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CAZyme Information: MGYG000003087_00966

You are here: Home > Sequence: MGYG000003087_00966

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 Merdibacter sp900543035
Lineage Bacteria; Firmicutes; Bacilli; Erysipelotrichales; Erysipelotrichaceae; Merdibacter; Merdibacter sp900543035
CAZyme ID MGYG000003087_00966
CAZy Family GH136
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1502 MGYG000003087_18|CGC1 162089.4 3.9877
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003087 2304658 MAG Spain Europe
Gene Location Start: 652;  End: 5160  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003087_00966.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH136 332 853 8.3e-97 0.9755600814663951

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam13229 Beta_helix 2.70e-08 548 754 9 156
Right handed beta helix region. This region contains a parallel beta helix region that shares some similarity with Pectate lyases.
TIGR02168 SMC_prok_B 4.72e-06 1147 1462 676 988
chromosome segregation protein SMC, common bacterial type. SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
cd04079 CBM6_agarase-like 1.65e-05 896 1017 5 130
Carbohydrate Binding Module 6 (CBM6); appended mainly to glycoside hydrolase (GH) family 16 alpha- and beta agarases. This family includes carbohydrate binding module 6 (CBM6) domains that are appended mainly to glycoside hydrolase (GH) family 16 agarases. These CBM6s are non-catalytic carbohydrate binding domains that facilitate the activity of alpha- and beta-agarase catalytic modules which are involved in the hydrolysis of 1,4-beta-D-galactosidic linkages. These CBM6s bind specifically to the non-reducing end of agarose chains, recognizing only the first repeat of the disaccharide, and directing the appended catalytic modules to areas of the plant cell wall attacked by beta-agarases. CBM6 is an unusual CBM as it represents a chimera of two distinct binding sites with different modes of binding: binding site I within the loop regions and binding site II on the concave face of the beta-sandwich fold. This family includes three tandem CBM6s from the Saccharophagus degradans agarase Aga86E, and three tandem CBM6s from Vibrio sp. strain PO-303 AgaA; in both these proteins these are appended to a GH16 domain. Vibrio AgaA also contains a Big-2-like protein-protein interaction domain. This family also includes two tandem CBM6s from an endo-type beta-agarase from a deep-sea Microbulbifer-like isolate, which are appended to a GH16 domain, and two of three CBM6s of Alteromonas agarilytica AgaA alpha-agarase, which are appended to a GH96 domain.
COG1196 Smc 0.001 1195 1470 555 863
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning].
pfam12733 Cadherin-like 0.003 1047 1112 10 87
Cadherin-like beta sandwich domain. This domain is found in several bacterial, metazoan and chlorophyte algal proteins. A profile-profile comparison recovered the cadherin domain and a comparison of the predicted structure of this domain with the crystal structure of the cadherin showed a congruent seven stranded secondary structure. The domain is widespread in bacteria and seen in the firmicutes, actinobacteria, certain proteobacteria, bacteroides and chlamydiae with an expansion in Clostridium. In contrast, it is limited in its distribution in eukaryotes suggesting that it was derived through lateral transfer from bacteria. In prokaryotes, this domain is widely fused to other domains such as FNIII (Fibronectin Type III), TIG, SLH (S-layer homology), discoidin, cell-wall-binding repeat domain and alpha-amylase-like glycohydrolases. These associations are suggestive of a carbohydrate-binding function for this cadherin-like domain. In animal proteins it is associated with an ATP-grasp domain.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AYE35145.1 7.04e-198 323 1472 26 1294
AZG68471.1 6.23e-126 293 761 73 560
QNK55088.1 3.31e-70 319 869 44 544
QJD84649.1 3.12e-66 333 868 255 739
QNK55089.1 8.74e-65 316 868 239 740

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
7V6M_A 1.36e-34 333 855 9 568
ChainA, Fibronectin type III domain-containing protein [Tyzzerella nexilis]
6KQT_A 3.13e-24 335 705 247 620
CrystalStructure of GH136 lacto-N-biosidase from Eubacterium ramulus - native protein [Eubacterium ramulus ATCC 29099]
6KQS_A 1.54e-22 335 705 247 620
CrystalStructure of GH136 lacto-N-biosidase from Eubacterium ramulus - selenomethionine derivative [Eubacterium ramulus ATCC 29099]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
E8MGH9 1.63e-08 1259 1445 1666 1862
Beta-L-arabinobiosidase OS=Bifidobacterium longum subsp. longum (strain ATCC 15707 / DSM 20219 / JCM 1217 / NCTC 11818 / E194b) OX=565042 GN=hypBA2 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
0.000402 0.998462 0.000523 0.000214 0.000209 0.000175

TMHMM  Annotations      download full data without filtering help

start end
1475 1497