ID Q3B8H8_XENLA Unreviewed; 461 AA.
AC Q3B8H8;
DT 22-NOV-2005, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2005, sequence version 1.
DT 27-MAR-2024, entry version 91.
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 Name=uba3.S {ECO:0000313|RefSeq:NP_001089719.1,
GN ECO:0000313|Xenbase:XB-GENE-947296};
GN Synonyms=MGC131020 {ECO:0000313|EMBL:AAI06400.1}, uba3
GN {ECO:0000313|RefSeq:NP_001089719.1,
GN ECO:0000313|Xenbase:XB-GENE-947296}, ube1c
GN {ECO:0000313|RefSeq:NP_001089719.1};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000313|EMBL:AAI06400.1};
RN [1] {ECO:0000313|RefSeq:NP_001089719.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=12454917; DOI=10.1002/dvdy.10174;
RA Klein S.L., Strausberg R.L., Wagner L., Pontius J., Clifton S.W.,
RA Richardson P.;
RT "Genetic and genomic tools for Xenopus research: The NIH Xenopus
RT initiative.";
RL Dev. Dyn. 225:384-391(2002).
RN [2] {ECO:0000313|EMBL:AAI06400.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo {ECO:0000313|EMBL:AAI06400.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|RefSeq:NP_001089719.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC106399; AAI06400.1; -; mRNA.
DR RefSeq; NP_001089719.1; NM_001096250.1.
DR STRING; 8355.Q3B8H8; -.
DR PaxDb; 8355-Q3B8H8; -.
DR DNASU; 734782; -.
DR GeneID; 734782; -.
DR KEGG; xla:734782; -.
DR AGR; Xenbase:XB-GENE-947296; -.
DR CTD; 734782; -.
DR Xenbase; XB-GENE-947296; uba3.S.
DR OMA; HIIEYVI; -.
DR OrthoDB; 20494at2759; -.
DR UniPathway; UPA00885; -.
DR Proteomes; UP000186698; Chromosome 4S.
DR Bgee; 734782; Expressed in muscle tissue and 19 other cell types or tissues.
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 InterPro; IPR033127; UBQ-activ_enz_E1_Cys_AS.
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.
DR PROSITE; PS00865; UBIQUITIN_ACTIVAT_2; 1.
PE 2: Evidence at transcript level;
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:UP000186698};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU368009}.
FT DOMAIN 373..460
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 461 AA; 51789 MW; DCFD6305DF524519 CRC64;
MADAEEPEKK RRRIEELPDE MAVNGGCGET GDWEGRWNHV KKFLERSGPF THPEFEPSNE
SLQFLLETCK LLVVGAGGLG CELLKNLALS GFRQIHVIDM DTIDVSNLNR QFLFRPKDVG
RPKAEVAADF INARIPDCCV TPHFKKIQDF DETFYREFHI IVCGLDSIIA RRWLNGMLMS
LLNYEDSVLQ QSTVIPLIDG GTEGFKGNSR VILPGMTACV ECTLELYPPQ INFPMCTIAS
MPRLPEHCIE YVRILQWPKE QPFGEGVQLD GDDPEHIEWI FTNSLERANQ FNIRGVTYRL
TQGVVKRIIP AVASTNAVIA AACATEVFKI ATSAYIPLNN YLVFNDVDGL YSYTFEAEKK
ENCPACSQLP QNIQFPSSAK LQEVLDYLTN DTLQMKAPAI TATLEGKNKT LYLQTVTSIE
ERTRPNLCRT LKELGLVDGQ ELAVADVTTP QTVLFKLHFT A
//
