ID V2XT32_MONRO Unreviewed; 860 AA.
AC V2XT32;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Transmembrane gtpase fzo1 {ECO:0000313|EMBL:ESK95665.1};
GN ORFNames=Moror_12532 {ECO:0000313|EMBL:ESK95665.1};
OS Moniliophthora roreri (strain MCA 2997) (Cocoa frosty pod rot fungus)
OS (Crinipellis roreri).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=1381753 {ECO:0000313|EMBL:ESK95665.1, ECO:0000313|Proteomes:UP000017559};
RN [1] {ECO:0000313|EMBL:ESK95665.1, ECO:0000313|Proteomes:UP000017559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK95665.1,
RC ECO:0000313|Proteomes:UP000017559};
RX PubMed=24571091; DOI=10.1186/1471-2164-15-164;
RA Meinhardt L.W., Costa G.G.L., Thomazella D.P.T., Teixeira P.J.P.L.,
RA Carazzolle M.F., Schuster S.C., Carlson J.E., Guiltinan M.J.,
RA Mieczkowski P., Farmer A., Ramaraj T., Crozier J., Davis R.E., Shao J.,
RA Melnick R.L., Pereira G.A.G., Bailey B.A.;
RT "Genome and secretome analysis of the hemibiotrophic fungal pathogen,
RT Moniliophthora roreri, which causes frosty pod rot disease of cacao:
RT mechanisms of the biotrophic and necrotrophic phases.";
RL BMC Genomics 15:164-164(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:ESK95665.1}.
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; AWSO01000068; ESK95665.1; -; Genomic_DNA.
DR RefSeq; XP_007845007.1; XM_007846816.1.
DR AlphaFoldDB; V2XT32; -.
DR STRING; 1381753.V2XT32; -.
DR KEGG; mrr:Moror_12532; -.
DR HOGENOM; CLU_011752_0_0_1; -.
DR OrthoDB; 1381184at2759; -.
DR Proteomes; UP000017559; 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:0000313|EMBL:ESK95665.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000017559};
KW Transmembrane {ECO:0000313|EMBL:ESK95665.1}.
FT DOMAIN 201..470
FT /note="Dynamin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51718"
FT REGION 77..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..99
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 860 AA; 94982 MW; B043FF4B19632874 CRC64;
MPQPYFPPRV TSPVKELANF SSITGERQLK VEDVQEQYIE QKDRLVNALD STKSILNGLR
KFNKEEWVVR YPQLRESASA PAEEPKEKRR KSLRRSMTFA DDPTRETEVV VKQGLTRSVT
LSSITDVREE QDDEQELPED ESLLPNSDFR VLRLDLKLGA NRSATAASLV SQLEKASIAN
LLDDRIESSL SHVDKLRLRV EDTSSKVLVT GDLNAGKSTF VNALLRREVM PVDQQPCTTA
FCEVHDAAEN QGKEEVHIIK AGAVYDINDE STFTRASLSE LEDIVSDNES SERMLKLYLA
DTRTPAESLL NNGVVDISLI DAPGLNRDSL KTTALFARQE EIDVVVFVVS AENHFTLSAR
EFLLNASKEK AYLFIVVNKY DQIKNKEKCR RLVLEQIKEL SPRTWQDAQD LVHFVDSAAA
LQPYTANPSF DDLESSLRSF VLVKRSKSKL QPVSTYLNNL LCDIDILAGA NAIVANSELE
QANAELSQVR PVLERMKQNR EVLEDSLDSV EEDGATSAAV RTKSVLNFAL ERVGQGKLGV
DRPLVPMPSY PGILGIWDYA RNVRRALVAS IDAAVKLAED EARVITSTGV DKIKNLADEH
LPEGVERNKR VFIPEAMFSA VRRGKGAAKS RRSSSYGNGA VVAGGIHGLG IGLAQRPDML
ETTFLDLFDV HHQFWLHFGD GHDSKKDEDS APTALGLVSV GLGAVTMVGG QAIGAKGLIE
GIIRVTDLFG NETARKWAAP VIGAFTIGLT AYLVLELPNS IPKTVGRRVK AAVERENADE
ENAFVEMHAG RISRETRKVL RLASWDLKGR FNSALEERGQ QVKAKEEQAK KATRAKEYFT
GVGTETGEVR VHAGLGVEAA
//
