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Database: UniProt
Entry: A0A316V8T9_9BASI
LinkDB: A0A316V8T9_9BASI
Original site: A0A316V8T9_9BASI 
ID   A0A316V8T9_9BASI        Unreviewed;       794 AA.
AC   A0A316V8T9;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=AFG1-like ATPase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=FA14DRAFT_161535 {ECO:0000313|EMBL:PWN33910.1};
OS   Meira miltonrushii.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Exobasidiomycetes; Exobasidiales; Brachybasidiaceae; Meira.
OX   NCBI_TaxID=1280837 {ECO:0000313|EMBL:PWN33910.1, ECO:0000313|Proteomes:UP000245771};
RN   [1] {ECO:0000313|EMBL:PWN33910.1, ECO:0000313|Proteomes:UP000245771}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCA 3882 {ECO:0000313|EMBL:PWN33910.1,
RC   ECO:0000313|Proteomes:UP000245771};
RX   PubMed=29771364; DOI=10.1093/molbev/msy072;
RA   Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA   Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA   Spatafora J.W., Aime M.C.;
RT   "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT   clade Ustilaginomycotina.";
RL   Mol. Biol. Evol. 0:0-0(2018).
CC   -!- SIMILARITY: Belongs to the AFG1 ATPase family.
CC       {ECO:0000256|ARBA:ARBA00010322}.
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DR   EMBL; KZ819604; PWN33910.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A316V8T9; -.
DR   InParanoid; A0A316V8T9; -.
DR   OrthoDB; 1617at2759; -.
DR   Proteomes; UP000245771; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR005654; ATPase_AFG1-like.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; NF040713; ZapE; 1.
DR   PANTHER; PTHR12169:SF2; AFG1P; 1.
DR   PANTHER; PTHR12169; ATPASE N2B; 1.
DR   Pfam; PF03969; AFG1_ATPase; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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:UP000245771}.
FT   REGION          538..561
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          597..624
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          722..794
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        603..623
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        751..794
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   794 AA;  89891 MW;  E910D81818266838 CRC64;
     MILRYSSRWQ PVRQSASLRL QSALTVRLLH HTPSTSQAYP ADLQTTDPLI AYRALASKGV
     LEEDAEQIRA LIELRKLTRV LQDYTPPSHL LGILHDPNGQ NGKGDLGSGG PPASEENVNA
     LVRYLSEEEQ VESLDTPKGL LLTGKPGTGK TFLVDLWFEH LPVQGKFRRH YHHMLLSIYR
     MVWVEAERRR IDAEAQWSSR ESVLPERGVG VVWERQEQNE TGSRTKSISQ WAKKLRGMPF
     MRLGSDAPAP VMSLDGASLN DDANKGMDVI KLAQLERQED KLAGLGTTLP MHVAAQLFLT
     HGHVLLLDEL QLLDIASATL LRRILTSYWR LGGVVIATSN RVPEDLYANN VQRRSLVAFL
     GALKERCPVV EVSGRDRRID RWKEGWDKFA QRGEKDDKSF FFLKSRPDED KAFQQIKDSL
     IAGRQREATV FDVYNRKVSV PESYPAVDGH PATACYTFDQ LCDQPLGPAD YLTLSSTYEL
     LILDDVPALD LVHRNQARRL ITLIDCLYES RTKLIIRSQV PLTKIFFARE GAEIARENER
     RHRMAAQGKT PTEEWRSDDD RNEEDLIQSA ALIQSEVLSE AAQDTEEGFR PNIVAYGPIV
     EDDQRAEPGR ESESQREERQ KGGLRNLSIF SGEEERFAYQ RAVSRLYEMS HASWADVTWR
     PLVESDRSAW QQSNVQQDAN FAANILRKSA AALATRKGLS TADRVEEGDF ADEASYDNLR
     ADQERKRINR SNGPPVLSPS HVWGVREDWG PKAGKWGKGV RGSRDDEMDP ENSESPRDRR
     ARLREERLRA SSDS
//
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