ID   D8VH16_9NEOP            Unreviewed;       275 AA.
AC   D8VH16;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 31.
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};
DE   Flags: Fragment;
GN   Name=SAE1 {ECO:0000313|EMBL:ADI82440.1};
OS   Heliconius heurippa.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC   Nymphalidae; Heliconiinae; Heliconiini; Heliconius.
OX   NCBI_TaxID=33423 {ECO:0000313|EMBL:ADI82440.1};
RN   [1] {ECO:0000313|EMBL:ADI82440.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=20442862; DOI=10.1371/journal.pgen.1000930;
RA   Salazar C., Baxter S.W., Pardo-Diaz C., Wu G., Surridge A., Linares M.,
RA   Bermingham E., Jiggins C.D.;
RT   "Genetic evidence for hybrid trait speciation in heliconius butterflies.";
RL   PLoS Genet. 6:E1000930-E1000930(2010).
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; GQ986253; ADI82440.1; -; Genomic_DNA.
DR   EMBL; GQ986263; ADI82450.1; -; Genomic_DNA.
DR   AlphaFoldDB; D8VH16; -.
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; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR045886; ThiF/MoeB/HesA.
DR   InterPro; IPR000594; ThiF_NAD_FAD-bd.
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; 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   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT   DOMAIN          2..251
FT                   /note="THIF-type NAD/FAD binding fold"
FT                   /evidence="ECO:0000259|Pfam:PF00899"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ADI82440.1"
FT   NON_TER         275
FT                   /evidence="ECO:0000313|EMBL:ADI82440.1"
SQ   SEQUENCE   275 AA;  30825 MW;  75CE57BAADE068B9 CRC64;
     SFKVLIIGLS GLGAEIAKNI ILSGVKSVCL LDDEKLTETD LYSQFLAPPD KIGENRAEIS
     LPRAKALNPM VDVSFVTKPV DDLPDDYFKA FDIVCATGLK QEQLERINNI CRDSNRKFLC
     GDVWGMFGYM FADLIDHEYS EEIVQHKAVK RGPDDNEKNA RETVSITVKR RAIYVPLQNA
     LSADWSKPEL RSRLRRGDPS YFVMKILLRF RDEYNRNPDP AQRKADTEIL LRMRDELVKE
     LSLPVGFISD SLLTDVFGIV SGAAAVVGGV IGQEV
//