ID   A0A1Y3N3J2_PIRSE        Unreviewed;       470 AA.
AC   A0A1Y3N3J2;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Aminopeptidase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PIROE2DRAFT_21276 {ECO:0000313|EMBL:OUM59134.1};
OS   Piromyces sp. (strain E2).
OC   Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC   Chytridiomycota incertae sedis; Neocallimastigomycetes; Neocallimastigales;
OC   Neocallimastigaceae; Piromyces.
OX   NCBI_TaxID=73868 {ECO:0000313|EMBL:OUM59134.1, ECO:0000313|Proteomes:UP000195826};
RN   [1] {ECO:0000313|EMBL:OUM59134.1, ECO:0000313|Proteomes:UP000195826}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2 {ECO:0000313|EMBL:OUM59134.1,
RC   ECO:0000313|Proteomes:UP000195826};
RG   DOE Joint Genome Institute;
RA   Haitjema C.H., Gilmore S.P., Henske J.K., Solomon K.V., De Groot R.,
RA   Kuo A., Mondo S.J., Salamov A.A., Labutti K., Zhao Z., Chiniquy J.,
RA   Barry K., Brewer H.M., Purvine S.O., Wright A.T., Boxma B., Van Alen T.,
RA   Hackstein J.H., Baker S.E., Grigoriev I.V., O'Malley M.A.;
RT   "A Parts List for Fungal Cellulosomes Revealed by Comparative Genomics.";
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
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; KZ151131; OUM59134.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y3N3J2; -.
DR   STRING; 73868.A0A1Y3N3J2; -.
DR   Proteomes; UP000195826; 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:SF2; M18 FAMILY AMINOPEPTIDASE 1-RELATED; 1.
DR   Pfam; PF02127; Peptidase_M18; 1.
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:UP000195826};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   470 AA;  51926 MW;  8664D0CAD9EAC6F4 CRC64;
     MADSKKSPTK QLQEKLFYKR KNAGLTMSEE DIKKSDAYNE DYKEFLGNSK IEREFAHNAI
     ERAKAKGFKE YTPGMGLKPG DKVYVNNRGK AVILAIIGEE PVKEGVHICA AHIDSPRLDL
     KQCPLYEDTE VALFKTHYYG GIKKYQWAVI PLALHGVVYK KDGSIVQVKV GEDENDPVFC
     VTDLLPHLSQ EQNKRSLPDG IRGEELNVVI GTLPFRDDEA SERVKTNIIK ILNDKYGIIE
     EDFLSAELEV VPAFKPKDVG FDRSIVGAYG QDDKVCSFAC LRAILDIDVV PKKTAVVCLA
     DKEEIGSEGN TGLRSSFLKY FVYDIAEDFG CKGRHVLSKS ECLSADVTVG VDPTFSDVTE
     KRNACYLNCG VGISKFTGAR GKSGSNDAHA EFVGRIRSLM DKHGVVWQTG ELGRVDLGGG
     GTVAAFIADL DVDTIDVGVP ILCMHAPFEL SAKLDNYNAY RCYNVFMSEK
//