ID A0A183J890_9BILA Unreviewed; 563 AA.
AC A0A183J890;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=E1 ubiquitin-activating enzyme {ECO:0000256|ARBA:ARBA00012990};
DE EC=6.2.1.45 {ECO:0000256|ARBA:ARBA00012990};
OS Soboliphyme baturini.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Dioctophymatida; Dioctophymatoidea; Soboliphymatidae; Soboliphyme.
OX NCBI_TaxID=241478 {ECO:0000313|Proteomes:UP000050793, ECO:0000313|WBParaSite:SBAD_0001249201-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:SBAD_0001249201-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
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}.
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 AlphaFoldDB; A0A183J890; -.
DR WBParaSite; SBAD_0001249201-mRNA-1; SBAD_0001249201-mRNA-1; SBAD_0001249201.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000050793; Unplaced.
DR GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.50.50.80; Ubiquitin-activating enzyme E1, inactive adenylation domain, subdomain 1; 1.
DR Gene3D; 1.10.10.2660; Ubiquitin-activating enzyme E1, SCCH domain; 1.
DR InterPro; IPR032420; E1_4HB.
DR InterPro; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR InterPro; IPR042449; Ub-E1_IAD_1.
DR InterPro; IPR019572; UBA_E1_SCCH.
DR InterPro; IPR042063; Ubi_acti_E1_SCCH.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR InterPro; IPR033127; UBQ-activ_enz_E1_Cys_AS.
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; PF00899; ThiF; 1.
DR Pfam; PF10585; UBA_E1_SCCH; 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 Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 4..65
FT /note="Ubiquitin-activating enzyme E1 four-helix bundle"
FT /evidence="ECO:0000259|Pfam:PF16191"
FT DOMAIN 152..338
FT /note="THIF-type NAD/FAD binding fold"
FT /evidence="ECO:0000259|Pfam:PF00899"
FT DOMAIN 339..526
FT /note="Ubiquitin-activating enzyme SCCH"
FT /evidence="ECO:0000259|Pfam:PF10585"
FT ACT_SITE 333
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ SEQUENCE 563 AA; 63498 MW; 2A804CA6EC5A9E9C CRC64;
LQLPLPEAIK DPEFLISDFA KFDRPAQLHL IWQAFDAFYE QKKFLPRPYN EADAGEMLFL
CEKLNAAAPE KTRLPDIDKD LVRLFSFQVE GNLIPITGFI GGIAAQEAMK GMTSIFTPIR
QWFYFDALEC LPDSDSPFKL NKQTCSARGS RYDGQVVVFG WPFQEALLRQ KWFIVGAGAI
GCELLKYFAH IGVACGPGGC LFLTDMDSIE TSNLNRQFLF HRQDVGSKKS EVAAKAAKSF
NPALNIKAMC DRVGGDTEQI FNDSFFENLD GVTNALDNVE ARTYMDRRCV YYRLPLVESG
TQGAKGNVQV VYPYLTESYS SSQDPPEKSI PICTLKNFPN AIEHTIQWAR DLFEGLFTIP
AELANQFLDD PRGFFERVDK MHAGQKAEML ASVKRVLIDD RPSNAEQCIT WARMRWEENF
NWQIRQLLHN FPADQVTLQG AKFWSGSKRC PHPLTFDAND PTHTEFVYSA SILRAQMYNI
IPIVDLTKVV EIATAQQPPP FVPKSGVRIA INDQEAQQAA QNGVEGKGAH RWQSDDLSRS
LFTVAFRRWP LPGVTPGFSQ IEA
//
