ID A0A0V0ZAV4_9BILA Unreviewed; 1295 AA.
AC A0A0V0ZAV4;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Rho guanine nucleotide exchange factor 2 {ECO:0000313|EMBL:KRY09620.1};
GN Name=Arhgef2 {ECO:0000313|EMBL:KRY09620.1};
GN ORFNames=T12_13952 {ECO:0000313|EMBL:KRY09620.1};
OS Trichinella patagoniensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=990121 {ECO:0000313|EMBL:KRY09620.1, ECO:0000313|Proteomes:UP000054783};
RN [1] {ECO:0000313|EMBL:KRY09620.1, ECO:0000313|Proteomes:UP000054783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS2496 {ECO:0000313|EMBL:KRY09620.1};
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:KRY09620.1}.
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DR EMBL; JYDQ01000266; KRY09620.1; -; Genomic_DNA.
DR STRING; 990121.A0A0V0ZAV4; -.
DR Proteomes; UP000054783; 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:UP000054783};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 316..365
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 474..681
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT REGION 179..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 944..971
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1158..1197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1268..1295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1021..1081
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 944..963
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1270..1295
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1295 AA; 144427 MW; 9BF3A93546AD1E90 CRC64;
MSNFAYRHLL VVHEYIVKNK LFKFISAAQR YHTTVLIGMK RDVSVSWPNL AEISSRTPST
SFSICCLIKS HSLTASSQSV EACQLSFADN GVDLAATASH GVHKHFADGS RRSCSGDDGT
PMKLAVDRGA PVKLSKSVEC VVPGTVRVNL GCSKSEVDLS QLSAASRLSE KRFSLGDQSS
LAQRLQDSSN EEDPAGTTAL TANPADQQKE LLKFVDNAVH LDRSFSSTPS IDVDSSLAYF
AVLPRDKPNE VSRERLRQIR ASSMVVPAIT PRLPLMGLLP KAVGKASNDK VDLKSIEKVL
KLRSSKKHAK VKEKKQHVWL QCQEKAGLNC DICNKAEGNY SFVRCTECHA VLHSHCKTAA
NKASCSRGKA ASKHSSVMFQ TRPLSLVSRF SSFRSDSSSS VIGQIYAETS NRSGPLPQSA
DCVISVLPDG AGVYTIPDEK WAELGLWSAE ADGNWWSTGR GKVARNYMST KEVKRQDIIH
ELVTTERHHC VTLVLLKHTY FDGLLGLNIL TNDELNMLMP HLELLLEVHL HFLQLLKKKV
DESVVVENVH EIFIEQANFL NAYLFIYFVY FIRQIFTGGV AEKMQLAYTT FCSRKDFSVQ
EYHRLCQTNP NFSNFMENMN KLPYFKARSL PDCLLLVTQR LSKYHSFVES LRKNTEDALL
KDEILKAEQA VKKLVANVDQ GIGDIQLQQL CKEIVAQMDT KESTTFLGKT FTKNELLSNT
RTLLHAGDVY WQNAMRKPTE VKMLLFSDII VFLQRVGNSY AFFSQDNKEC IISLLKLIVR
EKAGRSGSQG LYLISAAPSH AEMYEIICHT KKMLASWTER IQRAVDVCPP AAIEERPSSE
SVFAVEHEEQ LKTLFGKVNN CNDELKKLLD CQIEAYGEIL QLVHKMNIPD EEERMKIMKT
IDECLPAKIA ATAVARFADL MSQLVRERCK QQLLNLACPA DTATAQTTTS SDGSNINRSQ
TFHGMRNDSK KSKLYRKRVT VSGIPQRCEE NRIVETAIDN GMSGEIHADS KSAFCAVMSR
LKDAEIELDG MKHEKAMLLI ELEKEKSIRS SSAQNVYNAG LEELRRLHSD FEKRRSEFQQ
LVDEKKSDFE HRENAIREKE ERLNREDSEL QSKWQCLREA WEKLQLSGVP IRSLTSPLAP
STSCAAYIAT CNSSTNASNP VNHPPAGGDN SNNSGPIGKQ SNSTVANSTP TVGVDDSSNI
TCVRSGVGIS GGSTSASAEK QSFRKVQVPP YLLGSFVHSG RLPDDLVRQQ LPSKLLKDDM
FNSLSSRFQS SMKERRKGSP KVKDNHSINV KGKQK
//
