ID L5KR08_PTEAL Unreviewed; 751 AA.
AC L5KR08;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
DE Flags: Fragment;
GN ORFNames=PAL_GLEAN10011409 {ECO:0000313|EMBL:ELK13381.1};
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:ELK13381.1, 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};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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; KB030625; ELK13381.1; -; Genomic_DNA.
DR AlphaFoldDB; L5KR08; -.
DR STRING; 9402.L5KR08; -.
DR eggNOG; KOG0576; Eukaryota.
DR InParanoid; L5KR08; -.
DR Proteomes; UP000010552; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008349; F:MAP kinase kinase kinase kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd06613; STKc_MAP4K3_like; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR001180; CNH_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR021160; MAPKKKK.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR PANTHER; PTHR48012:SF6; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE KINASE 2; 1.
DR PANTHER; PTHR48012; STERILE20-LIKE KINASE, ISOFORM B-RELATED; 1.
DR Pfam; PF00780; CNH; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PIRSF; PIRSF038172; MAPKKKK; 2.
DR SMART; SM00036; CNH; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50219; CNH; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR038172-
KW 2}; Kinase {ECO:0000313|EMBL:ELK13381.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR038172-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000010552};
KW Transferase {ECO:0000313|EMBL:ELK13381.1}.
FT DOMAIN 1..258
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 413..724
FT /note="CNH"
FT /evidence="ECO:0000259|PROSITE:PS50219"
FT REGION 339..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 121
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR038172-1"
FT BINDING 7..15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR038172-2"
FT BINDING 30
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR038172-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ELK13381.1"
SQ SEQUENCE 751 AA; 83513 MW; EF3E2C3D78F1027C CRC64;
FELLQRVGAG TYGDVYKARD TVTSELAAVK IVKLDPGDDI SSLQQEITIL RECHHPNVVA
YIGSYLRNDR LWICMEFCGG GSLQEIYHAT GPLEERQIAY VCREALKGLH HLHSQGKIHR
DIKGANLLLT LQGDVKLADF GVSGELTASV AKRRSFIGTP YWMAPEVAAV ERKGGYNELC
DIWALGITAI ELGELQPPLF HLHPMRALML MSKSSFQPPK LRDKSRWTQN FHHFLKLALT
KNPKKRPTAE RLLQHPFTTQ QLPRALLTQL LDKANDPHLG TPSPEDCDLE WEEEWTLLGK
EELSGSLLQS VQEALEERSL TIRPALELQE LDSPDDAIGT IKRAPFLGPS SSELPAEDPL
SSPPGPDSPP LLPTSWATMK HQEDPERSSC HGLPPTPKVH MGACFSKVFN GCPLRIHAAV
TWIHPVTRDQ FLVVGAEEGI YTLNLHELHE DTLEKLISHR CIWLYCVNNV LLSLSGKSMH
IWAHDLPGLF EQRRLQQQVP LSIPTNRLTQ RIIPRRFALS TKIPDTKGCL QCRVVRNPYT
GSTFLLAALP ASLLLLQWYE PLQKFLLLKN FSSPLPSPAG MLEPLVLDGK ELPQVCVGAE
GPEGPGCRVL FHVLPLEAGL TPDVLIPPEG LPGSAQQVIQ VDRDTVLVCF DRCVRIVNLL
GEPTAALAPV LTFDFPIETV VCLQDSVLAF WSHGMQGRSL DTNEVTQEIT DETRVFRVLG
AHRDIILESI PTDNPGAHSN LYILTGHQSS Y
//
