ID A0A0N8CPE7_9CRUS Unreviewed; 852 AA.
AC A0A0N8CPE7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Putative Serine threonine-protein kinase {ECO:0000313|EMBL:JAL91843.1};
DE SubName: Full=Serine/threonine-protein kinase PDIK1L {ECO:0000313|EMBL:KZS10274.1};
GN ORFNames=APZ42_025278 {ECO:0000313|EMBL:KZS10274.1};
OS Daphnia magna.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda;
OC Diplostraca; Cladocera; Anomopoda; Daphniidae; Daphnia.
OX NCBI_TaxID=35525 {ECO:0000313|EMBL:JAL91843.1};
RN [1] {ECO:0000313|EMBL:JAL91843.1}
RP NUCLEOTIDE SEQUENCE.
RA Gilbert D., Podicheti R., Orsini L., Colbourne J., Pfrender M.;
RT "Daphnia magna gene sets from two clonal populations assembled and
RT annotated with EvidentialGene.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:JAL91843.1}
RP NUCLEOTIDE SEQUENCE.
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KZS10274.1, ECO:0000313|Proteomes:UP000076858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Xinb3 {ECO:0000313|EMBL:KZS10274.1,
RC ECO:0000313|Proteomes:UP000076858};
RC TISSUE=Complete organism {ECO:0000313|EMBL:KZS10274.1};
RA Gilbert D.G., Choi J.-H., Mockaitis K., Colbourne J., Pfrender M.;
RT "EvidentialGene: Evidence-directed Construction of Genes on Genomes.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; GDIP01111871; JAL91843.1; -; Transcribed_RNA.
DR EMBL; LRGB01001863; KZS10274.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N8CPE7; -.
DR STRING; 35525.A0A0N8CPE7; -.
DR EnsemblMetazoa; XM_032934746.2; XP_032790637.2; LOC116927709.
DR Proteomes; UP000076858; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:InterPro.
DR GO; GO:0004521; F:RNA endonuclease activity; IEA:InterPro.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR045133; IRE1/2-like.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR13954; IRE1-RELATED; 1.
DR PANTHER; PTHR13954:SF6; NON-SPECIFIC SERINE_THREONINE PROTEIN KINASE; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00248; ANK; 7.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50297; ANK_REP_REGION; 2.
DR PROSITE; PS50088; ANK_REPEAT; 4.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Kinase {ECO:0000313|EMBL:JAL91843.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000076858};
KW Transferase {ECO:0000313|EMBL:JAL91843.1}.
FT DOMAIN 36..312
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REPEAT 355..391
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 466..503
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 504..540
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 541..577
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
SQ SEQUENCE 852 AA; 97724 MW; 24D431949B86CEDA CRC64;
MQFIQILISV ASEAIKLEMT SPVFSSRVVK LDGIKFDHKD FLGKGSYGSV LRDGSFKGQK
VAIKRIEVIK DTDLSMDDQF NTLSQLDHPN VVKLLHCEDD NDFRYYTLES CVASLGQLFL
KSDDSQKYNG PMPHHVEALL QLALGLERIH SKNLIHGDLK PENVLISVGS AEQDEITLKW
AYFGLTRHAD ERGTETINQT RDNNAWLAPE VLLLKLSGNS QENKYQSTVK SDIFAQGLVF
GSLCLNGEHL YGSMENENEI SGNIIHRNPV NMPKMDRKLR NCYEDELFKK MLENDPAKRM
TSKEVVDQLK SIKDKLAGKE KELLRLCGRD TQLDLTEQIK NLILFGINLN AKDNDGSNAL
HLLCRYYSSS KLIDAIKIVI QSGINVNAKD KCGRNALHYL CRFNLSSNLI DAIQNLILAG
INVNEKGNNG WKALHYLCFF HSSPKLLNAI ESLIKHGINL NAEVEDGQNA LHLLCQVKDG
SPNFVDVIQL LIQHGIDTNA KNKNGCNALH FLCQNNSSAY LRDAIKLLIR QGIDVNAKDK
DGRNALHYLC RHNSSTNLRD AIQILFQYGI DVNEKDNHEW NALNFLVRNS MDKYLKSDVF
RFLIRHGVQV HNENDETSAK LFQDFFKENE NNGKKCFDFL VEEKIRLGWH DACEHCQQIL
SIEESPRARL WHHQMFSSCY LVFDSLMEEL EKWAKSSINK FGESELDIKN PTEWLRGIAE
EYQQNTTDKS YKEDFEVMAD VSEQVKDGNN SSHFNCDNYE RYLRSMYSIA EMTDSKESMG
HIKWCYLLPF DYPIDYSNDK TSIKQAKIEW DKTLFSWAHR ETDKDYGKFM TEDANDGFFL
PKEFKYKCHG EL
//
