ROCO8_DICDI
ID ROCO8_DICDI Reviewed; 1867 AA.
AC Q54M77; Q6XHA8;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Probable serine/threonine-protein kinase roco8;
DE EC=2.7.11.1;
DE AltName: Full=Ras of complex proteins and C-terminal of roc 8;
GN Name=roco8; ORFNames=DDB_G0286127;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 102-1867.
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).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AAFI02000085; EAL64356.1; -; Genomic_DNA.
DR EMBL; AY232270; AAO83653.1; -; Genomic_DNA.
DR RefSeq; XP_637871.1; XM_632779.1.
DR AlphaFoldDB; Q54M77; -.
DR SMR; Q54M77; -.
DR STRING; 44689.DDB0191480; -.
DR PaxDb; Q54M77; -.
DR PRIDE; Q54M77; -.
DR EnsemblProtists; EAL64356; EAL64356; DDB_G0286127.
DR GeneID; 8625468; -.
DR KEGG; ddi:DDB_G0286127; -.
DR dictyBase; DDB_G0286127; roco8.
DR eggNOG; KOG0192; Eukaryota.
DR HOGENOM; CLU_236521_0_0_1; -.
DR InParanoid; Q54M77; -.
DR OMA; MEPIVYW; -.
DR PhylomeDB; Q54M77; -.
DR PRO; PR:Q54M77; -.
DR Proteomes; UP000002195; Chromosome 4.
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: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:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR Gene3D; 1.10.10.10; -; 3.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR032171; COR.
DR InterPro; IPR000591; DEP_dom.
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; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF16095; COR; 1.
DR Pfam; PF00610; DEP; 2.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00049; DEP; 2.
DR SMART; SM00369; LRR_TYP; 4.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF46785; SSF46785; 2.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50186; DEP; 2.
DR PROSITE; PS51450; LRR; 7.
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; Kinase; Leucine-rich repeat; Nucleotide-binding;
KW Reference proteome; Repeat; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1867
FT /note="Probable serine/threonine-protein kinase roco8"
FT /id="PRO_0000358894"
FT DOMAIN 16..93
FT /note="DEP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00066"
FT DOMAIN 264..342
FT /note="DEP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00066"
FT REPEAT 491..512
FT /note="LRR 1"
FT REPEAT 515..536
FT /note="LRR 2"
FT REPEAT 540..561
FT /note="LRR 3"
FT REPEAT 563..584
FT /note="LRR 4"
FT REPEAT 586..607
FT /note="LRR 5"
FT REPEAT 609..631
FT /note="LRR 6"
FT REPEAT 633..656
FT /note="LRR 7"
FT REPEAT 657..678
FT /note="LRR 8"
FT DOMAIN 693..941
FT /note="Roc"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00758"
FT DOMAIN 1456..1864
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 96..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 121..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 763..813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 942..961
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1163..1207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1509..1546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 763..808
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1721
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 1462..1470
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 1483
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 1867 AA; 209114 MW; CB9DDB71563D31E8 CRC64;
MFDYNQLNKL KDKIQSSDGL QIKDRTYLYK TYRSVFVGYE CVDWIFGNCP DIKTREDAIK
LGQTLFDAGI ICNVTSGADP IFKDDYIFYQ FDNNKNNNNI NNNNNNATST ATTATAPITP
VSTKIGSIGK SSSKSSTAVD KMNNNNNNNN NNNNNNNNNN NNNSNNSNSN NNSSRRTSSV
PPPVLVTASL SSSTSSSSSS TTSTSSSLAS TNTNSNSTYN SNSFNKKHHR YSINELSKVV
LEDLNTVTLV KDELIQLSQE LMNGDKGLKL QKKKKGAAGT TISCFSGSQL IDWLVKKLEV
TRKESIQIAS ALMHLNIFIE VGTIFNSSNN NNNNNNGGGG VMSSTLSTTI PSSISLQQLS
NQSQSNSNSS SSSSILNLSF TAPISISSTT ATMSSSLSLS TTAATTTTTT TSSSLLNNSS
SGSGFLVPTL PASVLNSSSN SNNQLYSSSP LSLSTSSIPA FDNRIVEDCG NVFYEFLTKP
EAIINHVAMR RLDDLCLTHK CISIIPTTII NTSKFLRIID LSFNQLSESN QLESIATLYN
LESCNLSHNQ LSTLPSSFSR LELLTKLILS HNCFQVIPNV VFQLSNLEEL SLAANQLSSI
SESIGSLKSL EKLDLSFNKQ INKIPKELGL LVRLKSLNVL GSNKINELPS FLSTLPLLEQ
LDFSRDIIKS PPKEITSKGF THIIGYLKDL FEGTETLSHI KLMVLGSEKT GRSSLVKALT
KSQTKSLSRQ SANFLKKVTS SEVSLNDPIE IIQLKLDLPP EQQNGIMTSS SNLNLSTGTL
PPPTQLSSST SELKPQRKDS FGSSMTTPEK KRPTKRNVKL MIYDFRMPSI DVYYHTHQFF
LSERAFYLVT YDINKDLSHS GLEFWVESIK KKAPNAPIYI VATHIDTFNQ YGGDILVPLN
EIDQYLTQRS LEVTGVIGVS STTLRNIDLL KNEIIQTLLN QSNNNNNNNN NNNYNNNKQS
NSISTTNWLN ERIPSIYITL ETNLQEEAKK RPIVTWDEYQ NIAKLSNFTT SSYEKLVRAT
NTLNRWGSII WFEDSKSSLK DFVILDPQWF SDCFYKLLLA KHSFINSDGI LLLSNLKNIW
KPNIVPEQFH IKLLKLLERY QILYTLKNNS NLQQLQQQQQ QQKSFGNLSK ENSLNSMSYS
IESRSSSSPL PTVVTLSAEI SSSPSLSLSN SSQSVFTNPN NNNNNKSEQQ QQQQQQQQQP
QPISTSPKLL RNSLKNLKSI ENNSSSLSNN SILNSNSNSS GNLLQNGSYI SFNRIIIPCL
LPNGKPSHLA SLWDTWSGED EHQIGRYYQF RNISAKNCFE RVMVRFLYMM EPIVYWSTGI
LFRKTQTYRE NIKDSMSSCG TLVEFDTVTQ QLQIRVRGHE FDACAKLFQI VLENVDTILK
DYQINQSQTY IPCSCSCECR DLPHLFPIDL IEETFGKGES HTKCPITMKL VSLCKISPDI
TLSSVSSNKK VSKEDLIYQE EIGVGGFSRV YKGIYKNNTV AIKQFNFERM DLIDSTSFNN
LNSLTISPSN SSLSISLSSS TSSLSPPIVN NNNNNNNLNN NLNNLNNNNK LYIQQQQQTQ
QNQQQQQQQQ QQQQQQQQQQ QQQQQQQQQQ QQQQQQQNQQ QPKILQRNLS TSSLSSNSSQ
GEDSMNQISS GKLNAINEFR REVWLMSGLS HSNIVLMKGF CFEPYAIVME YMDIGSLSSF
LKKKKEDGQV LDWQMLLKIV TDIASGMAFL HNITPPLVHR DLKSPNILLA SHPTNPNEIS
AKVSDFGLSR SIVQNFSSKV VDNPTWQSPE VLKGMEYNEK SDIYSFGMIL WECYHLELPF
DEFDFKFMST LEDNILSGLR PSINQNCNRM YSSLITKCWN ADPNLRPSFN SILKTLNEIK
DSTINSK
