TRF2_THEAC
ID TRF2_THEAC Reviewed; 783 AA.
AC O93654;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Tricorn protease-interacting factor F2;
DE EC=3.4.11.-;
GN Name=trf2; OrderedLocusNames=Ta0301;
OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS 15155 / AMRC-C165).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273075;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-21; 334-360;
RP 411-418; 434-448; 453-460 AND 678-685.
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=9845366; DOI=10.1016/s0092-8674(00)81634-7;
RA Tamura N., Lottspeich F., Baumeister W., Tamura T.;
RT "The role of tricorn protease and its aminopeptidase-interacting factors in
RT cellular protein degradation.";
RL Cell 95:637-648(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=11029001; DOI=10.1038/35035069;
RA Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT acidophilum.";
RL Nature 407:508-513(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.
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.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the peptidase M1 family. {ECO:0000305}.
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DR EMBL; AF081951; AAC98289.1; -; Genomic_DNA.
DR EMBL; AL445063; CAC11446.1; -; Genomic_DNA.
DR PIR; T37457; T37457.
DR RefSeq; WP_010900730.1; NC_002578.1.
DR AlphaFoldDB; O93654; -.
DR SMR; O93654; -.
DR STRING; 273075.Ta0301; -.
DR MEROPS; M01.020; -.
DR EnsemblBacteria; CAC11446; CAC11446; CAC11446.
DR GeneID; 1455925; -.
DR KEGG; tac:Ta0301; -.
DR eggNOG; arCOG02969; Archaea.
DR HOGENOM; CLU_003705_0_3_2; -.
DR OMA; FIPCVDH; -.
DR OrthoDB; 3866at2157; -.
DR Proteomes; UP000001024; 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 1: Evidence at protein level;
KW Aminopeptidase; Cytoplasm; Direct protein sequencing; Hydrolase;
KW Metal-binding; Metalloprotease; Protease; Reference proteome; Zinc.
FT CHAIN 1..783
FT /note="Tricorn protease-interacting factor F2"
FT /id="PRO_0000095110"
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; 88855 MW; 274235AB250FB632 CRC64;
MNPGIEKYEI RFDFDLKDFT YTSHERIHLA GDWKDIKLDA VRLSVDKVTC NGQPMRFETG
QDTVTVKGSF HDKDVIDIDF HAKVSDTLMG LYLSRTKEGT MITTQFESNG ARMAFPCVDH
PAYKAVFAIT VVIDKDYDAI SNMPPKRIEV SERKIVEFQD TPKMSTYLLY IGVGKFKYAT
DKYRDIDLIL VSLKDIKSKY PLEIARKSIE FYESYFGIPY ALPKMHLISV PEFGAGAMEN
WGAITFREVA LMATENSGSI MKQNAAITIA HEIAHQWFGD LVTMKWWNDL WLNESFATFM
SYKTVDSFSK QWDVFADFIR SETGGALRSD SLKNTHPIEV DVKDPDEISQ IFDEISYGKG
ASILRMIEDY AGYEEFRKGI SKYLNDHRYG NAEGSDLWTA IEDVSGKPVK RVMEYWIKNP
GYPVVSVVKS GNKFRLTQEQ FFLDGTRGQG KWPIPLTVMT KSGKKAMLME ESAEIEDMVK
VNVNSSGFYR VSYDGESFET VMKNYSKLSN LDRWGLISDL YAFLISGRVS VDDYLARIKG
FFEDSDHLIV EEIASQLTGL YLLKPDSNRI RETAASYLSR QVVALGDKQK GEDDKISKIR
GIVTQDLAMV DDHFASDLAR KFSTLAEDPD LALAKSIAAA KAYGISELAS AADKYTDDEI
RVRIIAAMGW CSPSDLKSVF ELIDKGTIRK QDMLYVFSNM PANPKGRDFF FSNIDRIVAL
MEHAFEGTGY TSRILETAIP YLGLARYEDV KKKAEQIRKP SYNVGINKGL ETLEIVRKLY
NKL
