ID A0A093V7D4_TALMA Unreviewed; 630 AA.
AC A0A093V7D4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Serine/threonine-protein kinase gad8 {ECO:0000313|EMBL:KFX48085.1};
GN ORFNames=GQ26_0131570 {ECO:0000313|EMBL:KFX48085.1};
OS Talaromyces marneffei PM1.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=1077442 {ECO:0000313|EMBL:KFX48085.1, ECO:0000313|Proteomes:UP000029285};
RN [1] {ECO:0000313|EMBL:KFX48085.1, ECO:0000313|Proteomes:UP000029285}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PM1 {ECO:0000313|EMBL:KFX48085.1,
RC ECO:0000313|Proteomes:UP000029285};
RX PubMed=25330172; DOI=10.1371/journal.pgen.1004662;
RA Yang E., Wang G., Cai J., Woo P.C., Lau S.K., Yuen K.-Y., Chow W.-N.,
RA Lin X.;
RT "Signature Gene Expression Reveals Novel Clues to the Molecular Mechanisms
RT of Dimorphic Transition in Penicillium marneffei.";
RL PLoS Genet. 10:e1004662-e1004662(2014).
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:KFX48085.1}.
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DR EMBL; JPOX01000013; KFX48085.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093V7D4; -.
DR eggNOG; KOG0598; Eukaryota.
DR HOGENOM; CLU_000288_120_1_1; -.
DR Proteomes; UP000029285; 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-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd11651; YPK1_N_like; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR PANTHER; PTHR24351:SF243; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 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};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KFX48085.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 287..544
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 545..616
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT REGION 14..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 98..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..33
FT /note="Polar 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 630 AA; 70252 MW; 6AA90B8A33670484 CRC64;
MSWKLTKKLK ETHLAPLANS FGRSSSTSTI KGEPAEETPV PSPRPSIASQ VSNGIADSEA
LVSPPVALVK PGILIVTLHE GQGFSLSPHY QQIINSHYQN PNAPIRPNSS SSHSVQTGSY
TQPARPQSTS SGINAAPTIH GRYLTKYLPY ALLDFDKNQV FVDAVSGTPE NPLWAGDNTA
FKFDVSRQTE LSIQIYLRNP AARPGVGRSE DIFLGATKTQ PRLQETTTYV ENPKLSKKDN
QKAAAEQEKN VGQLGAEWLD LQFGTGSIKI GLSFVENRVH SMKLEDFELL KVVGRGSFGK
VMQVRKKDTK RIYALKTLRK AHIISRSEVA HTLAERSVLA QINNPFIVPL KFSFQSPEKL
YLVLAFVNGG ELFHHLQREQ RFDINRARFY TAELLCALEC LHGFKVIYRD LKPENILLDY
TGHIALCDFG LCKLDMKDED RTNTFCGTPE YLAPELLLGN GYTKSVDFWT LGVLLYEMLT
GLPPFYDENT NEMYKKIVQE PLTFPSHDIV PAAARDLLTR LLDRDPQRRL GANGAAEIKA
HHFFSNIDWR KLLQRKYEPT FKPSVIDALD TENFDPEFTG EMPVDSVVEG NALSQTMQDQ
FAGWSYNRPV AGFGDAGGSV RDPSFASIPE
//