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ROC11_DICDI
ID   ROC11_DICDI             Reviewed;        1487 AA.
AC   Q6XHA5; Q55EL5;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Probable serine/threonine-protein kinase roco11;
DE            EC=2.7.11.1;
DE   AltName: Full=Ras of complex proteins and C-terminal of roc 11;
GN   Name=roco11; ORFNames=DDB_G0268636;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=14654223; DOI=10.1016/j.bbamcr.2003.08.008;
RA   Bosgraaf L., van Haastert P.J.M.;
RT   "Roc, a Ras/GTPase domain in complex proteins.";
RL   Biochim. Biophys. Acta 1643:5-10(2003).
RN   [2]
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. ROCO subfamily. {ECO:0000305}.
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DR   EMBL; AY232273; AAO83656.1; -; Genomic_DNA.
DR   EMBL; AAFI02000004; EAL72907.1; -; Genomic_DNA.
DR   RefSeq; XP_647005.1; XM_641913.1.
DR   AlphaFoldDB; Q6XHA5; -.
DR   SMR; Q6XHA5; -.
DR   STRING; 44689.DDB0191297; -.
DR   PaxDb; Q6XHA5; -.
DR   EnsemblProtists; EAL72907; EAL72907; DDB_G0268636.
DR   GeneID; 8616698; -.
DR   KEGG; ddi:DDB_G0268636; -.
DR   dictyBase; DDB_G0268636; roco11.
DR   eggNOG; KOG0192; Eukaryota.
DR   eggNOG; KOG0619; Eukaryota.
DR   HOGENOM; CLU_002809_0_0_1; -.
DR   InParanoid; Q6XHA5; -.
DR   PhylomeDB; Q6XHA5; -.
DR   PRO; PR:Q6XHA5; -.
DR   Proteomes; UP000002195; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005525; F:GTP 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:0004713; F:protein tyrosine kinase activity; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   GO; GO:0036360; P:sorocarp stalk morphogenesis; IMP:dictyBase.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   Gene3D; 3.80.10.10; -; 1.
DR   InterPro; IPR032171; COR.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR020859; ROC_dom.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR020635; Tyr_kinase_cat_dom.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   Pfam; PF16095; COR; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00369; LRR_TYP; 3.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS51450; LRR; 3.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS51424; ROC; 1.
PE   3: Inferred from homology;
KW   ATP-binding; GTP-binding; Kinase; Leucine-rich repeat; Nucleotide-binding;
KW   Reference proteome; Repeat; Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..1487
FT                   /note="Probable serine/threonine-protein kinase roco11"
FT                   /id="PRO_0000358897"
FT   REPEAT          295..316
FT                   /note="LRR 1"
FT   REPEAT          318..340
FT                   /note="LRR 2"
FT   REPEAT          341..362
FT                   /note="LRR 3"
FT   DOMAIN          379..564
FT                   /note="Roc"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00758"
FT   DOMAIN          1185..1452
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          108..134
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          379..564
FT                   /note="Small GTPase-like"
FT   REGION          891..1007
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1464..1487
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1313
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         392..399
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00758"
FT   BINDING         448..452
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00758"
FT   BINDING         507..510
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00758"
FT   BINDING         1191..1199
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         1216
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   1487 AA;  168497 MW;  EB5CD8F6D89F408B CRC64;
     METSQIRNGF NKVEVDVVGP LKDLLVRVMK NINTPFKILN ETFKINYCDQ QETKTKSSFY
     IQTLDANDKS SLELTKSAIK NIQMQQQQQQ QQQQQQQQQQ HHDIFQFTQP SSSHNHSNHH
     HHHHQQQLQQ QQQQQLQQQM KTPKLLFFIV MSVGVGKSYI KNIKEEAGTI PILEWFTNYI
     RSWEEVFKLT SNQVTSHIKR QLLTKACTTG NINLLDEILL SGISKEQIKE TQTIGHGIIL
     KSLIVNNLDS IVVSGSMSLL GAVIDNDNDK KGSSLILSKL NLNLFPKSII TACFNLAELD
     LSYNNIKEIP KEICQLKHLK ILNMNNNQLD DLPLELANLT NLKYLAVQDN PLNKFPHHII
     EQGTKRTLVF LKNIIEGKKS ETWNKVKLMF VGQEGVGKSS LCKALMGSRR RSSSSFAAEL
     QKSGDTISTE GVKIQSIKGK KIDFYAWDFG GQQVFYPTHQ FFLTNQALYL LVFKLTDPNF
     AERVNYWTLQ IKANSGLSVP MIFLVGTHCD ACTPEQLSSA EQILKENFVK YSRIRQNAIS
     FVSCTNGTGI KELKKILTNE AEKSNLIKSN IPGSYLILEQ RLTDRGANSS RILINQNNIN
     QNNNNNNNNN NHNNCNNNEN CTTTAATAGT TTMTSTTTTT TNYSNENILN TSSNSLIALF
     TRSNSNSNLS NNYQKPLVNQ KYIDYNDFER ECKLSHLAQE EIQGATEFLH NMGIILHYDT
     PILRSLVVLD PQWLADVMSS LITFSHNWIK NGILNHSELV SIWSGKYDQS IWPSLLKLLE
     KFEVSYELPN EFPSRSLIPS LLPEEPIDRI QEIKEKLWIP LPEAIESKRV QIFGCQYNFD
     FMPLGFFPRL LLRILLIKGI DIKTYWANGI LLDILTTEDI KIQKLNHKKH SILPNNSSST
     SSSTSSSTSS STSSSSSSST SSSSTSTTTT TVQIQSSPFG NSTTIVNKLT NIDNNNNNNN
     NNNNNNNNNN NINNNNNNNN NNNNNNNNNN NNNNNNNNNN NNNNNNIKNI INNFENQNNL
     NNIITNNFGG KFEIIKKNDF ESPLSSKKPK HQVLVTFKNQ KSFESKDKDT YKLNVEIRSF
     NVSNNNDKDF LASLFFQQLL STIDTLLSGS YGGLKVTRLI PCIHCIEKDP HSEPHLFDIN
     SCISQLLLGK SQLVCGKDST TPVRIDYIAP DLSIKKIPIL LEDQVVCEEQ IGVGGFGLVH
     KGKLILQDKS LVVAIKSYIV GNSSASDIIR KFQEFHHEMY IMSSLNHLNI VKLFGSMQNP
     PRMVMEFAPH GDLYHFLEKK KNIKWSFKVR LMLDIAKGIE YLQNQNPPIV HRDLRSPNIF
     LFSLDENAPV CAKVADFGLS QQSLYSVSGL LGNFQWMAPE TIGAEESYTE KIDTYSFSMI
     LFTILTGECP FDEFTSFGKM EFIRKIREED LRPTIPSDCP PTISNLIELC WSGDPKKRPH
     FSYIVKELTN FYYNLNLSPI PEQKSINDKS PHPDLISNGV PKLQIAK
 
 
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