ID B2VVM6_PYRTR Unreviewed; 412 AA.
AC B2VVM6;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Ubiquitin-like 1-activating enzyme E1A {ECO:0000256|ARBA:ARBA00044354};
GN ORFNames=PTRG_01238 {ECO:0000313|EMBL:EDU40676.1};
OS Pyrenophora tritici-repentis (strain Pt-1C-BFP) (Wheat tan spot fungus)
OS (Drechslera tritici-repentis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=426418 {ECO:0000313|EMBL:EDU40676.1, ECO:0000313|Proteomes:UP000001471};
RN [1] {ECO:0000313|Proteomes:UP000001471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pt-1C-BFP {ECO:0000313|Proteomes:UP000001471};
RX PubMed=23316438; DOI=10.1534/g3.112.004044;
RA Manning V.A., Pandelova I., Dhillon B., Wilhelm L.J., Goodwin S.B.,
RA Berlin A.M., Figueroa M., Freitag M., Hane J.K., Henrissat B., Holman W.H.,
RA Kodira C.D., Martin J., Oliver R.P., Robbertse B., Schackwitz W.,
RA Schwartz D.C., Spatafora J.W., Turgeon B.G., Yandava C., Young S., Zhou S.,
RA Zeng Q., Grigoriev I.V., Ma L.-J., Ciuffetti L.M.;
RT "Comparative genomics of a plant-pathogenic fungus, Pyrenophora tritici-
RT repentis, reveals transduplication and the impact of repeat elements on
RT pathogenicity and population divergence.";
RL G3 (Bethesda) 3:41-63(2013).
CC -!- PATHWAY: Protein modification; protein sumoylation.
CC {ECO:0000256|ARBA:ARBA00004718}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family.
CC {ECO:0000256|ARBA:ARBA00005673}.
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DR EMBL; DS231615; EDU40676.1; -; Genomic_DNA.
DR RefSeq; XP_001931571.1; XM_001931536.1.
DR AlphaFoldDB; B2VVM6; -.
DR STRING; 426418.B2VVM6; -.
DR EnsemblFungi; EDU40676; EDU40676; PTRG_01238.
DR GeneID; 6338689; -.
DR eggNOG; KOG2014; Eukaryota.
DR HOGENOM; CLU_002556_4_1_1; -.
DR InParanoid; B2VVM6; -.
DR OMA; EFFGQFD; -.
DR OrthoDB; 5483037at2759; -.
DR Proteomes; UP000001471; Unassembled WGS sequence.
DR GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR InterPro; IPR000011; UBQ/SUMO-activ_enz_E1-like.
DR PANTHER; PTHR10953:SF162; SUMO-ACTIVATING ENZYME SUBUNIT 1; 1.
DR PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 1.
DR Pfam; PF00899; ThiF; 1.
DR PRINTS; PR01849; UBIQUITINACT.
DR SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 1.
PE 3: Inferred from homology;
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000001471};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 53..380
FT /note="THIF-type NAD/FAD binding fold"
FT /evidence="ECO:0000259|Pfam:PF00899"
SQ SEQUENCE 412 AA; 44918 MW; FB4B46C52D6D793A CRC64;
MADMTEPSAI PPPAANGALP AEDAAGQTVA AIAEADKISA GKRGSVANEI ALYDRQIRLW
GVQAQQKIRT ANILLVCFKA LANEIAKNLV LAGIGSITLA DHQVVTEDDL GAQFFLTDAD
VGKNRAEAAA PEVRKLNPRV TVKTLTTDIR NVQDPNFYAA YDIIITTDMD FMSTTAVNAG
ARIAKKPFYA GASHGMYGYI FADLVEHHFV IEREKSNRDT QVGPESTTRS VKGVQVKKEN
GKVVELVSKR EVYSPLMLVK DSPLPAEIAN NARRLKRVHP LLTCVRALWE YQRNGHGIYP
SHTQQELTLF TTIANVKHQE LLLPTDSLKA DVLRNFLQNL GSELAPVTAF LGGQLAQDVI
NVLGQREQPI QNLMLFDGED SAGPVYTLHP IFPDTPLPII QSVPVEASIT VL
//
