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CAZyme Information: MGYG000001160_00538

You are here: Home > Sequence: MGYG000001160_00538

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 CAG-274 sp000432155
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; CAG-274; CAG-274; CAG-274 sp000432155
CAZyme ID MGYG000001160_00538
CAZy Family PL1
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1639 MGYG000001160_11|CGC2 171199.74 4.4251
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001160 2196853 MAG Austria Europe
Gene Location Start: 37918;  End: 42837  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001160_00538.

CAZyme Signature Domains help

Family Start End Evalue family coverage
PL1 248 451 8.6e-33 0.8663366336633663
CBM77 744 832 6.3e-18 0.8737864077669902

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG3866 PelB 1.74e-27 188 533 46 343
Pectate lyase [Carbohydrate transport and metabolism].
smart00656 Amb_all 1.14e-19 257 454 12 190
Amb_all domain.
cd14256 Dockerin_I 2.17e-14 1047 1101 1 55
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.
pfam18283 CBM77 2.36e-13 745 837 13 108
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.
pfam00404 Dockerin_1 3.48e-12 1048 1101 1 54
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
BBF42492.1 2.98e-152 6 698 5 673
ACR71161.1 2.64e-124 34 843 41 895
ADU23076.1 1.26e-113 38 510 761 1209
CDR31241.1 1.86e-85 38 669 333 893
QQY82326.1 3.62e-64 21 840 17 750

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3VMV_A 1.31e-15 256 450 74 246
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]
2QX3_A 2.60e-14 255 537 66 330
Structureof pectate lyase II from Xanthomonas campestris pv. campestris str. ATCC 33913 [Xanthomonas campestris pv. campestris],2QX3_B Structure of pectate lyase II from Xanthomonas campestris pv. campestris str. ATCC 33913 [Xanthomonas campestris pv. campestris]
2QY1_A 2.01e-13 255 537 66 330
ChainA, Pectate lyase II [Xanthomonas campestris pv. campestris],2QY1_B Chain B, Pectate lyase II [Xanthomonas campestris pv. campestris]
2QXZ_A 2.01e-13 255 537 66 330
ChainA, pectate lyase II [Xanthomonas campestris pv. campestris],2QXZ_B Chain B, pectate lyase II [Xanthomonas campestris pv. campestris]
5AMV_A 3.66e-13 261 458 127 326
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
Q8GCB2 2.79e-14 255 459 102 281
Pectate trisaccharide-lyase OS=Bacillus licheniformis OX=1402 GN=pelA PE=1 SV=1
Q65DC2 2.79e-14 255 459 102 281
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
B1B6T1 2.79e-14 255 459 102 281
Pectate trisaccharide-lyase OS=Bacillus sp. OX=1409 GN=pel PE=1 SV=1
P39116 2.29e-12 261 458 148 347
Pectate lyase OS=Bacillus subtilis (strain 168) OX=224308 GN=pel PE=1 SV=1
Q6CZT2 1.65e-11 337 533 163 363
Pectate lyase 3 OS=Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) OX=218491 GN=pel3 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
0.000292 0.998957 0.000175 0.000223 0.000177 0.000153

TMHMM  Annotations      download full data without filtering help

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