You are browsing environment: HUMAN GUT
CAZyme Information: MGYG000001833_01407
You are here: Home > Sequence: MGYG000001833_01407
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 | ||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; CAG-274; UMGS1441; | |||||||||||
| CAZyme ID | MGYG000001833_01407 | |||||||||||
| CAZy Family | PL1 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
|
|||||||||||
| Genome Property |
|
|||||||||||
| Gene Location | Start: 278; End: 5734 Strand: + | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| CBM77 | 1706 | 1810 | 7e-41 | 0.9902912621359223 |
| PL1 | 244 | 434 | 7.8e-38 | 0.8564356435643564 |
| CBM77 | 796 | 896 | 3e-21 | 0.9514563106796117 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| pfam18283 | CBM77 | 7.64e-39 | 1704 | 1812 | 1 | 108 | Carbohydrate binding module 77. This domain is the non-catalytic carbohydrate binding module 77 (CBM77) present in Ruminococcus flavefaciens. CBMs fulfil a critical targeting function in plant cell wall depolymerisation. In CBM77, a cluster of conserved basic residues (Lys1092, Lys1107 and Lys1162) confer calcium-independent recognition of homogalacturonan. |
| COG3866 | PelB | 4.33e-27 | 255 | 437 | 102 | 278 | Pectate lyase [Carbohydrate transport and metabolism]. |
| smart00656 | Amb_all | 4.04e-19 | 255 | 436 | 17 | 190 | Amb_all domain. |
| pfam18283 | CBM77 | 6.71e-17 | 795 | 901 | 3 | 108 | Carbohydrate binding module 77. This domain is the non-catalytic carbohydrate binding module 77 (CBM77) present in Ruminococcus flavefaciens. CBMs fulfil a critical targeting function in plant cell wall depolymerisation. In CBM77, a cluster of conserved basic residues (Lys1092, Lys1107 and Lys1162) confer calcium-independent recognition of homogalacturonan. |
| pfam00544 | Pec_lyase_C | 4.00e-13 | 290 | 432 | 64 | 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. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| BBF42492.1 | 1.85e-133 | 37 | 535 | 42 | 504 |
| ACR71161.1 | 5.18e-92 | 37 | 913 | 47 | 901 |
| ADU23076.1 | 4.08e-91 | 37 | 535 | 763 | 1239 |
| CDR31241.1 | 1.16e-84 | 35 | 538 | 333 | 812 |
| ADZ82421.1 | 2.61e-67 | 1 | 582 | 2 | 524 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 5FU5_A | 1.85e-35 | 1704 | 1814 | 6 | 113 | Thecomplexity of the Ruminococcus flavefaciens cellulosome reflects an expansion in glycan recognition [Ruminococcus flavefaciens] |
| 3VMV_A | 1.88e-16 | 254 | 434 | 79 | 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 | 5.88e-12 | 255 | 420 | 133 | 312 | Structureof the thermostable pectate lyase PL 47 [Bacillus sp. TS-47] |
| 2QXZ_A | 7.43e-12 | 317 | 445 | 128 | 259 | ChainA, pectate lyase II [Xanthomonas campestris pv. campestris],2QXZ_B Chain B, pectate lyase II [Xanthomonas campestris pv. campestris] |
| 2QY1_A | 7.43e-12 | 317 | 445 | 128 | 259 | ChainA, Pectate lyase II [Xanthomonas campestris pv. campestris],2QY1_B Chain B, Pectate lyase II [Xanthomonas campestris pv. campestris] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| P0C1C1 | 2.45e-15 | 211 | 451 | 71 | 297 | Pectate lyase 2 OS=Pectobacterium carotovorum OX=554 GN=pel2 PE=3 SV=1 |
| P0C1C0 | 3.27e-15 | 318 | 451 | 162 | 297 | Pectate lyase 1 OS=Pectobacterium carotovorum OX=554 GN=pel1 PE=1 SV=1 |
| Q6CZT3 | 1.86e-14 | 211 | 451 | 71 | 297 | Pectate lyase 2 OS=Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) OX=218491 GN=pel2 PE=1 SV=1 |
| Q6CZT4 | 2.49e-14 | 318 | 451 | 162 | 297 | Pectate lyase 1 OS=Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) OX=218491 GN=pel1 PE=1 SV=1 |
| B1B6T1 | 1.81e-13 | 203 | 437 | 61 | 277 | Pectate trisaccharide-lyase OS=Bacillus sp. OX=1409 GN=pel PE=1 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 |
|---|---|---|---|---|---|
| 0.000304 | 0.998983 | 0.000186 | 0.000200 | 0.000163 | 0.000148 |