You are browsing environment: HUMAN GUT
CAZyme Information: MGYG000003583_00048
You are here: Home > Sequence: MGYG000003583_00048
Basic Information |
Genomic context |
Full Sequence |
Enzyme annotations |
CAZy signature domains |
CDD domains |
CAZyme hits |
PDB hits |
Swiss-Prot hits |
SignalP and Lipop annotations |
TMHMM annotations
Basic Information help
| Species | Ruminococcus_C sp900770195 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Ruminococcus_C; Ruminococcus_C sp900770195 | |||||||||||
| CAZyme ID | MGYG000003583_00048 | |||||||||||
| CAZy Family | PL1 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
|
|||||||||||
| Genome Property |
|
|||||||||||
| Gene Location | Start: 41569; End: 45072 Strand: + | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| PL9 | 614 | 1022 | 1.3e-122 | 0.976 |
| PL1 | 243 | 412 | 1.8e-49 | 0.8118811881188119 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| COG3866 | PelB | 2.43e-57 | 106 | 517 | 2 | 340 | Pectate lyase [Carbohydrate transport and metabolism]. |
| smart00656 | Amb_all | 6.86e-38 | 233 | 414 | 5 | 190 | Amb_all domain. |
| pfam00544 | Pec_lyase_C | 1.04e-20 | 247 | 410 | 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 | 6.50e-12 | 1098 | 1154 | 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 | 2.24e-06 | 1099 | 1151 | 1 | 52 | 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. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| QMW93302.1 | 7.40e-282 | 35 | 1027 | 41 | 1083 |
| BBK78741.1 | 7.40e-282 | 35 | 1027 | 41 | 1083 |
| AOR96287.1 | 7.40e-282 | 35 | 1027 | 41 | 1083 |
| ADL51369.1 | 1.97e-263 | 54 | 1037 | 57 | 1252 |
| ACR72247.1 | 9.77e-249 | 59 | 1020 | 47 | 1045 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 1RU4_A | 2.03e-34 | 615 | 897 | 16 | 292 | ChainA, Pectate lyase [Dickeya chrysanthemi] |
| 3VMV_A | 1.03e-24 | 211 | 412 | 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 | 8.90e-19 | 247 | 410 | 135 | 330 | Structureof the thermostable pectate lyase PL 47 [Bacillus sp. TS-47] |
| 1PCL_A | 3.67e-17 | 184 | 410 | 18 | 276 | ChainA, PECTATE LYASE E [Dickeya chrysanthemi] |
| 3ZSC_A | 3.21e-16 | 247 | 395 | 71 | 221 | Catalyticfunction and substrate recognition of the pectate lyase from Thermotoga maritima [Thermotoga maritima] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| P0C1A6 | 1.76e-33 | 615 | 897 | 41 | 317 | Pectate lyase L OS=Dickeya chrysanthemi OX=556 GN=pelL PE=3 SV=1 |
| P0C1A7 | 1.76e-33 | 615 | 897 | 41 | 317 | Pectate lyase L OS=Dickeya dadantii (strain 3937) OX=198628 GN=pelL PE=1 SV=1 |
| P22751 | 2.34e-33 | 616 | 897 | 391 | 639 | Pectate disaccharide-lyase OS=Dickeya chrysanthemi OX=556 GN=pelX PE=1 SV=1 |
| Q8GCB2 | 3.64e-28 | 188 | 419 | 60 | 281 | Pectate trisaccharide-lyase OS=Bacillus licheniformis OX=1402 GN=pelA PE=1 SV=1 |
| Q65DC2 | 3.64e-28 | 188 | 419 | 60 | 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 |
SignalP and Lipop Annotations help
This protein is predicted as SP
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 0.000340 | 0.998862 | 0.000179 | 0.000246 | 0.000178 | 0.000152 |
