ID L8J2A8_9CETA Unreviewed; 719 AA.
AC L8J2A8;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=M91_11759 {ECO:0000313|EMBL:ELR63010.1};
OS Bos mutus (wild yak).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=72004 {ECO:0000313|EMBL:ELR63010.1, ECO:0000313|Proteomes:UP000011080};
RN [1] {ECO:0000313|EMBL:ELR63010.1, ECO:0000313|Proteomes:UP000011080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=yakQH1 {ECO:0000313|Proteomes:UP000011080};
RX PubMed=22751099; DOI=10.1038/ng.2343;
RA Qiu Q., Zhang G., Ma T., Qian W., Wang J., Ye Z., Cao C., Hu Q., Kim J.,
RA Larkin D.M., Auvil L., Capitanu B., Ma J., Lewin H.A., Qian X., Lang Y.,
RA Zhou R., Wang L., Wang K., Xia J., Liao S., Pan S., Lu X., Hou H., Wang Y.,
RA Zang X., Yin Y., Ma H., Zhang J., Wang Z., Zhang Y., Zhang D., Yonezawa T.,
RA Hasegawa M., Zhong Y., Liu W., Zhang Y., Huang Z., Zhang S., Long R.,
RA Yang H., Wang J., Lenstra J.A., Cooper D.N., Wu Y., Wang J., Shi P.,
RA Wang J., Liu J.;
RT "The yak genome and adaptation to life at high altitude.";
RL Nat. Genet. 44:946-949(2012).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JH880261; ELR63010.1; -; Genomic_DNA.
DR RefSeq; XP_005886756.1; XM_005886694.1.
DR AlphaFoldDB; L8J2A8; -.
DR STRING; 72004.ENSBMUP00000003220; -.
DR Ensembl; ENSBMUT00000003748; ENSBMUP00000003220; ENSBMUG00000002554.
DR GeneID; 102288324; -.
DR KEGG; bom:102288324; -.
DR CTD; 57144; -.
DR OrthoDB; 460351at2759; -.
DR Proteomes; UP000011080; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0031965; C:nuclear membrane; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
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:0006915; P:apoptotic process; IEA:InterPro.
DR GO; GO:0007010; P:cytoskeleton organization; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd01093; CRIB_PAK_like; 1.
DR CDD; cd06658; STKc_PAK5; 1.
DR Gene3D; 3.90.810.10; CRIB domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000095; CRIB_dom.
DR InterPro; IPR036936; CRIB_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR033923; PAK_BD.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR028754; STKc_PAK5.
DR PANTHER; PTHR48015; SERINE/THREONINE-PROTEIN KINASE TAO; 1.
DR PANTHER; PTHR48015:SF27; SERINE_THREONINE-PROTEIN KINASE PAK 5; 1.
DR Pfam; PF00786; PBD; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00285; PBD; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50108; CRIB; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Kinase {ECO:0000313|EMBL:ELR63010.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Reference proteome {ECO:0000313|Proteomes:UP000011080};
KW Transferase {ECO:0000313|EMBL:ELR63010.1}.
FT DOMAIN 11..24
FT /note="CRIB"
FT /evidence="ECO:0000259|PROSITE:PS50108"
FT DOMAIN 449..700
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 96..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 256..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 340..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..291
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..372
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 479
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 719 AA; 80864 MW; 7F66D433B00EC8D4 CRC64;
MFGKKKKKIE ISGPSNFEHR VHTGFDPQEQ KFTGLPQQWH SLLADTANRP KPMVDPSCIT
PIQLAPMKTI VRGNKPCKET SINGLLEDFD NISVTRSNSL RKESPPTPDQ GASSRGPGHR
EENGFLTFSQ YSSESDTTAD YASEKYREKS LYGDDLDPFY KGGHSARQNG HVLKMQHGEA
YYPEMQALQS DRARFPADYH AHLDSLSKPS EYSDLKWGFQ RASGSSPLDY PFQFIPSRTA
GTSGCSKESL AYSESEWGPS LDDYDRRPKS SYLCQTSPQP AMRQRSRSGS GLQEPMMPFG
ESAFKTHPQG HSYSSYTYPR LSEPTVCVPK VDYDRAQMVL SPPLSGSDTY PRGPSKLPQS
QSKAGYSSSS HQYPSGYHKA TLYHHPSLQT SSQYISTASY LSSLSISSST YPPPSWGSSS
DQQPSRVSHE QFRAALQLVV SPGDPREYLD NFIKIGEGST GIVCIATEKH TGKQVAVKKM
DLRKQQRREL LFNEVVIMRD YHHDNVVDMY NSYLVSDELW VVMEFLEGGA LTDIVTHTRM
NEEQIATVCL SVLRALSYLH NQGVIHRDIK SDSILLTSDG RIKLSDFGFC AQVSKEVPKR
KSLVGTPYWM APEVISRLPY GTEVDIWSLG IMVIEMIDGE PPYFNEPPLQ AMRRIRDSLP
PRVKDLHKVS SVLRAFLDLM LVREPARRAT AQELLRHPFL KLAGPPSCIV PLMRQYRHH
//
