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CAZyme Information: MGYG000001998_00359

You are here: Home > Sequence: MGYG000001998_00359

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 Lachnospira sp900552795
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Lachnospira; Lachnospira sp900552795
CAZyme ID MGYG000001998_00359
CAZy Family PL1
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
717 MGYG000001998_2|CGC2 78789.91 4.5378
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001998 2300661 MAG Spain Europe
Gene Location Start: 45353;  End: 47506  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 4.2.2.2

CAZyme Signature Domains help

Family Start End Evalue family coverage
PL1 177 430 6.8e-30 0.806930693069307

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
smart00656 Amb_all 7.59e-15 166 391 6 167
Amb_all domain.
COG3866 PelB 1.82e-09 181 478 104 321
Pectate lyase [Carbohydrate transport and metabolism].
pfam00544 Pec_lyase_C 5.01e-05 170 268 28 134
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.
NF033847 MCP_Sipho 2.98e-04 585 683 8 107
major capsid protein, Siphoviridae type. This protein is a phage major capsid protein, as reported in primary sequence submissions of a large number of Siphoviridae, many of which have hosts in the Mycobacterium and Gordonia genera of bacteria.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
ADL50775.1 2.52e-199 41 578 27 552
BAV13078.1 2.78e-199 41 578 30 555
QNF29855.1 3.53e-198 30 578 15 550
QYR22341.1 1.89e-190 24 588 9 561
AFH62972.1 7.04e-188 33 588 17 559

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5GT5_A 4.11e-39 67 578 8 446
Structuralbasis of the specific activity and thermostability of pectate lyase (pelN) from Paenibacillus sp. 0602 [Paenibacillus sp. 0602],5GT5_B Structural basis of the specific activity and thermostability of pectate lyase (pelN) from Paenibacillus sp. 0602 [Paenibacillus sp. 0602]
3KRG_A 7.86e-09 196 431 146 341
ChainA, Pectate lyase [Bacillus subtilis]
5AMV_A 7.86e-09 196 431 146 341
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]
1BN8_A 8.41e-09 196 431 167 362
BacillusSubtilis Pectate Lyase [Bacillus subtilis]
2BSP_A 1.95e-08 196 431 167 362
ChainA, PROTEIN (PECTATE LYASE) [Bacillus subtilis]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
D3JTC2 2.26e-39 49 437 20 378
Pectate lyase B OS=Paenibacillus amylolyticus OX=1451 GN=pelB PE=1 SV=1
Q9WYR4 1.25e-09 177 284 79 210
Pectate trisaccharide-lyase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=pelA PE=1 SV=1
B1L969 3.86e-09 177 284 77 208
Pectate trisaccharide-lyase OS=Thermotoga sp. (strain RQ2) OX=126740 GN=pelA PE=3 SV=1
P39116 4.61e-08 196 431 167 362
Pectate lyase OS=Bacillus subtilis (strain 168) OX=224308 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
0.002888 0.996033 0.000257 0.000360 0.000243 0.000200

TMHMM  Annotations      download full data without filtering help

start end
12 34
691 710