ROCO5_DICDI
ID ROCO5_DICDI Reviewed; 2800 AA.
AC Q1ZXD6; Q6XHB1;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Probable serine/threonine-protein kinase roco5;
DE EC=2.7.11.1;
DE AltName: Full=Ras of complex proteins and C-terminal of roc 5;
GN Name=roco5; ORFNames=DDB_G0294533;
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 -!- FUNCTION: May act as a serine/threonine-protein kinase and guanine-
CC nucleotide releasing factor. {ECO:0000250}.
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; AY232267; AAO83650.1; -; Genomic_DNA.
DR EMBL; AAFI02000111; EAS66840.1; -; Genomic_DNA.
DR RefSeq; XP_001134523.1; XM_001134523.1.
DR STRING; 44689.DDB0232931; -.
DR PaxDb; Q1ZXD6; -.
DR PRIDE; Q1ZXD6; -.
DR EnsemblProtists; EAS66840; EAS66840; DDB_G0294533.
DR GeneID; 8626589; -.
DR KEGG; ddi:DDB_G0294533; -.
DR dictyBase; DDB_G0294533; roco5.
DR eggNOG; KOG0192; Eukaryota.
DR eggNOG; KOG0619; Eukaryota.
DR HOGENOM; CLU_226859_0_0_1; -.
DR InParanoid; Q1ZXD6; -.
DR OMA; EREMNTP; -.
DR PRO; PR:Q1ZXD6; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:dictyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; 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:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0030587; P:sorocarp development; HMP:dictyBase.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 1.20.900.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 3.80.10.10; -; 3.
DR InterPro; IPR032171; COR.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
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; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
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; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR Pfam; PF16095; COR; 2.
DR Pfam; PF13516; LRR_6; 1.
DR Pfam; PF13855; LRR_8; 2.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00369; LRR_TYP; 7.
DR SMART; SM00233; PH; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF48065; SSF48065; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS51450; LRR; 11.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS51424; ROC; 1.
PE 3: Inferred from homology;
KW ATP-binding; GTP-binding; Guanine-nucleotide releasing factor; Kinase;
KW Leucine-rich repeat; Nucleotide-binding; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..2800
FT /note="Probable serine/threonine-protein kinase roco5"
FT /id="PRO_0000355210"
FT DOMAIN 227..508
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 540..649
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REPEAT 777..800
FT /note="LRR 1"
FT REPEAT 805..832
FT /note="LRR 2"
FT REPEAT 834..856
FT /note="LRR 3"
FT REPEAT 861..885
FT /note="LRR 4"
FT REPEAT 971..984
FT /note="LRR 5"
FT REPEAT 985..1007
FT /note="LRR 6"
FT REPEAT 1008..1031
FT /note="LRR 7"
FT REPEAT 1033..1056
FT /note="LRR 8"
FT REPEAT 1058..1077
FT /note="LRR 9"
FT REPEAT 1078..1101
FT /note="LRR 10"
FT REPEAT 1128..1151
FT /note="LRR 11"
FT REPEAT 1152..1174
FT /note="LRR 12"
FT REPEAT 1175..1197
FT /note="LRR 13"
FT REPEAT 1199..1222
FT /note="LRR 14"
FT DOMAIN 1244..1464
FT /note="Roc"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00758"
FT DOMAIN 2175..2440
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 123..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 417..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 926..946
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1605..1665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1688..1711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1886..2011
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2050..2070
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2452..2498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2544..2800
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..62
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..225
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 930..946
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1606..1665
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2570..2586
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2587..2603
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2610..2651
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2664..2682
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2690..2704
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2705..2726
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2727..2787
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 2300
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 1257..1264
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00758"
FT BINDING 1348..1352
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00758"
FT BINDING 1407..1410
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00758"
FT BINDING 2181..2189
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 2202
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CONFLICT 1885..1886
FT /note="MS -> SQ (in Ref. 1; AAO83650)"
FT /evidence="ECO:0000305"
FT CONFLICT 1890..1891
FT /note="HH -> QQ (in Ref. 1; AAO83650)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2800 AA; 307014 MW; 5054DE31502D9823 CRC64;
MEVIKKEKKD KEKKDKEEKK DKEKKDKSEK KEKKDKEKKE KEKKEKKEKE KEKEKDKEKD
GGLFSIVGGW VGNLTEPTPP PPPPPSSVSA QSTAEANAIL LNPTTQENHK KAMDFWVTNT
STTTTTTTTT SSNNIPSLVS VQNNNTSNNN INNNNKTSNT TGSNVSSSNN KETVKINVTS
LDSGGNNNAS GKDISNEHSP KNRKEKEKEK DKDNKEDSIN ESPVDENRRK LVEGFMKSLQ
GCSDAIKVIL DVFYQPLKKA DLLSQEELKA IFSLIESISS FQQTILIDFK KYISNWNSTT
QAQLHSTFLQ FVGYLKLYKV YGLQYNYSLS SLCLLMFDNQ RFESFINNAE SKLVNEHKYS
LAPLVPTSSS SSCVKPVSLS EILGSQYDQT TSQSTNNSSG SSFPAVTLRR TGHTFTGINS
ANSNNNNNNS GGGSSGINNS NSVTGKFTQE YTYSNLASLL ILPIHFLARF HQFFKSLIDS
IAVLNPDYKP YNNLYKQIVQ VVKDIVNESV NINKVISISK SIKSPTIGLF NSSDIVQNRK
FLKEGILIEQ FNNQRISYYT FLFSDIILFT EKIEDTSTIN NNTMMAYDGS FYLLKKLERI
VNIQVDDPEL GFEYRKGFQI KTKESSIFYM TSSEKEKSTW FQVLSQASLK SNQNQNQNQN
NLTNSYSSTV AGGRNSTIGL GGIDDFNNNN NGNNNGSNND DGPDEFEDAK DIALFCKMII
SGQRPKVELT SQMLKISDPK PLFAALASTH FVNQLIFIPL TMNDKYMQMT LGMMSLNKSI
THLTLSQNSI NDPCAVALGD MLRYNHSLIQ MDLSENTIAD KGLISLIDGI LSHPSITVVI
LTQNQITDTG AKHISKLLKF NQTLNALFLE DNNITQSMGA EIIDQWVSCH STVLSRITLP
SIPPEYSDRI KLKAISVTNR LDKKKKQLQV NQKSTTPSTS TSTTSSTIIN NNKGLLDLGS
CDYSEISLQL LNKLNMLSLD SRRISDLKEL YLDHNCISSI PVSILKELKN LQILDLSNNQ
LSSLPSEISE MKELKLLNVS HNNLSSLPIE LGTLCKLNHL DISFNFIETI NVNSLSQLVN
LKVLMMQRNY FNRLPIEIFT RLKSLESFSI AGSPCFHPIK QRIYEAIAIK ATKLDLSDCG
LSALPIEIGS ISSLIELDLT NNRIKDLPPQ IGKLSSLQTL NLSNNAIESL PWQLSQLTTL
KVLNITGNPI SFDGASNAKI SIPDVLSGDD LIGILKYLKL ASTKEKPCMR MKLMLVGQEN
VGKTSIAKCL KKEIIPVGKK LRQTIGLGTK KSKTPTLTEA NGSIDFNAPQ SINPLNTSLN
ISTDGINMDD WRPPSEDQSP PVTFSIWDFA GQEVYYSTHQ FFISSRSVFI VVFDMSVYNP
DETSRVPYWL QCIEAFGGNS PVILVGTHLD DLPNGVDVNQ ITQDIHSKYF TKFPNVKFFL
PVSCKSGKNI NKLQNHIVKL GKAEKKLGDL FSRSYFQLEN LILSEREMNT PPIITLSEFT
EMAISCGIPQ TSITAAADFL KELGVIVYFD DPKSGLDQFI FIDPPWLTRL MATIITSKPN
FVQSGVLDQS NLHQIWKPPD FPQHLHHVLL AILQKFEIVH PLPDPKATIS SSSSSPSTTQ
KSLNNSGSNL KSSGSAISTS SSSTTNGNKT LHRTNSTTNT TSLLNVSRFG NGSISKGSSL
SIIKKINDQS TSPSNSTTPS PNTSSNNFSD SITLVPKSST KHLVPILLSE ERPNSIEKLY
DQILLKSQQQ QPFLERIYQF EFLPIGFFSK LMIRTMHFTT VKEFWKNGLL VEKDDSQCLI
ESIQQFNQIN FKAWGKNPAS LLRFIIETAE VLISGWYKLH FHFLVPCNCI NCNSILISNI
GSINIINSTI NLSSNNNNNV NIVNMSQQQH HQQQQSPSTS TSSSSSLTSS QPSLSTPLTS
SQPSLSTSQP QLSTTTTTTA TTTTSSSSQS LASQQSSSQI QLTHSSSLSS MSGSISTNSL
NSNVSSSSST PSLLSPPLLN PDSTSSSNET SGDILDLDFA DYYDGESVSP GGTLKGKRKK
NPSKFLTLYR NTNKPKINGT TGSGSSSSIV TTAVSSSSSS SSSTSLSNTS SRQLDLSKIS
HLINQQLSFG PSKTQDLRTM FLYEEIERIF LSKKFEVVCR SSITGEETIV RLDSLVPELM
MSDIGPNFTL EYKDLEIIEK VGEGGFGIVY KGKLRGQLVA IKQITIDSGQ AEAASEIYRE
FRREVWLSNT LTHPSIVSLK GYCLDPCCIV MEYIPNGTLY SHLRKSFSSI TWQLKLKIAI
NIADAIKHMH GFTPKICHRD LKSPNILMLS DMNAAVVCKV SDFGETRAVV TSALGRDKLS
NPIWLSPEIM RGDEYTEKAD VYSFGIVLWE ILTGLLPFDE YPVAHSSFMY QLEDEITNGL
RPTIPQNSVC GHPDFITLIT DCWQNDPLKR PTFIDIHSRL LIMSGLNPAT ATTTNSAKST
ISTGFNSNSG ATTTTKPKSS TISSGSGTTS PPQPHPQLVR KLTQNFTPIA TSPTPSVIVS
SVPTTTTTTT TSVATTPTVQ TILAGGNITP KPSVPTAMKP NITPKPTLIS SQKPPAPNPV
PILKTPTPTN LSPTSISTPT TPTTPTTPTT PTTPTNSTSS NLKPTPTSKS NPSSPPQIAT
TATATQTPTP SPISVLKPPR SLPQKPVGTT QTTSTPPTNQ TPNPTIVTRP PLPSSLSSNS
INKPPSKPLP TPGGVTSPPP PPTTSSTTPI KFNSISAGNK TIGQSSTLPS STLKQFTANN
NTSPSGSSSL PNSTVSSPSS SFLLRPTGGT ISKKLPAIPK
