ID A0A1S3N3S2_SALSA Unreviewed; 1135 AA.
AC A0A1S3N3S2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=slk {ECO:0000313|RefSeq:XP_014010133.1};
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_014010133.1};
RN [1] {ECO:0000313|RefSeq:XP_014010133.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014010133.1};
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};
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DR RefSeq; XP_014010133.1; XM_014154658.1.
DR AlphaFoldDB; A0A1S3N3S2; -.
DR Ensembl; ENSSSAT00000148816; ENSSSAP00000113755; ENSSSAG00000078992.
DR GeneID; 106577016; -.
DR CTD; 568838; -.
DR OrthoDB; 2880940at2759; -.
DR Proteomes; UP000087266; Chromosome ssa18.
DR Bgee; ENSSSAG00000078992; Expressed in head kidney and 14 other cell types or tissues.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR022165; PKK.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR46538:SF1; NON-SPECIFIC SERINE_THREONINE PROTEIN KINASE; 1.
DR PANTHER; PTHR46538; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF12474; PKK; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000313|RefSeq:XP_014010133.1};
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 34..292
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 317..667
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 680..699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 733..905
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 934..965
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1024..1081
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 351..366
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..382
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..405
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..430
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..498
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..557
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..580
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 611..625
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 640..656
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 63
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1135 AA; 130858 MW; 8B96B149F377E628 CRC64;
MSFFNFRKIF KLGSDKKKKQ YEHVHRDENP EEIWEIIGEL GDGAFGKVYK AQNKQTGTLA
AAKVIDTKTE EELEDYMVEI DILASCDHRY IVKLLDAFYY ESKLWILIEF CAGGAVDAVM
LELERPLTEP QIRVVCRQTL EALAYLHEIK VIHRDLKAGN ILFSQEGDIK LADFGVSAKN
TMTLQRRDSF IGTPYWMAPE VVMCETSKDR PYDYKADIWS LGVTLIELAQ IEPPNHEMNP
MRVLLRIAKA DPPTLMQPSR WSPEFNDFLR KALDKNVDRR WCTAQLLQHP FVSSVVDNKP
LRELIAEANA DVLEEIEEGK EEDEEEETEA TLVVPGHKRA PSDTSMASSE DEKLSETTST
LDSVTEKTEP ETAEDKASDK LSDEGLGTSV GDRAEVEKLN EVSDASNEDL VDGQVKPMEP
KPEESPAGKP EEIPDCQITI VPEAPSDTQE SVIVSEETGE EEKVEDGPPQ VFPKERVEVE
EKKTEEEEVK KEPIKEEPEV ILQPPTKFTD PGDQPRSALE EPGAVLTEVN AKPEETEKET
LVEEMTEEVK PEADGVTDIN TDTDLNEDTD NTESDVNTDA EVDAAEGSTE VSADTEAQRD
NNVIPVVILE EGTTDEREEK PPAEEAPSQD AVSESKTDQE STPVKSKPDV EKDSDSGSSS
AADSNSMDLN LSISSFLSKK AEAGSVSIQD TRRQKKTLKK TRKFMVDGVE VSVTTSKIVT
DNDTKNEEMR FLRRQELREL RLLQKEEHRA QQALSDKLQQ QREQIYRRFE QEMTGKKRQY
DQEVENLEKK QKQTIERLEQ DHTNRLRDEA KRIKAEQDKE LSKFQNMLKN RKKEGVAQIM
IQSFQLSSCA LFNAQMQDEQ EFLQKQQQEL DGALKKIIQQ HKHEIATIER DCLNHKQQLM
RAREAAMWEL EERHLQEKHQ LLKQQLKDQY FMQRHQLLKR HEKEMEQMQR YNQRLIEEIK
NRQAQERGRL PKIQRGDAKT RMAMFKKSLR ITSAPGTPEQ EREKIKQFAA QEEKRQKNER
LHQHQKHENQ MRDLQLQCDS NIRELQQLQN EKCHLLIEHE TQKLKELDEE HSQELQEWRE
KLRPRKKALE EEFTRKLQEQ EVFFKMSGES ECLNPTTQSR VSKFYPIPSV HNSGL
//
