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YTYK2_DICDI
ID   YTYK2_DICDI             Reviewed;         918 AA.
AC   Q54R58;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Probable tyrosine-protein kinase DDB_G0283397;
DE            EC=2.7.10.2;
GN   ORFNames=DDB_G0283397;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC         [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Tyr protein
CC       kinase family. {ECO:0000305}.
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DR   EMBL; AAFI02000055; EAL65683.1; -; Genomic_DNA.
DR   RefSeq; XP_639033.1; XM_633941.1.
DR   AlphaFoldDB; Q54R58; -.
DR   SMR; Q54R58; -.
DR   STRING; 44689.DDB0229872; -.
DR   PaxDb; Q54R58; -.
DR   EnsemblProtists; EAL65683; EAL65683; DDB_G0283397.
DR   GeneID; 8624058; -.
DR   KEGG; ddi:DDB_G0283397; -.
DR   dictyBase; DDB_G0283397; -.
DR   eggNOG; KOG0192; Eukaryota.
DR   HOGENOM; CLU_317490_0_0_1; -.
DR   InParanoid; Q54R58; -.
DR   OMA; SLAWMAP; -.
DR   PRO; PR:Q54R58; -.
DR   Proteomes; UP000002195; Chromosome 4.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   Gene3D; 2.130.10.10; -; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00320; WD40; 4.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 2.
DR   PROSITE; PS50082; WD_REPEATS_2; 1.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Repeat;
KW   Transferase; Tyrosine-protein kinase; WD repeat.
FT   CHAIN           1..918
FT                   /note="Probable tyrosine-protein kinase DDB_G0283397"
FT                   /id="PRO_0000355146"
FT   DOMAIN          177..445
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REPEAT          626..667
FT                   /note="WD 1"
FT   REPEAT          684..722
FT                   /note="WD 2"
FT   REPEAT          724..765
FT                   /note="WD 3"
FT   REPEAT          776..820
FT                   /note="WD 4"
FT   REPEAT          823..862
FT                   /note="WD 5"
FT   REGION          1..122
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          457..504
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..49
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        55..81
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        95..122
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        307
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10028"
FT   BINDING         183..191
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         204
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   918 AA;  102616 MW;  2E67BA9688A5F45D CRC64;
     MFNNDKDDNN QGNENNENNK INIKTSIDMG NYINSSSLVE SFGSGSNRNN DKSEDVEYDD
     DDDDDDDEIA STEEEKESDL DSDSDLAPTQ IIVDDSDDFY NNNNGGGGGG GNEDISSTSP
     TLITSNSFND KINQIFSRGG SSLNSSFLNN GENKINFKQL VKLKSTLKKH EIPSRELTVE
     KEIGQGFFGK VYKARWRGKS VALKKITLIK FRDLTETEIF DKEVSIMSKL CHPTCVMFIG
     ACSLDGPSND RSIIMEYMEG GSLRRLLDEK SSYHLPPSLQ LSIARDIAEG MNYLHTNFKE
     GPIVHRDLTS SNILLNSSYT VAKINDFGLS KEMKPGPTEM TAAMGSLAWM APECFKAENY
     TEKVDVYSFA IILWEIVTCR DPYNGMEPLR LAFLASVEDY RLPLNGFPPY WVELISKCWN
     ITPSLRPSFK EILQILNQIE SDPLFLNLNL NCSSNNTSSG STSTSSGSSS SSDNNLTKSS
     ESNNNLRESN INNQIKSNKN SSKNGYYAQD INDYSLSMQV ETKNCIYNNV SDNVNNNNNN
     NNNNNNDNDF FKSSFTKKSF LSNNNYNNNN NNINNKNNNT NNLNDNLIIK SLNHISEQNS
     FLVSYQDSNI VKYFSLDNES LTSTLQMEQS VVCMKYQIIN EKVFLVVAMS NNNISLFELK
     KTDFSGSANS PTTLLPIKVI KCDEQRHTIK DITWNGTHVI TSSFKDSSIQ IWDLEKSLYP
     ISKMDNGGVG ILSIDSQSHQ PLMISGDSDG KVKLWDIRNS HCFRTLTHSP PSSSSGGSIG
     VDSVLFRSPH AVRDPIILTG SSKDCKFKVW NMYSSTCLNS FQSHNKDLLG IHRNQSSQQM
     ITWSSEGTIS LFNSGNNINN QNNQNNNNDC GNDNDSVEFS KVLNVNSMMS NEPLQSAQII
     SKNRIIFSSK NKFYSIIA
 
 
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