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Protein

Tricorn protease-interacting factor F3

Gene

trf3

Organism
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Proteases F1, F2 and F3 degrade oligopeptides produced by Tricorn (themselves probably produced by the proteasome), yielding free amino acids.

Cofactori

Zn2+1 PublicationNote: Binds 1 zinc ion per subunit.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei101 – 1011SubstrateBy similarity
Metal bindingi265 – 2651Zinc; catalytic
Active sitei266 – 2661Proton acceptorCurated
Metal bindingi269 – 2691Zinc; catalytic
Metal bindingi288 – 2881Zinc; catalytic
Sitei351 – 3511Transition state stabilizerBy similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

MEROPSiM01.021.

Names & Taxonomyi

Protein namesi
Recommended name:
Tricorn protease-interacting factor F3 (EC:3.4.11.-)
Gene namesi
Name:trf3
Ordered Locus Names:Ta0815
OrganismiThermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Taxonomic identifieri273075 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermoplasmataThermoplasmatalesThermoplasmataceaeThermoplasma
Proteomesi
  • UP000001024 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 780780Tricorn protease-interacting factor F3PRO_0000095112Add
BLAST

Proteomic databases

PRIDEiO93655.

Interactioni

Subunit structurei

Part of the tricorn proteolytic complex.1 Publication

Protein-protein interaction databases

STRINGi273075.Ta0815.

Structurei

Secondary structure

1
780
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 1311Combined sources
Turni14 – 174Combined sources
Beta strandi18 – 2710Combined sources
Beta strandi32 – 354Combined sources
Beta strandi40 – 467Combined sources
Beta strandi57 – 626Combined sources
Beta strandi66 – 7813Combined sources
Beta strandi80 – 9112Combined sources
Beta strandi95 – 995Combined sources
Turni101 – 1033Combined sources
Helixi105 – 1073Combined sources
Beta strandi119 – 1279Combined sources
Beta strandi132 – 1376Combined sources
Beta strandi139 – 15214Combined sources
Helixi160 – 1623Combined sources
Beta strandi165 – 1684Combined sources
Beta strandi171 – 1777Combined sources
Beta strandi180 – 1889Combined sources
Helixi194 – 21017Combined sources
Beta strandi215 – 22410Combined sources
Beta strandi237 – 2415Combined sources
Helixi242 – 2454Combined sources
Beta strandi249 – 2513Combined sources
Helixi253 – 26917Combined sources
Turni273 – 2753Combined sources
Beta strandi276 – 2805Combined sources
Helixi281 – 2833Combined sources
Helixi284 – 30219Combined sources
Turni304 – 3063Combined sources
Helixi308 – 3158Combined sources
Helixi317 – 3237Combined sources
Beta strandi326 – 3283Combined sources
Beta strandi337 – 3393Combined sources
Turni342 – 3454Combined sources
Helixi348 – 36518Combined sources
Helixi367 – 38115Combined sources
Beta strandi384 – 3863Combined sources
Helixi388 – 39912Combined sources
Helixi403 – 41210Combined sources
Beta strandi413 – 4153Combined sources
Beta strandi417 – 43418Combined sources
Beta strandi440 – 4423Combined sources
Beta strandi447 – 4537Combined sources
Beta strandi456 – 4627Combined sources
Beta strandi464 – 4696Combined sources
Beta strandi473 – 4775Combined sources
Helixi478 – 4803Combined sources
Beta strandi482 – 4876Combined sources
Helixi490 – 4989Combined sources
Helixi499 – 5024Combined sources
Helixi505 – 52117Combined sources
Beta strandi522 – 5243Combined sources
Helixi526 – 5338Combined sources
Helixi534 – 5363Combined sources
Helixi542 – 55615Combined sources
Helixi563 – 57715Combined sources
Helixi583 – 59917Combined sources
Helixi601 – 6088Combined sources
Helixi609 – 6168Combined sources
Helixi619 – 63214Combined sources
Helixi636 – 6449Combined sources
Helixi649 – 65911Combined sources
Helixi665 – 67612Combined sources
Helixi682 – 69211Combined sources
Helixi696 – 7049Combined sources
Helixi706 – 71712Combined sources
Beta strandi719 – 7213Combined sources
Helixi722 – 73413Combined sources
Turni735 – 7373Combined sources
Helixi741 – 7466Combined sources
Helixi754 – 77522Combined sources
Turni776 – 7794Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Z1WX-ray2.70A1-780[»]
1Z5HX-ray2.30A/B1-780[»]
3Q7JX-ray2.91A/B1-780[»]
ProteinModelPortaliO93655.
SMRiO93655. Positions 1-780.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO93655.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni230 – 2345Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the peptidase M1 family.Curated

Phylogenomic databases

eggNOGiarCOG02969. Archaea.
COG0308. LUCA.
HOGENOMiHOG000106482.
KOiK13722.
OMAiNDHISSP.

Family and domain databases

InterProiIPR024571. ERAP1-like_C_dom.
IPR001930. Peptidase_M1.
IPR014782. Peptidase_M1_N.
[Graphical view]
PANTHERiPTHR11533. PTHR11533. 1 hit.
PfamiPF11838. ERAP1_C. 1 hit.
PF01433. Peptidase_M1. 1 hit.
[Graphical view]
PRINTSiPR00756. ALADIPTASE.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O93655-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEVEKYDLTL DFDIQKRTFN GTETITADAG DIVLDAVGLQ INWMKVNGRD
60 70 80 90 100
TAFTYDGQTV RAPGDSQPQK IEISFAGKVS DSLSGIYYAG RENGMITTHF
110 120 130 140 150
EATDARRMFP CVDHPAYKAV FAITVVIDKD YDAISNMPPK RIEVSERKVV
160 170 180 190 200
EFQDTPRMST YLLYVGIGKF RYEYEKYRDI DLILASLKDI RSKYPLDMAR
210 220 230 240 250
KSVEFYENYF GIPYALPKMH LISVPEFGAG AMENWGAITF REIYMDIAEN
260 270 280 290 300
SAVTVKRNSA NVIAHEIAHQ WFGDLVTMKW WNDLWLNESF ATFMSYKTMD
310 320 330 340 350
TLFPEWSFWG DFFVSRTSGA LRSDSLKNTH PIEVDVRDPD EISQIFDEIS
360 370 380 390 400
YGKGASILRM IEDYAGYEEF RKGISKYLND HKFGNAEGSD LWTAIEDVSG
410 420 430 440 450
KPVKRVMEYW IKNPGYPVIK LKRNGRKITM YQTRFLLNGE EEGRWPVPVN
460 470 480 490 500
IKKKDGVERI LLEDEASIEA DGLIKINADS AGFYRVLYDD ATFSDVMGHY
510 520 530 540 550
RDLSPLDRIG LVDDLFAFLL SGHIDPETYR QRIRNFFDDE DHNVITAIVG
560 570 580 590 600
QMEYLRMLTH AFDDDARAFC RSRMQFLTGK QDENLKIALG RVSRLYVMVD
610 620 630 640 650
ESYAEEMSKL FKDFDSAEPE MRSSIATAYA LVTGDLKGLL EKFRSVDRDE
660 670 680 690 700
DRVRIISAFG KLKSNTDLST VYGMVEKTEI KKQDMISFFS SALETLPGRE
710 720 730 740 750
FIFANLDRII RLVIRYFTGN RTASRTVEMM IPVIGLDHPD AEDIVRNIGS
760 770 780
KNISMGLAKG IEMLAVNRKL VERIRQTAVK
Length:780
Mass (Da):89,380
Last modified:May 1, 1999 - v1
Checksum:iF499AB342BAB9218
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF081952 Genomic DNA. Translation: AAC98290.1.
AL445065 Genomic DNA. Translation: CAC11944.1.
PIRiT37456.
RefSeqiWP_010901227.1. NC_002578.1.

Genome annotation databases

EnsemblBacteriaiCAC11944; CAC11944; CAC11944.
GeneIDi1456360.
KEGGitac:Ta0815.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF081952 Genomic DNA. Translation: AAC98290.1.
AL445065 Genomic DNA. Translation: CAC11944.1.
PIRiT37456.
RefSeqiWP_010901227.1. NC_002578.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Z1WX-ray2.70A1-780[»]
1Z5HX-ray2.30A/B1-780[»]
3Q7JX-ray2.91A/B1-780[»]
ProteinModelPortaliO93655.
SMRiO93655. Positions 1-780.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi273075.Ta0815.

Protein family/group databases

MEROPSiM01.021.

Proteomic databases

PRIDEiO93655.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAC11944; CAC11944; CAC11944.
GeneIDi1456360.
KEGGitac:Ta0815.

Phylogenomic databases

eggNOGiarCOG02969. Archaea.
COG0308. LUCA.
HOGENOMiHOG000106482.
KOiK13722.
OMAiNDHISSP.

Miscellaneous databases

EvolutionaryTraceiO93655.

Family and domain databases

InterProiIPR024571. ERAP1-like_C_dom.
IPR001930. Peptidase_M1.
IPR014782. Peptidase_M1_N.
[Graphical view]
PANTHERiPTHR11533. PTHR11533. 1 hit.
PfamiPF11838. ERAP1_C. 1 hit.
PF01433. Peptidase_M1. 1 hit.
[Graphical view]
PRINTSiPR00756. ALADIPTASE.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The role of tricorn protease and its aminopeptidase-interacting factors in cellular protein degradation."
    Tamura N., Lottspeich F., Baumeister W., Tamura T.
    Cell 95:637-648(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165.
  2. "The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum."
    Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C., Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.
    Nature 407:508-513(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165.
  3. "Crystal structures of the tricorn interacting factor F3 from Thermoplasma acidophilum, a zinc aminopeptidase in three different conformations."
    Kyrieleis O.J., Goettig P., Kiefersauer R., Huber R., Brandstetter H.
    J. Mol. Biol. 349:787-800(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH ZINC IONS, COFACTOR.

Entry informationi

Entry nameiTRF3_THEAC
AccessioniPrimary (citable) accession number: O93655
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 1999
Last modified: December 9, 2015
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.