ID A0A087YE06_POEFO Unreviewed; 1154 AA.
AC A0A087YE06;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 2.
DT 27-MAR-2024, entry version 54.
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:ENSPFOP00000016259.2, 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:ENSPFOP00000016259.2}
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; AYCK01001784; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AYCK01001785; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_007545373.1; XM_007545311.2.
DR AlphaFoldDB; A0A087YE06; -.
DR STRING; 48698.ENSPFOP00000016259; -.
DR Ensembl; ENSPFOT00000016281.2; ENSPFOP00000016259.2; ENSPFOG00000016103.2.
DR GeneID; 103133538; -.
DR CTD; 568838; -.
DR eggNOG; KOG0579; Eukaryota.
DR GeneTree; ENSGT00940000156184; -.
DR OMA; ESRMEHG; -.
DR OrthoDB; 2880940at2759; -.
DR Proteomes; UP000028760; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR022165; PKK.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR46538:SF1; NON-SPECIFIC SERINE_THREONINE PROTEIN KINASE; 1.
DR PANTHER; PTHR46538; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF12474; PKK; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000028760};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 34..292
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 312..741
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 775..843
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 867..916
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 952..986
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1043..1096
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 352..366
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..403
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..491
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 514..546
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..566
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..626
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..643
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 644..658
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 699..727
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 63
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1154 AA; 132745 MW; 3962D9059806ED41 CRC64;
MSFFNFRKIF KLGPDKKKKQ YEHVHRDVNP EEIWEIIGEL GDGAFGKVYK AQNKQNGTLA
AAKVIDTKTE DELEDYMVEI DILASCNHHH IVKLLDAFYF EGKLWILIEF CAGGAVDAIM
LELERPLTEP QIRVVCKQTL EALTYLHENK VIHRDLKAGN ILLSLDGEVK LADFGVSAKN
TNTLQRRDSF IGTPYWMAPE VVMCETSKDR PYDYKADIWS LGVTLIELAQ VEPPNHEMNP
MRVLLKIAKS EPPTLMHPSR WSPEFNDFLR RSLDKNVDNR WSSTQLLQHP FVTSVTDSRP
LRELIAEAKA EVTEEIEDGK EEEEEEEPDT PAAVPGHKRA PSDVSMASSE EDKVPPTPSN
LESVTEKTEA EPVEDRSSDK LSDEGLGTSE VDKTEDEKLN EVSASSEDLT PAPAETSKDL
DSAKVQLDVD QTEEISGEAA VSKPDEVVKS QKPPSEVEEA EELKEISEKM DMEEETIQDK
MELDEDKQQP GEGGAADSVE SQEIPEGTTA DEVAVGEEES KDLKEEITEH MKVTEDGIKN
ITDETVENVD ADNSQSTLID TKINGDMDSK SSVEESSTEA VLENRSTENQ SEETKDEVPE
ESEPPKQENE SKVEEELEER APSESNQVSD DVKVTSEVSE VISQDVSVKE DGEKGTQADE
VTSQDSVSVQ ESETDSESRM EQGSPAVTKS DVEKDSDSGS SSAADSNSLD LNLSISSFLS
KSKDGGSISM QESKRQKKTL KKTRKFLVDG VEVSVTTSKI VTDNDAKSEE MRFLRRQELR
ELRLLQKEEQ RAQQELSNKL QQQREQIYRR FEQETTAKKR QYDQEVENLE KKQKQTIERL
EQDHTSRLRD EAKRIKADQD KELSKFQNML KNRKKEEQEF LQKQQQELDG ALKKIIQQHK
LEIATIERDC LNHKQQLLRA REAAMWELEE RHLQEKHQLL KQQLKDQYFM QRHQLLKRHE
KEMEQMQRYN QRLIEELKNK QNQERVRLPK IQRSDAKTRM AMFKKSLRIT VVAAMTPDQE
RERIKQFAAQ EEKRQKNERL HQHQKHENQM RDLQLQCDSN IRELQQLQNE KCHLLIEHET
QKLKELDEEH SQEIKDWREK LRPRKKALEE EFTRKLQEQE VFFKMSGESE CLNPTTQSRV
SKFYPIPNLQ NSGL
//
