SEY1_DICDI
ID SEY1_DICDI Reviewed; 894 AA.
AC Q54W90;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Protein SEY1 homolog {ECO:0000255|HAMAP-Rule:MF_03109};
DE EC=3.6.5.- {ECO:0000255|HAMAP-Rule:MF_03109};
GN ORFNames=DDB_0206311;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Probable GTP-binding protein that may be involved in cell
CC development. {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}.
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; AAFI02000033; EAL67525.1; -; Genomic_DNA.
DR RefSeq; XP_641502.1; XM_636410.1.
DR AlphaFoldDB; Q54W90; -.
DR SMR; Q54W90; -.
DR STRING; 44689.DDB0206311; -.
DR PaxDb; Q54W90; -.
DR EnsemblProtists; EAL67525; EAL67525; DDB_G0279823.
DR GeneID; 8622242; -.
DR KEGG; ddi:DDB_G0279823; -.
DR dictyBase; DDB_G0279823; sey1.
DR eggNOG; KOG2203; Eukaryota.
DR HOGENOM; CLU_011270_0_0_1; -.
DR InParanoid; Q54W90; -.
DR OMA; TNFDVMD; -.
DR PhylomeDB; Q54W90; -.
DR PRO; PR:Q54W90; -.
DR Proteomes; UP000002195; Chromosome 3.
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:0140221; C:pathogen-containing vacuole membrane; IDA:dictyBase.
DR GO; GO:0003925; F:G protein activity; IMP:dictyBase.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0016320; P:endoplasmic reticulum membrane fusion; IBA:GO_Central.
DR GO; GO:0007029; P:endoplasmic reticulum organization; IDA:dictyBase.
DR GO; GO:0051851; P:modulation by host of symbiont process; IMP:dictyBase.
DR GO; GO:1903371; P:regulation of endoplasmic reticulum tubular network organization; IMP:dictyBase.
DR GO; GO:1900101; P:regulation of endoplasmic reticulum unfolded protein response; IMP:dictyBase.
DR GO; GO:0090182; P:regulation of secretion of lysosomal enzymes; IMP:dictyBase.
DR GO; GO:0007033; P:vacuole organization; IMP:dictyBase.
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..894
FT /note="Protein SEY1 homolog"
FT /id="PRO_0000384943"
FT TOPO_DOM 1..800
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 801..821
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 822..824
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 825..845
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 846..894
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT DOMAIN 138..361
FT /note="GB1/RHD3-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT REGION 1..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 21..60
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..93
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 148..155
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
SQ SEQUENCE 894 AA; 104017 MW; DDDED27306E4CCB5 CRC64;
MSEEITTNQT VEEEQQTNQP RLSNENIKQE DEEQQVQEQQ EQQQQEQQEQ IDDQDTQQQE
DEFVVLEETK PVEPIRPTPT LQETPQQQKQ QTQEQEHEYQ DIVQFIDHKG DIVKEDNKNG
RTTFLSTLSN RDDFLTKGFD YSVISILGPQ SSGKSTLLNL LFNTRFAVMD ASTGRKQTTQ
GVWMGVASTT NNKNETFLIL DVEGTDGRER GEDEKAFERK TSLFSLALSS VLIINMWAHD
IGRYNAANIS LLKTVFELNL QLFQKKRNHK ILIFFLIRDH DGVTPLERLK ATLMEDITKL
WTDLQKPEEF VGTRESDFFD FEFTTLPHKI YSPTAFLGQV EQLKQRFSDS GADSFIPKRK
YRNDDIPADG FYQFSYQVWE TIKSNRDLDL PSQKEMLALY RCDEFVEQSM TQFTRDIKPI
KEHIERGRIQ EQFGEKSKRI LDQSLSVYDE PAQRYHLETV QKKRQVLTDR ILTELKYLFD
KQMERLNENT LVFYNSLIKE FTDSNTGSSS GSGNNNNKKR DGSSVLLTAA SVGIIPQFST
WSNGIKKKSI EYFEIVANQS IVPGSDWSFE NDLEQLKIKI DKELSILKEN QLVRLSKLMR
DKTFQQELTP LLTKITEQAP NNMWQKIKTY YDDALSSNEK EFRDRLVDFQ LDEQKVNELI
NKFREQLADG LKNKITERAE FLQMRMRKRF EEKFNMDNRN LPRKWTKTDD IASIFQDARQ
NAEKLIDLFS YLRLDEEDSN VSFFKRLDND EHEENTMVNS SKIIIPYKDC CLACENFRLT
IKSDYMQALS EQNRLTSGGG VPGYMIILLC VLGFNEFISI ISSPLLLLLT ILLGGVGFVL
FKLGLAGPFI DYSSQILVHF ISKVKDIVLH VEQLQEQNHN NNNNNNNTPK QKRE
