ID K9FMX4_PEND2 Unreviewed; 645 AA.
AC K9FMX4;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=cyclin-dependent kinase {ECO:0000256|ARBA:ARBA00012425};
DE EC=2.7.11.22 {ECO:0000256|ARBA:ARBA00012425};
GN ORFNames=PDIG_53980 {ECO:0000313|EMBL:EKV10910.1};
OS Penicillium digitatum (strain PHI26 / CECT 20796) (Green mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1170229 {ECO:0000313|EMBL:EKV10910.1, ECO:0000313|Proteomes:UP000009882};
RN [1] {ECO:0000313|Proteomes:UP000009882}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHI26 / CECT 20796 {ECO:0000313|Proteomes:UP000009882};
RX PubMed=23171342; DOI=10.1186/1471-2164-13-646;
RA Marcet-Houben M., Ballester A.-R., de la Fuente B., Harries E.,
RA Marcos J.F., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome sequence of the necrotrophic fungus Penicillium digitatum, the main
RT postharvest pathogen of citrus.";
RL BMC Genomics 13:646-646(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=2.7.11.22;
CC Evidence={ECO:0000256|ARBA:ARBA00000584};
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=2.7.11.22; Evidence={ECO:0000256|ARBA:ARBA00000875};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. CDC2/CDKX subfamily.
CC {ECO:0000256|ARBA:ARBA00006485}.
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:EKV10910.1}.
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DR EMBL; AKCT01000216; EKV10910.1; -; Genomic_DNA.
DR AlphaFoldDB; K9FMX4; -.
DR STRING; 1170229.K9FMX4; -.
DR eggNOG; KOG0600; Eukaryota.
DR HOGENOM; CLU_000288_17_4_1; -.
DR InParanoid; K9FMX4; -.
DR OMA; TIHRKME; -.
DR OrthoDB; 22668at2759; -.
DR Proteomes; UP000009882; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd07840; STKc_CDK9_like; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24056; CELL DIVISION PROTEIN KINASE; 1.
DR PANTHER; PTHR24056:SF546; CYCLIN-DEPENDENT KINASE 9; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EKV10910.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000009882};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 287..572
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 67..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 157..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 606..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..248
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..639
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 316
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 645 AA; 74725 MW; 2C6A3953097DC517 CRC64;
METLNTQHQQ AHTTVRPNRL HLTLEDEGDG LGRLRILELV IPLLADMMTI HRKMEIIFMP
KVNLASHNDP QSPRAGESDH YARPSSRDEG VNQAQAQPDG GNPQSMPPPT HESNETTPAN
KGGKFSFAFK SKAAPSPAPK PVPDLAQRMQ QVRELVPRVP EPPQQPRNRF TNGPLPKFKP
DLRADRRDRD RGRNRDRDRR DFREPREFRD PRDRRDDRRF DQRRDRRQGE RLPDKPSDWQ
DRRRGPSPQP PREALPPKQK RVLTRLKPRP TLPEEFANAE SVYYRKPGNE SVIGAGTYGK
VFKGIHVYTQ RKVALKKIRM EGEKDGFPVT AVREIKLLQH LRNHNVVSLL EVMVEKNECF
MVFEYLSHDL TGLINHPTFS LTLPHKKDLA KQMFEGLNYL HHRGVLHRDI KAANILISNR
GLLKFADFGL ARFFSKSRQL DYTNRVITIW YRPPELLLGE TRYGPAVDVW SAACVCMEMF
TKKAVFPGEG GELSQMDKIY NALGTPTKTE WPDLVEMPWF HLMRPTERRK RVFEDVYRDV
LTTGAMDLIS SIFRYDPSQR PSAEDVLKHP YFVSEEPAPH PPIELEHVEG DWHEFESKAL
RKEARRVEYQ NQKDRDKRKA DASVPSSDRD FKRTKQDSSD RVSAQ
//
