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Database: UniProt
Entry: A0A2M8W6J6_9MICO
LinkDB: A0A2M8W6J6_9MICO
Original site: A0A2M8W6J6_9MICO 
ID   A0A2M8W6J6_9MICO        Unreviewed;       908 AA.
AC   A0A2M8W6J6;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, 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=CLV34_2459 {ECO:0000313|EMBL:PJI86543.1};
OS   Luteimicrobium subarcticum.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Luteimicrobium.
OX   NCBI_TaxID=620910 {ECO:0000313|EMBL:PJI86543.1, ECO:0000313|Proteomes:UP000231586};
RN   [1] {ECO:0000313|EMBL:PJI86543.1, ECO:0000313|Proteomes:UP000231586}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22413 {ECO:0000313|EMBL:PJI86543.1,
RC   ECO:0000313|Proteomes:UP000231586};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): From Individual Species to Whole Genera.";
RL   Submitted (NOV-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   -!- 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:PJI86543.1}.
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DR   EMBL; PGTZ01000010; PJI86543.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2M8W6J6; -.
DR   OrthoDB; 9810148at2; -.
DR   Proteomes; UP000231586; 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   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; 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   4: Predicted;
KW   DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022932};
KW   Reference proteome {ECO:0000313|Proteomes:UP000231586};
KW   Transferase {ECO:0000256|ARBA:ARBA00022932}.
FT   DOMAIN          36..181
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          409..518
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          608..672
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          696..889
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        452..468
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        495..509
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        729..743
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   908 AA;  91843 MW;  6F3B3F70B661D956 CRC64;
     MSTALYRRYR PDTFADVIGQ EHVTGPLMQA LRTGRVNHAY LFSGPRGCGK TTSARILART
     LNCHRNTPEH PVDTPCGECP SCVDLARGGP GSLDVVEIDA ASHGGVDDAR ELRERATFAP
     TRDRFKVFIL DEAHMVTPQG FNALLKIVEE PPEHIRFIFA TTEPDKVIGT IRSRTHHYPF
     RLVPQDVLQP YLEQLCATED VEVGGGVLPL VIRAGGGSVR DTLSVLDQLI AGADETPSPE
     GADDSAGAAG PRGRVLGYEQ AVDLLGYTHA NLLDDVVDAL AAHDGASLFR VVERVVASGH
     EPRRFVEDVL ERLRDLVVLA VSDGDAGAVL AGLPAEQVER MRAQATALGL GELSRAADLA
     NAALTEMTGA TSPRLHLELL CARLLLPGAD DGAAGFGARL DRLERGWQAS GGPASAAPAA
     PAAPSPTASP AAASTVASDD VLGARPPRRE PSVRLAPVPT PAPEPAVATP EASPGDEVSS
     AADPSDAADP APAAPAEAAP APESPAAPAP PAAGRGAASV AHVESEVVRR RWDEVLSTLS
     RLSRAAWSLV HQNATVAGLD GNVLTLSFQS AGLQRALQGP KVEAVEQAVY ETLGFPVKVT
     AVVGGAAPAA TGAPRARENR APATTVEAPT DDAPGDRGPA SAGSRTSPPA GATVSPSVPS
     LPSPPAVASA GSDPAAGVAA AASSWGDVVV ALPGGASSVR PAPSVRPAPS VDGPAADAPR
     DADRTTDRPT PAASISGSDA PAAATQPAGS PVDPAPSDGA SAVGVASGPD DDLPPLAEPP
     HDVDDLPPWE DGAAPSVPTP SVPATPAPAT SAHAVSTREP TGQAPTVPGP ARPAPAGAGS
     TASVSTSPAG SGRPAPAVRG GGQGSSRPAP YGRPGQQRAP IPPDLVGPPL VAHMLGGVIL
     EEIVDNPD
//
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