ID A0A3P8U0P4_AMPPE Unreviewed; 1001 AA.
AC A0A3P8U0P4;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
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:ENSAPEP00000028862.1};
OS Amphiprion percula (Orange clownfish) (Lutjanus percula).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Amphiprion.
OX NCBI_TaxID=161767 {ECO:0000313|Ensembl:ENSAPEP00000028862.1, ECO:0000313|Proteomes:UP000265080};
RN [1] {ECO:0000313|Ensembl:ENSAPEP00000028862.1, ECO:0000313|Proteomes:UP000265080}
RP NUCLEOTIDE SEQUENCE.
RA Lehmann R.;
RT "Finding Nemo's genes: A chromosome-scale reference assembly of the genome
RT of the orange clownfish Amphiprion percula.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSAPEP00000028862.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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; A0A3P8U0P4; -.
DR STRING; 161767.ENSAPEP00000028862; -.
DR Ensembl; ENSAPET00000029622.1; ENSAPEP00000028862.1; ENSAPEG00000020511.1.
DR GeneTree; ENSGT00940000158826; -.
DR OMA; WSHCVEL; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000265080; Chromosome 3.
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:UP000265080};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 868..990
FT /note="Ubiquitin-activating enzyme E1 C-terminal"
FT /evidence="ECO:0000259|SMART:SM00985"
FT REGION 979..1001
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1001 AA; 111900 MW; E976F3B7D6A58BE6 CRC64;
MHQMAQSSVF LSGMGGLGVE IAKNIVLAGV KAVTLHDTKQ CETWDLGSNF FIRKEDVVSQ
RRRVEAVSPR VAELNPYVHV DTCSSALDDN TDLSFLRKYQ CVILTEARLS LQKRVNEFCH
SQQPPIRFIG CDAYGICVRV FCDFGGEFEV SDPTGEEPKE IFIQSITQDS PGVVTCMDNQ
PHGLQTGQSV VFREVNGMME LNSTARQVSV LSPHSFAIGD TSQLQPYAHG GFFVLVKTPK
TYKFETMEQQ LCDPQVLTPD FSKPEAPLQI HAAMFALDTF QEQHSRLPNI GCLQDAEALL
KLTEEVNATL KSKTPVNTEL VRCLSRTARG TLPPLAAAVG GVASQEVLKA ITGKFAPLQQ
WLYLDAIEVV RPLQSLSAED FFPRGDRYDG LRACVGESMC LELHKLRVFM VGCGAIGCEM
LKNFALLGVG LTKSSGEVCI TDPDLIEKSN LNRQFLFRPH HIQKPKSTTA AEATHDINPD
LQVDAHLNKV CPATENIYSD SFFTSLNLVV TALDNVEARR YVDSRCVSNQ RPLLDSGTMG
TKGHTEIIVP NLTESYNSHR DPPEEEIPFC TLKSFPSVIE HTIQWARDKF ENAFVHKPSM
YSSFWQTHSS AEVVLQRMQA GESLEGSFQV IKLLSRRPSQ WEQCVTIARL KFEKYFKRKA
LQLLHSFPLD TRLKDGSLFW QSPKRPPAPI DFDLNDSLHF TFIVSTARLF AGIYNIPYSE
TDLSEEAVTR ILSDVKIPEY KPSEKCIETD ETAKKPDQMK MPVSSEEERE AIIQLEQAIA
TDRVTPEGLQ MTPLQFEKDD DSNGHLDFVT SASSLRARMY SIEPADRLKT KRIAGKIIPA
IATATAAVAG LVALELIKVV GGYGFESFKN CFFNLAIPVV VLTEPAPVKQ TLIRNNIYFS
IWDCWTIFGH EDFTLSDFMN AVREKYGIEP TMVVHGVKML YVPVMPGHSK RLKLTMQKLI
KPSVDRRYVD LTVSFAPEAD GDEDLPGPPV RYYFSPDGET P
//