ID A0A182ERT6_ONCOC Unreviewed; 425 AA.
AC A0A182ERT6;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=SUMO-activating enzyme subunit 1 {ECO:0000256|ARBA:ARBA00044187};
DE AltName: Full=Ubiquitin-like 1-activating enzyme E1A {ECO:0000256|ARBA:ARBA00044354};
GN ORFNames=NOO_LOCUS10854 {ECO:0000313|EMBL:VDM94581.1};
OS Onchocerca ochengi (Filarial nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Onchocerca.
OX NCBI_TaxID=42157 {ECO:0000313|Proteomes:UP000077448, ECO:0000313|WBParaSite:nOo.2.0.1.t10854-RA};
RN [1] {ECO:0000313|Proteomes:UP000077448}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22919073; DOI=10.1101/gr.138420.112;
RA Darby A.C., Armstrong S.D., Bah G.S., Kaur G., Hughes M.A., Kay S.M.,
RA Koldkaer P., Rainbow L., Radford A.D., Blaxter M.L., Tanya V.N.,
RA Trees A.J., Cordaux R., Wastling J.M., Makepeace B.L.;
RT "Analysis of gene expression from the Wolbachia genome of a filarial
RT nematode supports both metabolic and defensive roles within the
RT symbiosis.";
RL Genome Res. 22:2467-2477(2012).
RN [2] {ECO:0000313|WBParaSite:nOo.2.0.1.t10854-RA}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
RN [3] {ECO:0000313|EMBL:VDM94581.1, ECO:0000313|Proteomes:UP000271087}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Laetsch R D., Stevens L., Kumar S., Blaxter L. M.;
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Protein modification; protein sumoylation.
CC {ECO:0000256|ARBA:ARBA00004718}.
CC -!- SUBUNIT: Heterodimer of SAE1 and UBA2/SAE2. The heterodimer corresponds
CC to the two domains that are encoded on a single polypeptide chain in
CC ubiquitin-activating enzyme E1. Interacts with UBE2I.
CC {ECO:0000256|ARBA:ARBA00026003}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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 EMBL; UYRW01006737; VDM94581.1; -; Genomic_DNA.
DR STRING; 42157.A0A182ERT6; -.
DR WBParaSite; nOo.2.0.1.t10854-RA; nOo.2.0.1.t10854-RA; nOo.2.0.1.g10854.
DR Proteomes; UP000077448; Unassembled WGS sequence.
DR Proteomes; UP000271087; Unassembled WGS sequence.
DR GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR GO; GO:0032446; P:protein modification by small protein conjugation; IEA:UniProt.
DR Gene3D; 2.40.30.180; Ubiquitin-activating enzyme E1, FCCH domain; 1.
DR Gene3D; 3.50.50.80; Ubiquitin-activating enzyme E1, inactive adenylation domain, subdomain 1; 1.
DR Gene3D; 3.40.50.12550; Ubiquitin-activating enzyme E1, inactive adenylation domain, subdomain 2; 1.
DR InterPro; IPR032420; E1_4HB.
DR InterPro; IPR032418; E1_FCCH.
DR InterPro; IPR042302; E1_FCCH_sf.
DR InterPro; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR InterPro; IPR042449; Ub-E1_IAD_1.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR InterPro; IPR000011; UBQ/SUMO-activ_enz_E1-like.
DR PANTHER; PTHR10953:SF162; SUMO-ACTIVATING ENZYME SUBUNIT 1; 1.
DR PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 1.
DR Pfam; PF16191; E1_4HB; 1.
DR Pfam; PF16190; E1_FCCH; 1.
DR Pfam; PF00899; ThiF; 1.
DR PRINTS; PR01849; UBIQUITINACT.
DR SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 1.
PE 3: Inferred from homology;
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000271087};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 33..395
FT /note="THIF-type NAD/FAD binding fold"
FT /evidence="ECO:0000259|Pfam:PF00899"
FT DOMAIN 206..274
FT /note="Ubiquitin-activating enzyme E1 FCCH"
FT /evidence="ECO:0000259|Pfam:PF16190"
FT DOMAIN 276..334
FT /note="Ubiquitin-activating enzyme E1 four-helix bundle"
FT /evidence="ECO:0000259|Pfam:PF16191"
SQ SEQUENCE 425 AA; 47404 MW; 551E181B580F1D51 CRC64;
SQIDSAIESA KMVVNSENGM TDNSDAVLDK NLYSRQIYAL GESAMMHLRK ASVLISGIGS
VGVEIAKNLI LGGIRQVTIH DIRDAKWLDL SAQFYLKESD IGRNRAEASF ERLAELNDSV
TCHLSMEPLT EDFVKKFDLT VLTDAPLSMQ LMVNDWTRKH NRRFITADAR GLFGFIFVDV
GAQFEVNDPN GERCKELLIE HIDAETGDVT TLDNVMHGLE DGDYVTFSEV KGMIELNGIK
PLEITVKKPD VFNIGKVAAK FSPYVEGGRF TQVKVPSSVS HKSLKESLNE PSIVMWDFAK
FDNPPQLHAL WQALYAFETK HGRSPMPRNK EDVDLLKTEL PPSVEPNEKL LRIFSYQACG
NLAPIASIVG GIAAQEAMKV ITHHMTPLKQ FLYIDCVEAL PGDWSPFDND KLTANDCKMV
SFNFT
//