ID   A0A3B4AR13_9GOBI        Unreviewed;       436 AA.
AC   A0A3B4AR13;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 23.
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};
OS   Periophthalmus magnuspinnatus.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Gobiaria; Gobiiformes; Gobioidei; Gobiidae; Oxudercinae; Periophthalmus.
OX   NCBI_TaxID=409849 {ECO:0000313|Ensembl:ENSPMGP00000019145.1, ECO:0000313|Proteomes:UP000261520};
RN   [1] {ECO:0000313|Ensembl:ENSPMGP00000019145.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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}.
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DR   AlphaFoldDB; A0A3B4AR13; -.
DR   STRING; 409849.ENSPMGP00000019145; -.
DR   Ensembl; ENSPMGT00000020413.1; ENSPMGP00000019145.1; ENSPMGG00000015565.1.
DR   UniPathway; UPA00885; -.
DR   Proteomes; UP000261520; Unplaced.
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   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   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|RuleBase:RU368009}.
FT   DOMAIN          347..435
FT                   /note="E2 binding"
FT                   /evidence="ECO:0000259|SMART:SM01181"
FT   ACT_SITE        229
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ   SEQUENCE   436 AA;  48893 MW;  12B9CD1E70075F2C CRC64;
     MADRVLFCFA SRMAVDGGHS DVSCDWDGRW NHVKKFLERP GPFTHPDFEP STETLQFLLE
     TCKILVIGAG GLGCELLKNL ALSGFRVIHV VDMDTIDVSN LNRQFLFRPK DVGRPKADVA
     AEFINNRVPG CEVVPHFKKI QDFDESFYRQ FHIIVCGLDS VIARRWMNGM LISLLSYEDG
     VLDSSSIIPL IDGGTEGFKG NARVILPGMS ACIDCTLELY PPQINFPMCT IASMPRIPEH
     CIEYARVLQW PKEKPFGEIS LDGDNPEHIQ WVFAKALERA AEFNITGVTY RLTQAACATE
     VFKIASSAYI PLNNYMVFND VDGLYTYTFE AERKDNCSAC SQVPQDLQFR PSAKLQEVLE
     YLTENSSLQM KSPAITTTLE GKNKTLYLQT VKSIEERTRP NLCKTLKELG LSDGQELAVA
     DVTTPQTVLF KLNFIA
//