ID A0A194PXA9_PAPXU Unreviewed; 1044 AA.
AC A0A194PXA9;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=E1 ubiquitin-activating enzyme {ECO:0000256|ARBA:ARBA00012990};
DE EC=6.2.1.45 {ECO:0000256|ARBA:ARBA00012990};
DE AltName: Full=Ubiquitin-activating enzyme E1 {ECO:0000256|ARBA:ARBA00030371};
GN ORFNames=RR46_11493 {ECO:0000313|EMBL:KPI95780.1};
OS Papilio xuthus (Asian swallowtail butterfly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC Papilionidae; Papilioninae; Papilio.
OX NCBI_TaxID=66420 {ECO:0000313|EMBL:KPI95780.1, ECO:0000313|Proteomes:UP000053268};
RN [1] {ECO:0000313|EMBL:KPI95780.1, ECO:0000313|Proteomes:UP000053268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ya'a_city_454_Px {ECO:0000313|EMBL:KPI95780.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KPI95780.1};
RX PubMed=26354079; DOI=10.1038/ncomms9212;
RA Li X., Fan D., Zhang W., Liu G., Zhang L., Zhao L., Fang X., Chen L.,
RA Dong Y., Chen Y., Ding Y., Zhao R., Feng M., Zhu Y., Feng Y., Jiang X.,
RA Zhu D., Xiang H., Feng X., Li S., Wang J., Zhang G., Kronforst M.R.,
RA Wang W.;
RT "Outbred genome sequencing and CRISPR/Cas9 gene editing in butterflies.";
RL Nat. Commun. 6:8212-8212(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine
CC = AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-
CC L-cysteine.; EC=6.2.1.45; Evidence={ECO:0000256|ARBA:ARBA00000488};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family.
CC {ECO:0000256|ARBA:ARBA00005673, ECO:0000256|RuleBase:RU000519}.
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; KQ459595; KPI95780.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A194PXA9; -.
DR STRING; 66420.A0A194PXA9; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000053268; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004839; F:ubiquitin activating enzyme activity; IEA:UniProtKB-EC.
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; IPR018074; UBQ-activ_enz_E1_CS.
DR InterPro; IPR033127; UBQ-activ_enz_E1_Cys_AS.
DR InterPro; IPR000011; UBQ/SUMO-activ_enz_E1-like.
DR NCBIfam; TIGR01408; Ube1; 1.
DR PANTHER; PTHR10953:SF4; UBA_E1_C DOMAIN-CONTAINING PROTEIN; 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.
DR PROSITE; PS00536; UBIQUITIN_ACTIVAT_1; 1.
DR PROSITE; PS00865; UBIQUITIN_ACTIVAT_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU000519};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU000519};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU000519};
KW Reference proteome {ECO:0000313|Proteomes:UP000053268};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU000519}.
FT DOMAIN 914..1039
FT /note="Ubiquitin-activating enzyme E1 C-terminal"
FT /evidence="ECO:0000259|SMART:SM00985"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 624
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ SEQUENCE 1044 AA; 116657 MW; 5BCE6FB686E27664 CRC64;
MSSAEVADNS VDPPAKKRKL NTGETRCKSA AMANNGTRVE DEIDESLYSR QLYVLGHDAM
RRMASSDVLV SGLGGLGVEV AKNVILGGVK SVTLHDDRVC TIADLSSQFY LSECAIGQNR
ALASCEQLAE LNHYVPTTAY TGALTEEFLK KFRVVVLTGA SWVEQERIAA ITHANNIALV
IADTRGLFSQ VFCDFGPEFT VLDVTGENPA SAMIAVITHE YEAVVTCLDD TRHGLEDGDY
VTFSEIQGMT ELNGCEPRKI KVLGPYTFSI GDTTNFTKYQ RGGIVTQVKM PKKINFKPLK
ESIKEPEFLI ADFGKFDYPQ QLHLAFAALH KFQEAEGRLP KPWCDADATK FLEYVKTLVK
DKEFCKEDVE LNTDLLEIFC KVSSGDLNPM NAAIGGVVAQ EVMKACSGKF HPIVQWLYLD
AIECLPKDRS ILTEETCKPV GSRYDGQVAV FGRDFQKRLG ELKYFIVGAG AIGCELMKNF
AMIGVGADGG CITVTDMDLI EKSNLNRQFL FRPSDVQKPK SSTAAKVIKK MNPSMNVVAH
ENRVCPETEC VYHDQFFEQL DGVANALDNV DARIYMDRRC VYYRKPLLES GTLGTKGNTQ
VVVPYLTESY SSSQDPPEKS IPICTLKNFP NAIEHTLQWA RDEFEGLFRQ AAEHAAQYFT
DPHFLERTIK LPGSQPLDAI ESVRNAINER PMNFEDCVTW ARLHWESQYS NQIKQLLFNF
PPDQPTLSGA PFWSGPKRCP SPLVFDPEDE LHLDYVVAAA NLRAQVYGLP TCVDREAIAR
MAASVEVPEF KPRRGVKMAV TDNHLAAQNN DHMDQDKVKN IISELPPPGS LGGLKITPLE
FEKDDDTNFH MDFIVAASNL RAANYKIPPA DRHRSKLIAG KIIPAIATTT SVVAGLVCLE
LYKLAQGYNV LEVFKNGFVN LALPFFGFSE PIAAPVNSYY DKKWTLWDRF EIKGEITLQQ
FLDYFKNEHK LEITMLSQGV CMLYSFFMPK GKKQERLNLP MSEVVMAVSK KKLEPHVKAL
VFELCCNDED DNDVEVPYVK YTLP
//
