ID A0A016SVA0_9BILA Unreviewed; 1054 AA.
AC A0A016SVA0;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=E1 ubiquitin-activating enzyme {ECO:0000256|ARBA:ARBA00012990};
DE EC=6.2.1.45 {ECO:0000256|ARBA:ARBA00012990};
GN Name=Acey_s0173.g391 {ECO:0000313|EMBL:EYB94264.1};
GN Synonyms=Acey-uba-1 {ECO:0000313|EMBL:EYB94264.1};
GN ORFNames=Y032_0173g391 {ECO:0000313|EMBL:EYB94264.1};
OS Ancylostoma ceylanicum.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=53326 {ECO:0000313|EMBL:EYB94264.1, ECO:0000313|Proteomes:UP000024635};
RN [1] {ECO:0000313|Proteomes:UP000024635}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX PubMed=25730766; DOI=10.1038/ng.3237;
RA Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA Aroian R.V.;
RT "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT ceylanicum identify infection-specific gene families.";
RL Nat. Genet. 47:416-422(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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EYB94264.1}.
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DR EMBL; JARK01001509; EYB94264.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A016SVA0; -.
DR STRING; 53326.A0A016SVA0; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000024635; Unassembled WGS sequence.
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; 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; 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:UP000024635};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU000519}.
FT DOMAIN 924..1050
FT /note="Ubiquitin-activating enzyme E1 C-terminal"
FT /evidence="ECO:0000259|SMART:SM00985"
FT ACT_SITE 626
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ SEQUENCE 1054 AA; 117891 MW; 3C07C51AB7474441 CRC64;
MHAMYRAFLM FLSQESAITL KNSSANSDSK RMTAAKNGQE AMDTDAAGLD TNLYSRQIYA
LGESAMINLR KASVLISGLG GVGVEIAKNL ILGGVRSVTL HDTKNARWID LSAQYYLTEE
DIGKNRAAAS FERLAELNDS VNCQLVVDQL TEDFVKQFDL VVLTDAPRSE QLKVAGWTRA
HNRCLLVADA RGLYSYIFAD FSNSFRVDDP NGEQIKEFLI EYIDAETGDV TTLENQMHGL
EDGDHVTFSE VKGMTQLNGC SPIKVTVKKP HVFNIGDAAK NLSPYEEGGR VKQVKVPTTV
SHKALADSLA EPEFVYWDFA KFDYPSQLHL LWNALYKFEA KHGRHPNPRS DSDVQLLKAE
LPSGAEVDEK LLKRFSYQAS GNLVTIASVV GGIAAQEAMK AVTHHMTPLK QWLYLDSDDA
LPGDWSEFDN AKLTEEDCKP RGCRYDGQAA VFGWKYQNAL FNQKWFVVGA GAIGCELLKN
LAMMGVACGE GGLIKITDMD QIEISNLNRQ FLFRMNDVGS KKSTVAGRAV KVFNKDVRIQ
ALSERVGADT EHIFNDDFFA ELDGVANALD NIDARRYMDR RCVFYRLPLL ESGTMGTKGN
TQVVYPYLTE SYGSSVDPPE KDIPICTLKN FPNEIQHTIQ WARDLFEGLF TGPAETANQF
LSDERSFLER LEQMNVSQRT QLLSQVKDVL IDSKPSNAED CVKWARLLFQ EHYHDNIAQM
LHSFPPDQVT DQGAKFWSGT KRCPHVLEFD PTQEEHRNFV YAASILRAQI YGIKPILDVD
LVMKIASSVQ PPPFKPRAGV KIAVTEAEAK ENAESEDANA DGVLEQLKVK LARLNTKSIQ
KLNPIDFEKD DDTNHHMEMI TAASNLRAEN YSIQPADRMK TKQIAGRIIP AIATTTATVA
GLVCIELYKM VGSNGLPKTP MTRFKNGFIN LALPFFGFSE PIAAPVKKYN ETSFTLWDRL
EIKGPKTLQE AVDWIQNETG LEVTMLSSGV SLIYSFFMDA KKRAHRMPMD VKAVVEDVSK
REVPRHQRSL VLEVMATDPN TDEDVEVPYI RYVL
//
