ID V9ECX3_PHYPR Unreviewed; 1124 AA.
AC V9ECX3;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Ubiquitin-activating enzyme E1 C-terminal domain-containing protein {ECO:0000259|SMART:SM00985};
GN ORFNames=F443_16994 {ECO:0000313|EMBL:ETI36974.1};
OS Phytophthora parasitica P1569.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=1317065 {ECO:0000313|EMBL:ETI36974.1, ECO:0000313|Proteomes:UP000018721};
RN [1] {ECO:0000313|EMBL:ETI36974.1, ECO:0000313|Proteomes:UP000018721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P1569 {ECO:0000313|EMBL:ETI36974.1,
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 -!- 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:ETI36974.1}.
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DR EMBL; ANIZ01002986; ETI36974.1; -; Genomic_DNA.
DR AlphaFoldDB; V9ECX3; -.
DR EnsemblProtists; ETI36974; ETI36974; F443_16994.
DR eggNOG; KOG2012; Eukaryota.
DR HOGENOM; CLU_002556_0_0_1; -.
DR OrthoDB; 168734at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000018721; 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 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 InterPro; IPR032420; E1_4HB.
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; 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:SF250; ENZYME E1, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 1.
DR Pfam; PF16191; E1_4HB; 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:UP000018721};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU000519}.
FT DOMAIN 956..1119
FT /note="Ubiquitin-activating enzyme E1 C-terminal"
FT /evidence="ECO:0000259|SMART:SM00985"
FT ACT_SITE 636
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ SEQUENCE 1124 AA; 126102 MW; E1A2B50B9D5BCF93 CRC64;
METTQQLEKD AGFMDKYSRQ IGAFGLETMA KLVKLKVLIV GLQGVGIECA KNLILAGPGA
ITLHDDGIAE IKDLGTNFFL TEQDVGQPRA SAVSHKLAEL NKMVSVAVHK GPLTEEVVAK
HNVVVFSHTS RKELVRWNHF CRQQSPQIGF ITCDIRGAFG YAFTDFGDEF KGFDATGEAP
ITRIITDITN DKDGVLSILG PDEDGKMHEM PDSDHDGWIE ISDVQGMKLK SNSNQSINTM
GPRRIKFANK KVFRNGKQTE VFDAYRLKIG DTSEFTPYEG GGVFTQHKKP FTVKFKSFEE
SLVSPVPEGE FGLMFTDGAK FGRAEQLHVI MWSLMEFEER HGHYPEPHND QDADEVVAIA
KEGIQHLSAF TREGANKQEV MKLEELDEKT AHQAALYAAV ELHPLAAFYG GVVAQEVVKF
TGKFTPLKQW LHLDAFEVLP DERPTDAKPI GSRYDHIITA FGLSFQKQLG NVRTFLVGCG
ALGCEYLKNF AMVGLACGDK GLVTVTDNDR IEVSNLNRQF LFREHNVGQP KSVAATAAVH
QMNADLKVKT LEQLVAPHTE NVFNDEFWAD LDVVTNALDN VKARLYVDSK CVFHKLPLLE
SGTLGTKCNV QVVIPYKTQS YADGPKDAEG DGIPMCTLRN FPSLIEHCIE WSRAQFEDLF
VVPAAEAKKF VEDRAAYLDQ VKKATLENPN PKLVAAAIVQ ELERLRSLRA TLQTAKDITF
EKCVTLAFEL MTSRFRDRIL QLIHNFPEDH LTNSGEKFWS GAKRFPQAVE KFDPQNPLHL
NFVRATANIL AVCYGIQPPP EQKLVSADSE WRDPSTYEEL GNKYVLPTWQ PSNEKIAADS
DEIKRLEQEK IKNSNDSDKN ELVELLHELE TFDLSGLSFE PADFEKDQDM NFHIDFIYAA
SNLRAFNYRI RDASRHKCKM IAGKIIPAIA TTTASVTGLA MLEMLKLMQR KELEAFKDSS
NSLGLNMYLM QEPAAPARAK DEYDVVEMSE VKCKPPGFTK WDSTLIELSS DSTLEDFLAQ
FKEKTELNCD LLFHRVAEMG NTSAAEKDPR YRTVSGLMLY DRNAFGKALK ELYADQMTKP
LRAFVESRYE GLVDCSRKYI ELQTSCSDDD GNVFKVPTVI CKFS
//
