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CAZyme Information: MGYG000003099_00682

You are here: Home > Sequence: MGYG000003099_00682

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 Barnesiella sp900538555
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Barnesiellaceae; Barnesiella; Barnesiella sp900538555
CAZyme ID MGYG000003099_00682
CAZy Family PL1
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
742 MGYG000003099_4|CGC1 80888.36 4.4593
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003099 3270064 MAG Spain Europe
Gene Location Start: 7853;  End: 10081  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003099_00682.

CAZyme Signature Domains help

Family Start End Evalue family coverage
PL1 219 388 1.5e-34 0.8267326732673267
CBM77 565 658 9e-17 0.8737864077669902

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG3866 PelB 4.32e-48 210 499 85 344
Pectate lyase [Carbohydrate transport and metabolism].
pfam18283 CBM77 6.97e-21 556 665 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 2.61e-20 224 384 17 184
Amb_all domain.
pfam00544 Pec_lyase_C 4.38e-11 198 384 7 209
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.
pfam18962 Por_Secre_tail 0.001 690 739 11 68
Secretion system C-terminal sorting domain. Species that include Porphyromonas gingivalis, Fibrobacter succinogenes, Flavobacterium johnsoniae, Cytophaga hutchinsonii, Gramella forsetii, Prevotella intermedia, and Salinibacter ruber have on average twenty or more copies of this C-terminal domain, associated with sorting to the outer membrane and covalent modification. This domain targets proteins to type IX secretion systems and is secreted then cleaved off by a C-terminal signal peptidease. Based on similarity to other families it is likely that this domain adopts an immunoglobulin like fold.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AQR94278.1 2.08e-167 21 532 83 594
AQS15728.1 3.55e-166 23 532 61 570
AGX44552.1 3.55e-166 23 532 61 570
AQS01745.1 3.55e-166 23 532 61 570
AQR91843.1 3.55e-166 23 532 61 570

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3VMV_A 1.20e-19 222 388 78 248
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]
1AIR_A 5.27e-12 219 405 85 276
ChainA, PECTATE LYASE C [Dickeya chrysanthemi],1O88_A Chain A, Pectate Lyase C [Dickeya chrysanthemi],1O8D_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi],1O8E_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi],1O8F_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi],1O8G_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi],1O8H_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi],1O8I_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi],1O8J_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi],1O8K_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi],1O8L_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi],1O8M_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi],1PLU_A Chain A, Protein (pectate Lyase C) [Dickeya chrysanthemi],2PEC_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi]
3ZSC_A 8.50e-12 220 363 65 213
Catalyticfunction and substrate recognition of the pectate lyase from Thermotoga maritima [Thermotoga maritima]
2EWE_A 1.25e-11 219 405 85 276
ChainA, Pectate lyase C [Dickeya chrysanthemi]
1VBL_A 2.36e-11 223 364 132 302
Structureof the thermostable pectate lyase PL 47 [Bacillus sp. TS-47]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q8GCB2 2.47e-19 162 364 58 250
Pectate trisaccharide-lyase OS=Bacillus licheniformis OX=1402 GN=pelA PE=1 SV=1
Q65DC2 2.47e-19 162 364 58 250
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
B1B6T1 2.47e-19 162 364 58 250
Pectate trisaccharide-lyase OS=Bacillus sp. OX=1409 GN=pel PE=1 SV=1
P0C1C3 7.79e-15 219 405 106 297
Pectate lyase 3 OS=Pectobacterium carotovorum subsp. carotovorum OX=555 GN=pel3 PE=3 SV=1
P0C1C2 1.04e-14 219 405 106 297
Pectate lyase 3 OS=Pectobacterium carotovorum OX=554 GN=pel3 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
0.000760 0.977499 0.020910 0.000351 0.000229 0.000205

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003099_00682.