ID A0A2Y9LSK4_DELLE Unreviewed; 765 AA.
AC A0A2Y9LSK4;
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=SRPK2 {ECO:0000313|RefSeq:XP_022410072.1};
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_022410072.1};
RN [1] {ECO:0000313|RefSeq:XP_022410072.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022410072.1};
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_022410072.1; XM_022554364.1.
DR AlphaFoldDB; A0A2Y9LSK4; -.
DR STRING; 9749.A0A2Y9LSK4; -.
DR KEGG; dle:111164614; -.
DR InParanoid; A0A2Y9LSK4; -.
DR OrthoDB; 912242at2759; -.
DR Proteomes; UP000248483; 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; 3.
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:SF6; SRSF PROTEIN KINASE 2; 1.
DR Pfam; PF00069; Pkinase; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF101447; Formin homology 2 domain (FH2 domain); 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_022410072.1};
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 127..763
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 285..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 374..552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..89
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..106
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..416
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..465
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..482
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..549
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 156
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 765 AA; 86477 MW; 0FBECBF5AD1622DF CRC64;
MGMQGCRGAK GEKRPREERW CETRGGAGQG RAHGEAGGAT RRVLAIQARK RRPKREKHPK
KPEPQQKAPL VPPPPPPPPP PPLADPAPPE PEEEILGSDD EEQEDPADYC KGGYHPVKIG
DLFNGRYHVI RKLGWGHFST VWLCWDMQGK RFVAMKVVKS AQHYTETALD EIKLLKCVRE
SDPTDPNKDM VVQLIDDFKI SGMNGIHVCM VFEVLGHHLL KWIIKSNYQG LPVRCVKSII
RQVLQGLDYL HSKCKIIHTD IKPENILMCV DDAYVRRMAA EATEWQKAGA PPPSGSAVST
APQQKPIGKI SKNKKKKLKK KQKRQAELLE KRLQEIEELE REAERKIIEE NVTSAVPSNE
QDDEYHPEVK LKTAGLEEAA EGETANNNGE AEDQEEKEDT EKENTEKDED DVEQELANVD
PTWMESPKTN GHIENGPFLL EQQLDDEDDD EEDCPNPEEY NLDEPNAESD YTYSSSYEQF
NGELPNGRHK IPESQFPEFS TSLFSGPLEP VACGSALSEG SPLTEHEESS PSHDRSRTVS
ASSTGDLPKT KTRAADLLVN PLDPRNADKI RVKIADLGNA CWVHKHFTED IQTRQYRSIE
VLIGAGYSTP ADIWSTACMA FELATGDYLF EPHSGEDYSR DEDHIAHIIE LLGSIPRHFA
LSGKYSREFF NRRDHIALII ELLGKVPRKY AMLGKYSKEF FTRKGELRHI TKLKPWSLFD
VLVEKYGWPH EDAAQFTDFL IPMLEMVPEK RASAGECLRH PWLNS
//
