Species | UMGS268 sp900540705 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes; Bacilli; Acholeplasmatales; Anaeroplasmataceae; UMGS268; UMGS268 sp900540705 | |||||||||||
CAZyme ID | MGYG000001957_00922 | |||||||||||
CAZy Family | PL1 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 304; End: 3621 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
PL1 | 787 | 956 | 1.8e-42 | 0.8168316831683168 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG3866 | PelB | 6.97e-56 | 646 | 1070 | 1 | 344 | Pectate lyase [Carbohydrate transport and metabolism]. |
smart00656 | Amb_all | 3.32e-34 | 789 | 957 | 17 | 190 | Amb_all domain. |
pfam00544 | Pec_lyase_C | 4.93e-19 | 753 | 953 | 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. |
NF033189 | internalin_A | 2.61e-15 | 383 | 581 | 509 | 702 | 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. |
pfam09479 | Flg_new | 3.84e-15 | 369 | 433 | 1 | 65 | Listeria-Bacteroides repeat domain (List_Bact_rpt). This model describes a conserved core region of about 43 residues, which occurs in at least two families of tandem repeats. These include 78-residue repeats which occur from 2 to 15 times in some proteins of Bacteroides forsythus ATCC 43037, and 70-residue repeats found in families of internalins of Listeria species. Single copies are found in proteins of Fibrobacter succinogenes, Geobacter sulfurreducens, and a few other bacteria. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
AQS15728.1 | 7.79e-161 | 584 | 1104 | 58 | 572 |
AGX44552.1 | 7.79e-161 | 584 | 1104 | 58 | 572 |
AQS01745.1 | 7.79e-161 | 584 | 1104 | 58 | 572 |
AQR91843.1 | 7.79e-161 | 584 | 1104 | 58 | 572 |
AQS11349.1 | 7.79e-161 | 584 | 1104 | 58 | 572 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3VMV_A | 1.07e-23 | 753 | 955 | 47 | 248 | 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] |
1VBL_A | 1.98e-17 | 785 | 953 | 129 | 330 | Structureof the thermostable pectate lyase PL 47 [Bacillus sp. TS-47] |
1AIR_A | 2.12e-12 | 771 | 1063 | 76 | 339 | 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] |
2QXZ_A | 7.38e-12 | 777 | 960 | 66 | 253 | ChainA, pectate lyase II [Xanthomonas campestris pv. campestris],2QXZ_B Chain B, pectate lyase II [Xanthomonas campestris pv. campestris] |
2QY1_A | 7.38e-12 | 777 | 960 | 66 | 253 | ChainA, Pectate lyase II [Xanthomonas campestris pv. campestris],2QY1_B Chain B, Pectate lyase II [Xanthomonas campestris pv. campestris] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P0DJ98 | 2.15e-41 | 4 | 220 | 12 | 223 | Putative membrane protein Bcell_0381 OS=Evansella cellulosilytica (strain ATCC 21833 / DSM 2522 / FERM P-1141 / JCM 9156 / N-4) OX=649639 GN=Bcell_0381 PE=4 SV=1 |
P0DJ97 | 2.19e-35 | 4 | 220 | 592 | 803 | Putative Gly-rich membrane protein Bcell_0380 OS=Evansella cellulosilytica (strain ATCC 21833 / DSM 2522 / FERM P-1141 / JCM 9156 / N-4) OX=649639 GN=Bcell_0380 PE=4 SV=1 |
Q8GCB2 | 8.47e-25 | 731 | 961 | 62 | 280 | Pectate trisaccharide-lyase OS=Bacillus licheniformis OX=1402 GN=pelA PE=1 SV=1 |
B1B6T1 | 8.47e-25 | 731 | 961 | 62 | 280 | Pectate trisaccharide-lyase OS=Bacillus sp. OX=1409 GN=pel PE=1 SV=1 |
Q65DC2 | 8.47e-25 | 731 | 961 | 62 | 280 | 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 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.999934 | 0.000121 | 0.000004 | 0.000000 | 0.000000 | 0.000000 |
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