ID W6UF17_ECHGR Unreviewed; 1373 AA.
AC W6UF17;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Signal recognition particle subunit SRP54 {ECO:0000256|ARBA:ARBA00034832};
DE EC=3.6.5.4 {ECO:0000256|ARBA:ARBA00035672};
DE AltName: Full=Signal recognition particle 54 kDa protein {ECO:0000256|ARBA:ARBA00034907};
GN ORFNames=EGR_05702 {ECO:0000313|EMBL:EUB59451.1};
OS Echinococcus granulosus (Hydatid tapeworm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC Eucestoda; Cyclophyllidea; Taeniidae; Echinococcus;
OC Echinococcus granulosus group.
OX NCBI_TaxID=6210 {ECO:0000313|EMBL:EUB59451.1, ECO:0000313|Proteomes:UP000019149};
RN [1] {ECO:0000313|EMBL:EUB59451.1, ECO:0000313|Proteomes:UP000019149}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24013640; DOI=10.1038/ng.2757;
RA Zheng H., Zhang W., Zhang L., Zhang Z., Li J., Lu G., Zhu Y., Wang Y.,
RA Huang Y., Liu J., Kang H., Chen J., Wang L., Chen A., Yu S., Gao Z.,
RA Jin L., Gu W., Wang Z., Zhao L., Shi B., Wen H., Lin R., Jones M.K.,
RA Brejova B., Vinar T., Zhao G., McManus D.P., Chen Z., Zhou Y., Wang S.;
RT "The genome of the hydatid tapeworm Echinococcus granulosus.";
RL Nat. Genet. 45:1168-1175(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.4;
CC Evidence={ECO:0000256|ARBA:ARBA00035589};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000256|ARBA:ARBA00035589};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004240}.
CC -!- SIMILARITY: Belongs to the GTP-binding SRP family. SRP54 subfamily.
CC {ECO:0000256|ARBA:ARBA00005450}.
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:EUB59451.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; APAU02000044; EUB59451.1; -; Genomic_DNA.
DR STRING; 6210.W6UF17; -.
DR EnsemblMetazoa; XM_024494951.1; XP_024350647.1; GeneID_36341417.
DR OrthoDB; 1110531at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000019149; Unassembled WGS sequence.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005786; C:signal recognition particle, endoplasmic reticulum targeting; IEA:UniProtKB-KW.
DR GO; GO:0008312; F:7S RNA binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; IEA:InterPro.
DR CDD; cd00078; HECTc; 1.
DR CDD; cd17875; SRP54_G; 1.
DR CDD; cd00201; WW; 4.
DR Gene3D; 2.20.70.10; -; 3.
DR Gene3D; 3.30.2160.10; Hect, E3 ligase catalytic domain; 1.
DR Gene3D; 3.30.2410.10; Hect, E3 ligase catalytic domain; 1.
DR Gene3D; 3.90.1750.10; Hect, E3 ligase catalytic domains; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.20.120.140; Signal recognition particle SRP54, nucleotide-binding domain; 1.
DR Gene3D; 1.10.260.30; Signal recognition particle, SRP54 subunit, M-domain; 1.
DR HAMAP; MF_00306; SRP54; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR036891; Signal_recog_part_SRP54_M_sf.
DR InterPro; IPR013822; Signal_recog_particl_SRP54_hlx.
DR InterPro; IPR004125; Signal_recog_particle_SRP54_M.
DR InterPro; IPR036225; SRP/SRP_N.
DR InterPro; IPR022941; SRP54.
DR InterPro; IPR006325; SRP54_euk.
DR InterPro; IPR000897; SRP54_GTPase_dom.
DR InterPro; IPR042101; SRP54_N_sf.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR NCBIfam; TIGR01425; SRP54_euk; 1.
DR PANTHER; PTHR11564:SF5; SIGNAL RECOGNITION PARTICLE 54 KDA PROTEIN; 1.
DR PANTHER; PTHR11564; SIGNAL RECOGNITION PARTICLE 54K PROTEIN SRP54; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF00448; SRP54; 1.
DR Pfam; PF02881; SRP54_N; 1.
DR Pfam; PF02978; SRP_SPB; 1.
DR Pfam; PF00397; WW; 4.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00962; SRP54; 1.
DR SMART; SM00963; SRP54_N; 1.
DR SMART; SM00456; WW; 4.
DR SUPFAM; SSF47364; Domain of the SRP/SRP receptor G-proteins; 1.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF47446; Signal peptide-binding domain; 1.
DR SUPFAM; SSF51045; WW domain; 4.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS00300; SRP54; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 3.
DR PROSITE; PS50020; WW_DOMAIN_2; 4.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000019149};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW Signal recognition particle {ECO:0000256|ARBA:ARBA00023135};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 802..836
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 835..868
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 918..951
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 954..987
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 1039..1373
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 441..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 538..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 727..815
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..457
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 744..781
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1341
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 1373 AA; 153733 MW; C4C05540F9ABF5A2 CRC64;
MVLAELGRKI TSALRSLGNA TIINEDVLNS LLKEICTALI ESDVNIRLVK QLRENVKSMI
NFDELAAGVN KRKLIESAVF NELVRIIDPQ VKAWQPTKGK SNVIMLVGLQ GSGKTTTATK
LAYHYQKKGW KTCLICADTY RAGAFDQLKQ NATKARIPYY GSYTEADPAV IAKEGVKRFN
EEKFEIIVVD TSGRHKQEEA LFEEMLQVSN AINPDHVIYV MDASIGQACE AQASAFKAMV
DVASVIVTKL DGHAKGGGAL SAVAATHSPI VFIGTGEHIE DFEPFRVHPF VKKLLGLGDL
EDLFEKVKDM KFDENEELIK KLKQGVFTLR SMYEQFQNIL KIGPLSAVLS SIPGLGQELF
TNDRESHRRL KRLMTIMDSM NDHELDSDDG ARLFNRQPGR IQRVARGAGV SQGEVKQLLV
QHTKFAQVVK KMGGINGLFQ QMPSGTGGGS GSGGGGQPSL SDMAAAARSV NSGKMAKLQA
SMARAMDPRV LHQMGGTAGL QNVLRQLQSV ASAKLHKHTR STALSRIRNP IFRVEFNTTS
WDAPPPSDSP TNTEHVTSNR GVTATKTGWN PHFNSRTNFN ININSHIEFL IVSQASVHAS
LNGGTGLVVG YSRLGIRDAL RNYGNNLEDA AFSLDILPLP TDQCVDGNTL PSLGTLSLFL
TASATAVNAA IVAANINQRS FSPSGYSAML QTNMEDEVQS RTLQCVLLCI LPMGKGDVQG
TCDSKCGFGV DRRHKRSHRS TPTAEESRSS TPAANSNTAP TNAVTNGSSD TSTTNRTPAT
GDLLTIPRRS NGGRRRSAPD TEGLPPQWER RTDPSTGRIY YVDHLTKRTQ WEKPQPLPSG
WERRLDQNNR VYYVDHNTRT TTWHPPSDHL LDNVVRWRQW YDIRAGNMRN QMSQLYASSG
WANGAGSSPA HSIPETLGPL PEGFERRRDS NGRVYYVNHR TKTTQWEDPR QTTVPLPSGW
EMRYTPEGFV FYVDHNTRTT TFKDPRQPGS ADSNQWTLDR KVASFRYLCH VNSSTDKVAI
RVRRSDLLND SFNQLLKVPA KSLRGRLSVT FEDEEALDYG GVQREWFFQL SDQLLNPMYC
LFEYASGNNF SLQINANSSV NPQHLQYFRF VGRFIALALF HGKFIDNGFT LPFYKRLLNK
PLSLNDLQTV DEEYYNSLLF IRENPIDDAD LELYFEADYE HFGQTITCEL KQGGKSIKVT
DANKEEYLSL MVNWRFSRGT EEQMEAFMAG FADVFPLQWL QYFDERELEM ILCGLQKIDV
DDWQQNTNYK DYTVSSKQIV WFWKFVRTLS TERRVRLLQF VTGTCRLPVG GFKELMGSNG
LQLFTIKRAG KENALPLSHT CFNRLDLPPY RSYEILVEKV TLAIDETEGF GLQ
//
