ID A0A0D2HN91_9EURO Unreviewed; 918 AA.
AC A0A0D2HN91;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
GN ORFNames=Z520_01763 {ECO:0000313|EMBL:KIY03296.1};
OS Fonsecaea multimorphosa CBS 102226.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX NCBI_TaxID=1442371 {ECO:0000313|EMBL:KIY03296.1, ECO:0000313|Proteomes:UP000053411};
RN [1] {ECO:0000313|EMBL:KIY03296.1, ECO:0000313|Proteomes:UP000053411}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 102226 {ECO:0000313|EMBL:KIY03296.1,
RC ECO:0000313|Proteomes:UP000053411};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Fonsecaea multimorphosa CBS 102226.";
RL Submitted (JAN-2015) 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};
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DR EMBL; KN848063; KIY03296.1; -; Genomic_DNA.
DR RefSeq; XP_016637418.1; XM_016772279.1.
DR AlphaFoldDB; A0A0D2HN91; -.
DR STRING; 1442371.A0A0D2HN91; -.
DR GeneID; 27707509; -.
DR VEuPathDB; FungiDB:Z520_01763; -.
DR OrthoDB; 5475340at2759; -.
DR Proteomes; UP000053411; 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 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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000053411}.
FT DOMAIN 59..310
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 411..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 508..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 729..779
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 831..856
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..547
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..779
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 838..856
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 88
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 918 AA; 102878 MW; F969E16F5D420A58 CRC64;
MSSAINDDEL SISLPQTDSS RTRPSLPTVV SPPARASLSH TPMAESPGTA RAMQRLHQYA
FVRNIGEGSF GKVKLARHKV TGQEVAMKTI SRRKLISRDM AGRIEREIQY LQLLRHPHII
KLYTVITTKT DIYMVLEYVP MELFDYIVKH GRLGEAKARK LFQQIICAVE YCHRHKIVHR
DLKPENLLLD KNMNVKIADF GLSNIMTDGN FLKTSCGSPN YAAPEVIGGK LYAGPEVDVW
SCGVILYVFL VGRLPFDDEF IPALFKKIQA GTFHIPSQTP PGAVNLIKRC LQVHPVHRIT
IPEIRQDEWF IKDLPAYLVD PVEEFLDTGV DPTKAIDPRQ LAPGKPLDVV EKIHEQVVGK
LGRTMGYAKE DVKDALSKDE PSAIKDAYLI VRENQLMISA PQYRTENPEL ESFMASSPPV
EPNYPNFPGS PRRFQDIDVK PLTPSRTDPH RASRSLSETP SSLREEEKPR ISNVRVLNTS
LPHVHEELLQ IREKAKAHGE DPDMILHQTQ GQDQEDEAES PIPEEIKDEH GNPIYRSKEE
QEATSRALKP HSRSVTALSV LREPKSRPEG MTSLPSDEKR PAPSKTKPRR WQFGIRSRNQ
PWEAMKCLYA ALKAQGAEWE VNPWLRPESM PDGDDEKDVI PPPPPDLEPG QRHQIMQQRF
SFVGEDYYIP RDPYNIRARI LKKGLLMPGE APSLSAHSSA VSLPAEAQTQ LKKHIEQLGY
ASEDVKHVLG INSPNGGPAN IKSPASSGHP TRPNTGGEPA THSQDAFTGP GQVSMSRPDS
LSALNKKIPS EHIGVWVFID IQLYTIEQGT FVVDFKCDGY QNVIWHDLKK ERDRNKTPSS
NSTVTSPTNS RPTSGFGEFI HTSSDRLDEM GADGYWKPVS KRYKNVEKEI SSPYPYLDVA
SDLVAQLVSL SAKAAQRS
//
