ID   E6ZVW7_SPORE            Unreviewed;       960 AA.
AC   E6ZVW7;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   SubName: Full=Related to FZO1-GTP-binding protein, required for biogenesis of mitochondria {ECO:0000313|EMBL:CBQ71274.1};
GN   ORFNames=sr16627 {ECO:0000313|EMBL:CBQ71274.1};
OS   Sporisorium reilianum (strain SRZ2) (Maize head smut fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Sporisorium.
OX   NCBI_TaxID=999809 {ECO:0000313|EMBL:CBQ71274.1, ECO:0000313|Proteomes:UP000008867};
RN   [1] {ECO:0000313|EMBL:CBQ71274.1, ECO:0000313|Proteomes:UP000008867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRZ2 {ECO:0000313|Proteomes:UP000008867};
RX   PubMed=21148393; DOI=10.1126/science.1195330;
RA   Schirawski J., Mannhaupt G., Muench K., Brefort T., Schipper K.,
RA   Doehlemann G., Di Stasio M., Roessel N., Mendoza-Mendoza A., Pester D.,
RA   Mueller O., Winterberg B., Meyer E., Ghareeb H., Wollenberg T.,
RA   Muensterkoetter M., Wong P., Walter M., Stukenbrock E., Gueldener U.,
RA   Kahmann R.;
RT   "Pathogenicity determinants in smut fungi revealed by genome comparison.";
RL   Science 330:1546-1548(2010).
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}.
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DR   EMBL; FQ311443; CBQ71274.1; -; Genomic_DNA.
DR   AlphaFoldDB; E6ZVW7; -.
DR   EnsemblFungi; CBQ71274; CBQ71274; sr16627.
DR   VEuPathDB; FungiDB:sr16627; -.
DR   eggNOG; KOG0448; Eukaryota.
DR   HOGENOM; CLU_011752_0_0_1; -.
DR   OrthoDB; 1381184at2759; -.
DR   Proteomes; UP000008867; Chromosome 21.
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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT   DOMAIN          265..532
FT                   /note="Dynamin-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51718"
FT   REGION          1..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          122..212
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          243..270
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        25..52
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        122..145
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        177..192
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   960 AA;  104887 MW;  82C9DC2C87476C4B CRC64;
     MSENNTTSHQ QYATPVKVMR SQTWDEADSH SLTVASPSTP ASKSTSLNGG ELFPSKQREI
     DQLRAQQDAQ QMLQQHQSEF EDSRDKLLGA IDNTSRLLAD MRDFNKNKRL IHYAAADDAA
     HAATSSRQQL PLHRRSQSNS PTHSLEEADA DLHSSSADSA AHRPKPPAIM RLNTVGGHVS
     LPSTPARRVS SSSSSSHHDD DDDDDNESDA STDMSVLKLD LRVGSVAANP QALVRSLERS
     SVAQLLDGRM EKSERHLENL KQRLSDTQSK VFVTGDLNAG KSTFVNALLR RPLMPTDQQP
     CTTVFCEVLD ASQLNSDVEE VHMLKPGVKY SAEDDSTFTR HTLEQVEQIV ADAEEVSPED
     APVLKCYAHD TRATQDSLLK NGIVDIALID APGLNRDSLK TTALFARQEE IDVVVFVVSA
     ENHFTLSAKE FLWNASHDKA FVFIVVNKFE SIKNKDKCRK LVLDQIRQLS PRTYDDAANL
     VHFVDSQAVF GDDDDCDSSD TGAAPDTPSE ELGRKVQGGE LVVASRSSES LQAFARLEAA
     LRDFVLLKRA KSKLLPSKTY MLRLLSDMTF LAKINTHVAQ IELAEAIKAL EVARPELARC
     QASQQKLETV VEGEEDQAVT AVMQEAQRKL ASAIELIGNG KPATEAVQLP AYPGLFNVRE
     YAQEVRHALT SSLELALRSV EDTARGTASQ AVDRVQKLGL AHLPDNEAQK RERIFNPQVM
     FGKRRAMPGL VGLGLGAQVV EVQASDFFDA YHHFTVVTGG SLSQDKSDKS GKSSDDELSL
     VSSVSLGLGA LTLMGGKALG AKTAVDVFVR ISDLVGNPTA RRWAGPVFAV VSTGLVVYFI
     YDLPNSVPRN VGRSIKCGLQ SGTLLRSSTT SDASSSSSEE ASFAAVHSAR VGRETRKVLR
     LASWDLQERF RVAIAQRRAE VERQEAKQAS ANLAIDWFDK TTARVTAIRG EVDEVKGLEA
//