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Database: UniProt
Entry: A0A239G9S7_9MICO
LinkDB: A0A239G9S7_9MICO
Original site: A0A239G9S7_9MICO 
ID   A0A239G9S7_9MICO        Unreviewed;       867 AA.
AC   A0A239G9S7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-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=SAMN06309944_1193 {ECO:0000313|EMBL:SNS65860.1};
OS   Micrococcales bacterium KH10.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales.
OX   NCBI_TaxID=1945885 {ECO:0000313|EMBL:SNS65860.1, ECO:0000313|Proteomes:UP000198369};
RN   [1] {ECO:0000313|EMBL:SNS65860.1, ECO:0000313|Proteomes:UP000198369}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KH10 {ECO:0000313|EMBL:SNS65860.1,
RC   ECO:0000313|Proteomes:UP000198369};
RA   Kim H.J., Triplett B.A.;
RL   Submitted (JUN-2017) 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; FZPE01000001; SNS65860.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A239G9S7; -.
DR   OrthoDB; 9810148at2; -.
DR   Proteomes; UP000198369; Unassembled WGS sequence.
DR   GO; GO:0009360; C:DNA polymerase III complex; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
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-KW.
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; 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:0000256|ARBA:ARBA00022932};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198369};
KW   Transferase {ECO:0000256|ARBA:ARBA00022932}.
FT   DOMAIN          36..305
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          389..479
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          494..556
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          650..832
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        389..428
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        435..476
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        541..556
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        656..672
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        767..821
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   867 AA;  90647 MW;  A1016F6DFF01F675 CRC64;
     MSQALYRRYR PESFDEVIGQ EHVTGPLMQA LKSGRVNHAY LFSGPRGCGK TTSARILARV
     LNCAANTEES PIAVPCGSCE SCMELGRGGS GSLDVVEIDA ASHGGVDDAR DLRERATFSP
     SRDRFKIFIL DEAHMVTSAG FNALLKIVEE PPPYLKFIFA TTEPDKVIGT IRSRTHHYPF
     RLVPPEVLQP YLEQVCAAEN IVTTPGVLPL VVRAGGGSVR DSLSVLDQLI SGADGNEVSY
     EIAAGLLGFT PVTLLDDVVE AVSGQDGAGL FRVVEQVIAT GHEPRRFVED LLERFRDLLV
     LKVSGEGGAA VFSSYPADQV ERMGQQAGSL GLAQLSRAAD IINVALTEMT GATSPRLHLE
     LLCARLLLPN AESELRSVLA RVENLESGAV TSGRGSVSNV QNAPAGSAAS QQTGRGLTAP
     QSTAVVAGPT PEGSAAQPVT ETQPAQAVQP AQTAQSAPQA GQTTQHARTA PRQSPARNNV
     DAALAAATRI VREEERSAAP ATAEQTAAAP QAGGVPEPES TPPSTEKQAA PEPQPTPTSP
     TSTSEPSASA PSVSGNVTKV ETEVLMRRWD DVLAEVSALR KATWALVKQN ATVGSLDGEV
     LTLLFASEGL ASAFKSGTHA QIVAEALSRS LGVTARVTAA VGDLPQAAAA ASTAATPRES
     HRQSSSTGSS DEPAAEEPAR PADTEPVPPH DDPPPVADTP QSADEDIPLP PEPDSHDDHN
     MVPPLPEAAP VVTEPQATPV PPGNRRSSER PVLPPIPSRR SHNGEKTTEA NSSTANDKAR
     TRPWQRGNGD DSTGSTDGRN ESNATGRAAS QRETPSAQSP AEQEAAAEAA WQATDTVELE
     DSSLVGAPLI AQILGGVVID EDIEQGD
//
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