ID A0A0C4DMU4_MAGP6 Unreviewed; 1037 AA.
AC A0A0C4DMU4;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Ubiquitin-like 1-activating enzyme E1A {ECO:0000256|ARBA:ARBA00044354};
GN ORFNames=MAPG_01107 {ECO:0000313|EMBL:KLU82028.1};
OS Magnaporthiopsis poae (strain ATCC 64411 / 73-15) (Kentucky bluegrass
OS fungus) (Magnaporthe poae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Magnaporthaceae; Magnaporthiopsis.
OX NCBI_TaxID=644358 {ECO:0000313|EnsemblFungi:MAPG_01107T0, ECO:0000313|Proteomes:UP000011715};
RN [1] {ECO:0000313|EMBL:KLU82028.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 64411 {ECO:0000313|EMBL:KLU82028.1};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Genome Sequencing Center for Infectious Disease;
RA Ma L.-J., Dead R., Young S., Zeng Q., Koehrsen M., Alvarado L., Berlin A.,
RA Chapman S.B., Chen Z., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D., Hepburn T., Howarth C., Jen D.,
RA Larson L., Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C.,
RA Haas B., Nusbaum C., Birren B.;
RT "The Genome Sequence of Magnaporthe poae strain ATCC 64411.";
RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000011715}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 64411 / 73-15 {ECO:0000313|Proteomes:UP000011715};
RA Ma L.-J., Dead R., Young S., Zeng Q., Koehrsen M., Alvarado L., Berlin A.,
RA Chapman S.B., Chen Z., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D., Hepburn T., Howarth C., Jen D.,
RA Larson L., Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C.,
RA Haas B., Nusbaum C., Birren B.;
RT "The genome sequence of Magnaporthe poae strain ATCC 64411.";
RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KLU82028.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 64411 {ECO:0000313|EMBL:KLU82028.1};
RA Ma L.-J., Dead R., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A.,
RA Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A.,
RA MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C., Neiman D.,
RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA Stolte C., Sykes S., Yandava C., Wortman J., Nusbaum C., Birren B.;
RT "Annotation of Magnaporthe poae ATCC 64411.";
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EnsemblFungi:MAPG_01107T0}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 64411 / 73-15 {ECO:0000313|EnsemblFungi:MAPG_01107T0};
RX PubMed=26416668; DOI=10.1534/g3.115.020057;
RA Okagaki L.H., Nunes C.C., Sailsbery J., Clay B., Brown D., John T., Oh Y.,
RA Young N., Fitzgerald M., Haas B.J., Zeng Q., Young S., Adiconis X., Fan L.,
RA Levin J.Z., Mitchell T.K., Okubara P.A., Farman M.L., Kohn L.M., Birren B.,
RA Ma L.-J., Dean R.A.;
RT "Genome sequences of three phytopathogenic species of the Magnaporthaceae
RT family of fungi.";
RL G3 (Bethesda) 5:2539-2545(2015).
RN [5] {ECO:0000313|EnsemblFungi:MAPG_01107T0}
RP IDENTIFICATION.
RC STRAIN=ATCC 64411 {ECO:0000313|EnsemblFungi:MAPG_01107T0};
RG EnsemblFungi;
RL Submitted (JUN-2015) to UniProtKB.
CC -!- PATHWAY: Protein modification; protein sumoylation.
CC {ECO:0000256|ARBA:ARBA00004718}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family.
CC {ECO:0000256|ARBA:ARBA00005673, ECO:0000256|RuleBase:RU000519}.
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DR EMBL; ADBL01000257; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; GL876966; KLU82028.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C4DMU4; -.
DR STRING; 644358.A0A0C4DMU4; -.
DR EnsemblFungi; MAPG_01107T0; MAPG_01107T0; MAPG_01107.
DR VEuPathDB; FungiDB:MAPG_01107; -.
DR eggNOG; KOG2012; Eukaryota.
DR OMA; GANLHAF; -.
DR OrthoDB; 20494at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000011715; 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 CDD; cd01491; Ube1_repeat1; 1.
DR CDD; cd01490; Ube1_repeat2; 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 Gene3D; 1.10.10.2660; Ubiquitin-activating enzyme E1, SCCH domain; 1.
DR Gene3D; 3.10.290.60; Ubiquitin-activating enzyme E1, UFD domain; 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; IPR018965; Ub-activating_enz_E1_C.
DR InterPro; IPR042449; Ub-E1_IAD_1.
DR InterPro; IPR038252; UBA_E1_C_sf.
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:SF162; SUMO-ACTIVATING ENZYME SUBUNIT 1; 1.
DR PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 1.
DR Pfam; PF16191; E1_4HB; 1.
DR Pfam; PF16190; E1_FCCH; 1.
DR Pfam; PF09358; E1_UFD; 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 Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000011715};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU000519}.
FT DOMAIN 904..1032
FT /note="Ubiquitin-activating enzyme E1 C-terminal"
FT /evidence="ECO:0000259|SMART:SM00985"
FT ACT_SITE 611
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ SEQUENCE 1037 AA; 115068 MW; BE84E940B47C7250 CRC64;
MADQRLPEVD LVTRMQVDDS VVNVVGGGEI DESLYSRQLY VLGHEAMRRM GASNVLIAGL
KGIGVEIAKN IALAGVKSLS LHDPAPVAIA DLSSQFFLRP EDVGKPRDQV TAPRVAELNA
YTPVTVHASS GLVDDLSQLD KYQVVVLTNA PLVVQKAVGD YCHSKGIYFV AADTFGLFGS
LFCDFGKEFT VIDATGENPL NGMVNGIDEE GVVTTPDDAR HGLEDGDYVT FTEVQGMEAL
NGCQPRKITV KGPYTFSIGD VSGLGTYERG GLYQQVKMPK LLDFKGFTDA LADPEFVITD
YAKFDRPQQL HVGFQALHAF AQTHSRLPRP FSTEDATVIV NSAKEFAKAA GLEVEFDEKL
LTELSYQATG DLNPMAAFFG GVTAQEVLKA VSGKFHPVKQ WMYFDSLESL PTNIPRSEEL
CRPLNCRYDG QIAVFGKQYQ DKVANMKQFL VGAGAIGCEM LKNWAMIGLG TGPEGKIVIT
DMDSIEKSNL NRQFLFRPKD VGQMKSDCAA KAAELMNPEL SGHIVCLKDR VSPETEHIFN
EEFWGGLDGV TNALDNVEAR TYVDRRCVFF HKPLLESGTL GTKGNTQVVL PKLTESYSSS
QDPPEQSFPM CTLRSFPNKI EHTIAWAREL FDSSFIRPAE TVNLYLSQPG YLESTLKQGG
NEKQTLETLR DYLTKDRARS FEDCVIWGRN LFEKNYNNAI RQLLHNFPKD SVSSTGTPFW
SGPKRAPDPL TFDPEDASHF GFVVAAASLH AFNYNINVKD KTKQDFLDVL SNMIVEEFEP
DPDVKIQADD KEPDPNAGAS AFDDTNELEQ IIKELPAPKD MAGFKLTPVE FEKDDDTNHH
IDFITAASNL RAANYKIEQA DRHKTKFIAG KIIPAIATTT ALVTGLVVLE LYKIIDGKDD
IEQYKNGFVN LALPFFGFSE PIASPKVEYK GPNGKVTLDK IWDRFELEDV TLRELMDDFE
KRGLTITMLS SGVSLLYAAF FPAAKLKERY PMKLSQLVEF ITKKPIPEHQ KEVIFEVVTE
DADGEDVEVP YLKVKVR
//
