ID   W2YGW3_PHYPR            Unreviewed;       524 AA.
AC   W2YGW3;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=AAA+ ATPase domain-containing protein {ECO:0000259|SMART:SM00382};
GN   ORFNames=F442_17684 {ECO:0000313|EMBL:ETP33868.1};
OS   Phytophthora parasitica P10297.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=1317064 {ECO:0000313|EMBL:ETP33868.1, ECO:0000313|Proteomes:UP000018948};
RN   [1] {ECO:0000313|EMBL:ETP33868.1, ECO:0000313|Proteomes:UP000018948}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P10297 {ECO:0000313|EMBL:ETP33868.1,
RC   ECO:0000313|Proteomes:UP000018948};
RG   The Broad Institute Genomics Platform;
RA   Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA   Machado M., Johnson C.S., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Phytophthora parasitica P10297.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family. RarA/MGS1/WRNIP1
CC       subfamily. {ECO:0000256|ARBA:ARBA00008959}.
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:ETP33868.1}.
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DR   EMBL; ANIY01003694; ETP33868.1; -; Genomic_DNA.
DR   AlphaFoldDB; W2YGW3; -.
DR   EnsemblProtists; ETP33868; ETP33868; F442_17684.
DR   Proteomes; UP000018948; Unassembled WGS sequence.
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:0006260; P:DNA replication; IEA:InterPro.
DR   CDD; cd00009; AAA; 1.
DR   CDD; cd18139; HLD_clamp_RarA; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 1.20.272.10; -; 1.
DR   Gene3D; 1.10.3710.10; DNA polymerase III clamp loader subunits, C-terminal domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR032423; AAA_assoc_2.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C.
DR   InterPro; IPR021886; MgsA_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR13779:SF7; ATPASE WRNIP1; 1.
DR   PANTHER; PTHR13779; WERNER HELICASE-INTERACTING PROTEIN 1 FAMILY MEMBER; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF16193; AAA_assoc_2; 1.
DR   Pfam; PF12002; MgsA_C; 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   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018948}.
FT   DOMAIN          118..235
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          29..93
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          255..276
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..52
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        258..276
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   524 AA;  58084 MW;  94B95619B1840D4C CRC64;
     MATTECPICS RHVRAENLML HVDACLAKQD QPKTQFRSPS PSAKTKSPTT SRTPNRSPPP
     QNSPSSSALK KRKRSTTDDV SAVPLAERMR PKDLDDLVGQ EELLGPGSLL SALIEADRVP
     NMILWGPPGC GKTTLAHVIS KNTDCKFISL SGATSKAGDM KDAVDRARGE RKMFRRRTIV
     FVDEIHRFNK SQQDFFLPPV EDGTITLIGA TTENPSFEVN NALLSRCRVY TLKKHTPESI
     EKIIRRALRD HAAGGVRSLK QSETQSNGGS LDQDDNANEV SIEAEDEAVK YLATQCAGDA
     RAALNCLEMA LQTAPMDTEK QVLRVSATHV KHCFAHRQTL FYDRNADMHY DVISALHKSI
     RGSDENATLY WLARMLEGGE NPLYVARRLI RVASEDVGLA APELLPMAVS AYQAAHFVGM
     PECDVVLAHV ATMLARAPKS IEVYAAYKRA KQSIHEWNKG ALPDVPLHIR NAPTKLMKEL
     GYAKGYKYNP HYTAEELKDQ TYLPDELLGT NFFEEAKTNR DAEC
//