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Database: UniProt
Entry: A0A3Q3LFC0_9TELE
LinkDB: A0A3Q3LFC0_9TELE
Original site: A0A3Q3LFC0_9TELE 
ID   A0A3Q3LFC0_9TELE        Unreviewed;      1168 AA.
AC   A0A3Q3LFC0;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Caspase recruitment domain family, member 11 {ECO:0000313|Ensembl:ENSMAMP00000008491.1};
OS   Mastacembelus armatus (zig-zag eel).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Anabantaria; Synbranchiformes; Mastacembelidae; Mastacembelus.
OX   NCBI_TaxID=205130 {ECO:0000313|Ensembl:ENSMAMP00000008491.1, ECO:0000313|Proteomes:UP000261640};
RN   [1] {ECO:0000313|Ensembl:ENSMAMP00000008491.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   AlphaFoldDB; A0A3Q3LFC0; -.
DR   STRING; 205130.ENSMAMP00000008491; -.
DR   Ensembl; ENSMAMT00000008715.2; ENSMAMP00000008491.1; ENSMAMG00000005729.2.
DR   GeneTree; ENSGT00940000158573; -.
DR   InParanoid; A0A3Q3LFC0; -.
DR   OrthoDB; 4213113at2759; -.
DR   Proteomes; UP000261640; Unplaced.
DR   GO; GO:0042981; P:regulation of apoptotic process; IEA:InterPro.
DR   GO; GO:0050896; P:response to stimulus; IEA:UniProt.
DR   CDD; cd00992; PDZ_signaling; 1.
DR   Gene3D; 2.30.42.10; -; 1.
DR   Gene3D; 1.10.533.10; Death Domain, Fas; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   InterPro; IPR001315; CARD.
DR   InterPro; IPR011029; DEATH-like_dom_sf.
DR   InterPro; IPR008145; GK/Ca_channel_bsu.
DR   InterPro; IPR008144; Guanylate_kin-like_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   PANTHER; PTHR14559; CASPASE RECRUITMENT DOMAIN FAMILY; 1.
DR   PANTHER; PTHR14559:SF4; CASPASE RECRUITMENT DOMAIN-CONTAINING PROTEIN 11; 1.
DR   Pfam; PF00619; CARD; 1.
DR   Pfam; PF00625; Guanylate_kin; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF47986; DEATH domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50156; PDZ domain-like; 1.
DR   PROSITE; PS50209; CARD; 1.
DR   PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR   PROSITE; PS50106; PDZ; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000261640};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443}.
FT   DOMAIN          11..103
FT                   /note="CARD"
FT                   /evidence="ECO:0000259|PROSITE:PS50209"
FT   DOMAIN          703..772
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          1024..1154
FT                   /note="Guanylate kinase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50052"
FT   REGION          431..487
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          529..606
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          628..651
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          145..418
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        465..484
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        529..587
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        636..651
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1168 AA;  135147 MW;  9E11B61FB2AC34D9 CRC64;
     MENGTCGLSN NVEALWENVE CKRYELCRII SPAKLTPYLR QCKVLDEQDE DEILNSMLLV
     SKTNRTSRLL DILHTKGERG YVAFLESLEF YYPDQYKLVT GKDPTRRFST IVVEEGHEGL
     TQFLMNEVMK LQQQSKVKTL QHVELSRKNC TLEDEQKKLR LANQELQAFQ QRYNKLREER
     NTYSDELLRV KDENYKLAMR YATLSEEKNM AVMRSRDLQL EIDQLKHRLN KAEEECKMER
     RQSLKLKNDI ENRPKKEQIF ELERENEMLK IKLQELQSII QPGPLPESDK AILDILEHDR
     QEALEDRQDL VNRLYNLHEE VRQAEELRDK YLEEKEDLEL KCSTLQKDCE MYHNRMDTII
     IQLEEVEKER DQAFRARDEA QHQFSQSLID KDKYRKQIRE LEERNDELHI EIVRKDAKLV
     TLESRLRRMS KDNVNDQSLP RDVPPTIISQ GEEFKPIQGQ SEWSSDESPE EKNVPEDPPF
     KRRLNLKAGN RVKSPVCVYK NLPVSSEASQ PAALSVNRRD FLDIQMPKSQ VNSNSLPPSP
     SFQMSPTYTP PSAPALSSSC PSASPLPFTP VEQNNRPNIQ RFRNDSILST LPEPPEKASL
     YRREREKEHD FYPRSLSDFD SNNMEMEFED EVQRGPPSVH SSSSSHQSEG MDTYDLEQVN
     NIFRKLSLER PFRPSLSSFS RISSSLKPVQ ELLLPGDNLL KDIALVGGND SGIFVSSVHS
     GSAAEKAGLR EGHHLLLLEG CIRGESQSVS LDTSTQEEAH WTLQHCSGPV RLHYRANYDA
     YRRLQRDLAD GTLASGDSFY IRVNLNISGQ SDSCSLSVRC DEVVHILDTR YQGRCEWLCS
     RVDPYTSSDL MDRGTIPSNS RAQQLLLVKI QKLLCRGGKE ENEIHRNSRI SLQPEEASLL
     PDPKSSPRLS RASIFLTQIL QFVSRVDIKY KRMNSNERVR IINSGNTTLP RQGFEMLRPE
     DAADPDSELS RGLNLIPYSP VTPQRTQRRR PVLFTPTSLA KTIIQKILNM GGAMEFNICK
     PDTLTKEEFH LKQNVEPFIH YKEKHATFEC ITRENIEAVA AKGKHCLLEA ELSCVKDLLR
     REIYPIIIYV KICEKNVKKL RKLLQRVESE EEFVRSCRAK EKELEGIPCL YATLEPETWA
     GTDDLIRVIK DRILEEQKKI VWVEQDLL
//
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