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Database: UniProt
Entry: A0A095ZJV9_9BACT
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ID   A0A095ZJV9_9BACT        Unreviewed;      1235 AA.
AC   A0A095ZJV9;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE            EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN   ORFNames=HMPREF2137_05525 {ECO:0000313|EMBL:KGF34983.1};
OS   Hoylesella buccalis DNF00853.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Hoylesella.
OX   NCBI_TaxID=1401074 {ECO:0000313|EMBL:KGF34983.1, ECO:0000313|Proteomes:UP000029556};
RN   [1] {ECO:0000313|EMBL:KGF34983.1, ECO:0000313|Proteomes:UP000029556}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DNF00853 {ECO:0000313|EMBL:KGF34983.1,
RC   ECO:0000313|Proteomes:UP000029556};
RA   McCorrison J., Sanka R., Torralba M., Gillis M., Haft D.H., Methe B.,
RA   Sutton G., Nelson K.E.;
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   -!- 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:KGF34983.1}.
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DR   EMBL; JRNN01000061; KGF34983.1; -; Genomic_DNA.
DR   RefSeq; WP_036872450.1; NZ_JRNN01000061.1.
DR   AlphaFoldDB; A0A095ZJV9; -.
DR   OrthoDB; 9803237at2; -.
DR   Proteomes; UP000029556; 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: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          5..82
FT                   /note="Polymerase/histidinol phosphatase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00481"
SQ   SEQUENCE   1235 AA;  140791 MW;  C210EAC0838D95BD CRC64;
     MNDFVHLHVH TYYSILDGQS PVKRLVDKAV TDGMRGLAIT DHGNMFGIKE FFDYANTVNK
     QLKADGKQPF KPIFGCEMYV ARRSRFDKVK DMGDMSGYHL IVLAKNYRGY KNLIKLVSHA
     WEEGYYMRPR TDREELEKYH EDLIVCSACL AGEVPRKIIA GDMAGAREAV EWYKRVFGDD
     YYLEIQRHEV KDPSIRANRE AYPMQQRANQ LIFNLAKEYG IKVVCTNDVH FVDKENAEAH
     DHLLCLSTGK DLDDPTRMLY SKQEWFKTRE EMNSIFSDVP ETMANTIEIL NKVETYSINH
     DPIMPNFPIP ESFGKEEDWK QKFTEEDLLR EFTTDENGEN PMSEEDAQKR VDHLGGYEKM
     YRIKFEADYL QHLAYEGAKP LYGDPLPKEV DDRIRFELHV MKTMGFPGYF LIVSDFIRAA
     REELGVMVGP GRGSAAGSVV AYCLGITKID PLKYDLLFER FLNPDRISLP DIDTDFDDDG
     RGKVLKWVMD KYGHENCAHI ITYGSMATKN SIKDVARVEK LPLERANALC KAIPDRLPDK
     MKMNLTNAIK CTPELQMAEA STDIRESNTI KYAKMLEGTV RGTGIHACGF IICRDPISDW
     VPVSTADDPD FKDEKTNCTQ YDGHVIEETG LIKMDFLGLK TLSELKEAVK NVKLTKNIDI
     DLDKIPIDDE LTYKLYQEGR TIGTFQFESA GMQNYLRQLS PTKFEDLIAM NALYRPGPMD
     NIPSFIARKK GEEEITYPIP VMERYLKDTY GITVYQEQVM LLSRLLANFT RGESDALRKA
     MGKKKKAIVD AMKPKFIEGG KKNGYDENVL DKIWADWEKF ASYAFNKSHA ACYSWVAFQT
     AYLKAHYPAE FMAAIMSRRK DQITEISKLM DECKSLRIAT LGPDVNESYQ KFGVNHKGEI
     RFGLAAIKGM GDAAATAIIQ EREAHGLYQD IFDFAHRVDF TQVNRKAFES LALSGGFDSF
     GIPRESYFTA NNKGELFIDT LVRYGQLYQN KKSEIEHSLF GGVDAVEIAT PPIPKPELWS
     NIEKLNREHD LVGIYLSAHP LDEFSIVLKS MCNTSCTELG DKAELAKKAD VVFAGMITDV
     KDKFTRTGKP CGFVTIEDFS GTGEIAFFGE EWGKWKGMMV VGSTVYLTGK CSQRYRDSNY
     YDFRINDVQY LQTVRDKQIH RLTIVVDSEA IDEVVVNDIV SMLQDSKGNT QLCFQVADKQ
     HQTSILLHSG LHQISLGHDL IRYIEGNPNM NYLVN
//
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