ID A0A5D6Y0E3_9STRA Unreviewed; 1072 AA.
AC A0A5D6Y0E3;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=E1 ubiquitin-activating enzyme {ECO:0000256|ARBA:ARBA00012990};
DE EC=6.2.1.45 {ECO:0000256|ARBA:ARBA00012990};
GN ORFNames=PybrP1_003692 {ECO:0000313|EMBL:TYZ63723.1};
OS [Pythium] brassicae (nom. inval.).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Pythiales; Pythiaceae;
OC Globisporangium.
OX NCBI_TaxID=1485010 {ECO:0000313|EMBL:TYZ63723.1, ECO:0000313|Proteomes:UP000323770};
RN [1] {ECO:0000313|EMBL:TYZ63723.1, ECO:0000313|Proteomes:UP000323770}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P1 {ECO:0000313|EMBL:TYZ63723.1,
RC ECO:0000313|Proteomes:UP000323770};
RA Kaundal R., Smith E.A., Mohammadi M., Stanghellini M.;
RT "Complete genome sequence of Pythium brassicum P1, an oomycete root
RT pathogen: insights into its host specificity to brassicaceae.";
RL Submitted (AUG-2019) 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:TYZ63723.1}.
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DR EMBL; SMMQ01002345; TYZ63723.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5D6Y0E3; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000323770; 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:UP000323770};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU000519}.
FT DOMAIN 936..1066
FT /note="Ubiquitin-activating enzyme E1 C-terminal"
FT /evidence="ECO:0000259|SMART:SM00985"
FT ACT_SITE 645
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ SEQUENCE 1072 AA; 116480 MW; 8F934265FFDC3765 CRC64;
MSAKPVTAGD VSATADGVRN IVHVDDGVPA AAAAAAAAMD VDASAIDEGL YSRQLYVMGH
EAQLRMGAAN VLVVGLDGLG VEIAKNIVLA GVKSVTLHDD APASLLDLSA QFYLSERDVG
APRAQVSAKK LAELNPYVHV HAHSGDISEA FLQQFRVVVV VNAALSEAKR INALCHAHGI
AFVSTEARGV FGAVFCDFGD AFVVSDRDGE QPVSCMVASI ANSTPPLVTV SDDARHQLET
GDVVTFREIS GFPFLNECAP RRVTVTGPFT FTLDPLDDAD AAQFARGAPS VGGYVTQVKQ
PLTVAFQRLE SALARPGEFL VSDFAKLNRS ELLHVAFQAL DAYRAAHDGR FPTPGSLADG
DEVHALAVAL NQQAANVGGF AVPSDLLESA DAKKVVRALA SGASGVISPM AAFLGGIVGQ
EALKACSGKF TPIQQFFYFD ALECLPDAVF AGDTSEFAPV GSRYDGQLVV FGKMLQATVQ
NLSLFLVGAG AIGCEMLKNW AMMGVATGAN SVIHVTDMDT IEKSNLNRQF LFRSKDVQQP
KSTVAGRAIK EMNPDVNVQS YVARVGSESE TQFNDEFFES LAGVCTALDN VEARLYMDQR
CLFYGLPMFE SGTLGTKGNT QIVVPHKTEN YGASRDPPEK SIPICTLKNF PNAIEHTLQW
ARDWFEGEFF QAPSDVNQYL AGPDFVKQLN DQQNTKLETL ERLQQSLVDQ RPSSFEDCVA
WARFKFEDLF SNQIKQLLHN FPLDQVTTTG TPFWSGPKRP PTPVAFDARD PVHLDFIVAV
AASRAKTYGL PNHADRARIA KTLATIHVPE FAPREGVKIA ATDAEMKEEA ARAPRLDNPD
AQAEHLLAAL PTAASLSDFR MAPIEFDKDD DAHMEVIVAT SNLRARSYKI PEADMHKSRF
IAGKIIPAIA TTTALVTGLV CFEFLKAFQG KPLDHYKNGF VNLALPLFAF SEPVAPKTTT
TMLRGEEYKW TAWDRLDLPA GDLTLKELLA HFEKEYEAEI SMLSYGVTIL YAMYSQKSRA
KERLAMTIPE LVETVTKKPL DASLKYLILE VCAMDADGED IELPYVRYHT RQ
//
