Family Search for PF20238 (BIM1-like_dom)
PF20238 hits 38 sequences in PaperBLAST's database above the trusted cutoff. Showing hits to curated sequences only. Or see all hits or try another family.
X325_EMENI / Q5B428 Lytic polysaccharide monooxygenase-like protein ANIA_04702; LPMO-like protein ANIA_04702; X325 family protein ANIA_04702 from Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) (see paper)
Aligns to 22:201 / 244 (73.8%), covers 99.3% of PF20238, 105.2 bits
- function: Lytic polysaccharide monooxygenase-like protein that has diverged to biological functions other than polysaccharide degradation since it does not perform oxidative cleavage of polysaccharides (PubMed:37452022). Acts as a cell surface-bound protein that functions in the copper-accumulation pathway (By similarity). May also act as the major cell wall sensor that regulates MAP kinase-dependent hyphal anastomosis, the fusion of hyphal cells (By similarity).
cofactor: Cu(2+) (Binds 1 copper ion per subunit.)
X325_WAIAR / A0A4P9I8G4 Lytic polysaccharide monooxygenase-like protein X325; LPMO-like protein X325; X325 family protein from Waitea arvalis (Laetisaria arvalis) (see paper)
Aligns to 19:170 / 238 (63.9%), covers 100.0% of PF20238, 104.9 bits
- function: Lytic polysaccharide monooxygenase-like protein that has diverged to biological functions other than polysaccharide degradation since it does not perform oxidative cleavage of polysaccharides (PubMed:31932718). Acts as a cell surface-bound protein that functions in the copper-accumulation pathway (By similarity). May also act as the major cell wall sensor that regulates MAP kinase-dependent hyphal anastomosis, the fusion of hyphal cells (By similarity).
cofactor: Cu(2+) (Binds 1 copper ion per subunit.)
X325_LACBS / B0CPC6 Lytic polysaccharide monooxygenase-like protein X325; LPMO-like protein X325; X325 family protein from Laccaria bicolor (strain S238N-H82 / ATCC MYA-4686) (Bicoloured deceiver) (Laccaria laccata var. bicolor) (see paper)
Aligns to 20:163 / 206 (69.9%), covers 99.3% of PF20238, 104.4 bits
- function: Lytic polysaccharide monooxygenase-like protein that has diverged to biological functions other than polysaccharide degradation since it does not perform oxidative cleavage of polysaccharides (PubMed:31932718). Involved in fungal-cell-wall remodeling during Laccaria-Populus symbiosis (PubMed:31932718). Acts as a cell surface- bound protein that functions in the copper-accumulation pathway (By similarity). May also act as the major cell wall sensor that regulates MAP kinase-dependent hyphal anastomosis, the fusion of hyphal cells (By similarity).
cofactor: Cu(2+) (Binds 1 copper ion per subunit.)
X325_NEUCR / V5IRP6 Lytic polysaccharide monooxygenase-like protein ham-7; LPMO-like protein ham-7; Hyphal anastamosis protein 7; X325 family protein ham-7 from Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) (see 3 papers)
Aligns to 16:183 / 229 (73.4%), covers 100.0% of PF20238, 103.2 bits
- function: Lytic polysaccharide monooxygenase-like protein that has diverged to biological functions other than polysaccharide degradation since it does not perform oxidative cleavage of polysaccharides (Probable). Acts as the major cell wall sensor that regulates MAK-1- dependent hyphal anastomosis, the fusion of hyphal cells (PubMed:21666072, PubMed:22879952, PubMed:25279949). May also act as a cell surface-bound protein that functions in the copper-accumulation pathway (By similarity).
cofactor: Cu(2+) (Binds 1 copper ion per subunit.)
disruption phenotype: Leads to alteration in cell fusion between conidial anastomosis tubes (PubMed:21666072). Displays reduced basal MAK-1 activity (PubMed:22879952, PubMed:25279949).
X325_YARLI / Q6C0J1 Lytic polysaccharide monooxygenase-like protein X325; LPMO-like protein X325; X325 family protein from Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica) (see paper)
Aligns to 16:160 / 261 (55.6%), covers 100.0% of PF20238, 101.0 bits
- function: Lytic polysaccharide monooxygenase-like protein that has diverged to biological functions other than polysaccharide degradation since it does not perform oxidative cleavage of polysaccharides (PubMed:31932718). Acts as a cell surface-bound protein that functions in the copper-accumulation pathway (By similarity).
cofactor: Cu(2+) (Binds 1 copper ion per subunit.)
X325_PODAN / A0A090CRQ9 Lytic polysaccharide monooxygenase-like protein X325; LPMO-like protein X325; X325 family protein from Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383) (Pleurage anserina) (see paper)
Aligns to 20:159 / 229 (61.1%), covers 99.3% of PF20238, 99.6 bits
- function: Lytic polysaccharide monooxygenase-like protein that has diverged to biological functions other than polysaccharide degradation since it does not perform oxidative cleavage of polysaccharides (PubMed:31932718). Acts as a cell surface-bound protein that functions in the copper-accumulation pathway (By similarity). May also act as the major cell wall sensor that regulates MAP kinase-dependent hyphal anastomosis, the fusion of hyphal cells (By similarity).
cofactor: Cu(2+) (Binds 1 copper ion per subunit.)
X325_CRYNH / J9VHN6 Copper acquisition factor BIM1; BCS-inducible membrane protein 1; Copper binding and release protein 1; Lytic polysaccharide monooxygenase-like protein BIM1; LPMO-like protein BIM1; X325 family protein BIM1 from Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii) (see 2 papers)
Aligns to 18:166 / 218 (68.3%), covers 97.9% of PF20238, 97.4 bits
- function: Lytic polysaccharide monooxygenase-like protein that has diverged to biological functions other than polysaccharide degradation since it does not perform oxidative cleavage of polysaccharides (Probable). Cell surface-bound protein that functions in the copper- accumulation pathway shared by the CUF1-dependent copper transporter CTR1 (PubMed:31932719, PubMed:35737716). Involved in maintaining cell wall integrity during copper deficiency (PubMed:35737716). Binds Cu(2+) with an estimated 1:1 stoichiometry and might serve as an extracellular copper ligand (PubMed:31932719). FRE4 and FRE7 metalloreductases probably function together with CTR1 and BIM1 to liberate the Cu(2+) bound to the BIM1 copper-binding site for subsequent import of Cu(+) into the cell by CTR1, via the reduction of BIM1-bound Cu(2+) to Cu(+) to reduce binding affinity for BIM1 but increase affinity for CTR1 (PubMed:31932719). Facilitates copper acquisition in the brain of mammalian hosts and acts as a copper-dependent virulence trait in fungal meningitis (PubMed:31932719). While BIM1 plays a critical role in cryptococcal meningitis, at least in part through its role in copper acquisition, it could play additional roles during copper limitation or as a means to invade and colonize host tissues in the brain, by compromising host carbohydrate integrity via its lytic polysaccharide monooxygenase (LPMO) activity, which has still to be determined (PubMed:31932719).
cofactor: Cu(2+) (Binds 1 copper ion per subunit.)
subunit: Interacts with the CUF1-dependent copper transporter CTR1.
disruption phenotype: Exhibits growth defect on copper-deficient medium ot in the presence of the copper-specific chelator bathocuproine disulfonic acid (BCS) (PubMed:31932719). Shows a reduction in cell- associated copper, in the enzymatic activity of Cu/Zn superoxide dismutase, in laccase-dependent melanin production and in the accumulation of cellular iron, a well-established copper-dependent process (PubMed:31932719). Shows a distinct cell wall electron density pattern, which is not due to overall difference in cell associated copper levels or copper adsorption ability (PubMed:35737716). Leads to a reduction in the inner cell wall chito-oligomer layer when exposed to copper-deficiency (PubMed:35737716). Does not affect virulence in an A/J mouse pulmonary infection model (PubMed:31932719).
Or search for genetic data about PF20238 in the Fitness Browser
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory