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ROCO9_DICDI
ID   ROCO9_DICDI             Reviewed;        3365 AA.
AC   Q6XHA7; Q54JA1;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Probable serine/threonine-protein kinase roco9;
DE            EC=2.7.11.1;
DE   AltName: Full=Ras of complex proteins and C-terminal of roc 9;
GN   Name=roco9; ORFNames=DDB_G0288183;
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; AY232271; AAO83654.1; -; Genomic_DNA.
DR   EMBL; AAFI02000109; EAL63322.1; -; Genomic_DNA.
DR   RefSeq; XP_636835.1; XM_631743.1.
DR   STRING; 44689.DDB0191512; -.
DR   PaxDb; Q6XHA7; -.
DR   PRIDE; Q6XHA7; -.
DR   EnsemblProtists; EAL63322; EAL63322; DDB_G0288183.
DR   GeneID; 8626504; -.
DR   KEGG; ddi:DDB_G0288183; -.
DR   dictyBase; DDB_G0288183; roco9.
DR   eggNOG; KOG0192; Eukaryota.
DR   eggNOG; KOG0619; Eukaryota.
DR   HOGENOM; CLU_225060_0_0_1; -.
DR   InParanoid; Q6XHA7; -.
DR   OMA; FHFEFNE; -.
DR   PRO; PR:Q6XHA7; -.
DR   Proteomes; UP000002195; Chromosome 5.
DR   GO; GO:0005829; C:cytosol; TAS:dictyBase.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
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:0006468; P:protein phosphorylation; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   Gene3D; 1.10.555.10; -; 1.
DR   Gene3D; 3.80.10.10; -; 4.
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; IPR010569; Myotubularin-like_Pase_dom.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF06602; Myotub-related; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   SMART; SM00369; LRR_TYP; 11.
DR   SMART; SM00324; RhoGAP; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF48350; SSF48350; 1.
DR   SUPFAM; SSF52799; SSF52799; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS51450; LRR; 13.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
PE   3: Inferred from homology;
KW   ATP-binding; GTPase activation; Kinase; Leucine-rich repeat;
KW   Nucleotide-binding; Reference proteome; Repeat;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..3365
FT                   /note="Probable serine/threonine-protein kinase roco9"
FT                   /id="PRO_0000358895"
FT   DOMAIN          243..437
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT   DOMAIN          804..1484
FT                   /note="Myotubularin phosphatase"
FT   REPEAT          1510..1526
FT                   /note="LRR 1"
FT   REPEAT          1527..1549
FT                   /note="LRR 2"
FT   REPEAT          1550..1572
FT                   /note="LRR 3"
FT   REPEAT          1576..1599
FT                   /note="LRR 4"
FT   REPEAT          1600..1622
FT                   /note="LRR 5"
FT   REPEAT          1624..1645
FT                   /note="LRR 6"
FT   REPEAT          1646..1668
FT                   /note="LRR 7"
FT   REPEAT          1670..1691
FT                   /note="LRR 8"
FT   REPEAT          1697..1720
FT                   /note="LRR 9"
FT   REPEAT          1722..1743
FT                   /note="LRR 10"
FT   REPEAT          1744..1770
FT                   /note="LRR 11"
FT   REPEAT          1772..1789
FT                   /note="LRR 12"
FT   REPEAT          1790..1812
FT                   /note="LRR 13"
FT   REPEAT          1814..1835
FT                   /note="LRR 14"
FT   REPEAT          1837..1861
FT                   /note="LRR 15"
FT   REPEAT          1863..1887
FT                   /note="LRR 16"
FT   DOMAIN          3008..3269
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..177
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          397..497
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          944..985
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1044..1098
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1261..1301
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1932..1963
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2190..2389
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2507..2567
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2674..2704
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3311..3365
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..31
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        39..54
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        55..171
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        397..445
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        455..475
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        476..494
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        955..971
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        3132
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         3014..3022
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         3035
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   3365 AA;  380768 MW;  354AF3C8328A8E0F CRC64;
     MTSIANLFDK KSKRSNEDTG EKEETKKSRS GTLKFKTLFG TSKKDKEKKI LQQLQQQQDD
     EQQQQQQQFM EGDNNNNNTN SLNTPSVEGD SENINRLAAS TNSTSYSSLR SSSTRSIDYN
     PSNNGGNGGI RSDSFYSQTS ESSDITSTST TSPTMSAASS SSSSGTVKTP KPPKSSKLKH
     IYNSLKFKSL KTEKNGSSSS IKSNISNFEF IMPNTPLPIF DQQSPPIHFY NSNQFSDFQY
     FGTPLYSLIK RQDNGLSIPI LLEKSISFLE GHCHVEDLFF RKYNNEKVKF MRNSFERTGD
     FNFYYPDPQD PYDVAALLVE FIASLPDQLL NVELYNAIKN HTSALNSQYG GYWDIQYLAQ
     KLSVESREFL QRLLFFLKKH VSACLFKQQQ QQQQQRESTE VLTLSLSSST STLEPEPQPL
     PLSTSTQRLP QQSSDDNSNN DNNNKNDNDN DNDNDNNNDN NNINNDNGEI IPPSIQVTPP
     TSPQTQPKQQ QPPQPPQKTL IEKLSELFTP LFVNYKTHSA FYSSTSTLIT SCEDIFVHID
     ERPITLPGEF IMMQIKNVII PPTNLKLEHT ISSSSKSDKN DKNDKNGNTD VTLWQSGTLF
     ITNYRMIWKK DESNSIDSES NSILLPEDII TPTQSFSSIN NNNNNNSSKF VEIKLYSFEI
     ILTSIIKWES FGKSLKSTTP MMSTPTTFQN GGVNRSQFQI FLCYCKNIRF QYMGFSDESN
     FRDLEKLNLI LAYYINPLID FGRYFSSVNN EIPRAPLLAN NNNSSSNLIS LGRSGITNTS
     TANINGSNRN SVGGNGSHDY TTNIWDIYSP LIEGQRLKLD LDKDWRVVEF LSRDTSTIYP
     KRILIPNLIG DELLQSYVRK TQSKIPIFSW SNQNNKSMLF RICVYNQPFN NKFNSGGTLA
     YNNNSTIINN NSVIITNSST IGTNTSGISN SNHLIVGEIE PPSPIKKRQQ QIVDKKDTSS
     PLSSLRSSKG IPSKSSKKDK QGFLSSSTSS IIPIQTTIST DTVDVKLYNL FVNKEEQLQS
     STSSSPSTSL NNSSNNLNKE FQQIHQQMQQ NQLNSSSNNN NNNNNNNNNN NNNNNNNNNN
     NNNNNNNNNN NNNNNNKINK RQNEATIVFT NKVGGTSDNH INIISVYEQF KMNSSNIIFL
     SIPTREQVEA CWFDLYQSIT SFDGSMDAWK SIEESKWVDS VKLLLEGCVK VSNLLDEGSS
     VLLKPPIDSP LHTLDLASIS SLTMVLSDPF YRTLDGFLIL IEKEWIQYGF PFNNINYHKE
     QNNLNNNNGN KENSSSSSSS SSSTSTTPSI TKKSSGSISK GSSGIASLIN DLDKYDSNFV
     LPDTIHTESQ KKKTYLFQDQ YESSILVNRS FSPIFVQFLD AVWQLQRQFP FHFEFNESLL
     LLLVKESFSG RFGNFLYSEA LRDSERKFLK RSPSIWTFIN QNKSTFINLL YKHSANSSSS
     SSSTNKLPSP ISPRQSFIFK QEDFNEMIKP SCDNDQIILW SSFFTEFINS RESQQISKKL
     IGKVKCDLIS QKLTFLSIDR NLLSYFSTLT KLNLSRNYFN TFPIEIILLS NLTHLWLQDN
     RIKSIPSSLL KLIGSKLKLQ EFDLSHNLLE SLHKSIYTLS TLTKLVLDNN KLIIIPESIS
     KMKQLKCLSV QNNRLSSFPQ ALSLCVGLEE LYVQNNQIRE LPLGFFKLGS LRMLDLRNNQ
     ITKFKCHKLD DKSCFLMNEI IHFRMGPNPL QKLSNQMFEM RSLIHLELTG CSLSTVPLKL
     LDNLVNLEAL YLNQNKLSEI SIDFKRLFKL SVLDLSDNQF TNVPIHAMLP SLKKLYLHNN
     QLYNISFNDF NLPLLSELRL DGNKLTYVSP SIGTKLLSLT LLNLDRNPQI TTLPHTLALL
     KKLKSLIVNS NIMESPFREL ETTDAILRYL TLQMQQSQFH PRNKLIIISD ITNPQIKNEF
     IKNLTIAKPL TSKEREKEKE KEKEKEKEKK HKNIGYGSKD KDKKGININY QQQHQQQQQY
     QQHQYSSQIG FNQNLPIKWE IDYENYPNSA LYNLASTIHC TNSFISQPIM ISSSNQECTK
     LNKEEFLNSR FNTQEISKKK NLTIFIRDLS QLNSSGSASA SGNGSGNGNG IGISNTNCSQ
     HLFSKRAVYC LVWALSESEE PTRIYKWLES IRDRCTFATV FIVGLYNSDY CQDVPKDYYT
     FITPKIEQKC HNLFPNFTFS FINILNNNNN NNNNNNNNNN NNNNNSGGNV VPVQPSINNS
     IDNNVENTNN NNNIINNNNN NNNNNNNNNN NNNSYNSNSN SNSNNNNNNN SNNNNNNNIN
     NNNINNNNNN NNNNNNNNNN NNNNNNSNNN SNNNSNSNSN SNSNNSNNNN INNNNSNNNN
     NNNNNNNNNN NNNNNNNNNN NNNNNDNDNN NNDNNNNLNN SNLNNNNGSN INISSSNNIL
     GGMPKLREEI KNVFLNFKPF GTKVSSSQKL FEKHIKTLQT PFISKKELFS IGEMCKLDKI
     ETKNTCELLT ELGLLFWSED HDWVILDPIW LSNTLNLLLT LKQSSSAPST PPQIPLNSTN
     LNNTSIPSQI TTTSTNSSST STSTSTSTST STSTSTSTST STPLQTPTSL VSLSNISLST
     ISIPIQPNTS SILLDSSMND SFNKESSGSN KVANPTIRKR DIILMSNLEG IWNDIPTRLY
     PYLLTLAKKF NIAYQIDTLY DPTSWGFVYP SPISNQQQQQ QQQSSTQHQH QHHHHQQQQQ
     TSINLNRLSI SGSPSLRSIS IRNGGNINTL NSSGSNNSSP LKFPNLALSP IRNGSNSNLT
     HHHGSNSSLN NLLSPLKNLQ LQQKYDKLKL LNEKVIFLPN ELPNEPPMSM DKMFLDVGEP
     RSLCRIFQFE KKIPSSFFPR LLSQLYMFCS IKHCWKNGVI LENCYLSFPV ARRFPMSPNA
     KNPFRRSSTI SVLEADDLVS IQVLGDTKIE ISSSKMCRHI LQIFESILES YNQLAYTIYI
     SCIHCIETLP KSEQYLFSLN QIEESVIKGK TYQSCPIHSS IPIKLNQLAP DLTMNDLRHK
     LIDFKEVELD PNPIGEGGTA TVYKGKWRQS DVAIKLLKTD VVGSDFSKVF AEYRREIFCL
     SSFIHDNILD LKGFCLEPLA IITEFQSGGN LYDYIHDLKN PLDWQLRIKI AKGIAASLQT
     LHDSRPSVVH RDLKSPNILL SSKDSLTMEC HLCDFSLSGF STTVANRSVQ NPVWLAPEVI
     NNELCSDKSD VYAYGVILFE LLSRTRFFSN ITFMSEVEGL ITEGVRPSLP SHNLPEYDSL
     LNICWAQDPT CRPSFIEITK KLEEIELILK THTPVEPVYT ETSKNQHIQL NRGNTIYTLV
     KRPITPIQQQ QQQKQQQLQQ QKQSPKQLQQ QKPLPTPPKQ LSNNDSTPTK PLDDSSDSSS
     EDSNN
 
 
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