ID A0A3Q0RUY7_AMPCI Unreviewed; 452 AA.
AC A0A3Q0RUY7;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=NEDD8-activating enzyme E1 catalytic subunit {ECO:0000256|ARBA:ARBA00015203};
DE EC=6.2.1.64 {ECO:0000256|ARBA:ARBA00023624};
DE AltName: Full=NEDD8-activating enzyme E1C {ECO:0000256|ARBA:ARBA00030644};
DE AltName: Full=Ubiquitin-activating enzyme E1C {ECO:0000256|ARBA:ARBA00033110};
DE AltName: Full=Ubiquitin-like modifier-activating enzyme 3 {ECO:0000256|ARBA:ARBA00029566};
OS Amphilophus citrinellus (Midas cichlid) (Cichlasoma citrinellum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; New World cichlids;
OC Cichlasomatinae; Heroini; Amphilophus.
OX NCBI_TaxID=61819 {ECO:0000313|Ensembl:ENSACIP00000012160.1, ECO:0000313|Proteomes:UP000261340};
RN [1] {ECO:0000313|Ensembl:ENSACIP00000012160.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 -!- PATHWAY: Protein modification; protein neddylation.
CC {ECO:0000256|ARBA:ARBA00005032}.
CC -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family. UBA3
CC subfamily. {ECO:0000256|ARBA:ARBA00006310}.
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DR AlphaFoldDB; A0A3Q0RUY7; -.
DR STRING; 61819.ENSACIP00000012160; -.
DR Ensembl; ENSACIT00000012502.1; ENSACIP00000012160.1; ENSACIG00000009459.1.
DR GeneTree; ENSGT00550000074831; -.
DR OMA; HIIEYVI; -.
DR UniPathway; UPA00885; -.
DR Proteomes; UP000261340; Unplaced.
DR GO; GO:0019781; F:NEDD8 activating enzyme activity; IEA:UniProtKB-EC.
DR GO; GO:0045116; P:protein neddylation; IEA:UniProtKB-UniPathway.
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:SF233; 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 Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 363..451
FT /note="E2 binding"
FT /evidence="ECO:0000259|SMART:SM01181"
FT ACT_SITE 236
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ SEQUENCE 452 AA; 50668 MW; 54706C2DC5146B0F CRC64;
LLFSLFREKK RGRVVELTEK MVVDGDSRST CDWEDRWNHI KKFLERSGPF THPDFEPSTE
SLQFMLETCK ILVIGAGGLG CELLKDLALS GFRNIHVVDM DTIDVSNLNR QFLFRAKDVG
RPKADVAADF INSRVPGCCV VPHFTKIQDL NETFYRQFHI IVCGLDSIVA RRWMNGMLLS
LLVYEDGVLD PGSVIPLIDG GTEGFKGSAR VILPGMTACI DCTLEFYPPQ INFPMCTIAS
MPRLPEHCIE YVRILLWPKE MPFGDDVALD GDDPEHIQWV YQKSLERAAE FNITGVTYRL
TQGVVKRIIP AVASTNAVIA GKYAYLPLNN YMVFNDVDGM YTHTFEAERK ENCSACSQIP
LDLHFSPSSK LQEVLDYLTE SASLQMKSPA ITTTVDGKNK TLYLQSVASI EQRTRPNLAK
TLKELGLADG QELAVADVTT PQTMLLRLCF TS
//
