位置:首页 > 蛋白库 > SEY1_YARLI
SEY1_YARLI
ID   SEY1_YARLI              Reviewed;         938 AA.
AC   Q6C3B0;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Protein SEY1 {ECO:0000255|HAMAP-Rule:MF_03109};
DE            EC=3.6.5.- {ECO:0000255|HAMAP-Rule:MF_03109};
GN   Name=SEY1 {ECO:0000255|HAMAP-Rule:MF_03109};
GN   OrderedLocusNames=YALI0F01166g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Cooperates with the reticulon proteins and tubule-shaping DP1
CC       family proteins to generate and maintain the structure of the tubular
CC       endoplasmic reticulum network. Has GTPase activity, which is required
CC       for its function in ER organization. {ECO:0000255|HAMAP-Rule:MF_03109}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000255|HAMAP-Rule:MF_03109}; Multi-pass membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_03109}. Note=Enriched in the cortical ER.
CC       Concentrated in punctae along the ER tubules. {ECO:0000255|HAMAP-
CC       Rule:MF_03109}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC       superfamily. GB1/RHD3 GTPase family. RHD3 subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU01052}.
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; CR382132; CAG77654.1; -; Genomic_DNA.
DR   RefSeq; XP_504852.1; XM_504852.1.
DR   AlphaFoldDB; Q6C3B0; -.
DR   SMR; Q6C3B0; -.
DR   STRING; 4952.CAG77654; -.
DR   EnsemblFungi; CAG77654; CAG77654; YALI0_F01166g.
DR   GeneID; 2908213; -.
DR   KEGG; yli:YALI0F01166g; -.
DR   VEuPathDB; FungiDB:YALI0_F01166g; -.
DR   HOGENOM; CLU_011270_0_0_1; -.
DR   InParanoid; Q6C3B0; -.
DR   OMA; TNFDVMD; -.
DR   Proteomes; UP000001300; Chromosome F.
DR   GO; GO:0032541; C:cortical endoplasmic reticulum; IEA:EnsemblFungi.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR   GO; GO:0048309; P:endoplasmic reticulum inheritance; IEA:EnsemblFungi.
DR   GO; GO:0016320; P:endoplasmic reticulum membrane fusion; IBA:GO_Central.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_03109; Sey1; 1.
DR   InterPro; IPR030386; G_GB1_RHD3_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR008803; RHD3/Sey1.
DR   PANTHER; PTHR45923; PTHR45923; 1.
DR   Pfam; PF05879; RHD3; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51715; G_GB1_RHD3; 1.
PE   3: Inferred from homology;
KW   Coiled coil; Endoplasmic reticulum; GTP-binding; Hydrolase; Membrane;
KW   Nucleotide-binding; Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..938
FT                   /note="Protein SEY1"
FT                   /id="PRO_0000155138"
FT   TOPO_DOM        1..839
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   TRANSMEM        840..860
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   TOPO_DOM        861..863
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   TRANSMEM        864..884
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   TOPO_DOM        885..938
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   DOMAIN          192..423
FT                   /note="GB1/RHD3-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT   REGION          1..159
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          911..938
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          603..630
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   COMPBIAS        26..46
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        72..94
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        101..119
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        143..159
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        915..938
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         202..209
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
SQ   SEQUENCE   938 AA;  103133 MW;  9928611CAA0746D7 CRC64;
     MTSQSHGAPP VPSSRPPASR VPVSGYDSHD SHSVSSSHSS HSPVTTHHHP APPPPASRPV
     RESGVAPVTA PEPIAAPEPI AAPEPIPAPE PIAAPVPEGL KSEHKPVERE HKPVERKPVS
     SPAEKSIPAS SPVHKAAPTP AASHAVPTSQ KSAKSTPGSY AGIPSLQLID GNKEFNPDVS
     SYFKKVHLDR AGLDYHVVAV FGSQSTGKST LLNALFGTQF DVMNETARQQ TTKGIWMARA
     QLEAPHSANS AHSQDCSDSG VLVMDVEGTD GRERGEDQDF ERKSALFALA TSEVLIVNIW
     EHQIGLYQGA NMGLLKTVFE VNLNLFATSQ NRSLIMFVIR DHIGATPLAN LSTTLKTDMG
     KLWDSINKPE GLEHAKLEDF FDLQFTALPH KLLQPNEFYA DVEQLACRFT VPKDPNYVFK
     PVYHRNVPLD GWSFYAEQVW DQIEQNKDLD LPTQQILVAR FRCDEIAAGA LDIFLSLLVK
     IRDQLSGGAV ASAVLGGLMG EARKQTVDEY DSQASRYTPS VYSATLEKLE DRVDNDLGKV
     YQSYLAQLKR ESLEQFNAAL ESSSALTFGE NLSRASKAAH AHFIDNAKQV TAAIGQPNSS
     HFSYDDTLAA LEQELDTLRD HKSKVEIDRL ISRSAKRFKS SFHEEFDENL NKPDETVWDR
     ILESFETLLN ASIKKIDPNY SPSAPSAFSF GFGSPKTSAE GLKQIQQEAW AVFGAELKEL
     SKEEQVLSRL KNKFKESFRY DANGVPIVWR PGDDIDGAFA KSREQALEIM PLLSTAKLSS
     GKSIEPTVAL EDDEDDDDET AFAVILTPKR QASLIEKFKK QAEGLYLEAK RSTIQSTTQI
     PLYMYGLLLL LGWNEIMAVL RSPVYFMFLL VAAGAAYVIH TLHLWGPLTH MTNTMIAEAT
     DMAKAKLKQV LNEAPTGETR EREAPVGSSR DDVELKDL
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024