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Family Search for PF16332 (DUF4962)

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Running HMMer for PF16332

PF16332 hits 14 sequences in PaperBLAST's database above the trusted cutoff. Showing all hits. Or show only hits to curated sequences or try another family.

BT4652 heparan sulfate cleaving enzyme from Bacteroides thetaiotaomicron VPI-5482
BT4652, BT_4652 conserved hypothetical protein from Bacteroides thetaiotaomicron VPI-5482
Aligns to 31:503 / 872 (54.2%), covers 100.0% of PF16332, 772.6 bits

6ljaA / B3C5J6 Crystal structure of exohep from bacteroides intestinalis dsm 17393 complexed with disaccharide product (see paper)
Aligns to 8:481 / 841 (56.4%), covers 100.0% of PF16332, 738.8 bits

3aflA / A9CEJ9 Crystal structure of exotype alginate lyase atu3025 h531a complexed with alginate trisaccharide (see paper)
Aligns to 34:454 / 766 (55.0%), covers 83.4% of PF16332, 139.6 bits

A9CEJ9 guluronate-specific alginate lyase (EC 4.2.2.11); mannuronate-specific alginate lyase (EC 4.2.2.3) from Agrobacterium tumefaciens (see paper)
AAL43841.1 exotype alginate lyase (Atu3025) (EC 4.2.2.-) (see protein)
Atu3025 oligo alginate lyase from Agrobacterium tumefaciens str. C58 (Cereon)
Aligns to 44:464 / 776 (54.3%), covers 83.4% of PF16332, 139.5 bits

oal / Q9KWT4 oligoalginate lyase (EC 4.2.2.26) from Sphingomonas sp. (see 2 papers)
BAB03319.1 oligo alginate lyase (A1-IV;Oal) (EC 4.2.2.-) (see protein)
oal / BAB03319.1 oligo alginate lyase from Sphingomonas sp (see paper)
Aligns to 33:456 / 761 (55.7%), covers 84.7% of PF16332, 119.7 bits

Q5DWP2 mannuronate-specific alginate lyase (EC 4.2.2.3) from Sphingomonas sp. (see paper)
BAD90006.1 alginate lyase (A1-IV') (EC 4.2.2.3) (see protein)
Aligns to 37:404 / 812 (45.3%), covers 72.7% of PF16332, 85.0 bits

6jp4A / A0A4Y5UXE1 Crystal structure of the catalytic domain of a multi-domain alginate lyase dp0100 from thermophilic bacterium defluviitalea phaphyphila (see paper)
Aligns to 14:274 / 770 (33.9%), covers 36.1% of PF16332, 33.8 bits

E5X103 heparin lyase (EC 4.2.2.7) from Bacteroides eggerthii (see paper)
Aligns to 22:276 / 773 (33.0%), covers 34.9% of PF16332, 32.8 bits

C0JBW5 heparin lyase (EC 4.2.2.7) from Bacteroides stercoris (see paper)
ACN29695.1 acharan sulfate lyase 1/2 / heparin lyase II / heparanase II (AlsI;Als2;HepII) (EC 4.2.2.7|4.2.2.8|4.2.2.-) (see protein)
Aligns to 41:275 / 773 (30.4%), covers 34.9% of PF16332, 32.1 bits

3e80C / C6XZB6 Structure of heparinase ii complexed with heparan sulfate degradation disaccharide product (see paper)
Aligns to 16:290 / 747 (36.8%), covers 32.4% of PF16332, 30.4 bits

hepB / C6XZB6 heparinase II (EC 4.2.2.8; EC 4.2.2.7) from Pedobacter heparinus (strain ATCC 13125 / DSM 2366 / CIP 104194 / JCM 7457 / NBRC 12017 / NCIMB 9290 / NRRL B-14731 / HIM 762-3) (see 3 papers)
HEPB_PEDHD / C6XZB6 Heparin and heparin-sulfate lyase; Heparin lyase; Heparin-sulfate lyase; Heparinase II; HepII; EC 4.2.2.7; EC 4.2.2.8 from Pedobacter heparinus (strain ATCC 13125 / DSM 2366 / CIP 104194 / JCM 7457 / NBRC 12017 / NCIMB 9290 / NRRL B-14731 / HIM 762-3) (see 3 papers)
ACU04612.1 heparin lyase II / heparinase II (HepB;Phep_2408) (EC 4.2.2.7|4.2.2.8) (see protein)
Aligns to 40:314 / 772 (35.6%), covers 32.4% of PF16332, 30.3 bits

6hznA / Q9UL01 Crystal structure of human dermatan sulfate epimerase 1
Aligns to 96:330 / 743 (31.6%), covers 33.6% of PF16332, 29.6 bits

DSE_BOVIN / P0C2H4 Dermatan-sulfate epimerase; DS epimerase; Chondroitin-glucuronate 5-epimerase; EC 5.1.3.19 from Bos taurus (Bovine) (see paper)
Aligns to 109:354 / 958 (25.7%), covers 33.8% of PF16332, 29.3 bits

DSE / Q9UL01 dermatan-sulfate epimerase (EC 5.1.3.19) from Homo sapiens (see 4 papers)
DSE_HUMAN / Q9UL01 Dermatan-sulfate epimerase; DS epimerase; Chondroitin-glucuronate 5-epimerase; Squamous cell carcinoma antigen recognized by T-cells 2; SART-2; EC 5.1.3.19 from Homo sapiens (Human) (see 5 papers)
NP_001309866 dermatan-sulfate epimerase isoform a precursor from Homo sapiens
Aligns to 119:353 / 958 (24.5%), covers 33.6% of PF16332, 28.7 bits

Or search for genetic data about PF16332 in the Fitness Browser

by Morgan Price, Arkin group
Lawrence Berkeley National Laboratory