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CAZyme Information: MGYG000001402_02662

You are here: Home > Sequence: MGYG000001402_02662

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 Coprobacillus cateniformis
Lineage Bacteria; Firmicutes; Bacilli; Erysipelotrichales; Erysipelatoclostridiaceae; Coprobacillus; Coprobacillus cateniformis
CAZyme ID MGYG000001402_02662
CAZy Family GH55
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1155 MGYG000001402_1|CGC45 128002.08 4.7936
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001402 3861289 Isolate not provided not provided
Gene Location Start: 2698793;  End: 2702260  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.- 3.2.1.39 3.2.1.58

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH55 799 1065 1.1e-62 0.4337837837837838

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd00063 FN3 7.59e-11 320 406 1 90
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 9.25e-09 320 400 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 4.02e-06 325 402 5 85
Fibronectin type III domain.
pfam12708 Pectate_lyase_3 3.54e-05 554 716 38 190
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.
COG3401 FN3 0.006 431 541 179 284
Fibronectin type 3 domain [General function prediction only].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QLY78983.1 0.0 31 1145 30 1123
QLY78981.1 0.0 31 1145 30 1129
BCL56920.1 1.23e-302 149 1139 155 1181
QMW75525.1 7.54e-301 32 1139 30 1161
QPS14140.1 7.54e-301 32 1139 30 1161

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4TZ1_A 2.91e-118 511 1103 9 532
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]
4PEW_A 3.00e-118 511 1103 21 544
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]
4TYV_A 3.09e-118 511 1103 11 534
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 4.18e-118 511 1103 21 544
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
G2NFJ9 1.15e-117 511 1103 65 588
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
0.000213 0.999140 0.000173 0.000166 0.000152 0.000142

TMHMM  Annotations      download full data without filtering help

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