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Database: UniProt
Entry: A0A3S9PF08_STRLT
LinkDB: A0A3S9PF08_STRLT
Original site: A0A3S9PF08_STRLT 
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
//
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