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CAZyme Information: MGYG000002295_01129

You are here: Home > Sequence: MGYG000002295_01129

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 callidus
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Ruminococcus_C; Ruminococcus_C callidus
CAZyme ID MGYG000002295_01129
CAZy Family PL1
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1208 127416.87 4.3851
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002295 2957494 Isolate China Asia
Gene Location Start: 183704;  End: 187330  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002295_01129.

CAZyme Signature Domains help

Family Start End Evalue family coverage
PL9 609 1021 1.7e-122 0.9813333333333333
PL1 236 406 3e-44 0.8217821782178217

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG3866 PelB 1.05e-50 107 520 2 345
Pectate lyase [Carbohydrate transport and metabolism].
smart00656 Amb_all 8.58e-32 238 408 15 190
Amb_all domain.
pfam00544 Pec_lyase_C 2.97e-22 212 404 1 211
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.
cd14256 Dockerin_I 1.81e-13 1142 1198 1 57
Type I dockerin repeat domain. Bacterial cohesin domains bind to a complementary protein domain named dockerin, and this interaction is required for the formation of the cellulosome, a cellulose-degrading complex. The cellulosome consists of scaffoldin, a noncatalytic scaffolding polypeptide, that comprises repeating cohesion modules and a single carbohydrate-binding module (CBM). Specific calcium-dependent interactions between cohesins and dockerins appear to be essential for cellulosome assembly. This subfamily represents type I dockerins, which are responsible for anchoring a variety of enzymatic domains to the complex.
cd14253 Dockerin 1.59e-05 1143 1198 1 56
Dockerin repeat domain. Dockerins are modules in the cellulosome complex that often anchor catalytic subunits by binding to cohesin domains of scaffolding proteins. Three types of dockerins and their corresponding cohesin have been described in the literature. This alignment models two consecutive dockerin repeats, the functional unit.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AOR96287.1 3.41e-276 32 1024 37 1083
QMW93302.1 1.20e-273 32 1024 37 1083
BBK78741.1 1.20e-273 32 1024 37 1083
ACR72247.1 3.72e-268 49 1019 40 1047
ADL51369.1 2.54e-263 4 1026 8 1244

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1RU4_A 9.39e-31 612 893 18 292
ChainA, Pectate lyase [Dickeya chrysanthemi]
3VMV_A 1.44e-21 198 467 33 311
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]
1AIR_A 3.90e-16 151 451 13 293
ChainA, PECTATE LYASE C [Dickeya chrysanthemi],1O88_A Chain A, Pectate Lyase C [Dickeya chrysanthemi],1O8D_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi],1O8E_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi],1O8F_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi],1O8G_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi],1O8H_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi],1O8I_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi],1O8J_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi],1O8K_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi],1O8L_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi],1O8M_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi],1PLU_A Chain A, Protein (pectate Lyase C) [Dickeya chrysanthemi],2PEC_A Chain A, PECTATE LYASE C [Dickeya chrysanthemi]
2EWE_A 9.37e-16 151 451 13 293
ChainA, Pectate lyase C [Dickeya chrysanthemi]
1VBL_A 1.24e-15 242 404 135 330
Structureof the thermostable pectate lyase PL 47 [Bacillus sp. TS-47]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P22751 2.62e-34 608 926 388 677
Pectate disaccharide-lyase OS=Dickeya chrysanthemi OX=556 GN=pelX PE=1 SV=1
P0C1A6 5.37e-31 612 893 43 317
Pectate lyase L OS=Dickeya chrysanthemi OX=556 GN=pelL PE=3 SV=1
P0C1A7 7.82e-30 612 893 43 317
Pectate lyase L OS=Dickeya dadantii (strain 3937) OX=198628 GN=pelL PE=1 SV=1
Q65DC2 2.26e-21 188 413 60 281
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 2.26e-21 188 413 60 281
Pectate trisaccharide-lyase OS=Bacillus licheniformis OX=1402 GN=pelA 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
0.000250 0.999045 0.000175 0.000188 0.000164 0.000143

TMHMM  Annotations      download full data without filtering help

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