ID A0A1S3M8G5_SALSA Unreviewed; 846 AA.
AC A0A1S3M8G5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=LOC106571124 {ECO:0000313|RefSeq:XP_013999289.1};
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_013999289.1};
RN [1] {ECO:0000313|RefSeq:XP_013999289.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_013999289.1};
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 -!- SUBCELLULAR LOCATION: Cell projection, dendrite
CC {ECO:0000256|ARBA:ARBA00004279}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. SNF1 subfamily. {ECO:0000256|ARBA:ARBA00006234}.
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DR RefSeq; XP_013999289.1; XM_014143814.1.
DR AlphaFoldDB; A0A1S3M8G5; -.
DR GeneID; 106571124; -.
DR OrthoDB; 5475340at2759; -.
DR Proteomes; UP000087266; Chromosome ssa15.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd12196; MARK1-3_C; 1.
DR CDD; cd14072; STKc_MARK; 1.
DR CDD; cd14407; UBA_MARK3_4; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR Gene3D; 3.30.310.80; Kinase associated domain 1, KA1; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR028375; KA1/Ssp2_C.
DR InterPro; IPR001772; KA1_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR049508; MARK1-4_cat.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR015940; UBA.
DR PANTHER; PTHR24346; MAP/MICROTUBULE AFFINITY-REGULATING KINASE; 1.
DR PANTHER; PTHR24346:SF1; MAP_MICROTUBULE AFFINITY-REGULATING KINASE 3; 1.
DR Pfam; PF02149; KA1; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00627; UBA; 1.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00165; UBA; 1.
DR SUPFAM; SSF103243; KA1-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50032; KA1; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50030; UBA; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000313|RefSeq:XP_013999289.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW Transferase {ECO:0000313|RefSeq:XP_013999289.1}.
FT DOMAIN 76..334
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 353..392
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT DOMAIN 797..846
FT /note="KA1"
FT /evidence="ECO:0000259|PROSITE:PS50032"
FT REGION 397..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 591..751
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..449
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..479
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..533
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 591..639
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..701
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 705..751
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 105
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 846 AA; 93969 MW; CDC52655D0C132C5 CRC64;
MNCHQHKTGQ AVCSDAIQIA NARMKGSHSV KRHRITIHTS HTDGRNEVTT RPVRSGARCR
NSIASCADEQ PHIGNYRLLK TIGKGNFAKV KLARHILTGR EVAIKIIDKT QLNPTSLQKL
FREVRIMKIL NHPNIVKLFE VIETEKTLYL VMEYASGGEV FDYLVAHGRM KEKEARAKFR
QIVSAVQYCH QKHIVHRDLK AENLLLDADM NIKIADFGFS NEFVMGSKLD TFCGSPPYAA
PELFQGKKYD GPEVDVWSLG VILYTLVSGS LPFDGQNLKE LRERVLRGKY RIPFYMSTDC
ENLLKRFLVL NPAKRGTLEV REEGQNQIMK DRWINAGCEE DEMKPFVEPE TDITDQKRID
IMVGMGYTRE EVTESLTRMK YDEITATYLL LGRKSTELEA SDSSSSSNLS LAKARPASEH
NNNGQSPAHL KAQRSISGTQ KQRRYSDQAG PSIPSVGYPK RSQTTSDDNG DHKEDGGAQP
RKSVSSGGRG GSGAPASPLL GNANNPNKAD IPDHKKGSTT PSTNSTSGGM RRRNTYVCSE
RNASDRNSVI QNGKENSMSE MLAACATSPS AYAKALTVSS ASVRLRHQKA ASLSASGHTC
RQTLPPTDGD FFRPNTSTTS GQRNPGGSST HSISSSATPP DRLRFPRGTA SRSTFHGGQL
RERRTATYNG PPASPTLSHD ATPLSQSRSR GTTNLFTKLT SKLTRRGPAE FERNGRLESS
SRNMSGDQKE DQQHPQPPHG QHPKDTKPRS LRFTWSMKTT SSMEPHDMMR EIRKVLDANN
CDYEQRERFL LLCVHGDGHA ESLVQWEMEV CKLPRLSLNG VRFKRISGTS IAFKNIASKI
ANELKL
//
