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Database: UniProt
Entry: V5E8T2_KALBG
LinkDB: V5E8T2_KALBG
Original site: V5E8T2_KALBG 
ID   V5E8T2_KALBG            Unreviewed;       626 AA.
AC   V5E8T2;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   ORFNames=PSEUBRA_SCAF3g04245 {ECO:0000313|EMBL:EST06736.1};
OS   Kalmanozyma brasiliensis (strain GHG001) (Yeast) (Pseudozyma brasiliensis).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Kalmanozyma.
OX   NCBI_TaxID=1365824 {ECO:0000313|EMBL:EST06736.1, ECO:0000313|Proteomes:UP000019377};
RN   [1] {ECO:0000313|Proteomes:UP000019377}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GHG001 {ECO:0000313|Proteomes:UP000019377};
RX   PubMed=24356824; DOI=10.1128/genomea.00920-13;
RA   Oliveira J.V.D.C., dos Santos R.A.C., Borges T.A., Riano-Pachon D.M.,
RA   Goldman G.H.;
RT   "Draft genome sequence of Pseudozyma brasiliensis sp. nov. strain GHG001, a
RT   high producer of endo-1,4-xylanase isolated from an insect pest of
RT   sugarcane.";
RL   Genome Announc. 1:E0092013-E0092013(2013).
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
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DR   EMBL; KI545873; EST06736.1; -; Genomic_DNA.
DR   RefSeq; XP_016291725.1; XM_016438182.1.
DR   AlphaFoldDB; V5E8T2; -.
DR   STRING; 1365824.V5E8T2; -.
DR   GeneID; 27420860; -.
DR   eggNOG; KOG2464; Eukaryota.
DR   HOGENOM; CLU_013161_0_0_1; -.
DR   OMA; QAWDRWD; -.
DR   OrthoDB; 5491350at2759; -.
DR   Proteomes; UP000019377; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0035173; F:histone kinase activity; IEA:UniProt.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR024604; GSG2_C.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   PANTHER; PTHR24419; INTERLEUKIN-1 RECEPTOR-ASSOCIATED KINASE; 1.
DR   PANTHER; PTHR24419:SF18; SERINE_THREONINE-PROTEIN KINASE HASPIN; 1.
DR   Pfam; PF12330; Haspin_kinase; 1.
DR   SMART; SM01331; DUF3635; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019377};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          224..581
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          24..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          86..116
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          139..166
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          564..583
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        24..41
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   626 AA;  67783 MW;  81311A6A6C4F8F55 CRC64;
     MTPRRPVPTK SYFAEKARQL AELASEEDKE AQLSERSKGI KAVRARPRKT IATAGRGNSR
     KSMAAKPRQT SALGYSLNSA IAISDSSMSS ATGVSDSSFD AAGTSQSSIS FLGQSSDESR
     DLAAKSSIAA AKAKAKQNKR VTRRIAATSD DEDEVQGGSE DESEQDPALQ LAAAVADLAV
     ADEDDATAID DHLDGLLAAV SQAKPKAFST VIQQLRASKA STSQRRLEKI GEASYSEVFK
     ISSSRSNTSA DSDRQEALVL KIIPISSSSI SNNDNEDLPY TSPAADVERE IRLMQLIGRE
     ASVADSFVSL RAVHVVRGAY PAPLLQAWDR WDAKRRVRTG EGAENIRPHV LGRQQVYALL
     VMTDGGMDLE SLKLRSWSQA ASIFRQVAIG LGKMETKYEF EHRDLHWGNI LVQAVATTSQ
     AHDDGGGLSW LLDPSASGVK ATIIDFTLSR ARTSPVTAKR SKSVEVLHYP FDDESLFEGS
     GGPQFDVYRE MRTVTKDSWA AHCPATNVLW LRYLVHKLIE VKCRNLKVPK GSDADAQREL
     RSFDVLQKAA ARLDEAAQTL LNAAPPKRGP VAGRKPMHPR ARKSVLPAAT IGARKGRATM
     MVTPLQPAES ETKAVRSAAD LVSFLD
//
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