ID A0A3B3DME0_ORYME Unreviewed; 915 AA.
AC A0A3B3DME0;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=IQ motif and Sec7 domain ArfGEF 2a {ECO:0000313|Ensembl:ENSOMEP00000031086.1};
GN Name=IQSEC2 {ECO:0000313|Ensembl:ENSOMEP00000031086.1};
OS Oryzias melastigma (Marine medaka).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=30732 {ECO:0000313|Ensembl:ENSOMEP00000031086.1, ECO:0000313|Proteomes:UP000261560};
RN [1] {ECO:0000313|Ensembl:ENSOMEP00000031086.1}
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 AlphaFoldDB; A0A3B3DME0; -.
DR STRING; 30732.ENSOMEP00000031086; -.
DR PaxDb; 30732-ENSOMEP00000031086; -.
DR Ensembl; ENSOMET00000022036.1; ENSOMEP00000031086.1; ENSOMEG00000015738.1.
DR GeneTree; ENSGT00940000159667; -.
DR OMA; MSVSHRV; -.
DR Proteomes; UP000261560; 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 454..646
FT /note="SEC7"
FT /evidence="ECO:0000259|PROSITE:PS50190"
FT REGION 195..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 247..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..362
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..379
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..429
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 915 AA; 101829 MW; 05FE62354AFDE560 CRC64;
ETLTFSDSSF GHPPPFHRYS NNPLPSLCDP YSPASTGRPL GTSYPASLAL RKQEEEESKR
CKALSDSYEL STDLQDKKVE MLERKYGGQF VSRRAARTIQ TAFRRYRMKK NFERLRSSAS
ESRMTRRIIL SNMRMQVCVK YPFFYSPTKL RRGLPCLSTS CDKCILGSAL QTVSASLLRT
SVSLQVKSLA DSMDDSLTCQ NTNTSSRRPA GRAEGIRGGG AAMHEDSTAT SFSDVTLYMD
DGCLPSSPLS RPASSSDTDY WGGGGAGGRE DSRETEGGSN ASRRSSTPCT ECRGEYRVRA
AGGGGGHLPV LTIEPPSDSS VDMSDRSVGG CHLQSPPSSP LPSPVPPLTP LSPLPPPLTP
SPLSSSSSSV LQNMEAQQQH LAHHPHLHHH HLLCSDGDNE SVNSTTTNSN DDTTVNNCSS
GSSSRDSLRE PVGGATLGKQ TYQRESRHSW DSPAFNNDVV QRRQYRIGLN LFNKKPEKGI
QYLIERGFVS DTPVGIARFI LERKGLSRQM IGEFLGSRQQ FNKDVLNCVL DEMDFSGMDL
DDALRKFQAQ IKVQGEAQRV ERLVEAFSQR YCICNPVLIR QFQNPDTIFI LAFAIILLNT
DMYSPNVKPE RKMKLEDFIK NLRGVDNGQD IPRDLLVAIY GRIQKWELRT NDDHVSQVQA
VERMVVGKKP RRVFVCLLQV LSLPHRRLVC CCQLFEVPDP NRAQRSGVHQ REVFLFNDLL
MVTKIFQKKK TSVTYSFRQS FPLLDMQVHT FQNSYYPHGI KLTSANPGGE RKVLIIFTAP
SQQDRARFTS DLRESIAEVQ EMEKYRVESE LEKQKGVMRP AGSGGGPMKG EVVNGTLGRP
SLDDTYASVD GLKRTALSSS LRDLSETGKR GRRNSVGSLD STIEVSWSVH EARCACCMFP
CMFQQNLKSL ISPVY
//