ID A0A1H5GRR2_9MICO Unreviewed; 1059 AA.
AC A0A1H5GRR2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, 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=SAMN04488554_1738 {ECO:0000313|EMBL:SEE18389.1};
OS Ruania alba.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Ruaniaceae; Ruania.
OX NCBI_TaxID=648782 {ECO:0000313|EMBL:SEE18389.1, ECO:0000313|Proteomes:UP000199220};
RN [1] {ECO:0000313|Proteomes:UP000199220}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21368 {ECO:0000313|Proteomes:UP000199220};
RA Varghese N., Submissions S.;
RL Submitted (OCT-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}.
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DR EMBL; FNTX01000001; SEE18389.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H5GRR2; -.
DR STRING; 648782.SAMN04488554_1738; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000199220; 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; SSF160975; AF1531-like; 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:UP000199220};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01902}.
FT DOMAIN 8..75
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1059 AA; 114603 MW; 5F7AA2FC5D9CC670 CRC64;
MFEHVSYAEL HAHSAFSFLD GASQPEELVI EAARLGLSAI GITDHNGLYG VVRFSEAALA
ANMPALYGAE LSLDTPVRPT GMPDPAGTHL LVLARGPEGY RRLSRSIGTA HLASGRKGEA
VYRLPELADM AGGNWLVLTG CRKGAVRRAL EPEPGQFDLT AARTELDQLV DLFGAENVAV
EISDTGAPLD SVRNDALAEL AGRARVPLVA TGAVHCATPA DQRLAHVLAA VRSRSSLDEL
DGWLPASAPH LRSGAEMLAR HHRHPRAVST AAALAAECTF DLHLVAPNLP PCPVPDGHTE
ATWLRELTYR GARERYGPPD VPRHSGAYAM IEHELDVITA LDFPGYFLIV HEIVDFCRRE
GILCQGRGSA ANSAVCFALG ITAVDAVQHQ LLFERFLSPG RTGPPDIDLD IESGRREEVI
QHVYASYGRT HAAQVANVIS YRPRSAVRDA ARAFGYDTGQ QDAWSKSIEQ WGTLRGSSDL
DGAPAEVVDT AEKMLRLPRH LGIHSGGMVL CDRPVIDVCP VEWATMPGRT VLQWDKDDCA
DAGLVKFDLL GLGMLTALRL AFTMIAETDD IELGLHSLPQ DDTAVYDLLC AADTVGVFQV
ESRAQMATLP RLRPRTFYDI VVEVALIRPG PIQGDAVHPY INRRNGREKV TYLHPLLEPA
LKKTLGVPLF QEQLMQIAID VASFTPDEAD QLRRAMSAKR SAERMEALHQ RLLDGMAANG
VSLEIGEQIF DKLKAFADFG FPESHAFSFA YLVYASAWLK VHHPEAFYAG LLAAQPMGFY
SPQSLVADAR RRGVRVERAS VVASQVQACV ERAETPDGGG LALRLGLAPV RGVGEKTAER
IVAAREESPF VDAADLARRV RLSTAQLEAL ATAGALADLG HDRRQGVWVA GALAGESGRS
HGRWTQEPLP FTSVGLDVPD LPAMDEVTTA VADVWATGIS PSSFPTQFRR DDLDEAGVLR
VRDVPGAGSR RVQVAGVVTH RQRPGTAKGV TFLSLEDETG LLNVICSAGL WQRYRKVALS
SAALVVRGVV EHADNVTNLM ADRIEALSLR VPSRSRDFQ
//
