ID A0A329RTD6_9STRA Unreviewed; 1124 AA.
AC A0A329RTD6;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Ubiquitin-like modifier-activating enzyme 1 {ECO:0000313|EMBL:RAW27861.1};
GN ORFNames=PC110_g15739 {ECO:0000313|EMBL:RAW27861.1}, PC117_g13956
GN {ECO:0000313|EMBL:KAG2929621.1};
OS Phytophthora cactorum.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=29920 {ECO:0000313|EMBL:RAW27861.1, ECO:0000313|Proteomes:UP000251314};
RN [1] {ECO:0000313|EMBL:RAW27861.1, ECO:0000313|Proteomes:UP000251314}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=10300 {ECO:0000313|EMBL:RAW27861.1,
RC ECO:0000313|Proteomes:UP000251314};
RA Armitage A.D., Lysoe E., Nellist C.F., Harrison R.J., Brurberg M.B.;
RT "Draft genome of the strawberry crown rot pathogen Phytophthora cactorum.";
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KAG2929621.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=4040 {ECO:0000313|EMBL:KAG2929621.1};
RA Armitage A.D., Nellist C.F., Bates H., Vickerstaff R.J., Harrison R.J.;
RT "Effector identification in a new, highly contiguous assembly of the
RT strawberry crown rot pathogen Phytophthora cactorum.";
RL Submitted (OCT-2018) 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:RAW27861.1}.
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DR EMBL; RCMK01000422; KAG2929621.1; -; Genomic_DNA.
DR EMBL; MJFZ01000531; RAW27861.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A329RTD6; -.
DR STRING; 29920.A0A329RTD6; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000251314; Unassembled WGS sequence.
DR Proteomes; UP000736787; 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:UP000251314};
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; 126208 MW; 2BF43ABB1361F359 CRC64;
METTQQLEKD AGFMDKYSRQ IGAFGLETMA KLVKLKVLIV GLQGVGIECA KNLILAGPGS
ITLHDDGIAE IKDLGTNFFL TEQDLGQPRA SSVSHKLAEL NKMVSVAVHK GPLTEDVVAK
HNVVVFSHTS RKELVRWNHF CRQQSPQIGF IMCDIRGAFG YAFTDFGDEF KGFDATGEAP
ITRIITDITN DKDGVLSILG PDEDGKMHEM PDSDHDGWIE ISDVQGMKLK SDPDQSINTL
GPRRIKFANK KVFRNGKQTE VFDAYRLKIG DTSEFTPYEG GGVFTQHKKP FTVNFKSLEE
SLVSPVPEGE FGLMFTDGAK FGRAEQLHVI MWSLMEFEER HGHYPEPHND EDADEVVAIA
KEGIQHLSDF TREGAHKQEV MKLEELDEKI VRQAALYSAV ELHPLAAFYG GVIAQEVVKL
TGKFTPLKQW LHLDAFEVLP DERPTDAKPI GSRYDHMITT FGLSFQKQLG NVRTFLVGCG
ALGCEYLKNF AMIGIACGDK GLVTVTDNDR IEVSNLNRQF LFREHNVGQP KSVAATAAVH
QMNSDLKVKT LEQLVAPHTE NVFNDEFWTD LDVVTNALDN VKARLYVDSK CVFHKLPLLE
SGTLGTKCNV QVVIPYKTQS YADGPKDAEG DGIPMCTLRN FPSLIEHCIE WSRAQFEDLF
VVPSTEAKKF VEDRAAYLDQ VKKATLENPN PKLVSAAIVQ ELERLRSLRA TLQTAKEITF
EKCVTLAFEL MTSQFRDRIL QLIHNFPEDH LTNSGEKFWS GAKRFPQAVD KFDPENPLHL
NFVRATANIL AVCYGIQSPP EQNLIAADSE WRDPSTYEEL GSKYVPPTWK PSNEKIAADS
DEIKRLEQEK IKNSNDSDKN ELVELLYELE TFDLSGLSFE PADFEKDQDM NFHIDFIYAA
SNLRAFNYRI RDASRHKCKM IAGKIIPAIA TTTASVTGLA MLEMLKLMQR KDLEAFKDSS
NSLGLNMYLM QEPAAPARAK DEYDVVEMSE VKCKPPGFTK WDSTLIEISS DSTLEDFLAQ
FKEKTELNCD LLFHSVAEMG NTSAAEKDLR YRTVSGLMLY DRNAFGKALK ELYADQMTKP
LRAFVESRYE GLVDCGRKYI ELQTSCSDDD GNAFKVPTVI CKFS
//
