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Database: UniProt
Entry: S9V8N0_9TRYP
LinkDB: S9V8N0_9TRYP
Original site: S9V8N0_9TRYP 
ID   S9V8N0_9TRYP            Unreviewed;       462 AA.
AC   S9V8N0;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=NEDD8-activating enzyme E1 catalytic subunit {ECO:0000256|RuleBase:RU368009};
DE            EC=6.2.1.64 {ECO:0000256|RuleBase:RU368009};
GN   ORFNames=STCU_07756 {ECO:0000313|EMBL:EPY23341.1};
OS   Strigomonas culicis.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Strigomonadinae; Strigomonas.
OX   NCBI_TaxID=28005 {ECO:0000313|EMBL:EPY23341.1, ECO:0000313|Proteomes:UP000015354};
RN   [1] {ECO:0000313|EMBL:EPY23341.1, ECO:0000313|Proteomes:UP000015354}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23560078;
RA   Motta M.C., Martins A.C., de Souza S.S., Catta-Preta C.M., Silva R.,
RA   Klein C.C., de Almeida L.G., de Lima Cunha O., Ciapina L.P., Brocchi M.,
RA   Colabardini A.C., de Araujo Lima B., Machado C.R., de Almeida Soares C.M.,
RA   Probst C.M., de Menezes C.B., Thompson C.E., Bartholomeu D.C., Gradia D.F.,
RA   Pavoni D.P., Grisard E.C., Fantinatti-Garboggini F., Marchini F.K.,
RA   Rodrigues-Luiz G.F., Wagner G., Goldman G.H., Fietto J.L., Elias M.C.,
RA   Goldman M.H., Sagot M.F., Pereira M., Stoco P.H., de Mendonca-Neto R.P.,
RA   Teixeira S.M., Maciel T.E., de Oliveira Mendes T.A., Urmenyi T.P.,
RA   de Souza W., Schenkman S., de Vasconcelos A.T.;
RT   "Predicting the Proteins of Angomonas deanei, Strigomonas culicis and Their
RT   Respective Endosymbionts Reveals New Aspects of the Trypanosomatidae
RT   Family.";
RL   PLoS ONE 8:E60209-E60209(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|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:EPY23341.1}.
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DR   EMBL; ATMH01007756; EPY23341.1; -; Genomic_DNA.
DR   AlphaFoldDB; S9V8N0; -.
DR   EnsemblProtists; EPY23341; EPY23341; STCU_07756.
DR   OrthoDB; 20494at2759; -.
DR   UniPathway; UPA00885; -.
DR   Proteomes; UP000015354; 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   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:UP000015354};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|RuleBase:RU368009}.
FT   DOMAIN          41..359
FT                   /note="THIF-type NAD/FAD binding fold"
FT                   /evidence="ECO:0000259|Pfam:PF00899"
SQ   SEQUENCE   462 AA;  49940 MW;  8CBA353DF2FCD91E CRC64;
     MSGSAGSCEA PIDRCVDRCS GLQHLVRAGR YTLSAEEGGA DLSGLAEVEV LIVGAGGTGS
     EILHLLAMSG FARLTILDMD RIELSNLNRQ FLFQEKDIGA FKSDVAAAFV RARCPGVAIH
     AVVGSAEEQS DDFYRRFDLI FLALDSNAVR HWVNRKVVEL GTWEVVPRAA VPGLAAADAH
     AAPFVRVLRA CTPLVDVGTE GYRGHTKFRH PPRLPCLACA MDPTPGEEKV PMCTLHTIPR
     LPQHCVLYAK EKLWRDAFPD TDLDADREEH IRWLTEQARQ RQREFGIHGD ITEKYVLGVV
     KNVVPAVGFT NAFVAGQAVT EVVKRFTGVG ESREVFWVYS GLNGSFLMAT AETGLPSCPV
     CGPVPVLALR ADMTLAEVRA AAAAQLRLTV TAAAPLLWTG PGGRLIQAPA GAAGDAMTLL
     SLFAQAGAEP YLREQWCTDA VLPYMTITAE ERSCQVLCKC TL
//
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