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Database: UniProt
Entry: S0E0U2_GIBF5
LinkDB: S0E0U2_GIBF5
Original site: S0E0U2_GIBF5 
ID   S0E0U2_GIBF5            Unreviewed;       493 AA.
AC   S0E0U2;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   22-NOV-2017, entry version 20.
DE   SubName: Full=Probable aspartyl aminopeptidase {ECO:0000313|EMBL:CCT66313.1};
GN   ORFNames=FFUJ_03332 {ECO:0000313|EMBL:CCT66313.1};
OS   Gibberella fujikuroi (strain CBS 195.34 / IMI 58289 / NRRL A-6831)
OS   (Bakanae and foot rot disease fungus) (Fusarium fujikuroi).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Hypocreales; Nectriaceae;
OC   Fusarium; Fusarium fujikuroi species complex.
OX   NCBI_TaxID=1279085 {ECO:0000313|EMBL:CCT66313.1, ECO:0000313|Proteomes:UP000016800};
RN   [1] {ECO:0000313|Proteomes:UP000016800}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 195.34 / IMI 58289 / NRRL A-6831
RC   {ECO:0000313|Proteomes:UP000016800};
RX   PubMed=23825955; DOI=10.1371/journal.ppat.1003475;
RA   Wiemann P., Sieber C.M.K., von Bargen K.W., Studt L., Niehaus E.M.,
RA   Espino J., Huss K., Michielse C., Albermann S., Wagner D.,
RA   Bergner S.V., Connolly L.R., Fischer A., Reuter G., Kleigrewe K.,
RA   Bald T., Wingfield B., Ophir R., Freeman S., Hippler M., Smith K.M.,
RA   Brown D.W., Proctor R.H., Munsterkotter M., Freitag M., Humpf H.U.,
RA   Guldener U., Tudzynski B.;
RT   "Deciphering the cryptic genome: genome-wide analyses of the rice
RT   pathogen Fusarium fujikuroi reveal complex regulation of secondary
RT   metabolism and novel metabolites.";
RL   PLoS Pathog. 9:E1003475-E1003475(2013).
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|RuleBase:RU004386}.
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DR   EMBL; HF679025; CCT66313.1; -; Genomic_DNA.
DR   EnsemblFungi; CCT66313; CCT66313; FFUJ_03332.
DR   EnsemblFungi; EBT00022341037; EBP00022356023; EBG00022326038.
DR   OrthoDB; EOG092C3JCE; -.
DR   Proteomes; UP000016800; Chromosome 3.
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   InterPro; IPR023367; Peptidase_M42_dom2.
DR   PANTHER; PTHR28570; PTHR28570; 1.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
DR   SUPFAM; SSF101821; SSF101821; 2.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:CCT66313.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000016800};
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:UP000016800};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   493 AA;  54054 MW;  84086F30C12F438D CRC64;
     MAPPQEALDF IEFVNESPTP YHAVQSASTR FEKAGFKLIR ERDSWASTLR PGGKYYLTRN
     ASTIVAFTIG RKWRPGNPVA IIGAHTDSPC LRLKPVSKKS NVGYLQIGVE TYGGGIWTSW
     FDRDLSIAGR VLVKEGDNFV SKLVKVDKPL VRIPTLAIHL HRQTNFDPNK ETELFPIAGL
     VAAELNKGTK DEKPEEKKDD NEEDEEFRPL KVMAERHHPQ VLDVIAAEAG VEVSAIIDFE
     LVLYDTQKSC IGGLSDEFIF SPRLDNLGMT YCSVEGLIES VKDESSLEED STIRLIVCFD
     HEEIGSTSAQ GANSNLLPSV IRRLSVLPGK DTASEGSYEA VHHDNEEATA YEQTLSRSFL
     VSADMAHSVH PNYAGKYESS HQPAMNGGTV IKINANQRYA TNSPGIVLLQ ECARTVGVPL
     QLFVVRNDSP CGSTIGPGLA AALGMRTLDL GNPQLSMHSI RETGGTADVA YGIKLFKGFF
     ENYGSLEPKI LID
//
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