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CAZyme Information: MGYG000004547_01878

You are here: Home > Sequence: MGYG000004547_01878

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 MGYG000004547_01878
CAZy Family PL1
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1304 139553.38 4.6826
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004547 2604006 MAG France Europe
Gene Location Start: 173;  End: 4087  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004547_01878.

CAZyme Signature Domains help

Family Start End Evalue family coverage
PL1 214 386 5.3e-45 0.8415841584158416

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG3866 PelB 8.41e-47 90 521 6 340
Pectate lyase [Carbohydrate transport and metabolism].
smart00656 Amb_all 3.30e-29 221 386 17 189
Amb_all domain.
pfam00544 Pec_lyase_C 7.63e-18 193 383 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 1.30e-09 1045 1101 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.
pfam00404 Dockerin_1 4.21e-06 1046 1101 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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AQR94278.1 1.51e-136 22 545 78 579
AEI31450.1 1.93e-134 23 551 43 564
ADZ19854.1 1.93e-134 23 551 43 564
AWV80498.1 1.93e-134 23 551 43 564
AAK78780.1 1.93e-134 23 551 43 564

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3VMV_A 2.37e-26 192 385 46 248
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 1.21e-18 227 526 94 344
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]
1VBL_A 1.83e-18 221 383 133 330
Structureof the thermostable pectate lyase PL 47 [Bacillus sp. TS-47]
2EWE_A 2.92e-18 227 526 94 344
ChainA, Pectate lyase C [Dickeya chrysanthemi]
3ZSC_A 6.31e-17 217 375 65 222
Catalyticfunction and substrate recognition of the pectate lyase from Thermotoga maritima [Thermotoga maritima]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q8GCB2 9.46e-26 165 390 55 279
Pectate trisaccharide-lyase OS=Bacillus licheniformis OX=1402 GN=pelA PE=1 SV=1
Q65DC2 9.46e-26 165 390 55 279
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 9.46e-26 165 390 55 279
Pectate trisaccharide-lyase OS=Bacillus sp. OX=1409 GN=pel PE=1 SV=1
P04959 1.28e-21 125 526 15 366
Pectate lyase B OS=Dickeya chrysanthemi OX=556 GN=pelB PE=3 SV=1
Q5AVN4 5.73e-19 221 411 99 291
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

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
0.000310 0.998939 0.000199 0.000180 0.000166 0.000160

TMHMM  Annotations      download full data without filtering help

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