ID A0A420P6E1_FUSOX Unreviewed; 1034 AA.
AC A0A420P6E1;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=E1 ubiquitin-activating enzyme {ECO:0000256|ARBA:ARBA00012990};
DE EC=6.2.1.45 {ECO:0000256|ARBA:ARBA00012990};
GN ORFNames=BFJ68_g14739 {ECO:0000313|EMBL:RKK95525.1}, FOXYS1_553
GN {ECO:0000313|EMBL:KAF5268549.1};
OS Fusarium oxysporum (Fusarium vascular wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=5507 {ECO:0000313|EMBL:RKK95525.1, ECO:0000313|Proteomes:UP000285860};
RN [1] {ECO:0000313|EMBL:RKK95525.1, ECO:0000313|Proteomes:UP000285860}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fo_A28 {ECO:0000313|EMBL:RKK95525.1,
RC ECO:0000313|Proteomes:UP000285860};
RX PubMed=30202022; DOI=10.1038/s41598-018-30335-7;
RA Armitage A.D., Taylor A., Sobczyk M.K., Baxter L., Greenfield B.P.,
RA Bates H.J., Wilson F., Jackson A.C., Ott S., Harrison R.J., Clarkson J.P.;
RT "Characterisation of pathogen-specific regions and novel effector
RT candidates in Fusarium oxysporum f. sp. cepae.";
RL Sci. Rep. 8:13530-13530(2018).
RN [2] {ECO:0000313|EMBL:KAF5268549.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 39464 {ECO:0000313|EMBL:KAF5268549.1};
RA Kim H.-S., Busman M., Brown D.W., Divon H., Uhlig S., Proctor R.H.;
RT "Identification and distribution of gene clusters putatively required for
RT synthesis of sphingolipid metabolism inhibitors in phylogenetically diverse
RT species of the filamentous fungus Fusarium.";
RL Submitted (FEB-2020) 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:RKK95525.1}.
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DR EMBL; JAAFOW010000082; KAF5268549.1; -; Genomic_DNA.
DR EMBL; MRCY01000132; RKK95525.1; -; Genomic_DNA.
DR VEuPathDB; FungiDB:FOC1_g10010163; -.
DR VEuPathDB; FungiDB:FOC4_g10011741; -.
DR VEuPathDB; FungiDB:FOIG_08280; -.
DR VEuPathDB; FungiDB:FOMG_12315; -.
DR VEuPathDB; FungiDB:FOXG_08380; -.
DR VEuPathDB; FungiDB:FOXG_08381; -.
DR VEuPathDB; FungiDB:FOZG_06864; -.
DR VEuPathDB; FungiDB:HZS61_012779; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000285860; Unassembled WGS sequence.
DR Proteomes; UP000558688; 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:UP000558688};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU000519}.
FT DOMAIN 901..1029
FT /note="Ubiquitin-activating enzyme E1 C-terminal"
FT /evidence="ECO:0000259|SMART:SM00985"
FT ACT_SITE 608
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ SEQUENCE 1034 AA; 115506 MW; 09A72989EAC9F2D0 CRC64;
MAEQKQPEVD LATRMQVDES VVGHNEIDES LYSRQLYVLG HEAMKRMGAS NVLIVGLKGL
GVEIAKNIAL AGVKSLTLYD PAPVQIADLS SQFFLTPSDV GKPRDEVTVP RVAELNAYTP
VKLHQSPGLD GELSQFDKYQ VVVLTNAPIH QQKAIGDYCH SKGIYVVIAD TYGLFGSVFC
DFGEKFTCID PTGETPLNGI VAGIDEEGLV SALDETRHGL EDGDYVTFSE VEGMEALNGA
EPRKITVKGP YTFSIGDVSG LGQYKRGGMY QQVKMPKIIN FKDFTTALKE PEFLISDFAK
FDRPQQLHLG FQALHAFQLT HKRLPNPMDN DDAIVVLGAA KKFAEQEGLD IQLDEKLLKE
LSYQAQGDLN PMAAYFGGIV AQEVLKAVSG KFQPINQWMY FDSLESLPTS TKRSAELCKP
IGSRYDGQIA VFGTEFQDKI ANLKQFLVGA GAIGCEMLKN WAMIGLGTGP EGKIWVTDMD
SIERSNLNRQ FLFRADDVGQ MKSDRAALAV QRMNPDLEGH MVTLKERVSP ETENVFNEDF
WRNLDGVTNA LDNVEARTYV DRRCVFFQKP LLESGTLGTK GNTQVVLPHL TESYSSSQDP
PEKEFPMCTI RSFPNKIDHT IAWAKEYMFE KLFVKAPQTV NLYLTQPQFI ENSMKQGGNQ
KETLETIRNY LTTERPRTFE DCIAWARQLF ETEFSNKIQQ LLYNFPKDSE TSSGTPFWSG
PKRAPDALKF DPNNPSHFGF IVAAANLHAF NYNIKSPGTD RSIYLRELDN VIVPDFTPSS
NVKIQADDKE PVEPESSNFD DNDEIEKLTA SLPSPSSLSG FQLVPVDFEK DDDSNHHIDF
ITACSNLRAE NYKIEPADRH KTKFIAGKII PAIATTTALV TGLVVLELYK IIDGKDDLEQ
YKNGFINLAL PFFGFSEPIA SPKVEYQGPD GKVTLDKIWD RFEIEDITLK ELLDTFKAKG
LTISMLSSGV SLLYASFFPP SKLKERYDLK LSQLVETISK KPIPSHQKEV IFEIVAEDLA
EEDVEVPYIK VKMA
//
