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Y0038_DICDI
ID   Y0038_DICDI             Reviewed;        1192 AA.
AC   Q54VU5;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Probable inactive serine/threonine-protein kinase DDB_G0280131;
GN   ORFNames=DDB_G0280131;
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   -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC       inactive.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC       protein kinase family. {ECO:0000305}.
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DR   EMBL; AAFI02000035; EAL67292.1; -; Genomic_DNA.
DR   RefSeq; XP_641260.1; XM_636168.1.
DR   AlphaFoldDB; Q54VU5; -.
DR   SMR; Q54VU5; -.
DR   STRING; 44689.DDB0230038; -.
DR   PaxDb; Q54VU5; -.
DR   EnsemblProtists; EAL67292; EAL67292; DDB_G0280131.
DR   GeneID; 8622392; -.
DR   KEGG; ddi:DDB_G0280131; -.
DR   dictyBase; DDB_G0280131; -.
DR   eggNOG; ENOG502RSQH; Eukaryota.
DR   HOGENOM; CLU_271739_0_0_1; -.
DR   InParanoid; Q54VU5; -.
DR   OMA; LWEMFAR; -.
DR   PRO; PR:Q54VU5; -.
DR   Proteomes; UP000002195; Chromosome 3.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   Gene3D; 1.25.10.10; -; 2.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000225; Armadillo.
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   Pfam; PF00514; Arm; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   SMART; SM00185; ARM; 3.
DR   SUPFAM; SSF48371; SSF48371; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..1192
FT                   /note="Probable inactive serine/threonine-protein kinase
FT                   DDB_G0280131"
FT                   /id="PRO_0000355171"
FT   DOMAIN          521..783
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          23..90
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          144..189
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          201..236
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          301..406
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          478..499
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          790..831
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        23..76
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        147..177
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        201..234
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        301..338
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        373..395
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        790..828
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         527..535
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         549
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   1192 AA;  132491 MW;  C5B97018E847F4A6 CRC64;
     MSELDDLLNE MLAESEAALN GQSTINLNNN NSNNNNNNNN NGNSATKISF QEQMPNGNGN
     SSTTTTTAAQ QSATEKRKSR LSQHPSNLNE GGFDYLDTLL NDMSDESIRN SIKTDNSRIK
     SLRLTSTFDL ESTLKDLEET FMKDSSIQNK RKPSSYLSKN LSPPSNPSNI ISNNNASTLP
     LPPPPSQQDD VVIIAKLPPP VSISLPPPPT TEELPLPPPS TEELQLPPPP PTTTTADEQI
     LTDSVKNGNP ILKRVSSERA IILTKEAIDA ADLLDEMIES FGGIPEPNGN NSLPKEIKTT
     SIPTPIVTPS TTTSTNTTTA ATVNKLNASK SPNGTLTTRP AAKLGAPVDI QVSSPKAPTP
     IPTLSSPSPS QSAAPQPAAP QPTPTSQPQP PTTTVSTPVS PTFKDSDQLL DDMISHFKES
     NSNLLTSSSN LDPSAPKVVY TSQQFYPLSV EEQSLQSKVK VQLTPDEQVI QKILGNNDLD
     DDITNKNNDN NSNGNNNNKE LIDEQNQIEQ QQSDKSWYIK AQPSDIIGSG NNGTTQRAGI
     HKDKRIVMKQ WNFITSQATP MLFNEIEQLV AIKHPNILAL AGASFDNQTF TTFTEYITGS
     NLDIVIKNLD EKNELQLILR LSEEIASAMS FLHSFNIVHR SLHPKNILLN SDLKIYIKDY
     GFTSLKDETL KKKFMSFQLK NQLLHTQYLA PELFNVLSGS KGGYDTKVDV FSFGVLLWEM
     FARDIKLSDL KSNTVNGYTH YLRPPLPNCP FTIEKLIKLC LSTDPSVRPT FTTILKILRQ
     PLHTIQRFNK PTQQQQQQQQ QDQQQQQPEQ QLTSSTSSTS TQDSLVSQEQ VEEKIKNEMN
     NLLNPNKRFN ESLDPEKRVK IEKIANVVKD LISQPTLLNL HRASQTIDQL CKNVENIEYL
     LEADFVPLIF QLMDQPYDEI QLSCLKQFST LIEHNEEIMN LFRNLLGINI LMETLNSQKE
     NILFITLRLL SQLSNGADRE ENREQILIKG GIPLLINLLS HQNELIRLQI LWCLTLLLES
     NSVQVEFVKL GGVNQLLDMM VHSINSGFDL RVASALARVI SLKSVQDQIN LGHYRERVVK
     KYLSLLGDTQ FEALRMLGLE AIACLVSNKD SQFILTASNI VDLLLSYLDP NSTSMAPQMT
     ALKIILVLSV NPIHIPYLKS SNIIEPLQYL KSSPHPSIQK AVEKILMLVS SK
 
 
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