SEY1_TRYB2
ID SEY1_TRYB2 Reviewed; 854 AA.
AC Q388F1;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 78.
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=Tb10.61.2200;
OS Trypanosoma brucei brucei (strain 927/4 GUTat10.1).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX NCBI_TaxID=185431;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=927/4 GUTat10.1 {ECO:0000312|Proteomes:UP000008524};
RX PubMed=16020726; DOI=10.1126/science.1112642;
RA Berriman M., Ghedin E., Hertz-Fowler C., Blandin G., Renauld H.,
RA Bartholomeu D.C., Lennard N.J., Caler E., Hamlin N.E., Haas B., Bohme U.,
RA Hannick L., Aslett M.A., Shallom J., Marcello L., Hou L., Wickstead B.,
RA Alsmark U.C.M., Arrowsmith C., Atkin R.J., Barron A.J., Bringaud F.,
RA Brooks K., Carrington M., Cherevach I., Chillingworth T.J., Churcher C.,
RA Clark L.N., Corton C.H., Cronin A., Davies R.M., Doggett J., Djikeng A.,
RA Feldblyum T., Field M.C., Fraser A., Goodhead I., Hance Z., Harper D.,
RA Harris B.R., Hauser H., Hostetler J., Ivens A., Jagels K., Johnson D.,
RA Johnson J., Jones K., Kerhornou A.X., Koo H., Larke N., Landfear S.,
RA Larkin C., Leech V., Line A., Lord A., Macleod A., Mooney P.J., Moule S.,
RA Martin D.M., Morgan G.W., Mungall K., Norbertczak H., Ormond D., Pai G.,
RA Peacock C.S., Peterson J., Quail M.A., Rabbinowitsch E., Rajandream M.A.,
RA Reitter C., Salzberg S.L., Sanders M., Schobel S., Sharp S., Simmonds M.,
RA Simpson A.J., Tallon L., Turner C.M., Tait A., Tivey A.R., Van Aken S.,
RA Walker D., Wanless D., Wang S., White B., White O., Whitehead S.,
RA Woodward J., Wortman J., Adams M.D., Embley T.M., Gull K., Ullu E.,
RA Barry J.D., Fairlamb A.H., Opperdoes F., Barrell B.G., Donelson J.E.,
RA Hall N., Fraser C.M., Melville S.E., El-Sayed N.M.A.;
RT "The genome of the African trypanosome Trypanosoma brucei.";
RL Science 309:416-422(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; CM000208; EAN78819.1; -; Genomic_DNA.
DR RefSeq; XP_827931.1; XM_822838.1.
DR AlphaFoldDB; Q388F1; -.
DR SMR; Q388F1; -.
DR STRING; 5691.EAN78819; -.
DR PaxDb; Q388F1; -.
DR GeneID; 3662737; -.
DR KEGG; tbr:Tb10.61.2200; -.
DR VEuPathDB; TriTrypDB:Tb927.10.14510; -.
DR eggNOG; KOG2203; Eukaryota.
DR InParanoid; Q388F1; -.
DR OMA; YHVVGVF; -.
DR Proteomes; UP000008524; Chromosome 10.
DR GO; GO:0005737; C:cytoplasm; IDA:GeneDB.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
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:0005739; C:mitochondrion; IDA:GeneDB.
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 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; 2.
DR Pfam; PF05879; RHD3; 2.
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..854
FT /note="Protein SEY1 homolog"
FT /id="PRO_0000384963"
FT TOPO_DOM 1..724
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 725..745
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 746..748
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 749..769
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 770..854
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT DOMAIN 49..291
FT /note="GB1/RHD3-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT REGION 808..854
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 336..386
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT COMPBIAS 815..839
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 840..854
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 59..66
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
SQ SEQUENCE 854 AA; 95106 MW; 354483EC4FBE4107 CRC64;
MAAFSGETAV KGIHLINDDG ELLPEADIND FLISALAGKG SSDILYRTGV NYHVVGVFGG
QSSGKSTLLN SLFQTEFMTM DEAHHRGQTT KGAFMTRAIL DAQTHRKERE EGEGADLLKR
EKPQPLFVLD FEGTDGIERG EDQNFERQLS LFALSVADIL IINMWAVDVG RFNAANMNLL
RTVFEVNLQL FSHGSYVKEE KPTLLVVLRD FTENDPAPSF ETVRKSFDKI WGNIQKPESF
TDATIDVVFD LRYRVLPHYK LQRPEFDSAV SEFREWFVSP KNSNFLFSNC SMFRGVPADG
MPSYLSNCWN AICSSKDLDI PTQRDMLARH RCADAKHAAI EEFKEVCEEY TKKIQRGDVI
PQFTRALEET IERLLKNFSD QTKLYKVSVV HETAEALEEE LGDMELHLLK QYAKSIAVTV
LAALDGVIGS SVDEAVRWLQ NEARSVLLLE GKDNKGDRID GGGLAQGVLD TAEGLVDNKR
CRLFVEEFWK RICLSLQGAF DMLNGCSKSH QAALSSLYGK FATAIMDDQA VREGVAHAAM
EGAQHKLRNR FVAMAENAAE TVHQVFEQAL TSKTDGTVRF FRTTDGLLGA EKQARQAGLV
LLGCLLYYRL KLVPVEVDAG EVEGEGTTRA LQRLVRDRCR FQVRDNRTEK NFFLHFTNIS
DVPRYPLDAP TSVVDSGDTT ADTVNADNVL LSHNALQCAF HLYKQKADFT LQMQLRNIES
GKQSLPPWVL PVMLLLGWNE LYYLLTSPIL LIAIIVIAVL FFKTFLKSQL EVLEEKCPVW
LVVSVKALLQ QAQALQNAYA PTEAVRGGGG GAQFRDPTQA TSVSGASAGV SSESSSAASP
RRRVCRESRD KGED
