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Database: UniProt
Entry: A0A147END5_9MICO
LinkDB: A0A147END5_9MICO
Original site: A0A147END5_9MICO 
ID   A0A147END5_9MICO        Unreviewed;      1051 AA.
AC   A0A147END5;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012417};
DE            EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN   ORFNames=NS354_07320 {ECO:0000313|EMBL:KTR85862.1};
OS   Leucobacter chromiiresistens.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Leucobacter.
OX   NCBI_TaxID=1079994 {ECO:0000313|EMBL:KTR85862.1, ECO:0000313|Proteomes:UP000070810};
RN   [1] {ECO:0000313|EMBL:KTR85862.1, ECO:0000313|Proteomes:UP000070810}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NS354 {ECO:0000313|EMBL:KTR85862.1,
RC   ECO:0000313|Proteomes:UP000070810};
RX   PubMed=26793183;
RA   Midha S., Bansal K., Sharma S., Kumar N., Patil P.P., Chaudhry V.,
RA   Patil P.B.;
RT   "Genomic Resource of Rice Seed Associated Bacteria.";
RL   Front. Microbiol. 6:1551-1551(2016).
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}.
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:KTR85862.1}.
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DR   EMBL; LDRK01000038; KTR85862.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A147END5; -.
DR   PATRIC; fig|1079994.3.peg.1587; -.
DR   Proteomes; UP000070810; 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:UP000070810};
KW   Transferase {ECO:0000256|ARBA:ARBA00022932}.
FT   DOMAIN          36..180
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          385..670
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          756..812
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          829..1024
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        486..507
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1051 AA;  103027 MW;  59AA37ADA691D5DD CRC64;
     MVAALYRRYR PEAFSEMIGQ SQVTDPLMTA LRTGRIGHAY LFSGPRGCGK TTSARILARC
     LNCAEGPTDS PCGVCESCVE LSRDGGGSLD VVEIDAASHG GVDDARDLRE RAVFAPARDR
     FKIFIIDEAH MVTPGGFNAL LKIVEEPPPH VKFVFATTEP EKVIGTIRSR THHYPFRLIA
     PGTLIDYVQS LCDSEGVQVE PGVLPLVVRA GGGSVRDTLS ILDQLIAGSE TALVTAERAA
     GLLGFTHAEL LDDAVAALGA HDAAAAFRAA DRVVQTGQDP RRFVEDLLER LRDLIVVNAT
     TVDGAAAIFR GVPQDQLSRM FEQARAFGRG ELSRVADVVS GALDKMAGAT APRLQLELMI
     ARALVHAPEA VAGADSAAPR IAAAPAGATP GAGNASADNA GPRPSAPGSA GPRPSAPGSA
     GPGASTAGSA GPGASAHGPQ SQSDPLAALA AARSAAAEHT APAAPTPTVP AAPVPAAPAG
     DDSNGSPASA GGQSAPNAAQ TAASIREFLT QDDAAAHAAP GGAASQSGPG AASDAQPGPP
     ASRPGADHAA ASAGAPHPNE GAAKFGRPIS AVLSSAQIES IGSDAPAPPP ETPAGPVSAV
     PGAAAAGAAA AGAAAGGAAA PQGGAAAPAT AAAGSPGTPS AGAVPSPDSA AAPATDAEAT
     GVDGAETDAS TGGYEDLLEV WPDLLEELLE LDRDAWNAVR VVAPLALDGD VLTVGLSSES
     DLAAFKSTGA GPLRETILSA VGISVKYKPK RMPAGEAAAG RGAAREPSAA ADAEEPHQAG
     SAHVPTEASA TAQADTAVDA ARAAEAAPDD DPMVRAAARL SGLGPALAAP AWADPQPDAA
     TSTANGGAAA PASSPEEPEQ VSSGAHPSAP HPGGAAPHAG PHAAGAPDAP APVPSGAGEP
     EAAVSPSSTG ALDTAAASSG AEPGEAAPRF PDPAAFGDPY ADDPGDGPDD AGEGDPYADA
     PGIAAPAGLA PTSGPAPTSG PAPTAAPHAP APNAASEPVE PATSPVSSGT PGTPATPAPP
     AARPAFTRYG EAIVREVLGA RFVEERPLPQ R
//
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