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Database: UniProt
Entry: U1GLU0_ENDPU
LinkDB: U1GLU0_ENDPU
Original site: U1GLU0_ENDPU 
ID   U1GLU0_ENDPU            Unreviewed;       561 AA.
AC   U1GLU0;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   07-JUN-2017, entry version 13.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ERF73183.1};
GN   ORFNames=EPUS_03024 {ECO:0000313|EMBL:ERF73183.1};
OS   Endocarpon pusillum (strain Z07020 / HMAS-L-300199) (Lichen-forming
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Verrucariales; Verrucariaceae; Endocarpon.
OX   NCBI_TaxID=1263415 {ECO:0000313|EMBL:ERF73183.1, ECO:0000313|Proteomes:UP000019373};
RN   [1] {ECO:0000313|Proteomes:UP000019373}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Z07020 / HMAS-L-300199 {ECO:0000313|Proteomes:UP000019373};
RX   PubMed=24438332; DOI=10.1186/1471-2164-15-34;
RA   Wang Y.-Y., Liu B., Zhang X.-Y., Zhou Q.-M., Zhang T., Li H.,
RA   Yu Y.-F., Zhang X.-L., Hao X.-Y., Wang M., Wang L., Wei J.-C.;
RT   "Genome characteristics reveal the impact of lichenization on lichen-
RT   forming fungus Endocarpon pusillum Hedwig (Verrucariales,
RT   Ascomycota).";
RL   BMC Genomics 15:34-34(2014).
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|RuleBase:RU004386}.
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DR   EMBL; KE720972; ERF73183.1; -; Genomic_DNA.
DR   RefSeq; XP_007801157.1; XM_007802966.1.
DR   MEROPS; M18.001; -.
DR   EnsemblFungi; ERF73183; ERF73183; EPUS_03024.
DR   GeneID; 19238072; -.
DR   Proteomes; UP000019373; Unassembled WGS sequence.
DR   GO; GO:0000324; C:fungal-type vacuole; IEA:EnsemblFungi.
DR   GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR   GO; GO:0070006; F:metalloaminopeptidase activity; IEA:EnsemblFungi.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR001948; Peptidase_M18.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|RuleBase:RU004386};
KW   Complete proteome {ECO:0000313|Proteomes:UP000019373};
KW   Hydrolase {ECO:0000256|RuleBase:RU004386};
KW   Metal-binding {ECO:0000256|RuleBase:RU004386};
KW   Metalloprotease {ECO:0000256|RuleBase:RU004386};
KW   Protease {ECO:0000256|RuleBase:RU004386};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019373};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   561 AA;  60458 MW;  781347E12308227C CRC64;
     MVQKTSSGFR ASIDEPEPLS PSENFRRPTL QSLSMRSTQI ASATVTPIPD RASSTIMSRD
     ASPISSSQSS NRHVPSPIAA ETYTEPYLKF MSQNPTVFHA VDAFSTQLAS SGFEHLSERD
     RWTTKLRPGG KYYTTRNGSA LIAFAIGKEY KLGNGVGIVA GHVDALTAKL KPIPKLQTKA
     GYVQLGVAPY AGGLNDTWWD RDLGIGGRVL VKDSKTGKIE KKLVKLDWPI ARIPTLAPHF
     GMAAVGPFNK ETQMVPIIGL DNSDLSGVGN HPPHDSKIKA GTFAATQPER LVRAIASEMS
     IDDYSSIINW ELELYDTQPA QLGGLDKEFI FAGRVDDKLC CYSAIEALLA TSSDTSPGIV
     KMVGCFDDEE IGSLLRQGAK SNFMGSIIDR ICEGMLYYQS NEASNRGGGP QFTPQLGPNL
     INQTLANSFL VSSDVIHAVN PNFLGASLEN HAPRLNVGVA ISADSNGHMT TDAVSTALLQ
     RIAENCGSVL QVFQIRNDVR SGGTIGPMTS SQLGIRAVDA GIPQLSMHSI RATTGSLDPG
     LGVRLFKGFF DWFEVVDSEF R
//
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