ID A0A0V1L7N6_9BILA Unreviewed; 2697 AA.
AC A0A0V1L7N6;
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:KRZ55006.1};
GN Name=trio {ECO:0000313|EMBL:KRZ55006.1};
GN ORFNames=T02_10333 {ECO:0000313|EMBL:KRZ55006.1};
OS Trichinella nativa.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6335 {ECO:0000313|EMBL:KRZ55006.1, ECO:0000313|Proteomes:UP000054721};
RN [1] {ECO:0000313|EMBL:KRZ55006.1, ECO:0000313|Proteomes:UP000054721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS10 {ECO:0000313|EMBL:KRZ55006.1};
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:KRZ55006.1}.
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DR EMBL; JYDW01000125; KRZ55006.1; -; Genomic_DNA.
DR STRING; 6335.A0A0V1L7N6; -.
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 1355..1530
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1547..1653
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 2136..2311
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT REGION 546..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1685..1712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1835..1863
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1923..1962
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2030..2063
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2104..2130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2509..2572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2642..2697
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 995..1029
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1687..1712
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1840..1861
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2104..2129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2520..2549
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2558..2572
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2654..2690
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2697 AA; 304767 MW; AB7F826803C04E7E 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 VSQVYAEIHS DSQRLLYEFD RLKRLYNFGI GQEDGDDATR 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 VKERVYIVDD
VVGVMIRTIQ 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
//
