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Database: UniProt
Entry: U5H6H2_USTV1
LinkDB: U5H6H2_USTV1
Original site: U5H6H2_USTV1 
ID   U5H6H2_USTV1            Unreviewed;       441 AA.
AC   U5H6H2;
DT   11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 1.
DT   24-JAN-2024, entry version 49.
DE   RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN   ORFNames=MVLG_02872 {ECO:0000313|EMBL:KDE06836.1};
OS   Microbotryum lychnidis-dioicae (strain p1A1 Lamole / MvSl-1064) (Anther
OS   smut fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Microbotryales; Microbotryaceae; Microbotryum.
OX   NCBI_TaxID=683840 {ECO:0000313|EMBL:KDE06836.1};
RN   [1] {ECO:0000313|Proteomes:UP000017200}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=p1A1 Lamole {ECO:0000313|Proteomes:UP000017200};
RA   Cuomo C., Perlin M., Young S.K., Zeng Q., Gargeya S., Alvarado L.,
RA   Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M., Goldberg J.,
RA   Griggs A., Gujja S., Heilman E., Heiman D., Howarth C., Mehta T.,
RA   Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA   Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C., Birren B.;
RT   "The genome sequence of Microbotryum violaceum strain p1A1 Lamole.";
RL   Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KDE06836.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=P1A1 Lamole {ECO:0000313|EMBL:KDE06836.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Butler R., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA   Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA   Heilman E., Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P.,
RA   Mehta T., Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M.,
RA   Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S.,
RA   White J., Yandava C., Wortman J., Nusbaum C., Birren B.;
RL   Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:KDE06836.1, ECO:0000313|Proteomes:UP000017200}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=p1A1 Lamole {ECO:0000313|Proteomes:UP000017200}, and P1A1
RC   Lamole {ECO:0000313|EMBL:KDE06836.1};
RX   PubMed=26076695; DOI=10.1186/s12864-015-1660-8;
RA   Perlin M.H., Amselem J., Fontanillas E., Toh S.S., Chen Z., Goldberg J.,
RA   Duplessis S., Henrissat B., Young S., Zeng Q., Aguileta G., Petit E.,
RA   Badouin H., Andrews J., Razeeq D., Gabaldon T., Quesneville H., Giraud T.,
RA   Hood M.E., Schultz D.J., Cuomo C.A.;
RT   "Sex and parasites: genomic and transcriptomic analysis of Microbotryum
RT   lychnidis-dioicae, the biotrophic and plant-castrating anther smut
RT   fungus.";
RL   BMC Genomics 16:461-461(2015).
RN   [4] {ECO:0000313|EnsemblFungi:MVLG_02872T0}
RP   IDENTIFICATION.
RG   EnsemblFungi;
RL   Submitted (JUN-2015) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447}.
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DR   EMBL; AEIJ01000271; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; GL541666; KDE06836.1; -; Genomic_DNA.
DR   AlphaFoldDB; U5H6H2; -.
DR   SMR; U5H6H2; -.
DR   EnsemblFungi; MVLG_02872T0; MVLG_02872T0; MVLG_02872.
DR   HOGENOM; CLU_621426_0_0_1; -.
DR   InParanoid; U5H6H2; -.
DR   OrthoDB; 4946at2759; -.
DR   Proteomes; UP000017200; Unassembled WGS sequence.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd05471; pepsin_like; 1.
DR   Gene3D; 2.40.70.10; Acid Proteases; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR034164; Pepsin-like_dom.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR   PANTHER; PTHR47966:SF75; ENDOPEPTIDASE (CTSD), PUTATIVE (AFU_ORTHOLOGUE AFUA_4G07040)-RELATED; 1.
DR   Pfam; PF00026; Asp; 1.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000017200};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..441
FT                   /note="Peptidase A1 domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5009724455"
FT   DOMAIN          105..422
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   REGION          38..83
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        56..74
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   441 AA;  47605 MW;  02F9CD3802D43CF1 CRC64;
     MFFRASTVFT SLLLVAPALA EAPSPDKRGF KLELHSRASH NPQHAGKAPK SGHAQPYAKR
     LKHGPAHPRR GGAKAHQGHP PFLAATKAGS RQSFANLANV ENIDWSVEVT FGSPPQRVPL
     FLSMGSSLSS VADQNIKSDA KTRYNPSKSL TARNMTKAQV DPNTGVTFIT YKDKISIGGF
     EVSDQTFAVM TSTPNGDPLE RVYDSPVPWA GALALGRTSK GTPSLSFLEN LIRSKVIDNA
     VCGISLTVEG GALFFGGIDS HSFKGKIVWS PVETHYMEGF WTIKTGGWGW KGKVATGTAG
     LLQFAPENTY TYISAILGNK LFAGIKHHVD SKTQRYLLPC NSNASDTIGF FIHNRMFPVP
     IPDLILFPSD SDPTMCHTAL LQVTNKHILD DYTVVMGALH MRSFYTILSY EKEHGGPAIG
     LAESSIKVMG GDPGPGGHSE K
//
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