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Database: UniProt
Entry: A0A1S3MVQ6_SALSA
LinkDB: A0A1S3MVQ6_SALSA
Original site: A0A1S3MVQ6_SALSA 
ID   A0A1S3MVQ6_SALSA        Unreviewed;      1537 AA.
AC   A0A1S3MVQ6;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
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=LOC106575325 {ECO:0000313|RefSeq:XP_014007267.1};
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_014007267.1};
RN   [1] {ECO:0000313|RefSeq:XP_014007267.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_014007267.1};
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   -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC       protein kinase family. STE20 subfamily.
CC       {ECO:0000256|ARBA:ARBA00008874}.
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DR   RefSeq; XP_014007267.1; XM_014151792.1.
DR   OrthoDB; 2904475at2759; -.
DR   Proteomes; UP000087266; Chromosome ssa17.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd06636; STKc_MAP4K4_6_N; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR001180; CNH_dom.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR47096:SF1; CNH DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR47096; MISSHAPEN LIKE KINASE 1; 1.
DR   Pfam; PF00780; CNH; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00036; CNH; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50219; CNH; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 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, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|RefSeq:XP_014007267.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022777,
KW   ECO:0000313|RefSeq:XP_014007267.1}.
FT   DOMAIN          25..289
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          1224..1511
FT                   /note="CNH"
FT                   /evidence="ECO:0000259|PROSITE:PS50219"
FT   REGION          305..351
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          399..466
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          533..1083
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1097..1128
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        305..320
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        321..337
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        553..568
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        581..645
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        658..690
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        837..866
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        886..919
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        924..939
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        972..992
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1046..1063
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         54
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1537 AA;  172359 MW;  0D9B478D14C283D4 CRC64;
     MANDSPAKSL VEIDLASLRD PAGIFELVEV VGNGTYGQVY KGRHVKTGQL AAIKVMDVTE
     DEEEEIKLEI NMLKKYSHHR NIATYYGAFI KKSPPGHDDQ LWLVMEFCGA GSITDLVKNT
     KGNQLKEDWI AYISREILRG LAHLHAHHVI HRDIKGQNVL LTENAEVKLV DFGVSAQLDR
     TVGRRNTFIG TPYWMAPEVI ACDENPEATY DYRSDLWSTG ITAIEMAEGA PPLCDMHPMR
     ALFLIPRNPP PRLKSKKWSK KFCSFIEGSL VKNYNQRPPT EQLLKHPFIR DQPNERQVRI
     QLKDHIDRTK KKRGEKDETE YEYSGSEEEE EDAGEQEGEP SSIVNMPGES TLRKDFIRLQ
     QENKERSEAL RRQQLLQEQQ LREQEEYKRQ LLAERQKRIE QQKEQRRRLE EQQRREREMR
     RQQEREQRRR EQEEKRRMEE MERRRKEDDE RRRAEEEKRR SDREQEYIRR QLEEEQRHLE
     ILQQQLLHEQ AMLLPRTLHQ EFKWRELEEQ RKAERLHKRL QQEQAYLLSL QHDNKPPQQT
     QPPQPCQKTK DPKGMSPDST SKAPQTTSPG PVGDRAPAPQ PHFLNNSNAI ASRRTSCDNT
     RSPQAHFLDN VTANAPRRMS SDTTKSPQTT SRDNTTKAPQ KPSPNSVDKD SEKTPSDHSD
     ALATQSTDVT KPSQTGVLDG PKSPQTDRSE PSGALGDPRP IREADERFRK NIQGSPQTAP
     PTKQPPVPPR SEPFSNGGSS ESVPPAMHRP MEPQVQWSHL AALKSSSAAP PPVVSRSHSF
     SEPAVPSFAH LHLRSQEPHS HHHHPSAAAP SAARTDPQPP ASGPSDEVPP RVPVRTTSRS
     PVLSRRDSPL QASAPPSNQA VQRNAGSNAE PRLLWDRVEK LVPRPGSGSS SGSSNSSSQA
     GSGERFRARS SSKSEGSPLQ RPDNAAKKPD DKKDFARPNR PADLTALAKE LRAVDDVRPP
     NKVTDYSSSS EESGTTDEDD DEEVDQDAAD ESTSGAEDTR AGRGLSNGET ASLKTLLAHD
     DSENDLTTPS KDGTLVIRQS AGDKKRPAVN VSSSSSGPSV AHGQAVQVHT PPGPGNGHQE
     KNGFAGRIHL LPDLIQQSHH SPTSSSSSIS NSPSSSSSHV SPAMSPQTPL DKLTAIETQS
     ASNTMQKHKS SSSFTPFIDP RLLQVSPSSG SSLNNMAAFG NDGRLVDALR ADPSRKGSVV
     NVNPVNTRPQ SDTPEIRKYK KRFNSEILCA ALWGVNLLVG TESGLMLLDR SGQGKVYPLI
     SRRRIQQMDV LEGLNVLVTI SGKKNKLRVY YLSWLRNKIL HNDPEVEKKQ GWVTVGELEG
     CVHYKVVKYE RIKFLVLALK NSVEVYAWAP KPYHKFMAFK SFGDLVHKPL LVDLTVEEGQ
     RLKVIYGSSN GFHAVDVDSG AVYDIYLPTH IQTNIQSHAI IILPNTDGIE LLVCYEDEGV
     YVNTYGRITK DVVLQWGEMP TSVAYIRSNQ IMGWGEKAIE IRSVETGHLD GVFMHKRAQR
     LKFLCERNDK VFFASVRSGG SSQVYFMTLG RTSLLSW
//
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