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SEY1_PLAF7
ID   SEY1_PLAF7              Reviewed;         937 AA.
AC   Q8ILT5; A0A144A1B3;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 2.
DT   03-AUG-2022, entry version 95.
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};
GN   ORFNames=PF14_0159, PF3D7_1416100;
OS   Plasmodium falciparum (isolate 3D7).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX   NCBI_TaxID=36329;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3D7;
RX   PubMed=12368864; DOI=10.1038/nature01097;
RA   Gardner M.J., Hall N., Fung E., White O., Berriman M., Hyman R.W.,
RA   Carlton J.M., Pain A., Nelson K.E., Bowman S., Paulsen I.T., James K.D.,
RA   Eisen J.A., Rutherford K.M., Salzberg S.L., Craig A., Kyes S., Chan M.-S.,
RA   Nene V., Shallom S.J., Suh B., Peterson J., Angiuoli S., Pertea M.,
RA   Allen J., Selengut J., Haft D., Mather M.W., Vaidya A.B., Martin D.M.A.,
RA   Fairlamb A.H., Fraunholz M.J., Roos D.S., Ralph S.A., McFadden G.I.,
RA   Cummings L.M., Subramanian G.M., Mungall C., Venter J.C., Carucci D.J.,
RA   Hoffman S.L., Newbold C., Davis R.W., Fraser C.M., Barrell B.G.;
RT   "Genome sequence of the human malaria parasite Plasmodium falciparum.";
RL   Nature 419:498-511(2002).
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; LN999946; CZT99872.1; -; Genomic_DNA.
DR   RefSeq; XP_001348332.2; XM_001348296.2.
DR   AlphaFoldDB; Q8ILT5; -.
DR   SMR; Q8ILT5; -.
DR   STRING; 5833.PF14_0159; -.
DR   PRIDE; Q8ILT5; -.
DR   EnsemblProtists; CZT99872; CZT99872; PF3D7_1416100.
DR   GeneID; 811740; -.
DR   KEGG; pfa:PF3D7_1416100; -.
DR   VEuPathDB; PlasmoDB:PF3D7_1416100; -.
DR   HOGENOM; CLU_312978_0_0_1; -.
DR   InParanoid; Q8ILT5; -.
DR   OMA; WREISMA; -.
DR   PhylomeDB; Q8ILT5; -.
DR   Proteomes; UP000001450; Chromosome 14.
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: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; 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..937
FT                   /note="Protein SEY1 homolog"
FT                   /id="PRO_0000384955"
FT   TOPO_DOM        1..848
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   TRANSMEM        849..869
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   TOPO_DOM        870..872
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   TRANSMEM        873..893
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   TOPO_DOM        894..937
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   DOMAIN          34..280
FT                   /note="GB1/RHD3-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT   COILED          319..339
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   COILED          725..750
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
FT   BINDING         44..51
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03109"
SQ   SEQUENCE   937 AA;  110609 MW;  0105532D574D6D20 CRC64;
     MEKGVEKTQI IDYDGNVIED LKEWMIDNKL NDLGFSYNVI AVLGSQSSGK STLLNNLFKT
     SFDVMNTKQG HSQTTKGLWL SYDKFDDETN NSSSFFKLKK KNKPTLILDV EGTDSKERGD
     NRLTFEHRSA LFCLALADCV IVNLWYHSLG NFTASNYGLL KTVMEVNLEL FQQEKNSPKT
     ILLFTVRDWF EEFAPIEVVR NKILDEYINK IWKEMKKPKE AEKLNINNFF IIEVVGLSHG
     IIKKEDFLKD VNNLRDKWIN NLRPSKYSRN IPSDGFAQYC NNIWNTIVKQ SQLDIPSQKE
     MLSTFRCQEI KNNVINNINK EIKEKSIESH NKVIENFKEW AEKNIIQKCL DDYFKDASRY
     KENICLRTSQ ELLDYLFTQL QAIVDNNLQY IQRTLCTKFF NELSNMYKIC TIEKNTFSFS
     RDSNLKTVKD NNKNTSHEDI KRDLLNNNQD KCVHLWSNFL YNADKLEYFT FCNFYENYEK
     SNIEIKTNMK NDDNLKNDDN LKNDAHNNIT THQFNYKPTL SVLSTSIYKD SNRIRNIQCG
     ILLNKTRQTI KNSFKNMDTY LLTTKNTEEY WNNTVQLVLK LQDNINTHLT KCFINLKGTN
     HNNLNIYNDD MMYNNDDMVF NNNDDDDNNN NNNNNNYYYY NKNDDANLSK DENYNNKFSF
     SLTNEKGIFQ NINNNNEGSD EICYTNALKK IDLIKNKQVY KSTINEDINN KLQNKKYIHE
     LKNYYLDEIM DVLKNKLDEI SENLATIIIQ RFESVFNYDE YEQPRQWRDI SMAELKKIFL
     KSKNYAFLII DILQKNIKVE LIDDYLPNNF IKDEIIEKGK IKAKRRIQEI CRDAQYIQET
     GSKMSLKNVP VVFWIILLLF GWNEILFFIR MFFKLNVILP LFFAAAFIVS TFVYNGNTQA
     LSYINKIIFY MAKNSYNFFK HIQAISNPPP KNVQKQE
 
 
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