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Database: UniProt
Entry: A0A0I9TVH0_9MYCO
LinkDB: A0A0I9TVH0_9MYCO
Original site: A0A0I9TVH0_9MYCO 
ID   A0A0I9TVH0_9MYCO        Unreviewed;      1177 AA.
AC   A0A0I9TVH0;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE            EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN   ORFNames=ABH38_09400 {ECO:0000313|EMBL:KLO37111.1};
OS   Mycobacterium haemophilum.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=29311 {ECO:0000313|EMBL:KLO37111.1, ECO:0000313|Proteomes:UP000036334};
RN   [1] {ECO:0000313|EMBL:KLO37111.1, ECO:0000313|Proteomes:UP000036334}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UC1 {ECO:0000313|Proteomes:UP000036334};
RA   Greninger A.L., Cunningham G., Miller S.;
RT   "Genome sequence of Mycobacterium haemophilum.";
RL   Submitted (MAY-2015) 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:KLO37111.1}.
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DR   EMBL; LDPR01000006; KLO37111.1; -; Genomic_DNA.
DR   RefSeq; WP_047313897.1; NZ_LDPT01000003.1.
DR   AlphaFoldDB; A0A0I9TVH0; -.
DR   STRING; 1202450.B586_12910; -.
DR   PATRIC; fig|29311.18.peg.2694; -.
DR   OrthoDB; 9803237at2; -.
DR   Proteomes; UP000036334; 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   Reference proteome {ECO:0000313|Proteomes:UP000036334};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          7..74
FT                   /note="Polymerase/histidinol phosphatase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00481"
SQ   SEQUENCE   1177 AA;  128611 MW;  A6BAE7EDD193908C CRC64;
     MNQSSFVHLH NHTEYSMLDG AAKITPMLAE VERLQMPAVG MTDHGNMFGA SEFYNTASKA
     GIKPIIGVEA YIAPGSRFDT RRITWGDPSQ KADDVSAGGA YTHLTMVAEN AAGLRNLFKL
     SSLASFEGQL SKWSRMDAEL IAEHAEGIII TTGCPSGEVQ TRLRLGHDRE ALEAAAKWRE
     IVGPDNYFLE LMDHGLSIEQ RVREGLLDIG RKLNIPPLAT NDCHYVTRDA AHNHEALLCV
     QTGKTLSDPN RFKFDGDGYY LKSAAEMRQL WDDQVPGACD STLLIAERVQ SYAEVWEPRN
     RMPVFPVPEG HDQASWLRHE VDAGLGRRFP GGPPDGYVER AAYEIDVICD KGFPAYFLIV
     ADLINYARSV GIRVGPGRGS AAGSLAAYAL GITDIDPIPH GLLFERFLNP ERTSMPDIDI
     DFDDRRRGEM VRYAADKWGH DRVAQVITFG TIKTKAALKD SARIHYGQPG FAMADRITKA
     LPPPIMAKDI PLSGITDPAH ERFKEAAEVR SLIETDPDVR TIYQTARGLE GLIRNAGVHA
     CAVIMSSEPL TEAIPLWKRP QDGAIITGWD YPSCEAIGLL KMDFLGLRNL TIIGDAIENI
     KANRGIDLDL ESVPLDDQAT YELLGRGDTL GVFQLDGGPM RDLLRRMQPT GFEDIVAVLA
     LYRPGPMGMN AHNDYADRKN NRQAIKPIHP ELEEPLREIL AETYGLIVYQ EQIMRIAQKV
     ASYSLARADI LRKAMGKKKR EVLEKEFEGF SEGMQANGFS AGSIKALWDT ILPFADYAFN
     KSHAAGYGLV SYWTAYLKAN FAGEYMAGLL TSVGDDKDKA AVYLADCRKL GITVLPPDVN
     ESGLNFASVG VDIRYGLGAV RNVGANVVGS LIKTRSDKGK FVDFSDYLNK IDISACNKKV
     TESLIKAGAF DSLGHSRKGL FLVHTDAVDS VLGTKKAEAI GQFDLFGGTD AGTDAVFTIK
     VPDDEWEDKH KLALEREMLG LYVSGHPLNG VAHLLAAQVD TAIPTILDGD VSNDTQVRVG
     GILAAVNRRV NKNGMPWASA QLEDLTGGIE VMFFPHTYSS YGADIIDDAV VLVNAKVAVR
     DDRIALIANE LVVPDFSNAQ ADRPLAVSLP TRQCTFDKVS ALKQVLARHP GTSQVHLRLI
     SGDRITTLEL DQSLRVTPSP ALMGDLKALL GPGCLGG
//
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