ID A0A1S3MNJ9_SALSA Unreviewed; 1387 AA.
AC A0A1S3MNJ9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 30.
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=LOC106573896 {ECO:0000313|RefSeq:XP_014004808.1};
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_014004808.1};
RN [1] {ECO:0000313|RefSeq:XP_014004808.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014004808.1};
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. {ECO:0000256|ARBA:ARBA00009903}.
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DR RefSeq; XP_014004808.1; XM_014149333.1.
DR OrthoDB; 2915765at2759; -.
DR Proteomes; UP000087266; Chromosome ssa16.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00992; PDZ_signaling; 1.
DR CDD; cd05609; STKc_MAST; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 1.20.1480.20; MAST3 pre-PK domain-like; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR037711; MAST.
DR InterPro; IPR015022; MAST_pre-PK_dom.
DR InterPro; IPR023142; MAST_pre-PK_dom_sf.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24356:SF140; MICROTUBULE-ASSOCIATED SERINE/THREONINE-PROTEIN KINASE 3; 1.
DR PANTHER; PTHR24356; SERINE/THREONINE-PROTEIN KINASE; 1.
DR Pfam; PF08926; DUF1908; 1.
DR Pfam; PF17820; PDZ_6; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF140482; MAST3 pre-PK domain-like; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50106; PDZ; 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};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|RefSeq:XP_014004808.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 333..606
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 607..679
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT DOMAIN 875..963
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 1..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 682..758
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 774..818
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 967..1125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1304..1387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 712..726
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 727..758
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 973..993
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1004..1045
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1055..1077
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1085..1125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1309..1324
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1387 AA; 154510 MW; D7A6FE6FCC6CF165 CRC64;
MQPLQPLTNP TSLELPEQQQ EESWRGDTVS HSVTPSLPTL RPHRAEGRRW SLASLPSSGY
GTNPPSSTVS SSSSSQERLH QLPYQPTQDQ LHFLFKHFRS SENVADEEVR PSPFIRPRSH
SLSPGRTMGS FDNEVVMMNH VYKERFPKAT VQMEERLLDI VTACSPDSTL PLSDGVLGFI
QHQLVELVRD CLDKSHTGLV TSRYFVELQD KLEKLLHEAY DRSESEEVSV ITQLVKKILI
IISRPARLLE CLEFDPEEFY HLLEAAEGHA KEGQGIKTDI PRYIINQLGL TRDPLEDMVQ
LEQSAPSMTV KFDVEQNKCP QTPTRRKPLE SDFETIKLIS NGAYGAVYLV RHRNTRQRFA
MKKINRQNLV LRNQIQQVFV ERDILTFAEN PFVVSMFCSF ETRRHLCMVM EYVEGGDCAN
LLKNMGPLPV DMTRMYFAET VLALEYLHNY GIVHRDLKPD NLLITSMGHI KLTDFGLSRV
GLMNMTTNLY EGHMEKDTRE FIDKQVCGTP EYIAPEVILR QGYGKPVDWW AMGVILYEFL
VGCVPFFGDT PEELFGQVVS DDITWPDGDE ALPADAQDMI TRLLRQSPLE RLGTGGAPEV
KQHPFFLHLD WNGLLRQKAE FIPQLEAEDD TSYFDTRSER YHHLASDEDD ETNDEESSLE
IRQFSSWSNR LSKVYSSTEH LATPSNLSFS SGHSEDKEGW DGCFTPSPGG DIHRQERQHQ
DRRGSLRPRA SSSSSQSERS ASPLVMSSTH SLETTPRFAF STDDEAEVVV SNLHRIRSNS
TGAKHSSPKD HGASRRFGNQ LETPDRQTPD SPRLGGKLPK CASVSALSLV ITADDMLGGL
QPSPILTRSL SSNPSSRDSS PSRDLSLSLS ILGPPIVIHS SGRKYGFTMQ AIRVYMGDSD
VYTVHHMVSS VEYGSPAHEA GLRAGDLITH VNGESVQGLV HTEIMELLLK SGGKVALQTT
ALENTSIKVG PARKTSHKGK MARRSKKSKR RDNQDRRRSV LKKLSKQSTV MHSSRSFNSG
LQHHSVSSSE SLPGSPTHSL SPGPSTPCRS PAPDHQAGDT NSPQSTSPSS LHGLASKLGT
QRYTKVGRRK STSSIPPSPL ACNSSTQPLS PQRSPSPLFG ITKTFHSKTL SPPTIVRHCL
RPRSAEPPHS PLLKRVQSAE RLSSAYHTDK KSYPHRRHTL EVPFQDEVEG VCGRGDHGRL
LVGYGGCQRL RDWASERSEQ LVVMRKLNLS ERRDSFKKQE AVQEVSFDEP DNQKTIPTVT
ATTLNAPGGN RVPQRAASWT SISQTSEELT VVKRFNVVPQ IAVQGLTESE DQDDWEPCSD
GEEDDGERQE PKYTDSNTAA GQGCLSHGKI SSKAPEVTAA LHKESPASDQ VGDTAVDSSP
QKGKLRK
//