ID   TRF2_THEVO              Reviewed;         783 AA.
AC   Q978U3;
DT   31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Tricorn protease-interacting factor F2;
DE            EC=3.4.11.-;
GN   Name=trf2; OrderedLocusNames=TV1322; ORFNames=TVG1363786;
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: Monomer. Part of the Tricorn proteolytic complex (By
CC       similarity). {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; BAB60464.1; -; Genomic_DNA.
DR   RefSeq; WP_010917557.1; NC_002689.2.
DR   AlphaFoldDB; Q978U3; -.
DR   SMR; Q978U3; -.
DR   STRING; 273116.14325561; -.
DR   MEROPS; M01.020; -.
DR   PRIDE; Q978U3; -.
DR   EnsemblBacteria; BAB60464; BAB60464; BAB60464.
DR   GeneID; 1441439; -.
DR   KEGG; tvo:TVG1363786; -.
DR   eggNOG; arCOG02969; Archaea.
DR   HOGENOM; CLU_003705_0_1_2; -.
DR   OMA; FIPCVDH; -.
DR   OrthoDB; 3866at2157; -.
DR   PhylomeDB; Q978U3; -.
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..783
FT                   /note="Tricorn protease-interacting factor F2"
FT                   /id="PRO_0000095111"
FT   ACT_SITE        272
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         107
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   783 AA;  88980 MW;  57CDF0F111C31054 CRC64;
     MDFSIEEYDL TFDFDLSEFT YRGKEKIKLS GEANELVLDS VRLSIDSVKL NGSAVDFDVN
     DKALRIESRI KSGDVVDIDF HAKVSDTLMG LYLSKTREGT MITTQFESTG ARMAFPCIDH
     PAYKAVFSIT LVIDKDYDAI SNMPVKKVET SDRKIVEFEK TPRMSTYLLY IGVGKFKYAS
     ERYKDREIIL ASLKDIKSKY PIDIAKRSIE FYEGYFGIPY ALPKMHLISV PEFGAGAMEN
     WGAITFREIA LMATEDSGSL MKQNAAITIA HEIAHQWFGD LVTMKWWNDL WLNESFATFM
     SYKTVDSFSK QWDVFSDFIK SETGGALRSD SLKNTHPIEV DVKDPDEISQ IFDEISYGKG
     ASILRMIEDY VGAEDFRKGI SKYLKEHAYG NAEGSDLWNA IETESGKPVN RIMEAWITKA
     GYPVLKVNKD GNRIRLTQEQ FYLDGTSGNT EWPIPLTIIT KKGKVSMLME DEVYIDEMLK
     LNANNSGFYR VMYDNDTFNT VISSLDKFSN LDKWGLLNDM YAFLVSGRLS VNEYVERIKN
     FLNDEDHLVV EEIASQLTSL YLIKPSSQVV YQLAKDYLRN QVQRLGTKKK GEDDKISKLR
     GIVYQDLVTV DEDFAKELSP QFASLSEDPD LALAKAVAKA RTDGLNELID AANKYTDDEI
     RVRVIAAMGW CSKDQLSTIF SLIDNGTIKK QDMLYVFSFV VTNPSGRDFF FQNIDKIVSL
     MEHAFEGTGY TSRILEGSIP YIGLEKYEEI KAKASQIRSP SYNVGIDKGL ETLEIIRKLY
     NKL