ID A0A261XUQ0_9FUNG Unreviewed; 1014 AA.
AC A0A261XUQ0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-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=BZG36_05058 {ECO:0000313|EMBL:OZJ02072.1};
OS Bifiguratus adelaidae.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Endogonomycetes; Endogonales; Endogonales incertae sedis; Bifiguratus.
OX NCBI_TaxID=1938954 {ECO:0000313|EMBL:OZJ02072.1, ECO:0000313|Proteomes:UP000242875};
RN [1] {ECO:0000313|EMBL:OZJ02072.1, ECO:0000313|Proteomes:UP000242875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AZ0501 {ECO:0000313|EMBL:OZJ02072.1,
RC ECO:0000313|Proteomes:UP000242875};
RX PubMed=28876195; DOI=10.1080/00275514.2017.1364958;
RA Torres-Cruz T.J., Billingsley Tobias T.L., Almatruk M., Hesse C.,
RA Kuske C.R., Desiro A., Benucci G.M., Bonito G., Stajich J.E., Dunlap C.,
RA Arnold A.E., Porras-Alfaro A.;
RT "Bifiguratus adelaidae, gen. et sp. nov., a new member of Mucoromycotina in
RT endophytic and soil-dwelling habitats.";
RL Mycologia 109:363-378(2017).
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:OZJ02072.1}.
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DR EMBL; MVBO01000193; OZJ02072.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A261XUQ0; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000242875; 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:UP000242875};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU000519}.
FT DOMAIN 883..1008
FT /note="Ubiquitin-activating enzyme E1 C-terminal"
FT /evidence="ECO:0000259|SMART:SM00985"
FT ACT_SITE 595
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ SEQUENCE 1014 AA; 113712 MW; 1D56FC68E2F2A98B CRC64;
MAQNDTKMDT DQQIDEGLYS RQLYVLGHEA MKKMSTSNVL IVGLRGLGVE IAKNVVLAGV
KSVTLYDPEP ASISDLSTQY YLHPEDVGKP RASVTCPRLA ELNAYVPVSV LEGDLTHEQV
VKYNILVVTE MSLERQLELN DFCHQNGIKF ISTEVRGLFG RVFNDFGEDF EVLDATGEQP
LTGMVAAIDN DTEGVVTCLD ETRHGLEDGD YVTFTEVQGM TELNGYEPIK VKVLGPYTFS
IGDTSAFAKY QRGGIFTQVK VPQIVQFSSF KDTLAEPEFV LSDFAKFDRP AQLHVGFQAL
HVFATQNDNN LPRSYNEEDA SKVYEITKQL NEKLKEKAEL DEKLIKKLSY QARGDLSPMV
AVFGGLVAQE VLKAASGKFN PIKQYFYFDS LESIPSNYEI SEADAAPMGT RYDGQIAVLG
RKFQEKIANA KQFLVGAGAI GCEMLKNWAM MGLGTGPNGR ITITDMDTIE KSNLNRQFLF
RTKDVGKLKS QCAADAIVAM NPDMKDKIDV HQERVGPDTE NVYDDAFFES LDGVTNALDN
VEARQYVDRR CVYYRKPLLE SGTLGTKGNT QVVIPFLTES YSSSQDPPEK SIPICTLKNF
PNAIEHTIQW ARDLFEGLFV QPAENVNMYL TKPDFVETTL KQTGNQKEAL ESIRNFLVTE
RVMSFEECVR WARFKFEEHF NNNIQQLLFN FPADATTSTG TAFWSGPKRA PAPIVFDPSN
NNHLDFVIFA ANLHAFNYGL QGKTDREWFK QVLSDIMVPE FSPKSGVKID VTEAEAAQPV
SSDADEIDRL ISDLPSPKTL AGVRLNPAEF EKDDDSNFHI DFITAASNLR AINYGIAPAD
RHKTKFIAGK IIPAIATTTS LVTGLVCLEL YKVVDGKQKI EDYKNGFVNL ALPFFGFSEP
IAMPKLKYHD TEFSLWDRFD IKGDPTLQEL MDFFQQEHEL EVTMLSSGVT MLYSFFMPKK
KLEERLPMRM SKLVETVSKK PVPPHVKSLV VEICVNDKEG EDVEVPYVRV QIRD
//
