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Database: UniProt
Entry: A0A448KA93_9ACTO
LinkDB: A0A448KA93_9ACTO
Original site: A0A448KA93_9ACTO 
ID   A0A448KA93_9ACTO        Unreviewed;      1087 AA.
AC   A0A448KA93;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, 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   Name=dnaX_1 {ECO:0000313|EMBL:VEG73846.1};
GN   ORFNames=NCTC11923_00458 {ECO:0000313|EMBL:VEG73846.1};
OS   Actinomyces slackii.
OC   Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC   Actinomyces.
OX   NCBI_TaxID=52774 {ECO:0000313|EMBL:VEG73846.1, ECO:0000313|Proteomes:UP000276899};
RN   [1] {ECO:0000313|EMBL:VEG73846.1, ECO:0000313|Proteomes:UP000276899}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC11923 {ECO:0000313|EMBL:VEG73846.1,
RC   ECO:0000313|Proteomes:UP000276899};
RG   Pathogen Informatics;
RL   Submitted (DEC-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   -!- SIMILARITY: Belongs to the DnaX/STICHEL family.
CC       {ECO:0000256|ARBA:ARBA00006360}.
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DR   EMBL; LR134363; VEG73846.1; -; Genomic_DNA.
DR   RefSeq; WP_034514961.1; NZ_LR134363.1.
DR   AlphaFoldDB; A0A448KA93; -.
DR   STRING; 1278298.GCA_000428685_02133; -.
DR   KEGG; asla:NCTC11923_00458; -.
DR   Proteomes; UP000276899; Chromosome 1.
DR   GO; GO:0009360; C:DNA polymerase III complex; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR   CDD; cd00009; AAA; 1.
DR   CDD; cd18137; HLD_clamp_pol_III_gamma_tau; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 1.20.272.10; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C.
DR   InterPro; IPR022754; DNA_pol_III_gamma-3.
DR   InterPro; IPR012763; DNA_pol_III_sug/sutau_N.
DR   InterPro; IPR045085; HLD_clamp_pol_III_gamma_tau.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR02397; dnaX_nterm; 1.
DR   PANTHER; PTHR11669:SF0; PROTEIN STICHEL-LIKE 2; 1.
DR   PANTHER; PTHR11669; REPLICATION FACTOR C / DNA POLYMERASE III GAMMA-TAU SUBUNIT; 1.
DR   Pfam; PF13177; DNA_pol3_delta2; 1.
DR   Pfam; PF12169; DNA_pol3_gamma3; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF48019; post-AAA+ oligomerization domain-like; 1.
PE   3: Inferred from homology;
KW   DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932};
KW   Nucleotidyltransferase {ECO:0000313|EMBL:VEG73846.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000276899};
KW   Transferase {ECO:0000313|EMBL:VEG73846.1}.
FT   DOMAIN          36..180
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          372..514
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          595..1059
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        990..1007
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1045..1059
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1087 AA;  108657 MW;  FAC53376DF6C3DD3 CRC64;
     MTTALYRRYR PDTFQDVIGQ EHVTAPLMAA LRAERVTHAY LFSGPRGCGK TTSARILARC
     LNCAQAPTDT PCGQCPSCRN LATGGPGSLD VVEIDAASHN GVDDARDLRE RAAFAPARDR
     YKIFILDEAH MVTAQGFNAL LKLVEEPPAH VKFIFATTEP EKVIGTIRSR THHYPFRLVP
     PDTLEGYLGH LCGAEGVSAG PGVFPLVVRA GGGSVRDTLS VMDQLIGGAV DGAVDYQRAV
     ALLGYTDTTM LDQCVDAIAA GDGAGVFRVV DRVVTSGHDP RRFVEDLLQR LRDLLVIALA
     GSQAGPALGS LPDDELTRMD LQARTMGAAV LSRAADTTAQ ALTAMVGATS PRLQLELLVA
     RLVIPAQPRG EAQAPAAPVG SAGSAGPAQQ GGQVAPAASA GAGSGRAVAG TTAPASRPGE
     TPAGPGGASG SDGPAAGAGS PVVVDWEGTG ASAPASPSPE PTQARAAAQA PQAAPQAVSA
     PPAVEDSGAA DGERPQPGVP SSPPAAAQGP GAAEAEMIRT RWEEVLEAAK RSRRATWALV
     GPNSRPGTLT AGVFTLLFNA PGLVGAFENG GHGPIFSAAI HQALGLRVEV HAILAGPDGP
     GGPGGPGGGA PDPSVPSGPG GQADWAAPVA PASAGDVGGW ERSASPGGGA LGPQALDQGS
     ASGVEPDPRA SAAALGPEPE EEPGEPTAAE EPEPVWDEAV PPEPLADVEV PASEPANEPA
     NEPANELANQ SAYEEAESWT PGPGTTVPWA GESAIEQDWA VGPAAGRGMP QAQAAPGSEP
     SEEIGAEPQG QSDRPEPATA TPVADDAAPG DQAADISVPP VEDPAPADDG WGPVAVPGGQ
     ATPDAAGSVE ADGGSGPASV DDDGWGPVAV PGGQATPDAA ESVEADGGSG PALADDDGWG
     PVAVPGGQAS PAAVEPAEAP EDSGAGERDG AQVPAASPEP EAPLATVHRL RALPPMPEPQ
     PQQAAPQRPG LTPVSWDGPA FSDGVPLPEE PGDPDGPAGP EPASPGIAAP SPDAATWTPT
     GVPGSKLAAA MAAARAAAEA TEFSLEEDTP SEDDEDAEDA GVVGLEVVKR ILGATVIEEV
     TVTQEGH
//
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