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Database: UniProt
Entry: N4TYB2_FUSC1
LinkDB: N4TYB2_FUSC1
Original site: N4TYB2_FUSC1 
ID   N4TYB2_FUSC1            Unreviewed;       493 AA.
AC   N4TYB2;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   22-NOV-2017, entry version 13.
DE   SubName: Full=Aspartyl aminopeptidase {ECO:0000313|EMBL:ENH64197.1};
GN   ORFNames=FOC1_g10013468 {ECO:0000313|EMBL:ENH64197.1};
OS   Fusarium oxysporum f. sp. cubense (strain race 1) (Panama disease
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Hypocreales; Nectriaceae;
OC   Fusarium; Fusarium oxysporum species complex.
OX   NCBI_TaxID=1229664 {ECO:0000313|EMBL:ENH64197.1, ECO:0000313|Proteomes:UP000016928};
RN   [1] {ECO:0000313|Proteomes:UP000016928}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=race 1 {ECO:0000313|Proteomes:UP000016928};
RA   Fang X., Huang J.;
RT   "Genome sequencing and comparative transcriptomics of race 1 and race
RT   4 of banana pathogen: Fusarium oxysporum f. sp. cubense.";
RL   Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|RuleBase:RU004386}.
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DR   EMBL; KB730528; ENH64197.1; -; Genomic_DNA.
DR   EnsemblFungi; ENH64197; ENH64197; FOC1_g10013468.
DR   OrthoDB; EOG092C3JCE; -.
DR   Proteomes; UP000016928; 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   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:ENH64197.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000016928};
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:UP000016928};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   493 AA;  54127 MW;  C16A27AC9600C60B CRC64;
     MAPPQEALDF IEFVNESPTP YHAVQSASAR FEKAGFKLIR ERDSWASTLR PGGKYYLTRN
     ASTIVAFTIG RKWRPGNPVA IIGAHTDSPC LRLKPVSKKT NVGYLQIGVE TYGGGIWTSW
     FDRDLSIAGR VLVKEGDNFV SKLIKVDKPL IRIPTLAIHL HRQTNFDPNK ETELFPIAGL
     VAAELNKGTK DEKPEEKKDD NEEDEEFRPL KVMTERHHPQ VLDVIAAEAG VEVSAIIDFE
     LILYDTQKSC IGGLNDEFIF SPRLDNLGMT YCSVEGLIES VKDESSLEED STIRLTVCFD
     HEEIGSTSAQ GANSNLLPSV IRRLSVLPGK DTASEGSYEA VHHDNEEATA YEQTLSRSFL
     VSADMAHSVH PNYAGKYESS HQPAMNGGTV IKINANQRYA TNSPGIVLLQ ECARTTGVPL
     QLFVVRNDSP CGSTIGPGLA AALGMRTLDL GNPQLSMHSI RETGGTADVA YGIKLFKGFF
     ENYGSLEPKI LID
//
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