ID A0A1Y2GV54_9FUNG Unreviewed; 1007 AA.
AC A0A1Y2GV54;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=E1 ubiquitin-activating enzyme {ECO:0000256|ARBA:ARBA00012990};
DE EC=6.2.1.45 {ECO:0000256|ARBA:ARBA00012990};
GN ORFNames=BCR41DRAFT_319616 {ECO:0000313|EMBL:ORZ24962.1};
OS Lobosporangium transversale.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mortierellomycotina;
OC Mortierellomycetes; Mortierellales; Mortierellaceae; Lobosporangium.
OX NCBI_TaxID=64571 {ECO:0000313|EMBL:ORZ24962.1, ECO:0000313|Proteomes:UP000193648};
RN [1] {ECO:0000313|EMBL:ORZ24962.1, ECO:0000313|Proteomes:UP000193648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 3116 {ECO:0000313|EMBL:ORZ24962.1,
RC ECO:0000313|Proteomes:UP000193648};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) 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}.
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:ORZ24962.1}.
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DR EMBL; MCFF01000008; ORZ24962.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2GV54; -.
DR STRING; 64571.A0A1Y2GV54; -.
DR InParanoid; A0A1Y2GV54; -.
DR OrthoDB; 20494at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000193648; 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:UP000193648};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU000519}.
FT DOMAIN 877..1002
FT /note="Ubiquitin-activating enzyme E1 C-terminal"
FT /evidence="ECO:0000259|SMART:SM00985"
FT ACT_SITE 589
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ SEQUENCE 1007 AA; 112797 MW; 845DB7F0ABB26559 CRC64;
MDVEKENVID ESLYSRQLYV LGHEAMKKMG TSNILIVGLK GLGIEIAKNV VLAGVKSVTL
YDPAPVQLSD LSTQFFLTKE DVGQPRDVVS RPRLAELNAY VPVRILEGEL TTDKLSQFKV
VVVTETSLEK QLEINEYTHV HGIHFISAEI HGLFASAFND FGRAFHVVDV TGEEALSGMV
AEISSDKEGI VTCLDETRHG LEDGDHVTFV EVVGMEALNG CAPRKIKVLG PYTFSIGDTS
GLGTYVSGGL FQQVKMPKLV DFASLKDSLQ KPEFLTTDYG KFDRPAQLHI GFQALHSFTT
KNGRQPRPRN VEDAKQVWAL ANEINDKAPE KTELDEKLIQ ELAFQAVGDL SPMVAVIGGT
VAQEVLKACT GKFSPIHQWM YFDSLESLPT SITLTEEACQ PIGSRHDNQI AVFGKEFQER
IENFREFLVG AGAIGCEMLK NWAMMGLGTG PKGMIHVTDM DTIEKSNLNR QFLFRPADVG
KLKSRSAAEA IAKMNPATVG HVQAYEERVG VDSEKVYGDD FFANLDGVTN ALDNLDARKY
MDRRCVYFRK SLLESGTLGT KGNVQVVVPF VTESYSSSQD PPETSIPLCT LKNFPNAIEH
TIQWARDAFE GFFKQPAENV NLYLSQPNYI EGLLKDRGNS TETLKTIQKY LVTNKPLTFE
ECITWARLQF EEQFNNNIQQ LLFNFPKDSV TSSGTLFWSA PKRAPTPLEF NIDDPSHLEF
IIAAANLHAF NYGLKGETNP EVFRQALSTL VVPEFKPKSG VKIQVNENEN MPTEESDQAE
LQKLIDTLPA PSTLAGYRLH PVEFEKDDDT NFHIDFITAT SNLRAANYGI TPADKHRTKF
IAGRIIPAIA TTTAMVTGLV CLELYKLIDN RTKIDDYKNG FVNLALPFFG FSEPIAAPKF
KYHETEFTLW DRFEINEDLT LREFLNYFKE KHELDIAMVS AGVSMLYTSF MPKDKREERL
TMPFSKLVET VSKKSTPPHV KAHTVEVVCY DRNKQDVEVP YVVVRFR
//
