ID K5XEF9_AGABU Unreviewed; 1931 AA.
AC K5XEF9;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=AGABI1DRAFT_105233 {ECO:0000313|EMBL:EKM81753.1};
OS Agaricus bisporus var. burnettii (strain JB137-S8 / ATCC MYA-4627 / FGSC
OS 10392) (White button mushroom).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Agaricaceae; Agaricus.
OX NCBI_TaxID=597362 {ECO:0000313|EMBL:EKM81753.1, ECO:0000313|Proteomes:UP000008493};
RN [1] {ECO:0000313|Proteomes:UP000008493}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JB137-S8 / ATCC MYA-4627 / FGSC 10392
RC {ECO:0000313|Proteomes:UP000008493};
RX PubMed=23045686; DOI=10.1073/pnas.1206847109;
RA Morin E., Kohler A., Baker A.R., Foulongne-Oriol M., Lombard V., Nagy L.G.,
RA Ohm R.A., Patyshakuliyeva A., Brun A., Aerts A.L., Bailey A.M.,
RA Billette C., Coutinho P.M., Deakin G., Doddapaneni H., Floudas D.,
RA Grimwood J., Hilden K., Kuees U., LaButti K.M., Lapidus A., Lindquist E.A.,
RA Lucas S.M., Murat C., Riley R.W., Salamov A.A., Schmutz J., Subramanian V.,
RA Woesten H.A.B., Xu J., Eastwood D.C., Foster G.D., Sonnenberg A.S.,
RA Cullen D., de Vries R.P., Lundell T., Hibbett D.S., Henrissat B.,
RA Burton K.S., Kerrigan R.W., Challen M.P., Grigoriev I.V., Martin F.;
RT "Genome sequence of the button mushroom Agaricus bisporus reveals
RT mechanisms governing adaptation to a humic-rich ecological niche.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:17501-17506(2012).
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:0000256|ARBA:ARBA00001433};
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:0000256|ARBA:ARBA00000775};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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; JH971387; EKM81753.1; -; Genomic_DNA.
DR RefSeq; XP_007327595.1; XM_007327533.1.
DR STRING; 597362.K5XEF9; -.
DR GeneID; 18822114; -.
DR KEGG; abp:AGABI1DRAFT105233; -.
DR eggNOG; KOG0198; Eukaryota.
DR HOGENOM; CLU_001658_1_0_1; -.
DR InParanoid; K5XEF9; -.
DR OMA; FPRRPTH; -.
DR OrthoDB; 1362351at2759; -.
DR Proteomes; UP000008493; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR CDD; cd00029; C1; 1.
DR CDD; cd00014; CH_SF; 1.
DR CDD; cd06627; STKc_Cdc7_like; 1.
DR Gene3D; 3.30.60.20; -; 1.
DR Gene3D; 1.10.418.10; Calponin-like domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR001715; CH_dom.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR003096; SM22_calponin.
DR PANTHER; PTHR48016; MAP KINASE KINASE KINASE SSK2-RELATED-RELATED; 1.
DR PANTHER; PTHR48016:SF4; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00307; CH; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR00888; SM22CALPONIN.
DR SMART; SM00109; C1; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50021; CH; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000008493};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 453..564
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 1277..1530
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1618..1665
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 86..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 139..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 452..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 576..682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 720..757
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 863..966
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 987..1214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1567..1616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1752..1931
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..313
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..335
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..470
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 602..618
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 883..966
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1051..1068
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1090..1118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1119..1140
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1154..1171
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1752..1784
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1813..1859
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1873..1912
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1306
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1931 AA; 209079 MW; 67F30E3D359C3DAD CRC64;
MPPHQRTTPQ IPSLPASPPL VLDGSSRTFT RLSSLKQTIR TATRSKKSPA SEADDPAATI
TLKGKGKEVV TVEDVPKERD RMNVFGKLGT TFRRARKESS SQLSQGNSAD HNDRAATRTT
YTAPSLRGAS LSSPALHLSS QALPSPKSQP SVLASSSSGA AALVSPTRDR SKRVSLQPHS
PETGSPVSRR ERQTRNPSTR HRATKSNPPD PAPTLKNPPR GSSRHPDSQS TRPSMDTDSL
PETPSPSPPA HRGRLVFAPP AARSESSTPR TARPISPLRA RSPTHPRVLT PTTRGLTSSS
TSHLPSSSPP HRRSSVDAPR RSSIDSSRRP SVDSPRRNSG EISRLSSRGS PVDRRVESPT
PVRPRPISPQ QRSYAQNRHY NFSSASLISP SYNAEHRERI RKAASMLCKE MIRPPSFISR
SDQAKRDWEA VEIRMQPLAR LERVWGMSSI SSSNNLNSST SGISSNGSSG VGEERERRAF
CEAVRDGFVL CQLMNKLRGG NAVRPDPRED GFIKSSNVTR FLAGCASYGL GSEDLFQRDD
LIEGTGESLA RVAHTIITLI QFVETPAPSR IKWIKGASQR SKGASPTSSA VPGPYMRGSI
GRAASSTPNL SPQSVSPRKR YSPPAGLPPL RSDSSEEALV STSPLRPVHK SKDYRAGVNV
LGSDSEMTTP GDLTDREGGR ESVDNMEGEE VVVKSTPVAF VLKPPPKSPL RARTIRNRQE
RNDQEISEWA RKAAVPSSSP TASRMRYEPG SPTALRHDLG LSRTDSVVAE STRASVGSSS
FLGSPVGFGQ SNESSYARQS VASTAMTDTT ITTQVSSILD HSPRVGRSSD NNKFGTIRTM
TTDLTSESPS IGRAEGADIV EESTDGNGKM DLMSLLTPPT PPPKGHRERR GSNTHGHAVD
LTRVAEEPDE SGLLSCRGKG KEKMRQRDPK GKTLIEESST KGQKQREGKG GKGGGGEESE
KAADRIHAVH LHKAKWPDDF LEAFQMRNPI SRSPSPLNSD PLPPTHSYPT PVSRSVSPPS
KLAIVDGGRR LSDSSEVACL APRRPTHLSR HSLDTPGSGS SSSLLPKEAS QLRRDVSPDG
VRGASGSGSR LVVRRTSTNK SLLSQTRTSN NLSRYSPDVE GSESREKSPD GIRKERRGSS
GIKPVPVPFP RGEHSNTPSP SPRTESVIKA TRDASNLGAA ESAKSSEATA QEKRPRPPRG
RFQSEINGSS RVKLRPNSYD ELGARPVRSR IESMVNLGRA DAALASASDL MVRDSADGSA
VRKTLVVKEE GKPPTHFQLG NCIGKGQFGS VYRALNLTTG QMVAVKRLRL EGLKEDEIST
LMREVDLLKS LSHPGIVKYE GMTRDDDTLN IILEYAENGS LAHTLKAFGK LNEKLVASYV
VKILEGLHYL HQSDVVHCDL KAANILTTKN GNVKLSDFGV SLNLRAVERQ TQNDVAGTPN
WMAPEVIELK GASTKSDIWS LGCTVIELLT GRPPYGEISN SMTVMFRIVE DEMPIPPGCS
ELLQDFLEQC FNKNPVMRPN AELLCEHPWL KNNWVALKDL RPQDSIPFLR RVSADLQKSD
MTRYFAGLPE SPTTTEFPRD VAGSPSPVPP ASPVGKRTSN ASIRPAPPVR DTEYHPSDHN
FVKTTFSKPV VCRVCLENVK KSAVLCAECS LIAHSKCAPN APPTCDLRSQ LLLYAHYAEQ
GNPAGLYSNP LFDHPEIPCG PTAMSDIPYV AHNTPRTSFD TQHVHHSTSP IPSSPPTAFK
FMAAFKRSRS SLTNEAASTS GTQAPDADNL DSRTAVPSTS VNKSGELHFE ERPQLPRKNH
AVLHKRSRER PRSYTSTSTG LSSLRSATTA AESLNSSTAE TGRNVRVSGA GTTSSHDRTS
SSGHKMEQAR SRKTISIKTQ APSGATSDVE TNDFAELSTA SSVLPGSLSL DTNRRTRSKH
ESKQSGNCIV Q
//
