ID B8MA84_TALSN Unreviewed; 821 AA.
AC B8MA84;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE SubName: Full=Carbon catabolite derepressing protein kinase Snf1, putative {ECO:0000313|EMBL:EED18586.1};
GN ORFNames=TSTA_123150 {ECO:0000313|EMBL:EED18586.1};
OS Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS 1006) (Penicillium stipitatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441959 {ECO:0000313|EMBL:EED18586.1, ECO:0000313|Proteomes:UP000001745};
RN [1] {ECO:0000313|Proteomes:UP000001745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006
RC {ECO:0000313|Proteomes:UP000001745};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
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};
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DR EMBL; EQ962655; EED18586.1; -; Genomic_DNA.
DR RefSeq; XP_002482578.1; XM_002482533.1.
DR AlphaFoldDB; B8MA84; -.
DR STRING; 441959.B8MA84; -.
DR GeneID; 8108230; -.
DR VEuPathDB; FungiDB:TSTA_123150; -.
DR eggNOG; KOG0583; Eukaryota.
DR HOGENOM; CLU_000288_59_6_1; -.
DR InParanoid; B8MA84; -.
DR OMA; QNGRMKE; -.
DR OrthoDB; 5475340at2759; -.
DR PhylomeDB; B8MA84; -.
DR Proteomes; UP000001745; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd14079; STKc_AMPK_alpha; 1.
DR CDD; cd14334; UBA_SNF1_fungi; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR Gene3D; 3.30.310.80; Kinase associated domain 1, KA1; 2.
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 InterPro; IPR013896; SNF1_UBA.
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 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; 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:EED18586.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000001745};
KW Transferase {ECO:0000313|EMBL:EED18586.1}.
FT DOMAIN 80..331
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 422..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 517..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..450
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 472..488
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 526..540
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 109
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 821 AA; 91095 MW; 5CDA69CCC6F70D60 CRC64;
MAAAFDDEDL SVSLASIPPN PNNKKPRDQS NTDAIMSSSN PAAMAMPPPP RPNNNGGNRS
SSGSVQSPAT RRDMQRLDQY KTVKVLGEGS FGKVKLAIHQ PSGRQVALKI IPRRKLLSRD
MVGRVEREIQ YLQLLRHPHI IKLYTVIPTK SDIVMVLEYA ERELFDYLVK RGKCNDDEAR
KFFQQIICAV EYCHRHKIVH RDLKPENLLI DSEKNVKIAD FGLSNIMTDG NFLKTSCGSP
NYAAPEVISG KLYAGPEVDV WSCGVILYVL LVGRLPFDDD YIPALFKKIA AGNFHMPSYI
SPGAARLIRA MLQVHPVHRI SIAEIRQDPW FLDGLPKYLQ LPQEEFVTTG ADPNKAVDRR
KFAPGKSSSV QQKIHDFAIT KLEHSMGYKK EEIEDALRKA EPSAVKDAFF IIAENELMQT
NSPQEDSLDM SSPPAPSSPM HDSSGYSSPR APKSAAAALR QENALTPLTP QAREATPPPA
PPPTAPTTYG AMPIEEPRVS HVRILPTSLP YVHDQIMEQR DGTRRQKAQT SSSAGQGRAE
DRTLEQQAAT FRALKPHARS VIDLDKLRLE PPEKFHAAPM PSKRSRKWQF GIRSRNQPYE
AMFCLYKAIE AVGGVWEIIP AEPEGDAPLP KPDPNQPMPL QRKYPDLPSD YYIPKDPWFI
RARLLKEGVT APGVSLSAHS SRSDLGDLRR KVNLMNASIS AEDKAAIAAA VQASAENITN
NTGGGSGGGS TSIPSSLEQV QSLRISYGVW VFIDIQLYQL EATNYMVDFK CDGYQNVIRA
DLDGEWRPVS KRIRNKEKEV TSPYPYLDVA SDLVAQLAIA S
//
