ID A0A1R4HM43_9MICO Unreviewed; 1130 AA.
AC A0A1R4HM43;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=FM113_03535 {ECO:0000313|EMBL:SJN08615.1};
OS Leucobacter sp. 7(1).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Leucobacter.
OX NCBI_TaxID=1255613 {ECO:0000313|EMBL:SJN08615.1, ECO:0000313|Proteomes:UP000195513};
RN [1] {ECO:0000313|EMBL:SJN08615.1, ECO:0000313|Proteomes:UP000195513}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7(1) {ECO:0000313|Proteomes:UP000195513};
RA Peterson S.W.;
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}.
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DR EMBL; FUID01000014; SJN08615.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R4HM43; -.
DR Proteomes; UP000195513; 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:UP000195513};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01902}.
FT DOMAIN 4..102
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1130 AA; 122675 MW; 18070AF0E71A0827 CRC64;
MPYAELHAHS HFSFLDGSAT PEELVAEATR LGLNGLALTD HDGFYGAAVF AEAAEAATRA
AAERAAATEH TAATEYTAAA EHTAAAPAPL LTVYGAELSL GLDVPQLGAA DPTGTHLLVL
ARGAEGYHRL AGAITEGQLT GGEKGRPSYD LDMLAELGRE HWAILTGCRK GAVRQALDAA
PTRAAGEEHA RAELRRLTER FGTDNTYVEL TQHGHPGDDL RNAQLAQLAA EFGLPTLVTG
NVHYATAAQA PLAEAMAAVR ARRSLDELDP YLPATGAARL RSGAAQLRRF AAYPDAVART
VPLARELAFS LRSARPKLPR LPVPTGHTPM TWLRELAWAG AERRYGALTE AIRTRIEREL
EVIEEKDFPG YFLIVYDIVQ EARRRGILCQ GRGSAANSAI CYVLEITAVD SIRYGLPFER
FLSSMRDEEP DIDVDFDSER REEVIQYVYE TYGRRNAAQV ANIISYRPKA AIRDAAKALG
YSAGQQRAWT KAMERWRAIE ADPESPIPLP VQHLAQQFLG APRHLGIHSG GMVLTERPVG
EVCPIEHARM DRRTVLQWDK ESCESMGLVK FDMLGLGMLS ALQKTMDLIA EATGERWTLE
TVPKEEPGVY DMLCRADAIG VFQLESRAQL NTLPRLRPRS FYDLVIEIAL IRPGPIQGGA
VHPYLRRRNG DEPVTYPHPK LEDVLKRTLG VPLFQEQLMQ MAMAVGGCSA EDADLLRRAM
GSKRGEERIT ALKEKLFTGM AENGITGEDA THLYSQIEAF ASFGFAESHS ISFALLVYIS
SWFKLHYPGA FLAGLLRSQP MGFYAPRTLV ADARRHGVEI RAVDVQRSGV FAGLEAVDVA
PTRAGSGSVS ASSHPEHAAC TADDPVRSLA PHEATVQVPP FEPSLPDTSG AHRRDGGFAV
RLGLSEVRGI EPATAERIVR ARADGPFVDL ADLARRADLD RSRLEALATA GACESFGVGR
REALWAAAPA ADNRERFLPG IAVHVQPPLL PVLSRSEQTA LDLWSTGIVT NDHPLALLRD
ELDGRGVLRS DRTGHGTPGT VVTVAGLVTH RQRPSTAGGI TFLTLEDEAG TVNIVTFAQV
WQRNRLVARA SPALIVRGLL ERSPEGVVNV VAHTFEPLAA PASVGSRDFH
//
