ROCO6_DICDI
ID ROCO6_DICDI Reviewed; 2147 AA.
AC Q54WS5; Q6XHB0;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Probable serine/threonine-protein kinase roco6;
DE EC=2.7.11.1;
DE AltName: Full=Ras of complex proteins and C-terminal of roc 6;
GN Name=roco6; ORFNames=DDB_G0279417;
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
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; AY232268; AAO83651.1; -; Genomic_DNA.
DR EMBL; AAFI02000031; EAL67647.1; -; Genomic_DNA.
DR RefSeq; XP_641642.1; XM_636550.1.
DR AlphaFoldDB; Q54WS5; -.
DR SMR; Q54WS5; -.
DR STRING; 44689.DDB0214834; -.
DR PaxDb; Q54WS5; -.
DR PRIDE; Q54WS5; -.
DR EnsemblProtists; EAL67647; EAL67647; DDB_G0279417.
DR GeneID; 8622048; -.
DR KEGG; ddi:DDB_G0279417; -.
DR dictyBase; DDB_G0279417; roco6.
DR eggNOG; KOG0192; Eukaryota.
DR HOGENOM; CLU_231803_0_0_1; -.
DR InParanoid; Q54WS5; -.
DR OMA; YRVKLMI; -.
DR PhylomeDB; Q54WS5; -.
DR PRO; PR:Q54WS5; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:dictyBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 2.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR032171; COR.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR025875; Leu-rich_rpt_4.
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; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR020859; ROC_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR Pfam; PF16095; COR; 1.
DR Pfam; PF12799; LRR_4; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00369; LRR_TYP; 7.
DR SMART; SM00233; PH; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF50998; SSF50998; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51450; LRR; 9.
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.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
PE 3: Inferred from homology;
KW ATP-binding; GTP-binding; Kinase; Leucine-rich repeat; Membrane;
KW Nucleotide-binding; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transferase; Transmembrane;
KW Transmembrane helix; WD repeat.
FT CHAIN 1..2147
FT /note="Probable serine/threonine-protein kinase roco6"
FT /id="PRO_0000358892"
FT TOPO_DOM 1..1055
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1056..1076
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1077..2147
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 69..89
FT /note="LRR 1"
FT REPEAT 101..122
FT /note="LRR 2"
FT REPEAT 124..145
FT /note="LRR 3"
FT REPEAT 148..169
FT /note="LRR 4"
FT REPEAT 171..192
FT /note="LRR 5"
FT REPEAT 193..214
FT /note="LRR 6"
FT REPEAT 215..236
FT /note="LRR 7"
FT REPEAT 237..256
FT /note="LRR 8"
FT REPEAT 306..328
FT /note="LRR 9"
FT REPEAT 329..350
FT /note="LRR 10"
FT REPEAT 352..372
FT /note="LRR 11"
FT DOMAIN 390..750
FT /note="Roc"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00758"
FT REPEAT 1051..1098
FT /note="WD 1"
FT REPEAT 1237..1263
FT /note="LRR 12"
FT REPEAT 1274..1297
FT /note="LRR 13"
FT REPEAT 1325..1348
FT /note="LRR 14"
FT DOMAIN 1356..1627
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REPEAT 1735..1774
FT /note="WD 2"
FT REPEAT 1778..1820
FT /note="WD 3"
FT DOMAIN 1821..1923
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REPEAT 2031..2068
FT /note="WD 4"
FT REGION 390..750
FT /note="Small GTPase-like"
FT REGION 491..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 602..621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 905..995
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1653..1699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 905..986
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1481
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 403..410
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00758"
FT BINDING 634..638
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00758"
FT BINDING 691..694
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00758"
FT BINDING 1362..1370
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 1383
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CONFLICT 2..17
FT /note="NSIHKQHYTINSNHYN -> ISFLNHLYPINRNLYK (in Ref. 1;
FT AAO83651)"
FT /evidence="ECO:0000305"
FT CONFLICT 28
FT /note="N -> K (in Ref. 1; AAO83651)"
FT /evidence="ECO:0000305"
FT CONFLICT 39..57
FT /note="TNNKSNNNSNNNNNETLED -> PIIKGIIISIINNIEPLKN (in Ref.
FT 1; AAO83651)"
FT /evidence="ECO:0000305"
FT CONFLICT 797..798
FT /note="DE -> NQ (in Ref. 1; AAO83651)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2147 AA; 239183 MW; D472CAAF5002514A CRC64;
MNSIHKQHYT INSNHYNESI NINSLLLNDL NDEKRTTSTN NKSNNNSNNN NNETLEDIIE
FNNNNCNGDM KYLDLSKRMI YSLELMMIPE IENRFQGDFK SISILNLNDN LLGEIPESLK
QLTQLISLSI RGNHILEIPL WFPEEFKLLR KLDVSHNAIS SVPNTFNKFS ILEDLNLSNN
YISYIHPSLF PEGIMRLNLS NNLFREVELP PWFESLLTLD ISGNKLKHLG NLPFHLVRVS
IDDNHLESID HKVILRNKDL ALKFNQSFSD IVLERIYQCW YTGDPVLDLS GLGMCVVPPI
LGMLVHLTHL DLSGNCISVL PPELANLTEL VRLDLSFNIL TTLPLYIVSY KRLEHLDLQG
TLDTLVSPPR RIAETGKLID IQRYFHDLFQ GEPSYRVKLM IVGQENVGKT SLVKCLKMKK
KFSKNSDHLG TNVSTDGIDI DEIKFNLDIE LPSNPSSNSL ISNSLSNSSI SSNNINSNNN
INVHSNGGGI NSNGVNSNSQ ININSSSGNI HSNGGGVGNV NSSGGIHSNN SSGGGGGSNS
FLNNTNSNGT NNNSSNLNIN TNSNNVNSSG GGNNYHPPVG TNTSMSNIQV IGSSGSNLGS
GSNLSIGGSN GNNNNNSGGS GTMVNQRVTM SIWDCAGQEL YYTSHQMFLT DSALYVVVWN
LCKPEVNSRV EFWLHSIRSK AENAPILLIG THLDDYLATH SESELDEILE NIYSKYFRKF
RLKGISILSC STGVGFDNFL DLLKKTVVEL PSLKQSLPEL YLKLEKLIIK KRSTLVPPVL
TWQSFSQMVL SNLDFHDEIH VKVATKALVP LGSISFFDEP GLDQYVFLDP QWLTGVFSSI
ITTKHKFIKD GVLKKSDLYQ IWKPPHFIED EGLHSLLINL LERFELMFPL DSDLVSLSSS
NGNNGNSYVN NNNNNNNNSN NNNNGSNKSS PFKTTPSSPS TLRLVDSKSK GSHSSNPILS
GNNSSSKNST STKRSISGSP LRSRSNSDLD LIGGGGGSPI NGSSIDYSSK SNTLTPGLFN
ELNQKFIIPS QLPEIRPSFG LLWPSLDHSR VEFNRWIQLS FAPAGLFSRL LIRLLISKEF
DMKPILYWRN GVVVESQSGK SFLSTSTALI EMVPSYANCS STIKISVRGD RRTGRGLSAK
LLRLIVEIAD TLCTSWYHLE TNQVIPCPHC INKPNCTLFS LSDCEAVASS GVWYLLCGDR
KINFETFVPD VAMSDFWGSG SKKFNYDQIK MHKEKRILSI KPASFGNNQI QFEVRVPPSP
PPPPVQQIIN NGADDNITTT TLAVNNIKVL ESGGSQPPSP RSGKDVTHEL PIINRLEIIQ
PTSDESSLIQ VEFDHNNQTL VISGTYKYGD LLEIEFESPK LIGRGASGKI YRANLNDTMV
AVKQLEVVGE DAPRIFSEFR REIHVMSDLK HSNVVNLLGF TLSPFTMVME YIDCGDLHKF
LHSPIGDQLN GNWALILKLA LDIAKGMEFL HSVTPPLLHR DLKSPNVLLS MKDGVYTAKV
GDFGLSSRMF IQALKHKLRN FPVGNITWVA PEILREEEYT VKSDVYAFGL ILHELLTRKH
PYREFNYSMV SLQEDAIKNG LRPTISPSYT QTVTGHEYCG LIQDCWDSDI DRRPTFNKIV
KRIKQIIGRD VNNILMVNGV SVVSGIQSPN SLADSQPFHY HQQQQPSLNS TNQLQQQQYS
SVLTSPRSNL SDSSNSSQNI ANKSLNNISA TSLGDLGGND ENLGGQLQYS MRVPQPEAKV
NQLVWEVNSR RVWGGCESGE IIVWNAENGN QIFREQKLHP GPIRSLALVN QEDIWSAGGI
GPQQSTIRIW NAWRFNLDDQ SGTKSDFITK KGRGGSTFGR KSWRLRWFVL SRFDKTLKYY
SKQTDKEPSC SLILEGAWLE EISPPGYKVS LHLIHPEKRT MEMEFKSESE KSSWLTAINR
VINQNIPLYE IALGKQMTSG SENDYITNLL SVGPNVWVSL KETPSILVYN VKSKELVTKI
SLNDDQSSDQ WGKTGAVNMM LVNNFVWITG GSKLTQIDSQ SYQLLEVHGN HYSKPITSMA
LVEKNVWISC EDESLSVWDG DTGSFIRKVG SPIGSPTKPT VYTKLLYFSG YVWACTQGSI
HIYCIHSLTC KKKVESKNHP NSIVDLIKVF QQTVWSCCGT NNVCIWS
