Species | Barnesiella sp900538705 | |||||||||||
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Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Barnesiellaceae; Barnesiella; Barnesiella sp900538705 | |||||||||||
CAZyme ID | MGYG000000956_02046 | |||||||||||
CAZy Family | PL1 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 6083; End: 9655 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
PL1 | 195 | 385 | 2.2e-43 | 0.9356435643564357 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG3866 | PelB | 3.71e-45 | 171 | 427 | 62 | 323 | Pectate lyase [Carbohydrate transport and metabolism]. |
smart00656 | Amb_all | 4.30e-28 | 222 | 385 | 19 | 190 | Amb_all domain. |
pfam00544 | Pec_lyase_C | 1.11e-19 | 185 | 381 | 1 | 211 | Pectate lyase. This enzyme forms a right handed beta helix structure. Pectate lyase is an enzyme involved in the maceration and soft rotting of plant tissue. |
NF033188 | internalin_H | 5.76e-06 | 822 | 996 | 299 | 482 | InlH/InlC2 family class 1 internalin. Internalins, as found in the intracellular human pathogen Listeria monocytogenes, are paralogous surface or secreted proteins with an N-terminal signal peptide, leucine-rich repeats, and usually a C-terminal LPXTG processing and cell surface anchoring site. See PMID:17764999 for a general discussion of internalins. Members of this family are internalin H (InlH), or internalin C2, two class 1 (LPXTG-type) internalins that are closely related, one apparently derived from the other through a recombination event. |
NF033189 | internalin_A | 9.53e-06 | 874 | 1046 | 563 | 743 | class 1 internalin InlA. Internalins, as found in the intracellular human pathogen Listeria monocytogenes, are paralogous surface or secreted proteins with an N-terminal signal peptide, leucine-rich repeats, and usually a C-terminal LPXTG processing and cell surface anchoring site. See PMID:17764999 for a general discussion of internalins. Members of this family are internalin A (InlA), a class 1 (LPXTG-type) internalin. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QUT73893.1 | 2.77e-178 | 21 | 542 | 21 | 541 |
QCD40816.1 | 2.83e-176 | 23 | 542 | 69 | 587 |
QCP73706.1 | 2.83e-176 | 23 | 542 | 69 | 587 |
BCJ94010.1 | 2.47e-165 | 21 | 542 | 41 | 564 |
AIQ71967.1 | 3.52e-161 | 30 | 542 | 43 | 557 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3VMV_A | 1.41e-21 | 185 | 434 | 47 | 300 | Crystalstructure of pectate lyase Bsp165PelA from Bacillus sp. N165 [Bacillus sp. N16-5],3VMW_A Crystal structure of pectate lyase Bsp165PelA from Bacillus sp. N165 in complex with trigalacturonate [Bacillus sp. N16-5] |
1PCL_A | 2.09e-17 | 180 | 452 | 42 | 328 | ChainA, PECTATE LYASE E [Dickeya chrysanthemi] |
1VBL_A | 5.17e-16 | 222 | 381 | 135 | 330 | Structureof the thermostable pectate lyase PL 47 [Bacillus sp. TS-47] |
1AIR_A | 2.21e-15 | 185 | 394 | 51 | 270 | ChainA, PECTATE LYASE C [Dickeya chrysanthemi],1O88_A Chain A, Pectate Lyase C [Dickeya chrysanthemi],1O8D_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi],1O8E_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi],1O8F_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi],1O8G_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi],1O8H_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi],1O8I_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi],1O8J_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi],1O8K_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi],1O8L_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi],1O8M_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi],1PLU_A Chain A, Protein (pectate Lyase C) [Dickeya chrysanthemi],2PEC_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi] |
2EWE_A | 5.29e-15 | 185 | 394 | 51 | 270 | ChainA, Pectate lyase C [Dickeya chrysanthemi] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q8GCB2 | 5.00e-22 | 162 | 390 | 61 | 281 | Pectate trisaccharide-lyase OS=Bacillus licheniformis OX=1402 GN=pelA PE=1 SV=1 |
Q65DC2 | 5.00e-22 | 162 | 390 | 61 | 281 | Pectate trisaccharide-lyase OS=Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46) OX=279010 GN=BLi04129 PE=3 SV=1 |
B1B6T1 | 5.00e-22 | 162 | 390 | 61 | 281 | Pectate trisaccharide-lyase OS=Bacillus sp. OX=1409 GN=pel PE=1 SV=1 |
Q60140 | 1.82e-19 | 166 | 381 | 60 | 310 | Pectate lyase OS=Pseudomonas viridiflava OX=33069 GN=pel PE=3 SV=1 |
Q51915 | 1.42e-18 | 166 | 381 | 61 | 311 | Pectate lyase OS=Pseudomonas marginalis OX=298 GN=pel PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.001427 | 0.865008 | 0.132598 | 0.000387 | 0.000284 | 0.000256 |
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