KINX_DICDI
ID KINX_DICDI Reviewed; 1094 AA.
AC Q23915; Q54QZ4;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Probable serine/threonine-protein kinase kinX;
DE EC=2.7.11.1;
GN Name=kinX; ORFNames=DDB_G0283391;
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].
RC STRAIN=AX3;
RX PubMed=7857991; DOI=10.1016/0167-4889(94)00241-6;
RA Wetterauer B.W., Hamker U., von Haeseler A., MacWilliams H.K., Simon M.-N.,
RA Veron M.;
RT "A protein kinase from Dictyostelium discoideum with an unusual acidic
RT repeat domain.";
RL Biochim. Biophys. Acta 1265:97-101(1995).
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. {ECO:0000305}.
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DR EMBL; Z37981; CAA86053.1; -; Genomic_DNA.
DR EMBL; AAFI02000055; EAL65680.1; -; Genomic_DNA.
DR PIR; S52076; S49313.
DR RefSeq; XP_639097.1; XM_634005.1.
DR AlphaFoldDB; Q23915; -.
DR SMR; Q23915; -.
DR STRING; 44689.DDB0191487; -.
DR PaxDb; Q23915; -.
DR PRIDE; Q23915; -.
DR EnsemblProtists; EAL65680; EAL65680; DDB_G0283391.
DR GeneID; 8624121; -.
DR KEGG; ddi:DDB_G0283391; -.
DR dictyBase; DDB_G0283391; kinX.
DR eggNOG; ENOG502RYA2; Eukaryota.
DR HOGENOM; CLU_284199_0_0_1; -.
DR InParanoid; Q23915; -.
DR OMA; DNWMAPE; -.
DR PRO; PR:Q23915; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1094
FT /note="Probable serine/threonine-protein kinase kinX"
FT /id="PRO_0000327648"
FT DOMAIN 22..281
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 301..884
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 676..978
FT /note="40 X 9 AA approximate repeats of V-K-V-E-E-P-V-E-E"
FT REGION 946..1083
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..328
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..345
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..384
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..425
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..454
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..524
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 527..552
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..584
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 587..607
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 608..639
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 640..659
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 673..796
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 797..812
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 813..884
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 946..969
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 979..1060
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 146
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 28..36
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 49
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CONFLICT 581
FT /note="Q -> H (in Ref. 1; CAA86053)"
FT /evidence="ECO:0000305"
FT CONFLICT 653
FT /note="E -> D (in Ref. 1; CAA86053)"
FT /evidence="ECO:0000305"
FT CONFLICT 1031
FT /note="I -> L (in Ref. 1; CAA86053)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1094 AA; 126718 MW; B109D1B8E8778E0A CRC64;
MGSVDTSVPS FDRAWSIKYE DLDFISEIGS GGFGKVFKGE YLGAPVAIKK IHILPDDPNR
VDLEKFLNRE IETIKLFTHP NVIQFVGISE NNGILFIVTE LIEGGDLQYY LKNQSIDLPW
FLRANIALDV SLAMSYLHSK SIVHRDLKST NLLVDKNWKI KVCDFGFARI VEEDNNKSMT
ICGTDNWMSP EMITGLDYDE RSDIFSFGIV LLEIISRVKP APYMRDASFG LAEDIVRNQL
IPTDCPESLI DLTFNCCSVD PNNRPSFKEI SQTLKQIKTT LDSNIVYPEI RDFEQQQKIS
TTNGNNKQNG GAPKINNLPL QYSNNNNNIY DDDDDDDDDD DDNDSFPRPY SDNSNSNVTL
ESNSNYNSST INGQEQQEQQ EQQQQQQVKE ERDEGEIEQD DDNIEVYDSD YQKKLEEHQK
ELLERQNQNQ EGSTDENEVY EQEEEEEEED EEEQVISTPA KKRISFGQDT FHTYEAYRTD
DEDDDDDEED EEEGDEYDHG YDDFDEDDED DEEYDEDEDD EDERQIQYYQ QQLQYQQQLQ
KQQEQEYQRQ QQLQLQREEE EYQRQLQQQQ QQQQQQQQQQ QQHQQQYDDD DDDDDEEEEE
YDDVIRHDTD SEEESKDKTP LPWDQHFEKQ KESENKVEQE ETNVVVANSQ ETEQQQQQQQ
QPKEEEEEEP TKVEDVKVET EEQTKEEHDV KVDEESTKVD EPVDEPTKVE ESVEQVKAEE
PNKVEELVEE VKVEEEPTNV EEVKAEEPVE EVKVEEPVEE VKAEEPVEEV KAEEPVEEVK
TEEPVEEVKV EEPVEEVKVE EPVEEVEAEE SVQEPVEEVK VDEPTKVEEP TKVEEPIEEV
KVEEPTKVEE SIEEVKVEEP TKVEEPVEEI KPEEPTKVEE SVEDVKVEDV KVEEVKAEEP
TKAEESVEDV KVEEPIKVEE PVKVEEPVKV EEPVKVEEPI KVEEPIKVEE PIKVEEPIKV
EEPIKVEEPV KVEVASPVVQ EQPPQQEEKP EVVSTSTITI ASSPQQSSNS PPSTPVKQPQ
QQEIEVNSTP IKQQQQQQQT PTQQTQTPTK QHTEINVQPT PTKTPPLPPQ TNEKIPLISP
NNKSNRGCCS CFIQ
