ID   A0A0B4I4M9_METMF        Unreviewed;       895 AA.
AC   A0A0B4I4M9;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   SubName: Full=GTPase FZO1 {ECO:0000313|EMBL:KIE02994.1};
DE   Flags: Fragment;
GN   ORFNames=MAJ_01296 {ECO:0000313|EMBL:KIE02994.1};
OS   Metarhizium majus (strain ARSEF 297).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium;
OC   Metarhizium majus.
OX   NCBI_TaxID=1276143 {ECO:0000313|EMBL:KIE02994.1, ECO:0000313|Proteomes:UP000031176};
RN   [1] {ECO:0000313|EMBL:KIE02994.1, ECO:0000313|Proteomes:UP000031176}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ARSEF 297 {ECO:0000313|EMBL:KIE02994.1,
RC   ECO:0000313|Proteomes:UP000031176};
RX   PubMed=25368161; DOI=10.1073/pnas.1412662111;
RA   Hu X., Xiao G., Zheng P., Shang Y., Su Y., Zhang X., Liu X., Zhan S.,
RA   St Leger R.J., Wang C.;
RT   "Trajectory and genomic determinants of fungal-pathogen speciation and host
RT   adaptation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:16796-16801(2014).
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:KIE02994.1}.
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DR   EMBL; AZNE01000003; KIE02994.1; -; Genomic_DNA.
DR   RefSeq; XP_014581987.1; XM_014726501.1.
DR   AlphaFoldDB; A0A0B4I4M9; -.
DR   HOGENOM; CLU_011752_0_0_1; -.
DR   OrthoDB; 1381184at2759; -.
DR   Proteomes; UP000031176; 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   Reference proteome {ECO:0000313|Proteomes:UP000031176}.
FT   DOMAIN          257..563
FT                   /note="Dynamin-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51718"
FT   REGION          1..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          135..200
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          472..513
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        22..47
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        146..184
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KIE02994.1"
SQ   SEQUENCE   895 AA;  98105 MW;  5648CE4CDA8DB37B CRC64;
     MSQDYFTGKG KGPLRSDPDP DAPKNSSPSS SSRPHYMTVG SGSTSEHAAR LQNMLDVDSG
     YGGSVAGEDH HIAMTSATNS TSDSSQHPRG KASAGHQMWY YRQRAILGRS INKVLDLLQS
     LQQMNTEWPA HYPTIRPADA TSSERPGMGR TYSVSGDAAS SSSTTAQPPL LRRSLTSVDA
     SPAESSRAAK NRPAPEPRLV SPQIAQELSI LKLDLKLGAL HQAELVHSLE KNSVAALLDG
     KISSSIRHLL SLRERIEDTS SKVLITGDLN AGKSTFCNAL LRRKVLPEDQ QPCTAIFCEV
     LDARENAGIE EVHAVHKDCT YSRHDETTYD VYALTELEKI VTDNETYTQC KVYVKDIRTV
     DESLLNNGVV DIALIDAPGL NSDTTKTTAI FARQEEIDVV VFVVSAANHF TQSAKEFIDA
     AAAEKAYLFI VVNGYDTIRD KERCQKLILD QVSGLSPDTR KESSDLVHFV SSNAIPAGPA
     PPGGPRGNGS GSSSGGGGGD DPGDDGAKGK GKDLDKIRDF EALEASLRRF VLEKRARSKL
     APARTYLLNI LNDIHSLAQV NEEVAQSEID RVSAELREIE PQLASSRKAR SEVSEQIDRN
     IEETCQDVYD HSRAELNTAI TQAGRTNYDV PYPGIFGAFQ YADDVKEAML SHITDAVTRC
     EEYGREKSVQ GVNTIKQLGL LHVGDEFQNL QFRPDVMFRR KRDALARQVH IPTELWDFVD
     WSTLLQRQEK FAGTGMALTV AGAVVPRMLG MSNWMDHAML TTRVLSNENL RQLIVPGIVI
     AAIAGAAYVL QQIPNSLPPR LATKISSQLA ELDYIHANSS RISSSVRKVL RFPADSLRVG
     LDQSVKDLGN KRDEADKVRH ESEEASKFFH ELVGRSQVQR SMVEAVDLDA PQELH
//