ID A0A0L1JDA7_ASPNO Unreviewed; 796 AA.
AC A0A0L1JDA7;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Carbon catabolite derepressing protein kinase {ECO:0000313|EMBL:KNG89398.1};
GN ORFNames=ANOM_001868 {ECO:0000313|EMBL:KNG89398.1};
OS Aspergillus nomiae NRRL 13137.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1509407 {ECO:0000313|EMBL:KNG89398.1, ECO:0000313|Proteomes:UP000037505};
RN [1] {ECO:0000313|EMBL:KNG89398.1, ECO:0000313|Proteomes:UP000037505}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 13137 {ECO:0000313|EMBL:KNG89398.1,
RC ECO:0000313|Proteomes:UP000037505};
RA Moore M.G., Shannon B.M., Brian M.M.;
RT "The Genome of the Aflatoxigenic Filamentous Fungus Aspergillus nomius.";
RL Submitted (JUN-2014) 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 -!- 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:KNG89398.1}.
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DR EMBL; JNOM01000032; KNG89398.1; -; Genomic_DNA.
DR RefSeq; XP_015410321.1; XM_015547125.1.
DR AlphaFoldDB; A0A0L1JDA7; -.
DR STRING; 1509407.A0A0L1JDA7; -.
DR GeneID; 26803672; -.
DR OrthoDB; 5475340at2759; -.
DR Proteomes; UP000037505; 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; 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 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:KNG89398.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000037505};
KW Transferase {ECO:0000313|EMBL:KNG89398.1}.
FT DOMAIN 71..322
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 412..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 501..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 613..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 687..713
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..480
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 501..538
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 554..576
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 615..630
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 100
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 796 AA; 89290 MW; EB49ECCB149A28C0 CRC64;
MAAAFDDEDL SVPLPSYDRD RRRERASGAT PPNSNFAGMT MPPPSRPIGR GGDPSMQSPA
TTRDMQRLDQ YQTVKVLGEG SFGKVKLAIH QPSGRQVALK IISRRKLLSR DMVGRVEREI
QYLQLLRHPH IIKLYTVIAT KTDIVMVLEY AERELFDYLV KRGRCNDAEA RKFFQQIICA
VEYCHRHKIV HRDLKPENLL IDSEKNVKIA DFGLSNIMTD GNFLKTSCGS PNYAAPEVIS
GKLYAGPEVD VWSCGVILYV LLVGRLPFDD DYIPALFKKI AAGNFHMPPY ISSGAARLIR
SMLQVHPVHR LTIPEIRQDP WFQKDLPKYL QPPPEEFIAT GVDPNKAIDP RKIAPGKPIS
VQHKIHQVAI AKLERNMGYG REDIEDALKN PEPSAIKDAF FIIVENEMMQ TNSPTDENLM
SSAPPPPSGR TPASPATTGR PAAAPSQGAP AGPPTRTRSG SQRQSFQLHQ PSDSDNLETS
RISHVRILPT SLPYVHDQLM EQREREQRAR AADRLAEEQA RSGSDASEDP HRSGLDGRSL
AEQEATAKAL KPHSRSIVDL DKLRLEPPEA RNAPHQPRKT RKWQFGIRSR NQPYEQCFIS
IKLLQRREDD GKFFQPSTQI GSQSADEPTP LQSKYPDLPP DYYIPKDPWF IRARLLKEGV
KAPGLSGSVH SSRSDISELR RKFNLAGGPS SVDEKSHSPN EHLSASGPSS ASQHLSIPRV
AYGVWVFVDI QLYQLEENNY MVDFKCDGYQ NVIRAESDTE WHPISKRFRN KEKEITSPYP
FLDVASDLVA QLAVAS
//
