ID A0A091S4Y8_MERNU Unreviewed; 475 AA.
AC A0A091S4Y8;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Serine/threonine-protein kinase 4 {ECO:0000256|ARBA:ARBA00039974};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
DE Flags: Fragment;
GN ORFNames=N331_02884 {ECO:0000313|EMBL:KFQ35585.1};
OS Merops nubicus (Northern carmine bee-eater).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Coraciiformes; Meropidae; Merops.
OX NCBI_TaxID=57421 {ECO:0000313|EMBL:KFQ35585.1, ECO:0000313|Proteomes:UP000052967};
RN [1] {ECO:0000313|EMBL:KFQ35585.1, ECO:0000313|Proteomes:UP000052967}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N331 {ECO:0000313|EMBL:KFQ35585.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily.
CC {ECO:0000256|ARBA:ARBA00008874}.
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DR EMBL; KK714625; KFQ35585.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091S4Y8; -.
DR Proteomes; UP000052967; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0051262; P:protein tetramerization; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd21887; SARAH_MST1; 1.
DR CDD; cd06612; STKc_MST1_2; 1.
DR Gene3D; 1.10.287.4270; -; 1.
DR Gene3D; 4.10.170.10; p53-like tetramerisation domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR024205; Mst1_2_SARAH_domain.
DR InterPro; IPR036674; p53_tetramer_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR011524; SARAH_dom.
DR PANTHER; PTHR48015; SERINE/THREONINE-PROTEIN KINASE TAO; 1.
DR PANTHER; PTHR48015:SF32; SERINE_THREONINE-PROTEIN KINASE 4; 1.
DR Pfam; PF11629; Mst1_SARAH; 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; PS50951; SARAH; 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|EMBL:KFQ35585.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000052967};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 18..269
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 421..468
FT /note="SARAH"
FT /evidence="ECO:0000259|PROSITE:PS50951"
FT REGION 293..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 47
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFQ35585.1"
FT NON_TER 475
FT /evidence="ECO:0000313|EMBL:KFQ35585.1"
SQ SEQUENCE 475 AA; 53949 MW; B068D360431CFBF5 CRC64;
QLKKLDEDSL TKQPEEVFDV LEKLGEGSYG SVFKAIHKET GQVVAIKQVP VESDLQEIIK
EISIMQQCDS PHVVKYYGSY FKNTDLWIVM EYCGAGSVSD IIRLRNKTLT EEEIATIVKS
TLKGLEYLHF MRKIHRDIKA GNILLNTEGH AKLADFGVAG QLTDTMAKRN TVIGTPFWMA
PEVIQEIGYN CVADIWSLGI TAIEMAEGKP PYADIHPMRA IFMIPTNPPP TFRKPDLWSD
SFTDFVEQCL VKSPEQRATA TQLLQHPFVK SAKGVSVLRD LINEAMEIKL KRQEAQQSEL
DQEDEENSEE DETDSGTMVR ASGDETGTIR AVNTMTDGAN TMIEHDGTLE SQLGTMVINT
EEEEEEGTMK RRDETMQPAK PSFLEYFEQK EKENQINSFG KNVSGQTKNS SDWKVPQDGD
YGFLKTWSVD ELQRRLSALD PMMEQEIEEI RQKYQSKRQP ILDAIEAKKR RQQNF
//
