ID Q5CW40_CRYPI Unreviewed; 346 AA.
AC Q5CW40;
DT 12-APR-2005, integrated into UniProtKB/TrEMBL.
DT 12-APR-2005, sequence version 1.
DT 24-JAN-2024, entry version 91.
DE RecName: Full=NEDD8-activating enzyme E1 catalytic subunit {ECO:0000256|RuleBase:RU368009};
DE EC=6.2.1.64 {ECO:0000256|RuleBase:RU368009};
DE Flags: Fragment;
GN ORFNames=cgd8_1730 {ECO:0000313|EMBL:EAK89686.1};
OS Cryptosporidium parvum (strain Iowa II).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Cryptosporidiidae; Cryptosporidium.
OX NCBI_TaxID=353152 {ECO:0000313|EMBL:EAK89686.1, ECO:0000313|Proteomes:UP000006726};
RN [1] {ECO:0000313|EMBL:EAK89686.1, ECO:0000313|Proteomes:UP000006726}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Iowa II {ECO:0000313|Proteomes:UP000006726};
RX PubMed=15044751; DOI=10.1126/science.1094786;
RA Abrahamsen M.S., Templeton T.J., Enomoto S., Abrahante J.E., Zhu G.,
RA Lancto C.A., Deng M., Liu C., Widmer G., Tzipori S., Buck G.A., Xu P.,
RA Bankier A.T., Dear P.H., Konfortov B.A., Spriggs H.F., Iyer L.,
RA Anantharaman V., Aravind L., Kapur V.;
RT "Complete genome sequence of the apicomplexan, Cryptosporidium parvum.";
RL Science 304:441-445(2004).
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|RuleBase:RU368009};
CC -!- PATHWAY: Protein modification; protein neddylation.
CC {ECO:0000256|RuleBase:RU368009}.
CC -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family. UBA3
CC subfamily. {ECO:0000256|RuleBase:RU368009}.
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:EAK89686.1}.
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DR EMBL; AAEE01000003; EAK89686.1; -; Genomic_DNA.
DR RefSeq; XP_627079.1; XM_627079.1.
DR AlphaFoldDB; Q5CW40; -.
DR STRING; 353152.Q5CW40; -.
DR EnsemblProtists; EAK89686; EAK89686; cgd8_1730.
DR GeneID; 3374408; -.
DR KEGG; cpv:cgd8_1730; -.
DR InParanoid; Q5CW40; -.
DR OMA; ATSCNPY; -.
DR OrthoDB; 20494at2759; -.
DR UniPathway; UPA00885; -.
DR Proteomes; UP000006726; Chromosome 8.
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 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 InterPro; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR InterPro; IPR023318; Ub_act_enz_dom_a_sf.
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; PF00899; ThiF; 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:UP000006726};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU368009}.
FT DOMAIN 50..341
FT /note="THIF-type NAD/FAD binding fold"
FT /evidence="ECO:0000259|Pfam:PF00899"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EAK89686.1"
SQ SEQUENCE 346 AA; 38984 MW; B7AE90E0DEFD4C5D CRC64;
KFGEFFFVKF LLKLIAPPQL STFSFIYTPQ HGKAIMNSEC KTLEKDIGLA YCKVLLVGVG
GIGTEILRCL IFSGFRRIDI VDYDYVEVSN ISRQLFFNLG DEGKSKVHVL AANATNHFKS
AKGLEIKPFH SDISDFFSKF NVTPSDYKII LSGLDNIHAR RTLNAIVMTQ SSPQAYPILL
DSGTEGFNGH SRIIIPGETS CYECTMGLNV QDTNFPLCEI KEFPRTPIHC IAYANFIYEE
DEQDNEDFKN HKILKIYQLA QEHAKSFGIQ GVTLELTKQI IGNIFPTLLS TNTIIASSVV
SQAIKYLRGS GQAKNLKNYF MYYGQTGIYS SCFEIHKDEN CIFCKI
//
