TRF3_THEAC
ID TRF3_THEAC Reviewed; 780 AA.
AC O93655;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Tricorn protease-interacting factor F3;
DE EC=3.4.11.-;
GN Name=trf3; OrderedLocusNames=Ta0815;
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].
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).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH ZINC IONS, AND
RP COFACTOR.
RX PubMed=15893768; DOI=10.1016/j.jmb.2005.03.070;
RA Kyrieleis O.J., Goettig P., Kiefersauer R., Huber R., Brandstetter H.;
RT "Crystal structures of the tricorn interacting factor F3 from Thermoplasma
RT acidophilum, a zinc aminopeptidase in three different conformations.";
RL J. Mol. Biol. 349:787-800(2005).
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;
CC Evidence={ECO:0000269|PubMed:15893768};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:15893768};
CC -!- SUBUNIT: Part of the tricorn proteolytic complex.
CC {ECO:0000269|PubMed:15893768}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the peptidase M1 family. {ECO:0000305}.
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DR EMBL; AF081952; AAC98290.1; -; Genomic_DNA.
DR EMBL; AL445065; CAC11944.1; -; Genomic_DNA.
DR PIR; T37456; T37456.
DR RefSeq; WP_010901227.1; NC_002578.1.
DR PDB; 1Z1W; X-ray; 2.70 A; A=1-780.
DR PDB; 1Z5H; X-ray; 2.30 A; A/B=1-780.
DR PDB; 3Q7J; X-ray; 2.91 A; A/B=1-780.
DR PDBsum; 1Z1W; -.
DR PDBsum; 1Z5H; -.
DR PDBsum; 3Q7J; -.
DR AlphaFoldDB; O93655; -.
DR SMR; O93655; -.
DR STRING; 273075.Ta0815; -.
DR MEROPS; M01.021; -.
DR EnsemblBacteria; CAC11944; CAC11944; CAC11944.
DR GeneID; 1456360; -.
DR KEGG; tac:Ta0815; -.
DR eggNOG; arCOG02969; Archaea.
DR HOGENOM; CLU_003705_0_1_2; -.
DR OMA; AWQANWP; -.
DR OrthoDB; 3866at2157; -.
DR BRENDA; 3.4.11.7; 6324.
DR EvolutionaryTrace; O93655; -.
DR PRO; PR:O93655; -.
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 3D-structure; Aminopeptidase; Cytoplasm; Hydrolase; Metal-binding;
KW Metalloprotease; Protease; Reference proteome; Zinc.
FT CHAIN 1..780
FT /note="Tricorn protease-interacting factor F3"
FT /id="PRO_0000095112"
FT ACT_SITE 266
FT /note="Proton acceptor"
FT /evidence="ECO:0000305"
FT BINDING 101
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 230..234
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 265
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT BINDING 269
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT BINDING 288
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT SITE 351
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT STRAND 3..13
FT /evidence="ECO:0007829|PDB:1Z5H"
FT TURN 14..17
FT /evidence="ECO:0007829|PDB:1Z5H"
FT STRAND 18..27
FT /evidence="ECO:0007829|PDB:1Z5H"
FT STRAND 32..35
FT /evidence="ECO:0007829|PDB:1Z5H"
FT STRAND 40..46
FT /evidence="ECO:0007829|PDB:1Z5H"
FT STRAND 57..62
FT /evidence="ECO:0007829|PDB:1Z5H"
FT STRAND 66..78
FT /evidence="ECO:0007829|PDB:1Z5H"
FT STRAND 80..91
FT /evidence="ECO:0007829|PDB:1Z5H"
FT STRAND 95..99
FT /evidence="ECO:0007829|PDB:1Z5H"
FT TURN 101..103
FT /evidence="ECO:0007829|PDB:1Z5H"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:1Z5H"
FT STRAND 119..127
FT /evidence="ECO:0007829|PDB:1Z5H"
FT STRAND 132..137
FT /evidence="ECO:0007829|PDB:1Z5H"
FT STRAND 139..152
FT /evidence="ECO:0007829|PDB:1Z5H"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:1Z5H"
FT STRAND 165..168
FT /evidence="ECO:0007829|PDB:1Z5H"
FT STRAND 171..177
FT /evidence="ECO:0007829|PDB:1Z5H"
FT STRAND 180..188
FT /evidence="ECO:0007829|PDB:1Z5H"
FT HELIX 194..210
FT /evidence="ECO:0007829|PDB:1Z5H"
FT STRAND 215..224
FT /evidence="ECO:0007829|PDB:1Z5H"
FT STRAND 237..241
FT /evidence="ECO:0007829|PDB:1Z5H"
FT HELIX 242..245
FT /evidence="ECO:0007829|PDB:1Z5H"
FT STRAND 249..251
FT /evidence="ECO:0007829|PDB:3Q7J"
FT HELIX 253..269
FT /evidence="ECO:0007829|PDB:1Z5H"
FT TURN 273..275
FT /evidence="ECO:0007829|PDB:1Z5H"
FT STRAND 276..280
FT /evidence="ECO:0007829|PDB:1Z5H"
FT HELIX 281..283
FT /evidence="ECO:0007829|PDB:1Z5H"
FT HELIX 284..302
FT /evidence="ECO:0007829|PDB:1Z5H"
FT TURN 304..306
FT /evidence="ECO:0007829|PDB:1Z5H"
FT HELIX 308..315
FT /evidence="ECO:0007829|PDB:1Z5H"
FT HELIX 317..323
FT /evidence="ECO:0007829|PDB:1Z5H"
FT STRAND 326..328
FT /evidence="ECO:0007829|PDB:3Q7J"
FT STRAND 337..339
FT /evidence="ECO:0007829|PDB:1Z1W"
FT TURN 342..345
FT /evidence="ECO:0007829|PDB:1Z5H"
FT HELIX 348..365
FT /evidence="ECO:0007829|PDB:1Z5H"
FT HELIX 367..381
FT /evidence="ECO:0007829|PDB:1Z5H"
FT STRAND 384..386
FT /evidence="ECO:0007829|PDB:1Z5H"
FT HELIX 388..399
FT /evidence="ECO:0007829|PDB:1Z5H"
FT HELIX 403..412
FT /evidence="ECO:0007829|PDB:1Z5H"
FT STRAND 413..415
FT /evidence="ECO:0007829|PDB:3Q7J"
FT STRAND 417..434
FT /evidence="ECO:0007829|PDB:1Z5H"
FT STRAND 440..442
FT /evidence="ECO:0007829|PDB:1Z1W"
FT STRAND 447..453
FT /evidence="ECO:0007829|PDB:1Z5H"
FT STRAND 456..462
FT /evidence="ECO:0007829|PDB:1Z5H"
FT STRAND 464..469
FT /evidence="ECO:0007829|PDB:1Z5H"
FT STRAND 473..477
FT /evidence="ECO:0007829|PDB:1Z5H"
FT HELIX 478..480
FT /evidence="ECO:0007829|PDB:1Z5H"
FT STRAND 482..487
FT /evidence="ECO:0007829|PDB:1Z5H"
FT HELIX 490..498
FT /evidence="ECO:0007829|PDB:1Z5H"
FT HELIX 499..502
FT /evidence="ECO:0007829|PDB:1Z5H"
FT HELIX 505..521
FT /evidence="ECO:0007829|PDB:1Z5H"
FT STRAND 522..524
FT /evidence="ECO:0007829|PDB:1Z5H"
FT HELIX 526..533
FT /evidence="ECO:0007829|PDB:1Z5H"
FT HELIX 534..536
FT /evidence="ECO:0007829|PDB:1Z5H"
FT HELIX 542..556
FT /evidence="ECO:0007829|PDB:1Z5H"
FT HELIX 563..577
FT /evidence="ECO:0007829|PDB:1Z5H"
FT HELIX 583..599
FT /evidence="ECO:0007829|PDB:1Z5H"
FT HELIX 601..608
FT /evidence="ECO:0007829|PDB:1Z5H"
FT HELIX 609..616
FT /evidence="ECO:0007829|PDB:1Z5H"
FT HELIX 619..632
FT /evidence="ECO:0007829|PDB:1Z5H"
FT HELIX 636..644
FT /evidence="ECO:0007829|PDB:1Z5H"
FT HELIX 649..659
FT /evidence="ECO:0007829|PDB:1Z5H"
FT HELIX 665..676
FT /evidence="ECO:0007829|PDB:1Z5H"
FT HELIX 682..692
FT /evidence="ECO:0007829|PDB:1Z5H"
FT HELIX 696..704
FT /evidence="ECO:0007829|PDB:1Z5H"
FT HELIX 706..717
FT /evidence="ECO:0007829|PDB:1Z5H"
FT STRAND 719..721
FT /evidence="ECO:0007829|PDB:1Z5H"
FT HELIX 722..734
FT /evidence="ECO:0007829|PDB:1Z5H"
FT TURN 735..737
FT /evidence="ECO:0007829|PDB:1Z5H"
FT HELIX 741..746
FT /evidence="ECO:0007829|PDB:1Z5H"
FT HELIX 754..775
FT /evidence="ECO:0007829|PDB:1Z5H"
FT TURN 776..779
FT /evidence="ECO:0007829|PDB:1Z5H"
SQ SEQUENCE 780 AA; 89380 MW; F499AB342BAB9218 CRC64;
MEVEKYDLTL DFDIQKRTFN GTETITADAG DIVLDAVGLQ INWMKVNGRD TAFTYDGQTV
RAPGDSQPQK IEISFAGKVS DSLSGIYYAG RENGMITTHF EATDARRMFP CVDHPAYKAV
FAITVVIDKD YDAISNMPPK RIEVSERKVV EFQDTPRMST YLLYVGIGKF RYEYEKYRDI
DLILASLKDI RSKYPLDMAR KSVEFYENYF GIPYALPKMH LISVPEFGAG AMENWGAITF
REIYMDIAEN SAVTVKRNSA NVIAHEIAHQ WFGDLVTMKW WNDLWLNESF ATFMSYKTMD
TLFPEWSFWG DFFVSRTSGA LRSDSLKNTH PIEVDVRDPD EISQIFDEIS YGKGASILRM
IEDYAGYEEF RKGISKYLND HKFGNAEGSD LWTAIEDVSG KPVKRVMEYW IKNPGYPVIK
LKRNGRKITM YQTRFLLNGE EEGRWPVPVN IKKKDGVERI LLEDEASIEA DGLIKINADS
AGFYRVLYDD ATFSDVMGHY RDLSPLDRIG LVDDLFAFLL SGHIDPETYR QRIRNFFDDE
DHNVITAIVG QMEYLRMLTH AFDDDARAFC RSRMQFLTGK QDENLKIALG RVSRLYVMVD
ESYAEEMSKL FKDFDSAEPE MRSSIATAYA LVTGDLKGLL EKFRSVDRDE DRVRIISAFG
KLKSNTDLST VYGMVEKTEI KKQDMISFFS SALETLPGRE FIFANLDRII RLVIRYFTGN
RTASRTVEMM IPVIGLDHPD AEDIVRNIGS KNISMGLAKG IEMLAVNRKL VERIRQTAVK
