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Database: UniProt
Entry: F9FFF7_FUSOF
LinkDB: F9FFF7_FUSOF
Original site: F9FFF7_FUSOF 
ID   F9FFF7_FUSOF            Unreviewed;       493 AA.
AC   F9FFF7;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   28-FEB-2018, entry version 27.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EGU84350.1};
GN   ORFNames=FOXB_05136 {ECO:0000313|EMBL:EGU84350.1};
OS   Fusarium oxysporum (strain Fo5176) (Fusarium vascular wilt).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Hypocreales; Nectriaceae;
OC   Fusarium; Fusarium oxysporum species complex.
OX   NCBI_TaxID=660025 {ECO:0000313|EMBL:EGU84350.1, ECO:0000313|Proteomes:UP000002489};
RN   [1] {ECO:0000313|EMBL:EGU84350.1, ECO:0000313|Proteomes:UP000002489}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fo5176 {ECO:0000313|EMBL:EGU84350.1,
RC   ECO:0000313|Proteomes:UP000002489};
RX   PubMed=21942452; DOI=10.1094/MPMI-08-11-0212;
RA   Thatcher L.F., Gardiner D.M., Kazan K., Manners J.;
RT   "A highly conserved effector in Fusarium oxysporum is required for
RT   full virulence on Arabidopsis.";
RL   Mol. Plant Microbe Interact. 25:180-190(2012).
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:EGU84350.1}.
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DR   EMBL; AFQF01001664; EGU84350.1; -; Genomic_DNA.
DR   MEROPS; M18.002; -.
DR   OrthoDB; EOG092C3JCE; -.
DR   Proteomes; UP000002489; 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   Gene3D; 2.30.250.10; -; 1.
DR   InterPro; IPR001948; Peptidase_M18.
DR   InterPro; IPR023358; Peptidase_M18_dom2.
DR   PANTHER; PTHR28570; PTHR28570; 1.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|RuleBase:RU004386};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002489};
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:UP000002489};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   493 AA;  54096 MW;  886DB6F236FADB20 CRC64;
     MAPPQEALDF IEFVNESPTP YHAVQSASAR FEKAGFKLIR ERDSWASTLR PGGKYYLTRN
     ASTIVAFTIG RKWRPGNPVA IIGAHTDSPC LRLKPVSKKT NVGYLQIGVE TYGGGIWTSW
     FDRDLSIAGR VLVKEGDNFV SKLIKVNKPL 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 ECARTAGVPL
     QLFVVRNDSP CGSTIGPGLA AALGMRTLDL GNPQLSMHSI RETGGTADVA YGIKLFKGFF
     ENYGSLEPKI LID
//
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