FRAY2_DICDI
ID FRAY2_DICDI Reviewed; 1028 AA.
AC Q551H4; Q869U1;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Serine/threonine-protein kinase fray2 {ECO:0000250|UniProtKB:O61125, ECO:0000312|EMBL:EAL69242.1};
DE EC=2.7.11.1;
DE AltName: Full=STE20-like kinase fray2 {ECO:0000250|UniProtKB:O61125};
GN Name=fray2 {ECO:0000312|EMBL:EAL69242.1}; ORFNames=DDB_G0229911;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1] {ECO:0000312|EMBL:EAL69242.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4 {ECO:0000312|EMBL:EAL69242.1};
RX PubMed=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [2] {ECO:0000312|EMBL:EAL69242.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4 {ECO:0000312|EMBL:EAL69242.1};
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 [3] {ECO:0000250|UniProtKB:O61125}
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; AAFI02000015; EAL69242.1; -; Genomic_DNA.
DR RefSeq; XP_643160.1; XM_638068.1.
DR AlphaFoldDB; Q551H4; -.
DR SMR; Q551H4; -.
DR STRING; 44689.DDB0229911; -.
DR PaxDb; Q551H4; -.
DR EnsemblProtists; EAL69242; EAL69242; DDB_G0276577.
DR GeneID; 8620567; -.
DR KEGG; ddi:DDB_G0276577; -.
DR dictyBase; DDB_G0276577; fray2.
DR eggNOG; KOG0582; Eukaryota.
DR HOGENOM; CLU_294823_0_0_1; -.
DR InParanoid; Q551H4; -.
DR OMA; HVSTDCR; -.
DR Reactome; R-DDI-380972; Energy dependent regulation of mTOR by LKB1-AMPK.
DR PRO; PR:Q551H4; -.
DR Proteomes; UP000002195; Chromosome 2.
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 InterPro; IPR017441; Protein_kinase_ATP_BS.
DR Pfam; PF00069; Pkinase; 1.
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.
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..1028
FT /note="Serine/threonine-protein kinase fray2"
FT /id="PRO_0000361651"
FT DOMAIN 71..330
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 368..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 486..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 580..914
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..700
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 701..853
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 854..868
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 869..897
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 195
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 77..85
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 100
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 230
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:O61125"
SQ SEQUENCE 1028 AA; 115488 MW; E38F2C8AD56063DF CRC64;
MSDDKYHHDK HHDKHHIDSK QSTAAALSSS STLASSSSMT TTTTTTSTTT TAASPITPKP
RKNYPNSADQ YELKETIGKG GSGLVQRAIC LPFQENVAIK IIDLEHCKNV SLEEIRKEIQ
AMSLCHHPNV VAYHTSFVYN ESLWVIMDFL SAGSCSDIMR FSFPQGFEEH VIATILKEAL
KAICYFHKTG RIHRDIKSGN ILIDSNGNIQ LSDFGVSATL IDTGETSRNT FVGTPCWMAP
EIMEQVNYDY AVDIWSFGIT ALELARGKAP FAEYPPMKVL LLTLQNPPPS LEGDGESKWS
HSFKDLVEKC LQKDPSKRPL PSKLLEHRFF KQAKKPDYLV QHILAKLPPL GQRYQMLSED
SFAMLRNTSS PQFDTGHSNS ADEWIFPNEN NDNNNSSTTT TTTTTTTTNP SNNNNNNNNK
TKENLTQSPF ETPSHTPSTS PGSTPSHSRT STPTSNHTAL GSSSTVVPPP VVPLTLPTAI
PVTAAAYHQQ QQHHHLSHSS GSIPNHNASS NLGASAHSNV HGLAHSSIHP TSSAASTTVV
NNTQQPQTLQ PPQQQHQLQQ PIKTPSPINA INIVKLNQSD LITPPKTSPK KEGSIPSSSS
HGNIPSLVTT SPKSPLQHQQ QIPQQQQDPA MINSNNSSIS SNGAYNRELI SASGSALSKP
PSPSSDKENN STSKSNKSKS RQSSRASSLS ESSDSTSHTS SSDEHSSRYE SDRKSYKKKK
SSSSSSNSKR DRERERDRDR SNKTYKNSRS RNVSRDRERE RDRHNRSRDR DRERERERDR
DRERDRDRSR DRSRDRSRDR ERDRSRDRSR DRDRSRDRSR DRSRERDRDR SRDRSRDRSR
SRDSDSRDRS RDRSRSHSNR RRSRSRDSRN KSRDRSSDSD RSRDRSRDRD YKSSKYKKSS
RGTSGRKNNK IQSKLDSQAT HISYLEDKIS TLTNWLQQQN LLNTSNGQVL SPTDPNLVSK
LQTQLDVLQS ENSYLRNENI NLKTIVNGSN STNNSLNQSS GMAFRNSVSS LHQLNMSNSS
NNSRPQTQ
