GenomeNet

Database: UniProt
Entry: A0A165EYL7_EXIGL
LinkDB: A0A165EYL7_EXIGL
Original site: A0A165EYL7_EXIGL 
ID   A0A165EYL7_EXIGL        Unreviewed;       466 AA.
AC   A0A165EYL7;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   07-JUN-2017, entry version 6.
DE   SubName: Full=Peptidase M18, aminopeptidase I {ECO:0000313|EMBL:KZV87984.1};
GN   ORFNames=EXIGLDRAFT_651670 {ECO:0000313|EMBL:KZV87984.1};
OS   Exidia glandulosa HHB12029.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Auriculariales; Exidiaceae; Exidia.
OX   NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV87984.1, ECO:0000313|Proteomes:UP000077266};
RN   [1] {ECO:0000313|EMBL:KZV87984.1, ECO:0000313|Proteomes:UP000077266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB12029 {ECO:0000313|EMBL:KZV87984.1,
RC   ECO:0000313|Proteomes:UP000077266};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K.,
RA   Labutti K., Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T.,
RA   Yoshinaga Y., Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi
RT   Provides Insights into the Origins of Lignocellulose Decay
RT   Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|RuleBase:RU004386}.
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; KV426110; KZV87984.1; -; Genomic_DNA.
DR   EnsemblFungi; KZV87984; KZV87984; EXIGLDRAFT_651670.
DR   Proteomes; UP000077266; 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:KZV87984.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000077266};
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:UP000077266};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   466 AA;  50087 MW;  EA89BE2CD00CEDEB CRC64;
     MHFAQKPPAA SGLINFVNAS PSPFHAVASA AKLLEDAGFV KIREQDEWEN DVEPGGSYYF
     TRNELAVVAF TLPDDWQPGR GLSMVATHLD SPSLRVRPVS KKSAEGYLQV GVETYGGGIW
     HTWIDRDLSV AGRVVIKDAS SGAFRTRLVK VDRPLLRIPS LAVHLDGSVN SSFSFNRETQ
     FVPILGLVSS ESSRQQDDPA ILSMFASDNH HAELLEAVAD DLGVRAADIE ELELALYDTQ
     PATLGGAKNE FVFSPRLDNQ FSTFCATQAL VESVSSTKAL SRRNGNVNVI MLFNHEEIGS
     VSTSGAQSSL AKTLIERLSP GAGLTARSIA KSFLISSDVG HAVHPSYPSK HERNHKPVLN
     GGVAIKTNAG QRYTSEGVGT FIVKQLAASR GGTLQQYEVP NDITAGSTVG PHLSTIGMRT
     IDVGAPILSM HSIREQAGVD DVQALVDLFG AFFESYTDVA AKLQVD
//
DBGET integrated database retrieval system