ID A0A0L0V1U2_9BASI Unreviewed; 676 AA.
AC A0A0L0V1U2;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Ubiquitin-activating enzyme E1-like {ECO:0008006|Google:ProtNLM};
GN ORFNames=PSTG_13363 {ECO:0000313|EMBL:KNE93250.1};
OS Puccinia striiformis f. sp. tritici PST-78.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=1165861 {ECO:0000313|EMBL:KNE93250.1, ECO:0000313|Proteomes:UP000054564};
RN [1] {ECO:0000313|Proteomes:UP000054564}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race PST-78 {ECO:0000313|Proteomes:UP000054564};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Hulbert S., Chen X., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Larimer J., McCowan C., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Puccinia striiformis f. sp. tritici PST-78.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Protein modification; protein sumoylation.
CC {ECO:0000256|ARBA:ARBA00004718}.
CC -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family.
CC {ECO:0000256|ARBA:ARBA00005673}.
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:KNE93250.1}.
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DR EMBL; AJIL01000141; KNE93250.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L0V1U2; -.
DR STRING; 1165861.A0A0L0V1U2; -.
DR OrthoDB; 20494at2759; -.
DR UniPathway; UPA00886; -.
DR Proteomes; UP000054564; Unassembled WGS sequence.
DR GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR GO; GO:0016925; P:protein sumoylation; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.10.10.520; Ubiquitin activating enzymes (Uba3). Chain: B, domain 2; 1.
DR Gene3D; 3.50.50.80; Ubiquitin-activating enzyme E1, inactive adenylation domain, subdomain 1; 1.
DR Gene3D; 3.10.290.20; Ubiquitin-like 2 activating enzyme e1b. Chain: B, domain 3; 1.
DR InterPro; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR InterPro; IPR042449; Ub-E1_IAD_1.
DR InterPro; IPR023318; Ub_act_enz_dom_a_sf.
DR InterPro; IPR019572; UBA_E1_SCCH.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR InterPro; IPR033127; UBQ-activ_enz_E1_Cys_AS.
DR PANTHER; PTHR10953:SF5; SUMO-ACTIVATING ENZYME SUBUNIT 2; 1.
DR PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 1.
DR Pfam; PF00899; ThiF; 1.
DR Pfam; PF10585; UBA_E1_SCCH; 1.
DR SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 1.
DR PROSITE; PS00865; UBIQUITIN_ACTIVAT_2; 1.
PE 3: Inferred from homology;
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Reference proteome {ECO:0000313|Proteomes:UP000054564};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 17..423
FT /note="THIF-type NAD/FAD binding fold"
FT /evidence="ECO:0000259|Pfam:PF00899"
FT DOMAIN 323..386
FT /note="Ubiquitin-activating enzyme SCCH"
FT /evidence="ECO:0000259|Pfam:PF10585"
FT REGION 579..663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..623
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 635..659
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 184
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ SEQUENCE 676 AA; 75409 MW; F3495B78828C77C6 CRC64;
MAQTSTSPSR YSHLETLFGP RTRDRIRNCS VLVIGAGGIG CELLKNLVCT GFGNITIVDL
DTVDTSNLNR QFLFQKKHVK RPKAIVARET ASAFNPDVTI HALHANVMDP QFDQAYFKSF
DLVLNALDNL AARRHVNKMC VMTKVPLIES GTAGYNGQVQ PIRSGKMECY DCQPKPLPKT
FPVCTIRSTP STAIHCIVWA KDYLFPQLFG PEDENEGADL DEAVKNGESV KEVETLKEEV
KRMKEIRAQL DSPEMSKIVF EKLFQEDIKR LLMMEDMWEH RRAPTPLNYD QLASQELNQP
ENGHQNQQAV PSAGGLKDQQ TLTLKNSFDL FCSSLLALGK RIQSDAAHEP LRWDKDDDDA
LDFVTAASNL RATIFDISQK TRFDVKEMAG NIIPAIATTN SAVSALIVFQ AIKILSQSKE
QDKTTQKDIE ANEGGQPDHL PRIAACRPWY SKTAERMIVA GSIDPPNPHC EVCQVVYSTV
HVHPDCTLKE FIKQVLKGKL YDDEDEESIT IQEGDRLLYD PDYTDNSIKT FKELNLIDGQ
VERVLRITDE AEQYVPLMCT ISKSSAPTTA DKILVEDLPD ILPHRPAPKP VSKPASDLGD
NSDIEQVDAQ NGSNGTKKRR TGPAVSGSNK DDDIIVVIDQ LDDDHSNPRP TKKIKLDQHQ
SNHPVSNDLV EIVEIS
//
