ID G8YUX6_PICSO Unreviewed; 785 AA.
AC G8YUX6;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Piso0_000249 protein {ECO:0000313|EMBL:CCE72659.1};
GN Name=Piso0_000249 {ECO:0000313|EMBL:CCE72659.1};
GN ORFNames=GNLVRS01_PISO0A05192g {ECO:0000313|EMBL:CCE72659.1};
OS Pichia sorbitophila (strain ATCC MYA-4447 / BCRC 22081 / CBS 7064 / NBRC
OS 10061 / NRRL Y-12695) (Hybrid yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Millerozyma.
OX NCBI_TaxID=559304 {ECO:0000313|EMBL:CCE72659.1, ECO:0000313|Proteomes:UP000005222};
RN [1] {ECO:0000313|Proteomes:UP000005222}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4447 / BCRC 22081 / CBS 7064 / NBRC 10061 / NRRL
RC Y-12695 {ECO:0000313|Proteomes:UP000005222};
RX DOI=10.1534/g3.111.000745;
RA Leh Louis V., Despons L., Friedrich A., Martin T., Durrens P.,
RA Casaregola S., Neuveglise C., Fairhead C., Marck C., Cruz J.A.,
RA Straub M.L., Kugler V., Sacerdot C., Uzunov Z., Thierry A., Weiss S.,
RA Bleykasten C., De Montigny J., Jacques N., Jung P., Lemaire M., Mallet S.,
RA Morel G., Richard G.F., Sarkar A., Savel G., Schacherer J., Seret M.L.,
RA Talla E., Samson G., Jubin C., Poulain J., Vacherie B., Barbe V.,
RA Pelletier E., Sherman D.J., Westhof E., Weissenbach J., Baret P.V.,
RA Wincker P., Gaillardin C., Dujon B., Souciet J.L.;
RT "Pichia sorbitophila, an interspecies yeast hybrid reveals early steps of
RT genome resolution following polyploidization.";
RL G3 (Bethesda) 2:299-311(2012).
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DR EMBL; FO082059; CCE72659.1; -; Genomic_DNA.
DR AlphaFoldDB; G8YUX6; -.
DR STRING; 559304.G8YUX6; -.
DR eggNOG; KOG0598; Eukaryota.
DR HOGENOM; CLU_000288_52_2_1; -.
DR InParanoid; G8YUX6; -.
DR OMA; SYAMGTT; -.
DR Proteomes; UP000005222; Chromosome A.
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; 2.60.40.150; C2 domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
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:SF245; AGC_AKT PROTEIN KINASE SCK2; 1.
DR PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR Pfam; PF00168; C2; 2.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50004; C2; 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}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000005222};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 190..354
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 388..649
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 650..725
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT REGION 1..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 125..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 248..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 736..785
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..45
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..177
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..268
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 749..773
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 427
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 785 AA; 87080 MW; 8D5AA778FB603BA4 CRC64;
MADFAKSIFG LGSFYKKEPG GPEKHQGATG VDPESDKDRV PVLHGASEEP QRFVASNEQY
DYPGGSGSED RVYQGNSKFL PRGLANVTPT TAVSTASPAY GFTLTNPEAT NSEDFLQRTF
KSRGAVDPAA EGGPADNQNP SSQHSELSHH TDDIHSYPSQ NLSTNTSQDS NFAQMGDGGS
SHPLIITTDE SGHQKYYSSK NSSQPKGKLK ITILQARDLL INSPVSSPYV VCTFESSEFV
THTPASYNKS LSHNSSSSRL QSSALPMASR DLSRKGKAPP LYKRQSSTQH LQLDNFNAGS
ANPAWNHEAT FDVVGSKSEL DISVYDSAHD DSFLGHVRIF PPTTSNKQTT AQWFDLKARI
MGERVSGAIK VKCEYTSLDK KSYGPDDFEI LRLLGKGTFG QVYQVKKKDT DRIYAMKVLS
KKVIVKKKEI AHTIGERNIL VRTSAAASPF IVGLKFSFQT PSDLYLVTDY MSGGELFWHL
QKEGRFSEDR AKFYIAELVL ALEHLHDSDI VYRDLKPENI LLDANGHISL CDFGLSKANL
NNDGTTNTFC GTTEYLAPEV LLDESGYTKM VDFWSLGVLI FEMCCGWSPF YADNTQQMYK
NIAFGKVRFP KEVLSAEGRS FVKGLLNRNP KHRLGATNDA SELRAHPFFH DIDWELLKTK
NIPPPFKPHI SSETDTSNFD PEFTNEPTAN LRKHLEIAST PLSPGIQANF KGFTYVDDSA
MEDHFGRSYR VNAFKNPGSF IPGDPNLPPD EDVIDDEQDD ESDSMDVDPE HVDDDEQFVN
GRFDL
//
