Species | Merdibacter sp900543035 | |||||||||||
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Lineage | Bacteria; Firmicutes; Bacilli; Erysipelotrichales; Erysipelotrichaceae; Merdibacter; Merdibacter sp900543035 | |||||||||||
CAZyme ID | MGYG000003087_00966 | |||||||||||
CAZy Family | GH136 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 652; End: 5160 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH136 | 332 | 853 | 8.3e-97 | 0.9755600814663951 |
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. |
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 |
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] |
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 |
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 |
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