ID M6W3G2_9LEPT Unreviewed; 1158 AA.
AC M6W3G2;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=LEP1GSC161_1314 {ECO:0000313|EMBL:EMO59774.1};
OS Leptospira santarosai str. CBC1416.
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=1193059 {ECO:0000313|EMBL:EMO59774.1, ECO:0000313|Proteomes:UP000012149};
RN [1] {ECO:0000313|EMBL:EMO59774.1, ECO:0000313|Proteomes:UP000012149}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBC1416 {ECO:0000313|EMBL:EMO59774.1,
RC ECO:0000313|Proteomes:UP000012149};
RA Harkins D.M., Durkin A.S., Brinkac L.M., Haft D.H., Selengut J.D.,
RA Sanka R., DePew J., Purushe J., Matthias M.A., Vinetz J.M., Sutton G.G.,
RA Nierman W.C., Fouts D.E.;
RL Submitted (JAN-2013) 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:EMO59774.1}.
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DR EMBL; AKWE02000016; EMO59774.1; -; Genomic_DNA.
DR AlphaFoldDB; M6W3G2; -.
DR Proteomes; UP000012149; 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 Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 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; IPR012340; NA-bd_OB-fold.
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; SSF50249; Nucleic acid-binding proteins; 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 ECO:0000313|EMBL:EMO59774.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EMO59774.1}.
FT DOMAIN 1..58
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1158 AA; 130948 MW; 9F607DF77886337B CRC64;
MLDGAIRIKE LMQHVKENGM SSVAMTDHGN MFGAVEFYNE ATKQGIKPII GSEFYVSPNR
KQETEMVKIA DGSAYHLILL AKNEEGYKNL IRLSSKSYTE GFYKKARIDY DLLDKHSEGL
VCLTACLAGE VNRKILEGKI DESFQLAGKL NEIFRKEDFY MEIQNHGIPE QMTVAKQIYD
FGKKTGIPLV VTNDSHFLKK NDQEAQDILL RIGMQKRITD PMEFGFNGEF YVKSPDEMAR
VFPEIPEAFY NTLEISNKVN LKLQFGNYLL PEFEVPEGYD ADSYLEKLIW EGIERKYPNL
SPEIKDRVVF ELNTIKNMKF AGYFLIVQDY INYAKRNGIP VGPGRGSAAG SIVAYALGIT
NVEPLQHNLL FERFLNPDRK DMPDIDTDFC VERREEVINY IRRRYGEEKV GQIITFNSLA
AKAALKDVAR VLNLPFGEAN EMTKAFPNKL GMSIAEALAT SSELKNFSEK DDINHKIFAI
AQRLEGNYRQ PGRHAAGVVI SPYPLEEVVP LSTVAEKERP GFRSIVTQYD KNNLESIGLI
KMDILGLKNL TTLDYAIKLI ERRRGVRIDL DEISYKDANT YALLRKANTL GIFQLESTGI
TDLVAKSQVN NFDEIVALIA LYRPGPMGEG MLDEYLDRKS GRKQVTYPHP SCEPILKETF
GVPVYQEQVM SISRVVGGFS VGDSDVLRKA MAKKKADLME KLKYQFVEGA VKQGIQEKVA
KDLFEQLERF GGYGFNKSHS VAYAIITYQT AYLKANYTIE YLTALLASDH GKTTDIVKYI
NNAREMGIRI LNPDVSESQA SFNVIDDTTI RFGLSAMKGV GEAAANSIIE ARIKAGSFKT
LQDFAFNIDT RLINKKVFEA LIQAGALDSF GYTRKCLFES VDSILTFAQK EQERANEGQF
SLFGEAESSF TLNLPKDALE WEIDEKLKRE KMIAGLYLSG HPLDKYEKQL ESLKTIPIEK
FDNLKSGSKV EVAGVISSKN IKLSKRNEEF ANFKLEDRTG EIECVAFAKT YQKYKEFIKE
DQAIFIKGDL DKIEVGDTEL RGQVKVNSIE ILDDATIEDK LEKSLHLRLE ERHAEDPELI
PKLYALLACY KGESSVYFHI VENREEKSVI RAHNTYSIQP IPELFLRLAD LLGDRSVFYS
VGEQLKVINK DQVAGNVG
//
