ID L5L0U0_PTEAL Unreviewed; 662 AA.
AC L5L0U0;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
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_GLEAN10003163 {ECO:0000313|EMBL:ELK17030.1};
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:ELK17030.1, 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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC protein kinase family. RAF subfamily. {ECO:0000256|ARBA:ARBA00010507}.
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DR EMBL; KB030414; ELK17030.1; -; Genomic_DNA.
DR AlphaFoldDB; L5L0U0; -.
DR STRING; 9402.L5L0U0; -.
DR eggNOG; KOG0193; Eukaryota.
DR InParanoid; L5L0U0; -.
DR Proteomes; UP000010552; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd20870; C1_A_C-Raf; 1.
DR CDD; cd17133; RBD_ARAF; 1.
DR Gene3D; 3.30.60.20; -; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR003116; RBD_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR23257:SF727; NON-SPECIFIC SERINE_THREONINE PROTEIN KINASE; 1.
DR PANTHER; PTHR23257; SERINE-THREONINE PROTEIN KINASE; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF02196; RBD; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00455; RBD; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS50898; RBD; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ELK17030.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Reference proteome {ECO:0000313|Proteomes:UP000010552};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ELK17030.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 59..131
FT /note="RBD"
FT /evidence="ECO:0000259|PROSITE:PS50898"
FT DOMAIN 138..184
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 350..626
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 199..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 280..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..330
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 376
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 662 AA; 73778 MW; BC7FECBC48BDFC33 CRC64;
MDPDAPCPEL EEWFDPGQNH RAPWHLPSPT SARLDKVLGS MEPPRAPPAN GAEPSRAVGT
VKVYLPNKQR TVVTVRDGMS VYDSLDKALK VRGLNQDCCV VYRLIKGRKT VTAWDTAIAP
LDGEELIVEV LEDVPLTMHN FVRKTFFSLA FCDFCLKFLF HGFRCQTCGY KFHQHCSSKV
PTVCVDMSTN RRQFYHSVQD LSGGSRQHEA PSNRPLNEPL TPQGPSSCTQ HRDPEHFPFP
APANAPLQRI RSTSTPNVHM VSTTAPMDSS LIQLTTQSFS TDAAGNRGGG DGAPRGSPSP
ATVSSGRKSP HSKSPSEQRE RKPLADDKKK VKNLGYRDSG YYWEVPPSEV QLLKRIGTGS
FGTVFRGRWH GDVAVKVLKV AQPTAEQAQA FKNEMQVLRK TRHVNILLFM GFMTRPGFAI
ITQWCEGSSL YHHLHVADTR FDMVQLIDVA RQTAQGMDYL HAKNIIHRDL KSNSIYLSLS
KAGWPLTSVD IFLHEGLTVK IGDFGLATVK TRWSGAQPLE QPSGSVLWMA AEVIRMQDPN
PYSFQSDVYA YGVVLYELMT GSLPYSHIGS RDQIIFMVGR GYLSPDLSKI SSNCPKAMRR
LLSDCLKFQR EERPLFPQIL ATIELLQRSL PKIERSASEP SLHRTQADEL PACLLSAARL
VP
//
