ID V3ZQN4_LOTGI Unreviewed; 344 AA.
AC V3ZQN4;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=LOTGIDRAFT_182121 {ECO:0000313|EMBL:ESO93718.1};
OS Lottia gigantea (Giant owl limpet).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Patellogastropoda; Lottioidea; Lottiidae; Lottia.
OX NCBI_TaxID=225164 {ECO:0000313|EMBL:ESO93718.1, ECO:0000313|Proteomes:UP000030746};
RN [1] {ECO:0000313|EMBL:ESO93718.1, ECO:0000313|Proteomes:UP000030746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23254933; DOI=10.1038/nature11696;
RA Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P.,
RA Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R.,
RA Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., Aerts A.,
RA Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., Lindberg D.R.,
RA Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.;
RT "Insights into bilaterian evolution from three spiralian genomes.";
RL Nature 493:526-531(2013).
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; KB201890; ESO93718.1; -; Genomic_DNA.
DR RefSeq; XP_009055349.1; XM_009057101.1.
DR AlphaFoldDB; V3ZQN4; -.
DR STRING; 225164.V3ZQN4; -.
DR EnsemblMetazoa; LotgiT182121; LotgiP182121; LotgiG182121.
DR GeneID; 20244477; -.
DR KEGG; lgi:LOTGIDRAFT_182121; -.
DR CTD; 20244477; -.
DR HOGENOM; CLU_002556_4_0_1; -.
DR OMA; EFFGQFD; -.
DR OrthoDB; 5483037at2759; -.
DR Proteomes; UP000030746; 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 CDD; cd01492; Aos1_SUMO; 1.
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 Reference proteome {ECO:0000313|Proteomes:UP000030746};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 14..336
FT /note="THIF-type NAD/FAD binding fold"
FT /evidence="ECO:0000259|Pfam:PF00899"
FT REGION 176..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 344 AA; 38677 MW; 484ACF0873672DB5 CRC64;
MSGENITEDE AALYDRQIRL WGLDAQKRLR ASKVLLIGLK GLGAEVAKNI VLSGIKSLTL
LDHTVVDEED KNSQFLIPHS ELGKNRAVSS LERTQCLNPM VNVTADTEDI NSKSDDYFKQ
YDVICATCCQ PSLLTKLDNL CAENNIKFFA GDIFGYYGFM FSDLGKHEYA EEIPKLNQKS
DKQDEEGSGE PSVKKAKKDE TETVVIKKEE IFSTFQSALD VDWTVTTNQS KINRTPNTHY
ITLAILNFME EHKRRPLLTS VENDVKALCE CRTKIMEKNK LTDKKFPVDF TEYCFSELSP
VCAIVGGVLG QEIIKAVSQR DPPHNNFFFY NGVEGTGMVD KIGN
//
