ID A0A232FA34_9HYME Unreviewed; 538 AA.
AC A0A232FA34;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=NEDD8-activating enzyme E1 regulatory subunit {ECO:0000256|ARBA:ARBA00015407, ECO:0000256|PIRNR:PIRNR039099};
GN ORFNames=TSAR_004454 {ECO:0000313|EMBL:OXU27293.1};
OS Trichomalopsis sarcophagae.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Proctotrupomorpha;
OC Chalcidoidea; Pteromalidae; Pteromalinae; Trichomalopsis.
OX NCBI_TaxID=543379 {ECO:0000313|EMBL:OXU27293.1, ECO:0000313|Proteomes:UP000215335};
RN [1] {ECO:0000313|EMBL:OXU27293.1, ECO:0000313|Proteomes:UP000215335}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Alberta {ECO:0000313|EMBL:OXU27293.1,
RC ECO:0000313|Proteomes:UP000215335};
RC TISSUE=Whole body {ECO:0000313|EMBL:OXU27293.1};
RX PubMed=28648823; DOI=10.1016/j.cub.2017.05.032;
RA Martinson E.O., Mrinalini, Kelkar Y.D., Chang C.H., Werren J.H.;
RT "The Evolution of Venom by Co-option of Single-Copy Genes.";
RL Curr. Biol. 27:2007-2013(2017).
CC -!- PATHWAY: Protein modification; protein neddylation.
CC {ECO:0000256|ARBA:ARBA00005032, ECO:0000256|PIRNR:PIRNR039099}.
CC -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family. ULA1
CC subfamily. {ECO:0000256|ARBA:ARBA00006868,
CC ECO:0000256|PIRNR:PIRNR039099}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OXU27293.1}.
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DR EMBL; NNAY01000633; OXU27293.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A232FA34; -.
DR STRING; 543379.A0A232FA34; -.
DR UniPathway; UPA00885; -.
DR Proteomes; UP000215335; Unassembled WGS sequence.
DR GO; GO:0019781; F:NEDD8 activating enzyme activity; IEA:UniProtKB-UniRule.
DR GO; GO:0045116; P:protein neddylation; IEA:UniProtKB-UniRule.
DR CDD; cd01493; APPBP1_RUB; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR030667; APP-BP1.
DR InterPro; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR PANTHER; PTHR10953:SF29; NEDD8-ACTIVATING ENZYME E1 REGULATORY SUBUNIT; 1.
DR PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 1.
DR Pfam; PF00899; ThiF; 1.
DR PIRSF; PIRSF039099; APP-BP1; 1.
DR SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000215335};
KW Ubl conjugation pathway {ECO:0000256|PIRNR:PIRNR039099}.
FT DOMAIN 18..524
FT /note="THIF-type NAD/FAD binding fold"
FT /evidence="ECO:0000259|Pfam:PF00899"
SQ SEQUENCE 538 AA; 60502 MW; 00D5F6242F26CC64 CRC64;
MASPAPKSPE QSEKSRKYDR QLRLWNDHGQ SFLESAHVCL INANALGTEI LKSLVLPGIG
AFTIIDGNKV TDEDIGSNFF LDADSTGKSR AQIATQLLLE LNSDVRGDYI DEGPEQILNN
SPDFFNNFTI VIACAMPEKS LIILSKKLWE LDIPLIVCRS IGFIGCARVQ IKEHTVVEMH
PDNEIPDLRL DKPFEGLKDH FDSIDLEAMD LKDHSHTPYV TVLYKYLQKW LETHQDLPKT
RVEKEEFKEM IRDGIRKDEN GVPVGEENFE EAIRAVNTCI RPTTVSGTVS EVLNDNSCIN
LNSKSSSFWI IAKAIRDFME HEGGGLLPLT GALPDMVADT EKFISLQQVY HKQAVADVEA
VWRRTLMLLR QLGKPSDSIP EKDVKLFCRH ASELCVQRGT CIADEYDPKL INTNKIAQEL
ENPESLMVYY VVLRGVEKFQ AEYNAYPGEF DDHVEPDIVK LKACISKLLG EWGCGPLVKD
DYVHEVCRFG GAELHSISAT LGGLVAQETV KFITHQYKPI SNTFIYDATI LEGATFFF
//
