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 27-MAR-2024, entry version 115.
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 (Social amoeba).
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 SMR; Q6XHA7; -.
DR STRING; 44689.Q6XHA7; -.
DR PaxDb; 44689-DDB0191512; -.
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; FPFHFEF; -.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd00159; RhoGAP; 1.
DR CDD; cd13999; STKc_MAP3K-like; 1.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 4.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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 PANTHER; PTHR48051; -; 1.
DR PANTHER; PTHR48051:SF1; ZGC:77287; 1.
DR Pfam; PF06602; Myotub-related; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00364; LRR_BAC; 7.
DR SMART; SM00365; LRR_SD22; 5.
DR SMART; SM00369; LRR_TYP; 11.
DR SMART; SM00324; RhoGAP; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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
//
