SEY1_PLAKH
ID SEY1_PLAKH Reviewed; 883 AA.
AC B3LAJ9;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Protein SEY1 homolog {ECO:0000255|HAMAP-Rule:MF_03109};
DE EC=3.6.5.- {ECO:0000255|HAMAP-Rule:MF_03109};
GN Name=SEY1 {ECO:0000250|UniProtKB:A0A509AN59}; ORFNames=PKH_133110;
OS Plasmodium knowlesi (strain H).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX NCBI_TaxID=5851;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H;
RX PubMed=18843368; DOI=10.1038/nature07306;
RA Pain A., Boehme U., Berry A.E., Mungall K., Finn R.D., Jackson A.P.,
RA Mourier T., Mistry J., Pasini E.M., Aslett M.A., Balasubrammaniam S.,
RA Borgwardt K., Brooks K., Carret C., Carver T.J., Cherevach I.,
RA Chillingworth T., Clark T.G., Galinski M.R., Hall N., Harper D., Harris D.,
RA Hauser H., Ivens A., Janssen C.S., Keane T., Larke N., Lapp S., Marti M.,
RA Moule S., Meyer I.M., Ormond D., Peters N., Sanders M., Sanders S.,
RA Sargeant T.J., Simmonds M., Smith F., Squares R., Thurston S., Tivey A.R.,
RA Walker D., White B., Zuiderwijk E., Churcher C., Quail M.A., Cowman A.F.,
RA Turner C.M.R., Rajandream M.A., Kocken C.H.M., Thomas A.W., Newbold C.I.,
RA Barrell B.G., Berriman M.;
RT "The genome of the simian and human malaria parasite Plasmodium knowlesi.";
RL Nature 455:799-803(2008).
CC -!- FUNCTION: Probable GTP-binding protein involved in generating and
CC maintaining the structure of the tubular endoplasmic reticulum network.
CC {ECO:0000250|UniProtKB:A0A509AN59}.
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; AM910995; CAQ42803.1; -; Genomic_DNA.
DR RefSeq; XP_002260831.1; XM_002260795.1.
DR AlphaFoldDB; B3LAJ9; -.
DR SMR; B3LAJ9; -.
DR STRING; 5851.B3LAJ9; -.
DR EnsemblProtists; CAQ42803; CAQ42803; PKH_133110.
DR GeneID; 7322988; -.
DR KEGG; pkn:PKNH_1342000; -.
DR VEuPathDB; PlasmoDB:PKNH_1342000; -.
DR HOGENOM; CLU_312978_0_0_1; -.
DR InParanoid; B3LAJ9; -.
DR OMA; WREISMA; -.
DR PhylomeDB; B3LAJ9; -.
DR Proteomes; UP000031513; Chromosome 13.
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; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..883
FT /note="Protein SEY1 homolog"
FT /id="PRO_0000384956"
FT TOPO_DOM 1..795
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 796..816
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 817..819
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TRANSMEM 820..840
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT TOPO_DOM 841..883
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT DOMAIN 33..279
FT /note="GB1/RHD3-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT COILED 673..693
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT BINDING 43..50
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
SQ SEQUENCE 883 AA; 102015 MW; 78A1320621567C31 CRC64;
MQMDRKTQII DYDGNMIADL KEWMIRNKLA NLGFNYNVVA ILGSQSSGKS TLLNNLFKTS
FDVMNTKLGH SQTTQGLWLS FDTFEESPVS PLEKGNSTTP INPTLILDVE GNDSKERGDN
RLTFEHRSAL FSLALADCLI VNLWYHSLGN FTASNYGLLK TVMEVNLELF QQDKNCPKTI
LLFTVRDWFE EFASIDIVKN KIVEEYLNKI WAEMKKPPSA KKANINNYFI VEVVGLSHAI
IKKTEFLNDV ENLRKKWINE LRPLQYSRNI PSDGFAHYCN NIWNTIVKQS QLDIPSQKEM
LATFRCQEIK NNVISNTSKM IKEKLTASSS QPTSASIDEF KSWAEKDIVE KSLDEYFVDA
SRYTESICLK TSEELLESLF IQLQTIVDNN LNFTQRVLSA KFANELNTMY SVCTSDKNVF
LFSKESNLQV HKDGNGSNSS KEDKKDENTS QDKCIRLWSS FLSNADKLEY ITFCNFFESY
QKCNIEIRKK NKIHEFNYKP SLNILLTSIC KDMNRIRNTQ FTVLLERTRA TIKSRFKNMD
NLLITTKNPE EYWNHTLKIV KALQESINNN LTKCFINLKG GGPGSSVAGI SNELFDHDED
NTFHVDSPSE GHRSISDNRT AHENKHYVDE NLLNYKKIDI IKNKGKYISS VSEEIDKQIK
NKKAISELNN YYLDEIMDVL KSKLDEISDN LSSIIIQRFE SVFNYDDAEQ PRHWREISMA
ELKKIFRESK NYAFLIIDIL QKNIKVELID DYLPNNFIKD EVIEKGKNKA KRKIQEICRD
AQYIQETGGK MSLKNVPLFF WVILLILGWN ELLFFIRFFF RLNIILPLFL AAAVILSTLF
FNGNMEVLST INKVVFFLAK SSFGFYRQLQ TMGEKVAQVP TAD