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Database: UniProt
Entry: L2GYG7_VAVCU
LinkDB: L2GYG7_VAVCU
Original site: L2GYG7_VAVCU 
ID   L2GYG7_VAVCU            Unreviewed;       470 AA.
AC   L2GYG7;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 2.
DT   22-NOV-2017, entry version 21.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ELA48372.2};
GN   ORFNames=VCUG_00208 {ECO:0000313|EMBL:ELA48372.2};
OS   Vavraia culicis (isolate floridensis) (Microsporidian parasite).
OC   Eukaryota; Fungi; Microsporidia; Pleistophoridae; Vavraia.
OX   NCBI_TaxID=948595 {ECO:0000313|EMBL:ELA48372.2, ECO:0000313|Proteomes:UP000011081};
RN   [1] {ECO:0000313|Proteomes:UP000011081}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=floridensis {ECO:0000313|Proteomes:UP000011081};
RG   The Broad Institute Genome Sequencing Platform;
RA   Cuomo C., Becnel J., Sanscrainte N., Young S.K., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA   Berlin A., Chapman S.B., Gearin G., Goldberg J., Griggs A., Gujja S.,
RA   Hansen M., Heiman D., Howarth C., Larimer J., Lui A.,
RA   MacDonald P.J.P., McCowen C., Montmayeur A., Murphy C., Neiman D.,
RA   Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA   Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The genome sequence of Vavraia culicis strain floridensis.";
RL   Submitted (MAR-2011) 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; GL877405; ELA48372.2; -; Genomic_DNA.
DR   RefSeq; XP_008073144.1; XM_008074953.1.
DR   EnsemblFungi; ELA48372; ELA48372; VCUG_00208.
DR   GeneID; 19878098; -.
DR   EuPathDB; MicrosporidiaDB:VCUG_00208; -.
DR   InParanoid; L2GYG7; -.
DR   OrthoDB; EOG092C3JCE; -.
DR   Proteomes; UP000011081; 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; 2.
DR   PRINTS; PR00932; AMINO1PTASE.
DR   SUPFAM; SSF101821; SSF101821; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|RuleBase:RU004386};
KW   Complete proteome {ECO:0000313|Proteomes:UP000011081};
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:UP000011081};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   470 AA;  53037 MW;  9A460ABC844CAA1B CRC64;
     MTNKICTLKM SLITDYLKYL DRCLTPYHVV VETITILDEQ GYKRISLQDL DSIGPGKYYI
     FVFNTVIIPI VIPVDPVGIR MVATHSDSPV LKLKPNFSDT AENMCIARLR PYGGGLWHTW
     FDRSLSVGGL VMLKNGRRVL VDRMFDVVVP SLPPHLNNSK VYNNGFLYDK ERVLNGLVMV
     DTKLDDKVFT GQGFDMDDKV GNRCDSGCGK CESNDEHDRS LSSNSVLVEE NSLHANSQPT
     CQDKSMLDTR DKSENDVHFK LEDIISHNLS LYDLAHAEIL NEQLIMSARQ DNLLSTFVGL
     KALNTEGRSI KVLAVFDFEE IGSMQLDGAR CTFLKDVYTR LQKNLANPYD SMIISLDVAH
     TYNFNYDEFY EKKHRIKFNK GIVVKHSAAY ATDMDGTAFI KQLSGFKCQD FCLRNDIRGG
     GTIGTMLSTL LGTRCIDLGS PIMAMHSIRE TSSCKDVTDT FQLLYDFYKS
//
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