ID A0A0K3C6A6_RHOTO Unreviewed; 927 AA.
AC A0A0K3C6A6;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Serine/threonine-protein kinase {ECO:0008006|Google:ProtNLM};
GN Name=FGENESH: predicted gene_2.244 {ECO:0000313|EMBL:CTR05214.1};
GN ORFNames=AAT19DRAFT_12183 {ECO:0000313|EMBL:PRQ76765.1},
GN BN2166_0010750 {ECO:0000313|EMBL:CTR05214.1};
OS Rhodotorula toruloides (Yeast) (Rhodosporidium toruloides).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=5286 {ECO:0000313|EMBL:CTR05214.1, ECO:0000313|Proteomes:UP000199069};
RN [1] {ECO:0000313|EMBL:CTR05214.1, ECO:0000313|Proteomes:UP000199069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Single colony {ECO:0000313|EMBL:CTR05214.1};
RA Cajimat M.N.B., Milazzo M.L., Fulhorst C.F.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PRQ76765.1, ECO:0000313|Proteomes:UP000239560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 0880 {ECO:0000313|EMBL:PRQ76765.1,
RC ECO:0000313|Proteomes:UP000239560};
RX PubMed=29521624;
RA Coradetti S.T., Pinel D., Geiselman G., Ito M., Mondo S., Reilly M.C.,
RA Cheng Y.F., Bauer S., Grigoriev I., Gladden J.M., Simmons B.A., Brem R.,
RA Arkin A.P., Skerker J.M.;
RT "Functional genomics of lipid metabolism in the oleaginous yeast
RT Rhodosporidium toruloides.";
RL Elife 7:0-0(2018).
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DR EMBL; CWKI01000002; CTR05214.1; -; Genomic_DNA.
DR EMBL; LCTV02000002; PRQ76765.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K3C6A6; -.
DR STRING; 5286.A0A0K3C6A6; -.
DR OMA; IQIHKSM; -.
DR OrthoDB; 5471704at2759; -.
DR Proteomes; UP000199069; Unassembled WGS sequence.
DR Proteomes; UP000239560; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd13118; POLO_box_1; 1.
DR CDD; cd13117; POLO_box_2; 1.
DR CDD; cd14099; STKc_PLK; 1.
DR Gene3D; 3.30.1120.30; POLO box domain; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR033701; POLO_box_1.
DR InterPro; IPR033695; POLO_box_2.
DR InterPro; IPR000959; POLO_box_dom.
DR InterPro; IPR036947; POLO_box_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24345; SERINE/THREONINE-PROTEIN KINASE PLK; 1.
DR PANTHER; PTHR24345:SF0; SERINE_THREONINE-PROTEIN KINASE PLK1; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00659; POLO_box; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF82615; Polo-box domain; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50078; POLO_BOX; 2.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000199069};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 153..410
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 711..778
FT /note="POLO box"
FT /evidence="ECO:0000259|PROSITE:PS50078"
FT DOMAIN 812..858
FT /note="POLO box"
FT /evidence="ECO:0000259|PROSITE:PS50078"
FT REGION 1..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 491..660
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..136
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..538
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..594
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 632..647
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 927 AA; 103597 MW; 7EB1943627D03E93 CRC64;
MLALQPQQPV QPTRRAIPLS RSSSSLRKTA PAPASTRQPL SSVQPGQPQR DTDTLSAYPA
KVARGQREEA SARTRPSSTI APQPPLAPST RTVQARQRVD SKHEVQTERE AEQPEPKEDD
KGKEQAAAKS SRNKLTDQWD EPPAQIRRGA VHLERGRLLG EGGFARVYLC TEPDGKSYKA
MKVIHKQQLK STKTKSKLFA EIKIHQAMQH PNVIAFECCF EDEHNVYMQL ELCARGSLLD
LLRIRKRFSE PESRFYLTQL VGAVDYLHSN SVIHRDLKLG NLMVDGNMNL KVGDFGLAAL
VKFPGERKKT ICGTPNYIAP EILFESKGTG HSFEVDIWSI GVILYTLLIG KPPFQTKDVK
NIYRKIRDNA YTFPSDHCLS PESTSLISSI LQPDPLSRPS LPSILFSSWF ITGPFPSRIS
SRALDPDRAK EMCEEWRYMT KRQSWDNFRR CKRKSGIVEV EEGVEVEGAV RKGEAAQVVE
AVSQALPTVA EAVEEEDEPE PEPIQQEEVV QPPKKAMRMV RPNEEREAKG RVEKEVRAAT
APDSPISELL RSARKPLMVS PSSRAIPSTS SSSALRRTAT TSVDSLQQRL AAASVSDPPA
QAAPSAATDA RRTDSAAAQP SRHRRAGAQS PVDVPPAPPP AAPAPPPAKS ATTTTHPSRS
LYDSTWRSFD TFLSCTSLAD VSAVCASFVD ALPDEDELRA SKVFVSSWVD YTHRCGTAYS
LTDGSAGVYF NDSTTMVLSP DKEHFDYIAN RHANVYTRRH YALSTVPEDL DRKAYLLRYF
EDYMAKTLRR NVEWQFQDVE RLKNMDFLVK YYRMKNAILF KLSNDVLQFN FFDHFKLIIT
SSGLVISVIT PTFTLETYTL PQLFRAAAQL GHYSHPTRRP NPSSDRGRKL ADLEVLIEKV
AYCKDVLRTL VNRRTGKEAE GEGGNKE
//
