ID A0A287A4L4_PIG Unreviewed; 433 AA.
AC A0A287A4L4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 2.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=NEDD8-activating enzyme E1 catalytic subunit {ECO:0000256|RuleBase:RU368009};
DE EC=6.2.1.64 {ECO:0000256|RuleBase:RU368009};
GN Name=UBA3 {ECO:0000313|Ensembl:ENSSSCP00000038718.2,
GN ECO:0000313|VGNC:VGNC:104088};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000038718.2, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000038718.2, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000038718.2,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000038718.2}
RP IDENTIFICATION.
RG Ensembl;
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|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}.
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DR AlphaFoldDB; A0A287A4L4; -.
DR Ensembl; ENSSSCT00000062691.3; ENSSSCP00000038718.2; ENSSSCG00000011506.5.
DR VGNC; VGNC:104088; UBA3.
DR GeneTree; ENSGT00550000074831; -.
DR UniPathway; UPA00885; -.
DR Proteomes; UP000008227; Chromosome 13.
DR Bgee; ENSSSCG00000011506; Expressed in stomach and 43 other cell types or tissues.
DR ExpressionAtlas; A0A287A4L4; baseline and differential.
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; 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; 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 1: Evidence at protein 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 Proteomics identification {ECO:0007829|PeptideAtlas:A0A287A4L4};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU368009}.
FT DOMAIN 344..432
FT /note="E2 binding"
FT /evidence="ECO:0000259|SMART:SM01181"
FT ACT_SITE 216
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ SEQUENCE 433 AA; 48563 MW; C12759153E20EA50 CRC64;
MAVDGGCGDT GDWEGRWNHV KKFLERSGPF THPDFEPSTE SLQFLLETCK VLVIGAGGLG
CELLKNLALS GFRQIHVIDM DTIDVSNLNR QFLFRPKDVG RPKAEVAAEF LNDRVPNCNV
VPHFNKIQDF NDTFYRQFHI IVCGLDSIIA RRWINGMLIS LLNYEDGVLD PSSIVPLIDG
GTEGFKGNAR VILPGMTACI ECTLELYPPQ VNFPMCTIAS MPRLPEHCIE YVRILQWPKE
QPFGEGVPLD GDDPDHIQWI FQKSLERASQ YNIRGVTYRL TQGKLVNSRE LSVCATEVFK
IATSAYIPLN NYLVFNDVDG LYTYTFEAER KENCPACSQL PQNIQFSPSA KLQEVLDYLT
NSASLQMKSP AITATLEGKN RTLYLQSVTS IEERTRPNLS KTLKELGLVD GQELAVADVT
TPQTVLFKLH FTS
//
