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Database: UniProt
Entry: A0A0A0A9I3_CHAVO
LinkDB: A0A0A0A9I3_CHAVO
Original site: A0A0A0A9I3_CHAVO 
ID   A0A0A0A9I3_CHAVO        Unreviewed;      1006 AA.
AC   A0A0A0A9I3;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Connector enhancer of kinase suppressor of ras 2 {ECO:0000313|EMBL:KGL90602.1};
DE   Flags: Fragment;
GN   ORFNames=N301_11186 {ECO:0000313|EMBL:KGL90602.1};
OS   Charadrius vociferus (Killdeer) (Aegialitis vocifera).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Charadriiformes; Charadriidae; Charadrius.
OX   NCBI_TaxID=50402 {ECO:0000313|EMBL:KGL90602.1, ECO:0000313|Proteomes:UP000053858};
RN   [1] {ECO:0000313|EMBL:KGL90602.1, ECO:0000313|Proteomes:UP000053858}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N301 {ECO:0000313|EMBL:KGL90602.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the CNKSR family.
CC       {ECO:0000256|ARBA:ARBA00009498}.
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DR   EMBL; KL871140; KGL90602.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A0A9I3; -.
DR   STRING; 50402.A0A0A0A9I3; -.
DR   Proteomes; UP000053858; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0009966; P:regulation of signal transduction; IEA:InterPro.
DR   CDD; cd00992; PDZ_signaling; 1.
DR   CDD; cd01260; PH_CNK_mammalian-like; 1.
DR   CDD; cd09511; SAM_CNK1_2_3-suppressor; 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; IPR049628; CNK1-3_SAM.
DR   InterPro; IPR010599; CNK2/3_dom.
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:SF12; CONNECTOR ENHANCER OF KINASE SUPPRESSOR OF RAS 2; 1.
DR   Pfam; PF06663; CNK2_3_dom; 1.
DR   Pfam; PF10534; CRIC_ras_sig; 1.
DR   Pfam; PF00595; PDZ; 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:KGL90602.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053858};
KW   Transferase {ECO:0000313|EMBL:KGL90602.1}.
FT   DOMAIN          1..55
FT                   /note="SAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50105"
FT   DOMAIN          63..157
FT                   /note="CRIC"
FT                   /evidence="ECO:0000259|PROSITE:PS51290"
FT   DOMAIN          194..276
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          545..644
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          390..419
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          460..493
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          685..740
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          755..835
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        390..412
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        710..730
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KGL90602.1"
FT   NON_TER         1006
FT                   /evidence="ECO:0000313|EMBL:KGL90602.1"
SQ   SEQUENCE   1006 AA;  113924 MW;  67F2D92C985CB782 CRC64;
     GLDDCLQQYI KNFEKEKING EQLLHITHQE LEELGVTRIG HQELILEAVD LLCALNYGLE
     TENLRTLSHK LNASAKNLQN FITGRRRSGH YDGRASRRLP NDFLTSVVDL IGAAKNLLAW
     LDRSPFVSVT EYSLLKNNIV QLCLELTTIV QQDCTVYETE NKILHVCKTL SGICDHIISL
     SSDSLVSQSA HLEVVHLTSI MPSEGLGMYI KSTYDGLHVI TGTTENSPAD QCKKIHAGDE
     VIQVNHQTVV GWQLKNLVNA LREDPNGVIL TLKKRPQNTL VSAPALLKNV RWKPLALQPV
     IPTSPTSSST TPTSTMGISS KMENSALQDV FILSPMSGLY GPRDEIGIMS CDDISKFGKP
     GMKGSESPNY FLEHESGKYY TLIEGEGHPV GSEYERSRAT GVRRREKTPT HGDLRPVSMP
     TEYSWIGESK EQNMYKRGSR DSENSLLRYL SDDKILVIQE EPLTQKDNKR DTGRRSRKKG
     KNTSSPNYPI SPPVLTSTIN ARLEPGQQDV LNFSLAENNT VPLYHVRSSL TSGSRRRISC
     KDLGHGDCEG WLWKKKDAKG YFTQKWKKYW FILKDSSLYW YTNQNDEKAE GFISLPEFRI
     DRAIECRRKH AFKACHPKIK SFYFATDCLE EMNRWMNRLG LAAIGYTPDD KEMHPDEDYW
     SESDQDDIDG SLTLKQEGSA TLCDTYHRTP SVNSSSPFPE AKHGRHFSSE STYSHSSAED
     SRQDVAGSTH SSGCRPPYRE RRSWQDLIET PLTSSGLHFL QTVPPDTEYM SGRSGMSPDK
     RRQATLPVQR RHNYEQDGPF PLVECQRGHS SYSRPQKQRS QSLPRNRDVR GKGCVQSIEG
     TDDKLEEKVP IRRHNSFCVE GFFIYFLSEN VKEIGENTDG LQELYKSLEQ ASLSAFGEQR
     PSTKQEFRRS FVKRCNDPVI NEKLHHIRVL KSTLKAKEGD LTVINSLLDD PNLTSKKFKD
     WKLKNYEFFL DICEYSAAVK SQNGASELAT SAPMLTHTHS FIETHV
//
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