SEY1_SCHJY
ID SEY1_SCHJY Reviewed; 764 AA.
AC B6K0N7;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 03-AUG-2022, entry version 56.
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; ORFNames=SJAG_02595;
OS Schizosaccharomyces japonicus (strain yFS275 / FY16936) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=402676;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=yFS275 / FY16936;
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
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; KE651166; EEB07508.1; -; Genomic_DNA.
DR RefSeq; XP_002173801.1; XM_002173765.2.
DR AlphaFoldDB; B6K0N7; -.
DR SMR; B6K0N7; -.
DR STRING; 4897.EEB07508; -.
DR EnsemblFungi; EEB07508; EEB07508; SJAG_02595.
DR GeneID; 7047701; -.
DR VEuPathDB; FungiDB:SJAG_02595; -.
DR eggNOG; KOG2203; Eukaryota.
DR HOGENOM; CLU_011270_0_0_1; -.
DR OMA; TNFDVMD; -.
DR OrthoDB; 418635at2759; -.
DR Proteomes; UP000001744; Unassembled WGS sequence.
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..764
FT /note="Protein sey1"
FT /id="PRO_0000385000"
FT TOPO_DOM 1..659
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 660..680
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 681..683
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 684..704
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 705..764
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT DOMAIN 31..246
FT /note="GB1/RHD3-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT REGION 731..764
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 302..322
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT COILED 421..443
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT COMPBIAS 737..764
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 41..48
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
SQ SEQUENCE 764 AA; 87647 MW; 513A145AFFBAC465 CRC64;
MQQSAQLITE NKEFNEDFPR FLKDVGLDNV GFDYHVVAVL GSQSTGKSTL LNKLFGTQFS
TMDTVRRQQT TKGIWVSRGK DSSILIMDVE GTDGRERGDD QDFERKSALF SIATSEVIIV
NMWENQIGLY QGSNMTLLKT VFEVNLQLFH ENIERSRLQF VIRDFLGSTS LDNLSETLMT
DLNRTWASIS KPEGLENSVI TDFFDVDFSA LPHKVLCAEA FDEETDKLRE QFLDEKNPKY
LFKPCYHKRI PADGFPLYTQ GIWQLIQNNR DLDLPTQQQL LAQYRCDEFI AEAMVSFDEQ
CEELLTFLKT HQSIENLLQR LEAIQTSTFS IFDENARRYQ SEVYTKKRQE LDRMMKTRLA
VPIQRYLAAI HKELVAGFPE RIATLVKDAC FKDVARVTVS EMVSVMHSEA AALQKEGFVC
DAEQTVETLR VELLQLVRSM REERLAQISA KLMVQFEQEF ADAIDVSFHH LTKDIWDNIM
HKFDELREKV LDEMLRSLNE YIDDEMDEDA ELLRTKHMFK LKRSTWLVLR RTLENETAEP
ILQQRLRTHF EDSFRYDSRG IPKMWKKSDI LENDFNKSLQ DTLQLIDVLA IVRLKDGSVP
TVDVPLAEEG EDTASNLEAD TFFTFLNRKK KANIHVSVKR AADLVFLDCK RSIISTATRV
PGYFWALLAV LGWNEFVSVL KNPVLLTLLL IVVSFLFILV QTGLAGPVKA FAERSVRNAV
NSMGEKLAEK LDDYRSTSPA SETTSGRVIS AENSSVDEKV STTP
