ID A0A1L8GQP3_XENLA Unreviewed; 802 AA.
AC A0A1L8GQP3;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN Name=braf.S {ECO:0000313|RefSeq:XP_018109661.1,
GN ECO:0000313|Xenbase:XB-GENE-1014207};
GN Synonyms=B-Raf {ECO:0000313|RefSeq:XP_018109661.1}, b-raf1
GN {ECO:0000313|RefSeq:XP_018109661.1}, braf
GN {ECO:0000313|RefSeq:XP_018109661.1}, braf1
GN {ECO:0000313|RefSeq:XP_018109661.1}, rafb1
GN {ECO:0000313|RefSeq:XP_018109661.1};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000313|Proteomes:UP000186698, ECO:0000313|RefSeq:XP_018109661.1};
RN [1] {ECO:0000313|RefSeq:XP_018109661.1}
RP IDENTIFICATION.
RC STRAIN=J_2021 {ECO:0000313|RefSeq:XP_018109661.1};
RC TISSUE=Erythrocytes {ECO:0000313|RefSeq:XP_018109661.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 RefSeq; XP_018109661.1; XM_018254172.2.
DR AlphaFoldDB; A0A1L8GQP3; -.
DR STRING; 8355.A0A1L8GQP3; -.
DR PaxDb; 8355-A0A1L8GQP3; -.
DR GeneID; 398973; -.
DR AGR; Xenbase:XB-GENE-1014207; -.
DR CTD; 398973; -.
DR Xenbase; XB-GENE-1014207; braf.S.
DR OMA; MYLMEYQ; -.
DR OrthoDB; 4560496at2759; -.
DR Proteomes; UP000186698; Chromosome 3S.
DR Bgee; 398973; Expressed in oocyte and 19 other cell types or tissues.
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; 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}; Kinase {ECO:0000256|ARBA:ARBA00022777};
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:UP000186698};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022777};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT REGION 127..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 304..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 382..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 427..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..336
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..460
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..485
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 517
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 802 AA; 89151 MW; 31DBABCD7E7A14E5 CRC64;
MAALSGGSAE GLSLLNGDLL ESDTGGLGGA GEMSVSGGFP EEVWNIKQMI KLTQEHIEAL
LDKFGGEHNP PSIYLEAYEE YTSKLDLLQQ REQQLLESMG NGTDSSSLSS ELTLSSVPSN
LSLAPSTLSA LGTPSDPSRI NPKSPQKPIV RVFLPNKQRT VVPARSGVTV RDSLKKALMM
RGLIPECCAV YRVQDGEKKP IGWDTDISWI TGEELHVEVL ENVPLTTHNF VRKTFFTLAF
CDFCRKLLFQ GFRCQTCCYK FHQRCSTEVP LMCVNYDRLD LLFVSKFFEH HPISQEEAPF
EEFVPAVESS TPPPPPDATG PPSLPSTSPS KSIPIPQPLR PDEDHRNQFG QRDRSSSAPN
VHINTIEPVN IDDLIRDQGL QRSEGAPSVQ PTRCHRKYHS RDPSPLLHTL PSEIVFDFES
DPVCRGSTPG LSATPPASLP GSLTNVKALQ KSPGQQRERK SSSSSSEDRS RMKTLGRRDS
SDDWEIPDGQ ITVGQRIGSG SFGTVYKGKW HGDVAVKMLN VTAPTPQQLQ AFKNEVGVLR
KTRHVNILLF MGYSTKPQLV IVTQWCEGSS LYHHLHIIET KFEMIKLIDI ARQTAQGMDY
LHAKSIIHRD LKSNNIFLHE DLTVKIGDFG LATVKSRWSG SHQFEQLSGS ILWMAPEVIR
MQDNNPYSFQ SDVYAFGIVL YELMTGQLPY SNINNRDQII FMVGRGYLAP ELSKVRSNCP
KAMKRLMADC LKKKRDERPL FPQILASIEL LARSLPKIHR SASEPSLNRA GFQTEDFSLY
TCASPKTPIQ GGGYGGFVIR AL
//
