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Database: UniProt
Entry: A0A0W7VSZ5_9HYPO
LinkDB: A0A0W7VSZ5_9HYPO
Original site: A0A0W7VSZ5_9HYPO 
ID   A0A0W7VSZ5_9HYPO        Unreviewed;       563 AA.
AC   A0A0W7VSZ5;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   22-NOV-2017, entry version 11.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KUF01469.1};
GN   ORFNames=TGAM01_04009 {ECO:0000313|EMBL:KUF01469.1};
OS   Trichoderma gamsii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Hypocreales; Hypocreaceae;
OC   Trichoderma.
OX   NCBI_TaxID=398673 {ECO:0000313|EMBL:KUF01469.1, ECO:0000313|Proteomes:UP000054821};
RN   [1] {ECO:0000313|EMBL:KUF01469.1, ECO:0000313|Proteomes:UP000054821}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T6085 {ECO:0000313|EMBL:KUF01469.1,
RC   ECO:0000313|Proteomes:UP000054821};
RA   Baroncelli R., Vannacci G.;
RT   "The genome sequence of Trichoderma gamsii T6085.";
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|RuleBase:RU004386}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KUF01469.1}.
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DR   EMBL; JPDN01000019; KUF01469.1; -; Genomic_DNA.
DR   RefSeq; XP_018662588.1; XM_018804159.1.
DR   EnsemblFungi; KUF01469; KUF01469; TGAM01_04009.
DR   GeneID; 29984242; -.
DR   Proteomes; UP000054821; 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   InterPro; IPR023367; Peptidase_M42_dom2.
DR   PANTHER; PTHR28570; PTHR28570; 1.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
DR   SUPFAM; SSF101821; SSF101821; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|RuleBase:RU004386};
KW   Complete proteome {ECO:0000313|Proteomes:UP000054821};
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:UP000054821};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   563 AA;  60337 MW;  41F7C6B11FE6D48E CRC64;
     MTRRVPSALS LRQQASAYST TSASSVASSS TASTARIPAP TAPVQSLASS KHFVLADMNG
     RPSVDSRACI KCIAKLSPSE IQQVNWHIAE ENKCQLCAVK DLKPEAFTKP FLDFLRENPT
     VFHAVDYFKS KLNDAGYEEL PARDSWANKI QPGGKYWVTR NGSSIIAFAV GKAYKPGNGV
     GMIAGHIDAL TARLKPVSTK PNTAGYVQLG VAPYAGALNQ TWWDRDLSIG GRVIVSDEKT
     GKTTSKLVEL DWPIAKIPTL APHFGVGMMG QNNPETQAVP VIGLESSNGA DTEILGSAGS
     FVNTQPPKLV KLISKQLGIT SYDSIVNWEL ELFDSQPATV FGLDKELITA GRIDDKLCSW
     SALMGLLHTT ESDDDSYIKL VALFDDEEIG SLLRQGARGN FLPSTVERAV EALNPSSYGP
     GVIGQTFAKS FLLSADVSHA GHPNFIGNYL PEHIPKLNVG LVVCGDSNGH MTTDAVSSAI
     LHRVANLCGA KLQDFQIRND SRSGGTVGPM LSSAMGVRAA DAGLPQLSMH SIRATTGSLD
     PGLGVQFFKG FLDFWEKVDG EWE
//
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