ID   A0A395N9Y8_TRIAR        Unreviewed;       893 AA.
AC   A0A395N9Y8;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Transmembrane gtpase fzo1 {ECO:0000313|EMBL:RFU72627.1};
GN   ORFNames=TARUN_9634 {ECO:0000313|EMBL:RFU72627.1};
OS   Trichoderma arundinaceum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=490622 {ECO:0000313|EMBL:RFU72627.1, ECO:0000313|Proteomes:UP000266272};
RN   [1] {ECO:0000313|EMBL:RFU72627.1, ECO:0000313|Proteomes:UP000266272}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 40837 {ECO:0000313|EMBL:RFU72627.1,
RC   ECO:0000313|Proteomes:UP000266272};
RX   PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA   Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA   Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA   Busman M., Gutierrez S.;
RT   "Evolution of structural diversity of trichothecenes, a family of toxins
RT   produced by plant pathogenic and entomopathogenic fungi.";
RL   PLoS Pathog. 14:e1006946-e1006946(2018).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC         Evidence={ECO:0000256|ARBA:ARBA00001270};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC       {ECO:0000256|ARBA:ARBA00004374}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004374}.
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:RFU72627.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; PXOA01000813; RFU72627.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A395N9Y8; -.
DR   STRING; 490622.A0A395N9Y8; -.
DR   Proteomes; UP000266272; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0007005; P:mitochondrion organization; IEA:UniProt.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR045063; Dynamin_N.
DR   InterPro; IPR030381; G_DYNAMIN_dom.
DR   InterPro; IPR027094; Mitofusin_fam.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR10465; TRANSMEMBRANE GTPASE FZO1; 1.
DR   PANTHER; PTHR10465:SF0; TRANSMEMBRANE GTPASE MARF-RELATED; 1.
DR   Pfam; PF00350; Dynamin_N; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51718; G_DYNAMIN_2; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000266272};
KW   Transmembrane {ECO:0000256|SAM:Phobius, ECO:0000313|EMBL:RFU72627.1};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        766..787
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          253..556
FT                   /note="Dynamin-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51718"
FT   REGION          1..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          136..164
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          473..508
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   893 AA;  98180 MW;  5D76F8DBDAC4875F CRC64;
     MSQEYFNDKG KSPAARDSDD ANLDPNMAGH AGSAGGRPNY MTVGNGTTSE HAARLQSMLD
     VDSGYGGSIM GDEPGMWEVA AHGDRRQSGA IHQMWYNSQR ATLGRSINKV LDLLHSLREI
     NALWPAHYPS VQRAEKMESD GPRPGILHSS TMEDLTARSN QAPPPLLRRA MTSLEDASAE
     SSQAAESRPV AEPRLVSPQI AQEFSVLKLD LKLGALHQTE LVHSLEKGSI ASLLDGKISS
     SIKHLVSLRE RIEDTSSKVL ITGDLNAGKS TFCNALLRRK VLPEDQQPCT AIFCEVLDAR
     ENAGIEEVHA VHKEMIYNRN DESTYDAYSL QELEKIVIDN EKYIQCKVYV KDVRTIDESL
     LNNGVVDIAL IDAPGLNSDT TKTTAIFARQ EEIDVVVFVV SAANHFTQSA KEFIWAAAAE
     KAYIFIVVNG YNFIRDKERC QKMILDQVAG LSPRTHKEAS ELVHFVSSNV IPMAPSPPGG
     PSGGGGSGSG SGGGDDPSDD KGKGKDLDKI RDFEKLEQSL RRFVLEKRAR SKLAPARTYL
     LNILNDVATL ATVNQEVAQS EFDRVTQELK ELEPQILASK KARSEVDEQV VHNIEETCKN
     IYDHTRGQLN AAITYAGSTK YDIPYPGLFG AFGYADDLKD AILSHIADAV NGCEDYARGQ
     TVRGVNAIKQ LGLLHVGDEF QNLHFRPDVM FRRKKDALAR QVDVPTEFAD FVDFSTLMHS
     QEKFAGTGMA LTIAGALVPR MLGMNSWVDH AITATKIIGN ENLRRLILPG IVIAVFFLAV
     AASAYVLQQI PNSLPHRLAR KIEAQLAQID YVHTNASRIS GAVRTVLRMP ADNLRVGLDH
     SVKDLNKKRE ETVKVKGESE RASKFFRKLV GESQVQKNMV EGVDLDTPPQ NLH
//