SEY1_CLAL4
ID SEY1_CLAL4 Reviewed; 834 AA.
AC C4Y2Z9;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 53.
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=CLUG_02912;
OS Clavispora lusitaniae (strain ATCC 42720) (Yeast) (Candida lusitaniae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Metschnikowiaceae; Clavispora.
OX NCBI_TaxID=306902;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42720;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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; CH408078; EEQ38786.1; -; Genomic_DNA.
DR RefSeq; XP_002617468.1; XM_002617422.1.
DR AlphaFoldDB; C4Y2Z9; -.
DR SMR; C4Y2Z9; -.
DR STRING; 306902.C4Y2Z9; -.
DR EnsemblFungi; EEQ38786; EEQ38786; CLUG_02912.
DR GeneID; 8497477; -.
DR KEGG; clu:CLUG_02912; -.
DR VEuPathDB; FungiDB:CLUG_02912; -.
DR HOGENOM; CLU_011270_0_0_1; -.
DR InParanoid; C4Y2Z9; -.
DR OMA; TNFDVMD; -.
DR Proteomes; UP000007703; 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..834
FT /note="Protein SEY1"
FT /id="PRO_0000384980"
FT TOPO_DOM 1..733
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 734..754
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 755..757
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 758..778
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 779..834
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT DOMAIN 63..296
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 REGION 670..689
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 659..688
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT COMPBIAS 674..689
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 73..80
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
SQ SEQUENCE 834 AA; 94785 MW; 36BF6612807F1103 CRC64;
MSNVPSPTVT LEGDSPDAAH EAVSSSSSSF VPVEIQDAIQ IIDEHKQFNK QILDYISSRS
RQPGDYRIIS VFGSQSTGKS TLLNHLFSTN FDVMDEVNRQ QTTKGIWMAV SPGVSNSLPA
NAHVPPENIL VMDVEGTDGR ERGEDQDFER KAALFALSTS EVLIVNMWES QVGLYQGANM
GLLKTVFEVN LSLFGKAKLQ NNDHKVLLLF VIRDHLGVTP MESLAATITQ DLLRIWEGLN
KPADVAHLAF DDFFDLAFHT LSHKVLQNEK FLDDVRSLGN KFLDTSSESF LFKPNYHHDI
PIEGWTMYAE NCWDQIDHNK DLDLPTQQIL VAKFKCDEVA AQCFEEFAKV SHELKNVAVS
ATQSTEPIDY KDTGLGFQDM KQSVLEDYDL GASKYNKSVY QQKRATLAEK IDSTLQDVFA
IYAKHLVTTS LKAVSAGLSR KTRSGTFVEA MEKLKQSSAH DFSQALALIS LDGALDTRPF
EKEYLAELEQ LVSKQQIVEL NSILSKALKK LNNGLSTCFV EELANPSELT WDHILEKFRG
LSKSALQKYE TEEGDYDFRL GTLPSMNKRA LKTFDFKSWE LLDNLIHKYI SKDNLLNILK
DRFDDKFRYD ENGVPRLYQN TKELEGSFSE SKTHALKAFP ILTVARLSDG TEVIPKYDVR
DKKLKRQYET VREEKEAEEE DEDEWDSEDD ENQRAFAELL SESEKAEVMA KFKREMDAKF
VETKRSIMQH VTQIPYYIYI VILVLGWNEF MAILRNPFFF TLLIMLAGAT YVMYSMNLLG
PASIVVQRMA NEALGLAKEK LREFVVDDHM QHGHNMKKMT TNDIELDDLS EEST
