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Database: UniProt
Entry: N6TTL1_DENPD
LinkDB: N6TTL1_DENPD
Original site: N6TTL1_DENPD 
ID   N6TTL1_DENPD            Unreviewed;       444 AA.
AC   N6TTL1;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 58.
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};
DE   Flags: Fragment;
GN   Name=109543973 {ECO:0000313|EnsemblMetazoa:ENN71721};
GN   ORFNames=D910_04598 {ECO:0000313|EMBL:ERL87199.1}, YQE_11644
GN   {ECO:0000313|EMBL:ENN71721.1};
OS   Dendroctonus ponderosae (Mountain pine beetle).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC   Curculionidae; Scolytinae; Dendroctonus.
OX   NCBI_TaxID=77166 {ECO:0000313|EMBL:ENN71721.1};
RN   [1] {ECO:0000313|Proteomes:UP000019118, ECO:0000313|Proteomes:UP000030742}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=23537049; DOI=10.1186/gb-2013-14-3-r27;
RA   Keeling C.I., Yuen M.M., Liao N.Y., Roderick Docking T., Chan S.K.,
RA   Taylor G.A., Palmquist D.L., Jackman S.D., Nguyen A., Li M., Henderson H.,
RA   Janes J.K., Zhao Y., Pandoh P., Moore R., Sperling F.A., W Huber D.P.,
RA   Birol I., Jones S.J., Bohlmann J.;
RT   "Draft genome of the mountain pine beetle, Dendroctonus ponderosae Hopkins,
RT   a major forest pest.";
RL   Genome Biol. 14:R27-R27(2013).
RN   [2] {ECO:0000313|EnsemblMetazoa:ENN71721}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (JAN-2017) to UniProtKB.
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; APGK01055118; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KB741259; ENN71721.1; -; Genomic_DNA.
DR   EMBL; KB631924; ERL87199.1; -; Genomic_DNA.
DR   RefSeq; XP_019769492.1; XM_019913933.1.
DR   AlphaFoldDB; N6TTL1; -.
DR   STRING; 77166.N6TTL1; -.
DR   EnsemblMetazoa; ENN71721; ENN71721; YQE_11644.
DR   GeneID; 109543973; -.
DR   KEGG; dpa:109543973; -.
DR   HOGENOM; CLU_013325_13_1_1; -.
DR   OMA; ATSCNPY; -.
DR   OrthoDB; 20494at2759; -.
DR   UniPathway; UPA00885; -.
DR   Proteomes; UP000019118; Unassembled WGS sequence.
DR   Proteomes; UP000030742; 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:UP000030742};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|RuleBase:RU368009}.
FT   DOMAIN          349..437
FT                   /note="E2 binding"
FT                   /evidence="ECO:0000259|SMART:SM01181"
FT   ACT_SITE        212
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ENN71721.1"
SQ   SEQUENCE   444 AA;  49396 MW;  9FE08B11F9F9D9E7 CRC64;
     MEEFQEGTQK RWIHLRNILE RPGPFSRPEY VPSPEILEFL LTSCKVLIIG AGGLGCELLK
     DLAMMGFRHL HIIDMDVIDL SNLNRQFLFR HKDIGLPKAE VAAKYVNARV QGCQVVPHYC
     PIQDRSEGFY QQFHVIVCGL DSVPARRWIN GMVVSLLCYD EDGVLDQSSV IPLVDGGTEG
     FKGNARVIVP GVTACIECTL DLYPPQVTYP LCTIANTPRL PEHCIEYVKV AQWPKDNPFG
     VDLDGDDAQH LTWVHEKAVE RATQFNIKGV TYRLVQGVVK NIIPAVASTN AVIAAVCATE
     VFKIASTSLV PLNNFMIFND IDGIYTYIYE AERKVDCTVC SNIPQLVTVE DPSKMKLKDL
     VELLRESPKF QMKSPGLTTT VNGTNKTLYM STIGAIEKMT KGNLTKSLLE LGLKDGQELM
     VADTTTPNAI IVKLAFKQSD TEMK
//
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