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Database: UniProt
Entry: G4UDA5_NEUT9
LinkDB: G4UDA5_NEUT9
Original site: G4UDA5_NEUT9 
ID   G4UDA5_NEUT9            Unreviewed;       535 AA.
AC   G4UDA5;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   25-OCT-2017, entry version 26.
DE   SubName: Full=Peptidase M18, aminopeptidase I {ECO:0000313|EMBL:EGZ75665.1};
GN   ORFNames=NEUTE2DRAFT_148746 {ECO:0000313|EMBL:EGZ75665.1};
OS   Neurospora tetrasperma (strain FGSC 2509 / P0656).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Sordariomycetidae; Sordariales; Sordariaceae;
OC   Neurospora.
OX   NCBI_TaxID=510952 {ECO:0000313|EMBL:EGZ75665.1, ECO:0000313|Proteomes:UP000008513};
RN   [1] {ECO:0000313|EMBL:EGZ75665.1, ECO:0000313|Proteomes:UP000008513}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=strain FGSC 2509 / P0656 {ECO:0000313|Proteomes:UP000008513};
RX   PubMed=21750257; DOI=10.1534/genetics.111.130690;
RA   Ellison C.E., Stajich J.E., Jacobson D.J., Natvig D.O., Lapidus A.,
RA   Foster B., Aerts A., Riley R., Lindquist E.A., Grigoriev I.V.,
RA   Taylor J.W.;
RT   "Massive changes in genome architecture accompany the transition to
RT   self-fertility in the filamentous fungus Neurospora tetrasperma.";
RL   Genetics 189:55-69(2011).
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|RuleBase:RU004386}.
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DR   EMBL; GL891107; EGZ75665.1; -; Genomic_DNA.
DR   MEROPS; M18.001; -.
DR   EnsemblFungi; EGZ75665; EGZ75665; NEUTE2DRAFT_148746.
DR   OMA; SIVNWEL; -.
DR   OrthoDB; EOG092C3JCE; -.
DR   Proteomes; UP000008513; 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   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   ECO:0000313|EMBL:EGZ75665.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008513};
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:UP000008513};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   535 AA;  58151 MW;  46F4536385CC64B9 CRC64;
     MVRATPEYLA ARTSMMSLRA QALEQSMMAS QTYYAPPQQP QQPVAANQIN AKDIKPEAFT
     KPYLEFMTEN PTVFHAVGYF KEKLDKAGYK ELHSRDSWSG QIKPGGKYYT TRNGSSIIAW
     AVGKAYKPGN GLAMVAGHID ALTARLKPIS TKPSHDGYVQ LGIAQYAGAL NSTWWDRDLS
     IGGRVIVKDP ETGKTSTKVV KLDWPIARIP TLAPHFGIGM TGHNNQETEM TPIIGLDNSD
     LNSSSTASSE KPIGPKGSFV STQPPKLVKL IASQLKIEEY TNILNWELEL YDSQPAQVGG
     IDKEFIFAGR IDDKLCSWAA FMALLHARDD EDSGVIKLVA LFDDEEIGSL LRQGARGNFL
     PIVIERTVEA LVANTNTLYQ NAFIGGTGLG PGLMGQTYAN SFLVSSDVTH AAHPNFTQTN
     LTDHSPRLNV GVALCVDASA HMTTDSVSMA ILDRVAELSG CVNQRHMIRN DSRSGGTVGP
     MLSSAMGVKA ADVGIPQLSM HSIRATTGSL DPGLGVKFYK GFLDEWEKVD KEWRA
//
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