ID I2JRS5_DEKBR Unreviewed; 509 AA.
AC I2JRS5;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 2.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=NEDD8-activating enzyme E1 regulatory subunit {ECO:0000256|PIRNR:PIRNR039099};
GN ORFNames=AWRI1499_4423 {ECO:0000313|EMBL:EIF45677.1};
OS Brettanomyces bruxellensis AWRI1499.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Brettanomyces.
OX NCBI_TaxID=1124627 {ECO:0000313|EMBL:EIF45677.1, ECO:0000313|Proteomes:UP000004997};
RN [1] {ECO:0000313|EMBL:EIF45677.1, ECO:0000313|Proteomes:UP000004997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AWRI1499 {ECO:0000313|EMBL:EIF45677.1,
RC ECO:0000313|Proteomes:UP000004997};
RX PubMed=22470482; DOI=10.1371/journal.pone.0033840;
RA Curtin C.D., Borneman A.R., Chambers P.J., Pretorius I.S.;
RT "De-Novo Assembly and Analysis of the Heterozygous Triploid Genome of the
RT Wine Spoilage Yeast Dekkera bruxellensis AWRI1499.";
RL PLoS ONE 7:E33840-E33840(2012).
CC -!- FUNCTION: Regulatory subunit of the dimeric UBA3-ULA1 E1 enzyme.
CC {ECO:0000256|PIRNR:PIRNR039099}.
CC -!- PATHWAY: Protein modification; protein neddylation.
CC {ECO:0000256|ARBA:ARBA00005032, ECO:0000256|PIRNR:PIRNR039099}.
CC -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family. ULA1
CC subfamily. {ECO:0000256|ARBA:ARBA00006868,
CC ECO:0000256|PIRNR:PIRNR039099}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EIF45677.1}.
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DR EMBL; AHIQ01000258; EIF45677.1; -; Genomic_DNA.
DR UniPathway; UPA00885; -.
DR Proteomes; UP000004997; Unassembled WGS sequence.
DR GO; GO:0019781; F:NEDD8 activating enzyme activity; IEA:UniProtKB-UniRule.
DR GO; GO:0045116; P:protein neddylation; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR030667; APP-BP1.
DR InterPro; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR PANTHER; PTHR10953:SF29; NEDD8-ACTIVATING ENZYME E1 REGULATORY SUBUNIT; 1.
DR PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 1.
DR Pfam; PF00899; ThiF; 1.
DR PIRSF; PIRSF039099; APP-BP1; 1.
DR SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000004997};
KW Ubl conjugation pathway {ECO:0000256|PIRNR:PIRNR039099}.
FT DOMAIN 10..503
FT /note="THIF-type NAD/FAD binding fold"
FT /evidence="ECO:0000259|Pfam:PF00899"
FT UNSURE 65
FT /note="E or Q"
FT /evidence="ECO:0000313|EMBL:EIF45677.1"
FT UNSURE 324
FT /note="D or N"
FT /evidence="ECO:0000313|EMBL:EIF45677.1"
SQ SEQUENCE 509 AA; 58135 MW; 2F1167EF6E388D00 CRC64;
MDEKDVNSKY DRQIRLWSSR GQKSLSRSSV CIIGANXTAS EXLKNIVLAG IGRAXIIDND
TKVNEDDIAS NFFISYGLXG KNRAEXITQN ISEXNKDVLI SVEXRXLKEL IKDVPFWNKF
DCVILNQYLP DSGMSEQLSN ILWENNVCLI KAVNXGLYGS VRIQMQEQDI LETHDNNLED
LRIDNCWSEL QDYIDXIDLD GMDDQTFSNV PXSIILSKIY QSFXRTKNQQ LTPSAIRTYI
KDHLRRTGEE ANLDQACNRA AIVLKRSSSI PSNLQDIFNN XKXXGDPXSL NNFWLLCRAL
KLFYEEEGIL PLSGVIPDME SXTDQYITLK KLYENKFNAD KNKXVQIVHR LLGEEXXPFT
DLQLTSFVKN CRFMQVHXGS RDLFRSEILT DRENSSELRN VNIYLALIST EEFFFKFHRL
PTMQDRXKLR TITISLLCRY NSVKDFPDGL DKVLDELCRC SGAQIHNISA LIGGIASQEA
IKVITGQYVT LDNCLSYDGI HSQAVTWKI
//