ID A0A1E5MKK3_9MICO Unreviewed; 1138 AA.
AC A0A1E5MKK3;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=Cus16_0912 {ECO:0000313|EMBL:OEI69083.1};
OS Curtobacterium sp. ER1/6.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Curtobacterium.
OX NCBI_TaxID=1891920 {ECO:0000313|EMBL:OEI69083.1, ECO:0000313|Proteomes:UP000095245};
RN [1] {ECO:0000313|EMBL:OEI69083.1, ECO:0000313|Proteomes:UP000095245}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ER1/6 {ECO:0000313|EMBL:OEI69083.1,
RC ECO:0000313|Proteomes:UP000095245};
RA Garrido L.M., Alves J.M., Oliveira L.S., Gruber A., Padilla G.,
RA Araujo W.L.;
RT "Draft genome sequence of Curtobacterium sp. strain ER1/6, an endophytic
RT strain isolated from Citrus sinensis with potential to be used as a
RT biocontrol agent.";
RL Submitted (AUG-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:OEI69083.1}.
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DR EMBL; MJAK01000002; OEI69083.1; -; Genomic_DNA.
DR RefSeq; WP_069711482.1; NZ_MJAK01000002.1.
DR AlphaFoldDB; A0A1E5MKK3; -.
DR STRING; 1891920.Cus16_0912; -.
DR PATRIC; fig|1891920.3.peg.1474; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000095245; 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:UP000095245};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01902}.
FT DOMAIN 60..128
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1138 AA; 124416 MW; A1B34714135E7432 CRC64;
MGYSNPPIPW SEFERALSDK RPDSAHAGDG GDSPAWSRKR SRYVPPPSAS DDDVPVVPYA
ELHAHSTFSF LDGASGPEHL VEEAARLHLH GLALTDHDGF YGAARMAEVA EAYPTVATVY
GTELSLGLTE PQNGVPDPEG THLLLLADGQ DGYHRLAAAV TRAHLAAGAE KGRPQYDLDE
LAAQADGHWR VLTGCRKGTV RRALEQGGES AADEALRALL DRFGTAGVVV ELTDQGEPLD
SARNDVLAAL AAQHGLPVVA TGNVHYATPD RFPVATALAA VRARRSLDEI DGWLPAAPTA
HLRSGAEMAR RFARWPGAVE TSVELADELG FRLRTAKPGL PDVEVPEGHT TMSWLRELTW
HGARRFYPGS ADGVDPQKRE RIERELSVIA DKDFPGYFLI VRDMVQYARD RGILCQGRGS
AANSAVCYLL EITAVDSIRY GLPFERFLSA MRDEEPDIDV DFDSDRREEV IQYVYEKYGR
FNAAQVANVI TYRPKGAVRD MAKALGHSPG QQDAWSKQVE RWGAVTESQD HDIPDTVVDM
AQQVLGFPRH LGIHSGGMVL TDRPVGEVVP IEHARMDGRT VLQWDKDDCA YMGLVKFDML
GLGMLAALQY SFDLADEHCG ERWDMHSIPK EEQGVYDQLC RADTIGVFQV ESRAQMGTLP
RLLPRRFYDL VIEVALVRPG PIQGGAVHPY IRRRTGEEPI TYIHPSLEPV LERTLGVPLF
QEQLMQMAIA VGGCSGDDAD LLRRAMGSKR GHEKIERLRE KLYAGMASND IHGADADAIY
AKIQAFANFG FAESHSISFA LIVYASAWMR LHYPGAFLAA LLRAQPMGFY SPQTLVADAR
RHGVRVLRPD VLRSGVDATL EPLDQHGGAA HPGADACLAE EQPPVLPFDG SRPDDTAEHR
RDGAFAVRLG LAEVASLGRR SAEAIVVERE AHGPFTDMSD LARRVRLTTA QLEALAAADA
FAGLGIDRRS GMWSAAQAAA ERPDQLPDTQ VTVQPPLFGQ MTSGDVLIAD MWSTGMSTDD
HPVRHVRPRL DARGVLSVLD TATAETGRRV EVGGIVTHRQ RPATASGITF LNVEDETGLV
NVICSVGVWG RYRRVARESP AVVVRGILER SPDGVVNLVA DQIEHLPLGV RTRSRDFQ
//
