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CAZyme Information: MGYG000004223_01551

You are here: Home > Sequence: MGYG000004223_01551

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 UMGS1883 sp900763305
Lineage Bacteria; Firmicutes_A; Clostridia; UMGS1883; UMGS1883; UMGS1883; UMGS1883 sp900763305
CAZyme ID MGYG000004223_01551
CAZy Family PL35
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1440 MGYG000004223_12|CGC1 160202.38 4.7603
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004223 2575981 MAG United Kingdom Europe
Gene Location Start: 56200;  End: 60522  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004223_01551.

CAZyme Signature Domains help

Family Start End Evalue family coverage
PL35 957 1133 1.9e-32 0.9776536312849162
CBM32 1322 1434 3.4e-18 0.8790322580645161

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam00754 F5_F8_type_C 2.22e-15 1310 1434 1 127
F5/8 type C domain. This domain is also known as the discoidin (DS) domain family.
smart00231 FA58C 2.99e-05 1313 1434 9 134
Coagulation factor 5/8 C-terminal domain, discoidin domain. Cell surface-attached carbohydrate-binding domain, present in eukaryotes and assumed to have horizontally transferred to eubacterial genomes.
pfam07833 Cu_amine_oxidN1 7.10e-04 478 543 1 71
Copper amine oxidase N-terminal domain. Copper amine oxidases catalyze the oxidative deamination of primary amines to the corresponding aldehydes, while reducing molecular oxygen to hydrogen peroxide. These enzymes are dimers of identical subunits, each comprising four domains. The N-terminal domain, which is absent in some amine oxidases, consists of a five-stranded antiparallel beta sheet twisted around an alpha helix. The D1 domains from the two subunits comprise the 'stalk' of the mushroom-shaped dimer, and interact with each other but do not pack tightly against each other.
pfam07940 Hepar_II_III 0.001 962 1129 29 191
Heparinase II/III-like protein. This family features sequences that are similar to a region of the Flavobacterium heparinum proteins heparinase II and heparinase III. The former is known to degrade heparin and heparin sulphate, whereas the latter predominantly degrades heparin sulphate. Both are secreted into the periplasmic space upon induction with heparin.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
ALS27107.1 6.27e-107 608 1433 699 1507
AZS17848.1 1.17e-105 350 1433 157 1273
QNK58643.1 1.17e-98 608 1433 794 1605
QNK56587.1 1.23e-98 602 1433 214 1022
QUH30172.1 1.57e-98 591 1430 58 886

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5ZU6_A 5.25e-16 1326 1431 45 151
ACBM32 derived from alginate lyase B (AlyB-OU02) [Vibrio]
7D29_A 1.67e-14 1326 1433 22 128
CBM32of AlyQ [Persicobacter sp. CCB-QB2],7D2A_A CBM32 of AlyQ in complex with 4,5-unsaturated mannuronic acid [Persicobacter sp. CCB-QB2]
5ZU5_A 3.27e-14 1326 1431 45 151
Crystalstructure of a full length alginate lyase with CBM domain [Vibrio splendidus]
5XNR_A 7.32e-13 1326 1433 22 128
TruncatedAlyQ with CBM32 and alginate lyase domains [Persicobacter sp. CCB-QB2]

Swiss-Prot Hits      help

has no Swissprot hit.

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
0.000297 0.999048 0.000180 0.000167 0.000157 0.000142

TMHMM  Annotations      download full data without filtering help

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