ID A0A151WVW5_9HYME Unreviewed; 1068 AA.
AC A0A151WVW5;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=ALC60_08924 {ECO:0000313|EMBL:KYQ51978.1};
OS Trachymyrmex zeteki.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Trachymyrmex.
OX NCBI_TaxID=64791 {ECO:0000313|EMBL:KYQ51978.1, ECO:0000313|Proteomes:UP000075809};
RN [1] {ECO:0000313|EMBL:KYQ51978.1, ECO:0000313|Proteomes:UP000075809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tzet28-1 {ECO:0000313|EMBL:KYQ51978.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KYQ51978.1};
RA Nygaard S., Hu H., Boomsma J., Zhang G.;
RT "Trachymyrmex zeteki WGS genome.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; KQ982696; KYQ51978.1; -; Genomic_DNA.
DR RefSeq; XP_018308411.1; XM_018452909.1.
DR AlphaFoldDB; A0A151WVW5; -.
DR STRING; 64791.A0A151WVW5; -.
DR GeneID; 108725715; -.
DR OrthoDB; 20494at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000075809; 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:UP000075809};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU000519}.
FT DOMAIN 938..1063
FT /note="Ubiquitin-activating enzyme E1 C-terminal"
FT /evidence="ECO:0000259|SMART:SM00985"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 646
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ SEQUENCE 1068 AA; 118715 MW; 67EC19AC8C7A9DA2 CRC64;
MSSAEVADSS VDPPAKKRRV GAASTTGGAD DELTTTNVAE MDVDMAKNGS TSSSSGSGGT
TGRAPTDIDE GLYSRQLYVL GHDAMRRMAS SDVLISGLGG LGVEVAKNVI LGGVKSVTLH
DHAVCKLADL GSQFYLTEAD VGKNRAAACC QRLSELNNYV PTRHYSGPLN EAYIQQFKVV
VLTETSLTEQ LRISQITRAN DIALILADSR GLFSQVFCDF GETFTVVDTN GESPVNAMVA
SISRDSEGVV TCLDDTRHGM EDGDYVTFSE VQGMTELNGC EPIKIKVLGP YTFSIGDTSR
FSEYVRSGIV TQVKMPKTLH FTPLQTSLKK PEFLVTDFGK FDYPEQLHLA FLALHQYMTD
RGTLPRPWNQ SDADEFIAIA EQTKTNYGFD TEINGELLRT FAKVSAGDLN PMNATIGGIV
AQEVMKACSG KFHPIYQWMY FDAIECLPVD YSELTEEDCC PTGSRYDSQM AVFGKKFQSK
IGSLKYFVVG AGAIGCELLK NFAMIGVGAE NGCVTVTDMD LIEKSNLNRQ FLFRPSDVQQ
SKSATAARVI KSMNPNMNVV AHENRVCPET EKIYNDDFFE VLDGVANALD NVSARIYMDR
RCVYYHKPLL ESGTLGTKGN TQVVVPFLTE SYSSSQDPPE KSIPICTLKN FPNAIEHTLQ
WARDNFEGLF RQSAENAAQY ISDSQFVDRT LKLPGVQPLE VLESVKTALI DERPSTFTDC
VTWARCHWQE QYSNQIRQLL FNFPPDQVTS SGQPFWSGPK RCPEPLIFDV NDSLHMDYIV
AAANLKAKVY GLSVIRDKEV ITRYLDFVKI PDFTPKSGVK IAETDSQVQV SNGSGNIDHE
RLSQLQEELP KVEDLNGLAI YPQEFEKDDD TNFHIDFIVA ASNLRATNYK ISPADRHKSK
LIAGKIIPAI ATTTSVVAGL VCLELYKLTR GVRDLSLYKN GFVNLALPFF GFSEPIAAPK
LKYYDIEWTL WDRFEVKGEL TLKEFLDYFK ERHNLEVTML SQGICMLYSF FMAKAKCQER
MGLLMSEVVK KVSKKKLEPH VRALVFELCC NDEDGNDVEV PYVRYTLP
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