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CAZyme Information: MGYG000004429_00082

You are here: Home > Sequence: MGYG000004429_00082

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; ;
CAZyme ID MGYG000004429_00082
CAZy Family PL1
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1067 111298.79 4.362
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004429 2352873 MAG Israel Asia
Gene Location Start: 10876;  End: 14079  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004429_00082.

CAZyme Signature Domains help

Family Start End Evalue family coverage
PL1 252 416 1.4e-40 0.801980198019802

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG3866 PelB 2.82e-45 228 420 83 279
Pectate lyase [Carbohydrate transport and metabolism].
smart00656 Amb_all 1.28e-32 252 418 17 190
Amb_all domain.
pfam00544 Pec_lyase_C 1.69e-15 214 414 1 211
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 0.001 1025 1061 18 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
AQR94278.1 2.60e-136 42 591 83 596
ACX62589.1 1.11e-135 38 598 31 567
AYB46946.1 4.55e-135 41 598 34 567
QOT09127.1 1.25e-134 38 598 31 567
AEI31450.1 1.84e-134 30 580 38 553

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3VMV_A 9.11e-22 211 416 42 248
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 5.96e-16 252 414 133 330
Structureof the thermostable pectate lyase PL 47 [Bacillus sp. TS-47]
1AIR_A 8.43e-14 290 496 129 337
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]
2EWE_A 2.01e-13 290 496 129 337
ChainA, Pectate lyase C [Dickeya chrysanthemi]
5AMV_A 6.73e-13 252 412 128 323
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
B1B6T1 2.39e-22 204 423 73 281
Pectate trisaccharide-lyase OS=Bacillus sp. OX=1409 GN=pel PE=1 SV=1
Q65DC2 2.39e-22 204 423 73 281
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
Q8GCB2 2.39e-22 204 423 73 281
Pectate trisaccharide-lyase OS=Bacillus licheniformis OX=1402 GN=pelA PE=1 SV=1
Q5AVN4 1.10e-13 252 439 99 289
Pectate lyase A OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=plyA PE=1 SV=1
P0C1C3 3.11e-13 290 441 152 310
Pectate lyase 3 OS=Pectobacterium carotovorum subsp. carotovorum OX=555 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
0.000418 0.998864 0.000183 0.000202 0.000150 0.000144

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004429_00082.