UniProt: R1ENC3

Database: UniProt
Entry: R1ENC3_BOTPV

LinkDB:  R1ENC3_BOTPV 
Original site:  R1ENC3_BOTPV

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Ontology (3)   
   GO (3)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   KEGG GENES (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (9)   
   InterPro (6)   
   Pfam (2)   
   SMART (1)   
Literature (1)   
   PubMed (1)   
All databases (17)   

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ID   R1ENC3_BOTPV            Unreviewed;       429 AA.
AC   R1ENC3;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 43.
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=UCRNP2_4215 {ECO:0000313|EMBL:EOD49032.1};
OS   Botryosphaeria parva (strain UCR-NP2) (Grapevine canker fungus)
OS   (Neofusicoccum parvum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC   Neofusicoccum.
OX   NCBI_TaxID=1287680 {ECO:0000313|EMBL:EOD49032.1, ECO:0000313|Proteomes:UP000013521};
RN   [1] {ECO:0000313|Proteomes:UP000013521}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCR-NP2 {ECO:0000313|Proteomes:UP000013521};
RX   PubMed=23766404; DOI=10.1128/genomea.00339-13;
RA   Blanco-Ulate B., Rolshausen P., Cantu D.;
RT   "Draft genome sequence of Neofusicoccum parvum isolate UCR-NP2, a fungal
RT   vascular pathogen associated with grapevine cankers.";
RL   Genome Announc. 1:E0033913-E0033913(2013).
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; KB916119; EOD49032.1; -; Genomic_DNA.
DR   RefSeq; XP_007583499.1; XM_007583437.1.
DR   AlphaFoldDB; R1ENC3; -.
DR   STRING; 1287680.R1ENC3; -.
DR   KEGG; npa:UCRNP2_4215; -.
DR   eggNOG; KOG2015; Eukaryota.
DR   HOGENOM; CLU_013325_13_1_1; -.
DR   OMA; ATSCNPY; -.
DR   OrthoDB; 20494at2759; -.
DR   UniPathway; UPA00885; -.
DR   Proteomes; UP000013521; 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   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.
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:UP000013521};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|RuleBase:RU368009}.
FT   DOMAIN          345..428
FT                   /note="E2 binding"
FT                   /evidence="ECO:0000259|SMART:SM01181"
SQ   SEQUENCE   429 AA;  47870 MW;  415B4D3BD56A9624 CRC64;
     MADSAEAVPA RWKYLHNIIN RTGPFTDPDW EPGMTTLESL ANVKILGAGG LGCEILKNLA
     LSGFKDIHVI DMDTIDVSNL NRQFLFRQSD VGKPKAEVAA RFVEKRVKGV KITPYCGKIQ
     DKDEDYYMQF TLVVCGLDSI EARRWINAML VGMVDGDNPD SLKPLIDGGT EGFKGQARVI
     LPTMTSCIEC QLDMHAPRAA VPLCTLATIP RQPQHCIEWA HIIAWEEERK EDTLDTDDPE
     HITWLYNKAL IRAKEFNIPG VTYSMTQGVV KNIIPAIAST NAIVAAACCN EAFKIASNTN
     PPLGMPDSGN GNYMMYTGDD SVYTYTFEHQ KKDDCAVCGT LAKKLEVDSK RSLEEFLESL
     AERPDTQFKK PSIRSEAKTL YQQFPPSLEE QTRPNLKRKL ADLVSNGEEV AVTDPAFATD
     FKYKLVFRE
//

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