ID A0A5C6NY90_9TELE Unreviewed; 829 AA.
AC A0A5C6NY90;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 02-APR-2025, entry version 13.
DE SubName: Full=Connector enhancer of kinase suppressor of ras 1 {ECO:0000313|EMBL:TWW71995.1};
GN ORFNames=D4764_16G0004920 {ECO:0000313|EMBL:TWW71995.1};
OS Takifugu flavidus (sansaifugu).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=433684 {ECO:0000313|EMBL:TWW71995.1, ECO:0000313|Proteomes:UP000324091};
RN [1] {ECO:0000313|EMBL:TWW71995.1, ECO:0000313|Proteomes:UP000324091}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTHZ2018 {ECO:0000313|EMBL:TWW71995.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:TWW71995.1};
RA Xiao S.;
RT "Chromosome genome assembly for Takifugu flavidus.";
RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the CNKSR family.
CC {ECO:0000256|ARBA:ARBA00009498}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:TWW71995.1}.
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DR EMBL; RHFK02000008; TWW71995.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5C6NY90; -.
DR Proteomes; UP000324091; Chromosome 16.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR CDD; cd06748; PDZ_CNK1_2_3-like; 1.
DR CDD; cd01260; PH_CNK_mammalian-like; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR InterPro; IPR051566; CNKSR.
DR InterPro; IPR017874; CRIC_domain.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR PANTHER; PTHR12844; CONNECTOR ENCHANCER OF KINASE SUPPRESSOR OF RAS; 1.
DR PANTHER; PTHR12844:SF10; CONNECTOR ENHANCER OF KINASE SUPPRESSOR OF RAS 1; 1.
DR Pfam; PF10534; CRIC_ras_sig; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00536; SAM_1; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR PROSITE; PS51290; CRIC; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000313|EMBL:TWW71995.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000324091};
KW Transferase {ECO:0000313|EMBL:TWW71995.1}.
FT DOMAIN 7..67
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 78..172
FT /note="CRIC"
FT /evidence="ECO:0000259|PROSITE:PS51290"
FT DOMAIN 209..291
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 472..572
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 297..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 346..460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 574..635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 729..763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..369
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..408
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..435
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..592
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 729..741
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 829 AA; 92716 MW; 6A9201EF49F374A8 CRC64;
MEPITAWSEE RVSQWLQGLD APLQLYPTSA WHLTGMDLLQ LTSKDLENLG VNKIGHQELI
LEAVEKLCFL MYGIGGESLR SVTEKLRAVS HSLQMGIQSR WRIIGYDGGS TTKLPTSVLQ
LVVELITSAK GLFSLLNRYQ FFQLSGGAIS KTIFSYCKEL GDIVNKQDST VYEKEKDIIS
VCRQVTAACD DILTTSPEAI LTHTAQLESV DLVPVSPGDK LGIEIASTGS SNHYVTGAAA
EPSSDVYLKI LAGDEVIQVN DQIVVGWSRA NLIKKLQENP SGVTLVLKKI PESVRRTHPL
QVSSTQRKAE SSEEEEEKDE ENLRHSLFER VAASVRSLSF RRAIQGPEAQ QQPMGQEESE
LASDYDAEES LTLTSYQDHQ GGVSPLSASG VFDSLRISPR PGEGRSPSPR SPSPFRPLRS
PSLQELNQDR ASISSCPEMV GHMGKKDREK TSLKGQTTAM SRRRVSCREL GKPDCDGWLW
KKRKESSVFL TQKWQRFWFV LKGPALYWYS SQQDEKAEGF VNISSYSIES AGEHKRKYVF
KMYHQRFQNF FFAADNVNDM SKWINYLITT IQKHKKQKGP DSEEECYSET ESESERSPSP
RRKKKVQSNT LPRQKWKNRA PLPSPLTGGS KGTVDEMGAM MNSIKEGGVS LTGQEQPFTH
DHFRRSFIRR CKNPVINEKV HTLRTLQSTL KAKEAELLQI SKILDDSEVT ASKFRQWKEQ
NEELVQEIER TTSLKASKDG DPTAESSPTE EPPSEPGEAG TEGAYRWSLS DGEQLVDAEP
SDVLLEMGSP GLETSPMLEL SLGSLQESIN KELSDMAMSG NSTENYFFI
//
