ID F0Y4F6_AURAN Unreviewed; 435 AA.
AC F0Y4F6;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE RecName: Full=NEDD8-activating enzyme E1 catalytic subunit {ECO:0000256|ARBA:ARBA00015203, ECO:0000256|RuleBase:RU368009};
DE EC=6.2.1.64 {ECO:0000256|ARBA:ARBA00023624, ECO:0000256|RuleBase:RU368009};
GN ORFNames=AURANDRAFT_22965 {ECO:0000313|EMBL:EGB10113.1};
OS Aureococcus anophagefferens (Harmful bloom alga).
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Pelagophyceae; Pelagomonadales;
OC Aureococcus.
OX NCBI_TaxID=44056 {ECO:0000313|Proteomes:UP000002729};
RN [1] {ECO:0000313|EMBL:EGB10113.1, ECO:0000313|Proteomes:UP000002729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP 1984 {ECO:0000313|Proteomes:UP000002729};
RX PubMed=21368207; DOI=10.1073/pnas.1016106108;
RA Gobler C.J., Berry D.L., Dyhrman S.T., Wilhelm S.W., Salamov A.,
RA Lobanov A.V., Zhang Y., Collier J.L., Wurch L.L., Kustka A.B., Dill B.D.,
RA Shah M., VerBerkmoes N.C., Kuo A., Terry A., Pangilinan J., Lindquist E.A.,
RA Lucas S., Paulsen I.T., Hattenrath-Lehmann T.K., Talmage S.C., Walker E.A.,
RA Koch F., Burson A.M., Marcoval M.A., Tang Y.Z., Lecleir G.R., Coyne K.J.,
RA Berg G.M., Bertrand E.M., Saito M.A., Gladyshev V.N., Grigoriev I.V.;
RT "Niche of harmful alga Aureococcus anophagefferens revealed through
RT ecogenomics.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:4352-4357(2011).
CC -!- FUNCTION: Catalytic subunit of the dimeric E1 enzyme, which activates
CC NEDD8. {ECO:0000256|RuleBase:RU368009}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + [NEDD8 protein] + [E1 NEDD8-activating enzyme]-L-
CC cysteine = AMP + diphosphate + [E1 NEDD8-activating enzyme]-S-[NEDD8
CC protein]-yl-L-cysteine.; EC=6.2.1.64;
CC Evidence={ECO:0000256|ARBA:ARBA00024626,
CC ECO:0000256|RuleBase:RU368009};
CC -!- PATHWAY: Protein modification; protein neddylation.
CC {ECO:0000256|ARBA:ARBA00005032, ECO:0000256|RuleBase:RU368009}.
CC -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family. UBA3
CC subfamily. {ECO:0000256|ARBA:ARBA00006310,
CC ECO:0000256|RuleBase:RU368009}.
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DR EMBL; GL833124; EGB10113.1; -; Genomic_DNA.
DR RefSeq; XP_009034946.1; XM_009036698.1.
DR AlphaFoldDB; F0Y4F6; -.
DR EnsemblProtists; EGB10113; EGB10113; AURANDRAFT_22965.
DR GeneID; 20219681; -.
DR KEGG; aaf:AURANDRAFT_22965; -.
DR eggNOG; KOG2015; Eukaryota.
DR InParanoid; F0Y4F6; -.
DR OMA; ATSCNPY; -.
DR OrthoDB; 20494at2759; -.
DR UniPathway; UPA00885; -.
DR Proteomes; UP000002729; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019781; F:NEDD8 activating enzyme activity; IEA:UniProtKB-UniRule.
DR GO; GO:0045116; P:protein neddylation; IEA:UniProtKB-UniRule.
DR CDD; cd01488; Uba3_RUB; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 1.10.10.520; Ubiquitin activating enzymes (Uba3). Chain: B, domain 2; 1.
DR Gene3D; 3.10.290.20; Ubiquitin-like 2 activating enzyme e1b. Chain: B, domain 3; 1.
DR InterPro; IPR014929; E2-binding.
DR InterPro; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR InterPro; IPR023318; Ub_act_enz_dom_a_sf.
DR InterPro; IPR030468; Uba3_N.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR InterPro; IPR033127; UBQ-activ_enz_E1_Cys_AS.
DR PANTHER; PTHR10953:SF6; NEDD8-ACTIVATING ENZYME E1 CATALYTIC SUBUNIT; 1.
DR PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 1.
DR Pfam; PF08825; E2_bind; 1.
DR Pfam; PF00899; ThiF; 1.
DR SMART; SM01181; E2_bind; 1.
DR SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 1.
DR PROSITE; PS00865; UBIQUITIN_ACTIVAT_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU368009};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU368009};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU368009};
KW Reference proteome {ECO:0000313|Proteomes:UP000002729};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU368009}.
FT DOMAIN 344..428
FT /note="E2 binding"
FT /evidence="ECO:0000259|SMART:SM01181"
FT ACT_SITE 210
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ SEQUENCE 435 AA; 47441 MW; 6E812B59EDBC49BF CRC64;
MYSNVDKLLT RPTSFGSETG SLAVGEFEAS PEVRDFVTSE CKVLVVGAGG LGCEILKDLA
LSGFADIHVI DMDTIDVSNL NRQFLFRAKD VGSPKATTAA AFINARCPKT TVTAHVGKVQ
EKDGDFYAQF NVVCSGLDNV EARRWLNSML VSLAEVDDDG NVVDPSQIIP MVDGGTEGFR
GQARVIIPRF TSCFECSLDS FPPQKTYPMC TIAETPRLPE HCISYAQLVE WPKAFPDKSV
DTDSPEDMTW IFQVAEARAR KFDIEGVTYM KTMGVVKNII PAVASTNAVV SAVCVNEVFK
LMTLCSQSLN TYMMYMGNHG VYTHTFEYKK KDDCPITSAR VRTLAVAPTM LLGTLIESMC
GPDSDLRLKA PSLTTASQSL YMRKPKALEA ATRANLGKPL SELVADDDEI TVTDAIFPGD
VSLTLKLSFE CEEAA
//
