logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000000134_01364

You are here: Home > Sequence: MGYG000000134_01364

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 Longibaculum muris
Lineage Bacteria; Firmicutes; Bacilli; Erysipelotrichales; Erysipelatoclostridiaceae; Longibaculum; Longibaculum muris
CAZyme ID MGYG000000134_01364
CAZy Family GH55
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1404 MGYG000000134_7|CGC1 155295.45 4.5589
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000134 3162983 Isolate Canada North America
Gene Location Start: 5582;  End: 9796  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.39 3.2.1.58 3.2.1.-

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH55 816 1100 1e-58 0.4527027027027027

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd00063 FN3 1.58e-14 326 416 1 93
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.
smart00060 FN3 1.10e-11 326 405 1 82
Fibronectin type 3 domain. One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.
pfam00041 fn3 1.18e-08 328 409 2 85
Fibronectin type III domain.
pfam12708 Pectate_lyase_3 0.007 525 755 15 211
Pectate lyase superfamily protein. This family of proteins possesses a beta helical structure like Pectate lyase. This family is most closely related to glycosyl hydrolase family 28.
pfam06160 EzrA 0.009 1235 1319 190 275
Septation ring formation regulator, EzrA. During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QLY78983.1 0.0 13 1321 5 1269
QLY78981.1 0.0 181 1153 170 1123
BCL56920.1 0.0 7 1320 5 1341
QMW75525.1 0.0 1 1263 1 1267
QPS14140.1 0.0 1 1263 1 1267

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4PEW_A 2.18e-113 516 1114 21 543
Structureof sacteLam55A from Streptomyces sp. SirexAA-E [Streptomyces sp. SirexAA-E],4PEW_B Structure of sacteLam55A from Streptomyces sp. SirexAA-E [Streptomyces sp. SirexAA-E]
4TZ1_A 4.04e-113 516 1114 9 531
Ensemblerefinement of the E502A variant of sacteLam55A from Streptomyces sp. SirexAA-E in complex with laminaritriose [Streptomyces sp. SirexAA-E],4TZ3_A Ensemble refinement of the E502A variant of sacteLam55A from Streptomyces sp. SirexAA-E in complex with laminaritetraose [Streptomyces sp. SirexAA-E],4TZ5_A Ensemble refinement of the E502A variant of sacteLam55A from Streptomyces sp. SirexAA-E in complex with laminarihexaose [Streptomyces sp. SirexAA-E],4TZ5_B Ensemble refinement of the E502A variant of sacteLam55A from Streptomyces sp. SirexAA-E in complex with laminarihexaose [Streptomyces sp. SirexAA-E]
4TYV_A 4.28e-113 516 1114 11 533
Ensemblerefinement of the E502A variant of sacteLam55A from Streptomyces sp. SirexAA-E in complex with glucose [Streptomyces sp. SirexAA-E],4TYV_B Ensemble refinement of the E502A variant of sacteLam55A from Streptomyces sp. SirexAA-E in complex with glucose [Streptomyces sp. SirexAA-E]
4PEX_A 5.78e-113 516 1114 21 543
Structureof the E502A variant of sacteLam55A from Streptomyces sp. SirexAA-E in complex with glucose [Streptomyces sp. SirexAA-E],4PEX_B Structure of the E502A variant of sacteLam55A from Streptomyces sp. SirexAA-E in complex with glucose [Streptomyces sp. SirexAA-E],4PEY_A Structure of the E502A variant of sacteLam55A from Streptomyces sp. SirexAA-E in complex with laminaritriose [Streptomyces sp. SirexAA-E],4PEZ_A Structure of the E502A variant of sacteLam55A from Streptomyces sp. SirexAA-E in complex with laminaritetraose [Streptomyces sp. SirexAA-E],4PF0_A Structure of the E502A variant of sacteLam55A from Streptomyces sp. SirexAA-E in complex with laminarihexaose [Streptomyces sp. SirexAA-E],4PF0_B Structure of the E502A variant of sacteLam55A from Streptomyces sp. SirexAA-E in complex with laminarihexaose [Streptomyces sp. SirexAA-E]
3TEU_A 8.96e-06 323 397 2 72
Crystalstructure of fibcon

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
G2NFJ9 1.64e-112 516 1114 65 587
Exo-beta-1,3-glucanase OS=Streptomyces sp. (strain SirexAA-E / ActE) OX=862751 GN=SACTE_4363 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
0.000228 0.999092 0.000176 0.000184 0.000156 0.000143

TMHMM  Annotations      download full data without filtering help

start end
9 31
1379 1398