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Database: UniProt
Entry: R7YYC6_CONA1
LinkDB: R7YYC6_CONA1
Original site: R7YYC6_CONA1 
ID   R7YYC6_CONA1            Unreviewed;       858 AA.
AC   R7YYC6;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 59.
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=W97_05882 {ECO:0000313|EMBL:EON66636.1};
OS   Coniosporium apollinis (strain CBS 100218) (Rock-inhabiting black yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetes incertae sedis; Coniosporium.
OX   NCBI_TaxID=1168221 {ECO:0000313|EMBL:EON66636.1, ECO:0000313|Proteomes:UP000016924};
RN   [1] {ECO:0000313|Proteomes:UP000016924}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 100218 {ECO:0000313|Proteomes:UP000016924};
RG   The Broad Institute Genome Sequencing Platform;
RA   Cuomo C., Gorbushina A., Noack S., Walker B., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA   Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C., Montmayeur A.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA   Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The genome sequence of Coniosporium apollinis CBS 100218.";
RL   Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
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   -!- 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; JH767581; EON66636.1; -; Genomic_DNA.
DR   RefSeq; XP_007781953.1; XM_007783763.1.
DR   AlphaFoldDB; R7YYC6; -.
DR   STRING; 1168221.R7YYC6; -.
DR   GeneID; 19903193; -.
DR   eggNOG; KOG0578; Eukaryota.
DR   HOGENOM; CLU_000288_26_2_1; -.
DR   OMA; KDSQHAN; -.
DR   OrthoDB; 460351at2759; -.
DR   Proteomes; UP000016924; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0019236; P:response to pheromone; IEA:UniProtKB-KW.
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; 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; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EON66636.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Pheromone response {ECO:0000256|ARBA:ARBA00022507};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016924};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          73..183
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          188..201
FT                   /note="CRIB"
FT                   /evidence="ECO:0000259|PROSITE:PS50108"
FT   DOMAIN          568..837
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          256..549
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        27..54
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        265..281
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        299..332
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        334..371
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        417..431
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        457..498
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        518..545
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   858 AA;  94387 MW;  BE651FD97F0653F1 CRC64;
     MTTSVYTPNQ FMNPGPAPRP PTDRPRFNLT PSASSLPGSM SGLSLQSPSS TGSQTSLLVN
     RSMTEKVGGG AYSVVKDGHA KVKEEGLFKG LVWSDRYLVL REFQLDFFKS NNTAKVSYSI
     QLRDITSITR SEVYSYSFEI TRTMSSGSGA SPPRDGPTKV LICKVDTDDE VYSWIDSIYQ
     RCPSMGGVSN PTNFTHRVHV GFDPTTGAFV GLPSEWEKLL TASAITKDDY AKNPKAVLEV
     LEFYTEKLVK RAEDPAAYPS LTPTPSIEPA MNKQLGYSNS GHSIAPPRPA PPNGFRREDS
     YNTPRSGTST PTTRTASERN VADRSQAQAQ AEAQAEERWR RKEEEQRQQR EREQQQREQE
     RREREEQDAY NASLPKTRTP LAKQEVGGGG YFDEPKDASA RYNAARPAPS APGGFKDRQQ
     SPGSQRQLNA QRAAPLPPAG QNGASAGARA PATKAPSAVQ RQPSSSSTQR YAPGQASQLS
     TQASNGVNGQ TSVQARQPAP THVKPLNVAT KQPTGAPSAN DERKKAEQAL TKKEEAPRKD
     VRMSSMSESE VMARLREVVS KDKPLDSYNK QKKIGQGASG SVYVARVRES APSPTARTLL
     RENGPRAQVA IKQMDLRNQP RKELIVNEII VMKDSKHPNI VNFLDAFLQE EQFELWVVME
     FMEGGALTDV IDNNTSISED QIATICLETC KGLEHLHSQN IIHRDIKSDN VLLDGRGNVK
     ITDFGFCAKL TEQRSKRATM VGTPYWMAPE VVKQKEYGSK VDIWSLGIMA IEMIESEPPY
     LNEEPLKALY LIATNGTPRL KKPDKLSKDL KAFLSVCLCV DVKSRASATE LMGHEFLKGG
     CSLASLAQLL AFRKSGAH
//
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