ID A0A5C3QL36_9AGAR Unreviewed; 741 AA.
AC A0A5C3QL36;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 18-JUN-2025, entry version 22.
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=BDV98DRAFT_567667 {ECO:0000313|EMBL:TFL01181.1};
OS Pterulicium gracile.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Pleurotineae; Pterulaceae; Pterula.
OX NCBI_TaxID=1884261 {ECO:0000313|EMBL:TFL01181.1, ECO:0000313|Proteomes:UP000305067};
RN [1] {ECO:0000313|EMBL:TFL01181.1, ECO:0000313|Proteomes:UP000305067}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 309.79 {ECO:0000313|EMBL:TFL01181.1,
RC ECO:0000313|Proteomes:UP000305067};
RX PubMed=30886374; DOI=.1038/s41559-019-0834-1;
RA Varga T., Krizsan K., Foldi C., Dima B., Sanchez-Garcia M.,
RA Sanchez-Ramirez S., Szollosi G.J., Szarkandi J.G., Papp V., Albert L.,
RA Andreopoulos W., Angelini C., Antonin V., Barry K.W., Bougher N.L.,
RA Buchanan P., Buyck B., Bense V., Catcheside P., Chovatia M., Cooper J.,
RA Damon W., Desjardin D., Finy P., Geml J., Haridas S., Hughes K., Justo A.,
RA Karasinski D., Kautmanova I., Kiss B., Kocsube S., Kotiranta H.,
RA LaButti K.M., Lechner B.E., Liimatainen K., Lipzen A., Lukacs Z.,
RA Mihaltcheva S., Morgado L.N., Niskanen T., Noordeloos M.E., Ohm R.A.,
RA Ortiz-Santana B., Ovrebo C., Racz N., Riley R., Savchenko A., Shiryaev A.,
RA Soop K., Spirin V., Szebenyi C., Tomsovsky M., Tulloss R.E., Uehling J.,
RA Grigoriev I.V., Vagvolgyi C., Papp T., Martin F.M., Miettinen O.,
RA Hibbett D.S., Nagy L.G.;
RT "Megaphylogeny resolves global patterns of mushroom evolution.";
RL Nat. Ecol. Evol. 3:668-678(2019).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP +
CC H(+); 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:ARBA00048679};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] +
CC ADP + H(+); Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00047899};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. SNF1 subfamily. {ECO:0000256|ARBA:ARBA00006234}.
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DR EMBL; ML178825; TFL01181.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5C3QL36; -.
DR STRING; 1884261.A0A5C3QL36; -.
DR OrthoDB; 193931at2759; -.
DR Proteomes; UP000305067; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:TreeGrafter.
DR FunFam; 3.30.200.20:FF:000042; Aurora kinase A; 1.
DR FunFam; 1.10.510.10:FF:000571; Maternal embryonic leucine zipper kinase; 1.
DR Gene3D; 3.30.310.80; Kinase associated domain 1, KA1; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR032270; AMPK_C.
DR InterPro; IPR028375; KA1/Ssp2_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR013896; SNF1_UBA.
DR PANTHER; PTHR24346; MAP/MICROTUBULE AFFINITY-REGULATING KINASE; 1.
DR PANTHER; PTHR24346:SF110; NON-SPECIFIC SERINE_THREONINE PROTEIN KINASE; 1.
DR Pfam; PF16579; AdenylateSensor; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF08587; UBA_2; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF103243; KA1-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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 Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:TFL01181.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000305067};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:TFL01181.1}.
FT DOMAIN 19..270
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 427..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 492..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..462
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..507
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 741 AA; 81850 MW; 57638875D09C40F5 CRC64;
MPADGHGGHV YSVNKLGEYK IIKNIAEGTF AVVKLARHTV TGHLVAMKFL SKALILHHKN
KKRVQKEIEF IRALRHPHII KLYEVISTPT DIIIVLEYAP GELFKYIQDN GRMPEHKARR
LFQQLISGIE YSHKKNIIHR DLKPENVLLD NDLNVKIADF GLSNEITDGD FMKTSCGSPN
YAAPEVISAA LYTGPEIDVW SAGVILYVAL CGCLPFEDEN LDSLFRKICQ GHYHMPQHLS
GSARSLIASM LIVDPVKRIT IEQITTHPFY TTSLPVYLTP LPPPVGPVIG QLSSLVAPPK
KIVDFDIVGG IGKVEEGIID DLAGRLVGIS KDDIRAALRR PDGNQGNRVK VAYLLLRDKG
RMAMGRTLEE FEEEERENKL AAMDPRNALS PGPLIAIPGE MAEPNPFEAE LERQYIAETK
ATTLDEAIFS TGPVSPPPPR LAEELGTPYD GTGEEEGQEN EENGSVSGHF QVLDSSLPTQ
RPERHHLASY VIGKQQSSSA AGGSSSSRHG KHHRHVSGPD GLPRSKWHFG IRSRSPPMEV
MLEIYKTLKT LGMEWKEKKD LGGLGGVEAA ALRNRDRYNR HNWGPSSDPR DTSATHQHYA
NHNHNRVAII ARNTEGDGQG YVNLKAAAAI YFVETRTRVQ DVVVLMNIQL YNVDSVNYLV
DFHHKKSYRA STRKGAEKWD MAEPHEVENV LVAGSPAGSL AGKIGYEGKE DEVVSPFVFM
DVACRLILEL AGGGQGPAQQ A
//
