ID L5JYV9_PTEAL Unreviewed; 1335 AA.
AC L5JYV9;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=PAL_GLEAN10003510 {ECO:0000313|EMBL:ELK03403.1};
OS Pteropus alecto (Black flying fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC Pteropodinae; Pteropus.
OX NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK03403.1, ECO:0000313|Proteomes:UP000010552};
RN [1] {ECO:0000313|Proteomes:UP000010552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
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 EMBL; KB031095; ELK03403.1; -; Genomic_DNA.
DR STRING; 9402.L5JYV9; -.
DR eggNOG; KOG0584; Eukaryota.
DR InParanoid; L5JYV9; -.
DR Proteomes; UP000010552; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR InterPro; IPR024678; Kinase_OSR1/WNK_CCT.
DR PANTHER; PTHR13902; SERINE/THREONINE-PROTEIN KINASE WNK WITH NO LYSINE -RELATED; 1.
DR PANTHER; PTHR13902:SF10; SERINE_THREONINE-PROTEIN KINASE WNK2; 1.
DR Pfam; PF12202; OSR1_C; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ELK03403.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000010552};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 88..151
FT /note="Serine/threonine-protein kinase OSR1/WNK CCT"
FT /evidence="ECO:0000259|Pfam:PF12202"
FT REGION 222..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 256..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 304..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 430..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 490..670
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 687..722
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 821..863
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 887..912
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 958..997
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1098..1119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1059..1090
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 304..318
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..346
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..508
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 691..711
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 830..863
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 896..912
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1335 AA; 142135 MW; 2B92CE7B1DE04919 CRC64;
MAEPRPAEGL VSSVCVTTPF ENFPPDISLM DFFFWLFFFF FFFFYNQKRV LNTTQYEIKD
LLSHAFFAED TGVRVELAEE DHGRKSTIAL RLWVEDPKKL KGKPKDNGAI EFTFDLERET
PDDVAQEMIE SGFFHESDVK IVAKSIRDRV ALIQWRRERI WPALQPQEQR DPGSPDKAKG
LHTPLQVQVT YHAQVGLLEP EEPEADQHLL PTVLPASATS LASDSTFDSG QGSTVYSDSQ
SSQQSVVLGS LVDSAPPTAQ SVCSPPVSMS DGPILPHSLP SLGAYQQPVA EQDKQPGLLQ
SCESYGGSDV TSGRELSDSC EGTFGGGKLE GKPSRKHHRR STRTRSRQER ASRPRLTILN
VCNTGDKMVE CQLETHNHKM VTFKFDLDGD APDEIATYMV EHDFILQAER ETFIEQMKDI
MDKAEDMLSE DTDVDRGSDP GASPPPLSTC GLGTGEESRQ SQANAPVYQQ NVLHTGKRWF
IICPVAEHPA AEAPESSPPP PLSSLQPEAS PDPAPCKDQL SLKEKSGFPA SPQLPSQPSS
RGAPGGVPVP LVPSSPPMTS VPQDMAAPAA SPKPEPAMGA AVQAGGPGTS QGIASEHETP
QPLAETHDAQ LATRPLGVAL GPCTSPPEAP QHPTGLEEPA SAREASAPGE ILPAPAPVPS
APGGTPQLAL GQSLTSVPNV VGAVSLATPQ LPSPPLGPAI PPQPPSALES DGEGPPPRVG
FVDSTIKSLD EKLRTLLYQE HVPTSSASAG TPVEVGDRDF TMEPPRGDWT YTEASGGDPA
LLSQLASDKS EMAPGPGDTL KQATSSPVAA ASSLSNMLGT DGGWVASGSP AASSAPQDAP
TSAIPAHPET TDQSSRVLGE TSAEPTQRCL GMLTKGSQAI QFQTHGIMAS GSPPKRPRQQ
DGSSPAKTVG RFSVISTQDE WTLASPHSLR YSAPPDVYLQ EGPQSPDMKL ALRRVQTASS
IEVGPGEPVS SDSGDECPRR RPSVQKHGSL PGSGSSVASD FVKKATAFLH RSSRAGSPGP
ETPNRTGVKV PTISVTSFHS QSSYISSDND SEIEDADIRK ELQSLREKHL KEISELQSQQ
KQEIEALYRR LGKPLPPNLG LFHTAPPAGR RRKTSKSKLK AGKLLNPLVQ QLKVVASSTG
SSTSSLVPGP EPGPPPTLHV QAQVNNSNNK KGTFTDDLHK LVDEWTSKTV GVAQLKPSLN
QLKQTQKLHN MEATAGWALG PGEIQAMNPP RAAVGTPCLA LAPGPLPTTV IPGTSLTLPV
PGTTLSGFSA SPCALPLGQY RSLFPASVSW SSWAAQEGSQ RPTWGPGLGV ADRPMLPVFL
RLPVARTHNP WLQIT
//
