ID A0A2Y9MWJ6_DELLE Unreviewed; 1317 AA.
AC A0A2Y9MWJ6;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=STK36 {ECO:0000313|RefSeq:XP_022423407.1};
OS Delphinapterus leucas (Beluga whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Delphinapterus.
OX NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022423407.1};
RN [1] {ECO:0000313|RefSeq:XP_022423407.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022423407.1};
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_022423407.1; XM_022567699.1.
DR Proteomes; UP000248483; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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:0016043; P:cellular component organization; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd14002; STKc_STK36; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
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; PTHR22983; PROTEIN KINASE RELATED; 1.
DR PANTHER; PTHR22983:SF6; SERINE_THREONINE-PROTEIN KINASE 36; 1.
DR Pfam; PF13646; HEAT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF48371; ARM repeat; 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_022423407.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000248483};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 4..254
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 309..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..324
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..345
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 33
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1317 AA; 144386 MW; B39D8697CB1070BC CRC64;
MEKYHVLEMI GEGSFGRVYK GRRKYSAQVV ALKFIPKLGR SEKELRNLQR EIEIMRGLRH
PNIVHMLDSF ETDKEVVVVT DYAEGELFQI LEDDGKLPEE QVQAIAAQLV SALYYLHSHR
ILHRDMKPQN ILLAKGGGIK LCDFGFARAM STNTMVLTSI KGTPLYMSPE LVEERPYDHT
ADLWSVGCIL YELAVGTPPF YTTSIFQLVS LILKDPVRWP PTISPCFKNF LQGLLTKDPR
QRLSWPDLLH HPFIAGRVTI LTESAGPDLG TPFTSRLPPE LQVLKDQQAH RLAPKGNRSR
ILRQAYKHMA EEAKQKKHQN TGPALEQEDR TSKVASGTAS LPRLKATPQE PSLLTGVLGS
EMKSSWAEWR AGEAPPAPWE NWITQDCEQA FPELRPEVVG QQSLDAVDLE NEEPDNDDAE
WRHLLETTEP VPVQLKAPLA LLCNPDFCQR IQSQLHEAGG QILKGVLEGA SHILPVLRVL
SSLLSSCGGD SVSLYSFCRG AGLPRLLLSL LRHSQESSSI QQQRWYGTFL RDLMAVIQAY
FACTFNLERS QTGDSLQVFQ EAADLFLELL GKLLAQPDDS EQTLRRDSLM CFTVLCEAMD
GNSWTISRAF YSSLMTTQRA VLDGLLHGLT VPQLPFHSPP GAPEVSQPLR EQSEDLPGAL
SSALAALCTA PVGLPGLWEA KEQISRHLAN QLTEDSNQLR SCLISGLQHP ILCLHLLKVL
YSCCRVSEPL CRLLGQEPLA LESLWKLVQG KVKVVDWEES AEVTLYLLSL LVLHLQDLPS
GMEKLGSEVA TVFTHSHVVS LVSAAACLLG QLGQQGVTFD LQPVEWIAAA THALSAPAEV
RLTPPGGCGF YDGLLMLLLQ LFTQQGKGNP ISVVASSEMW TVLWHRFSMV LRLPEEASVQ
EEELSLSSPQ SPEPDWTLIS PQGMAALLSL AMATFTQEPQ LCLSYLSQRG SILMSTLKHL
LSPSFLHHLT QAPQGPEFLP VVVLSVCQLL CFPFALDVDA DLLEGVLADL TDSEVTAHLL
QVCRHHLPLT QAELPISLLT RLALSEPPSL NQFVSTVAAC PTTTISFLSA ALLGDQPLLT
SDLLSLLAHT ARVLSPSHLS FIQELLAGPD ESYRPLRSLL GHPENSVRAR TYGLLGHLLQ
HSGALRGALQ SQLGLLNLLL LGLGDKDPAV RRGASFAVGN AAYQAGPLGP ALAAAVPSMT
QLLGDPQAGI RRNAASALGN LGPEGLRDEL LRCQVPQRLL EVACGDPQPN VKEAALVALR
SLQQEPCIHQ VLVSLGASEK LALLSLGNQL LPRSSPRPAS AKHCRKLIHL LRPTHNT
//
