ID N1WIW0_9LEPT Unreviewed; 1158 AA.
AC N1WIW0;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=LEP1GSC060_3176 {ECO:0000313|EMBL:EMY77029.1};
OS Leptospira weilii serovar Ranarum str. ICFT.
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=1218598 {ECO:0000313|EMBL:EMY77029.1, ECO:0000313|Proteomes:UP000012313};
RN [1] {ECO:0000313|EMBL:EMY77029.1, ECO:0000313|Proteomes:UP000012313}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ICFT {ECO:0000313|EMBL:EMY77029.1,
RC ECO:0000313|Proteomes:UP000012313};
RA Harkins D.M., Durkin A.S., Brinkac L.M., Haft D.H., Selengut J.D.,
RA Sanka R., DePew J., Purushe J., Hartskeerl R.A., Ahmed A.,
RA van der Linden H., Goris M.G.A., Vinetz J.M., Sutton G.G., Nierman W.C.,
RA Fouts D.E.;
RL Submitted (MAR-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:EMY77029.1}.
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DR EMBL; AOHC02000041; EMY77029.1; -; Genomic_DNA.
DR AlphaFoldDB; N1WIW0; -.
DR STRING; 1218598.LEP1GSC060_3176; -.
DR Proteomes; UP000012313; 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:EMY77029.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EMY77029.1}.
FT DOMAIN 1..58
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1158 AA; 131054 MW; 4550AE47D2161FF5 CRC64;
MLDGAIRIKE LMQHVKEQGM SSVAMTDHGN MFGAVEFYNE AMKQGIKPII GSEFYVSPNR
KQESEMVKIA DGNAYHLILL AKNEEGYKNL IRLSSKSYTE GFYKKARIDY DLLDRHSNGL
VCLTACLAGE VNRKILEGKI DESFQLAGKL NEIFRKEDFY MEIQNHGIPE QMTVAKQIHD
FGKRSGIPLV VTNDSHFLKK NDQEAQDILL RIGMQKRITD PMEFGFNGEF YVKSPDEMAR
IFPEIPEAFH NTLEISNKVN LKLQFGNYLL PEFEVPDGYD ADSYLEKLIW EGIGRKYPNL
SPEIKDRVVF ELNTIKNMKF AGYFLIVQDY INYAKRNGIP VGPGRGSAAG SIVAYALGIT
NVEPLQHNLL FERFLNPDRK DMPDIDTDFC VERREEVINY IRRRYGEERV GQIITFNSLA
AKAALKDVAR VLNLPFGEAN EMTKAFPNKL GMSIAEALTA SSELKNFSEK DDINHKIFAI
AQRLEGNYRQ PGRHAAGVVI SPYPLEEVVP LSTVAEKERP GFRSIVTQYD KNNLESIGLI
KMDILGLKNL TTLDYAIKLI EQRRGIRINL DEISYDDANT YALLRKANTL GIFQLESTGI
TDLVAKSQVS NFDEIVALIA LYRPGPMGEG MLDEYLDRKS GKKQVTYPHP SCESILKETF
GVPVYQEQVM SISRVVGGFS VGDSDMLRKA MAKKKADLME KLKGQFVEGA VKQGTQEKVA
KDIFEQLERF GGYGFNKSHS VAYAIITYQT AYLKANYTIE YLTALLASDH GKTTDIVKYI
NNAREMGIRI LNPDVSQSQT SFSVIDDTTI RFGLSAMKGV GETAANSIIE ARTKVENFKT
LQGFALNIDT RLINKKVFEA LIQAGALDSF GYTRKCLFES VDSILTFAQK EQERTKEGQF
SLFGGEESSF TLNLPKDALE WEIDEKLRRE KAIAGLYLSG HPLDKYEKQL KSLRTIPIEK
FDDLKSGTKV EVAGVISSKN IKLSKRNEEF ANFKLEDRTG EIECVAFAKT YQKYKEFIKE
DQAIFIKGDL DKIEVGDTEL RGQVKVNSIE ILDDTTIEEK LEKSLHLRLE ERHTEDPELI
PKLYALLACY KGESSVYFHI VENQEEKQVI RAHDTYSIQP IKELFLRLAD LLGDRTVFYS
VGEQIKPINK NQIADNVG
//
