ID V9FDD5_PHYPR Unreviewed; 763 AA.
AC V9FDD5;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=E1 ubiquitin-activating enzyme {ECO:0000256|ARBA:ARBA00012990};
DE EC=6.2.1.45 {ECO:0000256|ARBA:ARBA00012990};
GN ORFNames=F443_06763 {ECO:0000313|EMBL:ETI49464.1};
OS Phytophthora parasitica P1569.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=1317065 {ECO:0000313|EMBL:ETI49464.1, ECO:0000313|Proteomes:UP000018721};
RN [1] {ECO:0000313|EMBL:ETI49464.1, ECO:0000313|Proteomes:UP000018721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P1569 {ECO:0000313|EMBL:ETI49464.1,
RC ECO:0000313|Proteomes:UP000018721};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA Machado M., Johnson C.S., Arredondo F., Hong C., Coffey M., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Phytophthora parasitica P1569.";
RL Submitted (NOV-2013) 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. {ECO:0000256|ARBA:ARBA00043952}.
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:ETI49464.1}.
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DR EMBL; ANIZ01001103; ETI49464.1; -; Genomic_DNA.
DR AlphaFoldDB; V9FDD5; -.
DR EnsemblProtists; ETI49464; ETI49464; F443_06763.
DR HOGENOM; CLU_002556_0_1_1; -.
DR OrthoDB; 20494at2759; -.
DR Proteomes; UP000018721; 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 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 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; IPR042449; Ub-E1_IAD_1.
DR InterPro; IPR019572; UBA_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; PF00899; ThiF; 2.
DR Pfam; PF10585; UBA_E1_SCCH; 1.
DR PRINTS; PR01849; UBIQUITINACT.
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:UP000018721};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU000519}.
FT DOMAIN 56..444
FT /note="THIF-type NAD/FAD binding fold"
FT /evidence="ECO:0000259|Pfam:PF00899"
FT DOMAIN 229..304
FT /note="Ubiquitin-activating enzyme E1 FCCH"
FT /evidence="ECO:0000259|Pfam:PF16190"
FT DOMAIN 305..376
FT /note="Ubiquitin-activating enzyme E1 four-helix bundle"
FT /evidence="ECO:0000259|Pfam:PF16191"
FT DOMAIN 467..647
FT /note="THIF-type NAD/FAD binding fold"
FT /evidence="ECO:0000259|Pfam:PF00899"
FT DOMAIN 654..750
FT /note="Ubiquitin-activating enzyme SCCH"
FT /evidence="ECO:0000259|Pfam:PF10585"
FT ACT_SITE 648
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ SEQUENCE 763 AA; 83876 MW; 0766DA9B984B9E17 CRC64;
MLSVCHDASA STMSSHAVTA GDVNETADGV RNLVHVTDNA MDIDQSGAAS IDEGLYSRQL
YVMGREAQLR MGTSNVLIVG LNGLGVEIAK NVILAGVKSV TLHDDTPASK LDLASQFYLT
EGDMGKPRAA VSVKKLAELN PYVPVRCYSG EITEEFLLGF RAVVLVNAPL KEAKRINAIC
HAKSIAFITT EARGVFGSVF CDFGDEFIVS DRDGVEPVSC LISSISNSAP PLVTVNDDTR
HGLETGDLVS FREVAGFPFL NDSKPRKVTV TGPFTFTLDI IDEADKKLFE EGQSFTGGYV
TQVKQPLVTK FKSLENALAA PGEFLINDFA KLGRSELLHV AFQALDAFQE KHQGNYPKPG
CMEDAEEVFT LSCEINKQFA AKKQFSVEGI DDADSKKIIQ ALAAGAVGVI SPMAAFLGGI
VGQEALKACS GKFTPIQQFF YFDAVECLPD AVYAGTPDEF APTGSRYDGQ IVVFGRKLQE
KINSLNMFLV GAGAIGCEML KNWAMMGVAS SKDGTIHITD MDTIEKSNLN RQFLFRSKDV
QQAKSSVAAR AIKEMNPDVN VQSYVSRVGA ESEDQFNDDF FESLSGVCTA LDNVEARLYM
DQRCLFYGLP MFESGTLGTK GNTQIVVPHK TENYGASRDP PEKSIPICTL KNFPNAIEHT
LQWARDWFEG EFFQAPSDVN RYLEGPAFMK ELNEQQNTKI ETLERLKSSL VDDRPMSFED
CISWARFKFE ELFSNQIKQL LYNFPLDQVR PSRLRLSDFV VTT
//
