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Y3184_DICDI
ID   Y3184_DICDI             Reviewed;        1186 AA.
AC   Q54C77;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Probable inactive serine/threonine-protein kinase DDB_G0293184;
GN   ORFNames=DDB_G0293184;
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).
RN   [2]
RP   IDENTIFICATION.
RX   PubMed=16596165; DOI=10.1371/journal.pgen.0020038;
RA   Goldberg J.M., Manning G., Liu A., Fey P., Pilcher K.E., Xu Y., Smith J.L.;
RT   "The dictyostelium kinome -- analysis of the protein kinases from a simple
RT   model organism.";
RL   PLoS Genet. 2:E38-E38(2006).
CC   -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC       inactive as it lacks an expected active site aspartate residue.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC       protein kinase family. {ECO:0000250|UniProtKB:Q54QI2}.
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DR   EMBL; AAFI02000199; EAL60944.1; -; Genomic_DNA.
DR   RefSeq; XP_629342.1; XM_629340.1.
DR   AlphaFoldDB; Q54C77; -.
DR   SMR; Q54C77; -.
DR   STRING; 44689.DDB0229972; -.
DR   PaxDb; Q54C77; -.
DR   PRIDE; Q54C77; -.
DR   EnsemblProtists; EAL60944; EAL60944; DDB_G0293184.
DR   GeneID; 8629066; -.
DR   KEGG; ddi:DDB_G0293184; -.
DR   dictyBase; DDB_G0293184; -.
DR   eggNOG; KOG0198; Eukaryota.
DR   eggNOG; KOG4269; Eukaryota.
DR   HOGENOM; CLU_272428_0_0_1; -.
DR   InParanoid; Q54C77; -.
DR   OMA; KRTNQMA; -.
DR   Reactome; R-DDI-75153; Apoptotic execution phase.
DR   PRO; PR:Q54C77; -.
DR   Proteomes; UP000002195; Chromosome 6.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR   GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   Gene3D; 1.10.555.10; -; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SUPFAM; SSF48350; SSF48350; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Coiled coil; GTPase activation; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..1186
FT                   /note="Probable inactive serine/threonine-protein kinase
FT                   DDB_G0293184"
FT                   /id="PRO_0000370210"
FT   DOMAIN          173..437
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   DOMAIN          1004..1186
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT   REGION          1..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          99..122
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          447..468
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          530..551
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          766..911
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          959..988
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          631..659
FT                   /evidence="ECO:0000255"
FT   COILED          875..909
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        28..55
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        766..841
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        847..897
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         179..187
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P28523,
FT                   ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         205
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P28523,
FT                   ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   1186 AA;  134168 MW;  287F58A8B14EDEEC CRC64;
     MEQEDQQYEE DSSQFNKNNY VPDDNSGEKE QPATTTEITT TTTTTTPTAI DNNDSDLTED
     VINAVSKYKD GTSSKSVKKT RRKFAMNIAT DEVFNLPPME QQQQQQHLQP PLSPNSASNT
     NFGAAATFSP TSILSKNNKI ITSQQTSSTS ISPLKPSPLS FSSGILPPSS RIYESPPTLG
     KYDKVILVIL SQQYLQNQVN IFPIKLIDRE RINLIHQNIL SNEFQLLKSL KHSGIVNYIG
     MINDNTGFGI VQEFYENGSL SDIYNRSGAF QESLVAKYTL QILEALGYIH SQGIVHRNLK
     SNNVLLAKGG KVKISDFAIG IRSSAIEPSI RFSLNGYPFW TSPEVLSMKP FNHKVDSWSI
     GCLIMELIVG HPPFSHLGPM EALIEIINPS TTILPNCLDE NEQSLFSLEL NQFLELCFKK
     EPSDRASVHD LLRHPWLSMF NDSSSSSSSS SSQAHPTVQS NNLNGNVNSR THGEFYSLDF
     LSQFEQNEKE ISKILSSGDQ LDSTSNQIDL KKFQFKHYNK KQQQQYNYNY NNYNNNNNNN
     NNTNDNDNEC GEQTEEINLS SLSKDEQIER LKAIIDQNET MANNLKYTMQ EVLQEQTKYY
     EICESMKSKT LEILNQNKTG ARISAHSNSL LKRTNQMAND LGRKYEILQS NIKRLEDYLI
     TKDDCAKKLA NVVYRNKISF DSLLNPTLAA NLLYQIGSKT WKKGQEKRAF ATLKDNFLFF
     FKNEKSSYPI DVIYLNDKRN ISITSIQDSK KKAYIICIGT TIHDQNNLDP SNNNESVNLS
     TSPGSLVNSN SNPSISNSLN NNNNNNNNNN NNNNGNPNVI ITTNNNCNSN SNGNNIATPP
     ISIPNGKEVK EGKEIKEIKE PKEKDKDKEK DKDKEKDKDK EKDKDKEKEK DKDKENNNNN
     NSNNNNNNGN NYNSSETIWC LLAFDNSKNM ENWYGVLDSV VPWYDKRAYE ISKPMLPIEN
     KKHQKQKSLD STNKQSPGSL GGAGGDVSWK KESGGIKFQG VVGVRLDDLM TRESPTAELP
     YFLSKMLKFL EKNVDEEGIL RLSGSSTEIL EMKQQLQRGE SIDYTYKDPH AVTGLLKLFL
     RELPESILPE HLRIQSTEIL SNGRFGEKEK IKEIQTLLSN LSRPHYNVLK HMLFFAKLVV
     DRSEYNKMVI ANVTTCFSPT LRIPPGLFNF LINTYDLSFP KFNLSV
 
 
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