ID A0A3S9PF08_STRLT Unreviewed; 1161 AA.
AC A0A3S9PF08;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 14.
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=EKH77_06675 {ECO:0000313|EMBL:AZQ70940.1};
OS Streptomyces luteoverticillatus (Streptoverticillium luteoverticillatus).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=66425 {ECO:0000313|EMBL:AZQ70940.1, ECO:0000313|Proteomes:UP000267900};
RN [1] {ECO:0000313|EMBL:AZQ70940.1, ECO:0000313|Proteomes:UP000267900}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 15060 {ECO:0000313|EMBL:AZQ70940.1,
RC ECO:0000313|Proteomes:UP000267900};
RA Feng Z., Chen G., Zhang J., Zhu H., Yu X., Zhang W., Zhang X.;
RT "The whole draft genome of Streptomyce luteoverticillatus CGMCC 15060.";
RL Submitted (DEC-2018) 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}.
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DR EMBL; CP034587; AZQ70940.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S9PF08; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000267900; Chromosome.
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:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd04485; DnaE_OBF; 1.
DR Gene3D; 1.10.150.870; -; 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 Reference proteome {ECO:0000313|Proteomes:UP000267900};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 14..81
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1161 AA; 124128 MW; 97917191CDEBB304 CRC64;
MAAAFRATPG SGFTHLRVAS GFSARYGAAH PERLAERAAE RGMDALALTD RDSLAGAVRF
AKAAAGAGVR PLFGVDLAVS GPLPADGPTV RHRAPARGGA FVDESAPRAV FLARDGAPAW
AALCGLVSAA HVSGAERPEV PREELARAAT GIRAPLTVLL GPDSETGRAL AAGRPDRAAR
LLRPWREMFG DGLRLEAVWH GRTGTGPGSL RLAARTVGFA ADQGVRAVLS NAVRYADPGQ
GPVADVLDAA RRLVPTGRRP EALDSGERWL KDPAAMTAAA ARIAEAAGLG RAGAHRLLAT
TEDTAAECLV DPQDHLGLGS VHFPEPHLVG TGPRTSARVL RSRCAAALVR RDRDRDRRYW
DRLDDELRIV EQRGLASYFL TVAQVVDDTR ALGIRVTARG SGAGSLVNHL LGIAHADPVE
HGLLMERFLS TRRTALPDID IDVESARRLD VYRAIFDRFG AERVATVAMP ETYRIRHAVR
DVGAALGMAP DVVDRLAKSF PHIRARDARA ALAELPELRE IAAGPLGPGN TRLWELVEAL
DALPRGVAMH PCGVLLSDAT LRARTPVVPT SGEGFAMSQF DKDDVEDLGL LKLDVLGVRM
QSAMAHAVGE LERATGRRID LDDPAQVPPG DRRTYALIRS TETLGCFQIE SPGQRDLIGR
LQPSTFHDLV VDISLFRPGP VAADMVRPFI EARHGRAPAR YPHPDLKEAL AETHGVVVFH
EQIIEILRIM TGCDRGCADE TRRALSDPAR VGRVRDWFAS AAEARGYAPD AVRRTWEIVE
AFGSYGFCKA HAVAFAVPTY QSAWLKAHHP AAFYAGLLTH DPGMYPKRLL LADARRRGVP
ILPLDVNRSG TAYSIELVSD GVSGDGVLGV RLALSEVQGI SEAEARRIVA GRPYTSLQDL
WQRARPGRPV TERLARVGAL DAFGANRRDL LLHIAELHRG GRRVSAAQPT LIDSARTEPA
GLPDLDAAER LGAELSVLGM DASRHLMTDH RAFLTELGAI PARRLRDARH GETVLVAGAK
AATQTPPVRS GRRVIFTTLD DGTGLVDCAF FDDSHAACAH VVFHSWLLLV RGVVQRRGPR
SLSVVGAAAW DLGELAALRA EGGLGAVATV LAAPAAPGGP VGRRIRLSNG YAMHPWADLQ
PAGEGAPTGR KLWHASSGSA G
//