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CAZyme Information: MGYG000001660_00348

You are here: Home > Sequence: MGYG000001660_00348

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 HGM11788 sp900760465
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; CAG-274; HGM11788; HGM11788 sp900760465
CAZyme ID MGYG000001660_00348
CAZy Family PL1
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1402 149220.13 4.3006
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001660 2161039 MAG United States North America
Gene Location Start: 19019;  End: 23227  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001660_00348.

CAZyme Signature Domains help

Family Start End Evalue family coverage
PL1 240 434 1.5e-32 0.8762376237623762
CBM77 787 886 2.5e-16 0.9514563106796117

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG3866 PelB 1.05e-24 251 524 98 340
Pectate lyase [Carbohydrate transport and metabolism].
smart00656 Amb_all 1.74e-15 253 436 15 190
Amb_all domain.
pfam00404 Dockerin_1 2.17e-11 1339 1393 1 56
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.
cd14256 Dockerin_I 5.31e-11 1338 1393 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.
pfam00544 Pec_lyase_C 1.18e-08 290 432 64 211
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
BBF42492.1 1.76e-131 1 619 1 612
ADU23076.1 6.23e-97 37 528 763 1239
ACR71161.1 6.60e-96 37 891 47 890
CDR31241.1 1.84e-86 35 531 333 812
QEH68115.1 2.70e-69 1 527 2 478

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3VMV_A 3.55e-15 254 437 79 251
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 1.19e-12 211 433 50 258
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]
5AMV_A 1.67e-12 229 416 102 302
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 1.89e-12 229 416 123 323
BacillusSubtilis Pectate Lyase [Bacillus subtilis]
2EWE_A 2.84e-12 211 433 50 258
ChainA, Pectate lyase C [Dickeya chrysanthemi]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P04959 4.39e-14 211 442 71 289
Pectate lyase B OS=Dickeya chrysanthemi OX=556 GN=pelB PE=3 SV=1
B1B6T1 5.58e-14 254 436 108 276
Pectate trisaccharide-lyase OS=Bacillus sp. OX=1409 GN=pel PE=1 SV=1
Q65DC2 5.58e-14 254 436 108 276
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 5.58e-14 254 436 108 276
Pectate trisaccharide-lyase OS=Bacillus licheniformis OX=1402 GN=pelA PE=1 SV=1
P0C1C1 1.38e-13 211 527 71 363
Pectate lyase 2 OS=Pectobacterium carotovorum OX=554 GN=pel2 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
0.000287 0.998927 0.000209 0.000207 0.000168 0.000151

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001660_00348.