GenomeNet

Database: UniProt
Entry: A0A0N8H7T0_9HYPO
LinkDB: A0A0N8H7T0_9HYPO
Original site: A0A0N8H7T0_9HYPO 
ID   A0A0N8H7T0_9HYPO        Unreviewed;       496 AA.
AC   A0A0N8H7T0;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   10-MAY-2017, entry version 9.
DE   SubName: Full=Aspartyl aminopeptidase {ECO:0000313|EMBL:KPM42628.1};
GN   ORFNames=AK830_g3944 {ECO:0000313|EMBL:KPM42628.1};
OS   Neonectria ditissima.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Hypocreales; Nectriaceae;
OC   Neonectria.
OX   NCBI_TaxID=78410 {ECO:0000313|EMBL:KPM42628.1, ECO:0000313|Proteomes:UP000050424};
RN   [1] {ECO:0000313|EMBL:KPM42628.1, ECO:0000313|Proteomes:UP000050424}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R09/05 {ECO:0000313|EMBL:KPM42628.1,
RC   ECO:0000313|Proteomes:UP000050424};
RA   Gomez-Cortecero A., Harrison R.J., Armitage A.D.;
RT   "Draft genome of a European isolate of the apple canker pathogen
RT   Neonectria ditissima.";
RL   Submitted (SEP-2015) 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:KPM42628.1}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; LKCW01000045; KPM42628.1; -; Genomic_DNA.
DR   EnsemblFungi; KPM42628; KPM42628; AK830_g3944.
DR   Proteomes; UP000050424; 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:KPM42628.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000050424};
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:UP000050424};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   496 AA;  54379 MW;  35F408B6E2EBADFE CRC64;
     MAPPQEAVDF VDFVNASPTP YHAVRSASER FEKAGFTLIR ERDSWASALH PGGKYYLTRN
     ASTIVAFTIG RKWRPGNPVA IVGAHTDSPC LRIKPVSKKS NVGFLQVGVE TYGGGIWHSW
     FDRDLSIAGR VLVKEGENFV QKLIKVEKPL LRIPTLAIHL HRQTNFDPNK ETELFPIAGL
     ATAELNKGVK SEEQAEKKDD AEEEKEEDFK PLQAMTERHH PHVLDVIASE AGVDVSSVVD
     FELVLYDTQK SCIGGINDEF VFSPRLDNLG MTYCSVEGLI TSVEDENALD DDSCIRLTVC
     FDHEEIGSTS AQGANSNLLP SVLRRLSVLP GNRDAASDGS YEAIHHDGED ATAYEQTLSR
     SFLISADMAH SVHPNYSGKY ESSHQPVMNA GTVIKINANQ RYATNSPGIV LLQECARTAG
     VPLQLFVVRN DSPCGSTIGP GLAAKLGMRT LDLGNPQLSM HSIRETGGTA DVGYGIRLFK
     HFFEQYGTLE PKILID
//
DBGET integrated database retrieval system