Species | Ruminococcus sp900540005 | |||||||||||
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Lineage | Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Ruminococcus; Ruminococcus sp900540005 | |||||||||||
CAZyme ID | MGYG000001757_01998 | |||||||||||
CAZy Family | PL1 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 4414; End: 7185 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
PL1 | 264 | 448 | 1e-57 | 0.9076923076923077 |
CBM13 | 563 | 709 | 2.1e-21 | 0.6808510638297872 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG3866 | PelB | 8.93e-44 | 187 | 524 | 33 | 341 | Pectate lyase [Carbohydrate transport and metabolism]. |
pfam00544 | Pec_lyase_C | 3.54e-21 | 262 | 448 | 30 | 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. |
smart00656 | Amb_all | 4.74e-18 | 260 | 449 | 10 | 187 | Amb_all domain. |
pfam14200 | RicinB_lectin_2 | 5.56e-15 | 607 | 696 | 5 | 89 | Ricin-type beta-trefoil lectin domain-like. |
cd14256 | Dockerin_I | 1.15e-13 | 865 | 918 | 3 | 56 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
CBL16867.1 | 0.0 | 6 | 899 | 6 | 893 |
CDM68184.1 | 3.98e-119 | 34 | 627 | 26 | 585 |
CDM70399.1 | 3.37e-101 | 7 | 706 | 1 | 691 |
CBL17651.1 | 7.91e-98 | 36 | 899 | 32 | 873 |
AKQ74328.1 | 3.51e-94 | 37 | 528 | 30 | 482 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3ZSC_A | 2.01e-12 | 202 | 425 | 11 | 212 | Catalyticfunction and substrate recognition of the pectate lyase from Thermotoga maritima [Thermotoga maritima] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P94449 | 2.78e-62 | 186 | 527 | 34 | 339 | Pectin lyase OS=Bacillus subtilis OX=1423 GN=pelB PE=1 SV=1 |
O34819 | 6.84e-61 | 186 | 527 | 34 | 339 | Pectin lyase OS=Bacillus subtilis (strain 168) OX=224308 GN=pelB PE=3 SV=1 |
P27027 | 1.42e-50 | 187 | 528 | 10 | 307 | Pectin lyase OS=Pseudomonas marginalis OX=298 GN=pnl PE=1 SV=2 |
P24112 | 3.83e-45 | 200 | 528 | 12 | 309 | Pectin lyase OS=Pectobacterium carotovorum OX=554 GN=pnl PE=1 SV=1 |
Q00645 | 1.47e-15 | 193 | 493 | 39 | 304 | Pectate lyase plyB OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=plyB PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000259 | 0.999084 | 0.000179 | 0.000161 | 0.000146 | 0.000135 |
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