ID A0A3Q1HE31_ANATE Unreviewed; 2030 AA.
AC A0A3Q1HE31;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Discs, large homolog 5a (Drosophila) {ECO:0000313|Ensembl:ENSATEP00000005560.1};
OS Anabas testudineus (Climbing perch) (Anthias testudineus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000005560.1, ECO:0000313|Proteomes:UP000265040};
RN [1] {ECO:0000313|Ensembl:ENSATEP00000005560.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR STRING; 64144.ENSATEP00000005560; -.
DR Ensembl; ENSATET00000005651.2; ENSATEP00000005560.1; ENSATEG00000003830.2.
DR GeneTree; ENSGT00940000155303; -.
DR InParanoid; A0A3Q1HE31; -.
DR OMA; PCETITI; -.
DR OrthoDB; 2877432at2759; -.
DR Proteomes; UP000265040; 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:UP000265040};
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 701..791
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 786..877
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 1455..1534
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 1615..1695
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 1706..1774
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 1850..2016
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000259|PROSITE:PS50052"
FT REGION 103..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1091..1174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1186..1253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1329..1447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1539..1610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 149..484
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 513..677
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1094..1111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1158..1174
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1186..1207
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1218..1232
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1233..1247
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1329..1364
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1389..1433
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1539..1601
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2030 AA; 227701 MW; BF0BC07AAAA46165 CRC64;
MEPKHKELLD QCHQNLLESI TDADRVIELL IVSGTLSQLD RFELDQNCSS SAEKVDHLLK
MLMNKESDHF LDLCVALEKA YPDLYTALFS NNGGGPVDHS TGSTYSVLST MPSDSESSSS
LSSVGSPVNG EASSPPPAIN DNRPSGDNLD TILFQLRQVT RERDELRKRL ALASPGTTFD
DCRPNSKASH DYERLKSQCM RAMADLQSLQ NQHTKTLKRC EEAVKEADFY HMLHSRVLGE
QTQLKEEMET LRRDNAQLVR EHNHLKQSCE ELKRLHGQDQ KELADLRLQQ QQVMREKGSS
EVLNKMYDTA MDKLEGVKKE YDALSKRYSE KVANHNTDLS RLEQAEEENR RLQKQMDALL
KQRDSAMQYQ QQCSTSMRRF DSVQQELNKS SVQNKELQRE MERLQSEVTR YKNLQLKSAK
DCEKYKEERD SVFNEYRLIM SERDQVIKEL DKLQTELESA EARLKNTSSE RVVASEELEA
LRQELNSSLV DRDRAICERN ELLEKYCHEV KDKAEAQKEL SQACKDIEMV REERDVARKE
RTEAIIQRDQ LLREYYQARQ KQDSATLDME RANKEIEMLR KQYEAMSQEL KEATQEAEVA
KCRRDWAFQE RDKIVAERES IRTLCDNLRR ERDRAVSDLA DALRNLDDMR KQKNDSLREL
KELKEKMESQ LEKEARFCQL MAHSSHDSAI DTDSLEWETE VVEFEKDRDD MDLKALGFDI
AEGVNDPYLP GDCGIFVTRV DKGSIADGRL RVNDWLLKIN DIDLTNKDRK QVVKAVLNGG
GLINMVVRRR KSLGGRLVTP VHINLVGHKD CGIGLESGVF VTAVVQGSPA AREGSLTVGD
RLIAINGIAL DNKSVTECEA LLRSCRDSLS LSLMKFFPHS TSGQNIFESL RESSEKSNGR
IHLSEIHSRN SRNLKHNSST QTDIFCPDVG STSTSSISGE RKKVRGESDE AYCDISKPFS
TGSLHATSLR PASDLGTGRY GPSAFQECCP YTKAPSSLPF EPVSPSDCIT METTLEKKHS
GGTWPKMMVG GMSVAQDNTS PVTAAAQLSI YKSPKQRKSI FDPDTFKRPE TPSSKMEYMA
ANQIAAVAAS AAAASHSPQP SKAESLSSSS TPTPTPPTPP TRSDSFKFKH KHQSSSASDC
TITSDGKGEA VISMAAGESR ERSERERDRN GNHYFLDGKV LTSRKSCDED IGRTRGEEPE
VKRPRPKSAP ALRRRMTPQT ITLPTFQSYS NDEHSPEPRD MLRSSPSRSH RHSVGFVPTV
YNGILPPNSA HRGLSPCPAV TAVMRNPVYT VRSHRVHTSN CPSVASQICH QHTHTSPQHQ
GRLSLDLSQQ KRTNDYSEST SSRSSRASHG TNSLPSSARL GSANNVQYRA ERIKIPSTPR
YPRSMLGSDR GSLSHSECSS PSLITPPQSP LNLETSSFAS SQSQGSISTL PRISVSPVPI
GERRKDRPYL EEPRNVIVHK GAEPLGISIV GGENGGIFVS KVTGGSIAQQ AGLEYGDQLL
EYNGINLRNA TEQQARLIIG QQCDTITIMA QYNPHMYQLG NHSRSSSRLE PVSTQPTPQG
SGAATPDNHS TIDTLSEQDE GTLTPSSKQT TPTTSPRNLI RMPNEGSKKV GEPRLVNVHR
PGVEVGVTLC GGNLRGVYIE SLDEDSPARG TDGLLPGDLI LEYNSVNMKN KTAEEVYVEM
LKPAETVTLK VLYRPDDFNM LKDVPGDGFY IRALYDRVGE AEGDLSFKKD DILYVDESLP
KGSFGTWMAW QLDENAQQIQ RGQIPSKYMM DQEFYRRHSV TEIKEDSSKT LSAGARRSFF
RRKQKHKRSS SKDSKEMVAL DTISTDSIPF LDDCVSLAYQ RVQKVECTSP RPVLILGPLT
DPVKEMLVKE TPGKFCRCVL EVMKASQQAI ERGVKDCLFI DYKRRSGHFD VTTVASIKEI
TDKGCHCLLD IAPHAIERLH GVHIYPIVVF VRYKNAKQIK EQKDPIYLRD KVSQKHSKEQ
FEGAQKTEQE YSKFFTGIVQ GGTLPYICTQ IMTIVDQEQS KVLWTPLGCP
//