ID   SEY1_CRYHO              Reviewed;         815 AA.
AC   Q5CL93;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   12-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 59.
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=Chro.80282;
OS   Cryptosporidium hominis.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC   Eucoccidiorida; Eimeriorina; Cryptosporidiidae; Cryptosporidium.
OX   NCBI_TaxID=237895;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TU502;
RX   PubMed=15510150; DOI=10.1038/nature02977;
RA   Xu P., Widmer G., Wang Y., Ozaki L.S., Alves J.M., Serrano M.G., Puiu D.,
RA   Manque P., Akiyoshi D., Mackey A.J., Pearson W.R., Dear P.H., Bankier A.T.,
RA   Peterson D.L., Abrahamsen M.S., Kapur V., Tzipori S., Buck G.A.;
RT   "The genome of Cryptosporidium hominis.";
RL   Nature 431:1107-1112(2004).
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; AAEL01000059; EAL37374.1; -; Genomic_DNA.
DR   RefSeq; XP_667609.1; XM_662517.1.
DR   AlphaFoldDB; Q5CL93; -.
DR   SMR; Q5CL93; -.
DR   GeneID; 3415472; -.
DR   KEGG; cho:Chro.80282; -.
DR   VEuPathDB; CryptoDB:Chro.80282; -.
DR   VEuPathDB; CryptoDB:ChTU502y2012_421g0325; -.
DR   VEuPathDB; CryptoDB:CHUDEA8_2410; -.
DR   VEuPathDB; CryptoDB:GY17_00000673; -.
DR   InParanoid; Q5CL93; -.
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   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..815
FT                   /note="Protein SEY1 homolog"
FT                   /id="PRO_0000384942"
FT   TOPO_DOM        1..737
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   TRANSMEM        738..758
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   TOPO_DOM        759..761
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   TRANSMEM        762..782
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   TOPO_DOM        783..815
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   DOMAIN          28..260
FT                   /note="GB1/RHD3-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT   COILED          298..321
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   BINDING         38..45
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
SQ   SEQUENCE   815 AA;  93613 MW;  A061CDEC7DAF43F6 CRC64;
     MRQIIDYDCN FKEEVGEVLK DISTSQNTLG FNVISILGCQ STGKSTLLNA LFDTHFKVLD
     KLTSGYCQTT KGLWLGCGTE SFNSPILIWD VEGTDSLERG EDRATFENRA ALFSLAVSDC
     MILNIPLMNL TTYSSSNFGL LKTILNSWFS LKLDQNGITR GNIRKTTLLF AVRDITINDN
     DEMLGRKVVQ ILDLLWRQVA ESQNSLGNQI PASFSDIFEV KVYGIPSLPN DYDGFKQVVA
     AIRYDLTTSI LPKDYTRRIP LEGLEMYCKT VWKCIVDCQE LNIPSQIKLV SRFRCEQAKD
     DILDGYKKSI KDLQKKMEKR EFGFNEFSDC TLLVLENSLA AYFEVASKYD HEMSTNSSIS
     LLVFIFHEFQ NAVNSRMSLE RQDLRQYTNI LDYYKKGIED HQVQYDKENN EESHYVSFDS
     SSWVNKELLK FDSLSLKWKT EFPSVISRQH LISPIKEKCI PDILNEISLS SQGKEVFLAT
     YNTQEQRKLL SETLEIHSKK IYEKLVEEFF ESLIKDILKE ISPLLGDHFL SDPKLKLDDF
     WELTGSSIVN IHRLLVSKYE QQWITLFKNS NMNEFTSSGL EEEIALQLVL KFIQLIQQQS
     KYFHINIVDR FKNEFELDQD GVPRQWIGED AKTMKELFIK AKNNSLQITN VFYPRKDQLI
     PLSGRFSNLF DKIIENSEDL SGIIALNKGH GNGKFLDSVP LISESNLKEI ESKASQEITS
     IFSKAQLIQS TGRQPQNIPW WIYLLIIILG FDEITYVLTS PVLVTLLLLL ASFIYSYLTG
     NFSSFCNYSQ QFVIISTKIL HYISGAIHSS LDNRK