ID A0A091GU21_9AVES Unreviewed; 1262 AA.
AC A0A091GU21;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
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=N303_15063 {ECO:0000313|EMBL:KFO77622.1};
OS Cuculus canorus (common cuckoo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Cuculiformes; Cuculidae; Cuculus.
OX NCBI_TaxID=55661 {ECO:0000313|EMBL:KFO77622.1, ECO:0000313|Proteomes:UP000053760};
RN [1] {ECO:0000313|EMBL:KFO77622.1, ECO:0000313|Proteomes:UP000053760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N303 {ECO:0000313|EMBL:KFO77622.1};
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};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. {ECO:0000256|ARBA:ARBA00009903}.
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DR EMBL; KL447826; KFO77622.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091GU21; -.
DR STRING; 55661.A0A091GU21; -.
DR Proteomes; UP000053760; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00992; PDZ_signaling; 1.
DR CDD; cd05609; STKc_MAST; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 1.20.1480.20; MAST3 pre-PK domain-like; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR037711; MAST.
DR InterPro; IPR015022; MAST_pre-PK_dom.
DR InterPro; IPR023142; MAST_pre-PK_dom_sf.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24356:SF140; MICROTUBULE-ASSOCIATED SERINE_THREONINE-PROTEIN KINASE 3; 1.
DR PANTHER; PTHR24356; SERINE/THREONINE-PROTEIN KINASE; 1.
DR Pfam; PF08926; DUF1908; 1.
DR Pfam; PF17820; PDZ_6; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF140482; MAST3 pre-PK domain-like; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KFO77622.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000053760};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 337..610
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 611..682
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT DOMAIN 916..999
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 64..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 111..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 645..664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 691..752
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 766..790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 814..856
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 882..902
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1004..1184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1200..1226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1243..1262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..126
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..722
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 727..752
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1013..1029
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1040..1079
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1092..1113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1134..1149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1150..1167
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFO77622.1"
FT NON_TER 1262
FT /evidence="ECO:0000313|EMBL:KFO77622.1"
SQ SEQUENCE 1262 AA; 139849 MW; 6C9399BE397BB466 CRC64;
SCRSSNRKSL VVGTPSPTLS RPLSPLSVPT AGSSPLDSPR NFSASTSINF PFARRTDGRR
WSLASLPSSG YGTNTPSSTV SSSSSSQERL HQLPYQPTPD ELHFLSKHFR STESVTDEEG
RHSPCLRPRS RSLSPGRTGG TFDNEVVMMN HVYKERFPKV NARTGEDHGY STLPLADGVL
GFIHHQIIEL ARDCLAKSQG ALITSRYFME LQEKLEKMLR DAQERSESEE VKFIDQLVRK
LLIIISRPAR LLECLEFDPE EFYHLLEAAE GHAKVGQGIK TDIPRYIISQ LGLVKDPLEE
MVQMDHFDSG NTITPENDDA CESSAPVPRR KPCEGDFETI KLISNGAYGA VYLVRHRETR
QRFALKKINK QNLILRNQIQ QVFVERDILT FAENPFVVSM FCSFETKRHL CMVMEYVEGG
DCATLLKNMG PLPVDMAKMY FAETVLALEY LHNYGIVHRD LKPDNLLITS MGHIKLTDFG
LSKIGLMNMT TNLYEGHMEK DTREFMDKQV CGTPEYIAPE VILIQGYGKP VDWWAMGIIL
YEFLVGCVPF FGDTPEELFG QVISDEIMWP EGDEALPTDA QDLITRLLRQ CPLERLGTGG
AHEVKHHSFF LHLDWNGLLR QKAEFIPQLE SEDDTSYFDT RSERYRHLDS EDEETNDEES
SVEIGQFSSC SHRFSKVYSS SEFLAAHSNL SLSSSDQSHS EDKEERWDRH SGDEDRNRLA
GTEPRLRSWT SCGSTSYTSR HERSRSPATL ASTYSLDTMP KFAFSSEDES PCVAPSKPER
PKFVLGDPDV GTGGAVKPSA LSADLVSLNR IRLRSNSTGT KNSTPRGLEP GKSRRLSSQK
DVADRQRTSP GGRVPKSASV SALSLIITSD DFGSGALMSP ISPHSLSSNP SSRDSSPSRD
SSLAIASLRP PIIIHSSGKK YGFTLRAIRV YMGDSDVYTV HHMVWSVEEG SPAQEAGLRA
GDLITHVNGE SVLGLVHRDV VELLLKSGNK VALRTTALEN TSIKIGPARK NSSKTRMARR
SKKSRKRDGQ DRRKTLFKKI SKQSSVLHTS RSFSSGLHHS LSSSESLPES PTHSLSPGPA
TPCRSPAPDL PTDAVSPQST SPSSSTPTSP AGHVRPSSLH GLAPKLGGQR YKVGRRKSTS
SIPPSPLACT PSSAQRPPSP QRSPSPLPGS RPRSAECPRS PLLKRVQSAE VVTILAEKKT
GGGRKLGYPG EHSYHPAGSR LSERHDRDQE VVVMRRLNLS ERRDSFKKQE AVQEVSFDEP
ET
//
