Species | UBA1394 sp900538575 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; UBA1394; UBA1394 sp900538575 | |||||||||||
CAZyme ID | MGYG000001756_00354 | |||||||||||
CAZy Family | PL1 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 63855; End: 67313 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
PL9 | 596 | 1021 | 5.6e-125 | 0.9866666666666667 |
PL1 | 233 | 401 | 4.8e-49 | 0.806930693069307 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG3866 | PelB | 4.73e-56 | 176 | 508 | 42 | 340 | Pectate lyase [Carbohydrate transport and metabolism]. |
smart00656 | Amb_all | 2.16e-38 | 236 | 403 | 19 | 190 | Amb_all domain. |
pfam00544 | Pec_lyase_C | 1.51e-21 | 236 | 399 | 38 | 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 | 4.27e-11 | 1081 | 1139 | 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 | 2.68e-08 | 1082 | 1138 | 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 |
---|---|---|---|---|---|
QMW93302.1 | 7.25e-278 | 50 | 1031 | 65 | 1091 |
BBK78741.1 | 7.25e-278 | 50 | 1031 | 65 | 1091 |
AOR96287.1 | 2.04e-277 | 50 | 1031 | 65 | 1091 |
ADL51369.1 | 5.23e-269 | 2 | 1028 | 10 | 1247 |
ABX41986.1 | 5.86e-257 | 50 | 1021 | 49 | 1151 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1RU4_A | 2.96e-36 | 606 | 883 | 25 | 294 | ChainA, Pectate lyase [Dickeya chrysanthemi] |
3VMV_A | 2.50e-24 | 177 | 401 | 9 | 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 | 3.50e-21 | 236 | 399 | 135 | 330 | Structureof the thermostable pectate lyase PL 47 [Bacillus sp. TS-47] |
5OLQ_A | 3.07e-17 | 606 | 882 | 12 | 320 | Rhamnogalacturonanlyase [Bacteroides thetaiotaomicron],5OLQ_B Rhamnogalacturonan lyase [Bacteroides thetaiotaomicron],5OLQ_C Rhamnogalacturonan lyase [Bacteroides thetaiotaomicron],5OLR_A Rhamnogalacturonan lyase [Bacteroides thetaiotaomicron],5OLR_B Rhamnogalacturonan lyase [Bacteroides thetaiotaomicron],5OLR_C Rhamnogalacturonan lyase [Bacteroides thetaiotaomicron],5OLS_A Rhamnogalacturonan lyase [Bacteroides thetaiotaomicron] |
5AMV_A | 4.28e-17 | 231 | 425 | 125 | 348 | Structuralinsights into the loss of catalytic competence in pectate lyase at low pH [Bacillus subtilis],5X2I_A Polygalacturonate Lyase by Fusing with a Self-assembling Amphipathic Peptide [Bacillus subtilis subsp. subtilis str. 168] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P0C1A6 | 7.89e-36 | 606 | 883 | 49 | 319 | Pectate lyase L OS=Dickeya chrysanthemi OX=556 GN=pelL PE=3 SV=1 |
P0C1A7 | 2.62e-35 | 606 | 883 | 50 | 319 | Pectate lyase L OS=Dickeya dadantii (strain 3937) OX=198628 GN=pelL PE=1 SV=1 |
P22751 | 2.87e-32 | 611 | 881 | 403 | 639 | Pectate disaccharide-lyase OS=Dickeya chrysanthemi OX=556 GN=pelX PE=1 SV=1 |
Q8GCB2 | 1.96e-28 | 179 | 408 | 51 | 281 | Pectate trisaccharide-lyase OS=Bacillus licheniformis OX=1402 GN=pelA PE=1 SV=1 |
Q65DC2 | 1.96e-28 | 179 | 408 | 51 | 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 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.094450 | 0.821205 | 0.082865 | 0.000822 | 0.000322 | 0.000316 |
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