ID A0A1S3NZ89_SALSA Unreviewed; 901 AA.
AC A0A1S3NZ89;
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=nek5 {ECO:0000313|RefSeq:XP_014020600.1};
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_014020600.1};
RN [1] {ECO:0000313|RefSeq:XP_014020600.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014020600.1};
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. NEK Ser/Thr
CC protein kinase family. NIMA subfamily. {ECO:0000256|ARBA:ARBA00010886}.
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DR RefSeq; XP_014020600.1; XM_014165125.1.
DR AlphaFoldDB; A0A1S3NZ89; -.
DR STRING; 8030.ENSSSAP00000061671; -.
DR PaxDb; 8030-ENSSSAP00000061671; -.
DR GeneID; 106582247; -.
DR KEGG; sasa:106582247; -.
DR OrthoDB; 198307at2759; -.
DR Proteomes; UP000087266; Chromosome ssa21.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
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; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR44899; CAMK FAMILY PROTEIN KINASE; 1.
DR PANTHER; PTHR44899:SF1; SERINE_THREONINE-PROTEIN KINASE NEK5; 1.
DR Pfam; PF00069; Pkinase; 1.
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 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_014020600.1};
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 4..263
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 308..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 451..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 519..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 601..672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 712..802
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 838..901
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..345
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..585
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 601..630
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 743..759
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 760..800
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 859..881
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 882..901
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 901 AA; 103398 MW; 1289223D9444DB8F CRC64;
MNQYEVVHQI GEGAFGKAFL ALDRDRDWGG ESQCVVKEIN LRKMSPMEKE ASKKEVMLLA
KMKHPNIVTF FKSFQESTNL YIVMEYCDGG DLMKKISMQR GVMFTEEQIV DWFVQICLGL
KHIHDRKVLH RDIKAQNIFL TKKGMKAKLG DFGIARMLNN TMELARTCVG TPYYLSPEIC
DNRPYNNKTD IWSLGCVLYE LCTLRHPFEG NSLRQLVVKI CTGRYNPVST RYSYDLRLLV
TQLFKVSPRD RPSVNSVLKR PFLEKHISKH LDPQVIEDEF SHTVLHRKRA AGPLPRVRAA
PVQITEIVPK ARVSERPPPR SKPGPSVKKP PPKPDWKPPT RVMPQHKPFH PRAAQIRVPV
ARQYGQQNPR WDGQAEVNPY DHYYAQLDAI QRRYSPLPPR PPLPSCHPPV VQERPVERYD
DRQNHPEPYQ LVAAACNEYR QRRQEANQYK LRAEKQLGLR PSTADAERYR QPEQDQGAAR
PAHPPTPHDR RQDGQQEYLR KLQHIRQQYY SEMRDIRMRA DAETQPPVKP GTYLVEKPGH
TEPPTHSGDQ DRDRPQPDQD IEGALRQIRQ ENRLERRELQ KKHKDKKAIM FEIKLNDARI
QEDEEKEKEE KRDEERIVED KREDEKEVDP LNQTLSFQAG EELRHRDWSG AGLGAGQDEG
TPRSEVRKGW GQAAPQTLLD ALAEMDVSSV CTTMAVPELG DAADLEGKAI GERRQWGAGP
PNTLLHALGQ AELTSTLDSV MPEPLTEKDR AKEPEKEGAE TEEKVEEDED SDVEMDEERL
EPRSDDDDTN FEESEDELRE EVAESMFNLF IMEDGESVKE EEGEKVVTDG VVGEIELDSQ
ETVDLQQRHP VIEPTGYTSI EGKPSQTQVQ AAGCETRAEQ PRNTQASDED CEASKKQQPE
H
//
