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Database: UniProt
Entry: A0A1V4KL14_PATFA
LinkDB: A0A1V4KL14_PATFA
Original site: A0A1V4KL14_PATFA 
ID   A0A1V4KL14_PATFA        Unreviewed;       486 AA.
AC   A0A1V4KL14;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Serine/threonine-protein kinase 4 {ECO:0000256|ARBA:ARBA00039974};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   Name=STK4 {ECO:0000313|EMBL:OPJ85091.1};
GN   ORFNames=AV530_018123 {ECO:0000313|EMBL:OPJ85091.1};
OS   Patagioenas fasciata monilis.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Patagioenas.
OX   NCBI_TaxID=372326 {ECO:0000313|EMBL:OPJ85091.1, ECO:0000313|Proteomes:UP000190648};
RN   [1] {ECO:0000313|EMBL:OPJ85091.1, ECO:0000313|Proteomes:UP000190648}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BTP2013 {ECO:0000313|EMBL:OPJ85091.1};
RC   TISSUE=Blood {ECO:0000313|EMBL:OPJ85091.1};
RA   Soares A.E., Novak B.J., Rice E.S., O'Connell B., Chang D., Weber S.,
RA   Shapiro B.;
RT   "Band-tailed pigeon sequencing and assembly.";
RL   Submitted (FEB-2016) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OPJ85091.1}.
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DR   EMBL; LSYS01002950; OPJ85091.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V4KL14; -.
DR   STRING; 372326.A0A1V4KL14; -.
DR   Proteomes; UP000190648; 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:OPJ85091.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000190648};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          29..280
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          432..479
FT                   /note="SARAH"
FT                   /evidence="ECO:0000259|PROSITE:PS50951"
FT   REGION          305..339
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         58
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   486 AA;  55470 MW;  C19399234BC03330 CRC64;
     METVQLRNPR RQLKKLDEDS LTKQPEEVFD VLEKLGEGSY GSVFKAIHKE TGQVVAIKQV
     PVESDLQEII KEISIMQQCD SPHVVKYYGS YFKNTDLWIV MEYCGAGSVS DIIRLRNKTL
     TEEEIATIVQ STLKGLEYLH FMRKIHRDIK AGNILLNTEG HAKLADFGVA GQLTDTMAKR
     NTVIGTPFWM APEVIQEIGY NCVADIWSLG ITAIEMAEGK PPYADIHPMR AIFMIPTNPP
     PTFRKPELWS DNFTDFVKQC LVKSPEQRAT ATQLLQHPFV KSAKGVSILR DLINEAMDIK
     LKRQEAQQRE LDQDDEENSE EDESDSGTMV RASGDETGTI RAVNTMSDGA NTMIEHDGTL
     ESQLGTMVIN TEEEEEEGTM KRRDETMQPA KPSFLEYFEQ KEKENQINSF GKNVSGQTKN
     SSDWKVPQDG DYEFLKTWSV DELQRRLSAL DPMMEQEIEE IRQKYQSKRQ PILDAIEAKK
     RRQQNF
//
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