ID A0A0B7FYP1_THACB Unreviewed; 757 AA.
AC A0A0B7FYP1;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Carbon catabolite-derepressing protein kinase {ECO:0000313|EMBL:CEL61979.1};
DE EC=2.7.11.1 {ECO:0000313|EMBL:CEL61979.1};
GN ORFNames=RSOLAG1IB_04730 {ECO:0000313|EMBL:CEL61979.1};
OS Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14) (Lettuce bottom
OS rot fungus) (Rhizoctonia solani).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Cantharellales; Ceratobasidiaceae; Rhizoctonia; Rhizoctonia solani AG-1.
OX NCBI_TaxID=1108050 {ECO:0000313|EMBL:CEL61979.1, ECO:0000313|Proteomes:UP000059188};
RN [1] {ECO:0000313|EMBL:CEL61979.1, ECO:0000313|Proteomes:UP000059188}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rhizoctonia solani AG1-IB 7/3/14 {ECO:0000313|EMBL:CEL61979.1};
RA Wibberg Daniel;
RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; LN679105; CEL61979.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B7FYP1; -.
DR STRING; 1108050.A0A0B7FYP1; -.
DR Proteomes; UP000059188; 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 GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd12122; AMPKA_C; 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; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24346; MAP/MICROTUBULE AFFINITY-REGULATING KINASE; 1.
DR PANTHER; PTHR24346:SF82; SERINE_THREONINE-PROTEIN KINASE MARK-A-RELATED; 1.
DR Pfam; PF16579; AdenylateSensor; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF103243; KA1-like; 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 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:CEL61979.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000059188};
KW Transferase {ECO:0000313|EMBL:CEL61979.1}.
FT DOMAIN 26..277
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 314..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 460..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 563..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 700..726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..503
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..547
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..598
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 701..726
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 55
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 757 AA; 83102 MW; 4AD087FBFB7772B1 CRC64;
MAPTAEPHAD VLAHIASLPP GNLGEYSIIK DIGEGTFGKV KLAVHTLTQA KVALKFISKE
RINALNMRTR VGREVSYLRL LRHPHVIKLY EIIVTLTDIV MVIEYAEGEL FNYIVENGRM
PESAARRFFQ QMMCAIDYSH RLKVVHRDLK PENVLLDGQN NVKIADFGLS NVMTDGDFLK
TSCGSPNYAA PEVIGGKLYA GPEIDVWSCG VILYVMLCGR LPFEDEHVPA LFRKITEGIY
HLPNYLSREA QELIRGMLAV DPVKRLTVPE ILAVPWVAVN MPHYLQPKRP VTPGMGTLHP
AYPHHPGIIG RGVGGSTNGS TFPSNGTTPA VSSSGSEHSS RNGGIVTPAS SVVTPVTERP
QVNTHMLGTL ASLVNGNSNG NGNGVIAGGG SDQGTPMASL SSLRHIKGLG KIEESIVLEL
AERCHVSVEE IKLALLRADD NAVKVAYMLA KDSARTGLCL DDDDEGDSPR GHPSQESEIF
WSPNYKPSQA PTPATPATPT TPVTPQPTNG LHPLSPQQAG MRPIADYDYD DDADEFDTDE
EDFDEEEWQN QNASHFAVLD TSLPPAHDTR TATNGTQPHH SYHRERGHRH RTHTNGQKSK
SPRWHFGIRS RSPPMEVMLE IYQTLKTLGM EWREKPGLNI VGRPEDEGCP GKDGKDIYYV
ETRCRIRDVV VRMDLQLYQV DPLNYLVDFR NLGCHHASTD PNAPSKFTDA SWPGNDSNSS
APRSPTLTEG AVLRADVCSP FLFLECACRL IVELAAG
//
