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Database: UniProt
Entry: G0SHL4_CHATD
LinkDB: G0SHL4_CHATD
Original site: G0SHL4_CHATD 
ID   G0SHL4_CHATD            Unreviewed;       484 AA.
AC   G0SHL4;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   07-JUN-2017, entry version 25.
DE   SubName: Full=Aspartyl aminopeptidase-like protein {ECO:0000313|EMBL:EGS17703.1};
GN   ORFNames=CTHT_0070450 {ECO:0000313|EMBL:EGS17703.1};
OS   Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Sordariomycetidae; Sordariales; Chaetomiaceae;
OC   Chaetomium.
OX   NCBI_TaxID=759272 {ECO:0000313|Proteomes:UP000008066};
RN   [1] {ECO:0000313|EMBL:EGS17703.1, ECO:0000313|Proteomes:UP000008066}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 1495 / CBS 144.50 / IMI 039719
RC   {ECO:0000313|Proteomes:UP000008066};
RX   PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA   Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R.,
RA   Devos D.P., Arumugam M., Bork P., Hurt E.;
RT   "Insight into structure and assembly of the nuclear pore complex by
RT   utilizing the genome of a eukaryotic thermophile.";
RL   Cell 146:277-289(2011).
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|RuleBase:RU004386}.
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DR   EMBL; GL988047; EGS17703.1; -; Genomic_DNA.
DR   RefSeq; XP_006697321.1; XM_006697258.1.
DR   MEROPS; M18.002; -.
DR   EnsemblFungi; EGS17703; EGS17703; CTHT_0070450.
DR   GeneID; 18261083; -.
DR   KEGG; cthr:CTHT_0070450; -.
DR   KO; K01267; -.
DR   OrthoDB; EOG092C3JCE; -.
DR   Proteomes; UP000008066; Unassembled WGS sequence.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
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   ECO:0000313|EMBL:EGS17703.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008066};
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:UP000008066};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   484 AA;  52430 MW;  0BD95B9C9AFE34F4 CRC64;
     MAPPQAALEF LDFVNASPTP YHATASAAAL LDAAGFTKIK ERDNWASTVQ PGGKYYLTRN
     GSSVVAFAVG KRWQPGNPIG MIGAHTDSPC LRVKPVSKRS ANGYLQVGVE TYGGGIWHSW
     FDRDLSVAGR VLVREGSEGG EPNFVQKLVK IDKPILRIPH LAIHLHRESN FNPNKEDELL
     PIAGLVEAEL NRPATETADS ASEADYQPLK ALPERHHPRF LELVAEQAGV DVSQIVDFEL
     VLYDTQKACI GGMNDEFIYS ARLDNLNSTF CAIKGLITSV STVPLDNDKS IRLVACFDHE
     EIGSLSAHGA DSNLLPAILR RLSVTPSLSD ASNPPSASST AFEQTLSTSF LLSADMAHAV
     HPNYAAKYER NHTPSINGGP VIKINANQRY ATNSPGIVLL QEVARSRAVP LQLFVVKNDS
     PCGSTIGPML SAKLGVRTLD MGNPQLAMHS IREMGGVKDV EFAVRLFEGF LSRFGELEGR
     ILVD
//
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