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Database: UniProt
Entry: A0A0V0UNL2_9BILA
LinkDB: A0A0V0UNL2_9BILA
Original site: A0A0V0UNL2_9BILA 
ID   A0A0V0UNL2_9BILA        Unreviewed;      1292 AA.
AC   A0A0V0UNL2;
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:KRX52744.1};
DE   Flags: Fragment;
GN   ORFNames=T09_5947 {ECO:0000313|EMBL:KRX52744.1};
OS   Trichinella sp. T9.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX52744.1, ECO:0000313|Proteomes:UP000054681};
RN   [1] {ECO:0000313|EMBL:KRX52744.1, ECO:0000313|Proteomes:UP000054681}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS409 {ECO:0000313|EMBL:KRX52744.1};
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:KRX52744.1}.
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DR   EMBL; JYDN01000228; KRX52744.1; -; Genomic_DNA.
DR   STRING; 181606.A0A0V0UNL2; -.
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          934..962
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1155..1194
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1265..1292
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1018..1078
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        934..954
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1267..1292
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KRX52744.1"
SQ   SEQUENCE   1292 AA;  144062 MW;  DB69648FC34ADEAA 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 ENRIVMRCTF KETAIDNGMS GEIHADSKSA FCAVMSRLKD
     AEIELDGMKH EKAMLLIELE KEKSIRSSSA QNVYNAGLEE LRRLHSDFEK RRSEFQQLVD
     EKKSDFEHRE NAIREKEERL NREDSELQSK WQCLREAWEK LQLSGVPIRS LTSPLAPSTS
     CAAYIATCNS STNASNPVNH PPAGGDNSNN SGPIGKQSNS TVANSTPTVG VDDSSNITCV
     RSGVGISGGS TSASAEKQSF RKVQVPPYLL GSFVHSGRLP DDLVRQQLPS KLLKDDMFNS
     LSSRFQSSMK ERRKGSPKVK DNHSINVKGK QK
//
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