ID A0A292Z2G0_9PSEU Unreviewed; 1145 AA.
AC A0A292Z2G0;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, 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=TOK_4453 {ECO:0000313|EMBL:GAY10097.1};
OS Pseudonocardia sp. N23.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Pseudonocardia.
OX NCBI_TaxID=1987376 {ECO:0000313|EMBL:GAY10097.1, ECO:0000313|Proteomes:UP000222857};
RN [1] {ECO:0000313|EMBL:GAY10097.1, ECO:0000313|Proteomes:UP000222857}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N23 {ECO:0000313|EMBL:GAY10097.1,
RC ECO:0000313|Proteomes:UP000222857};
RA Yamamoto N., Saito Y., Inoue D., Sei K., Ike M.;
RT "Characterization of newly isolated Pseudonocardia sp. N23 with high 1,4-
RT dioxane-degrading ability.";
RL Submitted (AUG-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:GAY10097.1}.
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DR EMBL; BEGX01000052; GAY10097.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A292Z2G0; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000222857; 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};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01902}.
FT DOMAIN 65..132
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
FT REGION 14..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1145 AA; 122730 MW; 77029726FC255270 CRC64;
MGFNNPDVSW AELESVLSGR PRDGASLTGG PPEGDGGDSP AWSRKREPYR APPLADGGGG
RVPYAELHCH SNFSFLDGAS HPEELVEEAA RLGLGAVALT DHDGMYGVVR FAEAAAELGV
ATVFGAELSL GLSAPQNGVP DPEGSHLLLL ARDPEGYRAL CRVISKAQIE GEEKGRPVYD
LDHVVGETAG RVVALTGCRK GAVRRALRSG GPAAAVEALT WLVDRFGREH VVVELTQHGL
PGDTERNDAL AALAADAGLP TVATTAAHYA TPGRYPLAGA LAAVRARRSL DEADGWLPPA
ATAHLRSGAE MAARFESRYP GAVGRAAAMG GECAFTLDLV APDLPPFEVP EGHDEASLLR
ERVHIGAMRR YGSQAENPEA AEMIQHEMTI IVEKNFPGYF LIVHDIVEFC RDNDILCQGR
GSAANSAVCF ALGITNVDAV ASGLLFERFL SPARDGYPDI DLDIESGRRE EVIQYVYGRY
GRGCAAQVAN VITYRPRSAV RDMAKALGFS PGQQDAWSTQ IERWHGIGGP DGPPAPEGMP
PAVLALAEQL LGFPRHLGIH SGGMVICDRP VSEVVPVEWA RMADRSVVQW DKDDCAAAGL
VKFDLLGLGM LTALHIMIDL VAEHHGRRIE LHELQPVDPE VYAMLQRADS VGVFQVESRA
QMATLPRLKP ERFYDLVVEV ALIRPGPIQG GSVHPYIRRR RGLETWQHEH PLLAGALQKT
LGVPLFQEQL MQVAVDVAGF SAADADELRR AMGSKRSTEK MERLRGRFFD GMAANGITGE
VADGIFTKML AFANFGFPES HSISFASLVY QSAWFKRYHP AAFCAALLNS QPMGFYSPQS
LVADARRHGV LVRGPDVCEG GAEATLEQEP RSEGGVAIRL GMGEVRSVGI DKAEEIEADR
VRNGRYRDLA DLARRVRLTA PQAEALATAG AFGCFGIDRR SALWAAGVVA AVRPEHLPGA
AVGMEAPALP GMTDVELTVS DVWATGVSPD SHPIEHLRPT LDGLGAVRID MLDEVGRRAM
AGTARRTGRG GLGGSEGGDA VVETLDPYDP DVRPPRVLVG GLVTHRQRPA TAGGVTFINL
EDETGMLNVT CSEGLWARYR SVALGSSALL VRGRLERSPE GVLNLVADRV QKLALAIAVP
SRDFR
//
