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Database: UniProt
Entry: A0A1S3RMA2_SALSA
LinkDB: A0A1S3RMA2_SALSA
Original site: A0A1S3RMA2_SALSA 
ID   A0A1S3RMA2_SALSA        Unreviewed;      1278 AA.
AC   A0A1S3RMA2;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
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=LOC106603600 {ECO:0000313|RefSeq:XP_014052952.1};
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_014052952.1};
RN   [1] {ECO:0000313|RefSeq:XP_014052952.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_014052952.1};
RG   RefSeq;
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   -!- 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_014052952.1; XM_014197477.1.
DR   AlphaFoldDB; A0A1S3RMA2; -.
DR   GeneID; 106603600; -.
DR   CTD; 50488; -.
DR   OrthoDB; 2904475at2759; -.
DR   Proteomes; UP000087266; Chromosome ssa04.
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   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}; Kinase {ECO:0000313|RefSeq:XP_014052952.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          25..289
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          965..1252
FT                   /note="CNH"
FT                   /evidence="ECO:0000259|PROSITE:PS50219"
FT   REGION          307..438
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          474..562
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          580..653
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          669..883
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        321..335
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        355..371
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        378..438
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        474..488
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        517..548
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        584..600
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        627..641
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        694..709
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        747..769
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        798..821
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        846..882
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   1278 AA;  145495 MW;  3FDD1D78FEFA857F CRC64;
     MSENAPTRSL DDIDLAALRD PAGIFELVEV VGNGTYGQVY KGRHVKTGQL AAIKVMDVTE
     EEEEEIKAEI NMLKKYSHHR NIATYYGAFV KKSPPGHDDH LWLVMEFCGA GSVTDLVKNT
     KGNSLKEDWI AYICREILRG LSHLHQHKVI HRDIKGQNVL LTENAEVKLV DFGVSAQLDR
     TVGRRNTFIG TPYWMAPEVI ACDENPDSTY DYRSDIWSLG ITAIETAEGA PPLCDMHPMR
     ALFLIPRNPP PKLKSKKWSK KFIDFIEGCL VKTYTSRPST EQLLKHSFIR DQPTERQVRI
     QLKDHIDRTR KKRGEKEETE YEYSGSDEED ENRGEDGESS TSILNVPGES TLRRDFLRLQ
     QENKERSEAL KRQQAQLAAQ RRDPEEHKRQ LLHDRQKRIE EQKEQRRRLE EQQRKEREMV
     RQQEKGPHRR LDDIRREEDR RLAEREQEYK RKQLEEQRQS ERLQRQLQQE HAYLVSLQQQ
     QQDKKPQPLY HYSKNVEPNN KPAWAREVEE RSKLNRQGSP KICNTVSDTA IQSRSDSISQ
     SGGGQAAQTP PMQRPVEPQG GQGKFQMAHL VPLKPYAAPV PRSQSLCDQP TKTMSAFPTQ
     DPSPTPRPVH SRELVRQNSD PTSESPAPQP RKREDRGPWI RLPEIEQPPK IPQRTASIAT
     ALNTNLSSGI RHPVRASNPD LSRNDRWERG DSMNLVSNLP QTGSLERHRI LSSSKIDSPI
     LGHDGRMTGH KPGESRTSSR PSRPASYKRA IGEDHGLYAK ERPEEQPRPP VKANDYSSSS
     EGSESSEESE SGEGNEEEDS PTDRPRDADT DSVNTMVVHE EEEEGEGGEE GQAGVYRDQT
     MLVQRTPEKR SHNGYTNLPD VVQPSHSPTD SASHSSPGKD SVYDYQSRGL VKASSGKSSF
     TTFVDLGMYQ PPGDTADAIS VGSLGSRFEQ LKMEVRKGSM VNVNPTNTRP HSDTPEIRKY
     KKRFNSEILC AALWGVNLLV GTENGLKLLD RSGQGKVYPL INSRRFQQMD VLEGLNLLIT
     ISGKKNKVRV YYLAWLRNKI LHNDPEVEKK QGWTTVGEME GCVHYKVVKY ERIKFLVIAM
     KNAVEVYAWA PKPYHKFMAF KSFGDLPHRP QLVDLTVEEG QRLKVIYGSI AGFHAIDVDS
     GNNYDIYIPV HIQCQIMPHA IVFLPSSDGM EMLLCYEDEG VYVNTYGRII KDVVLQWGEM
     PTSVAHICSN QIMGWGEKAI EIRAVETGHL DGVFMHKRAQ RLKFLCERND KVFFASVRSG
     GSSQVYFMTL NRNCIMNW
//
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