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CAZyme Information: MGYG000001024_01586

You are here: Home > Sequence: MGYG000001024_01586

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 HGM11521 sp900751885
Lineage Bacteria; Firmicutes_A; Clostridia; Monoglobales_A; UBA1381; HGM11521; HGM11521 sp900751885
CAZyme ID MGYG000001024_01586
CAZy Family GH146
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
940 106569.93 5.0114
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001024 2614111 MAG Sweden Europe
Gene Location Start: 5445;  End: 8267  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001024_01586.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH146 26 574 1.6e-157 0.9980119284294234

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam07944 Glyco_hydro_127 6.42e-112 26 574 1 503
Beta-L-arabinofuranosidase, GH127. One member of this family, from Bidobacterium longicum, UniProtKB:E8MGH8, has been characterized as an unusual beta-L-arabinofuranosidase enzyme, EC:3.2.1.185. It rleases l-arabinose from the l-arabinofuranose (Araf)-beta1,2-Araf disaccharide and also transglycosylates 1-alkanols with retention of the anomeric configuration. Terminal beta-l-arabinofuranosyl residues have been found in arabinogalactan proteins from a mumber of different plantt species. beta-l-Arabinofuranosyl linkages with 1-4 arabinofuranosides are also found in the sugar chains of extensin and solanaceous lectins, hydroxyproline (Hyp)2-rich glycoproteins that are widely observed in plant cell wall fractions. The critical residue for catalytic activity is Glu-338, in a ET/SCAS sequence context.
COG3533 COG3533 3.68e-75 27 654 12 572
Uncharacterized conserved protein, DUF1680 family [Function unknown].
pfam12733 Cadherin-like 2.86e-05 854 934 5 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
QJW37681.1 6.78e-247 19 936 369 1293
QDP74899.1 7.48e-246 19 936 369 1293
ARU52215.1 4.16e-245 19 936 369 1293
ARK06383.1 4.16e-245 19 936 369 1293
QUB98427.1 1.64e-244 19 936 369 1293

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6YQH_AAA 1.96e-91 12 802 18 780
ChainAAA, Acetyl-CoA carboxylase, biotin carboxylase [Bacteroides thetaiotaomicron VPI-5482]
5OPJ_A 3.21e-86 12 802 18 780
Beta-L-arabinofuranosidase[Bacteroides thetaiotaomicron]

Swiss-Prot Hits      help

has no Swissprot hit.

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
1.000036 0.000001 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001024_01586.