ID A0A0R3X277_HYDTA Unreviewed; 1223 AA.
AC A0A0R3X277;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=NEDD8-activating enzyme E1 catalytic subunit {ECO:0000256|RuleBase:RU368009};
DE EC=6.2.1.64 {ECO:0000256|RuleBase:RU368009};
GN ORFNames=TTAC_LOCUS7357 {ECO:0000313|EMBL:VDM31725.1};
OS Hydatigena taeniaeformis (Feline tapeworm) (Taenia taeniaeformis).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC Eucestoda; Cyclophyllidea; Taeniidae; Hydatigera.
OX NCBI_TaxID=6205 {ECO:0000313|Proteomes:UP000046396, ECO:0000313|WBParaSite:TTAC_0000737201-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:TTAC_0000737201-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDM31725.1, ECO:0000313|Proteomes:UP000274429}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalytic subunit of the dimeric E1 enzyme, which activates
CC NEDD8. {ECO:0000256|RuleBase:RU368009}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + [NEDD8 protein] + [E1 NEDD8-activating enzyme]-L-
CC cysteine = AMP + diphosphate + [E1 NEDD8-activating enzyme]-S-[NEDD8
CC protein]-yl-L-cysteine.; EC=6.2.1.64;
CC Evidence={ECO:0000256|RuleBase:RU368009};
CC -!- PATHWAY: Protein modification; protein neddylation.
CC {ECO:0000256|RuleBase:RU368009}.
CC -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family. UBA3
CC subfamily. {ECO:0000256|RuleBase:RU368009}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL2 family.
CC {ECO:0000256|ARBA:ARBA00005636}.
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DR EMBL; UYWX01020365; VDM31725.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R3X277; -.
DR STRING; 6205.A0A0R3X277; -.
DR WBParaSite; TTAC_0000737201-mRNA-1; TTAC_0000737201-mRNA-1; TTAC_0000737201.
DR UniPathway; UPA00885; -.
DR Proteomes; UP000046396; Unplaced.
DR Proteomes; UP000274429; Unassembled WGS sequence.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0019781; F:NEDD8 activating enzyme activity; IEA:UniProtKB-EC.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0043828; F:tRNA 2-selenouridine synthase activity; IEA:InterPro.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0045116; P:protein neddylation; IEA:UniProtKB-UniPathway.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR GO; GO:0002098; P:tRNA wobble uridine modification; IEA:InterPro.
DR Gene3D; 2.30.30.30; -; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.10.20.260; NEDD8-activating enzyme E1, catalytic subunit; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
DR Gene3D; 1.10.10.520; Ubiquitin activating enzymes (Uba3). Chain: B, domain 2; 1.
DR InterPro; IPR014929; E2-binding.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR037078; NEDD8-ac_enz1_catalyticsu_C.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR InterPro; IPR014722; Rib_uL2_dom2.
DR InterPro; IPR002171; Ribosomal_uL2.
DR InterPro; IPR022669; Ribosomal_uL2_C.
DR InterPro; IPR022666; Ribosomal_uL2_RNA-bd_dom.
DR InterPro; IPR017582; SelU.
DR InterPro; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR InterPro; IPR023318; Ub_act_enz_dom_a_sf.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR InterPro; IPR033127; UBQ-activ_enz_E1_Cys_AS.
DR NCBIfam; TIGR03167; tRNA_sel_U_synt; 1.
DR PANTHER; PTHR10953:SF6; NEDD8-ACTIVATING ENZYME E1 CATALYTIC SUBUNIT; 1.
DR PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 1.
DR Pfam; PF00581; Rhodanese; 1.
DR Pfam; PF00181; Ribosomal_L2; 1.
DR Pfam; PF03947; Ribosomal_L2_C; 1.
DR Pfam; PF00899; ThiF; 1.
DR SMART; SM01181; E2_bind; 1.
DR SMART; SM00450; RHOD; 1.
DR SMART; SM01383; Ribosomal_L2; 1.
DR SMART; SM01382; Ribosomal_L2_C; 1.
DR SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
DR SUPFAM; SSF50104; Translation proteins SH3-like domain; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
DR PROSITE; PS00865; UBIQUITIN_ACTIVAT_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU368009};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU368009};
KW Molybdenum cofactor biosynthesis {ECO:0000256|ARBA:ARBA00023150};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU368009};
KW Reference proteome {ECO:0000313|Proteomes:UP000274429};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU368009}.
FT DOMAIN 491..626
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT ACT_SITE 188
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ SEQUENCE 1223 AA; 138049 MW; CDB3C778D42C080D CRC64;
MVSHGNVCCD RTARWEAIEC ILGRSGPLQR SEFEPSSEAL MGFCHIDVVD MDTIDVSNLN
RQFLFTEKDV GRSKAEVAAD FIMRRIDTCK VTPHFKKIQD FGSNFYKQFD IVICGLDSVI
ARRWINSMLA SLLEYKEDGT PDFQTMIPLV DGGTEGFKGH VIVVLFGFTG CIECSLDLYP
PQVNYPLCTI AHTPRLPEHC VEFVRLLLWP KEQPFGPGVD IDGDSPDHLE WIFSHSSERA
KEYGIQGVDM RLVKGVVKRI VPSVASTNAV IASALVTEAF KLVTLCYDYL NSCMNFSDVE
GIYTYTFQIE RKDGCLVCNN APKKLEFPSK ATLRELVEHL KNDPTLQMHS PTITTVLNGS
NRTLFVDFDD AMQGLRANLS KSLGAFVAML YGIEMHFPFI LGLFTGSWSV TAPQSILVIF
NSLNRLVLPT FGRCFASQHR ANFKHQLKYV NLTDEPFAVA LSPEAAEHAP ASLPPPLDPA
PRGSIPWFTL DPTTTLLIDA RSPCEYDADH IEGAINVPIL SNQERMDVGK IFFAGDALEA
RLLGARFACT NIAQSLRPEG PLGRLFEISN RKSFSPQLIL VYCSRGGQRS MGLGTVLSEL
NYPGCEVACL AGGYRAWRRL LLRQLGIWPT LVGPGGLAGT LWVLSSLTGC GKTLLLEELE
AAGESTLNLE RMAEHKGSMF GGAAMQPTQR IFDARLHSGL RRCLTAPHVW TECESRSVGP
RCQLGDGFWQ RLRGTRSTAR VWLSAPLEAR VNWILQDYAD WLHNSEENLK RVFESLANYH
SKNRLESWRK LARNGDYAAF VAELLEHHYD PLYKKSRGPM LRHFTDMGLL HRVEVPVVSR
AYFQKQTLKA TLFPSRRIFG LLFVLPINEF PFFRCNRAFR TSCGLQRHPG ITYPHKLSWQ
WLIEKFVNPN QYTVDPIRKI RTGGRGPDGR IQYKHVTTGL NMPYFLVDYV RSRQMEAKEV
QEEVILKIAK NWWRDPYLAL TASGEVKRWI IATSNMKEGD VIRSHWEIPS IPVVPVLGDA
YPVGALPVGT QVCLIEMHPG EGAMICRAAG TSATVVRRGT AVHDLSGLRT QMDDMLSAEP
IDERFTSTLQ LDSSRREVRL LPTCVVVVGQ VSNETHNKQR YRKFGEKYWH GIKQRSGLYQ
KKTGRFGRKI YPVDPLLDCT REEVPDGEIR AKFTLPERPE LERRRVREIF ADSLLVRRPK
IRPVPGPNNA LPHTLPLFTW RHY
//
