ID A0A1M7NB60_9SPHI Unreviewed; 981 AA.
AC A0A1M7NB60;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012417};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=SAMN05216524_104536 {ECO:0000313|EMBL:SHN00797.1};
OS Mucilaginibacter sp. OK098.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Mucilaginibacter.
OX NCBI_TaxID=1855297 {ECO:0000313|EMBL:SHN00797.1, ECO:0000313|Proteomes:UP000184158};
RN [1] {ECO:0000313|EMBL:SHN00797.1, ECO:0000313|Proteomes:UP000184158}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK098 {ECO:0000313|EMBL:SHN00797.1,
RC ECO:0000313|Proteomes:UP000184158};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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};
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DR EMBL; FRCM01000004; SHN00797.1; -; Genomic_DNA.
DR RefSeq; WP_073404810.1; NZ_FRCM01000004.1.
DR AlphaFoldDB; A0A1M7NB60; -.
DR STRING; 1855297.SAMN05216524_104536; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000184158; 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 CDD; cd07431; PHP_PolIIIA; 1.
DR Gene3D; 1.10.150.870; -; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
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 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 Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..68
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 981 AA; 112179 MW; 04888584D8BF1A1B CRC64;
MYLNTHSQFS LRYGTMDIKA IVKGAKACGI EQLALTDINN SSGIMEFVRL AEKEGVKPIA
GMEFHRDKQL LYIGIARNRE GFKELNDFLT FHNVNHQPLP DQPWDFQNAY VIYPFTGDTD
LALKENEYIG IRYEQLNSLF GRPLAKIKDK LVALCPVTVS DKIEYRLHEY LRAIDLSTLL
TKVGESYKCR PNEMFLPPDD LRRQFSMYPF IISNTEKVMM ACDIKVPDEK SRNKKTFTGS
MQGDYDRLRE LTMEGMLYRF GTGHEKALKK IEEELLVIRD QGFAPYFLIT HDITTHFMKK
GYYHVGRGSG ANSTVAYCLR ITDVDPMELD LYFERFLNKS RTSPPDFDID YSWDQRVEVQ
QYIFDKYTYQ HVALLGTMST FKDRSVIREI GKVMGLPPAE IDSFTDRSIN DQRENNPAFK
KIMAVHDRMK NMPNQRSIHA GGVLISEEPI TYFTALDMPP KGMQTVQWDM YEAEAIGFEK
FDILSQRGIG HIKEAAQLIE DNKGEKVDIH DFRRFKSDGV INTQLKTSDS IGCFYIESPA
MRQLLRKLQC GDYLTLVAAS SIIRPGVAQS GMMQAYIRNF HNPENVVYLH PVMKEQLEET
YGVMVYQEDV IKVCIHFAGM DGSDADILRR GMSGKYRSKI EFDKLVDKFF IGAKALGRSD
DITAEVWRQV SSFAGYSFSK AHSASFAVES YQSLFLKTYY PMEFMVAVLN NYGGFYSRWL
YVHELQKAGA RVQLPCVNHS ETTVGIKGVD AFLGLIGISG LENRFIESIP EERHMNGPFC
GLEDFIKRTS ITLEQCITLI RVGALRFTGS SKKELLWEVH NYLGSKPPPK PVNELFNIPA
KACQLPELVN TALEDAYNEL ELLGYPVTLT MFDLLRSSFR GDVMTKDLVA HTGKIVRMVG
NYVCEKTVHT KNNKLMWFGT FLDAQGDFFD TTHFPDATPG YPFKGKGCYL IEGKVVQDFG
FPSVEVLKFF KLRIKDNPVY Y
//