ID A0A0V0TFD6_9BILA Unreviewed; 1638 AA.
AC A0A0V0TFD6;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Rho guanine nucleotide exchange factor 12 {ECO:0000313|EMBL:KRX37662.1};
GN Name=ADCK3 {ECO:0000313|EMBL:KRX37662.1};
GN ORFNames=T05_10717 {ECO:0000313|EMBL:KRX37662.1};
OS Trichinella murrelli.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=144512 {ECO:0000313|EMBL:KRX37662.1, ECO:0000313|Proteomes:UP000055048};
RN [1] {ECO:0000313|EMBL:KRX37662.1, ECO:0000313|Proteomes:UP000055048}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS417 {ECO:0000313|EMBL:KRX37662.1};
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 Membrane {ECO:0000256|ARBA:ARBA00004370}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the eukaryotic
CC ribosomal protein eS31 family. {ECO:0000256|ARBA:ARBA00009891}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the ubiquitin family.
CC {ECO:0000256|ARBA:ARBA00008373}.
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:KRX37662.1}.
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DR EMBL; JYDJ01000300; KRX37662.1; -; Genomic_DNA.
DR Proteomes; UP000055048; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005840; C:ribosome; IEA:InterPro.
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 GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR CDD; cd00029; C1; 1.
DR CDD; cd00992; PDZ_signaling; 1.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 3.30.60.20; -; 1.
DR Gene3D; 6.20.50.150; -; 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 Gene3D; 1.10.167.10; Regulator of G-protein Signalling 4, domain 2; 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR001331; GDS_CDC24_CS.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR041020; PH_16.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR015212; RGS-like_dom.
DR InterPro; IPR036305; RGS_sf.
DR InterPro; IPR044926; RGS_subdomain_2.
DR InterPro; IPR002906; Ribosomal_eS31.
DR InterPro; IPR038582; Ribosomal_eS31_euk-type_sf.
DR InterPro; IPR011332; Ribosomal_zn-bd.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR45872; RHO GUANINE NUCLEOTIDE EXCHANGE FACTOR 2, ISOFORM D; 1.
DR PANTHER; PTHR45872:SF2; RHO GUANINE NUCLEOTIDE EXCHANGE FACTOR 2, ISOFORM D; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF17838; PH_16; 1.
DR Pfam; PF09128; RGS-like; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR Pfam; PF01599; Ribosomal_S27; 1.
DR Pfam; PF00240; ubiquitin; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SMART; SM01402; Ribosomal_S27; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF48097; Regulator of G-protein signaling, RGS; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR SUPFAM; SSF57829; Zn-binding ribosomal proteins; 1.
DR PROSITE; PS00741; DH_1; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658};
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000055048};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 13..75
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 520..570
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 774..981
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1023..1138
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1488..1548
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
FT REGION 85..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 198..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 645..717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1143..1166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 160..187
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 85..99
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..126
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..667
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 668..694
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 695..714
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1151..1165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1638 AA; 185540 MW; F70640E787C81E09 CRC64;
MHFHGEHFAE ERNVLIKRDE NGYGLTVCGN NPVFVQSVRE GSAAAKAGVH VGECIIKVNG
VTVTSLDHLE VVKLISVAPY TTLTLSGGPS SSSAASSMGN DHYEKRDRCL ERRSTENAIR
PNSKKKQSEW HLKRKKIIQQ ILTEEKRQLQ VMLKGSDAHA DADQRIIEKM TRRIHNLEDQ
LNEVEKLDFE QENISLSNSG FRSHSDDLSS SLTMKSSKSH SDDVVASSST DDERLLTKSD
NIDEIRDHQI PVPVSEVPPE SPLLVHTLSM SNECDSAAVE LNSSSFDEPF SKLPMLKTHL
GHLAVFLHYL LSNSDPSYLL FYLLTDIFAL YIGKESKKWA YEIHSSFLLP YSPCRVSFTD
SSSWETVDAV LNDPNKHADS AQWRRLFSTA RGLAVQAINE QLADFRSKRI LGLGNVFGES
MLQRLQAGDS AHERKIFDAL IAPHLIAFFE EAADFDQLPK RIQVIVAALA TLYKHNNVKC
RNAAMEKLLE RCPTYIAKEK QRFARPLLPK ASRRALQIKA HCFNIAPVLQ TTFCYQCQKL
IWGIGAMSLF CGKCGVVLHK SCVENLAESC FGSMNLRRPL ILKKIVGRKN VESSMDNIEQ
SIEEGKISTA RTDASMLLKE NSGEGDGSSE KNLTRNFDKS GVTNAAVSKQ SAHIHNLSRS
QSMNIEEESY RGARRRSSDT SRRSHSDADK TESLTRISTT ESSTTVSVQD VSRERSPMIS
ELDSPLTSSV SFSNTLHDIH VELDSDFKVE NEIPLLEDFL DLESFQYLDK REKNRLEVIY
ELFHTEQTHV RNLKILYRLF YKQLLNFNVI SFEFASLLFS NLEDVLNLHV EMNEAMKNMM
QNNKLIGDIS IMMLQFDGKE RMRNIDSLHC QKLQSAIEAL KHRVVKDQKL REFLQVVESL
PVCRKLQLKD MLPMEMQRLT KYPLLLENVL KYTEDLSIDI IKRHCAKVMT VYHLLDPSEE
ADRLRTCIEC SRSILESVNS AKRNAENVLR LQRLQQMLDT TQFDKVNHPI VSEFCPLDVR
RFSLIHEGPL IWRLNKSKIV DLHVVLLDEI LLLLSPTSDG HLALRFHNIN ISCGKDEVKW
THCPLLKLNS LIAKDVATDK KAFFLVSTSP SGPQIYELAT QSKAEKQNWF KFIVEQIEAS
KEHEQKTSVR HGQAGQESKS GDSFYEIPNS ARKKSLTVRS QRTMKNPNFD ERVRVTCQPR
LISPSEINIC QPTVFQHSKP ILNPLEKLKQ EDKLVIRLLN EKLQIISSFF GQKNDLPPSS
AVDSRTSREA REFVISAIKQ TNRLLEAINE QTRLIEMENF ENGSVKYQVP EVECPSVPCY
QLTQIAAGLM TCLTNLLHSL QIMGDDLKRV QRELHQYKLS PERLLPFPEK ICQAVGTDIP
TDVTHEAACR KNLTDAAVQT EPASFLQTNN CDAVKKNAGK STEKFHTDDQ PTELSGRSII
KDALPTGSCN TAASEKPILR NGKMGTDGLC LFDTDIAKLE EQPCSEIITI ESNCTIGEIK
KQIQEEEESL CSSYLVLGGR PLEDDWTLAQ CNIQEFSTLD LSYRLLGGAK KRKKKMYTTP
KKIKHKKKKV KLAVLKYYKI DENGKVSRLR KECTSESCGA GVFMANHYNR QYCGKCYCTM
VVQDPVQREQ KPGKGKGH
//
