ID   A0A286UC59_9AGAM        Unreviewed;       863 AA.
AC   A0A286UC59;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Transmembrane GTPase fzo1 {ECO:0000313|EMBL:PAV17129.1};
GN   ORFNames=PNOK_0719300 {ECO:0000313|EMBL:PAV17129.1};
OS   Pyrrhoderma noxium.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Hymenochaetales; Hymenochaetaceae; Pyrrhoderma.
OX   NCBI_TaxID=2282107 {ECO:0000313|EMBL:PAV17129.1, ECO:0000313|Proteomes:UP000217199};
RN   [1] {ECO:0000313|Proteomes:UP000217199}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FFPRI411160 {ECO:0000313|Proteomes:UP000217199};
RA   Chung C.-L., Lee J.T., Akiba M., Lee H.-H., Kuo T.-H., Liu D., Ke H.-M.,
RA   Yokoi T., Roa M.B., Lu M.J., Chang Y.-Y., Ann P.-J., Tsai J.-N.,
RA   Chen C.-Y., Tzean S.-S., Ota Y., Hattori T., Sahashi N., Liou R.-F.,
RA   Kikuchi T., Tsai I.J.;
RT   "The Genomic Landscape Of Tree Rot In Phellinus noxius And Its
RT   Hymenochaetales Members.";
RL   bioRxiv 0:0-0(2017).
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:PAV17129.1}.
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DR   EMBL; NBII01000007; PAV17129.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A286UC59; -.
DR   STRING; 2282107.A0A286UC59; -.
DR   InParanoid; A0A286UC59; -.
DR   OrthoDB; 1381184at2759; -.
DR   Proteomes; UP000217199; Chromosome 7.
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:0000313|EMBL:PAV17129.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000217199};
KW   Transmembrane {ECO:0000313|EMBL:PAV17129.1}.
FT   DOMAIN          205..478
FT                   /note="Dynamin-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51718"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          72..108
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          121..145
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        130..145
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   863 AA;  95049 MW;  78B2BDA13EE77F7C CRC64;
     MAQKSRAKAS KSRSPEPQTA DKPVTRVEDV QEAYIKHKNQ LVNSIDESAK LLTELRDFNK
     DDWVVRYPHF NEESSTSAPI TPPATPAKRP SSLRRSMTFM DDPQNGTDVV VKCRTRKGQQ
     RSLSLAKIQD SPENEDDQEG DARLLPSKND LDFHVLKLDL KMGPHGSSTA STLVSQLEKS
     SIANLLDDRI NASLKHLDKL RTRVEDTSSK VLVTGDLNAG KSTLVNALLR RGVMPVDQQP
     CTTAFCEVHD ASENDGKEEI HILSVHNAST YSPKDENTFE RGTVDDLEDL IDENEDGSKI
     IKVYINDSRP SVDSFLNNGI ADISLIDAPG LNTDSVKTTA LFSRQEEIDV VVFVVSAENH
     FTLSAKEFLQ NASREKAYVF IVVNKFEGIR NKEKCRRAVL EQVKELSPLT YENAADLVHF
     VESSRVLDTQ PTNTAFNTLE SSLRSFVLQK RSKSKLHPAA NYLANLLSDV NLLAGSNAIL
     AKADLEKARD SLDRARPVLD KMKGGRTGLD DSLEHVEEQK TEKASRDTTE IINQALDKVG
     NGELGTENAV CKMPSFPGLL RLWDYVHDVR KALLTSIDEA VKLAEDEARL TTSDGVKDIS
     ALADRFLPEG VERSRRVFMP EAMFSRRRSA KNGKVRRGSS DAIVAGGLYG LGIGLAQRQD
     LLETSPLDVL DIAHHYHHYF GKEEDAAANS AEDDGMPSAL SVLSLGLGAL TMVGGKAIGV
     SSIVDGAVKI SDLLGNETAR KWIAPLLGAA ALGLSAYLII ELPSSIPRTV GRRIRATLVV
     PDQSGSTFVS SHSLRVARET RKVLRLAAYE QRERFRVAME ASAKEVENAE RIERQADKAL
     KWFENVQTRI GHVKVDVSEV GDL
//