLEHELR MIEELGFPGY FLVVYDIVAF
CREQDIYCQG RGSAANSAVC YALRITNVDA VRHRLLFERF LAPERDGPPD IDVDIESDRR
EEVIQHVYAR YGREHTAQVA NVISYRPRSA VRDVAKAFGF SPGQQDAWSK QIDRWGSVAA
VDVEDIPEQV VAYANELQTF PRHLGIHSGG MVICDRPVIE VCPVEWGRMP GRSVLQWDKD
DCAAVGLVKF DLLGLGMLSA LHYGYDLIGM SLDLGDMTLD DPEVYDMLCR ADSVGVFQVE
SRAQMATLPR LKPREFYDLV VEVALIRPGP IQGGSVHPYI RRKNGQEPVT FAHPLMRNAL
EKTLGVPLFQ EQLMQLAIDL AGFDAAGADQ LRRAMGAKRS VERMAQIADR LYAGMAERGI
TGELADDVYR KLTAFASYGF PESHAMSFAY LVYASSWLKR YHPGPFLAAL LNAQPMGFYS
PQTLVDDARR HGVEVRRPDI NASGAKAVLE STPETRWGSQ PGEPPHAWGL GGPAVRLGLG
SVRTLGDDVA ERIEAERTAH GPYRDMPDLA RRVGLTAAHL EALATADAFA CFGLTRRQAL
WAAGAAAQDR PGRLPGTVTG TTPPTLPGME AVDRLVADVW ATGLSPESHP ARFIRDRLDA
LGAVPIARLG RVEPGQRIRV GGIVTHRQRP ATAGGVTFLN LEDETGMLNV TCSPGLWQRY
RRIARTSGAL VVRGRLQRHE GVISLTADRL DAIEPPVTPA SRDFR
//
