ID A0A1S3LPG6_SALSA Unreviewed; 2403 AA.
AC A0A1S3LPG6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=LOC106567657 {ECO:0000313|RefSeq:XP_013992720.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_013992720.1};
RN [1] {ECO:0000313|RefSeq:XP_013992720.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_013992720.1};
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=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. {ECO:0000256|ARBA:ARBA00009903}.
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DR RefSeq; XP_013992720.1; XM_014137245.1.
DR GeneID; 106567657; -.
DR CTD; 375449; -.
DR OrthoDB; 2915765at2759; -.
DR Proteomes; UP000087266; Chromosome ssa01.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion 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; cd00992; PDZ_signaling; 1.
DR CDD; cd05609; STKc_MAST; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 1.20.1480.20; MAST3 pre-PK domain-like; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR037711; MAST.
DR InterPro; IPR015022; MAST_pre-PK_dom.
DR InterPro; IPR023142; MAST_pre-PK_dom_sf.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24356:SF224; MICROTUBULE-ASSOCIATED SERINE_THREONINE-PROTEIN KINASE 4; 1.
DR PANTHER; PTHR24356; SERINE/THREONINE-PROTEIN KINASE; 1.
DR Pfam; PF08926; DUF1908; 1.
DR Pfam; PF17820; PDZ_6; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF140482; MAST3 pre-PK domain-like; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|RefSeq:XP_013992720.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 369..642
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 643..716
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT DOMAIN 932..1015
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 88..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 137..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 719..745
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 824..861
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 899..920
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1026..1193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1215..1248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1328..1377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1392..1442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1645..1806
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1829..1889
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2020..2403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 722..736
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1029..1045
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1062..1132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1167..1181
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1328..1346
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1347..1377
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1398..1428
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1651..1665
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1727..1763
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1779..1806
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1829..1883
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2020..2043
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2064..2081
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2090..2117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2148..2186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2217..2234
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2256..2272
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2273..2294
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2296..2334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2335..2351
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2375..2403
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2403 AA; 263660 MW; F13EC8C3FB146549 CRC64;
MDESSILRRR GLQKELSLPR RGSFCRTSNR KSLIGSGQSS VLPRPHSPLS SHTGTSPQDS
PRNFSPSASA HFSFARRTDG RRWSLASLPS SGYGTNTPSS TVSSSCSSQE KLHQLPFQPT
PDELHFLSKH FCTESIAGDD RRRGTAPMRP RSRSLSPGRS PSCCDHEIIM MNHVYKERFP
KATAQMEERI QEIIRTSSPE SVLPLADGVL GFAHHQIIEL VRDCLEKSRL GHVTSRYFCE
LTDKLEKLFQ ESTSRSESQE VTFIKELVKK ILIVIARPAR LLECLEFDPE EFYHLLEAAE
GHAKEGQGIK TDIPRYIISQ LGLTRDPLEE IAQMTSYDSG IAETPETDDS SQSLNAVLRS
RRKPCEIDFE MNKLISNGAY GAVYLVRHKE TKQRFAMKKI NKQNLMLRNQ IQQAFVERDI
LTFAENPFVV SMFCSFETRR HLCMVMEYVE GGDCANLLKN MGPLPVDMAK MYFAETVLAL
EYLHNYGIVH RDLKPDNLLV TSMGHIKLTD FGLSKVGLMN MTTNLYEGHI EKDAREFSDK
QVCGTPEYIA PEVILRQGYG KPVDWWAMGI ILYEFLVGCV PFFGDTPEEL FGQVISDEIN
WPEGEDAPPA DSQELITLLL RQNPLERMGT GGAYEVKHHQ FFHTLDWDSL LRQKAEFIPQ
LESEDDTSYF DTRSDRYHHL ETEEEEEDTN DEDFNVELRQ FSSCSHRFSK VYSSLDLSRG
QLEGKGEPEE KKSESPLTVD SLSWTPEFTE MPSLTQSSDT ESPSMGPRLL PKFAISAEDG
DEESLALRDP TKLAFSIEED EADATTPGST HSGATLSVGS FSEHLDLHPS RGEGLDSPDS
SSKTPMDPGG QHGGLRPDRH GEKHGVVAKV PKSVSASALS LMIPGDIFGV SPLASPISPY
SLSSDPSSRD SSPSRDSSLS VINPRHPIII HSSGKKFGFT LRAIPVYACD RDVYTVYHTV
WSVEDLGPAH KAGLKAGDLI THVNGETVHG LVHTEVVELL LKSGSRVAIS TTAFENTFIK
TGPARRNSYR SKMVRRTKKP KKEKTQERRR SVFRRFAMQP SPLLHTSRSF SSFNRSLSSG
ESLPVSPTHS MSPRSPTAAF RPTPDFNQSG GNSSQSSSPS SSAPNSPAGS GHIRPSTLHG
LGPKLTGQRL RQGRRKSVGS IPLSPLARTP SPTPQPTSPQ RSPSPLLSHG SMGISKTTQA
FPVKMHSPPT IVRHMARPKS AEPPRSPLLK RVQSEEKLSP SYTGDKKHMC SRKHNLEVTQ
EESQGEELMP GDRDHHTLQS LEETSCEPPA ITRVRPAEQG CLKRPVGRKV GRQESMEELE
KEKLKAKVVM KRQDWSERRE SLQKQDALQE SDMSGAEGGR SQGRSQGSET VSLEGKTAST
TVKDVLYKKL NTRASEGSPE PLVGNSSDSP LCSIHPDWSP QKTEWQLSRQ SKEGGKPDRL
DFKAPNMEFA RKRQSFEERE DCMCRLSPVI HESLHFGSTR SKSLQLDSAL ALDHVKGTMG
SVHSSPEGLN PKIFAGRGEG SAVEKLQLIS SSEGSLRKTS SEYKLEGRLV SSLKPLEGTL
DIGLLSGPRV SKTDTCLSKM SDSDMGSIGT PTWLQSPVER QVLIPLLKPS DKQKSPPTSI
LSPGAVVALS NPIPANEEAS ISNTGLKFSS SGEKPHDRPS HHEPPTALSK AEVSDFGGKQ
ESRSSMITHD HRAFRHSTHF SNCGKTPSIR EVSNEDQEEE VEPPQETPAP AQQNNTDISK
TSDTVVVPKT ESPKNTAASF PASKVEVQAT APHAAVPVKQ SSDCQSGPSY LQSNEKQRPA
ENTSSITTVV KYNLEQTSYL SKQQMVYSSP STVTTTQTSI PAPISSLGDV NRTSGQMSPR
QDATGKTQNS DKVQSNRPVL NKDSEPASVS AVEELKAANA ARDKMAEVRE TSPKVDVKCV
LSKGILDTAT AKTEATQRCC EDACPIGSQV AISSVAKQIR QGPTSPKTKG SIAKTGEREK
PYLTHRLAET EKTWVKGALG AEIRVPKKLT ADVNTKETSP VLIVKQSPPS PASTNQTTFN
PKTKPRSEGE RERYEVKTPT PVVNLGLDSK QQETTVSMVK EIPDSKQEEP LLKTSVQSHI
VKESSDSKLN KSLCQTPVPT PVVRHHSDPK QKEPELHTFA PTPAQVIKDN LDSKQKSPPH
KTSASTSMIS KQKEITTSTV RQIIDSKQKS PPHKTLAPTA TPVMKEPAPV LAAPQQQAQK
EPPTGASAPS QSTPVPVLPA LAMRREAHPP NGGALSGRAS GSTGQEAVVQ TSREDQGRPR
VEAPRSEGLR SDSHKSLGGV DTTGPTPTST SNSTPQAKHS KAESRVTNSD KQVACSEKEQ
ADKKKRESGQ EAASTQKNTK RETLRVATVV KEGSGSDKDS ARHKQTKESP RGPAKKGNAE
FKK
//
