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Database: UniProt
Entry: A0A3Q2D471_CYPVA
LinkDB: A0A3Q2D471_CYPVA
Original site: A0A3Q2D471_CYPVA 
ID   A0A3Q2D471_CYPVA        Unreviewed;      1999 AA.
AC   A0A3Q2D471;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Disks large homolog 5-like {ECO:0000313|Ensembl:ENSCVAP00000013268.1};
OS   Cyprinodon variegatus (Sheepshead minnow).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Cyprinodontidae;
OC   Cyprinodon.
OX   NCBI_TaxID=28743 {ECO:0000313|Ensembl:ENSCVAP00000013268.1, ECO:0000313|Proteomes:UP000265020};
RN   [1] {ECO:0000313|Ensembl:ENSCVAP00000013268.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   RefSeq; XP_015245327.1; XM_015389841.1.
DR   Ensembl; ENSCVAT00000020743.1; ENSCVAP00000013268.1; ENSCVAG00000000872.1.
DR   GeneID; 107094188; -.
DR   CTD; 569065; -.
DR   GeneTree; ENSGT00940000155303; -.
DR   OrthoDB; 2877432at2759; -.
DR   Proteomes; UP000265020; 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; 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:UP000265020};
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          678..768
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          763..854
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          1424..1503
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          1584..1664
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          1675..1743
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          1855..1985
FT                   /note="Guanylate kinase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50052"
FT   REGION          88..123
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1035..1245
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1281..1391
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1507..1580
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          126..461
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          490..654
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        93..123
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1051..1081
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1128..1144
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1152..1177
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1281..1341
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1358..1391
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1507..1574
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1999 AA;  224512 MW;  C48371413EC02776 CRC64;
     MEPKHKELLD QCHQNLLESI TDADRVIELL IVSGTLSQLD RFELEQNCAS SAEKVDHLLK
     MLMNKESDHF LDLCVALEKA YPDLHSALFS NNGGGPVDHS TGSPVNGETS SPPPAVNDNR
     HASENLDTIL LQLRQVTRER DELRKRLALA SPGTTFDDCR PNPKASHDYE RLKSQCMRAM
     ADLQSLQNQH TKTLKRCEEA VKEADFYHML HSRVLGDQTQ LKEEMETVRR DNAQLVREHN
     HLKQNCEELK RLHSQDQQEL SDLRQQQQEV MREKGSSEVL NKLYDTAMDK LEGVKKDYDA
     LSKRFGEKVA NHNTDLSRLE QAEEENRRLQ KQMDALLKQR DSAMHYQQQF STSMRRFDSV
     QQELNKSSAQ NKELQREMER LQSEVTRYKN LQLKAAKDCE KYKEERDSVF NEYRLIMSER
     DQVIKELDKL QTELEAAEAR LKNTSSERVV ASEELEALRQ ELNSSLVDRD RAICERNELL
     EKYCHEVKDK AEAQKELSQA CKDIEMVREE RDVARKERTE AIIQRDQLLR EYYQARQKQD
     SATLDMERAN KEIEMLRKQY EAMSQELKEA TQEAEVAKCR RDWAFQERDK IVAERESIRT
     LCDNLRRERD RAVSDLADAL RNLDDMRKQK NDALRELKEL KEKMESQLEK EARFCQLMAH
     SSHDSAIDTD SLEWETEVVE FEKDREDMDL KALGFDIAEG VNDPYLPGDC GIFVTRVDKG
     SVADGRLRVN DWLLKINDID LSNKDRKQVV KAVLNGGGLI NMVVRRRKSL GGRLVTPVHI
     NLMGHKDSGI GLESGVFVTA IAQGSPAARE GSLTAGDRLI AINGIALDNK SVTECEALLR
     SCRDSLSLSL MKFFPHSTSG QNIFESLRDS SEKTNGRMLL SEIHSRNSRN LKHNSSTQTD
     IFCPDVGSAS SSSISGDRRK LRGDDEMYGD VSKPFSSVSL HATSLRPLAD LGTGRYGPSA
     FQECCSYTKG PSSLPFEPIS HSECINMETA LEKKHSGGTW PKMMVGGMSV VPDSSGPITA
     AAQLSIYKSP KQRKSIFDPD TFKRPETPSS KLEYLTANQM SAVSSHSPQS SKTESLSSSS
     TPTPTPPTPP TRSDSFKFKH KHQSSSASDC TITSDGKGEA SISMAAGEGR ERNERERDRN
     GNHYFLEGKV LTSRKSCDED IGRTRGEEPE VKRPRPKSAP ALRRRTPKTI THPIYQSYSN
     DDHSPDSRDV LHSSPSPSNR HSVGLVPAVY NGSLPPNSAH RGLSPCPAVT AVMRNPVYTV
     RSHRVHTSNC PSVASQICHQ HTHTSPQHQG RLSLDLSQQK RTSDYSETAS SRSSRASHGT
     NSLPSGTRLG SSSNVQYRTE RIKIPSTPRY PRSMLGSDRG SLSHSECSSP SLITPPQSPL
     NLETSSFVSS QSQGSISTLP RISVSPVPIG ERRKDRPYLE EPRNVIVHKG AEPLGISIVS
     GENGGIFVSK VTGGSIAHQA GLEYGDQLLE YNGINLRNAT EQQARLIIGQ QCDTITIMAQ
     YNPHMYQLGN HSRSSSRLEP VSTQLTPQGS GTATPDSHSA IDTLSEQDEG TLTPSSKQTT
     PTTSPNSCVR MPSESNRRVS EPRLVTVHRP GVEVGVTLCG GNLRGIYIES VDEDSPARGP
     DGLLPGDLIL EYNSVNMKNK XAEEVYVEML KPAETVTLKV QHQPDDFSSV KDVPGDGFYI
     RALYDRVGEA EGDLSFKKDD ILYVDESLPK GSFGTWMAWQ LDENAQQIQR GQIPSKYMID
     QEFYRRHSVT EMKEDSSKTI SAAARRSFFR RKQKHKRSSS KDSKEMVPLD TISTDSIPFL
     DDCVSLAYQR VQKVECTSPR PVLVLGPLSD PVKEMLVKES PGKFCRCLLE VMKASQQAIE
     RGVKDCLFID YKRRSGHFDV TTVASIKEIT DKGCHCLLDI APHAIERLHS VHIYPIVVFI
     RYKNAKQIKE QKDPIFLRDK VSQKHSKEQF ESAQKIEQEY SKFFTGIVQG GNLPYICTQI
     TTIVDQEQSK VLWTPLGSP
//
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