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Database: UniProt
Entry: A0A1W9P859_9BACT
LinkDB: A0A1W9P859_9BACT
Original site: A0A1W9P859_9BACT 
ID   A0A1W9P859_9BACT        Unreviewed;      1207 AA.
AC   A0A1W9P859;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE            EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN   ORFNames=B5M48_00550 {ECO:0000313|EMBL:OQX54588.1};
OS   Candidatus Omnitrophica bacterium 4484_213.
OC   Bacteria; Candidatus Omnitrophota.
OX   NCBI_TaxID=1968528 {ECO:0000313|EMBL:OQX54588.1, ECO:0000313|Proteomes:UP000192577};
RN   [1] {ECO:0000313|Proteomes:UP000192577}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Dombrowski N., Seitz K., Teske A., Baker B.;
RT   "Novel pathways for hydrocarbon cycling and metabolic interdependencies in
RT   hydrothermal sediment communities.";
RL   Submitted (MAR-2017) 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   -!- 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:OQX54588.1}.
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DR   EMBL; MZGK01000002; OQX54588.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W9P859; -.
DR   STRING; 1968528.B5M48_00550; -.
DR   Proteomes; UP000192577; Unassembled WGS sequence.
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   CDD; cd12113; PHP_PolIIIA_DnaE3; 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:SF0; DNA POLYMERASE III SUBUNIT ALPHA; 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   4: Predicted;
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          28..95
FT                   /note="Polymerase/histidinol phosphatase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00481"
SQ   SEQUENCE   1207 AA;  137580 MW;  7A51BCF959398A1B CRC64;
     MLKAVLHILG TSNQTNTSLP NVTHANFAHL HVHSQYSLLD GACKLPDLIK RSIELKFPAI
     AITDHGNMFG AIEFYQEAMK QGIKPIIGYE AYLAPESRFN RDPEVEKRGR KHLTLLVKDL
     KGYKNLVKLA TAAYLEGFYY KPRIDKEILS QYSEGLIGLS GCLHGEIPNY IINDQIDKAK
     KAIIDFQDIF GKDNFYLELQ DQLIPEQKKV NRELIKIAKE MNIELVATND VHYLHKSDSY
     NHEILLCLQT QTTLDDPKRM RFSTNKFYLK SEEEMKELFS EIPSALTNTL KVVNKCNLEL
     DFSKKYMPVF SPPQGLTDKE YLKELCQQRL KERFKEVHPE FSDTSVGGAS KAQFNGINPV
     KSAKGAVRPS ELFSRVNEEV IQRMNQELKI IEESGYASYF LIVQDFINFA KKNNIAVGPG
     RGSVAGSLVA YILGITDINP LKYNLLFERF LNYERITMPD IDIDFCYQRR DEVIDYVTQK
     YSKENVSQII TFGTMAAHGV IRDVGRVMGM PYSEVDRIAK LVPLTLNITI QEALYQEPRL
     KELYEQDKQI KRLLDISKSL EGLTRHASTH AAGVVISKQP LSDIVPLFKS PDGKIATQYS
     MFSLEKIGLL KMDFLGLRTL TVISKTIENI RRFSGKEISV ESIPLDDKKT YHLLCKGKST
     GVFQLESAGM QDLLKRIEPQ NFEDIIAILA LHRPGPLGSG MINDFVQRKH NPKLIKYDHP
     KLKPILKETY GIILYQEQIM QIAHILAGFS LTQADLLRRA ISKKIPEVIE QQKESFVEGC
     LKNGIRRRVA EKVFNLIEYF SGYGFNKSHS AAYALISYRT AYLKANCPLQ FMAALLTSEE
     DNTDKIADYV EECRKMGIRI LPPDVQQSFA EFTVEKDSIR FGLLAVKNVG RGAIDSIIKA
     RTRKNFFSLE DFCQRVDLRL VNKKVIESLI KCGAFDCFNL PRAQLIVDLE GSLQRANRLQ
     RDKSRGQLSL LDNLSYFEPR KEEKKITIKE WPRNQLLAFE KELLGFYFSG HPLAEYEQVL
     KRYSVSFTEL NNYSENEEVL VGGVVTKIKQ IVTKRGEKMA FFNLEISNGA IEIILFPKVF
     NKVSNYVKID APIFVEGKIS LRNNERKIIA EKLIPIEQIS QKYTASISLN LEADSDENLL
     RQIKRLVSAH QGDVPLYLIF SSPRGKHTIR SSLTAKCTES FLLQLEQLIG KERVTVEVNP
     VRKGGAF
//
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