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TRI1

Gene
tri1
Protein
Tricorn protease homolog 1
Organism
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Length
1067 amino acids
Function
Degrades oligopeptides in a sequential manner.
Similarity
Belongs to the peptidase S41B family.
Mass
115.647 kDa
Sequence
MGVTQPAAPAYLRFPHPHGELVAFTAEDDVWLAPLDGGRAWRVSADNVPVNHPRISPDGTKVAWTSTRDGAPEVHVAPVEGGPAKRLTHWGSIRTQVRGWTADGRVLALSTYGQASLRRSWARALPLDGGPATTLPYGPVGDVAQGPHTVLLSAPMGREAAWWKRYRGGTAGKLWIDREDDGEFVRLHDGLDGNIEYPFWVGDRIAFLSDHEGTGALYSSLADGSDLRRHTPVDGFYARHAATDGSRVVYASAGELWTLDDLDGAEPRRLDIRLGGARVDLQSYPVNAARWFGSASPDHTARGSAVAVRGGVHWVTHRSGPARALAATPGVRNRLPRTFRVDGEEWVVWVTDAEGDDALEFAPATGLAPGATARRLAAGQLGRVLHLAVAPDGSRVAVASHDGRVLLVERESGEVREVDRSEDGDASGLVFSPDSSWLAWSHPGPEPLRQLKLANTTDLSVSEATPLRFKDYSPAFTLDGKHLAFLSTRSFDPVYDEHVFDLAFVEGARPYLITLAATTPSPFGPQRHGRPFETPDREETPDSEGTPTTRIDIEGLADRIVPFPVEAARYSRLRAAKDGVLWLRHPLTGVLGASRANPEDPDPNTELERYDLAQQRVEHLGGDADHFEVSGDGKRVLLWTDGRLKVVPSDRRASGDEDSDTNITVDLGRVRQTVEPAAEWRQMFDETGRIMRDHYWRADMNGVDWDGVLDRYRPVLDRVATHDDLVDLLWEVHGELGTSHAYVTPRGGHGSGARQGLLGADLSRHEDGAWRIDRVLPSETSDPDARSPLAAPGVAVRAGDAIVAVAGQAVDPVTGPGPLLVGTAGKPVELTVSPSGGGEVRHAVVVPLADEEPLRYHAWVADRRAYVHEKSGGRLGYLHVPDMQAPGWAQIHRDLRVEVAREGLVVDVRENRGGHTSQLVVEKLARRIVGWDLPRGMRPTSYPQDAPRGPVVAVANEFSGSDGDIVNAAIKALGIGPVVGVRTWGGVIGIDSRYRLVDGTLITQPKYAFWLEGYGWGVENHGVDPDVEVPQRPQDHAAGRDPQLDEAIALALAALEETPAKTPPSLP

Gene
TRI1
Protein
Cytochrome P450 monooxygenase TRI1
Organism
Fusarium sporotrichioides
Length
542 amino acids
Function
Cytochrome P450 monooxygenase; part of 2-gene cluster involved in trichothecene C-8 modification that mediates the biosynthesis of T2-toxin (PubMed:14690377, PubMed:12620849). The biosynthesis of trichothecenes begins with the cyclization of farnesyl diphosphate to trichodiene and is catalyzed by the trichodiene synthase TRI5 (PubMed:3800398). Trichodiene undergoes a series of oxygenations catalyzed by the cytochrome P450 monooxygenase TRI4 (PubMed:7651333). TRI4 controls the addition of four oxygens at C-2, C-3, C-11, and the C-12, C-13-epoxide to form the intermediate isotrichotriol (PubMed:16917519). Isotrichotriol then undergoes a non-enzymatic isomerization and cyclization to form isotrichodermol (PubMed:2317042). During this process, the oxygen at the C-2 position becomes the pyran ring oxygen and the hydroxyl group at C-11 is lost (PubMed:2317042). More complex type A trichothecenes are built by modifying isotrichodermol through a series of paired hydroxylation and acetylation or acylation steps (PubMed:11352533). Isotrichodermol is converted to isotrichodermin by the acetyltransferase TRI101 (PubMed:10583973). TRI101 encodes a C-3 transacetylase that acts as a self-protection or resistance factor during biosynthesis and that the presence of a free C-3 hydroxyl group is a key component of Fusarium trichothecene phytotoxicity (PubMed:10583973). A second hydroxyl group is added to C-15 by the trichothecene C-15 hydroxylase TRI11, producing 15-decalonectrin, which is then acetylated by TRI3, producing calonectrin (PubMed:9435078, PubMed:8593041). A third hydroxyl group is added at C-4 by the cytochrome P450 monooxygenase TRI13, converting calonectrin to 3,15-diacetoxyspirpenol, which is subsequently acetylated by the acetyltransferase TRI7 (PubMed:12135578, PubMed:11352533). A fourth hydroxyl group is added to C-8 by the cytochrome P450 monooxygenase TRI1, followed by the addition of an isovaleryl moiety by TRI16 (PubMed:12620849, PubMed:14532047). Finally, the acetyl group is removed from the C-3 position by the trichothecene C-3 esterase TRI8 to produce T-2 toxin (PubMed:12039755).
Similarity
Belongs to the cytochrome P450 family.
Mass
62.613 kDa
Sequence
MSKVDKTGYAQWVYLLPERSSMMSFIDSMEDFRFDMLIYFLCFVVLGRAVQWFLRPKPNAPLLNPRRFFEFSDSRAVSEILYSTRQVLEDWFSKYPTKPMRIIADLGQITILPPSMADEIKNDPRLSFIKASTESAFHITIPGFEPFREGAKNEAGLIKNVLHKHLNKTLNHITTPLAEETCLAVQEYFGSDQGWHKVPLRDTLVPLVTRISTRIFLGQDLCRNQEWLRIAASYSSTSAEVANHLRRWPKPLRYLVSLLSPECQNLAKQVRNARALINPILERRRVEEGQEKGTSYNDSLEWFERYAREAYDPAATQLFLSVVSIHTTTDLLCQALEDISSHPEIIKPLQHEIREVLKQEGWNTKALYKMKLLDSVLKESQRLKPVQHATMLRLALEDITLEDGTFIPKGHQISVSCHAMRDNEIYENASSWDGYRYYRQREQSANEHKAQLSSTSPEHMGFGYGIHVCPGRFFAANEVKVIMIYLLLQYEWRTPPGSQPKPLSWCTTWATDPTFELEVRRKGSDDIPVELSHNTFSRESES

Gene
tri1
Protein
ADP-ribosylarginine hydrolase Tri1
Organism
Pseudomonas putida (strain DSM 28064 / B6-2)
Length
382 amino acids
Function
Orphan immunity component of an interbacterial competition system (also called effector-immunity systems); this bacteria does not encode an identifiable cognate effector protein. Expression of this protein in E.coli partially protects the cells against competition by wild-type S.proteamaculans (PubMed:30343895). Probably acts as an arginine mono-ADP-ribosylhydrolase, mediating the removal of mono-ADP-ribose attached to arginine residues on proteins. Probably de-ADP-ribosylates FtsZ and possibly other proteins (Probable).
Similarity
Belongs to the ADP-ribosylglycohydrolase family.
Mass
41.685 kDa
Sequence
MDESNLLQGISMIDLRSPDAILSDYAKRYAHLLPELSPQLQQRMAYMPEPDAPRLPLTKPAWLSDRSCTLTPGQAIDRAQGALLGLAIGDAVGTTLEFRRRDQGQVSDMVGGGPFRLAPGEWTDDTSMALCLADTYASQGKFDFATFADAMVRWYRQGENSANGRCFDIGNVTRRALEGWEAQGLAWMGNLEASTAGNGSLIRLAPTAIFRRHSLSATWWESVTQSSVTHRAIEVSECCKLFGAQLHLALNGADKEEALSPKVRPLQPRALIINAGEYKHKTREQIRSSGYVVDTLEAALWAVWNTDNFRDAILLAANLADDADSVAATAGQIAGALYGVSGMPPEWVAKVAWSRHICELASRLFELAPQGDEMDELLSGSE

Gene
tri1
Protein
ADP-ribosylarginine hydrolase Tri1
Organism
Pseudomonas putida (strain GB-1)
Length
371 amino acids
Function
Immunity component of an interbacterial competition system (also called effector-immunity systems). Expression in E.coli neutralizes the toxic effects of non-cognate S.proteamaculans effector protein Tre1 (Tre1-Sp); cannot be co-purified with Tre1-Sp from E.coli, suggesting they do not form a stable complex (PubMed:30343895). Probably acts as an arginine mono-ADP-ribosylhydrolase, mediating the removal of mono-ADP-ribose attached to arginine residues on proteins. Probably de-ADP-ribosylates FtsZ and possibly other proteins; the ability to hydrolyze ADP-ribosyl moities is not essential for neutralization of its cognate toxin, strongly suggesting its N-terminal extension occludes the active site of cognate toxin Tre1 (Probable).
Similarity
Belongs to the ADP-ribosylglycohydrolase family.
Mass
40.782 kDa
Sequence
MIDLRSPNALLSDYVERYAHLSPEPSRQLQQRMDYNVRADAPAEPASKPRWLQSRACTLTPEQALDRAKGALLGLAIGDAVGTTLEFLPRDREHVNDMVGGGPFRLAAGEWTDDTSMALCLADTYVSQGKFDYATYANALVRWYRHGENSVNGRCFDIGNATRNALEGWLREGIGWQGNYDPSTAGNGSIIRLAPTAIFRRHSLSASWWESVTQSSVTHNADEAVNCCQLLAAQLHLALNGADKEETLAPAVRSLRPRPMIINAGEYKQKSRDQIRSSGYVVDTLEAALWAVWNSNNFHDAILLAANLADDADSVAATAGQLAGALYGVSGMPPEWVEKVAWSQHIQKLAQELFDRAPQVDELDALLYGKR

Gene
tri1
Protein
ADP-ribosylarginine hydrolase Tri1
Organism
Serratia proteamaculans (strain 568)
Length
366 amino acids
Function
Immunity component of a contact-dependent interbacterial competition system (also called effector-immunity systems). Acts as an arginine mono-ADP-ribosylhydrolase, mediating the removal of mono-ADP-ribose attached to arginine residues on proteins. De-ADP-ribosylates FtsZ, is able to act on other proteins as well. Neutralizes the toxic activity of cognate toxin Tre1-Sp. Expression of this protein alone in E.coli partially protects the cells against competition by wild-type S.proteamaculans. Neutralizes Tre1-Sp both by occluding its active site via its N-terminal extension and by hydrolyzing the ADP-ribosyl moiety from FtsZ; the 2 activites are dissociable by mutagenesis.
Similarity
Belongs to the ADP-ribosylglycohydrolase family.
Mass
40.934 kDa
Sequence
MIDLREDTWTLQLYAQRYKGLSPKNSRELQLRMEYDPLKPNLPTSGEEQNSKPEWLNTPPCLIPESESLDKAKGALVGLAIGDAIGTTLEFLPRDKLHVNDMVGGGPFRLQPGEWTDDTSMALCLAESYISAGRLDITLFREKLVRWYRHGENSSNGRCFDIGNTTRNALEQYLKHGASWFGNTEPETAGNAAIIRQAPTSIFRRKSLQRTFADSDSQSMATHCAPESMASCQFLGFILNYLINGSSREKAFSPHVMPLPVRVLLINAGEYKEKKRDEIRSSGYVIDTLEAAMWAVWNTDNFHDAILLAANLGDDADSVAATTGQIAGALYGYSNIPKPWLDKLVQQERISNLAEQLFYMAPEEDF

Gene
TRI1
Protein
Protein TRI1
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Length
226 amino acids
Function
May be involved in transcription regulation.
Mass
26.471 kDa
Sequence
MADINKYIPMVDAILSVSNPDEISPKRVRKALQILYSVNLDSQRKLINELILERFGDIQENPRVLIPKNDLISRDQELSLRLQKEEERPLRSTRKRKGKSESKSKRKKKKNDSPDSNSISVRKVLLSAPLQKFLGSEELPRTQVVKMIWQYIKEHDLQNPKDRREILCDEKMEPIFGKKMTMFSMNKLLTKHLFNPDEIVKHEEEQKQTPEKEIKLENESLPNLSG