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Database: UniProt
Entry: A0A0C9ZSA4_9AGAM
LinkDB: A0A0C9ZSA4_9AGAM
Original site: A0A0C9ZSA4_9AGAM 
ID   A0A0C9ZSA4_9AGAM        Unreviewed;       862 AA.
AC   A0A0C9ZSA4;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 44.
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=PISMIDRAFT_353062 {ECO:0000313|EMBL:KIK25117.1};
OS   Pisolithus microcarpus 441.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Boletales; Sclerodermatineae; Pisolithaceae; Pisolithus.
OX   NCBI_TaxID=765257 {ECO:0000313|EMBL:KIK25117.1, ECO:0000313|Proteomes:UP000054018};
RN   [1] {ECO:0000313|EMBL:KIK25117.1, ECO:0000313|Proteomes:UP000054018}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=441 {ECO:0000313|EMBL:KIK25117.1,
RC   ECO:0000313|Proteomes:UP000054018};
RG   DOE Joint Genome Institute;
RA   Kuo A., Kohler A., Costa M.D., Nagy L.G., Floudas D., Copeland A.,
RA   Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A.,
RA   Lipzen A., Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA   Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA   Hua S.X.;
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000054018}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=441 {ECO:0000313|Proteomes:UP000054018};
RG   DOE Joint Genome Institute;
RG   Mycorrhizal Genomics Consortium;
RA   Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA   Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA   Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA   Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT   "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC       protein kinase family. STE20 subfamily.
CC       {ECO:0000256|ARBA:ARBA00008874}.
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DR   EMBL; KN833710; KIK25117.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C9ZSA4; -.
DR   STRING; 765257.A0A0C9ZSA4; -.
DR   HOGENOM; CLU_000288_26_2_1; -.
DR   OrthoDB; 460351at2759; -.
DR   Proteomes; UP000054018; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR   CDD; cd01093; CRIB_PAK_like; 1.
DR   CDD; cd13279; PH_Cla4_Ste20; 1.
DR   CDD; cd06614; STKc_PAK; 1.
DR   Gene3D; 3.90.810.10; CRIB domain; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR000095; CRIB_dom.
DR   InterPro; IPR036936; CRIB_dom_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR033923; PAK_BD.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR48015:SF6; SERINE/THREONINE-PROTEIN KINASE CLA4-RELATED; 1.
DR   PANTHER; PTHR48015; SERINE/THREONINE-PROTEIN KINASE TAO; 1.
DR   Pfam; PF00786; PBD; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00285; PBD; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50108; CRIB; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000054018};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          73..167
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          171..184
FT                   /note="CRIB"
FT                   /evidence="ECO:0000259|PROSITE:PS50108"
FT   DOMAIN          586..838
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          297..316
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          328..542
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        330..366
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        426..476
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         615
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   862 AA;  94661 MW;  A6FA4682CA10073D CRC64;
     MAFSQITATN LTPSRPAPQA PVRRTTDTTP PYNHTLQNSG YSAAFSSGSS YSPDYTGIGG
     SPLRSSDNAL NSNVIRYGMV SLKEEGFASF IFLRKWLVLR EETLSIHKTE SAPQQSVIPL
     KDITNIERVD LKPYCLLLET KEKRYHLSLK NDEELYGWQD DIYSRSPLMG VSNPTNFVHK
     VHVGFDPITG AFTGMPEQWS KLLTKSAITR EDYAKDPQAV LDVLEFYTDH QKRELEEMGM
     GMPPVSRSLS GNSAASTLGT LTPYAVDGPS APPRFNAGTG LGGSALAKLD ARPPAIKRQD
     SAPAEMSTAT APPQNGLSST ALAAARAAEL VNSSHTQHTS SLSTSQGGSA RPPIPAMLQS
     STPLQATRPA PPRPLLTATR PAPAAPKAVV PNHTPSSADL RARAQARNVP EQGAPKPSLD
     KAPSVDILAQ KEREQREQRK REEREREKEK EREREKERER ERERERERER QLKDQGDGQQ
     QRPALPIAKV APPGCKPAAH PAAGTTATTV GPLSVKPLQT TKKKDVPAPE VTVTSSEGED
     PAVAEAARKL NEKPKDKERR ISTMTEAQIM EKLRSVVAED DPKTLYSKIK KVGQGASGHV
     YVAKTLANGK KVAIKEMDLS HQPRKELIVN EILVMKESQH PNIVNFLDAY LVKNTELWVV
     MEYMEGGALT DVIENNTLEE DQISSISLET CKGLCHLHSQ SIIHRDIKSD NVLLDAQGRV
     KITDFGFCAK LTDQKSKRAT MVGTPYWMAP EVVKQKEYGA KVDIWSLGIM AIEMIENEPP
     YLDEEPLKAL YLIATNGTPT LKKPEALSKE LKSFLSVCLC VDVRSRANSS ELLNHDFLRK
     ACAPSGLASL LRFKTKQQAA SS
//
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