ID A0A3B3RYL5_9TELE Unreviewed; 1596 AA.
AC A0A3B3RYL5;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
OS Paramormyrops kingsleyae.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000023010.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000023010.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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=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. DMPK subfamily. {ECO:0000256|ARBA:ARBA00005719}.
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DR Ensembl; ENSPKIT00000003683.1; ENSPKIP00000023010.1; ENSPKIG00000006313.1.
DR GeneTree; ENSGT01030000234517; -.
DR Proteomes; UP000261540; Unplaced.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0048468; P:cell development; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd01243; PH_MRCK; 1.
DR Gene3D; 1.20.5.340; -; 1.
DR Gene3D; 3.30.60.20; -; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR001180; CNH_dom.
DR InterPro; IPR031597; KELK.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR014930; Myotonic_dystrophy_kinase_coil.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR22988; MYOTONIC DYSTROPHY S/T KINASE-RELATED; 1.
DR PANTHER; PTHR22988:SF31; SERINE_THREONINE-PROTEIN KINASE MRCK ALPHA; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00780; CNH; 1.
DR Pfam; PF08826; DMPK_coil; 1.
DR Pfam; PF15796; KELK; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00036; CNH; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF69322; Tricorn protease domain 2; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50219; CNH; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 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 Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW 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}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 77..343
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 344..414
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT DOMAIN 993..1043
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 1063..1183
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1209..1481
FT /note="CNH"
FT /evidence="ECO:0000259|PROSITE:PS50219"
FT REGION 624..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 661..680
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 920..954
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 106
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1596 AA; 180811 MW; FA35923AF501F091 CRC64;
MSGEVRLKKL EKLLLDGPVQ SAGQCCSVET LLDVLVCLYD ECSNSPLRRE KNVLEFLDWA
KPFTSKVKQM RLHRDDFEIL KVIGRGAFGE VAVVKVKNTD KVFAMKILNK WEMLKRAETA
CFREERDVLV NGDSQWITTL HYAFQDDNYL YLVMDYYVGG DLLTLLSKFE DRLPEEMARF
YLAEMVLAID SVHQLHYVHR DIKPDNILMD VNGHIRLADF GSCLKLTEDG TVQSSVAVGT
PDYISPEILQ AMEDGKGKYG PECDWWSLGV CMYEMLYGET PFYAESLVET YGKIMNHKER
FQFPPHVSDV SENAKDLIRR LICSREHRLG QNGIEDFKRH PFFSGIDWDN IRSCEAPYIP
EVSSPSDTSN FDVEDDCLKN SDTMPPPSHT TFSGHHLPFV GFTYTSHWSV IPRPSADSQR
FLSTSQPLEE SLATEAYERR LRRLEQEKLE LSRKLQESTQ TVQALQHSGG DGPVAASKEV
EIQSLKEEIE ALKKQIADSG RLEQQLEKAS SAHKDLEESS KHIKGLEKQV KSMNQEKDDF
QKELLEANNV LKSQAKELKE AHSQRKLAMQ EFSEMSERVT ELRSQKQRLS RQVRDREEEL
EGMSQKVEAL RLEVRKAERA RKEMEVQAEE RSEEAQKEKK LKERSDQFSR QLEEELEVLK
KQAGRAPGAG ASEQNQELGR LRTELEKKVA SYEEELSRRE MQHTGELKGL KKELRDAEAQ
HLTLKKEIMM LKDKLEKIRR ESQSEREEFK TEYKQKYERE RVLLSEENKK LSGELEKITS
MVETLGSTNR QLEEEMRDVA DKKESVAHWE AQITEIIQWV SDEKEARGYL QALATKMTEE
LESLALLRPP HPVLRCPRPV PGRDPDRLPR TSFLQDMPWK MRRFAKLDMS ARLELQSALD
AEIRAKQAIQ DELNKVKASS MSTECKLQDS ENRNQELMSE IEKLQKETEE LRTGKGESSL
GERGASPLHH PCHASSLSCR LWPPCTLHCT PKAHQFVVKT FSVPTKCKQC TSVMVGLMRQ
GCVCEACSFS CHVTCADKAP AVCPVPLDQT KGPLGVDPQK GTGTIFEGHV RVPKPAGVKK
GWQRAVAVVC DFKLFLYDLA EGKASQPGVM VSQVIDMRDE EFSVSSVSAS DVIHASRKDI
PCIFRVTASQ LSTSSRRKCS ILFLADSDLE RKKWVEILNE IHRLLRKSKL KERFVYVPKE
AYDSTLPLIK TAQSATIIDH ERIALGNEEG LYVIHITKDE IIRIGDNKKV HHMEQLPSEQ
LLAVISGRNR HVRLFPMSAL DGREVDFHKL PETRGCQALA SGPLRRGALV CLCVAMKRQV
LCYELSRGRT RHRKLREIQA PASVQWMALM GERLVVGYQG GFARYSLHGE AAPVSLLHPE
DTTLGFVGQL GLDALCAVSV SSKEFLLCFS GVGVYVDAHG RRSRQQELMW PAVPTSCCYN
APYLSVYSEN AVDVFDVNTM EWIQTIPLKK VGVGAGPACV FGWGWGGSQG STTHQCFFNP
VFKNLRWSTF LLPPSSLPHS SHFCWELGGT QSAACLGAPR TGFRNTALHA CLPASQVRPL
NMDGSLNVLG LETVRLVYFK NKMAGMSGFP ASCCFR
//
