ID A0A0N4T2L5_BRUPA Unreviewed; 763 AA.
AC A0A0N4T2L5;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=E1 ubiquitin-activating enzyme {ECO:0000256|ARBA:ARBA00012990};
DE EC=6.2.1.45 {ECO:0000256|ARBA:ARBA00012990};
GN ORFNames=BPAG_LOCUS2415 {ECO:0000313|EMBL:VDN83601.1};
OS Brugia pahangi (Filarial nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX NCBI_TaxID=6280 {ECO:0000313|Proteomes:UP000038020, ECO:0000313|WBParaSite:BPAG_0000244501-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:BPAG_0000244501-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDN83601.1, ECO:0000313|Proteomes:UP000278627}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine
CC = AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-
CC L-cysteine.; EC=6.2.1.45; Evidence={ECO:0000256|ARBA:ARBA00000488};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family.
CC {ECO:0000256|ARBA:ARBA00005673, ECO:0000256|RuleBase:RU000519}.
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; UZAD01000347; VDN83601.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N4T2L5; -.
DR STRING; 6280.A0A0N4T2L5; -.
DR WBParaSite; BPAG_0000244501-mRNA-1; BPAG_0000244501-mRNA-1; BPAG_0000244501.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000038020; Unplaced.
DR Proteomes; UP000278627; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd01490; Ube1_repeat2; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.40.50.12550; Ubiquitin-activating enzyme E1, inactive adenylation domain, subdomain 2; 1.
DR Gene3D; 1.10.10.2660; Ubiquitin-activating enzyme E1, SCCH domain; 1.
DR Gene3D; 3.10.290.60; Ubiquitin-activating enzyme E1, UFD domain; 1.
DR InterPro; IPR032420; E1_4HB.
DR InterPro; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR InterPro; IPR018965; Ub-activating_enz_E1_C.
DR InterPro; IPR038252; UBA_E1_C_sf.
DR InterPro; IPR019572; UBA_E1_SCCH.
DR InterPro; IPR042063; Ubi_acti_E1_SCCH.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR InterPro; IPR018075; UBQ-activ_enz_E1.
DR InterPro; IPR033127; UBQ-activ_enz_E1_Cys_AS.
DR NCBIfam; TIGR01408; Ube1; 1.
DR PANTHER; PTHR10953:SF4; UBA_E1_C DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 1.
DR Pfam; PF16191; E1_4HB; 1.
DR Pfam; PF09358; E1_UFD; 1.
DR Pfam; PF00899; ThiF; 1.
DR Pfam; PF10585; UBA_E1_SCCH; 1.
DR SMART; SM00985; UBA_e1_C; 1.
DR SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 2.
DR PROSITE; PS00865; UBIQUITIN_ACTIVAT_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU000519};
KW Ligase {ECO:0000256|RuleBase:RU000519};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU000519};
KW Reference proteome {ECO:0000313|Proteomes:UP000278627};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU000519}.
FT DOMAIN 614..758
FT /note="Ubiquitin-activating enzyme E1 C-terminal"
FT /evidence="ECO:0000259|SMART:SM00985"
FT ACT_SITE 311
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ SEQUENCE 763 AA; 86615 MW; 135A857A01C13713 CRC64;
MWDFAKFENP SQLHALWQAL HSFEAKHKRS PMPRSNEDVG LLKVELPPGA ELDENLLRIF
SYQACGNLAP IASIVGGIAA QEAMKAVMHH MTPLKQFLYI DCIEALPGDW SPFDNNNLTA
NDCEMKNCRY DGQVAVFGRA YQEALLIQKY FIVGAGAIGC ELLKNLAMMG VACGPEGKLK
ITDMDQIEIS NLNRQFLFRR NDVGNKKSEV AVKAVKDFNL NIKIDALSER VGAETESIFT
DDFFNDLNGV LNALDNVDAR RYMDRRCIYY RLPLLDSGTM GTKGNTQVVY PHLTESYGSS
VDPPEKDIPI CTLKNFPNEI QHTIQWARDL FEGLFTTPAE TANQFISDER GFLQRVDQMN
TAQRLHMLSK VEEALIRERP HSPEDCIKWA RMNFQEYFHN MIAQLLHMFP PDQVTEQGIK
FWSGSKRCPH VLDFNPDEPE HFNFVWAASI LRAHQYGITP IIDKKKFLAV LNEIHPPPFM
PKSDVKIAVT EAEAKQEEKA TADGKCDDVD EKLQSVMMNL AKLNKKATKS LIPIDFEKDD
DTNHHMEFIT AASNLRADNY QITPADVMKT KQIAGRIIPA LATTTSAVAG LVCIELYKMI
GNGHQPPNVP LKVFKNGFLN LALPFFGFSE PIAAPKKKVG FKVFFFTSSQ IIFPVLQCAD
GYFTLWDRFE IQGPKKMKEL IQWIKEETGL DVTMMSCGVS LIYSFFLSSD KRMERLEQDM
KDIVEEVTRK KIPDYVQSIV LEVIANNKDD EDVEIPYIKF NLR
//
