ID   L2GYG7_VAVCU            Unreviewed;       470 AA.
AC   L2GYG7;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 2.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=aspartyl aminopeptidase {ECO:0000256|ARBA:ARBA00011965};
DE            EC=3.4.11.21 {ECO:0000256|ARBA:ARBA00011965};
GN   ORFNames=VCUG_00208 {ECO:0000313|EMBL:ELA48372.2};
OS   Vavraia culicis (isolate floridensis) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Pleistophoridae;
OC   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., MacDonald P.J.P.,
RA   McCowen C., Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The genome sequence of Vavraia culicis strain floridensis.";
RL   Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of an N-terminal aspartate or glutamate from a
CC         peptide, with a preference for aspartate.; EC=3.4.11.21;
CC         Evidence={ECO:0000256|ARBA:ARBA00001335};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|ARBA:ARBA00008290, ECO:0000256|RuleBase:RU004386}.
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DR   EMBL; GL877405; ELA48372.2; -; Genomic_DNA.
DR   RefSeq; XP_008073144.1; XM_008074953.1.
DR   AlphaFoldDB; L2GYG7; -.
DR   STRING; 948595.L2GYG7; -.
DR   GeneID; 19878098; -.
DR   VEuPathDB; MicrosporidiaDB:VCUG_00208; -.
DR   HOGENOM; CLU_019532_2_0_1; -.
DR   InParanoid; L2GYG7; -.
DR   OMA; GPILKVN; -.
DR   OrthoDB; 1156at2759; -.
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   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.30.250.10; Aminopeptidase i, Domain 2; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR001948; Peptidase_M18.
DR   InterPro; IPR023358; Peptidase_M18_dom2.
DR   PANTHER; PTHR28570; ASPARTYL AMINOPEPTIDASE; 1.
DR   PANTHER; PTHR28570:SF3; ASPARTYL AMINOPEPTIDASE; 1.
DR   Pfam; PF02127; Peptidase_M18; 2.
DR   PRINTS; PR00932; AMINO1PTASE.
DR   SUPFAM; SSF101821; Aminopeptidase/glucanase lid domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW   ECO:0000256|RuleBase:RU004386};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU004386};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU004386};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000256|RuleBase:RU004386};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU004386};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011081};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, 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
//