Family Search for PF11578 (DUF3237)
April 2024: See Interactive Tools for Functional Annotation of Bacterial Genomes for advice on using these tools.
PF11578 hits 17 sequences in PaperBLAST's database above the trusted cutoff. Showing all hits. Or show only hits to curated sequences or try another family.
A1S_1106 hypothetical protein from Acinetobacter baumannii ATCC 17978
Aligns to 28:177 / 178 (84.3%), covers 99.3% of PF11578, 169.5 bits
Saro_1721 hypothetical protein from Novosphingobium aromaticivorans DSM 12444
Aligns to 30:177 / 178 (83.1%), covers 100.0% of PF11578, 165.1 bits
blr7842 blr7842 from Bradyrhizobium japonicum USDA 110
Aligns to 5:151 / 152 (96.7%), covers 98.7% of PF11578, 153.7 bits
CAC3321 Uncharacterized protein homolog of yveG B.subtilis from Clostridium acetobutylicum ATCC 824
Aligns to 9:157 / 158 (94.3%), covers 98.7% of PF11578, 152.9 bits
RPA1785 conserved hypothetical protein from Rhodopseudomonas palustris CGA009
Aligns to 3:152 / 153 (98.0%), covers 98.7% of PF11578, 150.7 bits
An08g03600 uncharacterized protein from Aspergillus niger
Aligns to 5:174 / 177 (96.0%), covers 100.0% of PF11578, 142.6 bits
AFUA_6G02870, XP_747789 conserved hypothetical protein from Aspergillus fumigatus Af293
Aligns to 246:398 / 399 (38.3%), covers 100.0% of PF11578, 142.3 bits
- Anti-Aspergillus Activities of the Respiratory Epithelium in Health and Disease
Bertuzzi, Journal of fungi (Basel, Switzerland) 2018 - “...identified the metalloprotease designated as MEP (or AFUA_8G07080), and another two uncharacterised proteins, AFUA_1G11480 and AFUA_6G02870, as putative mediators of A. fumigatus spore binding to the respiratory epithelium via the adhesion molecule E-cadherin although this hypothesis remains to be substantiated [ 30 , 31 , 32...”
- Important factors mediates the adhesion of aspergillus fumigatus to alveolar epithelial cells with E-cadherin
Xu, American journal of translational research 2016 - “...of mice against aspergillus fumigates. Mass spectrometry (MS) analysis indicated the following proteins AFUA_8G07080, AfA24A6.130c, XP_747789 can bind to E-cadherin. In conclusion, E-cadherin is a receptor for adhesion of A. fumigatus blastospores in epithelial cells. This may open a new approach to treat this fungal infection....”
- E-cadherin mediates adhesion of Aspergillus fumigatus to non-small cell lung cancer cells
Yan, Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine 2015 (PubMed)- “...for E-cadherin on A. fumigatus, AfA24A6.130c and XP_747789. Finally, the growth of E-cadherin-depleted A549 cells significantly increased by infection of A....”
Q0D146 Uncharacterized protein from Aspergillus terreus (strain NIH 2624 / FGSC A1156)
Aligns to 5:181 / 184 (96.2%), covers 99.3% of PF11578, 131.4 bits
Ccel_1655 DUF3237 family protein from Ruminiclostridium cellulolyticum H10
Ccel_1655 cellulosome protein dockerin type I from Clostridium cellulolyticum H10
2 alignments in 142:393 / 435 (49.7%), covering up to 96.6% of PF11578, 128.9 bits
NCU03313 hypothetical protein from Neurospora crassa OR74A
Aligns to 4:166 / 169 (96.4%), covers 100.0% of PF11578, 124.5 bits
AFUA_1G11480 conserved hypothetical protein from Aspergillus fumigatus Af293
Q4WSV7 Uncharacterized protein from Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293)
Aligns to 7:184 / 187 (95.2%), covers 81.9% of PF11578, 111.5 bits
- Anti-Aspergillus Activities of the Respiratory Epithelium in Health and Disease
Bertuzzi, Journal of fungi (Basel, Switzerland) 2018 - “...E-cadherin recently identified the metalloprotease designated as MEP (or AFUA_8G07080), and another two uncharacterised proteins, AFUA_1G11480 and AFUA_6G02870, as putative mediators of A. fumigatus spore binding to the respiratory epithelium via the adhesion molecule E-cadherin although this hypothesis remains to be substantiated [ 30 , 31...”
- Interplay between Gliotoxin Resistance, Secretion, and the Methyl/Methionine Cycle in Aspergillus fumigatus
Owens, Eukaryotic cell 2015 - “...3.99E02 6 2 2 38.3 17.7 9.1 AFUA_3G14540 AFUA_6G02450 AFUA_1G11480 1.053 2.33E04 21 60.3 AFUA_2G01010 1.051 9.37E03 11 27.6 AFUA_4G14000 Data are sorted by fold...”
- The proteomic signature of Aspergillus fumigatus during early development
Cagas, Molecular & cellular proteomics : MCP 2011 - “...AFUA_3G08380 AFUA_4G13120 AFUA_4G07710 AFUA_5G09230 AFUA_1G11480 AFUA_3G11070 AFUA_6G06750 AFUA_3G14490 AFUA_5G02910 AFUA_6G01940 AFUA_4G08240 AFUA_8G00630...”
- “...AFUA_6G11620 AFUA_4G07360 AFUA_6G02280 AFUA_2G11060 AFUA_1G11480 AFUA_7G00250 AFUA_1G13500 AFUA_3G11690 AFUA_6G12720 AFUA_1G11130 AFUA_5G05450 AFUA_2G02150...”
- The proteomic signature of Aspergillus fumigatus during early development
Cagas, Molecular & cellular proteomics : MCP 2011 - “...21 kDa 15 kDa 33 kDa UniProt ID Q9UVW1 Q4WSV7 Q4WM42 Q4WZQ9 Q4WEX7 Q4WJV5 Q4WEV9 Q4WXF4 Q4WP49 Q4WD81 Q8NKF4 Q4X1G7 Molecular & Cellular Proteomics 10.11 Q4WWT1...”
- “...Q4WN39 Q4WTX0 Q4WYW4 Q4WJV9 Q4WM07 Q4WNY2 O43099 Q4X164 Q4WSV7 Q4WA70 (1) Q4WSA0 Q4WY39 Q4WLQ2 Q4WSZ2 Q4WTM9 Q4WIE3 Q4WZH8 Q4WMV5 Q4W9S8 Molecular & Cellular...”
CPAR2_109010 uncharacterized protein from Candida parapsilosis
Aligns to 15:180 / 181 (91.7%), covers 99.3% of PF11578, 91.9 bits
PGUG_00755 uncharacterized protein from Meyerozyma guilliermondii ATCC 6260
Aligns to 17:180 / 184 (89.1%), covers 98.7% of PF11578, 87.3 bits
- The Possible Mechanisms Involved in Degradation of Patulin by Pichia caribbica
Zheng, Toxins 2016 - “...protein gi|146416825 44,146 5.33 Meyerozyma guilliermondii ATCC 6260 280 13 4 Unclassified 24 Hypothetical protein PGUG_00755 gi|146422888 20,317 5.45 Meyerozyma guilliermondii ATCC 6260 84 6 1 Unclassified 25 Hypothetical protein PGUG_04067 gi|146414736 34,234 6.64 Meyerozyma guilliermondii ATCC 6260 104 11 3 Unclassified 24 Hypothetical protein PGUG_03175...”
PSPTO3575 hypothetical protein from Pseudomonas syringae pv. tomato str. DC3000
Q87Z56 DUF3237 domain-containing protein from Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000)
Aligns to 22:171 / 173 (86.7%), covers 99.3% of PF11578, 85.4 bits
- Novel virulence gene of Pseudomonas syringae pv. tomato strain DC3000
Preiter, Journal of bacteriology 2005 - “...The accession numbers for DC3000 ORFs are PSPTO3575 (Q87Z56), PSPTO3577 (Q87Z54), and PSPTO3578 (Q87Z53) (9). Accession numbers for hypothetical TetR-like...”
- “...for possible clues to the function of TvrR. PSPTO3575, the divergently transcribed ORF upstream of tvrR, is predicted to encode a 173-amino-acid protein which...”
- Novel virulence gene of Pseudomonas syringae pv. tomato strain DC3000
Preiter, Journal of bacteriology 2005 - “...accession numbers for DC3000 ORFs are PSPTO3575 (Q87Z56), PSPTO3577 (Q87Z54), and PSPTO3578 (Q87Z53) (9). Accession numbers for hypothetical TetR-like proteins...”
- “...(pTvrR) is indicated by the double-headed arrow. PSPTO3575 (Q87Z56) is predicted to encode a 173-aminoacid protein of unknown function. PSPTO3577 (Q87Z54) is...”
ORF7_PENRF / W6Q4S2 PR-toxin biosynthesis cluster protein 7 from Penicillium roqueforti (strain FM164) (see 6 papers)
Aligns to 12:182 / 186 (91.9%), covers 94.0% of PF11578, 82.6 bits
- function: Part of the gene cluster that mediates the biosynthesis of PR-toxin, a bicyclic sesquiterpene belonging to the eremophilane class and acting as a mycotoxin (PubMed:24239699, PubMed:27921136). The first step of the pathway is catalyzed by the aristolochene synthase which performs the cyclization of trans,trans-farnesyl diphosphate (FPP) to the bicyclic sesquiterpene aristolochene (PubMed:8440737, PubMed:15186158, PubMed:24239699). Following the formation of aristolochene, the non-oxygenated aristolochene is converted to the trioxygenated intermediate eremofortin B, via 7-epi-neopetasone (PubMed:24239699, PubMed:26274339). This conversion appears to involve three enzymes, a hydroxysterol oxidase-like enzyme, the quinone-oxidase prx3 that forms the quinone-type-structure in the bicyclic nucleus of aristolochene with the C8-oxo group and the C-3 hydroxyl group, and the P450 monooxygenase ORF6 that introduces the epoxide at the double bond between carbons 1 and 2 (PubMed:24239699, PubMed:27921136). No monoxy or dioxy-intermediates have been reported to be released to the broth, so these three early oxidative reactions may be coupled together (PubMed:24239699). Eremofortin B is further oxidized by another P450 monooxygenase, that introduces a second epoxide between carbons 7 and 11 prior to acetylation to eremofortin A by the acetyltransferase ORF8 (PubMed:16345540, PubMed:24239699, PubMed:27921136). The second epoxidation may be performed by a second P450 monooxygenase (PubMed:24239699). After the acetylation step, eremofortin A is converted to eremofortin C and then to PR-toxin (PubMed:24239699). First the conversion of eremofortin A to eremofortin C proceeds by oxidation of the side chain of the molecule at C-12 and is catalyzed by the short-chain oxidoreductase prx1 (PubMed:16345540, PubMed:24239699). The cytochrome P450 monooxygenase ORF6 is probably also involved in this step (PubMed:27921136). The primary alcohol formed at C-12 is finally oxidized by the short-chain alcohol dehydrogenase prx4 that forms PR-toxin (PubMed:16345540, PubMed:24239699).
Psyr_3346 hypothetical protein from Pseudomonas syringae pv. syringae B728a
Aligns to 22:171 / 173 (86.7%), covers 99.3% of PF11578, 82.6 bits
PHNH_PENHR / A0A1S6PUA4 Hydroalkoxylation enzyme phnH; Phenalenone biosynthesis cluster protein H; EC 4.-.-.- from Penicillium herquei (see 2 papers)
Aligns to 24:145 / 149 (81.9%), covers 56.4% of PF11578, 55.3 bits
- function: Hydroalkoxylation enzyme; part of the gene cluster that mediates the biosynthesis of phenalenones such as herqueinone, compounds that have been reported to treat tumors, bacterial infections and/or mycoses, and rheumatic diseases (PubMed:26978228). The non- reducing polyketide synthase phnA synthesizes the heptaketide backbone and cyclizes it into the angular, hemiketal-containing naphtho-gamma- pyrone prephenalenone. The product template (PT) domain of phnA catalyzes only the C4-C9 aldol condensation, which is unprecedented among known PT domains (PubMed:28240554, PubMed:26978228). The transformation of prephenalenone to phenalenones requires an FAD- dependent monooxygenase phnB, which catalyzes the C2 aromatic hydroxylation of prephenalenone and ring opening of the gamma-pyrone ring simultaneously (PubMed:28240554, PubMed:26978228). Subsequent intramolecular deprotonation of C3 phenolic oxygen accelerates phenalenone ring closure to yield the tricyclic phenalenone core with a C2 hydroxylation (PubMed:28240554, PubMed:26978228). The prenyltransferase phnF further catalyzes reverse C-prenylation of phenalenone by direct electrophilic substitution at C6, or possibly via first a forward O-prenylation of a neighboring phenol in phenalenone, followed by a Claisen rearrangement (PubMed:28240554). The hydroalkoxylation enzyme phnH catalyzes the 5-exo-trigcyclization via acid catalysis after the spontaneous deprotonation of 7-OH, which leads to the formation of the dihydrobenzofuran atrovenetin (PubMed:28240554). Atrovenetin is further converted to deoxyherqueinone by the O-methyltransferase phnC which can methylate C2-OH to stabilize the northern portion of the phenalenone core (PubMed:28240554). Finally, the oxidoreductase phnG converts deoxyherqueinone to herqueinone via C6 hydroxylation (PubMed:28240554).
catalytic activity: 2,4,7,9-tetrahydroxy-6-methyl-8-(2-methylbut-3-en-2-yl)-1-oxo- 1H-phenalen-3-ol = (2'R)-atrovenetin (RHEA:62660)
Or search for genetic data about PF11578 in the Fitness Browser
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory