ID A0A2H3CP52_ARMGA Unreviewed; 1556 AA.
AC A0A2H3CP52;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=ARMGADRAFT_1067164 {ECO:0000313|EMBL:PBK84849.1};
OS Armillaria gallica (Bulbous honey fungus) (Armillaria bulbosa).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Physalacriaceae; Armillaria.
OX NCBI_TaxID=47427 {ECO:0000313|EMBL:PBK84849.1, ECO:0000313|Proteomes:UP000217790};
RN [1] {ECO:0000313|Proteomes:UP000217790}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ar21-2 {ECO:0000313|Proteomes:UP000217790};
RX PubMed=29085064; DOI=10.1038/s41559-017-0347-8;
RA Sipos G., Prasanna A.N., Walter M.C., O'Connor E., Balint B., Krizsan K.,
RA Kiss B., Hess J., Varga T., Slot J., Riley R., Boka B., Rigling D.,
RA Barry K., Lee J., Mihaltcheva S., LaButti K., Lipzen A., Waldron R.,
RA Moloney N.M., Sperisen C., Kredics L., Vagvoelgyi C., Patrignani A.,
RA Fitzpatrick D., Nagy I., Doyle S., Anderson J.B., Grigoriev I.V.,
RA Gueldener U., Muensterkoetter M., Nagy L.G.;
RT "Genome expansion and lineage-specific genetic innovations in the forest
RT pathogenic fungi Armillaria.";
RL Nat. Ecol. Evol. 1:1931-1941(2017).
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; KZ293695; PBK84849.1; -; Genomic_DNA.
DR STRING; 47427.A0A2H3CP52; -.
DR InParanoid; A0A2H3CP52; -.
DR OMA; EFYHRSG; -.
DR OrthoDB; 8734at2759; -.
DR Proteomes; UP000217790; 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, ECO:0000313|EMBL:PBK84849.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR000660-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000217790};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 10..120
FT /note="RWD"
FT /evidence="ECO:0000259|PROSITE:PS50908"
FT DOMAIN 207..498
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 544..919
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 142..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 613..644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 674..717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..191
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 674..693
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 773
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000660-1"
FT BINDING 550..558
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000660-2"
FT BINDING 573
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000660-2"
FT BINDING 574
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1556 AA; 174311 MW; CAB6823765330B04 CRC64;
MESTEELQKN ELTALQSIYA EDFQLIPPSK AWKGAASLPE ITIRVRHPER ANIGFDLNVK
FPKTYPTLTY PNFTVQKPRG LDHDQITKLN HTLQNEVRAS PRTEMVFQIV TFCQDWLSEN
VAAPAEVIGS LAVQMKQRAA EEERARQEQA EREAMERKQR MDKLAREFDA DVQKQQQLAR
EQHRTRQRAN SEATEVPDSS DTPTETFDED IEMNGIHFNT VKFFHRRNAY LGTIYGADPV
CDDVNATLPL ELHVITFDSH YYTTSQGRKK VKQVEEEITR LKSVRHPNVV RVLAVKLKAP
HSSGAPQLVI LSEQSPALSL KDVLDDCDSL REDRVSDYIA QILSGLNAVH VCDLVHRGIS
ATSIGLVSGN CPSQSKLIKL TKVGYHTRLL DLHRSNAFGY VNPPEERVMP EAWLSKDAKN
ESLLLYTHQR DIHAVGVVLL QMLLGLDVVE RFSDVHTALR SSTIPPALQQ HAMNMLVPPK
KSHTTCLTLL AGLAETSLHR TQRSLSISMS EPKTPMYAAV SGSPEFDYFR GAMFRQASRW
KEDWEELELL GKGAFGSVVK ARNRIDNRVY AVKKVRLRTL RSDTKIFREV NALSRLSHRF
IVRYYTTWVE TAEPTSTAAS DESESESDSY SQSNGTENGM TSVPSRIQSR EASGPIIFNM
DDLDDLGGTS RGSFPSIHFT GSSGSQEDTD SDNETPFGGL FRKAGEENGE GLGSMTPPLT
VQRTLYIQME FVERQTLKER VDEGISESEA WRLFQQIVDA LVHMSTLGII HRDIKLTNIF
IDAKGDCKVG DFGLATSSLA AVDPSDVSPR VVAQETDMTL EVGTRLYIAP EVQSRRRRPT
NHTKADMYSL GIVFFEMNYS FTTGSERISV IEALRRPEIV FPDSWDALRL PQREIITWLL
QHEPDDRPTA LELSQSPLLP SRLEDEYFKG ALKMMTKPDS PHHQAVLASL FKQSPRPVRS
FLYDHEAELP EHASLNGMVQ DHLTAIFRLR GAVDMEPPLL MPITSTEDDK DHAVFIDRHG
DIVKLPSSLL VTFARLAARG GITRIKRFHI ADVYRPQAAA GHPRPHKAAV FDIITPDLMS
GPVAAGAEIL AVADNCLDTF PSLAQMYEIH VSHSNIVDAV LSRLPAAHKS AIVEIINQPK
SSTSQKRALF LKKGLLRSTA DELEVLSDTY EDVELLLMRL DKLSSPLLET IRPAIEEIKT
VVKTASLAGV SRPIKFYPLM VGNHLKDFKH GILVEVVRRS KRIELLAAGG RYDNLITKFS
PPKPTAESIH AIGLQIAIDK ITAAVASFQS SSVKSLLKEA KSFGYWSPRR CDVYVISYHP
GYLQDRLELA SYLWRHNISA DVMYESAITN VETSVTDTCK REGILFTVNP KPKRDQTTGI
KVNAIFGNYN DEDILIPRQE LVAHLQEAIG VQKRADSATS GATTFFEGKN LLANKETTTL
DLQAVLPAET VKKGLRRNKL IVQDKAHELG TKIHRAFMSN MPIIVVDIPP ATLVALTRTN
TWITNDEAWK LISPGFNNHI YAQQVRDAVA TRKEDGFPFI LLYASREERA LLLQLC
//
