(data stored in SCRATCH zone)

SWISSPROT: Q75BV7_ASHGO

ID   Q75BV7_ASHGO            Unreviewed;       868 AA.
AC   Q75BV7;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 2.
DT   11-DEC-2019, entry version 108.
DE   SubName: Full=ACR164Cp {ECO:0000313|EMBL:AAS51390.2};
GN   ORFNames=AGOS_ACR164C {ECO:0000313|EMBL:AAS51390.2};
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811 {ECO:0000313|EMBL:AAS51390.2, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS51390.2, ECO:0000313|Proteomes:UP000000591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Pohlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2] {ECO:0000313|Proteomes:UP000000591}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC       superfamily. Dynamin/Fzo/YdjA family. {ECO:0000256|RuleBase:RU003932,
CC       ECO:0000256|SAAS:SAAS00534970}.
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DR   EMBL; AE016816; AAS51390.2; -; Genomic_DNA.
DR   RefSeq; NP_983566.2; NM_208919.2.
DR   STRING; 33169.AAS51390; -.
DR   EnsemblFungi; AAS51390; AAS51390; AGOS_ACR164C.
DR   GeneID; 4619698; -.
DR   KEGG; ago:AGOS_ACR164C; -.
DR   HOGENOM; HOG000206760; -.
DR   InParanoid; Q75BV7; -.
DR   KO; K22140; -.
DR   OMA; GYIQVAG; -.
DR   Proteomes; UP000000591; Chromosome III.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; IEA:EnsemblFungi.
DR   GO; GO:0031304; C:intrinsic component of mitochondrial inner membrane; IEA:EnsemblFungi.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0030061; C:mitochondrial crista; IEA:EnsemblFungi.
DR   GO; GO:0097002; C:mitochondrial inner boundary membrane; IEA:EnsemblFungi.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IEA:EnsemblFungi.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR   GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR   GO; GO:0061025; P:membrane fusion; IEA:EnsemblFungi.
DR   GO; GO:0000266; P:mitochondrial fission; IBA:GO_Central.
DR   GO; GO:0008053; P:mitochondrial fusion; IEA:EnsemblFungi.
DR   GO; GO:0000002; P:mitochondrial genome maintenance; IEA:EnsemblFungi.
DR   GO; GO:0007006; P:mitochondrial membrane organization; IEA:EnsemblFungi.
DR   GO; GO:0000001; P:mitochondrion inheritance; IEA:EnsemblFungi.
DR   CDD; cd08771; DLP_1; 1.
DR   InterPro; IPR001401; Dynamin_GTPase.
DR   InterPro; IPR019762; Dynamin_GTPase_CS.
DR   InterPro; IPR022812; Dynamin_SF.
DR   InterPro; IPR030381; G_DYNAMIN_dom.
DR   InterPro; IPR020850; GED_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR11566; PTHR11566; 1.
DR   Pfam; PF00350; Dynamin_N; 1.
DR   PRINTS; PR00195; DYNAMIN.
DR   SMART; SM00053; DYNc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00410; G_DYNAMIN_1; 1.
DR   PROSITE; PS51718; G_DYNAMIN_2; 1.
DR   PROSITE; PS51388; GED; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q75BV7.
DR   SWISS-2DPAGE; Q75BV7.
KW   GTP-binding {ECO:0000256|RuleBase:RU003932, ECO:0000256|SAAS:SAAS00959079};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU003932,
KW   ECO:0000256|SAAS:SAAS00959071};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000591}.
FT   DOMAIN          205..492
FT                   /note="Dynamin-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51718"
FT   DOMAIN          765..857
FT                   /note="GED"
FT                   /evidence="ECO:0000259|PROSITE:PS51388"
FT   REGION          122..144
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          159..181
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        160..179
FT                   /note="Acidic"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   868 AA;  96689 MW;  4205BEB38940868A CRC64;
     MVRTGQAHLC FCAGRALHGG LLRPAGRVGG AQLRFYVPLP AGSRPMLRSG GFPGMVMSQR
     GISFIPKLAV RMIKVPAYIG GGAAAVGSYI AYKVEEASSF TSDKLSQLRD FSSGVRDRLG
     EWLDAGGSEN GDGGQGGRDG GPVGDSVAAA TLLATLSEEE QAAAEDEDDE EEEDEDHTGD
     EILNLTKQMI EIRSILNRVD TNTPGVTLPS IVVVGSQSSG KSSVLESIVG RDFLPKGSNM
     VTRRPIELTL VNTPSGSETT ADFPTHRIYN LKDFREVKRI LMELNLAVPT HEAISEDPIQ
     LTIKSPRVPD LSLVDLPGYI QVEAADQPME LKSKIRNVCQ KYLAEPNIIL AISAADVDLA
     NSAALRASKL ADPQGLRTIG VITKLDLVEP SAARDLLMNK KYPLKMGYVG VITKGPVKTH
     RLFDQSAGKG VIFGGKGSKA KDQETERLET IQFEKNYFRE HRQEFASCQV TTKKLREKLI
     KILEVSMSNA LEPTSRVIQQ ELDDTSYLFK VEFNDRQLTP KSYLLSNVDV LKLAIKEFQE
     KFRRSELKSM LSADLDQRVL DLLASRYWKD DNLQELSKNL DDESSALYWH KKLELASSSL
     TKLGIGRLST TLVTNAILKE LENVLAMTPL KAHELIKELI TNTAVNVLNA KYYSTADQVE
     NCIKPFKYEI DLEDRDWSIA RDHSVALVQE ELRQCNERYQ MIKNSVGTRK LQQVMQYIKT
     DPTRKESLGF STMLLERGSE ALSLQDRASL LSFRLKMLKN KCNSTAEKDK CPEVFLNAVS
     DKLTSTAVLF LNVELLSDFF YNFPIELDKK LSALSEEQVE MFAKEDPRIS RHIELQKRKE
     LLELALEKID SILVFRKSYK NLAGKSHP
//

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