ID F9YVB1_CAPCC Unreviewed; 1485 AA.
AC F9YVB1;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012417};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN OrderedLocusNames=Ccan_10400 {ECO:0000313|EMBL:AEK23156.1};
OS Capnocytophaga canimorsus (strain 5).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Capnocytophaga.
OX NCBI_TaxID=860228 {ECO:0000313|EMBL:AEK23156.1, ECO:0000313|Proteomes:UP000008895};
RN [1] {ECO:0000313|EMBL:AEK23156.1, ECO:0000313|Proteomes:UP000008895}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5 {ECO:0000313|Proteomes:UP000008895};
RX PubMed=21914877; DOI=10.1128/JB.05853-11;
RA Manfredi P., Pagni M., Cornelis G.R.;
RT "Complete genome sequence of the dog commensal and human pathogen
RT Capnocytophaga canimorsus strain 5.";
RL J. Bacteriol. 193:5558-5559(2011).
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; CP002113; AEK23156.1; -; Genomic_DNA.
DR RefSeq; WP_013997146.1; NC_015846.1.
DR STRING; 860228.Ccan_10400; -.
DR KEGG; ccm:Ccan_10400; -.
DR eggNOG; COG0587; Bacteria.
DR HOGENOM; CLU_001600_1_1_10; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000008895; Chromosome.
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; cd06127; DEDDh; 1.
DR CDD; cd04485; DnaE_OBF; 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; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 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; IPR013520; Exonuclease_RNaseT/DNA_pol3.
DR InterPro; IPR004013; PHP_dom.
DR InterPro; IPR003141; Pol/His_phosphatase_N.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
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; PF00929; RNase_T; 1.
DR SMART; SM00479; EXOIII; 1.
DR SMART; SM00481; POLIIIAc; 1.
DR SUPFAM; SSF53098; Ribonuclease H-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:AEK23156.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008895};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AEK23156.1}.
FT DOMAIN 1..192
FT /note="Exonuclease"
FT /evidence="ECO:0000259|SMART:SM00479"
FT DOMAIN 261..349
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1485 AA; 169212 MW; 4024DDFEDE669650 CRC64;
MYLIFDTETT GLPKRWDAPI TDSDNWPRAV QIAWQLHDRH GELIEHKDFL ITPDDFNIPY
DAEKVHGIST ELAQQQGVSI QKVFEEFNEA LQKSTYVVGQ NIGFDINIMG AEFHRYGVDS
PLVNMPVLDT CTEITAELCK ISGGRGGRYK LPTLTELHEF LFNVPFAEAH NATADVEATT
RCFFELIRIG QGFETKDISA EYITEFQQYN PAEIQPIGLK HINLKKASEE IRKEIQKQSG
SGLSEQEINA NIALLEKAPF AHLHNHTQFS VLQATTSIQS LVKKTIQEKM PAVAMTDSGN
MMGAFHFIKE VLGHNKSAKA KNDEAIEKGE TPSEIEIKPI VGCEFNVCEN HLDKSHQDNG
YQVVMLAKNK NGYHNLAKMA SIAYTDGYYY VPRIDRNIVE KYKENLIVLT GGMNGEVPSK
VLNIGEKQAE TALLWWKNLF GEDLYIELMR HNQEDENRVN QVLIELSKKH QVKLVATNNT
FYINQKDANA HDILLCVKDG EKQATPIGRG RGYRFGMPNQ EYYYKSAEQM KTLFKDVPEA
ILNIQEIIDK IEIYNLAREV LLPKFQIPDE FLVEDDPDGK KGENKYLRHL TYLGAEKRYE
LPLSEEVIER LDFELMIIEK TGYPGYFLIV QDFIAAAREM GVSVGPGRGS AAGSAVAYCL
GITNIDPIKY DLLFERFLNP DRVSMPDIDI DFDDEGRSLV MDYVINKYGK NQVAQIITYG
TMAAKSSIRD TARVLDLPLH ESDRIAKLVP NMKLAKIFSM DDKQLKEKLR SDELPKVNEL
KQIAEGTDLA AETLQQAQVL EGSVRNTGIH ACGVIITPDD ITNFVPVSVA KDSDLFVTQF
DNSVVESAGL LKMDFLGLKT LTLIKDSVEL IKRRNGIEIN PDEIPIDDKK TYELFQRGET
VGIFQYESPG MQKYMRELKP TVFADLIAMN ALYRPGPLEY IPSFIKRKHG TEPIVYDLDA
MEEYLKETYG ITVYQEQVML LSQKLAGFSK GDADMLRKAM GKKIFALLEK LKPKFVEGGI
KNGHPADILE KIWKDWEAFA SYAFNKSHST CYAWIAYQTA YLKANYPAEF MAAVLSNNMN
DIKQVSFFLE ECQRMGIKVL SPDVNESFYK FTVNKDGNIR FGMGAIKGVG KNAVETIVDS
RKDGNYTSIF DVTRRVDFRN INKKAFENIA LAGGFDSFTK VHRAQYFHDE GDGIVFLEKA
IRYGNKYQEN KNSPQMSLFG ESSGVEIPEP TIPNCESWGN LEQLRREKEV VGIYISGHPL
DDFKHSLDNF CNLSLTQLQD LSPLINREIS IAGMITDVQH RTSKNGKGWA SFILEDYEGS
HEFRLFNDDY LKFRNYLILG TFLYCKFVVK EGWQKKDNNE KAEPRIQFTM MMQLQDVLTN
LAKKIALHLN IKDISTDLIK NYKNIIEKHR GNYPITFIVH NMEENIHLNM DNGQLKVDIS
KEFLEELDQK SVSYVLNDRK MEKLITKKKE EVEEEQLEVE LIEEN
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