ID V5F106_KALBG Unreviewed; 1451 AA.
AC V5F106;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Protein kinase {ECO:0000313|EMBL:EST08949.1};
GN ORFNames=PSEUBRA_SCAF13g01915 {ECO:0000313|EMBL:EST08949.1};
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:EST08949.1, 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 -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. MAP kinase kinase kinase subfamily.
CC {ECO:0000256|ARBA:ARBA00006529}.
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DR EMBL; KI545855; EST08949.1; -; Genomic_DNA.
DR RefSeq; XP_016293938.1; XM_016434571.1.
DR STRING; 1365824.V5F106; -.
DR eggNOG; KOG0198; Eukaryota.
DR HOGENOM; CLU_003051_3_0_1; -.
DR OMA; ARHSMMR; -.
DR OrthoDB; 145974at2759; -.
DR Proteomes; UP000019377; 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; PF07647; SAM_2; 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}; Kinase {ECO:0000313|EMBL:EST08949.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000019377};
KW Transferase {ECO:0000313|EMBL:EST08949.1}.
FT DOMAIN 59..122
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 1034..1310
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 160..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 229..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 270..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 394..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 477..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 570..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 615..676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 707..1019
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1315..1451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..181
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..248
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..373
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..432
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 621..647
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 707..722
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 768..791
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 832..886
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 941..962
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1356..1388
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1422..1451
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1063
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1451 AA; 152180 MW; 794A4D35AD6CD0BE CRC64;
MSAITPTSPG FPLTMGAGAS VHQLAGPSSM TGSPRSRPAT PLSAAYLPSG PTYDDLGRWD
DADVAAWLSS ARLGHHASTF ADNDIRGSVI LDVDQAALKE MGITMVKDRV RISAAIKLLN
KRCADSAMAR RPSVVSIPPL SPLATHALYA NEGEIEYLQN DPNADPSADG LNSQFGPNSM
SVRRGQMRPP PLTLKQSTSR GMPGYASPAN TINNNQGFGL SAARGLTPGA GRGSVWNTAS
SSTADGGMHR KVNSIGSLAA PAIVGAATGL PASRHPYGQS GQSSRPNTAT GASGHPSAHA
SQRGALPSIS PTSASFGSGP TSSLGRPATA TGAPSINSVA GGSSGSQGYS PLTPISEANS
YGATPTTPSA LHRQQQAMGY SVGRGLFVNA PRFAAASSAP EQQQPSSSGT LRHVDSGEGY
NQHANYSTAH QPTLEDLKRR TIKFISEEDN TTRTVNVSDC RDAYDVMSRV LRKFLKPPSG
NSYTPTADQG PTGDELGGTE TWGIFATSAD GQNTKALSDN ELLAICHAPQ PHDPLRERGL
TLRRIPNHLP GEDARRVPVR SGRNKLEAFF GERMPVAQMQ PAGPGSGPNG DDGDAGSVTI
SGKKMKRAST VSIMSGLGVG PLSHGSSSGS HPPTSGNYHT GNTGTIKASK RESKRHSPPP
IASKPSKIRN FFGQRPPSEL INTNLADFFP STDSKALQRT ARRSIYGRAS ASTRSKRNST
WSFVADPDAP PLPTKESYDG HEPPSERSSA SLRERGTPPI IQIAHDQPSE TDPFSNALRL
SSGSQTQPQP SGAGPPTLPP VVDRNSLDEW SRDLKAVGSP VAELPSTFPP NKPGRTMGQQ
QLPPPMQRSP SQGSTYINRP SVSRRTSGES ARSRRSLASQ VRQGLSAARE RNADTASLLT
VDEITQEVEN RKETTSLAGA GGGWVVDEDG VPIPIPGASA RSSSAAASTR PSSGATSSHV
HGSLTGHDEE DEEADDSVSE LRHSIAGHGD LSEGDSEPGL SDSDLGSDGS DTDDDDVAND
IYQPSAAAKA PIKWHKGALI GAGSFGNVFL GMNAKTGLLM AVKQVELPAA DSQVGQRKKS
MLDALESEIK LLKTLEHENI VQYLDSFADD THLNIFLEYV PGGSIVALLR NYGAFEEPLV
RNFVRQILKG LSFLHNRGIM HRDIKGANIL VDNKGGIKIS DFGISKKVES DLVLSTNKGG
SAGGGAGGPA NRPSLQGSVF WMAPEVVKQT SYTIKADIWS LGCLVVEMIS GTHPWAELNQ
MQALFQIGMG RKPTLPDEIS NECRDFLEKT FELDYNNRPS ADELLNHAFM GTEMTFPPSA
AAGGEDEDGS PAGATGHSGE AAEGETTVDA TADGETGTTR EGRDSKRSGR SKSLRRLERE
KRHKEAAAAT AAALDGGSPS TPTTRIAPHP ATLGAARSPT AGMPESVSTS SIATTRGIPS
PPTDASNDPA S
//
