ID   A0A109FH42_9BASI        Unreviewed;       470 AA.
AC   A0A109FH42;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=VWFA domain-containing protein {ECO:0000259|PROSITE:PS50234};
DE   Flags: Fragment;
GN   ORFNames=RHOSPDRAFT_18236 {ECO:0000313|EMBL:KWU44377.1};
OS   Rhodotorula sp. JG-1b.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX   NCBI_TaxID=1305733 {ECO:0000313|EMBL:KWU44377.1, ECO:0000313|Proteomes:UP000062823};
RN   [1] {ECO:0000313|EMBL:KWU44377.1, ECO:0000313|Proteomes:UP000062823}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JG-1b {ECO:0000313|EMBL:KWU44377.1,
RC   ECO:0000313|Proteomes:UP000062823};
RG   DOE Joint Genome Institute;
RA   Goordial J., Raymond-Bouchard I., Riley R., Ronholm J., Shapiro N.,
RA   Woyke T., Grigoriev I.V., Labutti K.M., Greer C., Whyte L., Bakermans C.;
RT   "Draft genome of eurypsychrophile Rhodotorula sp. JG1b isolated from
RT   permafrost in the hyper-arid Upper Elevation McMurdo Dry Valleys,
RT   Antarctica.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC   -!- SIMILARITY: Belongs to the ATPase inhibitor family.
CC       {ECO:0000256|ARBA:ARBA00010901}.
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DR   EMBL; KQ954480; KWU44377.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A109FH42; -.
DR   STRING; 1305733.A0A109FH42; -.
DR   OrthoDB; 1441553at2759; -.
DR   Proteomes; UP000062823; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0042030; F:ATPase inhibitor activity; IEA:InterPro.
DR   Gene3D; 1.20.5.500; Single helix bin; 1.
DR   Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR   InterPro; IPR007648; ATPase_inhibitor_mt.
DR   InterPro; IPR002035; VWF_A.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   PANTHER; PTHR34706:SF2; RFEF; 1.
DR   PANTHER; PTHR34706; SLR1338 PROTEIN; 1.
DR   Pfam; PF04568; IATP; 1.
DR   SUPFAM; SSF53300; vWA-like; 1.
DR   PROSITE; PS50234; VWFA; 1.
PE   3: Inferred from homology;
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Reference proteome {ECO:0000313|Proteomes:UP000062823}.
FT   DOMAIN          238..442
FT                   /note="VWFA"
FT                   /evidence="ECO:0000259|PROSITE:PS50234"
FT   REGION          50..176
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        115..152
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KWU44377.1"
SQ   SEQUENCE   470 AA;  50017 MW;  3AE1BED83B469221 CRC64;
     PSGHGQSSFN KREKAEEERY VREAELEKLK ALKKSIEASK ARLQDLEGQH KELEASIKSG
     DPQYGQQQAY GAPPVPGGRP PQQGAGGVGP QGQMPYPGAP PAMGGPGYGG HLQQQPQLYG
     GQQAPYGGQQ QQPGYGQPQG QYGQQQQPQG YGQPPAAYGA PGQQPGGGAG GPGGNQQMIT
     QILQQAVMDQ KIQAFYPPGS LEQLAARIAQ SGALPRIAAQ WNIPMEIAMD LAKLALFDTV
     MLVDDSGSMA FEENGSRIDD AKLIVSRVAT AATLFDTDGI SVFFLNSKTV GNNITSEQQA
     QQLLSGIRFS GLTPLGTASM FTLTDCPKHL AQSLDQKILQ PLLVGPARQN SLEKPLLVVA
     VTDGAPGGEA RDTIVKAIKN AKAALSQTRY GPDAISIQLA QIGNDMASRA FLEEIDNHPD
     IGGLVDTTSN YENEADDFMK TTGQELTPDL WLVKLMLGPI DSSYDLKDQK
//