GenomeNet

Database: UniProt
Entry: A0A0B4H6M0_9HYPO
LinkDB: A0A0B4H6M0_9HYPO
Original site: A0A0B4H6M0_9HYPO 
ID   A0A0B4H6M0_9HYPO        Unreviewed;       552 AA.
AC   A0A0B4H6M0;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   10-MAY-2017, entry version 11.
DE   SubName: Full=Vacuolar aspartyl aminopeptidase Lap4 {ECO:0000313|EMBL:KID87627.1};
GN   ORFNames=MGU_05276 {ECO:0000313|EMBL:KID87627.1};
OS   Metarhizium guizhouense ARSEF 977.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Hypocreales; Clavicipitaceae;
OC   Metarhizium.
OX   NCBI_TaxID=1276136 {ECO:0000313|EMBL:KID87627.1, ECO:0000313|Proteomes:UP000031192};
RN   [1] {ECO:0000313|EMBL:KID87627.1, ECO:0000313|Proteomes:UP000031192}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ARSEF 977 {ECO:0000313|EMBL:KID87627.1,
RC   ECO:0000313|Proteomes:UP000031192};
RX   PubMed=25368161; DOI=10.1073/pnas.1412662111;
RA   Hu X., Xiao G., Zheng P., Shang Y., Su Y., Zhang X., Liu X., Zhan S.,
RA   St Leger R.J., Wang C.;
RT   "Trajectory and genomic determinants of fungal-pathogen speciation and
RT   host adaptation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:16796-16801(2014).
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:KID87627.1}.
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; AZNH01000015; KID87627.1; -; Genomic_DNA.
DR   EnsemblFungi; KID87627; KID87627; MGU_05276.
DR   Proteomes; UP000031192; 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   ECO:0000313|EMBL:KID87627.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000031192};
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   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   552 AA;  59485 MW;  DBF1C804E9BC43CA CRC64;
     MTRRTPLPSP QSSVLPLRQP SAPAPAPVTT TTTTASPKSK NFILADMDGR ASRENRACAS
     CISKLTPSEI GQVNWHLAQD QACRLCQVAQ CKPEAFTKPF CDFLQENPTV FHTVDYFKRK
     LSDSGFEELS ARDSWNGKVH PGGKYWVTRN GSTIIAFTVG AAYKPGSGVA MIGGHIDALT
     ARLKPISNRP SKAGYVQLGV AQYAGGLNQT WWDRDLSIGG RVVVRDPETG KTSTKLVKLD
     WPIAKIPTLA PHFGVGMFGN NNKETQAVPV IGLQSSSQHD AEPLGPEGAF VNTQPPRLVQ
     LIAKQLGITS YASILNWELE LYDSQPAQTM GMDREFITAG RIDDKLCSWA ALTGLLAADT
     NTDDSYIKLV ALFDDEEIGS LLRQGARSNF LPIVIERTVE ALNPSTYGPG LLGQTYAKSF
     LLSADVTHAG NPNFLENYLD DHVPQLNVGI AICGDSNGNM TTDAVSTAIL RRVGEIIGAK
     TQDFQIRNDS RSGGTIGPSL SSAMGCRAAD AGLAQLSMHS VRATTGALDP GLGVKFFKGF
     LDLWEQIDGE WS
//
DBGET integrated database retrieval system