ID A0A067PVR8_9AGAM Unreviewed; 1587 AA.
AC A0A067PVR8;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=JAAARDRAFT_37399 {ECO:0000313|EMBL:KDQ55382.1};
OS Jaapia argillacea MUCL 33604.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Jaapiales; Jaapiaceae; Jaapia.
OX NCBI_TaxID=933084 {ECO:0000313|EMBL:KDQ55382.1, ECO:0000313|Proteomes:UP000027265};
RN [1] {ECO:0000313|Proteomes:UP000027265}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUCL 33604 {ECO:0000313|Proteomes:UP000027265};
RX PubMed=24958869; DOI=10.1073/pnas.1400592111;
RA Riley R., Salamov A.A., Brown D.W., Nagy L.G., Floudas D., Held B.W.,
RA Levasseur A., Lombard V., Morin E., Otillar R., Lindquist E.A., Sun H.,
RA LaButti K.M., Schmutz J., Jabbour D., Luo H., Baker S.E., Pisabarro A.G.,
RA Walton J.D., Blanchette R.A., Henrissat B., Martin F., Cullen D.,
RA Hibbett D.S., Grigoriev I.V.;
RT "Extensive sampling of basidiomycete genomes demonstrates inadequacy of the
RT white-rot/brown-rot paradigm for wood decay fungi.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:9923-9928(2014).
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};
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DR EMBL; KL197725; KDQ55382.1; -; Genomic_DNA.
DR STRING; 933084.A0A067PVR8; -.
DR HOGENOM; CLU_001222_2_0_1; -.
DR InParanoid; A0A067PVR8; -.
DR OrthoDB; 8734at2759; -.
DR Proteomes; UP000027265; 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; IPR041715; HisRS-like_core.
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_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR PANTHER; PTHR11042:SF197; EIF-2-ALPHA KINASE GCN2; 1.
DR PANTHER; PTHR11042; EUKARYOTIC TRANSLATION INITIATION FACTOR 2-ALPHA KINASE EIF2-ALPHA KINASE -RELATED; 1.
DR Pfam; PF12745; HGTP_anticodon2; 1.
DR Pfam; PF00069; Pkinase; 3.
DR Pfam; PF05773; RWD; 1.
DR Pfam; PF13393; tRNA-synt_His; 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 4: Predicted;
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:UP000027265};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 10..124
FT /note="RWD"
FT /evidence="ECO:0000259|PROSITE:PS50908"
FT DOMAIN 215..505
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 562..943
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 136..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 178..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 629..721
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..161
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..202
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 629..674
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 683..708
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 797
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000660-1"
FT BINDING 568..576
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000660-2"
FT BINDING 591
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000660-2"
FT BINDING 592
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1587 AA; 176741 MW; 3F0D98227D0965BB CRC64;
MESADERQHE EITVLQSIYA EDFLEVPPPK AWKGAARLPE FIIKVPHPDN TFASKVYFHL
HVKLPKTYPS IACPIFTIQQ PIRGLGPDHI TKLSSAIHAE AQSSKGSEMV FQIITFAQDW
LNTNIHPALE TPDSLAIQMN KRASDEERAR REREQELADL ERQKASQLAQ RLNEEIQADA
QRQQAEKEKF VRARKRAESD ATEVPSAGDT PTESFSSELE VQGVRFNSVK LFHPRKECLG
IIYLADPVCD DVQVTLPLEL HSVAFESPYY KTHQGRKKLM QLESEIQQLK RIRDPNLISI
YAVKLTFPHS SGPPRLVILA EQRSSLTLHD VLEDSDALRE DRATDYLRQI LSGLRAIHAN
NLMHRGLSPR CICLHKGDSA SSPKIVKLAK VSYYVRLQDL HRSNPFGPNV ARIAEDLAIP
EAWLPSDVVD SPLSYTTSRD IHQAGVVLLQ MLLGQDIFQH FPDPQTALKA LHVSPALHQV
ATGMLVPGKK RGPSCAALLA DLPRRSSDVV RPTTIATRSR GTSAAADLRT PMPQHISSSP
ESDYFRVPAP RQKHSSRWKE DWEELELLGK GAFGSVVKAR NKIDSRIYAV KKIKLRATQR
DDKIFREVNA LSRLSHRFIV RYYTTWVETS EPSGTPLSSG SDTESATEDG MTSVPIHHNS
GSTSEGSTGS SNDPFIIDLD DLGSGTGSQS SFPSIHFTRS GSTEAANDTD NGSEEDDDAE
NSAEIVRQLF SRPSNGNGFH TPSTIARTLY IQMEFVERQT LKERVAEGLS EDEAWRLFMQ
LVDALVHMST LGILHRDIKL TNIFIDGRGD CKVGDFGLAT SSLAAVDPSD VSPHAVTADS
DLTLEVGTML YIAPEVQSPR RGPRNHNKAD MYSLGVVFFE MNYFFSTGAE RVAVIEDLRR
PDIIFPPDWE NHRGRQRQII SSLLQHDPNA RPSALELSQS PLLPPRMEDE SFKGVIQMMS
NADSPQYQAL LSALFTQPQK RTRGFLYDNE AELPEHASLN DTVEETLAGI FHLHGAVDME
PPLLMPIVNA KDEPNRVLLL DQHGEVVSLP NNALVPFARL AARTNIRRIK RYHIGEIFKP
NLIAGHPKFS KAAVFDIITP DLENGPIAAT AEAIVVVHRC LDSFPGIGQN YEIRISHSSI
PDLALNRVSE EVRQDVIDII TQTKSSSSQK RALLLKKGLL RSTADELEIL SDLDYDPDGL
LSRLDKVSST LASLMAPLVK DIKKVMEFSA TAGVTKPIIF HPLMLGSHVS HFRDGVCFEV
VRRNKRSDIL AAGGRYDNLI SQFASPKAKS DAVRAVAVQI AIEKITLALA AFQSTSVRNL
VKEQKSFGFW SPRRCDVYVV SYHQGYLHDR LEVAALLWKN GISADVMYEA GLPDNDHESH
TDLCAREGIL FTVYPRPRSV RRDQPAFKIK SVLKGTEYEV ARQDLVSWLQ QQISEQKRVD
ASTSGVAIVA ENPQVIPNVI TRESSNTPDV QLLLPGDTKK QRKQAKQLFT DRAFSAGDQI
KSAFQSGMCV VAVDVPPTVF DAMVAARNSA WVSDEEAWRQ ILNGFPSGHS LYAHQVRDAV
SRKKGDGHRF VLLFSVRDER AQLLTLQ
//
