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Database: UniProt
Entry: A0A2Y9E8D2_TRIMA
LinkDB: A0A2Y9E8D2_TRIMA
Original site: A0A2Y9E8D2_TRIMA 
ID   A0A2Y9E8D2_TRIMA        Unreviewed;      1487 AA.
AC   A0A2Y9E8D2;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=IQ motif and SEC7 domain-containing protein 2 isoform X1 {ECO:0000313|RefSeq:XP_004389173.1};
GN   Name=LOC101359073 {ECO:0000313|RefSeq:XP_004389173.1};
OS   Trichechus manatus latirostris (Florida manatee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Afrotheria; Sirenia; Trichechidae; Trichechus.
OX   NCBI_TaxID=127582 {ECO:0000313|Proteomes:UP000248480, ECO:0000313|RefSeq:XP_004389173.1};
RN   [1] {ECO:0000313|RefSeq:XP_004389173.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the BRAG family.
CC       {ECO:0000256|ARBA:ARBA00006248}.
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DR   RefSeq; XP_004389173.1; XM_004389116.1.
DR   STRING; 127582.A0A2Y9E8D2; -.
DR   GeneID; 101359073; -.
DR   KEGG; tmu:101359073; -.
DR   InParanoid; A0A2Y9E8D2; -.
DR   OrthoDB; 204547at2759; -.
DR   Proteomes; UP000248480; 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; cd14686; bZIP; 1.
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;
KW   Reference proteome {ECO:0000313|Proteomes:UP000248480}.
FT   DOMAIN          745..938
FT                   /note="SEC7"
FT                   /evidence="ECO:0000259|PROSITE:PS50190"
FT   REGION          65..89
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          108..148
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          160..289
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          478..577
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          622..725
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1090..1258
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1270..1487
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        65..82
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        125..139
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        160..180
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        205..239
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        257..278
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        519..535
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        542..559
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        562..577
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        648..669
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        693..721
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1109..1123
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1157..1171
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1175..1192
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1193..1207
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1236..1250
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1273..1315
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1365..1379
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1422..1473
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1487 AA;  162807 MW;  6E355CDF12409165 CRC64;
     MEAGSATPGG TGSESPNRAV EYLLELNNII ESQQQLLETQ RRRIEELEGQ LDQLTQENRD
     LREESQLHRG ELHRDPHSAR DSPGRESQYQ NLRETQFHHR ELRESQFHQA ARDVGYPNRD
     GAYQNREAVY RDKERDASYP LQDSTYPPRE RDVAQCHLHH ENPALGRERG GREAGPAHSG
     REKEAGYSAA VGVGSRPPRE RGQLSRGASR SSSPGAGGGH STSTSTSPAT TLQRKSDGEN
     SRTVSVEGDA PGSDLSTAVD SPGSQPPYRL SQMPPTSSHM GGPPVGVGLP WAQRARLQPA
     SVALRKQEEE EIKRSKALSD SYELSTDLQD KKVEMLERKY GGSFLSRRAA RTIQTAFRQY
     RMNKNFERLR SSASESRMSR RIILSNMRMQ FSFEEYEKAQ NPAYFEGKPA SLDEGAMAGA
     RSHRLERGLS YGGSCGGGID GGGSSVTTSG EFSNDITELE DSFSKQVKSL AESIDEALNC
     HPSGPMSEEP GSAQLEKRES KEQQEDSSAT SFSDLPLYLD DPVPPPSPER LPSTEPPTQG
     RPEFWAPAPL PPVPPPVQPG TREDGGREEG TRRGPGCLEC RDFRLRAAHL PLLTIEPPSD
     SSVDLSDRSD RGSVHRQLVY EADGCSPHGT LKHKGPPGRA PIAHRHYPAP EGPAPAPPGP
     LPPAPNSGTG PSGVPGGRRL GKCEAAGENS DGGDNESLES SSNSNETINC SSGSSSRDSL
     REPPATGLCK QTYQRETRHS WDSPAFNNDV VQRRHYRIGL NLFNKKPEKG IQYLIERGFL
     SDTPVGVAHF ILERKGLSRQ MIGEFLGNRQ KQFNRDVLDC VVDEMDFSSM DLDDALRKFQ
     SHIRVQGEAQ KVERLIEAFS QRYCVCNPAL VRQFRNPDTI FILAFAIILL NTDMYSPSVK
     AERKMKLDDF IKNLRGVDNG EDIPRDLLVG IYQRIQGREL RTNDDHVSQV QAVERMIVGK
     KPVLSLPHRR LVCCCQLYEV PDPNRPQRLG LHQREVFLFN DLLVVTKIFQ KKKILVTYSF
     RQSFPLVEMH MQLFQNSYYQ FGIKLLSAVP GGERKVLIIF NAPSLQDRLR FTSDLRESIA
     EVQEMEKYRV ESELEKQKGM MRPNASQPGG AKDSVNGTLA RSSLEDTYGA GDGLKRGALS
     SSLRDLSDAG KRGRRNSVGS LDSTIEGSVI SSPRPHQRMP PPPPPPPPEE YKSQRPVSNS
     SSFLGSLFGS KRGKGPFQMP PPPTGQASAS SSSASSTHHH HHHHHHGHSH GGLGVLPNGQ
     SKLQALHAQY CQGPGPAPPP YLPSQQPPLP PPPQQPPPLP QLGSIPPPPA SAPPVGPHRH
     FHAHGPVPGP QHYTLGRPGR APRRGAGGHP QFAPHGRHPL HQPTSPLPLY SPAPQHPPTH
     KQGPKHFIFS HHPQMMPAAG AAGGPGSRPP GGSYSHPHHP QSPLSPHSPI PPHPSYPPLP
     PPSPHTPHSP LPPTSPHGPL HASGPPGTTN PPTANPKAKP SRISTVV
//
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