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Database: UniProt
Entry: A0A2Y9JZW2_ENHLU
LinkDB: A0A2Y9JZW2_ENHLU
Original site: A0A2Y9JZW2_ENHLU 
ID   A0A2Y9JZW2_ENHLU        Unreviewed;       831 AA.
AC   A0A2Y9JZW2;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
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=LOC111152251 {ECO:0000313|RefSeq:XP_022366406.1};
OS   Enhydra lutris kenyoni (northern sea otter).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC   Lutrinae; Enhydra.
OX   NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022366406.1};
RN   [1] {ECO:0000313|RefSeq:XP_022366406.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_022366406.1};
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_022366406.1; XM_022510698.1.
DR   STRING; 391180.A0A2Y9JZW2; -.
DR   KEGG; elk:111152251; -.
DR   OrthoDB; 912242at2759; -.
DR   Proteomes; UP000248482; Unplaced.
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; 2.
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; PTHR47634; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR47634:SF4; SRSF PROTEIN KINASE 1; 1.
DR   Pfam; PF00069; Pkinase; 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};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|RefSeq:XP_022366406.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000248482};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          256..829
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..111
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          188..238
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          414..523
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          570..594
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          629..656
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        93..111
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        197..219
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        220..235
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        452..511
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         285
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   831 AA;  92844 MW;  88854AFED672E33A CRC64;
     MERKGERWIG LRHEGQRPAG RGPSQHXELS LTAAVRSPGV RRPPSEVAPP LTPRLWAAGP
     RPSAPASFRA GSHRPLFPSR PTRALGPLQG PALGEPDRPP PAGPLTRPVP PPAHPAWALL
     CAPWAARRPA GRLALAAALA PEPPLRRAPH PGLAPLLGLH PHLDCLLSST FALHPSLSPA
     VLALQARKKR TKAKKDKAQR KSEIQHRGSA PHSESDLPEQ EEEILGSDDD EQEDPNDYCK
     GGYHLVKIGD LFNGRYHVIR KLGWGHFSTV WLSWDIQGKK FVAMKVVKSA EHYTETALDE
     IRLLKSVRNS DPNDPNREMV VQLLDDFKIS GVNGTHICMV FEVLGHHLLK WIIKSNYQGL
     PLPCVKKIIQ QVLQGLDYLH TKCRIIHTDI KPENILLSVN EQYIRRLAAE ATEWQRSGAP
     PPSGSAVSTA PQPKPADKMS KNKKKKLKKK QKRQAELLEK RMQEIEEMEK ESGPGQKRPN
     KQEESESPVE RPLKENPPNK MTQEKLEESS TIDQDQTLME RGVEGGAAEI NCNGVIEIVN
     YTENSNKETL RLKEDLHNAN DCDVQNLKQE TSFLSSQNGD SSTSQETDSC TPVTSEVSDT
     MMCQASPNVD QSFSEQDISQ LQESIRAEIP CEDEHEQEQN GPLDNKGKST AGNFLVNPLE
     PKNAEKLQVK IADLGNACWV HKHFTEDIQT RQYRSLEVLI GSGYNTPADI WSTACMAFEL
     ATGDYLFEPH SGEEYTRDED HIALIIELLG KVPRKLIVAG KYSKEFFTKK GDLKHITKLK
     PWGLFEVLVE KYEWSQEEAA GFTDFLLPML ELIPEKRATA ADCLRHPWLN S
//
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