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Database: UniProt
Entry: A0A3B3S458_9TELE
LinkDB: A0A3B3S458_9TELE
Original site: A0A3B3S458_9TELE 
ID   A0A3B3S458_9TELE        Unreviewed;      1628 AA.
AC   A0A3B3S458;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=IQ motif and Sec7 domain ArfGEF 2b {ECO:0000313|Ensembl:ENSPKIP00000025477.1};
GN   Name=IQSEC2 {ECO:0000313|Ensembl:ENSPKIP00000025477.1};
OS   Paramormyrops kingsleyae.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC   Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX   NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000025477.1, ECO:0000313|Proteomes:UP000261540};
RN   [1] {ECO:0000313|Ensembl:ENSPKIP00000025477.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the BRAG family.
CC       {ECO:0000256|ARBA:ARBA00006248}.
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DR   STRING; 1676925.ENSPKIP00000025477; -.
DR   Ensembl; ENSPKIT00000006213.1; ENSPKIP00000025477.1; ENSPKIG00000008307.1.
DR   GeneTree; ENSGT00940000159667; -.
DR   Proteomes; UP000261540; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0032012; P:regulation of ARF protein signal transduction; IEA:InterPro.
DR   CDD; cd13318; PH_IQSEC; 1.
DR   CDD; cd00171; Sec7; 1.
DR   Gene3D; 1.10.220.20; -; 1.
DR   Gene3D; 1.10.1000.11; Arf Nucleotide-binding Site Opener,domain 2; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR033742; IQSEC_PH.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR023394; Sec7_C_sf.
DR   InterPro; IPR000904; Sec7_dom.
DR   InterPro; IPR035999; Sec7_dom_sf.
DR   PANTHER; PTHR10663; GUANYL-NUCLEOTIDE EXCHANGE FACTOR; 1.
DR   PANTHER; PTHR10663:SF314; IQ MOTIF AND SEC7 DOMAIN-CONTAINING PROTEIN 2; 1.
DR   Pfam; PF16453; IQ_SEC7_PH; 1.
DR   Pfam; PF01369; Sec7; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00222; Sec7; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF48425; Sec7 domain; 1.
DR   PROSITE; PS50096; IQ; 1.
DR   PROSITE; PS50190; SEC7; 1.
PE   3: Inferred from homology;
FT   DOMAIN          743..936
FT                   /note="SEC7"
FT                   /evidence="ECO:0000259|PROSITE:PS50190"
FT   REGION          46..146
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          170..266
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          355..408
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          421..486
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          504..551
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          564..740
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1127..1187
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1209..1309
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1345..1383
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1412..1516
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1531..1608
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        46..64
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        132..146
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        183..223
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        243..258
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        425..446
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        593..617
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        635..651
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        665..681
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        689..718
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1162..1180
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1272..1295
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1364..1378
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1455..1481
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1495..1516
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1628 AA;  177246 MW;  F780FBCA45C2762C CRC64;
     METGQGSPES PNRAVEYLLE LNNIIESQQK LLETQRRRIE ELEVQLDRVN QENKDLRLDR
     RPRMPDVSGS AQPGSDAALP TNSHGDSAPP PPLPARERRG HARLTRGLSC GSAPVERGRP
     NRPDCSGAGH AKTLQRQLSS NSTPCNLTAT KASATTASSL LHPNLTANSH CRHHHCSHSR
     PRLSRSARSP PSAKHTEQAS VDTEPQRTES GSFSDSACSQ AAYPRSSERR GDAPRGPTVA
     ATSPVSLAWS QRTRHQPASL ALRKQEEEEN KRCKTLSDSY ELSTDLQDKK VEMLERKYGG
     YFLSRRAART IQTAFRQYRM NKNFERLRSS ASESRMTRRI ILSNMRMQYS FDERQPVTQQ
     QHYPHGAGPP SPPQHGRSRS PPTGPERDSG SPPRLQGNRS GEYTHLDDSF NKQVKSLADS
     IDDTLTCRPG RDDSQEGSRE GEGIGGVEGD DFGECVWSNS SNPLSRRGHS ERERGGGGGL
     SMHEDSTATS YSDVTLYMDD GLPSSPLSLD RAPSSTDTEY WGMGGGVGIR EDSRDTEGGG
     SSNSRRSTPC TECRDYRLRG AHLPLLTIEP PSDSSVDMSD RSDRGSLGRQ LVYEQEPSGS
     PQGTLKHGTS ARSMVAAQGQ TRAAGRPHPS IPSQVPHHPH HHHHHHPHHH HQYPDTPSSS
     SSPQQPPATP LSSSSSAPVP AGSLEQPCCS DGDNDSLNST TNSNETINCS SGSSSRDSLR
     EPLPPLGKQT YQRESRHSWD SPAFDNDVVQ RRQYRIGLNL FNKKPEKGIQ YLIERGFVSD
     TPVGIARFIL ERKGLSRQMI GEFLGNRQKQ FNKDVLDCVV DEMDFSGMDL DDALRKFQAQ
     IRVQGEAQKV ERLVEAFSQR YCVCNPAVVR QFQNPDTIFI LAFAIILLNT DMYSPNVKPE
     RKMKLEDFIK NLRGVDNGQD IPRDLLVGIY QRIQKWELRT NDDHVSQVQA VERLIVGKKP
     VLSLPHRRLV CCCQLYEVPD PNRPQRTGVH QREVFLFNDL LVVTKIFQKK KNSVTYSFRQ
     SFALVEMQVH MFQNSYYPHG IRLTSAIPGG ERKVLIVFTA PSQQDRTRFT TDLRESVAEV
     QEMEKYRVES ELEKQKGVMR PSLLTGGVLA GGGTVGGGVK SEVVNGSLGR PSLDDTYSTG
     EGLKRTALSS SLRDLSETGK RGRRNSVGSL DSTIEGSIIS SPRPHQRLPM ATMVSGCYGL
     EDYRSHRPIL SPGSGVGGGP GQQHNAAGTV GTGGGGPVSS SVEKGGMGNA TGGGSGSFLG
     SLFGSKRGKA PGPIIPPGPH YPAPVPPPTS GGPPPLSPSS LCQSDGGPSK IQALHAQYCH
     TGAGQPPPPY QHHHRYSVQT VPLPSQAASA PVANHHTLQR GSLPRRPPPA PSHAPPPPVS
     QHAMQGRYTG MALAGGCPVP LSPHSLHSPL PPYTLYHAQH TPSVRGGAPP GKPPLTLAHS
     QPHTHSHVHP GHAPHPSSHP VPPPHFVFGA PAQPPPGPIT ARLLPQGAQY LPQYPPLSSI
     PPPPPPPPPP PPPPFPPPFL PPYPSYASLP SPPPAPWPAT AGSWSTGGSG GRGPGQRHRY
     RGELQIQARQ SDQHRGLRDS LVWGRGTPGG TLRANSGDRA VVDQGGGASR KKRSFLRLCY
     FHLRFPHM
//
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