ID A0A3B3BP97_ORYME Unreviewed; 922 AA.
AC A0A3B3BP97;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Calcium/calmodulin dependent serine protein kinase {ECO:0000313|Ensembl:ENSOMEP00000007099.1};
GN Name=CASK {ECO:0000313|Ensembl:ENSOMEP00000007099.1};
OS Oryzias melastigma (Marine medaka).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=30732 {ECO:0000313|Ensembl:ENSOMEP00000007099.1, ECO:0000313|Proteomes:UP000261560};
RN [1] {ECO:0000313|Ensembl:ENSOMEP00000007099.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the MAGUK family.
CC {ECO:0000256|ARBA:ARBA00007014}.
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DR AlphaFoldDB; A0A3B3BP97; -.
DR Ensembl; ENSOMET00000004688.1; ENSOMEP00000007099.1; ENSOMEG00000008514.1.
DR GeneTree; ENSGT00940000155600; -.
DR Proteomes; UP000261560; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR CDD; cd00992; PDZ_signaling; 1.
DR CDD; cd12081; SH3_CASK; 1.
DR CDD; cd14094; STKc_CASK; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 6.10.140.620; -; 1.
DR Gene3D; 3.30.63.10; Guanylate Kinase phosphate binding domain; 1.
DR Gene3D; 1.10.287.650; L27 domain; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR035473; CASK_SH3.
DR InterPro; IPR008145; GK/Ca_channel_bsu.
DR InterPro; IPR008144; Guanylate_kin-like_dom.
DR InterPro; IPR020590; Guanylate_kinase_CS.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR014775; L27_C.
DR InterPro; IPR004172; L27_dom.
DR InterPro; IPR036892; L27_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR23122; MEMBRANE-ASSOCIATED GUANYLATE KINASE MAGUK; 1.
DR PANTHER; PTHR23122:SF40; PERIPHERAL PLASMA MEMBRANE PROTEIN CASK; 1.
DR Pfam; PF00625; Guanylate_kin; 1.
DR Pfam; PF02828; L27; 2.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00018; SH3_1; 1.
DR SMART; SM00072; GuKc; 1.
DR SMART; SM00569; L27; 2.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF101288; L27 domain; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR PROSITE; PS51022; L27; 2.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS50002; SH3; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 12..277
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 344..399
FT /note="L27"
FT /evidence="ECO:0000259|PROSITE:PS51022"
FT DOMAIN 415..472
FT /note="L27"
FT /evidence="ECO:0000259|PROSITE:PS51022"
FT DOMAIN 507..588
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 608..678
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 735..907
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000259|PROSITE:PS50052"
SQ SEQUENCE 922 AA; 104862 MW; A8CB123E0836061F CRC64;
MADDDILFED VYELCEVIGK GPFSVVRRCI NRETGQQFAV KIVDVAQFTS SPGLSTEDLK
REASICHMLK HSHIVELLET YSSDGMLYMV FEFMDGADLC FEIVKRADAG FVYSEAVASH
YMRQILEALR YCHDNNIIHR DVKPHCVLLA SKENSAPVKL GGFGVAIQLG ESGLVAGGRV
GTPHFMAPEV VKREPYGKPV DVWGCGVILF ILLSGCLPFY GTKERLFDAI CKGKYKQMNP
RQWNQISESA KDLVRRMLML DPAERITVYE ALNHPWLKER DRYAYKIHLP ETVEQLRKFN
ARRKLKGAVL AAVSSHKFNS FYGDPPEELH DFSDDPSSSG LLAAERAVSQ VLDSLEEIHA
LTDCSEKDLD FLHSVFQDQH LHTLLDLYDK INTKSSPQIR TPPSDAVQRA KENSFQDGSS
EALKHLECVL EEISCYPENH EAKELRRILT QPHFMALLQA HDVVAHEVYS DEALRVTPPP
ASPYLNGDSP ESANGDLDLE NVTRVRLVQF QKNTDEPMGI TLKLNELNHC IVARIMYGGM
IHRQGTLHVG DEIREINGIS VVNQTVEQLQ KMLREMRGSI TFKIVPSYQM HGSSCEIVSR
TPIKDKISVK IYVRAQFEYD PSKDELIPCK EAGVRFRVGD IIQIISKDDH NWWQGKLENT
KNGTAGLIPS PELQEWRVAC MAMEKTKQEQ QASCTWFGKK KKQYKDKYLA KHNAVFDQLD
LVTYEEVVKL PAFKRKTLVL LGAHGVGRRH IKNTLITKHP DRFAYPIPHT TRLPKKDEEN
GKNYYFVSHD QMMLDISNNE YLEYGSHEDA MYGTRLETIR KINQQGLVAI LDVEPQALKV
LRTAEFAPYV VFIAAPTITP GISEDESLQR LQKESEILQK TYAHCFDMTI INNEIDETIR
HLEDAMDVVS TTSQWVPVSW VY
//
