ID A0A091R0R3_LEPDC Unreviewed; 1597 AA.
AC A0A091R0R3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
DE Flags: Fragment;
GN ORFNames=N330_07771 {ECO:0000313|EMBL:KFQ15189.1};
OS Leptosomus discolor (Madagascar cuckoo roller) (Cuculus discolor).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Coraciiformes; Leptosomidae; Leptosomus.
OX NCBI_TaxID=188344 {ECO:0000313|EMBL:KFQ15189.1, ECO:0000313|Proteomes:UP000053001};
RN [1] {ECO:0000313|EMBL:KFQ15189.1, ECO:0000313|Proteomes:UP000053001}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N330 {ECO:0000313|EMBL:KFQ15189.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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; KK687478; KFQ15189.1; -; Genomic_DNA.
DR PhylomeDB; A0A091R0R3; -.
DR Proteomes; UP000053001; 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:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; IEA:InterPro.
DR CDD; cd14012; PK_eIF2AK_GCN2_rpt1; 1.
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:SF196; AGC FAMILY PROTEIN KINASE; 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; 2.
DR SMART; SM00591; RWD; 1.
DR SMART; SM00220; S_TKc; 2.
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}; Coiled coil {ECO:0000256|SAM:Coils};
KW Initiation factor {ECO:0000313|EMBL:KFQ15189.1};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KFQ15189.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR000660-2};
KW Protein biosynthesis {ECO:0000313|EMBL:KFQ15189.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053001};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..90
FT /note="RWD"
FT /evidence="ECO:0000259|PROSITE:PS50908"
FT DOMAIN 248..491
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 544..962
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 183..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 642..735
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 96..153
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 656..677
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 709..733
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 795
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 ECO:0000256|PROSITE-ProRule:PRU10141"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFQ15189.1"
FT NON_TER 1597
FT /evidence="ECO:0000313|EMBL:KFQ15189.1"
SQ SEQUENCE 1597 AA; 181281 MW; 8BE3BE359A35C8BB CRC64;
VRQPPEINLV LRPQGLTGDN EVYAKVDLWV KCPHTYPDTV PEIQLKNSKG LSNEKINELK
SRLAELAKQR CGEVMIFELA DHVQSFLSEY NKPPSKSFHE EMLKNHQKEQ ERLAQEELRR
AQEQREILNE IQRREEEKRE ERKKKEIAKQ ERLEIAALTS QENSHRRDTA GYRVASGLNG
SCLEHGVNNK HRTNSAGRSK RERHLSVGNN KESPGNYEVL NFSTSGAGQL TVHKGKCLGK
DEQLGKSVYN ALEICSGDFV LIYEWVLHWQ KKMGRFLTAH EVEKIEKCKK QLQGAETEFS
SLTKLSHPNI IHYKCMNLKE QDDSVVVDIL VEHISGCSLS TYLHKETPVP IEQLRHYVTQ
ILSALDYLHS NSVVHKVLCA SSILVDAEGN IKVTDYSISK RLADICKADV FEQTKVRFSE
DGLPSKPGKK GDVWSLGLLL LSLSQGQVTK EYPVAVPTSL PADFQDFLEK CVCLEDKERW
TPQQLLQHSF INIPRMKIPV AEENLDDSAA GIDCIETVVP SSQISSASFF TETQRQFSRY
YNEFEELKLL GKGAFGAVIK VRNKLDGCYY AVKRIRINPA SKQFRRIKGE VTLLSRLNHE
NIVRYYNAWI EKHESPVLTV SPSETTEEKR MPTKAGLFLT TEETNDVEAN APPPVLTSSV
EWSTSCERSS SNKFSGADQE SSDDDDDGDG VFSHSFLPTT DSESEIIFDN EDENSKGRSP
DEEGNEKNSH GGEDRTPVIQ TLHYLYIQME YCEKSTLRDT IDQGLCEDTS RLWRLFREIL
DGLAYIHEKG MIHRDLKPVN IFLDSDDHVK IGDFGLATDH PANAVVSKQE ESRSDSSAMS
DPSGNLTGMV GTALYVSPEV QGSTKSTYNQ KVDLFSLGII FFEMSYHPMS TASERIFVLG
QLRLPTIVFP KDFDEIKHAK QRLVITWLLN HDPAARPTAV ELLKSEHLPP PQMEESELHE
VLHHTLANVD GKAYRTMMSQ IFSQRISPAI DYTYDSDMLK GGFSIWAAKI QQHVCEIVSR
IFKRHGAIKL HTPLLMPRNK KLYEHNEASY FMDHSGMLVM LPYDLRIPFA RFVARNNISN
LKRYCIERVF RPRKLDRCHP KELLECAFDI ITSTGNSFLP IAETIYAISE IIQEFSVLQE
RNYSIYLNHT ALLKAILLHC GIPEDKLNQV YIILYDAVTE KLTKREVEAK FCNLSLTSNS
LSRLYRFIEQ KGEASNVFPF LNTMIKQKPG VTQLLKHGMK DLEEIIGLLK QLGIKLQVSI
NLGLVYKIQQ HNGIIFQFIA YIKRRQRTVP EILAAGGRYD HLIPQFRGPQ AVGPVPSAVG
VSIAIDKITA AVSGVEDSVS VSSCDLLVVS VGQMSMGRAI NIVQKLWTTG IPAEIMYDWS
QSQEELQEYC RCSGITYVAL VSDKEGSHVK VKSFEKDRQT EKRILESDLI DHLIQKLKIK
NCDERCSRET SDNLSVANQK GSFTNISGVF ESHGTLVVPN VSVIAPEKLS ASARRRQEIQ
VQTRLQTFIC SLQQKTSEIE ILAVDLPKAT VIHFLSLEFD GDRQAFDATV RQLMSRWPKQ
RCSYLQAICD EIYSIKMEKR VPALILYSYR DEYKVLF
//
