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Entry: A0A2S5BHQ0_9BASI
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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
//
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