ID A0A1S3NZA9_SALSA Unreviewed; 1242 AA.
AC A0A1S3NZA9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=LOC106582256 {ECO:0000313|RefSeq:XP_014020620.1};
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_014020620.1};
RN [1] {ECO:0000313|RefSeq:XP_014020620.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014020620.1};
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_014020620.1; XM_014165145.1.
DR AlphaFoldDB; A0A1S3NZA9; -.
DR GeneID; 106582256; -.
DR OrthoDB; 2904475at2759; -.
DR Proteomes; UP000087266; Chromosome ssa21.
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_014020620.1};
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_014020620.1}.
FT DOMAIN 25..289
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 929..1216
FT /note="CNH"
FT /evidence="ECO:0000259|PROSITE:PS50219"
FT REGION 303..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 400..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 584..659
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 677..747
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 766..816
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..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 588..606
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..659
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 680..709
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 724..744
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 779..800
FT /note="Acidic 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 1242 AA; 141089 MW; 476C4E03E87A2322 CRC64;
MANESPAKSL VDIDLAALRD PAGIFELVEV VGNGTYGQVY KGRHVKTGQL AAIKVMDVTE
DEEEEIKLEI NMLKKYSHHR NIATYYGAFI KKSPPGHDDQ LWLVMEFCGA GSITDLVKNT
KGNTLKEDWI AYISREILRG LAHLHAHHVI HRDIKGQNVL LTENAEVKLV DFGVSAQLDR
TVGRRNTFIG TPYWMAPEVI ACDENPDATY DYRSDLWSTG ITAIEMAEGA PPLCDMHPMR
ALFLIPRNPP PRLKSKKWSK KFCSFIEGSL VKNYTQRPPT DQLLKHPFIR DQPNERQVRI
QLKDHIDRTK KKRGEKDETE YEYSGSEEEE EEAQEQEGEP SSIVNQPGES TLRRDFIRLQ
QENKERSEAL RRQQLLQEQQ LREQEEYKRQ LLAERQKRIE QQKEQRRRLE EQQRREREMR
RQQEREQRRR EQDDKRRMEE VERRRKEEEE RRRAEEEKRR ADREQEYIRR QLEEEQRHLE
ILQQQLLHEQ AMLLVRPNSA DERYRKNIQG SPQAAQVKVQ PPVPPRAAET MANGNAPIAV
QPAMQRPMEP QVQWSHLAAS PVVSCSHSFS EPIVPSFAHL HLCSQEQHHH PAPSSPARTD
PQSNPQPKAL PLDKAPTDDT PPRVPVRTTS RSPVLSRRDS PLHGNSNATP NNPAGQRNTC
SAAAEPRLLW ERVEKLVPRP TSGSGSTCSS SGSSNSSSQP SSHSGSGERF RARSSSKSEG
SPLQHPEHAG KKPEERKESV RTNRLAGEVD LTALAKELRV VEDVQRPHKV TDYSSSSEES
GTTDEDEDDE EVDQEGGEES TSGPEDSHAV SSRLSNGEME SVKILIVHDK GESDCKDDTL
IVRPSHSVSN TMQKHKSSSS FTPFIDPRLL QVSTSGAALN NLAFGNDARL AEALRADPSR
KGSVVNVNPV NTRPQSDTPE IRKYKKRFNS EILCAALWGV NLLVGTESGL MLLDRSGQGK
VYPLISRRRF QQMDVLEGLN VLVTISGKKN KLRVYYLSWL RNKILHNDPE VEKKQGWVTV
GDLEGAVHYK VVKYERIKFL VLALKNSVEV YAWAPKPYHK FMAFKSFGDL VHKPLLVDLT
VEEGQRLKVI YGSSNGFHAV DVDSGAVYDI YLPTHIQTSI QSHAIIILPN TDGIELLVCY
EDEGVYVNTY GRITKDVVLQ WGEMPTSVAY IRSNQIMGWG EKAIEIRSVE TGHLDGVFMH
KRAQRLKFLC ERNDKVFFAS VRSGGASQVY FMTLGRTSLL SW
//
