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Database: UniProt
Entry: G4UR01_NEUT9
LinkDB: G4UR01_NEUT9
Original site: G4UR01_NEUT9 
ID   G4UR01_NEUT9            Unreviewed;       536 AA.
AC   G4UR01;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   07-JUN-2017, entry version 29.
DE   SubName: Full=Aspartyl aminopeptidase {ECO:0000313|EMBL:EGZ71901.1};
GN   ORFNames=NEUTE2DRAFT_110972 {ECO:0000313|EMBL:EGZ71901.1};
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:EGZ71901.1, ECO:0000313|Proteomes:UP000008513};
RN   [1] {ECO:0000313|EMBL:EGZ71901.1, 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; GL891236; EGZ71901.1; -; Genomic_DNA.
DR   MEROPS; M18.002; -.
DR   EnsemblFungi; EGZ71901; EGZ71901; NEUTE2DRAFT_110972.
DR   OMA; CFDHEEI; -.
DR   OrthoDB; EOG092C3JCE; -.
DR   Proteomes; UP000008513; 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:EGZ71901.1};
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   536 AA;  58021 MW;  9F727D5C95C09314 CRC64;
     MLATPRVSPS PRLFSAAIHS FSLRPNSNTA SSVPFHVVRC HFSSTAARMA PPKSAYGFLD
     FVNASPTPYH AVATSAALFE KAGFKLIRER DNWASVVQPG SKYYLTRNGS SIVAFAVGGK
     WKPGNPIGMI GAHTDSPCLR VKPASKRNAH GFLQVGVELY GGGIWHTWFD RDLSVAGRVL
     VKDGDGIFIQ KLVKVDKPIL RVPTLAIHLH RQSNFDPNKE DELLPILGLV EKELNKPAAE
     AAAAPEENAE ADADFQPLKA MTDRHHSQFL SVVASAAGIS SASDIVDFEL ILYDTQPSCL
     GGLNDEFIFS ARLDNLNMTY CSVMGLINSV SSNSSLENDP SIRLVSCFDH EEIGSLSAHG
     ADSNLLPAIL RRLSVIPSLN ADSTETTPVS ETAFEQTLAT SFLVSADMAH SVHPNYAGKY
     ETNHRPEMNK GTVIKVNANQ RYATNSPGIV LLQEVAKRAK VPLQVFVVRN DSPCGSTIGP
     MLSAKLGVRT LDLGNPQLSM HSIRETGGSW DVEHAIGLFK GFLEMYGGLE AKIFID
//
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