ID A0A0V1L674_9BILA Unreviewed; 2647 AA.
AC A0A0V1L674;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Triple functional domain protein {ECO:0000313|EMBL:KRZ55005.1};
GN Name=trio {ECO:0000313|EMBL:KRZ55005.1};
GN ORFNames=T02_10333 {ECO:0000313|EMBL:KRZ55005.1};
OS Trichinella nativa.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6335 {ECO:0000313|EMBL:KRZ55005.1, ECO:0000313|Proteomes:UP000054721};
RN [1] {ECO:0000313|EMBL:KRZ55005.1, ECO:0000313|Proteomes:UP000054721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS10 {ECO:0000313|EMBL:KRZ55005.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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:KRZ55005.1}.
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DR EMBL; JYDW01000125; KRZ55005.1; -; Genomic_DNA.
DR Proteomes; UP000054721; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR CDD; cd13240; PH1_Kalirin_Trio_like; 1.
DR CDD; cd13241; PH2_Kalirin_Trio_p63RhoGEF; 1.
DR CDD; cd00160; RhoGEF; 2.
DR CDD; cd00170; SEC14; 1.
DR CDD; cd00176; SPEC; 3.
DR Gene3D; 1.20.58.60; -; 4.
DR Gene3D; 3.40.525.10; CRAL-TRIO lipid binding domain; 1.
DR Gene3D; 1.20.900.10; Dbl homology (DH) domain; 2.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 2.
DR InterPro; IPR001251; CRAL-TRIO_dom.
DR InterPro; IPR036865; CRAL-TRIO_dom_sf.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR001331; GDS_CDC24_CS.
DR InterPro; IPR047054; Kalirin_TRIO_PH_1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR InterPro; IPR002017; Spectrin_repeat.
DR PANTHER; PTHR22826:SF117; PLECKSTRIN HOMOLOGY DOMAIN-CONTAINING FAMILY G MEMBER 4B-RELATED; 1.
DR PANTHER; PTHR22826; RHO GUANINE EXCHANGE FACTOR-RELATED; 1.
DR Pfam; PF13716; CRAL_TRIO_2; 1.
DR Pfam; PF00621; RhoGEF; 2.
DR Pfam; PF00435; Spectrin; 2.
DR SMART; SM00233; PH; 2.
DR SMART; SM00325; RhoGEF; 2.
DR SMART; SM00516; SEC14; 1.
DR SMART; SM00150; SPEC; 6.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 2.
DR SUPFAM; SSF50729; PH domain-like; 2.
DR SUPFAM; SSF46966; Spectrin repeat; 4.
DR PROSITE; PS00741; DH_1; 1.
DR PROSITE; PS50010; DH_2; 2.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658};
KW Reference proteome {ECO:0000313|Proteomes:UP000054721}.
FT DOMAIN 1305..1480
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1497..1603
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 2086..2261
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT REGION 516..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1635..1662
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1785..1813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1873..1912
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1980..2013
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2054..2080
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2459..2522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2592..2647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 945..979
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1637..1662
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1790..1811
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2054..2079
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2470..2499
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2508..2522
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2604..2640
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2647 AA; 298869 MW; AD75EE66432CD4B9 CRC64;
MANVQSFTQT DFASGLLKAS DVKHILNEKV ALLTGGRDRC GRPIISFPAR ENADKISAED
LRMVLLYLFA VPSDESKDIG FVVLIDMRNK MSWTSVKPIF KCLQSDFQIM RLSLEAVSAR
VNQQLPEAGK CDIFSKQVQS VYLVKPDRFW EKHKATVASN KYKFEVHTVS VENLVKYIDR
NQLTAEFDGT YPYNHEEWLN LRITLESFIW RSMDVLRIFN NIQKELEQHN LPTDVDHAKS
ALDEHAKLKK RIGKAPIEEL EQEGQRLAHR LAGGNEEVSS CTSDSDYASG GRNSQCNPDF
TCAVPHIASL LNNLRITRQN LYTQWQAHKI RLDQCFQLKL FEQDAEKMFV WIRQHADLFW
TNFSDVGDSH ESASAVQREH EQFTKAAVNT YVNINHIMTC AQRLLDNGHY ASPIIRAVAN
RLERDWKMFI NALDVRAGVL RLSLQFHLKS NQYLTNVKEW HRSCMSATEL PSTVAALEAA
IQEHQQLFET VSQVYAEATR DGKALIQSLK TPPALTLTDA ESTTTDSKST TTSGLSEDSQ
NLAPVVEIIH KLLGWQRQLE DAWQQKRIKL HHKLALLFFQ QDVKRVIDWL DDHGESFLRR
NHGVGRTLQR ARALQRSQQQ FEDVAKNTYT NADKLLVAAQ DLATGGELHP DQICSTAQQL
HSRISVFAKR VQARRNLLNY AVLFHTHYNE ITSWFKELER LDANVNVVGN TVQECEQHLD
QWLARTEATR QATLTARNEG MQLISLLRQQ SVLEGSDNVE SISFVEGMVK DIDTKQNHFE
ERWKVQRFQL DIGLQFRVFE QDSISVISQL DGWSEDMRAM SNNVTVDRVE KILPLHQENT
GQVQAAIADI MQSAQDVIQL IENSGIYLLV SSGGLVLDCI IRLTDKIRQQ ERDVLSLAED
VQSKLEQIVS LGQLQSLANQ VATCINNEEQ MLSATSAVPC TLNEAEQLQT EHRQFQLAIE
KTNESLLALQ QKAEAMLSKD HCEENMVRNI LEEVIVRWRP LIALTEERHK LLTSAVTYYK
TLDQVLPVLD SLEEDYQTER DWCSWYAKQA SSSQDPKSSS RLLQDKPSYM SQQIAKHKDN
KERFLRVGCS YARKNSDLFL KYVRRSMHQP QQQSVVISSK QVEGRVLQAL ENLRTRENHI
LSLWTKKKRR LDQCQEYVLL EASGLKFLNW IHDGGESYLT AHATNSLSRP VAEELLKEHD
NFVAKAKEQL ASVRLFLDVG DSMLKKDPQH IHYNDISQWM NTVKQQYNDF SQKIDLHRRR
LEAALGRPEK PTHELALDRQ SDSSLDEKFL DQKDALENKR KSAKRKDFIM AELLQTERVY
VNDLDVCIRS YMESMTTEPN VPASIAGKQD VIFLNLKQIH DFHSKIFLQE LEKYESLPED
VGHCFVTWAE KFQMYVSYCR LKPNSNNLVT QSDASSFFDE VQKLRGLSLP LAAYLIKPVQ
RITKYQLLLK DLLGCCEEEK GEIRDGLEVM LNVPKKANDI LHLSMLEGCS DVDSLGDVLL
QEQLIVWDPR QLIKKGRERQ VFLFEICMIF SKKVSDQTGK FKYVYKMRVL TSEMNVTEHI
EGDECKFAIW TGKVPNNDTK TILKASSLES KLTWVRRLRD LISERILHFD LPYLSLTKVR
GQQVNYHQKC AIDERRVSNQ SDTGSTNTEI SGENSAPATG DEMVSQNRCT DVVESKQHLP
SAEENAIVFL VTDDHIPLPE GAAHGQITVC KGERVQLVSA IVSDEGEFRM VRVLDTEQQQ
QMCREGYVPA DKLQLIATKI DSVDDDDDDD SEESAAVAIV EKRKITIEND DDNDEEEESE
EEEEEEKIEA ETENVEQMKR KNLRRCVEDY FFFLFFFLTE NLAENDENCQ EIGRKWFSLS
SQRRLVRHQF NSGSLCSSKS DSRKNSTAAV AGAAEQQSNS LNGGTSQEVT PGAAFPGSLA
PLNCRPSSLL SRAPTVVRSE IIAAELAPNV VDEDLTLPQD IVIPPPMESL ASEKLIAAND
QQKQSNSSNN NNNTSNNNSI TGSVTTSSGS SAGEELLLSS GGVISKMDRL QLYADDQSSS
QTCLSSSALA NQTAAGSLES EKSEPSLSAN GTRTTEISEQ QQAVEKRRYV LQELVETERD
YVKDLGSIVE GYITTIESME LPEDMKGKER IVFANIQQIY EFHKNIFSKE IEKCLEDYEA
AGRAFVKYER RLHMYVVYCQ NKPKSEFLVS EYESFFNDIK QKLGHRLTLT DLLIKPVQRI
MKYQLLLKDI VKYTARANED TTVLNKALQV MLVVPKACDN MMHVGRLQGF DGKITSQGKL
LHQGLVVYNS TLPLFKRRYS SFYFISRDRN LINVPFLGIS GQFQCERILL LVKVLPSGTL
LVSDNPSPQL FKPKERRVFL FEQSLIIADC IPSKKEFGCP NYIYKTHIMI NKLGLESDVP
GEPLRFILKN KDPANQVDTV VQANPGEKEQ WVSCIKQLLD TQMNFLKALQ HPIAYQKGLS
KDDSKEEVTA ELTTSSSIGG GGASGNGRLN VSSSGDFSEE SPARGMLNAC SRSRSQNSNL
VVPNSVSNVS ALRRASNAEG SVVETTKKSH MLPMRSGHLI AGAKEGTSDA ASPRSSKNKL
FGGIRHTLKS KTGGTATAAA AAAATGGGSS TSAFANTVPP SNTNSRSCGG SKTIKSPTSP
VSGIKPK
//
