ID A0A1Y1U8K5_9TREE Unreviewed; 672 AA.
AC A0A1Y1U8K5;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=BD324DRAFT_635501 {ECO:0000313|EMBL:ORX34348.1};
OS Kockovaella imperatae.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cuniculitremaceae; Kockovaella.
OX NCBI_TaxID=4999 {ECO:0000313|EMBL:ORX34348.1, ECO:0000313|Proteomes:UP000193218};
RN [1] {ECO:0000313|EMBL:ORX34348.1, ECO:0000313|Proteomes:UP000193218}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-17943 {ECO:0000313|EMBL:ORX34348.1,
RC ECO:0000313|Proteomes:UP000193218};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Louie K.B., Bewick A.J., Labutti K.,
RA Haridas S., Kuo A., Salamov A., Ahrendt S.R., Lau R., Bowen B.P.,
RA Lipzen A., Sullivan W., Andreopoulos W.B., Clum A., Lindquist E., Daum C.,
RA Northen T.R., Ramamoorthy G., Schmitz R.J., Gryganskyi A., Culley D.,
RA Magnuson J., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Widespread Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (MAR-2017) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ORX34348.1}.
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DR EMBL; NBSH01000014; ORX34348.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1U8K5; -.
DR STRING; 4999.A0A1Y1U8K5; -.
DR InParanoid; A0A1Y1U8K5; -.
DR OrthoDB; 460351at2759; -.
DR Proteomes; UP000193218; 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-KW.
DR GO; GO:0016310; P:phosphorylation; 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; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR48015; SERINE/THREONINE-PROTEIN KINASE TAO; 1.
DR PANTHER; PTHR48015:SF6; SERINE_THREONINE-PROTEIN KINASE CLA4-RELATED; 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:0000313|EMBL:ORX34348.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000193218};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000313|EMBL:ORX34348.1}.
FT DOMAIN 75..170
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 174..187
FT /note="CRIB"
FT /evidence="ECO:0000259|PROSITE:PS50108"
FT DOMAIN 402..654
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 58..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 285..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..313
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 431
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 672 AA; 74306 MW; 5FD1DE4F878016FE CRC64;
MSYNDISSLT PSRPAPTPPL RSSNGQSSER YAQRPQIPVD KPASAFSSTA YSSSFPTLGG
SAALGPSPPK TRQNEVLRTG PTSMKEEGLR SFLWSKRWLV LDSQSLAVFK NEHSASPSSL
LPLADVVDVQ RVDLKPFCIE VEIKDKLVYL AFRTDEEVYA WMEDIYSRSP LMGVSQPTNF
VHQVHVGFDP ISGGFTGLPP QWSKLLTSSA ITKEDAARHP EAVLDVLQFY TQQQIGQESQ
VLSDQSSAAE LRSNLNETSA ASRFNGVGLG GQLQRSQADG KKILSGHESH DSVRAARNRD
VNGSSSSRTD QTARVVPHEV AKPLVAERKA PPPPRAAPTR DPKPGVVEPV AEASRVAGQP
DRVGENSSST TRQERRISTM NETQIMEKLR SVVSPTDPNQ RYSKIKKVGQ GASGMVFVAK
TLATGKKVAI KQMDLAQQPR KELIVNEIIV MKESQHPNVV NFLDAFLIRS SELWIILEYM
EGGALTDVIE NNKMEERQIS AICLETCRGL QHLHSRSIIH RDIKSDNILM NTQGEVKITD
FGFCAKLTDQ KSKRATMVGT PYWMAPEVVK QKDYGPKVDI WSLGIMAIEM IENEPPYLDE
EPLKALYLIA TNGTPTLKAP ETLSQDLKHF LSVCLCVDVS FRATSTELLK HDFLRMACTV
QELAPLLKFK QI
//
