ID A0A0V0UND1_9BILA Unreviewed; 1286 AA.
AC A0A0V0UND1;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Rho guanine nucleotide exchange factor 2 {ECO:0000313|EMBL:KRX52747.1};
DE Flags: Fragment;
GN ORFNames=T09_5947 {ECO:0000313|EMBL:KRX52747.1};
OS Trichinella sp. T9.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX52747.1, ECO:0000313|Proteomes:UP000054681};
RN [1] {ECO:0000313|EMBL:KRX52747.1, ECO:0000313|Proteomes:UP000054681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS409 {ECO:0000313|EMBL:KRX52747.1};
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 -!- 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:KRX52747.1}.
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DR EMBL; JYDN01000228; KRX52747.1; -; Genomic_DNA.
DR Proteomes; UP000054681; Unassembled WGS sequence.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd20805; C1_DGK_rpt2; 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 InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR041020; PH_16.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR13944; AGAP007712-PA; 1.
DR PANTHER; PTHR13944:SF21; CYSTS, ISOFORM C; 1.
DR Pfam; PF17838; PH_16; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000054681};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 296..345
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 454..672
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT REGION 159..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 932..962
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1149..1188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1259..1286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1012..1072
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 932..954
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1261..1286
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRX52747.1"
SQ SEQUENCE 1286 AA; 143295 MW; 58EE22CAAC548A0B CRC64;
LFKFISTAQR YHTTVLIGMK RDVSVSWPNL AEIPSRTPST SFSICCLIKS HSLTASSQSV
EACQLSFADN GVDLAATASH GVHKHFADGS RRSCSGDDGT PMKLAVDRGA PVKLSKSVEC
VVPGTVRVNL GCSKSEVDLS QLSAASRLSE KRFSLGDQSS LAQRLHDSSN EEDPAGTTAL
TANPADQQKE LLKFVDNAVH LDRSFSSTPS IDVDSSLAYF AVLPRDKPNE VSRERLRQIR
ASSMVVPAIT PRLPLMGLLP KAVGKASNDK VDLKSIEKVL KLRSSKKHAK VKEKKQHVWL
QCQEKAGLNC DICNKAEGNY SFVRCTECHA VLHSHCKAAA NKASCSRGKA ASKHSSVMFQ
TRPLSLVSRF SSFRSDSSSS VIGQIYAETS NRSGPLPQSA DCVISVLPDG AGVYTIPDEK
WAELGLWSAE ADGNWWSTGR GKVARNYMST KEVKRQDIIH ELVTTERHHC ITLVLLKHTY
FDGLLGLNIL TNDELNMLMP HLELLLEVHL HFLQLLKKKV DESVVVENVH EIFIEQANFL
NAYLFIYLFC LLYKTDCAYL MMFLFVFTGG VAEKMQLAYT TFCSRKDFSV QEYHRLCQTN
PNFSIFMENM NKLPYFKARS LPDCLLLVTQ RLSKYHSFVE SLRKNTEDAL LKDEILKAEQ
AVKKLVANVD QGIGDIQLQQ LCKEIVAQMD TKESTTFLGK TFTKNELLSN TRTLLHAGDV
YWQNAMRKPT EVKMLLFSDI IVFLQRVGNS YAFFSQDNKE CIISLLKLIV REKAGRSGSQ
GLYLISAAPS HAEMYEIICH TKKMLASWTE RIQRAVDVCP PAAIEERPSS ESVFAVEHEE
QLKTLFGKVN NCNDELKKLL DCQIEAYGEI LQLVHKMNIP DEEERMKIMK TIDECLPAKI
AATAVARFAD LMSQLVRERC KQQLLNLACP TDTATAQTTT SSDGSNINRS QTFHGMRNDS
KKSKLYRKRV TVSGIPQRCE ENRIVETAID NGMSGEIHAD SKSAFCAVMS RLKDAEIELD
GMKHEKAMLL IELEKEKSIR SSSAQNVYNA GLEELRRLHS DFEKRRSEFQ QLVDEKKSDF
EHRENAIREK EERLNREDSE LQSKWQCLRE AWEKLQLSGV PIRSLTSPLA PSTSCAAYIA
TCNSSTNASN PVNHPPAGGD NSNNSGPIGK QSNSTVANST PTVGVDDSSN ITCVRSGVGI
SGGSTSASAE KQSFRKVQVP PYLLGSFVHS GRLPDDLVRQ QLPSKLLKDD MFNSLSSRFQ
SSMKERRKGS PKVKDNHSIN VKGKQK
//
