SEY1_THEAN
ID SEY1_THEAN Reviewed; 918 AA.
AC Q4U9I8;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 64.
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=TA08650;
OS Theileria annulata.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC Theileriidae; Theileria.
OX NCBI_TaxID=5874;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ankara;
RX PubMed=15994557; DOI=10.1126/science.1110418;
RA Pain A., Renauld H., Berriman M., Murphy L., Yeats C.A., Weir W.,
RA Kerhornou A., Aslett M., Bishop R., Bouchier C., Cochet M., Coulson R.M.R.,
RA Cronin A., de Villiers E.P., Fraser A., Fosker N., Gardner M., Goble A.,
RA Griffiths-Jones S., Harris D.E., Katzer F., Larke N., Lord A., Maser P.,
RA McKellar S., Mooney P., Morton F., Nene V., O'Neil S., Price C.,
RA Quail M.A., Rabbinowitsch E., Rawlings N.D., Rutter S., Saunders D.,
RA Seeger K., Shah T., Squares R., Squares S., Tivey A., Walker A.R.,
RA Woodward J., Dobbelaere D.A.E., Langsley G., Rajandream M.A., McKeever D.,
RA Shiels B., Tait A., Barrell B.G., Hall N.;
RT "Genome of the host-cell transforming parasite Theileria annulata compared
RT with T. parva.";
RL Science 309:131-133(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; CR940353; CAI76515.1; -; Genomic_DNA.
DR RefSeq; XP_953140.1; XM_948047.1.
DR AlphaFoldDB; Q4U9I8; -.
DR SMR; Q4U9I8; -.
DR STRING; 5874.XP_953140.1; -.
DR PRIDE; Q4U9I8; -.
DR GeneID; 3863163; -.
DR KEGG; tan:TA08650; -.
DR VEuPathDB; PiroplasmaDB:TA08650; -.
DR eggNOG; KOG2203; Eukaryota.
DR eggNOG; KOG3362; Eukaryota.
DR InParanoid; Q4U9I8; -.
DR OMA; TNFDVMD; -.
DR OrthoDB; 418635at2759; -.
DR Proteomes; UP000001950; Chromosome 4.
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 InterPro; IPR007529; Znf_HIT.
DR PANTHER; PTHR45923; PTHR45923; 1.
DR Pfam; PF05879; RHD3; 1.
DR Pfam; PF04438; zf-HIT; 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..918
FT /note="Protein SEY1 homolog"
FT /id="PRO_0000384958"
FT TOPO_DOM 1..701
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 702..722
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 723..725
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 726..746
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 747..918
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT DOMAIN 46..280
FT /note="GB1/RHD3-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT COILED 554..626
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT BINDING 56..63
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
SQ SEQUENCE 918 AA; 105667 MW; A13E99912AA2B5CC CRC64;
MESSNHLPNK DSDTVSVTPV EFSNYQCEIN PGFNDFLKKS GFEDFGFKFN VVTILGSQSS
GKSHLLNSLF NASFQTMDAS KGHSQTTKGI WGSLVLSKDT SMNATVVFDS EGTDSRERGE
GRLTFEHRSS LFCLALSDVV IVNIWYNSMG NLTGSNYGLL KTVVEANLEL VDTNNEENYK
TVLFFCVRDW SPSLSPLNVV KDYVLNNYMS SIWNEISKPA RFENLGVESL FEIRVFGLSN
AVTQSESFEM DVKEVKKTWN SLKPREYSRR VPSDGFFVYS KNVWKTIIEQ NHLDIPTQKE
MLSSYRCSEI KTMILESLTN ALPELKEKDF SEYLMGLLKK VENQYFSQAS RYDPVVSKKV
GKELLEQVCR KFQPFFESAL GDYVKKLAVE SSSLLDKEFS VNSSGKELKV SNARPYTVWP
NFSKKCEELQ KKQTEKLSHH LSSFKVTFKS TVSFEFEFEY QPLKDHLNLL VSSEFEVLRS
RHLELLKQQL DSMCNSCFAL VKNNMMDRSL NEDQFWDYFD ELFDETHKNC VDQLTTSYVG
LVKGATRTEF EQLSLVLLLK ATQSNFEELQ NNLEQLLLER FDKFFNYQEF KGELIPTEWH
KQSAQELNNR YKESKEDALT LLQVLKTTKT KKLPSFDANY VKKNQYFYST LEGPVSDKYS
SPLTEQFTIE LTNSCSKKFM EMYKNAQVVQ NAGTSVSSWR NIPPVFWLVL LVLGWNELRA
AFRVLLKFYI LIPLLIVSYF TFSYSANKLL GPKANEYVKP VRDKALSLLT ALFAWFVRTL
HMIASKSSSF KQQTKNLKMA KKGNKNRDSD DEYVGKTVTK SSHSIYKHRE PMDINLIVDH
DEVEAEKNNL PCWRAAYASG PARPQRHLCV ICGFFANYKC RNCATRRIEA INSYYCSLRC
LEVHNETNCG KAVHLAQW