ID A0A0V1NHK1_9BILA Unreviewed; 1263 AA.
AC A0A0V1NHK1;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Rho guanine nucleotide exchange factor 2 {ECO:0000313|EMBL:KRZ83283.1};
DE Flags: Fragment;
GN Name=Arhgef2 {ECO:0000313|EMBL:KRZ83283.1};
GN ORFNames=T08_13611 {ECO:0000313|EMBL:KRZ83283.1};
OS Trichinella sp. T8.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92180 {ECO:0000313|EMBL:KRZ83283.1, ECO:0000313|Proteomes:UP000054924};
RN [1] {ECO:0000313|EMBL:KRZ83283.1, ECO:0000313|Proteomes:UP000054924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS272 {ECO:0000313|EMBL:KRZ83283.1};
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:KRZ83283.1}.
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DR EMBL; JYDM01000220; KRZ83283.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1NHK1; -.
DR Proteomes; UP000054924; 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:UP000054924};
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..649
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT REGION 179..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 909..939
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1124..1160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1236..1263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 989..1049
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 909..931
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1238..1263
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRZ83283.1"
SQ SEQUENCE 1263 AA; 140557 MW; 905D821983AA01C3 CRC64;
LVVHEYIVKN NFPTLSFIER LFKFISTAQR YHTTVLIGMK RDVSVSWPNL AEIPSRTPST
SFSICCLIKS HSLTASSQSV EACQLSFADN GVDLAATASH GVHKHFADGS RRSCSGDDGT
PMKLAVDRGA PVKLSKSVEC VVPGTVRVNL GCSKSEVDLS QLSAASRLSE KRFSLGDQSS
LAQRLHDSSN EEDPAGATAL 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
DESFTGGVAE KMQLAYTTFC SRKDFSVQEY HRLCQTNPNF SIFMENMNKL PYFKARSLPD
CLLLVTQRLS KYHSFVESLR KNTEDALLKD EILKAEQAVK KLVANVDQGI GDIQLQQLCK
EIVAQMDTKE STTFLGKTFT KNELLSNTRT LLHAGDVYWQ NAMRKPTEVK MLLFSDIIVF
LQRVGNSYAF FSQDNKECII SLLKLIVREK AGRSGSQGLY LISAAPSHAE MYEIICHTKK
MLASWTERIQ RAVDVCPPAA IEERPSSESV FAVEHEEQLK TLFGKVNNYN DELKKLLDCQ
IEAYGEILQL VHKMNIPDEE ERMKIMKTID ECLPAKIAAT AVARFADLMS QLVRERCKQQ
LLNLACPTDT ATAQTTTSSD GSNINRSQTF HGMRNDSKKS KLYRKRVTVS GIPQRCEENR
IVETAIDNGM SGEIHADSKS AFCAVMSRLK DAEIELDGMK HEKAMLLIEL EKEKSIRSSS
AQNVYNAGLE ELRRLHSDFE KRRSEFQQLV DEKKSDFEHR ENAIREKEER LNREDSELQS
KWQCLREAWE KLQLSGVPIR SLTSPLAPST SCAAYIATCN SSTNASNPVN HPIAGGDNSN
NSGPIGKQSN STVANSTPTV GVDDSSNITC VRSGVGISGG STSASAEKQS FRKVQVPPYL
LGSFVHSGRL PDDLVRQQLP SKLLKDDMFN SLSSRFQSSM KERRKGSPKV KDNHSINVKG
KQK
//
