ID A0A061H0N2_9BASI Unreviewed; 1223 AA.
AC A0A061H0N2;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN ORFNames=PFL1_06790 {ECO:0000313|EMBL:EPQ25653.1};
OS Pseudozyma flocculosa PF-1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Pseudozyma.
OX NCBI_TaxID=1277687 {ECO:0000313|EMBL:EPQ25653.1, ECO:0000313|Proteomes:UP000053664};
RN [1] {ECO:0000313|EMBL:EPQ25653.1, ECO:0000313|Proteomes:UP000053664}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PF-1 {ECO:0000313|EMBL:EPQ25653.1,
RC ECO:0000313|Proteomes:UP000053664};
RX PubMed=23800965; DOI=10.1105/tpc.113.113969;
RA Lefebvre F., Joly D.L., Labbe C., Teichmann B., Linning R., Belzile F.,
RA Bakkeren G., Belanger R.R.;
RT "The transition from a phytopathogenic smut ancestor to an anamorphic
RT biocontrol agent deciphered by comparative whole-genome analysis.";
RL Plant Cell 25:1946-1959(2013).
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DR EMBL; KE361653; EPQ25653.1; -; Genomic_DNA.
DR RefSeq; XP_007882527.1; XM_007884336.1.
DR AlphaFoldDB; A0A061H0N2; -.
DR GeneID; 19320861; -.
DR KEGG; pfp:PFL1_06790; -.
DR eggNOG; KOG0032; Eukaryota.
DR HOGENOM; CLU_005063_0_0_1; -.
DR OrthoDB; 5491340at2759; -.
DR Proteomes; UP000053664; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR CDD; cd05117; STKc_CAMK; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR013094; AB_hydrolase_3.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR002168; Lipase_GDXG_HIS_AS.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24347:SF412; CALCIUM_CALMODULIN DEPENDENT PROTEIN KINASE I; 1.
DR PANTHER; PTHR24347; SERINE/THREONINE-PROTEIN KINASE; 1.
DR Pfam; PF07859; Abhydrolase_3; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS01173; LIPASE_GDXG_HIS; 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}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000053664}.
FT DOMAIN 34..290
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 381..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 433..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 916..1026
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1077..1223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..402
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..464
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 916..942
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 962..976
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1113..1133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 68
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1223 AA; 131327 MW; 660E3D89C7194E26 CRC64;
MVGQHLHHAF RSWFHETESD GTPLLPVPLS KKYKVLPDVL GQGSFAVVKK VIEKTTGEER
ALKIIAKKPL KDNNENMLRE EIAILGRVEH PNIIKMWDLY ETKEGVFIVT DLCRGGELFE
RLVEKVHYNE LDARHIVRQI VEGVDYLHGH DIIHRDLKPE NILLRDKSEP SSIAISDFGL
SRFIPDEGLL MTACGSPQYV SPEVLLGKGY GPAVDLWSTG VIAYALLAGY TPFYGDDQPS
LFQQILKMQV EFEPEYWGDV SETAKDFVLH CLCPADRRMT AKQALAHPWL ADLPPLHEEA
SRGCCLKDRA LRNLSATRRL RKAVTAVEAV NHLNRLHSLR QQHGTSMPEG QRTLLSIVTN
IQQQQLNGAS LETVQLDKDA TTPAGQENLP DAPNGNGNGS AEAQNDKKRK QRDSAMALDL
VVMSVFLPQN WGSAASGKPS GSSGSTTGGA GGSSGSTSGR AGTANVADAV QRTMGGQQEE
DEHGADDQDE GKPTAAAGQQ GGDKQTSGGA GVTLNTLLNQ YKSAEVPASA RLDPAVKTRE
PAKITLSNAW KYVPFLVNQG ISIGSALASH AIYGPPKKSW GVEMSVFTRV LRDVANYSEF
ASIAGLQQFF DLGAFLPTPK DGLITPVTFR VKRRNLRGFL AEADAAEDGK REISGEWVVG
KQTWRRLQAE WRNGKQKGKE RVILYIHGGA YFVMSAATHR PLTISLSKYT ECRVFGINYR
LAPDTRFPGA LHDCVASFFR LTDDLGIPAS NIVLGADSAG GGLALATMMY LRDNGYDLPS
GAMLFSPWVD LTMSCDSWET NSEFDYLPMP ISGDHMNPVS AYLGDNIDKY LTHPYASPLF
GDLHGLPPLL IQCGDAEVLR DEVTLLAHKA SLSGVAVRHE LYEDCVHVFQ AFLFLDASRK
ALQSARHFVR TALDKRGRKK AAEVSEGARR GLDREMRQNM EDTKGAKVGA STAGPPAPAA
DGDKDGKGKA ARPTGKDEDA TATTASADGG LDEIMNRPAA AAADDDDDDE AAEGRVGNPT
DEEDWELDRR ASGEFASAAV ADAAQKAAAG SLQAAQKAFG HDDDFATRAT SAGRDAVAKA
ATGGGDDDEV ADESDVATPM ARASPKQGHA RLASEGSATS SGGGSSSSSF PAITIEEARL
RGQAAMQQQL STHAPALSKF HAPQKPLTPR MRRSQSGREL SGLIKSFEES KGAGKALKTN
VWTPGGGYSE GDPAGGGGGG GGQ
//
