ID A0A0N1HLV3_9EURO Unreviewed; 931 AA.
AC A0A0N1HLV3;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Transmembrane GTPase fzo1 {ECO:0000313|EMBL:KPI38085.1};
GN ORFNames=AB675_1121 {ECO:0000313|EMBL:KPI38085.1};
OS Phialophora attinorum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Phialophora.
OX NCBI_TaxID=1664694 {ECO:0000313|EMBL:KPI38085.1, ECO:0000313|Proteomes:UP000038010};
RN [1] {ECO:0000313|EMBL:KPI38085.1, ECO:0000313|Proteomes:UP000038010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 131958 {ECO:0000313|EMBL:KPI38085.1,
RC ECO:0000313|Proteomes:UP000038010};
RA Moreno L.F., Stielow B.J., de Hoog S., Vicente V.A., Weiss V.A.,
RA de Vries M., Cruz L.M., Souza E.M.;
RT "Draft genome of the ant-associated black yeast Phialophora attae CBS
RT 131958.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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:KPI38085.1}.
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DR EMBL; LFJN01000020; KPI38085.1; -; Genomic_DNA.
DR RefSeq; XP_017998048.1; XM_018140047.1.
DR AlphaFoldDB; A0A0N1HLV3; -.
DR STRING; 1664694.A0A0N1HLV3; -.
DR GeneID; 28731917; -.
DR OrthoDB; 1381184at2759; -.
DR Proteomes; UP000038010; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000313|EMBL:KPI38085.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000038010};
KW Transmembrane {ECO:0000313|EMBL:KPI38085.1}.
FT DOMAIN 284..572
FT /note="Dynamin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51718"
FT REGION 1..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 87..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 153..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 501..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 868..895
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 23..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..545
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 931 AA; 101682 MW; 0480704A124A2E52 CRC64;
MSDKPSASAK GGSGKDKTAD DQNTETQSTS NSWVAPSFMT AGTGLESTHA AALMAQLEQD
SGYGSMPGDS QSRGGEMRAW EDGLLRDMPT PAHTPRLNGQ PDSLSENEKR VLASHVHQLQ
YNQNRVALAK AIGQTVELLK QLQDMNAHWP ATYPSVKRSE SPKRRPAINQ TQSTRDTSML
SRDTENIAAP RPSPLRRAGT TLGPGADAAG ESSTQAQQRK SPEPRLLTSQ IAQEFSILKL
DLKVGALSQA ELVHSLEKKS IASLLDGKIG QSVRHLLLLR DRIEDTSSKV LVTGDLNAGK
STFCNALLRR KILPEDQQPC TALFCEVLDA KENGGLEEVH AVHKDTIYNR NDESTFDAYS
LQELDKIVVD NDQYMQCKIY VKDIRSVDQS LLNNGIVDIA LIDAPGLNSD SVKTTAVFAR
QEEIDVVVFV VSAANHFTLS AKEFIWQAAH EKAYIFMVVN GFDNIRDQER CKRQILEQLA
KLSPYTYKEA KELVHFVSSN AVPVQPTHPP GGPGGDAGGS GSASGGSDPG DGDDDSKKGK
GKDKKKIEDF EGLEGALRRF VLEKRARSKL APAKTYLMNC LGDMNVLATV NRDVAQSELD
RVSQQLAEIE PEYEERQKQR NVVTEKLSKD VDGAVTDVYD HTKATLAATI SNVGHEDLGV
EYPGLFSAFQ YAEDLRVAML NSIADSVKSC EEYGRAKCVT GVSMIKSLGL LHVGDSYDQL
SFRSDMMFQR KRDALVRTVD TDVEIMDFFD VAGLWERQEK TLGTGLAVTL AGTLGTRAIG
GLGWVDGAYS ALRVVGSQNL RRIAAPAAVT AVVLAVAYVL STIPQTLPPR LARKLSATLT
GMDYPHANAH RISAEVRRVL RYPSQQLSVD LERGVEELKQ KREDVQKTKK ESDVALKYFG
NLVRDSSETR HRIEGIDLEG PLPGAAGAYA V
//
