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CAZyme Information: MGYG000004781_00465

You are here: Home > Sequence: MGYG000004781_00465

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; Lachnospiraceae; UMGS680;
CAZyme ID MGYG000004781_00465
CAZy Family CE17
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
371 MGYG000004781_3|CGC2 42388.06 5.9536
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004781 3497015 MAG China Asia
Gene Location Start: 53195;  End: 54310  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004781_00465.

CAZyme Signature Domains help

Family Start End Evalue family coverage
CE17 26 188 1.1e-77 0.9878787878787879
CBM35inCE17 229 370 3.8e-61 0.9463087248322147

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd00229 SGNH_hydrolase 1.92e-20 24 198 1 187
SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the typical Ser-His-Asp(Glu) triad from other serine hydrolases, but may lack the carboxlic acid.
pfam13472 Lipase_GDSL_2 2.89e-17 26 188 1 174
GDSL-like Lipase/Acylhydrolase family. This family of presumed lipases and related enzymes are similar to pfam00657.
cd01834 SGNH_hydrolase_like_2 3.82e-17 26 197 6 190
SGNH_hydrolase subfamily. SGNH hydrolases are a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases.
COG2755 TesA 3.08e-09 23 201 10 210
Lysophospholipase L1 or related esterase [Amino acid transport and metabolism].
pfam00657 Lipase_GDSL 1.75e-07 24 195 1 224
GDSL-like Lipase/Acylhydrolase.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
CBL01980.1 1.26e-154 1 371 1 359
AXB29270.1 7.91e-151 1 371 1 359
CBK82540.1 4.12e-147 5 371 5 384
BCN32107.1 1.94e-127 3 369 14 368
BCJ92770.1 2.36e-125 5 371 16 372

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6HH9_A 1.17e-121 6 369 17 367
Crystalstructure of a two-domain esterase (CEX) active on acetylated mannans co-crystallized with mannopentaose [Roseburia intestinalis L1-82],6HH9_B Crystal structure of a two-domain esterase (CEX) active on acetylated mannans co-crystallized with mannopentaose [Roseburia intestinalis L1-82],6HH9_C Crystal structure of a two-domain esterase (CEX) active on acetylated mannans co-crystallized with mannopentaose [Roseburia intestinalis L1-82],6HH9_D Crystal structure of a two-domain esterase (CEX) active on acetylated mannans co-crystallized with mannopentaose [Roseburia intestinalis L1-82]
6HFZ_A 2.69e-120 6 369 17 367
Crystalstructure of a two-domain esterase (CEX) active on acetylated mannans [Roseburia intestinalis L1-82],6HFZ_B Crystal structure of a two-domain esterase (CEX) active on acetylated mannans [Roseburia intestinalis L1-82],6HFZ_C Crystal structure of a two-domain esterase (CEX) active on acetylated mannans [Roseburia intestinalis L1-82],6HFZ_D Crystal structure of a two-domain esterase (CEX) active on acetylated mannans [Roseburia intestinalis L1-82]

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
1.000052 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004781_00465.