Family Search for PF11999 (Ice_binding)
April 2024: See Interactive Tools for Functional Annotation of Bacterial Genomes for advice on using these tools.
PF11999 hits 15 sequences in PaperBLAST's database above the trusted cutoff. Showing all hits. Or show only hits to curated sequences or try another family.
YP_523138 Ig-like, group 2 from Rhodoferax ferrireducens DSM 15236
Aligns to 318:524 / 526 (39.4%), covers 100.0% of PF11999, 252.0 bits
YP_676864 CHU large protein; antifreeze-related protein from Cytophaga hutchinsonii ATCC 33406
Aligns to 163:366 / 368 (55.4%), covers 99.5% of PF11999, 247.7 bits
ZP_01462925 antifreeze protein from Stigmatella aurantiaca DW4/3-1
Aligns to 281:469 / 473 (40.0%), covers 99.5% of PF11999, 225.3 bits
YP_749708 Ig-like, group 2 from Shewanella frigidimarina NCIMB 400
Aligns to 271:480 / 486 (43.2%), covers 100.0% of PF11999, 221.4 bits
YP_944155 hypothetical protein from Psychromonas ingrahamii 37
Aligns to 44:243 / 258 (77.5%), covers 100.0% of PF11999, 219.4 bits
IBP_LEUSY / C7F6X3 Ice-binding protein; Antifreeze protein; AFP; LeIBP from Leucosporidium sp. (strain AY30) (Arctic yeast) (see 6 papers)
Aligns to 36:241 / 261 (78.9%), covers 100.0% of PF11999, 212.6 bits
- function: Confers freeze tolerance. Binds to the surface of ice crystals and inhibits their growth. Has low thermal hysteresis (TH) activity, which is the ability to lower the freezing point of an aqueous solution below its melting point (PubMed:24699650, PubMed:22303017, PubMed:20067781, PubMed:22426061, PubMed:23203635, PubMed:22622645). The TH activity of this protein is approximately 0.2 degrees Celsius at 50 uM and 0.3 degrees Celsius at 400 uM (PubMed:24699650).
subunit: Homodimer (PubMed:22426061, PubMed:24699650, PubMed:22303017). Dimerization is not required for the thermal hysteresis (TH) activity (PubMed:22303017). - Convergent evolution and horizontal gene transfer in Arctic Ocean microalgae
Dorrell, Life science alliance 2023 - “...from Antarctic sea ice ( 62 , 63 ). Closely related was the patented sequence C7F6X3 of an IBP derived from Leucosporidium AY30 that was originally isolated from Svalbard ( 64 ). A third Basidiomycota IBP was from Typhula ishikariensis . T. ishikariensis is a snow...”
IBPKB_TYPIS / Q76CE6 Ice-binding protein K3-B1; Antifreeze protein 6; AFP6; TAFP-2; TisAFP6 from Typhula ishikariensis (Gray snow mold fungus) (see 2 papers)
Aligns to 36:241 / 243 (84.8%), covers 99.5% of PF11999, 210.8 bits
- function: Binds to the surface of ice crystals. Has low thermal hysteresis (TH) activity, which is the ability to lower the freezing point of an aqueous solution below its melting point (PubMed:22645341). The TH activity of this protein is approximately 0.3 degrees Celsius at 11 mM (PubMed:27613857).
- Whole-genome sequence and mass spectrometry study of the snow blight fungus Phacidium infestans (Karsten) DSM 5139 growing at freezing temperatures
Zerouki, Molecular genetics and genomics : MGG 2023 - “...32% shared identity with the antifreeze protein K3-B1 in the gray snow mold Typhula ishikariensis (Q76CE6). This enzyme binds to the surface of ice crystals and lowers the freezing point of an aqueous solution (Cheng et al. 2016 ). The phylogenetic analyses of the IBPs encoded...”
IBP_FLAFP / H7FWB6 Ice-binding protein; Antifreeze protein; AFP; FfIBP from Flavobacterium frigoris (strain PS1) (see 3 papers)
Aligns to 75:273 / 276 (72.1%), covers 100.0% of PF11999, 209.1 bits
- function: Has antifreeze activity for survival in a subzero environment. Binds to the surface of ice crystals and inhibits their growth. Has high thermal hysteresis (TH) activity, which is the ability to lower the freezing point of an aqueous solution below its melting point, and thus the freezing of the cell fluid can be prevented protecting the organism from ice damage (PubMed:22750870, PubMed:24699650, PubMed:27737617). The TH activity of this protein is 2.2 degrees Celsius at 5 uM and 2.5 degrees Celsius at 50 uM (PubMed:24699650).
subunit: Monomer. - Structure and application of antifreeze proteins from Antarctic bacteria
Muñoz, Microbial cell factories 2017 - “...: Figure S1), which decreases to 37 when amino acid sequences of 4NU3 (Uniprot entry: H7FWB6) and 3WP9 (Uniprot entry: A5XB26) are included in the alignment (Fig. 3 a). Motifs of regularly spaced-threonines T-x-x-T and T-x-T are present in the predicted -strands (Fig. 3 a). Fig.3...”
IBP_COLSX / A5XB26 Ice-binding protein; Antifreeze protein; AFP from Colwellia sp. (see 2 papers)
Aligns to 43:242 / 253 (79.1%), covers 100.0% of PF11999, 208.9 bits
- function: Binds to the surface of ice crystals and inhibits their growth (PubMed:17651136, PubMed:24938370). Has ice recrystallization inhibition (RI) activity (the ability to prevent the formation of larger grains of ice at the expense of smaller grains), which may protect membranes from freezing injury (Probable). Has high thermal hysteresis (TH) activity, which is the ability to lower the freezing point of an aqueous solution below its melting point, and thus the freezing of the cell fluid can be prevented protecting the organism from ice damage. The TH activity of this protein is 3.8 degrees Celsius at 14 mM (PubMed:24938370).
- Structure and application of antifreeze proteins from Antarctic bacteria
Muñoz, Microbial cell factories 2017 - “...to 37 when amino acid sequences of 4NU3 (Uniprot entry: H7FWB6) and 3WP9 (Uniprot entry: A5XB26) are included in the alignment (Fig. 3 a). Motifs of regularly spaced-threonines T-x-x-T and T-x-T are present in the predicted -strands (Fig. 3 a). Fig.3 Cartoon representations of AFP models...”
ZP_01118128 hypothetical protein from Polaribacter irgensii 23-P
Aligns to 64:263 / 265 (75.5%), covers 100.0% of PF11999, 207.3 bits
- Marine Antifreeze Proteins: Structure, Function, and Application to Cryopreservation as a Potential Cryoprotectant
Kim, Marine drugs 2017 - “...In addition, uncharacterized proteins similar to IBPs were found in sea ice bacteria Polaribacter irgensii (ZP_01118128; sequence identity: 61%, sequence similarity: 75%), Psychromonas ingrahamii (ZP_01349469; sequence identity: 59%, sequence similarity: 71%), and marine bacterium Shewanella frididimarina (YP_749708; sequence identity: 52%, sequence similarity: 69%). The first bacterial...”
- Possible role of horizontal gene transfer in the colonization of sea ice by algae
Raymond, PloS one 2012 - “...genome contains a putative 27.5 kDa IBP gene with a probable signal peptide (acc. no. ZP_01118128). Although this strain was obtained from the water column, another strain of P. irgensii was obtained from the bottom of an ice core in Antarctic sea ice [48] . Another...”
- Evolution of antifreeze protein genes in the diatom genus fragilariopsis: evidence for horizontal gene transfer, gene duplication and episodic diversifying selection
Sorhannus, Evolutionary bioinformatics online 2011 - “...Rhodoferax ferrireducens YP_523138 AF435948 Stigmatella aurantiaca ZP_01462925 GU207882 Bacterioidetes Cytophaga hutchinsonii YP_676864 AB517710 Polaribacter irgensii ZP_01118128 EU000226 Marivirga tractuosa YP_004052221 CP002349 Bacillariophyta Fragilariopsis curta GQ265833 GQ265834 GQ265835 GQ265836 GQ265838 GQ265837 GQ265839 GQ265840 Bacillariophyta Fragilariopsis curta GQ265842 GQ265843 GQ265841 Fragilariopsis cylindrus GQ232744 GQ232745 GQ232746 GQ232747 GQ232748 GQ232749...”
IBPKA_TYPIS / Q76CE8 Ice-binding protein K1-A; Antifreeze protein 8; AFP8; TAFP-3; TisAFP8 from Typhula ishikariensis (Gray snow mold fungus) (see 2 papers)
Aligns to 36:241 / 243 (84.8%), covers 99.5% of PF11999, 206.8 bits
- function: Binds to the surface of ice crystals (Ref.1, PubMed:20030710, PubMed:27613857). Inhibits growth of the ice crystals (PubMed:20030710). Has antifreeze activity for survival under snow cover. Has high thermal hysteresis (TH) activity, which is the ability to lower the freezing point of an aqueous solution below its melting point, and thus the freezing of the cell fluid can be prevented protecting the organism from ice damage (PubMed:20030710, PubMed:27613857). The TH activity of this protein is 2.0 degrees Celsius at 0.11 mM (PubMed:27613857).
7ddbA / Q76CE7 Crystal structure of fungal antifreeze protein with intermediate activity (see paper)
Aligns to 16:221 / 223 (92.4%), covers 99.5% of PF11999, 204.8 bits
- Ligand: magnesium ion (7ddbA)
IBP1_SHEFN / Q086E4 Ice-binding protein 1; Antifreeze protein 1; AFP 1; Ice adhesin 1 from Shewanella frigidimarina (strain NCIMB 400) (see paper)
Aligns to 670:889 / 892 (24.7%), covers 100.0% of PF11999, 200.5 bits
- function: Ice-binding adhesion protein that adsorbs this bacterium onto ice to maintain a favorable position in its aquatic habitat. Inhibits growth of the ice crystals. Has high thermal hysteresis (TH) activity, which is the ability to lower the freezing point of an aqueous solution below its melting point. The TH activity of this protein is approximately 1.4 degrees Celsius at 25 uM and little below 2 degrees Celsius at 80 uM.
IV454_32165 ice-binding family protein from Massilia antarctica
Aligns to 282:466 / 467 (39.6%), covers 70.2% of PF11999, 112.7 bits
D0EKL2 Antifreeze protein Afp1 from Glaciozyma antarctica
Aligns to 55:177 / 177 (69.5%), covers 48.6% of PF11999, 37.8 bits
- Solution structures, dynamics, and ice growth inhibitory activity of peptide fragments derived from an antarctic yeast protein
Shah, PloS one 2012 - “...an 18 kDa AFP with very low sequence identity to other AFPs (UniProtKB accession code D0EKL2 ). The sequence dissimilarity of this protein with other AFPs ignited our interest to unlock its structural and functional features, which is the main objective of this paper. The predicted...”
- “...data). At the moment, only one AFP gene has been completely characterized (UniProtKB accession code D0EKL2 ). The predicted secondary structure of G. antarctica AFP consisting of four -helices and three -strands ( Figure 1A ). The -helical region of non-glycosylated native AFP has been suggested...”
Or search for genetic data about PF11999 in the Fitness Browser
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory