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CAZyme Information: MGYG000004854_01126

You are here: Home > Sequence: MGYG000004854_01126

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; Oscillospirales; Ruminococcaceae; Ruminococcus;
CAZyme ID MGYG000004854_01126
CAZy Family PL1
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1263 MGYG000004854_4|CGC2 133233.72 4.6513
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004854 2725669 MAG Spain Europe
Gene Location Start: 185885;  End: 189676  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004854_01126.

CAZyme Signature Domains help

Family Start End Evalue family coverage
PL9 595 1003 7.6e-119 0.9813333333333333
PL1 238 407 1.8e-48 0.8118811881188119
CBM77 1051 1153 1.1e-41 0.9902912621359223

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG3866 PelB 3.59e-57 103 513 2 340
Pectate lyase [Carbohydrate transport and metabolism].
pfam18283 CBM77 7.37e-42 1049 1155 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.
smart00656 Amb_all 2.62e-36 242 409 19 190
Amb_all domain.
pfam00544 Pec_lyase_C 7.00e-20 242 405 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 6.77e-06 1193 1252 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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AOR96287.1 4.89e-282 2 1019 8 1101
QMW93302.1 1.54e-280 2 1019 8 1101
BBK78741.1 1.54e-280 2 1019 8 1101
ADL51369.1 4.21e-250 46 1010 49 1244
ACR72247.1 3.08e-237 57 1000 48 1044

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5FU5_A 3.58e-43 1047 1158 4 114
Thecomplexity of the Ruminococcus flavefaciens cellulosome reflects an expansion in glycan recognition [Ruminococcus flavefaciens]
1RU4_A 2.04e-35 593 883 11 294
ChainA, Pectate lyase [Dickeya chrysanthemi]
3VMV_A 2.52e-22 195 407 33 248
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 9.48e-21 242 405 135 330
Structureof the thermostable pectate lyase PL 47 [Bacillus sp. TS-47]
5AMV_A 6.48e-16 239 403 127 323
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P0C1A6 5.42e-35 593 883 36 319
Pectate lyase L OS=Dickeya chrysanthemi OX=556 GN=pelL PE=3 SV=1
P0C1A7 1.80e-34 593 883 36 319
Pectate lyase L OS=Dickeya dadantii (strain 3937) OX=198628 GN=pelL PE=1 SV=1
P22751 7.88e-32 599 881 391 639
Pectate disaccharide-lyase OS=Dickeya chrysanthemi OX=556 GN=pelX PE=1 SV=1
Q8GCB2 5.51e-25 189 480 64 335
Pectate trisaccharide-lyase OS=Bacillus licheniformis OX=1402 GN=pelA PE=1 SV=1
Q65DC2 5.51e-25 189 480 64 335
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
0.085055 0.867520 0.045387 0.001376 0.000383 0.000247

TMHMM  Annotations      download full data without filtering help

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