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Database: UniProt
Entry: A0A182ERT6_ONCOC
LinkDB: A0A182ERT6_ONCOC
Original site: A0A182ERT6_ONCOC 
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}.
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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
//
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