ID   APE1_SACS2              Reviewed;         784 AA.
AC   Q97VF1;
DT   31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Probable aminopeptidase 1;
DE            EC=3.4.11.-;
GN   Name=ape1; OrderedLocusNames=SSO2675; ORFNames=C30_037;
OS   Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS   (Sulfolobus solfataricus).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Saccharolobus.
OX   NCBI_TaxID=273057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=11427726; DOI=10.1073/pnas.141222098;
RA   She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA   Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA   Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA   Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA   Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA   Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT   "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(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; AE006641; AAK42793.1; -; Genomic_DNA.
DR   PIR; B90442; B90442.
DR   RefSeq; WP_009988593.1; NC_002754.1.
DR   AlphaFoldDB; Q97VF1; -.
DR   SMR; Q97VF1; -.
DR   STRING; 273057.SSO2675; -.
DR   MEROPS; M01.021; -.
DR   EnsemblBacteria; AAK42793; AAK42793; SSO2675.
DR   GeneID; 44128403; -.
DR   KEGG; sso:SSO2675; -.
DR   PATRIC; fig|273057.12.peg.2757; -.
DR   eggNOG; arCOG02969; Archaea.
DR   HOGENOM; CLU_003705_0_3_2; -.
DR   InParanoid; Q97VF1; -.
DR   OMA; AWQANWP; -.
DR   PhylomeDB; Q97VF1; -.
DR   Proteomes; UP000001974; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0070006; F:metalloaminopeptidase activity; IBA:GO_Central.
DR   GO; GO:0042277; F:peptide binding; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR   GO; GO:0043171; P:peptide catabolic process; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
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..784
FT                   /note="Probable aminopeptidase 1"
FT                   /id="PRO_0000095106"
FT   ACT_SITE        272
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         103
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         236..240
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         271
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         275
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         294
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   SITE            357
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   784 AA;  90143 MW;  45C98433821CD619 CRC64;
     MPNIEKYEIF LDFNGNEYEG VEKIYLNSEE EKLELDSVNL EIRSVKSDGK DTKFELKGEK
     LVIYGKIERE LEIKFKGKAS RDSILGIYVA PYDGKGMITT QFEAVYARRF IPCFDHPAMK
     ARFKLSVRVQ KGLKVISNMP VERIEEDVDG KVIYRFQETP KMSTYLLYLG IDEFEEISDN
     SKQPTVILAT VPGKSKRGLF AINVARKVIE FYEKYFEIPY QLPKVHLIQV PEFAAGAMEN
     WGAITFRETA LLADDSSSIS QKFRVAEVVA HELAHQWFGN LVTLKWWDDL WLNESFATFM
     SYKSIKHLFP QWDSEGHLIY DESIGALEDD SLSTTHPIEA HVKDPHEIEQ MFDNISYGKG
     ASILKMIEAY VGEENFRRGV VNYLNSFKFG NAEGKDLWNS ISNAAGQSIG EIMADWITKP
     GYPVIFVNAY GNSIRFSQKR FTLLDSGLNE VYKVPITYEI NDKFGTLLLD KESAEIRLDE
     GLKSIKVNIN RTGFYRVLYD SLNLAFSSKL NAYEELGLVN DYWNFLLADL IDAKTYFGVI
     GRFVYTSNSF VSREITSQLL TLYYLFKKNY GKDFLVNQVK IFRKANDDLG KLAYSTVISA
     LARMDEEFAL GLSTLFDQYE NIDSNIKEAV AIAYAVTNND FNTLLEKYKR YTIDEEKNRI
     LSAISSLRDP SIVVKVFSLI FERNIKAQDT RFVISSLLHN PHIREEVCSY LMNNFEEVKK
     FVNTVYGGPW GLGSIVRSMS FCGVDKPKDI IDFLEKVKFK EIERPIKESE ERIKVYSRLK
     QNLP