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
//