Species | Ruminococcus_C sp000980705 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Ruminococcus_C; Ruminococcus_C sp000980705 | |||||||||||
CAZyme ID | MGYG000001021_01869 | |||||||||||
CAZy Family | PL1 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 17499; End: 21140 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
PL9 | 610 | 1022 | 8.6e-125 | 0.984 |
PL1 | 235 | 405 | 4.6e-45 | 0.8217821782178217 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG3866 | PelB | 3.08e-52 | 106 | 511 | 2 | 340 | Pectate lyase [Carbohydrate transport and metabolism]. |
smart00656 | Amb_all | 6.65e-34 | 237 | 407 | 15 | 190 | Amb_all domain. |
pfam00544 | Pec_lyase_C | 1.15e-21 | 211 | 403 | 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. |
cd14256 | Dockerin_I | 5.13e-13 | 1147 | 1203 | 1 | 57 | Type I dockerin repeat domain. Bacterial cohesin domains bind to a complementary protein domain named dockerin, and this interaction is required for the formation of the cellulosome, a cellulose-degrading complex. The cellulosome consists of scaffoldin, a noncatalytic scaffolding polypeptide, that comprises repeating cohesion modules and a single carbohydrate-binding module (CBM). Specific calcium-dependent interactions between cohesins and dockerins appear to be essential for cellulosome assembly. This subfamily represents type I dockerins, which are responsible for anchoring a variety of enzymatic domains to the complex. |
pfam00404 | Dockerin_1 | 1.28e-07 | 1148 | 1202 | 1 | 55 | Dockerin type I repeat. The dockerin repeat is the binding partner of the cohesin domain pfam00963. The cohesin-dockerin interaction is the crucial interaction for complex formation in the cellulosome. The dockerin repeats, each bearing homology to the EF-hand calcium-binding loop bind calcium. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
AOR96287.1 | 2.48e-271 | 31 | 1020 | 37 | 1079 |
QMW93302.1 | 4.36e-269 | 31 | 1020 | 37 | 1079 |
BBK78741.1 | 4.36e-269 | 31 | 1020 | 37 | 1079 |
ADL51369.1 | 3.79e-264 | 49 | 1030 | 57 | 1247 |
ACR72247.1 | 4.02e-262 | 54 | 1015 | 47 | 1043 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1RU4_A | 2.61e-35 | 613 | 896 | 18 | 294 | ChainA, Pectate lyase [Dickeya chrysanthemi] |
3VMV_A | 9.78e-23 | 197 | 466 | 33 | 311 | 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] |
1AIR_A | 1.56e-17 | 150 | 412 | 13 | 266 | 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 | 3.76e-17 | 150 | 412 | 13 | 266 | ChainA, Pectate lyase C [Dickeya chrysanthemi] |
1VBL_A | 7.10e-17 | 241 | 403 | 135 | 330 | Structureof the thermostable pectate lyase PL 47 [Bacillus sp. TS-47] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P0C1A6 | 6.29e-36 | 613 | 907 | 43 | 334 | Pectate lyase L OS=Dickeya chrysanthemi OX=556 GN=pelL PE=3 SV=1 |
P22751 | 6.72e-36 | 612 | 894 | 391 | 639 | Pectate disaccharide-lyase OS=Dickeya chrysanthemi OX=556 GN=pelX PE=1 SV=1 |
P0C1A7 | 2.29e-34 | 613 | 896 | 43 | 319 | Pectate lyase L OS=Dickeya dadantii (strain 3937) OX=198628 GN=pelL PE=1 SV=1 |
Q65DC2 | 6.32e-23 | 187 | 412 | 59 | 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 |
Q8GCB2 | 6.32e-23 | 187 | 412 | 59 | 281 | Pectate trisaccharide-lyase OS=Bacillus licheniformis OX=1402 GN=pelA PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000231 | 0.999060 | 0.000158 | 0.000211 | 0.000166 | 0.000144 |
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