ID G0SZU7_RHOT2 Unreviewed; 815 AA.
AC G0SZU7;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=AGC/Akt protein kinase {ECO:0000313|EMBL:EGU11668.1};
GN ORFNames=RTG_02454 {ECO:0000313|EMBL:EGU11668.1};
OS Rhodosporidium toruloides (strain ATCC 204091 / IIP 30 / MTCC 1151) (Yeast)
OS (Rhodotorula glutinis (strain ATCC 204091)).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=1001064 {ECO:0000313|EMBL:EGU11668.1, ECO:0000313|Proteomes:UP000006141};
RN [1] {ECO:0000313|EMBL:EGU11668.1, ECO:0000313|Proteomes:UP000006141}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204091 / IIP 30 / MTCC 1151
RC {ECO:0000313|Proteomes:UP000006141};
RX PubMed=24526636; DOI=10.1128/genomeA.00046-14;
RA Paul D., Magbanua Z., Arick M.II., French T., Bridges S.M., Burgess S.C.,
RA Lawrence M.L.;
RT "Genome sequence of the oleaginous yeast Rhodotorula glutinis ATCC
RT 204091.";
RL Genome Announc. 2:E0004614-E0004614(2014).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGU11668.1}.
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DR EMBL; AEVR02000005; EGU11668.1; -; Genomic_DNA.
DR AlphaFoldDB; G0SZU7; -.
DR HOGENOM; CLU_000288_52_3_1; -.
DR InParanoid; G0SZU7; -.
DR Proteomes; UP000006141; Unassembled WGS sequence.
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 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; PF12330; Haspin_kinase; 1.
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};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EGU11668.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000006141};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 91..358
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 394..653
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 654..770
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT REGION 1..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 169..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 719..750
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 778..815
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..285
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..750
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 778..809
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 433
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 815 AA; 90122 MW; 198C29D3C77D1A38 CRC64;
MPDVSAMRND SPANNPPRRT RRSAFTDHST STSSSSSDSA SASTATSSPM TSPSVSARSH
STSPPLPPVS PPPSASTAIS RTEPDFSFKT QPSSLTRTKH PSQSAPRGKL VVKLIQARHL
SPPSSASRPY VVVTFDQNEF VSREPVHEEG EDAIGVAKPK PPTLLALQEQ GKPEGLRPST
LPATPGGGPN PGEKGNETAR VESGSGSASA SKAMAMPAEG TRAHGGAMSK SPSSMLGRSL
EEYRNGAVAA GTSSERATSP RPSRPALSPV NTTVWSPNDD PTTPTGAPRE PQGGILGAAD
DQMAYNPTWK HEVTFDVMNE KSVLQVQIYD RSIEEEMFLG VCEIRPRLVN NHTVDQWFPL
VARPGEDHEV TGEIRIQIRY EKFDSKKGLH PNDFDFLRMI GKGTFGRVFQ VRKKDTKRIY
AMKVLSKHEI IAKKEVAHTI GERKILQRSS DSPFLLGLKF SFQTETNLYL VMDYKSGGEL
FHHLQKEGRF TEDRARFYTA EIVLAFEHLH KFDIVYRDLK PENILLDATG HIVLCDFGLS
KPDLPSDALT NTFCGTTEYL APEVLLDDNG YSKIVDFWSL GVLLFEMCCG WSPFYAEDTQ
QMYKLICFGK VKFPRGVIGE DGKQFVKGLL NRNPKHRLGA QRDAAELKEH PFFKSIDWDL
LAQRAIPPPF KPYVDSDESV ANFDPEFTEA NLFDEAPHDV EFDDSDPSAD WLDHASKIGR
REVEKDGGAA PVEIRQQTRS RPSVQPLTSS VQENFRGFTF SGENESMLHN SAAFGHLRLD
DDDAQERNGD ASRRSSGSMR RSKGGHDDDE WEDER
//
