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CAZyme Information: MGYG000004570_00515

You are here: Home > Sequence: MGYG000004570_00515

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 Treponema_D berlinense
Lineage Bacteria; Spirochaetota; Spirochaetia; Treponematales; Treponemataceae; Treponema_D; Treponema_D berlinense
CAZyme ID MGYG000004570_00515
CAZy Family PL1
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1257 130963.11 7.7553
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004570 2364040 MAG France Europe
Gene Location Start: 185455;  End: 189228  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004570_00515.

CAZyme Signature Domains help

Family Start End Evalue family coverage
PL9 850 1235 1.1e-115 0.9466666666666667
PL1 254 423 2.4e-46 0.8118811881188119

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG3866 PelB 9.42e-50 239 542 82 340
Pectate lyase [Carbohydrate transport and metabolism].
smart00656 Amb_all 2.43e-30 253 425 14 190
Amb_all domain.
pfam00544 Pec_lyase_C 5.76e-17 254 421 34 211
Pectate lyase. This enzyme forms a right handed beta helix structure. Pectate lyase is an enzyme involved in the maceration and soft rotting of plant tissue.
pfam13229 Beta_helix 1.07e-06 929 1123 2 157
Right handed beta helix region. This region contains a parallel beta helix region that shares some similarity with Pectate lyases.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
ADL51369.1 2.33e-247 77 1248 60 1253
AUS06374.1 2.28e-244 78 1131 26 1152
QQY81127.1 1.86e-241 78 1131 26 1152
AOR96287.1 4.69e-211 57 1249 38 1091
QMW93302.1 1.00e-209 57 1249 38 1091

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1RU4_A 3.35e-33 827 1134 4 298
ChainA, Pectate lyase [Dickeya chrysanthemi]
3VMV_A 1.86e-22 257 423 81 248
Crystalstructure of pectate lyase Bsp165PelA from Bacillus sp. N165 [Bacillus sp. N16-5],3VMW_A Crystal structure of pectate lyase Bsp165PelA from Bacillus sp. N165 in complex with trigalacturonate [Bacillus sp. N16-5]
1VBL_A 3.13e-17 258 421 135 330
Structureof the thermostable pectate lyase PL 47 [Bacillus sp. TS-47]
3ZSC_A 3.80e-14 239 398 53 213
Catalyticfunction and substrate recognition of the pectate lyase from Thermotoga maritima [Thermotoga maritima]
5AMV_A 1.99e-13 258 419 130 323
Structuralinsights into the loss of catalytic competence in pectate lyase at low pH [Bacillus subtilis],5X2I_A Polygalacturonate Lyase by Fusing with a Self-assembling Amphipathic Peptide [Bacillus subtilis subsp. subtilis str. 168]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P0C1A7 2.88e-32 827 1134 29 323
Pectate lyase L OS=Dickeya dadantii (strain 3937) OX=198628 GN=pelL PE=1 SV=1
P0C1A6 5.22e-32 851 1134 53 323
Pectate lyase L OS=Dickeya chrysanthemi OX=556 GN=pelL PE=3 SV=1
P22751 5.52e-27 861 1134 411 646
Pectate disaccharide-lyase OS=Dickeya chrysanthemi OX=556 GN=pelX PE=1 SV=1
Q65DC2 2.71e-26 199 429 60 280
Pectate trisaccharide-lyase OS=Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46) OX=279010 GN=BLi04129 PE=3 SV=1
Q8GCB2 2.71e-26 199 429 60 280
Pectate trisaccharide-lyase OS=Bacillus licheniformis OX=1402 GN=pelA PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as LIPO

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000000 0.000002 1.000064 0.000000 0.000000 0.000000

TMHMM  Annotations      download full data without filtering help

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