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Y1197_DICDI
ID   Y1197_DICDI             Reviewed;        1347 AA.
AC   Q54JC7;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Probable serine/threonine-protein kinase DDB_G0288147;
DE            EC=2.7.11.1;
GN   ORFNames=DDB_G0288147;
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-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1;
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC       protein kinase family. {ECO:0000305}.
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DR   EMBL; AAFI02000109; EAL63361.1; -; Genomic_DNA.
DR   RefSeq; XP_636866.1; XM_631774.1.
DR   AlphaFoldDB; Q54JC7; -.
DR   SMR; Q54JC7; -.
DR   STRING; 44689.DDB0231197; -.
DR   PaxDb; Q54JC7; -.
DR   PRIDE; Q54JC7; -.
DR   EnsemblProtists; EAL63361; EAL63361; DDB_G0288147.
DR   GeneID; 8626477; -.
DR   KEGG; ddi:DDB_G0288147; -.
DR   dictyBase; DDB_G0288147; pkcA.
DR   eggNOG; KOG0192; Eukaryota.
DR   HOGENOM; CLU_257973_0_0_1; -.
DR   InParanoid; Q54JC7; -.
DR   OMA; NCGLASR; -.
DR   PRO; PR:Q54JC7; -.
DR   Proteomes; UP000002195; Chromosome 5.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0140582; P:adenylate cyclase-activating G protein-coupled cAMP receptor signaling pathway; IMP:dictyBase.
DR   GO; GO:0110014; P:negative regulation of aggregation involved in sorocarp development; IMP:dictyBase.
DR   GO; GO:1903669; P:positive regulation of chemorepellent activity; IMP:dictyBase.
DR   GO; GO:0010628; P:positive regulation of gene expression; IMP:dictyBase.
DR   GO; GO:1904007; P:positive regulation of phospholipase D activity; IMP:dictyBase.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   GO; GO:0009372; P:quorum sensing; IMP:dictyBase.
DR   GO; GO:0030833; P:regulation of actin filament polymerization; IMP:dictyBase.
DR   GO; GO:0022407; P:regulation of cell-cell adhesion; IMP:dictyBase.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   GO; GO:0048837; P:sorocarp sorus development; IGI:dictyBase.
DR   InterPro; IPR046349; C1-like_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR002219; PE/DAG-bd.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   SUPFAM; SSF57889; SSF57889; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Kinase; Metal-binding; Nucleotide-binding; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase; Zinc; Zinc-finger.
FT   CHAIN           1..1347
FT                   /note="Probable serine/threonine-protein kinase
FT                   DDB_G0288147"
FT                   /id="PRO_0000355155"
FT   DOMAIN          599..854
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ZN_FING         12..67
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT   REGION          262..316
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          333..402
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          463..485
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          937..1241
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1282..1310
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        266..316
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        333..365
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        366..399
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        938..967
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        993..1084
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1099..1241
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        724
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         605..613
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         626
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   1347 AA;  152496 MW;  6ACB56C1A00BBBCB CRC64;
     MQPNQLKRPS LNHRFEPYTL KHLTICKRCE KEIIGVSNSA QICYSCKNIY HTRCCKEIET
     KKLELICLGP PKKIKTVWKI ALIPSLFKSL FSKSKVIVNY SQQLINEKTF TLEAIKIWVD
     VMRVDNDRYI QITKYYDIFD EEVFNYIINM IIEKDINLPM VNIEFPVDLH SSVQQNQYIN
     DQAVSQEQKQ QQQQLQQQLI LQQQQQQQLQ QQQLNESYDN STINNLNYSN DISNAFSPRS
     VFSALELSSN AQVMNALELS VPFNEDDNND DSTLSASTYN RRNSNKNKNS NKNNTSSSSS
     APASASSSKH SNLNESFSSS TTAAAIVNNI DNSNNSNNLA ALSPRSTAST TTTTTTTTTT
     TSPKSNNHHH HQHHHQNSKS RKPSTIIINK KKIKSPKNKS SKRYMLTEQY KWSTQMIGLQ
     ILYRILFNEK NMIHFLNDKF MAPLAVLYPI LINRLKAISL GSDNNNNNNN NNNNNNNNSN
     NNNNNNNEDF KLLSINCKLL ISILNRMLDF ETLIPLFFTN KVIESIAKVN SDRESLRGKL
     SKDEFEVMDR VVLLLGKYFH LEPYHSLIER RPEWIDMIIN YSVEHKVGIL HHEITRNEVK
     INVEIYDSPL CTVYSGVYNG MDVAIKEFSQ DGMGFDWVSF YKEITIVSAS QHPKVIKCYG
     AHTKNTNKPF IVTELCSRGT ISNALNQIRK TTGQPPAIPL IVHMAIDAAQ SLEFIHSKNI
     IHRDVKGNNF LVNENWEVKL IDFGVSRFVE ARLGYTIVGT PNYMACELFN GQPYHQPADV
     FSFGVVLWEM FTQDTPYKNL TRIEQALFVQ SGGRPTIPPT VPTTIANLIE SCWVQTPHLR
     PTFTEILKVF YSLLTPPPDN EHLVPVVTRL FNSSIIQLKI LKYLDTNTLL NCGLASRQLR
     YNLYNGISME KKTFSNFWIK LMNFSKSKFR YELLSPSERK NDSTGSSPII MCIQPFSPNS
     QSKNNNNNKN HHSDDIIDDD DDDDDDKTYP SLVIPFSASS PTLNINSENK NNNNVNEDKT
     SDTSSNSNNN NNNNNNNNNN NNNNNNNNNN NNNSNNNNNN NNLRQNQFLG NDLNKSQDNN
     QLMDGSGGRR DRSRSKSRSR SASPSNNHLH DKSLMGLLSS SQTSEIGDNN TNNNSDNEVD
     NNNNNNNNNN NNNNNNNNNN NNNNNNNNNN NNNNNNNNNN IDNNNNNKDN NNILSSENNN
     NTTVIEQQQQ QQNVTNNNSN EPKNSNNEPK NSNITNNIVN PNVFTTTTTT TTTTRTTTTT
     VYDGTGTLNN LLFKINDGGI ISSDSSNSLS DPESEEYSMP IKRSSSIRSP GPVSAISPLF
     KSLSPNLSPI VPNIINGYSF ENTSACD
 
 
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