ID   TRF3_THEVO              Reviewed;         779 AA.
AC   Q97AJ6;
DT   31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Tricorn protease-interacting factor F3;
DE            EC=3.4.11.-;
GN   Name=trf3; OrderedLocusNames=TV0814; ORFNames=TVG0817891;
OS   Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC
OS   15438 / GSS1).
OC   Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC   Thermoplasmataceae; Thermoplasma.
OX   NCBI_TaxID=273116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1;
RX   PubMed=11121031; DOI=10.1073/pnas.97.26.14257;
RA   Kawashima T., Amano N., Koike H., Makino S., Higuchi S., Kawashima-Ohya Y.,
RA   Watanabe K., Yamazaki M., Kanehori K., Kawamoto T., Nunoshiba T.,
RA   Yamamoto Y., Aramaki H., Makino K., Suzuki M.;
RT   "Archaeal adaptation to higher temperatures revealed by genomic sequence of
RT   Thermoplasma volcanium.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:14257-14262(2000).
CC   -!- FUNCTION: Proteases F1, F2 and F3 degrade oligopeptides produced by
CC       Tricorn (themselves probably produced by the proteasome), yielding free
CC       amino acids. {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Part of the tricorn proteolytic complex. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase M1 family. {ECO:0000305}.
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DR   EMBL; BA000011; BAB59956.1; -; Genomic_DNA.
DR   RefSeq; WP_010917058.1; NC_002689.2.
DR   AlphaFoldDB; Q97AJ6; -.
DR   SMR; Q97AJ6; -.
DR   STRING; 273116.14325030; -.
DR   MEROPS; M01.021; -.
DR   EnsemblBacteria; BAB59956; BAB59956; BAB59956.
DR   GeneID; 1441906; -.
DR   KEGG; tvo:TVG0817891; -.
DR   eggNOG; arCOG02969; Archaea.
DR   HOGENOM; CLU_003705_0_1_2; -.
DR   OMA; AWQANWP; -.
DR   OrthoDB; 3866at2157; -.
DR   PhylomeDB; Q97AJ6; -.
DR   Proteomes; UP000001017; 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; Zinc.
FT   CHAIN           1..779
FT                   /note="Tricorn protease-interacting factor F3"
FT                   /id="PRO_0000095113"
FT   ACT_SITE        267
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         102
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         231..235
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         266
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
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         289
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   SITE            352
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   779 AA;  88069 MW;  6BC227F2ECECB201 CRC64;
     MDISEYDLTL DLDLQSKTFH GTETISASSG DFVLDAVGFN IEWIKVNGSD AKFEYDGNLL
     KINGLETAQK VEISYSGKIS DSLSGIYFAG RESNGMVTTH FEATDARRMF PCIDHPAYKA
     VFSITLVIDK DYDAISNMPI KKVETSDRKI VEFEKTPRMS TYLLYIGVGK FKYASERYKD
     REIILASLKD IKSKYPIDIA KRSIEFYEGY FGIPYALPKM HLISVPEFGA GAMENWGAIT
     FREIYLDIAD NSAASTLRLS ANVIAHEIAH QWFGDLVTMK WWNDLWLNES FATFMSYKTM
     DTIHPEWQFW GDFFVSRTSG ALRSDSLKNT HPIEVDVKDP DEISQIFDEI SYGKGASILR
     MIEDYVGAED FRKGISKYLK EHAYGNAEGS DLWNAIETES GKPVNRIMEA WITKAGYPIL
     KVSQDKTGIK VMQSRFFLGG GESTDRWPVP VKMRLNNGIS QMLLEEESTV ITDKDVIKLN
     ADNLGFYRVN YDDETFSKII ENMDKLTPLD RVGLVDDLFA FLMAGVITPD TYKNRIKSFF
     NDKDANVISN IVNQFEYLRI ITHYFDADAR EFLGTAIRYL ESADDENLKI AYGKASRLLA
     LLDEAYCETL APRFSNFEQQ TPELKSAIAT AYALSTGDVK GMVEKYRSLD RDEDKVKIIS
     GFGKLKSSTD LSVVSGMIEK GEIKKQDMLS FYLSALETMA GREYIYSNLE NIVKNVIRYF
     TGNRTASRTV EQILPVIGLT HPDAASIIER IGSKNTTMGL AKGKELLEVN RSLLERIGH