ID A0A2S5BHQ0_9BASI Unreviewed; 1646 AA.
AC A0A2S5BHQ0;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
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=BMF94_0504 {ECO:0000313|EMBL:POY76309.1};
OS Rhodotorula taiwanensis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=741276 {ECO:0000313|EMBL:POY76309.1, ECO:0000313|Proteomes:UP000237144};
RN [1] {ECO:0000313|EMBL:POY76309.1, ECO:0000313|Proteomes:UP000237144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD1149 {ECO:0000313|EMBL:POY76309.1,
RC ECO:0000313|Proteomes:UP000237144};
RX PubMed=29375494;
RA Tkavc R., Matrosova V.Y., Grichenko O.E., Gostincar C., Volpe R.P.,
RA Klimenkova P., Gaidamakova E.K., Zhou C.E., Stewart B.J., Lyman M.G.,
RA Malfatti S.A., Rubinfeld B., Courtot M., Singh J., Dalgard C.L.,
RA Hamilton T., Frey K.G., Gunde-Cimerman N., Dugan L., Daly M.J.;
RT "Prospects for Fungal Bioremediation of Acidic Radioactive Waste Sites:
RT Characterization and Genome Sequence of Rhodotorula taiwanensis MD1149.";
RL Front. Microbiol. 8:2528-2528(2018).
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};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. GCN2 subfamily. {ECO:0000256|ARBA:ARBA00037982}.
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:POY76309.1}.
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DR EMBL; PJQD01000005; POY76309.1; -; Genomic_DNA.
DR STRING; 741276.A0A2S5BHQ0; -.
DR OrthoDB; 8734at2759; -.
DR Proteomes; UP000237144; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004694; F:eukaryotic translation initiation factor 2alpha kinase activity; IEA:InterPro.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; IEA:InterPro.
DR CDD; cd14046; STKc_EIF2AK4_GCN2_rpt2; 1.
DR Gene3D; 3.40.50.800; Anticodon-binding domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR036621; Anticodon-bd_dom_sf.
DR InterPro; IPR016255; Gcn2.
DR InterPro; IPR024435; HisRS-related_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR006575; RWD-domain.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR PANTHER; PTHR11042; EUKARYOTIC TRANSLATION INITIATION FACTOR 2-ALPHA KINASE EIF2-ALPHA KINASE -RELATED; 1.
DR PANTHER; PTHR11042:SF184; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF12745; HGTP_anticodon2; 1.
DR Pfam; PF00069; Pkinase; 3.
DR Pfam; PF05773; RWD; 1.
DR PIRSF; PIRSF000660; Ser/Thr_PK_GCN2; 1.
DR SMART; SM00591; RWD; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 2.
DR SUPFAM; SSF54495; UBC-like; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50908; RWD; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR000660-
KW 2}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR000660-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000237144};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 18..127
FT /note="RWD"
FT /evidence="ECO:0000259|PROSITE:PS50908"
FT DOMAIN 243..509
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 568..979
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 644..708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 739..773
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1488..1541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..174
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..683
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1488..1516
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1524..1540
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 827
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000660-1"
FT BINDING 574..582
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000660-2"
FT BINDING 597
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000660-2"
FT BINDING 598
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1646 AA; 182571 MW; 64AEC14918073EF5 CRC64;
MASIGRGPAV STKLTNGSPS SRSSAIYGDD FEQTESRTAW KATHEFRICV RPEDEDLKDR
VSLWLRFKLP KRYPKVAPYI SGEEAKGLSK QHVAHLITTL LRAASNRLGE EMLYDLCSQA
SEYITERHVD SVRGAQPSLE DQMRKRGEEE AKASEESKLR EQAEREKREA EEAARLSHLI
SEDVRKREEL RLDRERRERE LDRERDSASL EVGAGGEKFV KMMVHPREGK SGAAIEGAVS
FKFPLLDDWL VRLFGAITRV SGTEAPATVF VVDILAPYYL SSQGKRKISK IETDLERIKA
LRHPNLFPLS GYRVVRHLPA YFPANPAAVG DLRPDRALEY FAQLVKVVEY LHSNNVVHRA
IRPKLVFVEG GKAAGGDDPV GLRLVGAGWY RRLIDLNKAE PWLQQPSREE LPEAWMSPEA
IAAPFTYDKA RDMFELGVLF AQMLFGTSVT ETFASPTDLV NSLPRTSPAA VRRTLRDLLL
TEGKKRPTAS RLAIQLSENS ESITLHTPMK LATTPPSALA GWPHANGGQK AMTPLVSPPP
SQLSRSIEGP NGFFVQPRLS GSRYRSEFEE LEFLGRGGGG QVVKARNRLD GHLYAVKKIR
LPHDRASENK ILREVTIWSR MNHPNIVRYH TAWTEVDDDH SLLTGGGSTG ATNSTLETGS
GLQITSSAEA KSRDSGDSDS TVSGSDETDT DRDVSSDDES DAPHDLQFGD FEDDLDFLSV
GHAHSRSVSY PSIHFGNDDD ASTAASDASS PALSRKASPA PGLKAPSPLS STPKQTRTLF
IQMEYVEKLT LREAIEDGVS EIDSWRWIFQ ILSAMVHFTS LSILHRDLKP SNIFIDVKGD
VRIGDFGLAV NQGGADGTGD VFLSADNTLD DSDLTSGVGT SLYIAPETMS RARAAAAKHY
SKKVDVYAFG IIVFELWHPF KTGMERIHVL HDLRRPEIKF PSTWDRALLP QQTRVVQACL
THDPELRPSP QDLLSSDMLP PRVGDDSIAE TIRLLSHSGT THAQKLITAL FAQSDEDRLR
KDFSYDFYDG SGAKADNDPY GQLVYDKLSR IFRQKGAVKV DSPLFMPHSQ IHAARKPVQL
LDADGTVVCL PFQLNIPFCR MVARDTSLTR LKRWTIAPIF RPAPAGGQPR AVLNAAFDIV
SDVAMPAMEA ECLFVTEEIL NAFPLTGTPA HLINHSKLLD TVLDIVPKKH REAVAEILVQ
HGRLQRSWLK TSTELLKLHG VTATICDALR AVDVIGDVSK IRNLVLSGPF RLTQAAKEGL
QEIESVVALC GQMGMRNLQV SPLLATNYDL HKNGTIFESH IVRGKSRDII AAGGRFDDVV
NRLAAPEVRM AGRCPHVVGF SMSISKLSLA AAEANTTTGK QAMSRKDEHL RSYGSWAIRR
CDVYVVSFSP GLIDLRLEIV KDLWRNGIKA DLMYDDDFLT LTPEQLVNAC RREGILWLII
VKPSVAGRSG AHDSETALKV KSVLRGSEEE VVRADLPAWL VQQLREQSGV DETAGGTNEP
PAESATGISD ASRSTQDYIP VLPEEESRPQ RGDVNRQKGR HNKRSLFAAR AQKNIEQAAK
SASEAPVFAI DLDGPAFERM AWSAEWISSD EAFKALLHTA PPGKRDYYSS IRAQVQRYKR
EHECSRFWLF SLRDDRSVLM SFFDRL
//