ID   APE1_SULTO              Reviewed;         786 AA.
AC   Q96ZT9;
DT   31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Probable aminopeptidase 1;
DE            EC=3.4.11.-;
GN   Name=ape1; OrderedLocusNames=STK_17460;
OS   Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
OS   (Sulfolobus tokodaii).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfurisphaera.
OX   NCBI_TaxID=273063;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX   PubMed=11572479; DOI=10.1093/dnares/8.4.123;
RA   Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M.,
RA   Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y.,
RA   Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T.,
RA   Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K.,
RA   Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H.;
RT   "Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon,
RT   Sulfolobus tokodaii strain7.";
RL   DNA Res. 8:123-140(2001).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the peptidase M1 family. {ECO:0000305}.
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DR   EMBL; BA000023; BAB66834.1; -; Genomic_DNA.
DR   RefSeq; WP_010979812.1; NC_003106.2.
DR   AlphaFoldDB; Q96ZT9; -.
DR   SMR; Q96ZT9; -.
DR   STRING; 273063.STK_17460; -.
DR   MEROPS; M01.020; -.
DR   EnsemblBacteria; BAB66834; BAB66834; STK_17460.
DR   GeneID; 1459799; -.
DR   KEGG; sto:STK_17460; -.
DR   PATRIC; fig|273063.9.peg.1992; -.
DR   eggNOG; arCOG02969; Archaea.
DR   OMA; AWQANWP; -.
DR   OrthoDB; 3866at2157; -.
DR   Proteomes; UP000001015; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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   CDD; cd09601; M1_APN-Q_like; 1.
DR   Gene3D; 1.10.390.10; -; 1.
DR   Gene3D; 2.60.40.1730; -; 1.
DR   InterPro; IPR045357; Aminopeptidase_N-like_N.
DR   InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR   InterPro; IPR024571; ERAP1-like_C_dom.
DR   InterPro; IPR034016; M1_APN-typ.
DR   InterPro; IPR001930; Peptidase_M1.
DR   InterPro; IPR014782; Peptidase_M1_dom.
DR   InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR   Pfam; PF11838; ERAP1_C; 1.
DR   Pfam; PF01433; Peptidase_M1; 1.
DR   Pfam; PF17900; Peptidase_M1_N; 1.
DR   PRINTS; PR00756; ALADIPTASE.
DR   SUPFAM; SSF63737; SSF63737; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase; Cytoplasm; Hydrolase; Metal-binding; Metalloprotease;
KW   Protease; Reference proteome; Zinc.
FT   CHAIN           1..786
FT                   /note="Probable aminopeptidase 1"
FT                   /id="PRO_0000095108"
FT   ACT_SITE        271
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         103
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         235..239
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         270
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         274
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         293
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   SITE            356
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   786 AA;  90740 MW;  0CE5B6CD13CEC2D3 CRC64;
     MVNVERYEIF LDFNEYSYEG MEKIKMKSDG EKVELDSVGL EIKEVKADGK QVKYETKNEK
     LIVYSKVNEE LEIRFSGKAD NKSILGIYVA PYDGNYLITT QFEPIYARKF IPCFDSPDMK
     AVFKLSVRVN RGQKVISNMP IISIRDDGEK IVYEFDETPR MSTYLLYLGI GDFEEISDES
     KKPKIILATT PGKSKRGIFA IEVARKVIDY YEKYFEIPYQ LPKLHLIEIP EFAAGAMENW
     GAITFRESAL LADESSSVSQ KLSVSAVIAH ELAHQWFGDM VTLKWWDDLW LNESFATFMA
     YKSLKEIFPQ WESEGHFIYD ETLSALTEDS LLNTHPIETH VKDPHEIEEM FDNISYGKGA
     SILRMIEAYV GEEVFRRGVV NYLNKFKFSN ASGSDLWNSI SEAYGSDISQ IMAEWITKPG
     YPVITVNVEG DSVEFFQRRF TLLNVNDSTI YKVPLTFEVN GKRQTLLLDK ESVKLNFDNA
     VSSIKVNLNR TGFYRVLYKP FELSFSSTLN SYEELGLVND YWNFLLAGLE SIKTYLTLIK
     RFSNTRNSFL SREIAFELMT LYYINKDKYY SIARDFLLNQ IKIYRNAKDD LGKMAYSSII
     RSLAIVDDDF ALGLSNLFQY YEQLDSNIKG AVAIAYAIST SDFNGLLDKY KSFNSDEEKL
     RMIDAITNIR DKSIVEKLAM LVFNRTIKYQ EAPHVINSLS NNPYVREELC NFLQGNFDMI
     KQFVVTVAGM WGLFYIIRGP MIMCGVNKPE ETIEFLDRIK TKEIARSVEI TKEYIKVYNR
     VKNLDL