ID   APE2_SULTO              Reviewed;         781 AA.
AC   Q974N6;
DT   31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Probable aminopeptidase 2;
DE            EC=3.4.11.-;
GN   Name=ape2; OrderedLocusNames=STK_06230;
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; BAB65621.1; -; Genomic_DNA.
DR   RefSeq; WP_010978604.1; NC_003106.2.
DR   AlphaFoldDB; Q974N6; -.
DR   SMR; Q974N6; -.
DR   STRING; 273063.STK_06230; -.
DR   MEROPS; M01.021; -.
DR   EnsemblBacteria; BAB65621; BAB65621; STK_06230.
DR   GeneID; 1458571; -.
DR   KEGG; sto:STK_06230; -.
DR   PATRIC; fig|273063.9.peg.707; -.
DR   eggNOG; arCOG02969; Archaea.
DR   OMA; FIPCVDH; -.
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..781
FT                   /note="Probable aminopeptidase 2"
FT                   /id="PRO_0000095109"
FT   ACT_SITE        273
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         105
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         237..241
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         272
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         276
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         295
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   SITE            358
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   781 AA;  90370 MW;  58BBF8386DF623FB CRC64;
     MVSIDKYEIF LDFDFKNLIY KGYEKIYLST DNEVVLDSVG LNIVSVKTEG KSVPFKISDS
     QIFIQTGKFD GVLEIEFEGK VKERGLVGIY KAPYDHSYII TTQFESVHAR EFIPCIDHPA
     FKARFKLSVK VDKDLDVISN MPIEDVREEG DKKIVTFQET PRMSTYLLYL GIGKFEEIKD
     KLGEVDIIVA TVPGRISKGK FALDVAKKVI EYYEDYFGIK YQLPKEHLIA IPEFAFGAME
     NWGAITFRET ALLADESSSV QQKMRVASVV AHELAHQWFG DLVTMKWWDD LWLNESFATF
     MSHKAIAELY KEWDFWGTFI NSETSGALFR DSLTTTHPIE AHVTSPEEIE QLFDDISYGK
     GASILRMIEA YLGDEDFRKG IQIYLNTYKY SNATGSDFWN SLEKGSGKPV SEIVKDWITK
     DGYPVVYVSV NGSKINLEQE RFYLKGNGKN AVYKVPLTLE VNGRKITYLL EKEKDSIDIG
     SDIKSIKVNI DRTGFYRVYY NDLSLVFNSK LSHLDKWGLF NDYFNFFLAG RVNYTTYESI
     AKQFMKDDNY LVVDELVSEL YYLWRVNRDK YKLLYEVLPY QVKRFSKRKD ELSRRTYSYL
     LSTFAFVDEK FASGLAVAFE KYDTLDPNVK EAVAIAYAVT YGEDAYDELL NKYRSEKFDE
     EKTRLLYGLL SFREPYLVVN TMSLALTGEI KRQDVARILP YASYNPYSRL ALWKWLKTHM
     EFLRSIYAGT AILGRTLRSV IPFLGLNNAE VVEYFTTNRF PEMEVEIKSG LEILDSLRRI
     I