ID A0A086GNW9_STRSC Unreviewed; 1172 AA.
AC A0A086GNW9;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
DE AltName: Full=Error-prone DNA polymerase {ECO:0000256|ARBA:ARBA00017273};
GN ORFNames=IQ62_32695 {ECO:0000313|EMBL:KFF97086.1};
OS Streptomyces scabiei.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1930 {ECO:0000313|EMBL:KFF97086.1, ECO:0000313|Proteomes:UP000028722};
RN [1] {ECO:0000313|EMBL:KFF97086.1, ECO:0000313|Proteomes:UP000028722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCPPB 4086 {ECO:0000313|EMBL:KFF97086.1,
RC ECO:0000313|Proteomes:UP000028722};
RA Harrison J., Sapp M., Thwaites R., Studholme D.J.;
RT "Genome sequencing of plant-pathogenic Streptomyces species.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-C family. DnaE2
CC subfamily. {ECO:0000256|ARBA:ARBA00007391}.
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:KFF97086.1}.
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DR EMBL; JPPX01000203; KFF97086.1; -; Genomic_DNA.
DR RefSeq; WP_037702058.1; NZ_KL997438.1.
DR AlphaFoldDB; A0A086GNW9; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000028722; 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-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd04485; DnaE_OBF; 1.
DR CDD; cd07431; PHP_PolIIIA; 1.
DR Gene3D; 1.10.10.1600; Bacterial DNA polymerase III alpha subunit, thumb domain; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR InterPro; IPR011708; DNA_pol3_alpha_NTPase_dom.
DR InterPro; IPR041931; DNA_pol3_alpha_thumb_dom.
DR InterPro; IPR040982; DNA_pol3_finger.
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 DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 5..72
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
FT REGION 933..953
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1107..1172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1172 AA; 126687 MW; A6D20BC3CA5A6C12 CRC64;
MPGFTHLHTV SGFSLRYGAS HPERLAERAS ERGMDALALT DRDTLAGTVR FAKACAGAGI
RPLFGVELAV EVPAAVRQAR RRAPVRGGAF IDESTPRVTF LAREGATGWA ELCRIVSAAH
AGSGPGGGRS EIPPLLPWSE CAAEGLTVLL GPASDVGRAL AAGRPDRAAK LLVPWRERYG
DALRLEAMWH GREGTGPGSL RLAARTVGFA AEQRVRPVLS NAVRYADPGM GPVADVLDAA
RRLVPVDPRG ELDSGEAWLK GADAMLAVAE RVVEAAGYRR DTAYRLLEQT RATAAECLVD
PEDDLGLGTV HFPEPHLVGA GRRTAQRALA SRVAAGMVRH GYGTRRAYWE RMHQELDVIA
HHGFASYFLT VAQVVDDVRR MGIRVAARGS GAGSLVNHLL DIAHADPVEH GLLMERFLSK
RRVALPDIDI DVESARRLEV YRAIIGRFGT DRVATVAMPE TYRVRHAVRD VGAALSLDPA
DIDRIAKSFP HIRARDARAA LEELPELRRL AGEKEKYGRL WELVEALDAL PRGVAMHPCG
VLLSDASLLS RTPVMPTSGE GLPMSQFDKD DVEDLGLLKL DVLGVRMQSA MAHAVAEVAR
ATGERVDLDA LDFERGAGDP ATYELIRSTE TLGCFQIESP GQRDLVGRLQ PATFHDLVVD
ISLFRPGPVA ADMVRPFIAA RHGRAPVRYP HDDLAEPLRE TYGVVVFHEQ VIDIVHLMTG
CGRDEADRVR RGLSDPGSQG RIRVWFAQHA AAKGYDAETI RRTWEIVEAF GSYGFCKAHA
VAFAVPTYQS AWLKTHHPAA FYAGLLTHDP GMYPKRLLLA DARRRGVPIL PLDVNRSAVA
HRIELVSDSG GSEDGSGEEE AWGIRLALCD VHGISEAEAA RIADGQPYTS LLDFWERARP
SRPLAGRLAQ VGALDAFGAN RRDLQLHLTE LQRSGRGAGG GQLPMAGGRR TASAGLPDLS
SAERLSAELG VLSMDVSRNL MDDHRAFLDE LGVVSARRLR EARHGETVLV AGAKAATQTP
PIRSGKRVVF TTLDDGTGLV DLAFFGDSHD ACAHTVFHSW LLLVRGVVQR RGPRSLSVVG
AAAWNLAELV ELRREGGLDA VAPRLAEPAD TGSVPDGGAF DGGRRGDTGR RIRMSTGYEM
HPWADLRPAG EEPSQGPSQV RKLWHQSPGS AG
//
