ID A0A1V6QGK1_9EURO Unreviewed; 892 AA.
AC A0A1V6QGK1;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=PENANT_c004G05313 {ECO:0000313|EMBL:OQD88338.1};
OS Penicillium antarcticum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=416450 {ECO:0000313|EMBL:OQD88338.1, ECO:0000313|Proteomes:UP000191672};
RN [1] {ECO:0000313|Proteomes:UP000191672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 31811 {ECO:0000313|Proteomes:UP000191672};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. MAP kinase kinase kinase subfamily.
CC {ECO:0000256|ARBA:ARBA00006529}.
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:OQD88338.1}.
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DR EMBL; MDYN01000004; OQD88338.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6QGK1; -.
DR STRING; 416450.A0A1V6QGK1; -.
DR OrthoDB; 145974at2759; -.
DR Proteomes; UP000191672; 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:0000165; P:MAPK cascade; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd09534; SAM_Ste11_fungal; 1.
DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 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; IPR029458; Ras-bd_By2.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR48016; MAP KINASE KINASE KINASE SSK2-RELATED-RELATED; 1.
DR PANTHER; PTHR48016:SF29; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 1A; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF14847; Ras_bdg_2; 1.
DR Pfam; PF00536; SAM_1; 1.
DR SMART; SM01304; Ras_bdg_2; 1.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000191672}.
FT DOMAIN 63..126
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 609..887
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 347..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 522..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..377
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..400
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 541..561
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 638
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 892 AA; 98318 MW; 28D11DB6ED771A0C CRC64;
MLAPKQYSAP LSVPSSQTPT AYHANPLQRP ATATRAQDGM GFASPTKSEL SEGQDDLASV
RAWDEKRVVA WLHSIKCGQY ESLFKANNFN GDNLLECDQK ILQEMGIKKV GDRVRIFVAI
KQLRAKSGTS SRQKNMDTLA ALEATALSNS SRYSHSRLPY RRTSQLADDY LNSKTLSQPA
SPPAGDSEKG PWRKDYLNHP SSGGSSSGRN PGTSNEGRIS HPRNPSLDGL TMGPLPPSSP
VIRVIYTGGQ TKVLDIRNCK TPDEVILCVL KKLQLPEHQY RNYCFYVLDG LDPDLSNCRK
LTEPELMEIC EGFNKSERGR LILRKIHAGE PDMDELRRAS QLAYDESQAT HHNALSNSNQ
RQKHKIQQLT GESWHNIKQP LSPLGPRHRP SNSSLEEQGP NGERNPVAKL RSFFGQRPPS
EMIIHELQSF FPSHDRENIE KTMRRSQRLS RAASRMSVVS NYSVASSMKD APPLPPLPPI
PPIPSIADAW LQGNGVAQAV RAPRPISVSK FNLPQTSYRD SIASSSLQPL QEESPIEPNR
KSYVSFESGS DEPPNTSRQS LFDESLSVAA TDGGSFNDRM SVIVAEDGEE EDDGLTDFLA
GNNFAPKNWM KGSLIGEGSF GSVFLALHAI TGELMAVKQV EIPSATKGTE FDQRKNLMVT
ALKHEIELLQ GMSHPNIVQY LGTVADDQYL NIFLEYVPGG SIATMLKQYN TFQEPLVKNF
VRQILAGLSY LHSRDIIHRD IKGANILVDN KGGVKISDFG ISKRVEASHL LGARASGGGG
GAGSHIHRTS LQGSVYWMAP EVVRQTAHTK KADIWSLGCL VVEMFIGAHP FPDCSQLQAI
FAIGSNKARP PAPDHVSQEA VEFLDMTFHL DYEQRPSADE LLKCEFLSAP IT
//
