ID A0A091N803_9PASS Unreviewed; 761 AA.
AC A0A091N803;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
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=N310_01788 {ECO:0000313|EMBL:KFP85948.1};
OS Acanthisitta chloris (rifleman).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Acanthisittidae;
OC Acanthisitta.
OX NCBI_TaxID=57068 {ECO:0000313|EMBL:KFP85948.1, ECO:0000313|Proteomes:UP000053537};
RN [1] {ECO:0000313|EMBL:KFP85948.1, ECO:0000313|Proteomes:UP000053537}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N310 {ECO:0000313|EMBL:KFP85948.1};
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=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC protein kinase family. RAF subfamily. {ECO:0000256|ARBA:ARBA00010507}.
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DR EMBL; KK844017; KFP85948.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091N803; -.
DR Proteomes; UP000053537; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd20871; C1_B-Raf; 1.
DR CDD; cd17134; RBD_BRAF; 1.
DR CDD; cd14062; STKc_Raf; 1.
DR Gene3D; 3.30.60.20; -; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR020454; DAG/PE-bd.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR003116; RBD_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR23257:SF731; NON-SPECIFIC SERINE_THREONINE PROTEIN KINASE; 1.
DR PANTHER; PTHR23257; SERINE-THREONINE PROTEIN KINASE; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF02196; RBD; 1.
DR PRINTS; PR00008; DAGPEDOMAIN.
DR SMART; SM00109; C1; 1.
DR SMART; SM00455; RBD; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50898; RBD; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KFP85948.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000053537};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KFP85948.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 109..181
FT /note="RBD"
FT /evidence="ECO:0000259|PROSITE:PS50898"
FT DOMAIN 188..234
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 452..712
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 255..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 287..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 389..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..421
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..446
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 478
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP85948.1"
FT NON_TER 761
FT /evidence="ECO:0000313|EMBL:KFP85948.1"
SQ SEQUENCE 761 AA; 85207 MW; B1CB1F7AA97E623C CRC64;
VWNIKQMIKL TQEHIEALLD KFGGEHNPPS IYLEAYEEYT SKLDALQQRE QQLLESMGNG
TDFSVSSSAS TDTVASSSSS SLSVAPSSLS VYQNPADMSR NNPKSPQKPI VRVFLPNKQR
TVVPARCGVT VRDSLKKALM MRGLIPECCA VYRIQDGEKK PIGWDTDISW LTGEELHVEV
LENVPLTTHN FVRKTFFTLA FCDFCRKLLF QGFRCQTCGY KFHQRCSTEV PLMCVNYDQL
DLLFVSKFFE HHPMPPEETS LGETTPASGS PKSSFSLTLF LRPPILPSPS PSKSIPIPQP
LRPADEDHRN QFGQRDRSSS APNVHINTIE PVNIDDLIRD QGLRGEGAPL NQLMRCLRKY
QSRTPSPLLH SVPSEIVFDF EPGPVFRGST AGLSATPPAS LPGSLTNVKA LQKSPGPQRE
RKSSSSSEDR NRMKTLGRRD SSDDWEIPDG QITVGQRIGS GSFGTVYKGK WHGDVAVKML
NVTAPTPQQL QAFKNEVGVL RKTRHVNILL FMGYSTKPQL AIVTQWCEGS SLYHHLHIIE
TKFEMIKLID IARQTAQGMD YLHAKSIIHR DLKSNNIFLH EDLTVKIGDF GLATVKSRWS
GSQQFEQLSG SILWMAPEVI RMQDKNPYSF QSDVYAFGIV LYELMTGQLP YSNINNRDQI
IFMVGRGYLS PDLSKVRSNC PKAMKRLMAE CLKKKRDERP LFPQILASIE LLARSLPKIH
RSASEPSLNR AGFQTEDFSL YACASPKTPI QAGGYGGFPV H
//
