ID W6MTQ8_9ASCO Unreviewed; 843 AA.
AC W6MTQ8;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Dynamin-type G domain-containing protein {ECO:0000259|PROSITE:PS51718};
GN ORFNames=KUCA_T00005857001 {ECO:0000313|EMBL:CDK29863.1};
OS Kuraishia capsulata CBS 1993.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetales incertae sedis; Kuraishia.
OX NCBI_TaxID=1382522 {ECO:0000313|EMBL:CDK29863.1};
RN [1] {ECO:0000313|EMBL:CDK29863.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS 1993 {ECO:0000313|EMBL:CDK29863.1};
RA Genoscope - CEA;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDK29863.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS 1993 {ECO:0000313|EMBL:CDK29863.1};
RA Morales L., Noel B., Porcel B., Marcet-Houben M., Hullo M-F., Sacerdot C.,
RA Tekaia F., Leh-Louis V., Despons L., Khanna V., Aury J-M., Barbe V.,
RA Couloux A., Labadie K., Pelletier E., Souciet J-L., Boekhout T.,
RA Gabaldon T., Wincker P., Dujon B.;
RT "Complete DNA sequence of /Kuraishia capsulata/ illustrates novel genomic
RT features among budding yeasts (/Saccharomycotina/).";
RL Submitted (FEB-2014) 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}.
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DR EMBL; HG793131; CDK29863.1; -; Genomic_DNA.
DR AlphaFoldDB; W6MTQ8; -.
DR STRING; 1382522.W6MTQ8; -.
DR HOGENOM; CLU_011752_0_0_1; -.
DR OrthoDB; 1381184at2759; -.
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}.
FT DOMAIN 209..496
FT /note="Dynamin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51718"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 432..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..451
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 843 AA; 94767 MW; 80138F1FEB79CF70 CRC64;
MSSPGLPHNP EDSDDAVTIT PDDEPRYNPT QLIYNRETGL EGSTLLNGET NGLTEGSSST
LANGFPRQSS DLMQSHLQQL QYNEHRISLN RSIGSALGIL GELRAENSKR PIFYPTDAED
SSNSKLIGSS SRLALIRQNS LAPAQNLIHK ATEIKDVEQF ELLTINLKLD QTSGVNAISS
LDRTGLASLF NDKVNHVMKH LQALKERIDD TSSKVFVTGD LNSGKSAFCN ALLRRRLLPE
DQQPCTSVFC EVIDARDNSG VEEVHAVSIG QAYNRRKETS YKIFGLKDLE DLVYRSDLYS
ILKIYVNDNR PIERSLLKNG VIDISLIDAP GLNLDSYQTT QVFSRQEEID LVVFVVNAEN
HFTLSGKEFI ASAAHDKNLM FIVVNKFDNI KDQDKCRHKI MDQVHVLSPE TYKDASEFVH
FVSSADVLEG LPEGGPDGDA DGKDDNDPLD YDSPEFDHLE ASLRRFILEK RSISKLLPVK
TYLGKLYSDL GKLCVINEKL YLQSRDDMLL ELNALTPKYE QAVAESTKIH DQIQKVIEST
SADVYSFSRN KITNTVNAIK DMPLAQYRGL ASLYVFAKET QFLMINELLN SVTDSENYAR
KRTGLAVDEI RQIGITQVAS AKLPNTRFKE EAMFTKKYHN LRKRLNEDIS PFDFFDPTFD
GFFRAIGLLR GGTSYQLQVW KSSASAMAVY SSTRVLQNGV AVLKNVVSVR DILSVGFFKK
VVTPVILTAG ALSVAYLVYD MPNAYQRKTA RKMSRQVQEE DYQHANSSRI AKECRKVLAY
PSRDVMNCLQ TSLEETATKK KQITESLKNS DMSYDFYRRL AKMITTQKTQ VESFSFEALH
SVD
//