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CAZyme Information: MGYG000003583_01057

You are here: Home > Sequence: MGYG000003583_01057

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 Ruminococcus_C sp900770195
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Ruminococcus_C; Ruminococcus_C sp900770195
CAZyme ID MGYG000003583_01057
CAZy Family PL1
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
958 MGYG000003583_56|CGC2 105364.17 5.3883
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003583 2191682 MAG Fiji Oceania
Gene Location Start: 93707;  End: 96583  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003583_01057.

CAZyme Signature Domains help

Family Start End Evalue family coverage
PL1 266 450 2.7e-55 0.9076923076923077
CBM13 721 878 2.2e-21 0.7925531914893617
CBM13 566 715 2e-20 0.723404255319149

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG3866 PelB 7.11e-38 176 522 17 341
Pectate lyase [Carbohydrate transport and metabolism].
pfam14200 RicinB_lectin_2 9.54e-20 700 794 1 88
Ricin-type beta-trefoil lectin domain-like.
pfam00544 Pec_lyase_C 5.31e-19 235 447 1 208
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.
smart00656 Amb_all 2.41e-17 262 450 10 186
Amb_all domain.
pfam14200 RicinB_lectin_2 3.16e-17 652 749 2 89
Ricin-type beta-trefoil lectin domain-like.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
CBL16867.1 0.0 37 937 33 892
CDM68184.1 5.70e-121 40 624 29 584
CDM70399.1 2.17e-107 40 710 31 697
QHZ48014.1 4.24e-98 35 531 26 484
VEB20252.1 8.25e-98 37 523 28 479

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3ZSC_A 6.76e-11 202 444 14 226
Catalyticfunction and substrate recognition of the pectate lyase from Thermotoga maritima [Thermotoga maritima]
5B2H_A 1.79e-09 635 761 163 280
Crystalstructure of HA33 from Clostridium botulinum serotype C strain Yoichi [Clostridium botulinum],5B2H_B Crystal structure of HA33 from Clostridium botulinum serotype C strain Yoichi [Clostridium botulinum]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P94449 3.97e-63 187 524 33 338
Pectin lyase OS=Bacillus subtilis OX=1423 GN=pelB PE=1 SV=1
O34819 2.32e-60 187 524 33 338
Pectin lyase OS=Bacillus subtilis (strain 168) OX=224308 GN=pelB PE=3 SV=1
P27027 8.20e-48 189 523 10 304
Pectin lyase OS=Pseudomonas marginalis OX=298 GN=pnl PE=1 SV=2
P24112 6.74e-40 186 523 7 306
Pectin lyase OS=Pectobacterium carotovorum OX=554 GN=pnl PE=1 SV=1
Q00645 5.82e-11 195 427 39 234
Pectate lyase plyB OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=plyB 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
0.000352 0.998776 0.000398 0.000156 0.000152 0.000144

TMHMM  Annotations      download full data without filtering help

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