ID A0A096LPP0_POEFO Unreviewed; 573 AA.
AC A0A096LPP0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
OS Poecilia formosa (Amazon molly) (Limia formosa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000021131.1, ECO:0000313|Proteomes:UP000028760};
RN [1] {ECO:0000313|Proteomes:UP000028760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA Schartl M., Warren W.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPFOP00000021131.1}
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};
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DR EMBL; AYCK01005084; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A096LPP0; -.
DR Ensembl; ENSPFOT00000029172.1; ENSPFOP00000021131.1; ENSPFOG00000003901.2.
DR GeneTree; ENSGT00940000155656; -.
DR Proteomes; UP000028760; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP 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; cd02677; MIT_SNX15; 1.
DR CDD; cd05576; STKc_RPK118_like; 1.
DR Gene3D; 1.20.58.80; Phosphotransferase system, lactose/cellobiose-type IIA subunit; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR007330; MIT_dom.
DR InterPro; IPR036181; MIT_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR035053; STK_RPK118-like.
DR PANTHER; PTHR15508; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR PANTHER; PTHR15508:SF2; RIBOSOMAL PROTEIN S6 KINASE DELTA-1; 1.
DR Pfam; PF04212; MIT; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00745; MIT; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF116846; MIT domain; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000028760};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 145..566
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 315..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..330
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 573 AA; 62397 MW; 27255732D088E642 CRC64;
MASGSTSPNQ PQGEATNISS ICSPRLPSLR ERRTPSPAPV PASSAPNPEV SCPNRTPLFS
RSLRKTSGVN ATDVKSDYLD KASELIGFAV QKESEQDYQA AFLYYRSGVD LLLQGVQGEP
SASRREAVKK KTAEYLMRAE QISGLHLRSN MGQGSTQTVA FGAQCCSSSS RGGQQSPSDE
LIAYRVIGVI NKVLLVIDKR TQETFILKGL RKSSDCGQAK KTIMPLSVPH MVQLRKFIIS
EDTVFLLLHY AEGGKLWSHI GLQKEGEIPF MSPVKSAVPA GLRDQIGAQT DSGATSEEEC
TNSYLSLCNE YEQEKVEPDA LEEEVDERSE QEMLSLEVPN TTATASSYSR SLLSNDSLSS
PGGSQELGFF NLDGESSGVN KATGGSDFDK EVSRLFAELD ELSLAATQAH IPEEFVRCWA
VEIVTALDCL HQEGIICRDL NPNNILLDHQ GHVQLTYFCS WCDVEESCDK EAMANMYCAP
EVGGISEETP SCDWWSLGAI LFELLTGTSL LSCHPAGIGR HTALNIPECV SEEARSLLEQ
LLQYNPMERL GAGVGGVDDI KSHPFFATVD WAK
//
