ID A0A0V1CYE7_TRIBR Unreviewed; 1387 AA.
AC A0A0V1CYE7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 22-FEB-2023, entry version 29.
DE RecName: Full=DH domain-containing protein {ECO:0000259|PROSITE:PS50010};
GN ORFNames=T03_14482 {ECO:0000313|EMBL:KRY54279.1};
OS Trichinella britovi (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY54279.1, ECO:0000313|Proteomes:UP000054653};
RN [1] {ECO:0000313|EMBL:KRY54279.1, ECO:0000313|Proteomes:UP000054653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS120 {ECO:0000313|EMBL:KRY54279.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRY54279.1}.
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DR EMBL; JYDI01000072; KRY54279.1; -; Genomic_DNA.
DR STRING; 45882.A0A0V1CYE7; -.
DR Proteomes; UP000054653; Unassembled WGS sequence.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 1.20.900.10; Dbl homology (DH) domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR InterPro; IPR039919; ARHGEF10/ARHGEF17.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR001331; GDS_CDC24_CS.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR12877; RHO GUANINE NUCLEOTIDE EXCHANGE FACTOR; 1.
DR PANTHER; PTHR12877:SF15; RHO GUANINE NUCLEOTIDE EXCHANGE FACTOR 17; 1.
DR Pfam; PF19057; PH_19; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR Pfam; PF19056; WD40_2; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS00741; DH_1; 1.
DR PROSITE; PS50010; DH_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000054653}.
FT DOMAIN 519..681
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT REGION 119..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 333..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1017..1039
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 664..708
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 119..152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..173
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..373
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1387 AA; 154743 MW; A194D58C6F565069 CRC64;
MPVTISADEC DSMALRDWSG RGERHLRKRY SRSFTMSPPA GAKPSTRAVV LDGSAVGSVA
LAGKRGSLTS VNKKPDLPVW ARMPALRKTN SVPSSICNGE AGTMLFSIGS ASRKSSSQSA
SSCFSNCLTP PGLEQPSSDE PDWSTPRGSF AVTNDHSLDH DHNRDHDDDH DRDRGEDQDA
DDEDTTGLLS PSTTNTDISE LQAAAQTIEA LSRRNWRRVS DFTSALPLTE MNLSPTSTAL
DRHRVSRRSG ITTHLGGQPR GVIQFLPSVR KSDILSRNVH QAYMVDKVRR QRLCSDGNLI
SMPQMADQLC LRVPPTAVGD SDVSDAQMRL GVLSSKNSSP NSCRSSTPRS GYNGRGSSRY
VGAETSPRKS LSTTGAGRPP PDMLLTNADD DRFSTLDTLD SVNRFTSLLR SLRSPSAGIP
DADRYPSSTA DCTLSSSSEL SDITDYSYNS PPSEGILSDS DSSFLQADLL LWRRRSKGSI
RKHQARYKNS YCERIIRNRN FLCRKFETSG SCKNSCFKYL RPLKRPELCS LVELGTLNEI
FFQVPEMLGH HELFLAALKS RLDFWDCKQK IGDVVLNNFT KQSVIDTYTA FINNWKNARV
AIRKACIAKP AFAKYLERCS REHQNKLNLD ALLIMPVQRI PRYELLIKEL VKHTSVEHPD
HALLLRAGKE IHELASKIDQ IQQETGFSDQ MQQKLREIEA IVEGLDDLVS PERTFYRCDQ
VYVETPSGKK DRCLFLFSDL LLITTVTSKS GSNLSKSSQQ TSPGLSRNFF EKHKFRLLLK
LSLQDLSIVD NKKLLIMKVR EDIANLQEDL RVVGKLAELT LLLKIDHKGI SKEIENLSDF
IKVTLGTKHE ELAKDPNLAS LNLMVTTEFG NEPLLMTFRN TEKRLTWERN FEDAKYAFAL
SQSQRQPPAF VKFIAANRTR AGLHFTCASP AWPRNSVGTS DVWMCSSDQC SGQLCVLSAS
TDFEVININS LCNSRISCIC CIPGNGGPRN AIVVGAKSRK LPSRGILTNN NHLTMPTNID
LDSDTTDNES STEESRISEV DRVDDKLSRN YMLSTVSQKI PHLDAENCEF LFTTWIGTEN
GIIQIYDRNE SMRTGKCKSE MQLQSSIRCM LYHENKIFVA LGDGSVGLYD CDDENQKSMK
FLELEEKFAP ISAMVIAVNK LWCGSRNHIL VINLSTFKIE CLFAVNNDRE STIECLASSA
LAVWLSMYNS AVVKLYHAHK RECLIEINVA PTVTKTLAGC DDIIRQHKLA CLRVTSLLCC
KEMLWVGTSA GVLCYLPIPQ VTHQTLKITT IPGISGTNIG HMGPCRFLVS LEVPEYIMDE
FVAGKRAKRN DLSRRRMSLN VASLQQKNVY VISGGEGLED FQDSQNDEND DTFGLEDSTN
YLIIWKA
//
