SEY1_CRYNB
ID SEY1_CRYNB Reviewed; 829 AA.
AC P0CQ47; Q55M25; Q5K8P4;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 42.
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}; OrderedLocusNames=CNBI1870;
OS Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=283643;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B-3501A;
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(2005).
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; AAEY01000044; EAL18926.1; -; Genomic_DNA.
DR RefSeq; XP_773573.1; XM_768480.1.
DR AlphaFoldDB; P0CQ47; -.
DR SMR; P0CQ47; -.
DR PRIDE; P0CQ47; -.
DR EnsemblFungi; AAW46519; AAW46519; CNL04960.
DR EnsemblFungi; EAL18926; EAL18926; CNBI1870.
DR GeneID; 4938147; -.
DR KEGG; cnb:CNBI1870; -.
DR VEuPathDB; FungiDB:CNBI1870; -.
DR HOGENOM; CLU_011270_0_0_1; -.
DR Proteomes; UP000001435; Chromosome 9.
DR GO; GO:0032541; C:cortical endoplasmic reticulum; IEA:EnsemblFungi.
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:0048309; P:endoplasmic reticulum inheritance; IEA:EnsemblFungi.
DR GO; GO:0016320; P:endoplasmic reticulum membrane fusion; IEA:EnsemblFungi.
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; Transmembrane; Transmembrane helix.
FT CHAIN 1..829
FT /note="Protein SEY1"
FT /id="PRO_0000410234"
FT TOPO_DOM 1..721
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 722..742
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 743..745
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 746..766
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 767..829
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT DOMAIN 87..310
FT /note="GB1/RHD3-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT REGION 806..829
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 487..525
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT COMPBIAS 813..829
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 97..104
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
SQ SEQUENCE 829 AA; 93002 MW; 66ECAEBC71E9C8FA CRC64;
MNQTPQIAQD LLKNPPQELQ QLLNDPRTPD SARKAVQELQ APFVGPGTAG NKDGAKESPR
LQIVNENQEF TKELSPYLAK WDLLDKGFAY DVVAVFGSQS TGKSTLLNRL FGTTFDVMDE
SKRQQTTKGI WMCPSQYSNT LVMDVEGTDG RERGEDQDFE RKSALFSLAS TEVLIVNLWE
HQIGLYNGAN MGLLKTVFEV NLGLFGGGGD NTKPKPQEKT LILFVIRDHV GATPMSNLTA
TLTQDMERIW DSLSKPAHLE DAVLSSYFDL SFAALPHKVL MPEKFEEAVL ELRQRFTDRS
REDYVFQPAY HKRIPADGVS FYMEGIWQQV LTNKDLDLPT QQELLAQFRC DEISTVVFEA
FLASAKIVRR PVEAGSVVEG LGALMRDWLE TALGKFDRDA SRYHSAVYQR KRLDLLASLH
ASLSPLFLGQ LKNLHKIETA KFSKDIVAGV KEPGYDFGVV VEEGKRRARE RFLAGAKEVK
VEETDWEYEH ELALLDEDLK LIADKCRADE TKKMVNAIER NVKRQILEPV EVAMSQPTKT
MWDTVLKTYS DVIEAAEEAY LSKAKSYNCS DEENSTALAS LRARAWLALR RKLEEQTSDS
TVLTTLRTKF EDSFRYDEAG VPRVWRPEDD IEAAFRKAKD ETLGLLPLFA NIAPTEGSLL
PELPPPEPSF DVESDPSPFD PSTAFTLLTA TKLLSLESRF KRDADAAYVE AKRSMVSSVA
QIPVWMYGVL VVLGWNEAMA VLFNPLYFAM LLVLAASGYI ILQLGLAGPI LQIASTVIRE
IRQMVVKKLR EAFADVPEAQ RILAQPVTAS SSDEQERKGD LIKGEMLEK
