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Database: UniProt
Entry: G3PUF0_GASAC
LinkDB: G3PUF0_GASAC
Original site: G3PUF0_GASAC 
ID   G3PUF0_GASAC            Unreviewed;      1031 AA.
AC   G3PUF0;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   RecName: Full=SUMO-activating enzyme subunit 1 {ECO:0000256|ARBA:ARBA00044187};
DE   AltName: Full=Ubiquitin-like 1-activating enzyme E1A {ECO:0000256|ARBA:ARBA00044354};
GN   Name=UBA6 {ECO:0000313|Ensembl:ENSGACP00000021237.1};
OS   Gasterosteus aculeatus (Three-spined stickleback).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC   Gasterosteus.
OX   NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000021237.1, ECO:0000313|Proteomes:UP000007635};
RN   [1] {ECO:0000313|Ensembl:ENSGACP00000021237.1, ECO:0000313|Proteomes:UP000007635}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSGACP00000021237.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- PATHWAY: Protein modification; protein sumoylation.
CC       {ECO:0000256|ARBA:ARBA00004718}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
CC   -!- SUBUNIT: Heterodimer of SAE1 and UBA2/SAE2. The heterodimer corresponds
CC       to the two domains that are encoded on a single polypeptide chain in
CC       ubiquitin-activating enzyme E1. Interacts with UBE2I.
CC       {ECO:0000256|ARBA:ARBA00026003}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family.
CC       {ECO:0000256|ARBA:ARBA00005673}.
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DR   AlphaFoldDB; G3PUF0; -.
DR   STRING; 69293.ENSGACP00000021237; -.
DR   Ensembl; ENSGACT00000021278.1; ENSGACP00000021237.1; ENSGACG00000016096.1.
DR   eggNOG; KOG2012; Eukaryota.
DR   GeneTree; ENSGT00940000158826; -.
DR   InParanoid; G3PUF0; -.
DR   OMA; WSHCVEL; -.
DR   TreeFam; TF300586; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000007635; Unassembled WGS sequence.
DR   Bgee; ENSGACG00000016096; Expressed in liver and 13 other cell types or tissues.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   CDD; cd01491; Ube1_repeat1; 1.
DR   CDD; cd01490; Ube1_repeat2; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 2.40.30.180; Ubiquitin-activating enzyme E1, FCCH domain; 1.
DR   Gene3D; 3.50.50.80; Ubiquitin-activating enzyme E1, inactive adenylation domain, subdomain 1; 1.
DR   Gene3D; 3.40.50.12550; Ubiquitin-activating enzyme E1, inactive adenylation domain, subdomain 2; 1.
DR   Gene3D; 1.10.10.2660; Ubiquitin-activating enzyme E1, SCCH domain; 1.
DR   Gene3D; 3.10.290.60; Ubiquitin-activating enzyme E1, UFD domain; 1.
DR   InterPro; IPR032420; E1_4HB.
DR   InterPro; IPR032418; E1_FCCH.
DR   InterPro; IPR042302; E1_FCCH_sf.
DR   InterPro; IPR045886; ThiF/MoeB/HesA.
DR   InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR   InterPro; IPR018965; Ub-activating_enz_E1_C.
DR   InterPro; IPR042449; Ub-E1_IAD_1.
DR   InterPro; IPR038252; UBA_E1_C_sf.
DR   InterPro; IPR019572; UBA_E1_SCCH.
DR   InterPro; IPR042063; Ubi_acti_E1_SCCH.
DR   InterPro; IPR035985; Ubiquitin-activating_enz.
DR   InterPro; IPR018075; UBQ-activ_enz_E1.
DR   InterPro; IPR000011; UBQ/SUMO-activ_enz_E1-like.
DR   NCBIfam; TIGR01408; Ube1; 1.
DR   PANTHER; PTHR10953:SF162; SUMO-ACTIVATING ENZYME SUBUNIT 1; 1.
DR   PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 1.
DR   Pfam; PF16191; E1_4HB; 1.
DR   Pfam; PF16190; E1_FCCH; 1.
DR   Pfam; PF09358; E1_UFD; 1.
DR   Pfam; PF00899; ThiF; 2.
DR   Pfam; PF10585; UBA_E1_SCCH; 1.
DR   PRINTS; PR01849; UBIQUITINACT.
DR   SMART; SM00985; UBA_e1_C; 1.
DR   SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 2.
PE   3: Inferred from homology;
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007635};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT   DOMAIN          899..1021
FT                   /note="Ubiquitin-activating enzyme E1 C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00985"
SQ   SEQUENCE   1031 AA;  115518 MW;  4CB5D8AC996AD087 CRC64;
     PSMAADSMEI DDSLYSRQRY VLGDSAMHQM AQSSVFLSGM GGLGIEIAKN IVLAGVKAVT
     LHDTKRCETW DLGSNFFIHN EDVSTQKRRW RPRVEAVCPR VAELNPYVHV DVSSEALDDN
     NDLGFLGKYQ CVILTEARLS LQKRVNDFCH FHQPPIRFIG CDAYGICARV FCDFGEEFEV
     SDPTGEEPKE IFIQSITQGD RGVVTCMDNQ PHGLQTGQSV VFREVNGMVE VNGTARPIAV
     VLSPHSFEIG DTSQFQPYQH GGFFVLVKTP KTYRFETLER QLCDPHVLTP DFSKPEAPLQ
     IHAAMLALDA FQEQHSRLPN TGCSQDAEVL LKLNEEVNQT LRNKASVNVE LVRCLSRTAR
     GTLPPLAAAV GGLASQEVLK AITGKFAPLQ QWFYLDAVEV VRPLQSVAAE EFLPRGDRYD
     GLRACIGEPM CVALHKLRVF MVGCGAIGCE MLKNFALLGV GLTSSSGEVC ITDPDLIEKS
     NLNRQFLFRP RHIQKPKSTT AAEATLEINP DLQVDAHLNK VCPATESVYN DAFYSRVNLV
     VTALDSVEAR RYVDSRCLSN QRPLLDSGTM GTKGHTEIIV PNLTESYNSH RDPPEEEIPF
     CTLKSFPSVI EHTIQWARDK FENLFAHKPS MYNSFWQTHP SVEVVLQRMQ MGESLEGSFQ
     VIKLLSKRPS RWDQCIAIGR LKFEKYFKRK ALQLLHSFPL DTRLKDGSLF WQSPKRPPAP
     IDFDLRDSLH FSFIVSTARL FAGIYNIPYS PKDVTEEEVT RLLSDVKIPE YRPSEKCIET
     DETAKKPDSV KLPLSSEEER EAIAQLEHAI ATDNVTQSGC RWSPLQFEKD DDLNGHMDFV
     TAASALRARM YAIEPADRLK TKRIAGKIIP AIATATAAVA GLVALELVKV VGGYEFELFK
     NCFFNLAIPV VVLTEPAPVK QSLIRDNIYF SIWDCWSVFG HEDFTLSDFI NAVREKYGIE
     PTMVVHGVKM LYVPVMPGHS KRLKLTMQKL IKPSGDRRYV DLTVSFAPET DGDDDLAGPP
     VRYFFSRNGE T
//
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