FRAY1_DICDI
ID FRAY1_DICDI Reviewed; 574 AA.
AC Q54XL6;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Serine/threonine-protein kinase fray1 {ECO:0000250|UniProtKB:O61125, ECO:0000312|EMBL:EAL68033.1};
DE EC=2.7.11.1;
DE AltName: Full=STE20-like kinase fray1 {ECO:0000250|UniProtKB:O61125};
GN Name=fray1 {ECO:0000312|EMBL:EAL68033.1}; ORFNames=DDB_G0278863;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1] {ECO:0000312|EMBL:EAL68033.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4 {ECO:0000312|EMBL:EAL68033.1};
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] {ECO:0000305}
RP CLASSIFICATION.
RX PubMed=16842885; DOI=10.1016/j.ejcb.2006.05.013;
RA Arasada R., Son H., Ramalingam N., Eichinger L., Schleicher M., Rohlfs M.;
RT "Characterization of the Ste20-like kinase Krs1 of Dictyostelium
RT discoideum.";
RL Eur. J. Cell Biol. 85:1059-1068(2006).
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 Evidence={ECO:0000250|UniProtKB:O61125};
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; Evidence={ECO:0000250|UniProtKB:O61125};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:O61125};
CC -!- PTM: Undergoes autophosphorylation in the catalytic domain.
CC {ECO:0000250|UniProtKB:O61125}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily. {ECO:0000250|UniProtKB:O61125,
CC ECO:0000269|PubMed:16842885}.
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DR EMBL; AAFI02000024; EAL68033.1; -; Genomic_DNA.
DR RefSeq; XP_647787.1; XM_642695.1.
DR AlphaFoldDB; Q54XL6; -.
DR SMR; Q54XL6; -.
DR STRING; 44689.DDB0230012; -.
DR PaxDb; Q54XL6; -.
DR EnsemblProtists; EAL68033; EAL68033; DDB_G0278863.
DR GeneID; 8621746; -.
DR KEGG; ddi:DDB_G0278863; -.
DR dictyBase; DDB_G0278863; fray1.
DR eggNOG; KOG0582; Eukaryota.
DR HOGENOM; CLU_475244_0_0_1; -.
DR InParanoid; Q54XL6; -.
DR OMA; HHHFHFP; -.
DR PhylomeDB; Q54XL6; -.
DR Reactome; R-DDI-380972; Energy dependent regulation of mTOR by LKB1-AMPK.
DR PRO; PR:Q54XL6; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:1902554; C:serine/threonine protein kinase complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0043539; F:protein serine/threonine kinase activator activity; IBA:GO_Central.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0032147; P:activation of protein kinase activity; IBA:GO_Central.
DR GO; GO:0006611; P:protein export from nucleus; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Manganese; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..574
FT /note="Serine/threonine-protein kinase fray1"
FT /id="PRO_0000361650"
FT DOMAIN 97..357
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 24..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 381..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 461..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 532..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..39
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..445
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..509
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 221
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 103..111
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 126
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 256
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:O61125"
SQ SEQUENCE 574 AA; 64223 MW; 9D344378077A91C8 CRC64;
MEINNSNNNN NYVCAQHNRI EHANHHDLPD SDSDSSSREE ELMNSSGGGN GKEPIGEKKK
LPSHISEVIS NERRESIIRE LQQIKTISDY PSQANQYNLI EPIGEGTEGR VFKAYCIPLK
ENVAIKVVEL DKMDPQFVKD VIKEVKVMNG NNHPNLIHYH TSFLENNQLW LVMDYLGGGS
LADIMKFKYP DGIPEVLAVT VLKSLLKGLE YLHSHQRIHR DLKSDNILIG EDGAIELADF
GVSAMFEKNT CCSRKTIVGT PCWMAPEIIS ERGYNQGVDI WSFGITAIEL IRGKPPGYDL
PPSKVFMNLL FGNSPSLQEE EDKGVCSHLY KDLVDKCLQK EPSKRPNASK LLEHKVFKQA
KKNNYIVSHL LHGLTPCEDR YRESMSPASS NTPSPDSSRP SSPEHYNHGN VVNSPLQKNI
KPSSLNKSSS SLELKNKNLS NPDLVNMPRA ASHPVELNAL ELSSGSGPLS QSSDLPHGHL
HKIGTPKKKH SPSGSIGDSH GSISPPLSTS PEKERKKGFF NHFRRHSIAK LFGSPKEGDH
NHQHHKSEGD HEHHHFHFPW KHHHHSSSNN HVET
