ROCO4_DICDI
ID ROCO4_DICDI Reviewed; 1726 AA.
AC Q6XHB2; Q54J79;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Probable serine/threonine-protein kinase roco4;
DE EC=2.7.11.1;
DE AltName: Full=Ras of complex proteins and C-terminal of roc 4;
GN Name=roco4; ORFNames=DDB_G0288251;
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; AY232266; AAO83649.1; -; Genomic_DNA.
DR EMBL; AAFI02000109; EAL63307.1; -; Genomic_DNA.
DR RefSeq; XP_636808.1; XM_631716.1.
DR PDB; 4F0F; X-ray; 1.80 A; A=1019-1292.
DR PDB; 4F0G; X-ray; 2.00 A; A=1019-1292.
DR PDB; 4F1M; X-ray; 2.04 A; A=1019-1292.
DR PDB; 4F1O; X-ray; 2.30 A; A=1019-1292.
DR PDB; 4F1T; X-ray; 2.30 A; A=1019-1292.
DR PDB; 4YZM; X-ray; 3.00 A; A/B=1019-1292.
DR PDB; 4YZN; X-ray; 1.55 A; A=1019-1292.
DR PDBsum; 4F0F; -.
DR PDBsum; 4F0G; -.
DR PDBsum; 4F1M; -.
DR PDBsum; 4F1O; -.
DR PDBsum; 4F1T; -.
DR PDBsum; 4YZM; -.
DR PDBsum; 4YZN; -.
DR AlphaFoldDB; Q6XHB2; -.
DR SMR; Q6XHB2; -.
DR STRING; 44689.DDB0191509; -.
DR PaxDb; Q6XHB2; -.
DR PRIDE; Q6XHB2; -.
DR EnsemblProtists; EAL63307; EAL63307; DDB_G0288251.
DR GeneID; 8626525; -.
DR KEGG; ddi:DDB_G0288251; -.
DR dictyBase; DDB_G0288251; roco4.
DR eggNOG; KOG0192; Eukaryota.
DR HOGENOM; CLU_002809_0_0_1; -.
DR InParanoid; Q6XHB2; -.
DR OMA; KFQEFQR; -.
DR PhylomeDB; Q6XHB2; -.
DR PRO; PR:Q6XHB2; -.
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:0005739; C:mitochondrion; IEA:GOC.
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; IDA:dictyBase.
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:0004713; F:protein tyrosine kinase activity; IEA:InterPro.
DR GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; IMP:dictyBase.
DR GO; GO:0042331; P:phototaxis; IMP:dictyBase.
DR GO; GO:0000302; P:response to reactive oxygen species; IMP:dictyBase.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0031150; P:sorocarp stalk development; IMP:dictyBase.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 2.130.10.10; -; 2.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR032171; COR.
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; IPR020635; Tyr_kinase_cat_dom.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR Pfam; PF16095; COR; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00369; LRR_TYP; 2.
DR SMART; SM00219; TyrKc; 1.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF50978; SSF50978; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51450; LRR; 3.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS51424; ROC; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; GTP-binding; Kinase; Leucine-rich repeat;
KW Nucleotide-binding; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transferase; WD repeat.
FT CHAIN 1..1726
FT /note="Probable serine/threonine-protein kinase roco4"
FT /id="PRO_0000355209"
FT REPEAT 256..277
FT /note="LRR 1"
FT REPEAT 280..301
FT /note="LRR 2"
FT REPEAT 303..324
FT /note="LRR 3"
FT REPEAT 326..347
FT /note="LRR 4"
FT DOMAIN 364..544
FT /note="Roc"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00758"
FT DOMAIN 1026..1292
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REPEAT 1422..1461
FT /note="WD 1"
FT REPEAT 1463..1502
FT /note="WD 2"
FT REPEAT 1506..1546
FT /note="WD 3"
FT REPEAT 1589..1627
FT /note="WD 4"
FT REPEAT 1633..1670
FT /note="WD 5"
FT REPEAT 1674..1714
FT /note="WD 6"
FT REGION 800..890
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1319..1385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1154
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 377..384
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00758"
FT BINDING 428..432
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00758"
FT BINDING 487..490
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00758"
FT BINDING 1032..1040
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 1055
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT TURN 1023..1025
FT /evidence="ECO:0007829|PDB:4F0G"
FT STRAND 1026..1034
FT /evidence="ECO:0007829|PDB:4YZN"
FT STRAND 1036..1045
FT /evidence="ECO:0007829|PDB:4YZN"
FT TURN 1046..1048
FT /evidence="ECO:0007829|PDB:4YZN"
FT STRAND 1051..1056
FT /evidence="ECO:0007829|PDB:4YZN"
FT TURN 1061..1063
FT /evidence="ECO:0007829|PDB:4F0F"
FT HELIX 1067..1082
FT /evidence="ECO:0007829|PDB:4YZN"
FT STRAND 1093..1097
FT /evidence="ECO:0007829|PDB:4YZN"
FT TURN 1098..1101
FT /evidence="ECO:0007829|PDB:4YZN"
FT STRAND 1102..1105
FT /evidence="ECO:0007829|PDB:4YZN"
FT HELIX 1113..1117
FT /evidence="ECO:0007829|PDB:4YZN"
FT HELIX 1126..1144
FT /evidence="ECO:0007829|PDB:4YZN"
FT STRAND 1146..1148
FT /evidence="ECO:0007829|PDB:4YZN"
FT HELIX 1157..1159
FT /evidence="ECO:0007829|PDB:4YZN"
FT STRAND 1160..1163
FT /evidence="ECO:0007829|PDB:4YZN"
FT STRAND 1173..1175
FT /evidence="ECO:0007829|PDB:4YZN"
FT STRAND 1182..1185
FT /evidence="ECO:0007829|PDB:4F1T"
FT TURN 1195..1197
FT /evidence="ECO:0007829|PDB:4YZN"
FT HELIX 1200..1203
FT /evidence="ECO:0007829|PDB:4YZN"
FT STRAND 1204..1206
FT /evidence="ECO:0007829|PDB:4YZN"
FT HELIX 1207..1209
FT /evidence="ECO:0007829|PDB:4F0G"
FT HELIX 1213..1228
FT /evidence="ECO:0007829|PDB:4YZN"
FT TURN 1232..1235
FT /evidence="ECO:0007829|PDB:4YZN"
FT HELIX 1240..1249
FT /evidence="ECO:0007829|PDB:4YZN"
FT HELIX 1262..1271
FT /evidence="ECO:0007829|PDB:4YZN"
FT HELIX 1276..1278
FT /evidence="ECO:0007829|PDB:4YZN"
FT HELIX 1282..1290
FT /evidence="ECO:0007829|PDB:4YZN"
SQ SEQUENCE 1726 AA; 193282 MW; 4F757B2BF814FC4B CRC64;
MDSSQQLQES QQLQQQYTRV GIDVIGPMKD LIISVMNSLD TTFKIINETY RIVYFDTDET
KLTSSNLDSD DEEFESDDDA DEEADLQIQA SCNLYTFDGK NRQSVDEIKR IVQHLNETQS
QQNDNQAVPV IPTFFVVVNI GVGPSFVSEI KSAAGTTQFI EWIVNDQASK EVFKVSTNLL
SHHKKQIELT HACTVGDVNY LDQIILSGVS TDQLKEAHKA GHAIVFDSLL THNSNSLVVT
GTMALLGAIV ENGDRKGKRL SLSRSNLSRF PMSITQMCTH LVELDLSDNK ITELPKDIQL
LKSLRILILR GNLLEDIPLE ICYLGDLKIL ELQENPLNNF PLSVVQSGTK NLLLFCKNIL
ERKKSETWNK VKLMFVGQEG VGKTSLCQAL KGSKKKKAEL QVTGDTVSTE GVKIQNIKNK
KVEFHAWDFG GQQVFYPTHQ FFLTTHALYL VVFKLTDPNF AERVNYWVRQ VKSNSSGAVP
AIFLVGTHSD VCTPEQLQEA ESILKANFVK YSRVKENTIN FVCCATGKGI KELKKRLIHE
AEKSHLIKKD IPGNYMVLEA RLTNRGANPG RMAVSGSPIG GGSSAQLSSN AINSQKERYI
DYDDYMNECK LSHLQPEEIK GATDFLHNLG IILHFDTPTL KNLVVLDPQW LADVMSSLIT
FSHNWIKRGI LNHSELVAVW GGKYDQSLWP LLLKLLEKFE VSYELPNIAK SLIPSLLPED
AEGEISTIKD REWVTLPQAI ESGRCQVFGC DYNFDFMPLG FFARLLLRIL LISGVEVRTY
WRNGVLLDIL TPEQVKLQQS KQQQLQQQQQ QQNNNESNDS SVNNNNNNNN NNNNNNIINS
SSSSSLNLTQ TSTSTSPSKL SLNNSQINNS NSTLNSQQLI NPSVSPLSST TPRHQALITF
IKKKSFESKD KDSYKLNIEV RSFNTTIEKD HSASLFFQQI LFTIDTLLAS SYVGLEITRM
IPCIHCVQKN PRADPYYFDF SSCISALQDG KPHLFCRNDP SIPVRIDYIA PDLCLKKVPT
LADNEIEYEK QIGKGGFGLV HKGRLVKDKS VVAIKSLILG DSEGETEMIE KFQEFQREVF
IMSNLNHPNI VKLYGLMHNP PRMVMEFVPC GDLYHRLLDK AHPIKWSVKL RLMLDIALGI
EYMQNQNPPI VHRDLRSPNI FLQSLDENAP VCAKVADFGL SQQSVHSVSG LLGNFQWMAP
ETIGAEEESY TEKADTYSFA MILYTILTGE GPFDEYSYGK IKFINMIREE GLRPTIPEDC
PPRLRNVIEL CWSGDPKKRP HFSYIVKELS ELRNGNTTST TTNTSSTTNN LNSANVSIAS
TSSNADDGSQ TNNNNNNNNN NNNNNNNNSG SSIALSPSRS FEQQTTTTTT TTTSPSSPST
SFINSSGSYN TESYSVASSS TTNLLNTLNN ANQPVNFIGT ASVHKKMEVL AGVEAGETVW
TKSADSSLCF WSTKKGHLIN ELKCPHTVAT TMMIKVGKYI WEATNSNGIY IWDMGTMTIV
QQLTTPHKGD VCLHFVEYGD NNGVWSGGSE GTVCLWDMQT FEKKHSFSLE SAITAMSYFG
NNTLYIASGS HIVVFKTKTL LMNVNQNWKH STGSITSILA MKDEVWSGGS DGRIYIWKVK
NEFELQKVQS LEAHHEKITS LIHLEDNVLS GSTDKCISLF KISDPKKPFT TQEHHKQGVT
SIVKVQSHIV WAITSDTTTP LVLWNIPQKW EKKTANGILP RLKFFR
