ID A0A091NCP1_APAVI Unreviewed; 759 AA.
AC A0A091NCP1;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 22-FEB-2023, entry version 30.
DE SubName: Full=Connector enhancer of kinase suppressor of ras 2 {ECO:0000313|EMBL:KFP86862.1};
DE Flags: Fragment;
GN ORFNames=N311_09351 {ECO:0000313|EMBL:KFP86862.1};
OS Apaloderma vittatum (Bar-tailed trogon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Trogoniformes; Trogonidae; Apaloderma.
OX NCBI_TaxID=57397 {ECO:0000313|EMBL:KFP86862.1, ECO:0000313|Proteomes:UP000054244};
RN [1] {ECO:0000313|EMBL:KFP86862.1, ECO:0000313|Proteomes:UP000054244}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N311 {ECO:0000313|EMBL:KFP86862.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KL380356; KFP86862.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091NCP1; -.
DR Proteomes; UP000054244; 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 Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
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 PANTHER; PTHR12844; CONNECTOR ENCHANCER OF KINASE SUPPRESSOR OF RAS; 1.
DR PANTHER; PTHR12844:SF21; 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 SMART; SM00228; PDZ; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS51290; CRIC; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:KFP86862.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054244};
KW Transferase {ECO:0000313|EMBL:KFP86862.1}.
FT DOMAIN 1..38
FT /note="CRIC"
FT /evidence="ECO:0000259|PROSITE:PS51290"
FT DOMAIN 75..157
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 430..529
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 184..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 340..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 541..626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 718..759
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..409
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 541..556
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..572
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..605
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 735..759
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP86862.1"
FT NON_TER 759
FT /evidence="ECO:0000313|EMBL:KFP86862.1"
SQ SEQUENCE 759 AA; 86276 MW; 472DE27CF7F4AB7E CRC64;
FLFRSPFAAV TDYSVTRNNV IQLCLELTTI VQQDCTVYET ENKILHVCKT LSGVCDHIIS
LSSDPLVSQS AHLEVIQLTN IKPSEGLGMY IKSTYDGLHV ITGTTENSPA DRCKKIHAGD
EVIQVNHQTV VGWQLKNLVN ALREDPSGVI LTLKKRPQSM LTSAPALLKN MRWKPLALQP
LIPRSPTSSV ATPSSTISTP TKRDSSALQD LYIPPPPTEP YVPRDEKGNL PCDDVGRHIV
GKPVHTGSES PNSFLDQEYR KRFNVVEEDA VLYCYEYEKG RTSGPGRRES TPTYGKLRPI
SMPVEYNWVG DYEDPNKIKR DSRRENSLLR YMSNEKIGQE DYIFQRNSKK DTGKKSKKKG
DKSSSPSHYS LLPSLQMESL RQEVMGTPGP ETSLYHTFQQ SSLQQKSKKK NKAPIPGKSK
RRISCKDLGR GDCEGWLWKK KDAKSYFSQK WKKYWFVLKD TSLYWYINEE DEKAEGFISL
PEFKIDRASE CRKKYAFKAC HPKIKSFYFA AEHLDDMNRW LNRINMLAAG YAERERIKQE
QDYWSESDKE EADTPSTPKQ DSPPPPYDTY PRPPSMSCAS PYVEPKHSRL SSTETSQSQS
SHEEFRPEAA GSITDSPVRK TASQRRSWQD LIETPLTSSG LHYLQTLPLE DSVFSEAAVV
SPEHRRQSTL PTQKCHLQDH YGPFPLVEGE RMQALNGNGG KPRSFTLPRD SGFNHCCQNL
SIGATDHHEE AQQKEVEEDE EEEEEEEEGK AAEENQEDK
//
