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Database: UniProt
Entry: A0A3Q1C363_AMPOC
LinkDB: A0A3Q1C363_AMPOC
Original site: A0A3Q1C363_AMPOC 
ID   A0A3Q1C363_AMPOC        Unreviewed;      1811 AA.
AC   A0A3Q1C363;
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=Disks large homolog 5-like {ECO:0000313|Ensembl:ENSAOCP00000014826.1};
GN   Name=DLG5 {ECO:0000313|Ensembl:ENSAOCP00000014826.1};
OS   Amphiprion ocellaris (Clown anemonefish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Amphiprion.
OX   NCBI_TaxID=80972 {ECO:0000313|Ensembl:ENSAOCP00000014826.1, ECO:0000313|Proteomes:UP000257160};
RN   [1] {ECO:0000313|Ensembl:ENSAOCP00000014826.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   Ensembl; ENSAOCT00000031612.1; ENSAOCP00000014826.1; ENSAOCG00000019649.1.
DR   GeneTree; ENSGT00940000155303; -.
DR   Proteomes; UP000257160; Unplaced.
DR   GO; GO:0042981; P:regulation of apoptotic process; IEA:InterPro.
DR   CDD; cd01671; CARD; 1.
DR   CDD; cd00992; PDZ_signaling; 4.
DR   CDD; cd11860; SH3_DLG5; 1.
DR   Gene3D; 2.30.42.10; -; 4.
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; IPR006907; DLG5_N.
DR   InterPro; IPR035537; DLG5_SH3.
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   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   PANTHER; PTHR46360; DISKS LARGE HOMOLOG 5; 1.
DR   PANTHER; PTHR46360:SF1; DISKS LARGE HOMOLOG 5; 1.
DR   Pfam; PF00619; CARD; 1.
DR   Pfam; PF16610; dbPDZ_assoc; 1.
DR   Pfam; PF00625; Guanylate_kin; 1.
DR   Pfam; PF00595; PDZ; 4.
DR   Pfam; PF04822; Takusan; 1.
DR   SMART; SM00072; GuKc; 1.
DR   SMART; SM00228; PDZ; 4.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF47986; DEATH domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50156; PDZ domain-like; 4.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS50209; CARD; 1.
DR   PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR   PROSITE; PS50106; PDZ; 4.
DR   PROSITE; PS50002; SH3; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000257160};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          1..92
FT                   /note="CARD"
FT                   /evidence="ECO:0000259|PROSITE:PS50209"
FT   DOMAIN          596..688
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          683..774
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          1261..1340
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          1394..1474
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          1485..1553
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          1667..1797
FT                   /note="Guanylate kinase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50052"
FT   REGION          94..114
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          833..874
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          967..1071
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1145..1260
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1345..1392
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          165..234
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          283..386
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          415..575
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        97..113
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        837..872
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        967..990
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        999..1028
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1049..1071
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1149..1179
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1194..1241
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1811 AA;  203639 MW;  C78C32535580F34E CRC64;
     MEPKHKELLE KCYQNLVESI TDADRVVDVL AHCGTLSQSE RYELGHNCSS NSEKVDLLLK
     ILTSKDRDHF AEFCSALEAT HPHLHSVLLN GIGPVDHTTG TPGQASSPPP AHMESHQVNE
     KMETVLFQLR HVTRERDDLR KRLALSSPGT TFDDCRPNSK AGHDYERLKL QCMKAMADLQ
     SLQNQHSTTL KRCEEAVKKA DFYHTLHSRL ASEHTQLKEE LEAVRQDNIQ LVREHNHVKQ
     ACEELRRLHD DDQREVADMR MLHQQVMREG SSDVLNKLYD TAVDKLEAMK SDYEALRKHY
     NEKTANHNAD LSRLDQAEEE NHRLQKQLDM LLKQRDAAIH YQQQYSSSIR RFDNTQQELS
     KATAQNKELQ REMDRLQSET TRLKTQQLKA AKDSEKYKEE RDSVISEYRL IMSERDQVIK
     EVDRLQTGLE VAEAKLKNTS SERRVANEEL EALRQKQDCA TLDMERANKE IEMLRKQYEA
     ISQELKEALQ EAEVAKCRRD WAFQERDKIV AERESIRTLC DNLRRERDRA VSDLADALRN
     LDDMRKQKND ASRELKELKE KLEDQLEKEA RYRQLMAHSS HDSAIDTDSM EWETEVVELE
     KHRVRIDMDL KALGFDIAEG VNDPYLPGDC GIFVTKVDKG SIAEGRLRVN DWLLKINDVD
     LTNKDRTQVI KTVLSGEGVI NMVVRRRKSL GGRIITPIQI NLAGQKDSGI GLESGVFVAT
     LAAGSPAARD CNLTVGDRLL AINGIALENK SLSECESLLR NCHSSLSISL MKFLPQSSSG
     QSLFETLRDS EKTSRVQTCE VHTRNCRNSK HNCSTQTDIC SCDLGSREED TCKDTGDSLD
     SSSSSAHSHH KPFSNSSLHS HSLSTSHSSS EPHPEFCYRR QDLHHRPFTF TPVISDCTSP
     QAAVDQLQSS PVKASGGTWP RVIAGASIPE CTQLSIYKKP KQRKSIFDVN AFRRPETTPK
     LDYMSLSQLP KHSPQSSLSE SAQTPPTPPA RSDSFRFKHR QQNSSASDST ITTGTPPASP
     AQATSRQDDG EVGKQHYYTD APPGETKTNS KKPAEEEGSR HRTEVLEKKR YRPKSAPALR
     RNVTPLHIPV PIGLAPCPAV TAVMRNPVYT AWSHEIQTNN CPPAPSSGIH PPQHQGRLSL
     DLSHKRTGDM TETSCSQPPH STHSLPSSAR LSSSATLQFR AERIKIPPTR YPRSTGSDRG
     SLSHSECSSP TPPMSPVNLE TSSFTSSQSQ SSISTQPRIS VSPAPVGDRR KDGPYLEEPR
     NVTVQKGAEP LGISIVSGEN GGVFVSKVTA GSIAHQARLE YGDQLLEFNG INLRNANEQQ
     ARLVIGQQCD TVTILAQYNP HMFQLGNHSR SGNQPTPRES GATTPDHHSN VDTLSEQDEG
     TMTPPSKQTT PSRLVRLKRI HVELGVQICG GNLYGIFVES LDDDSPAKSA DGLLTGDLIL
     EYNGISMKNK TKEDAYLELL KPAETITFKV QNRVDILAEI KESPGDGFFI RALYEKVAEV
     EQDLSFKKDD ILYVEDTLPN GNFGYWMAWQ LDENAQKLEK GQIPSKYMMD QEFYRRHSMA
     DMKDDNGTSK TLSAAARRSF FRRRLKHKRS GSKDGKDLTA LDAISTDSLP ITEDGVSLMY
     QRVQKVECSS PRPVLVLGPL VEASKDMLVK EAPAKFCRCL PEIMKASQQA IERGVKDCVF
     IDYKRRSGHF DVTTVASIKE ITEKDCHCLL DIAPHAIERL HSVHIYPIVI FIRYKNAKQI
     KEQKDPLYLR DKLSQKHSKE QFEAAQKVEQ EYSRFFTGVV QGGSVSYICT QIMTIVEQEQ
     SKVLWIPDGA P
//
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