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SEY1_PICST
ID   SEY1_PICST              Reviewed;         827 AA.
AC   A3LWM9;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 2.
DT   03-AUG-2022, entry version 73.
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}; ORFNames=PICST_84922;
OS   Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS   Y-11545) (Yeast) (Pichia stipitis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX   NCBI_TaxID=322104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX   PubMed=17334359; DOI=10.1038/nbt1290;
RA   Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA   Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA   Passoth V., Richardson P.M.;
RT   "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT   yeast Pichia stipitis.";
RL   Nat. Biotechnol. 25:319-326(2007).
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}.
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DR   EMBL; CP000500; ABN67661.2; -; Genomic_DNA.
DR   RefSeq; XP_001385690.2; XM_001385653.1.
DR   AlphaFoldDB; A3LWM9; -.
DR   SMR; A3LWM9; -.
DR   STRING; 4924.XP_001385690.2; -.
DR   EnsemblFungi; ABN67661; ABN67661; PICST_84922.
DR   GeneID; 4839766; -.
DR   KEGG; pic:PICST_84922; -.
DR   eggNOG; KOG2203; Eukaryota.
DR   HOGENOM; CLU_011270_0_0_1; -.
DR   InParanoid; A3LWM9; -.
DR   OMA; TNFDVMD; -.
DR   OrthoDB; 418635at2759; -.
DR   Proteomes; UP000002258; Chromosome 6.
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; IEA:UniProtKB-UniRule.
DR   GO; GO:0007029; P:endoplasmic reticulum organization; IEA:UniProtKB-UniRule.
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..827
FT                   /note="Protein SEY1"
FT                   /id="PRO_0000384997"
FT   TOPO_DOM        1..719
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   TRANSMEM        720..740
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   TOPO_DOM        741..743
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   TRANSMEM        744..764
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   TOPO_DOM        765..827
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   DOMAIN          63..291
FT                   /note="GB1/RHD3-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          389..409
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   COILED          472..492
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   COILED          803..823
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   BINDING         73..80
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
SQ   SEQUENCE   827 AA;  95440 MW;  CBC0A52C6FF73D62 CRC64;
     MSQSSPSNAE TDEDLSTTSS SSSFVPIEQH QIQDAIQVID ENKEFNKNIL PYVVKTTPIS
     SVGNNYHIIS VFGSQSTGKS TLLNRLFNTN FDVMDESRRQ QTTKGIWMAH SPQVSTTKQM
     DTHQENIFVM DVEGTDGRER GEDQDFERKA ALFALATSEI LIVNIWETQI GLYQGANMGL
     LKTVFEVNLT LFGKSKLEKN DHKVLLLIVI RDHVGLTPKE NLSSTITQDL LKIWESLNKP
     AELAHLQFED FFDTDFHTLR HKVLQPKEFL EDVNELGDRL VVKKDLFRPN YHHNIPIDGW
     TMYAENCWQQ IDSNKDLDLP TQQILVAKFK CDEISASVYE EFHQKFKAIS SANTPGISTL
     DYQDLGLLLV DLRSDTLENY DLSASRYTKS VYEQRKDLLK EKLNEKFREF FDAHIKHLSE
     KSVKEFETNI VGLKGKNFDK EATRLTRETT DYFINSAILL SLENELDYDV HVSNLQDQLT
     KLIQQQQLVE LKNIVNKSIK KLSSGLTKAV SFELADPTET SWNNILSKFK EFVLDFLSKN
     ELEEEAGTYD FGLGTNRAQN KEAVETFKFK SWNAFYEIIH KIISKDNLLT LLKDRFDDKF
     RYDENGLPRM YQNTVELETN FGISKSFALR IVPLLTIAKL NDNSEILPDY DIFDSKLRAK
     YLGLVENEHD SEDEEDEEDR CFAEIISESE KAEVLNKFKK ETDARFIETK RSIVQHVTQI
     PYYIYLVIMV LGWNEFMAIV RNPLFFSLVL VFGAGLYILY SMNLLKPAMV VVQRLIDEII
     AMAKEKMREF LIDDHPTQAH NLQKISASNR EKVEEEKVVE TIEMQDL
 
 
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