ID A0A2T8HIP1_9SPHI Unreviewed; 1017 AA.
AC A0A2T8HIP1;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012417};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=DC487_09965 {ECO:0000313|EMBL:PVH25240.1};
OS Sphingobacterium corticibacter.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Sphingobacterium.
OX NCBI_TaxID=2171749 {ECO:0000313|EMBL:PVH25240.1, ECO:0000313|Proteomes:UP000245627};
RN [1] {ECO:0000313|EMBL:PVH25240.1, ECO:0000313|Proteomes:UP000245627}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2c-3 {ECO:0000313|EMBL:PVH25240.1,
RC ECO:0000313|Proteomes:UP000245627};
RA Li Y.;
RT "Sphingobacterium cortibacter sp. nov.";
RL Submitted (APR-2018) 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 -!- 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:PVH25240.1}.
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DR EMBL; QDKG01000003; PVH25240.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T8HIP1; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000245627; 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 Gene3D; 1.10.150.870; -; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 2.
DR InterPro; IPR011708; DNA_pol3_alpha_NTPase_dom.
DR InterPro; IPR040982; DNA_pol3_finger.
DR InterPro; IPR004805; DnaE2/DnaE/PolC.
DR InterPro; IPR029460; DNAPol_HHH.
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 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 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:UP000245627};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..68
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1017 AA; 116508 MW; 83438919005D63FE CRC64;
MYLNCRSYHS LRYGTLSIEK LVEQAAAAGA TSLALTDINT VTGIYEFAQK CHQKHIKPVV
GMEMRENNEL YYILLAKNSH GVGAICQLRT THNLEETGLP AKCPALPDTA IIYTMSQAPA
VLGEHEYIGV QPHEINLLIR PQWQRYFAKM VILAPITISD EESYQLHRIL RAIDRNVLLS
KVSKEDCCRP DEYFLPVQDL RAIFQAYPQI VANTQQLLES CSFDFEFTTP KNKKHFTDSR
ESDRLLLTEL TEKGLLRRYG ADHTLARQRA ERELKVIDEL NFSGYFLITW DIVQYSNSQG
FMHIGRGSGA NSIIAYCLGI TDICPLELDL YFERFLNLNR KVPPDFDIDW GWQERDIILR
YIFDRYGKDH VAFCGTNIAF KYRSIFRELG KVFGLPKEEL DALATQSMDQ HDTNSVVRKI
HHYANMLEQY PNQRSMHACG ILISEAPITQ YSALELPPKG FPIVQFDMHV AEGIGLEKFD
ILSQRGIGSI NDAVKIIAQN RGITIDIRNT QISKEEAQCN DHLARGQTIG CFYIESPAMR
GLLRRLKCAD YRTLVAASSI IRPGVAQSGM MKEYIFRHNY PDQFEYMHEV FREHLGETYG
IMVYQEDVIK IAMHFGGLSA ADGDVLRRAM SGKGRSLEAL QRVRSNFFDS CAQKGHDPQL
SQEVYRQVES FAGYSFCKAH SASYAVESYQ SLYLKVYYPM EFMVAVINNQ GGFYRTEVYI
HEARMSGATI QNPCVNHSDI ITTLYGTDVY LGFMHLQGLE SKLADQIVAQ RLKHGAYISL
EDLLRRVPMG IESIQTLIFI GALRFTGKSK SELLVHARLL LVSFKPQTQQ PVLLHEPARE
YTLPKLERSA FEDAFDEIEL LGFPTSCSPF DLLQTRYRGT IMVNELTQHH KKQVKMLAYL
ISRKHVPTKR GTMYFGTWVD VQGNYFDTAH FPDCLAEYPF KGGGCYLLLG TVEVDYHFPT
ITIHKMAKMA FIPDPRYAYD QKRQYDTQRR IQEDVSMTNR KPYPQAHEVN FPRQKMC
//