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CAZyme Information: MGYG000001183_00039

You are here: Home > Sequence: MGYG000001183_00039

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 UMGS1441 sp900551755
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; CAG-274; UMGS1441; UMGS1441 sp900551755
CAZyme ID MGYG000001183_00039
CAZy Family PL1
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1157 MGYG000001183_1|CGC1 122128.86 4.3385
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001183 2128086 MAG Austria Europe
Gene Location Start: 46850;  End: 50323  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001183_00039.

CAZyme Signature Domains help

Family Start End Evalue family coverage
PL1 241 407 4.1e-42 0.8118811881188119

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG3866 PelB 6.96e-50 96 411 2 279
Pectate lyase [Carbohydrate transport and metabolism].
smart00656 Amb_all 3.84e-30 243 409 17 190
Amb_all domain.
pfam00544 Pec_lyase_C 1.39e-18 239 405 31 211
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 2.69e-06 860 914 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.
pfam00404 Dockerin_1 0.005 861 914 1 56
Dockerin type I repeat. The dockerin repeat is the binding partner of the cohesin domain pfam00963. The cohesin-dockerin interaction is the crucial interaction for complex formation in the cellulosome. The dockerin repeats, each bearing homology to the EF-hand calcium-binding loop bind calcium.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
BCJ94010.1 3.45e-191 23 587 32 566
ACX62589.1 8.15e-189 1 600 1 573
AYB46946.1 1.90e-187 1 593 1 566
QOT09127.1 2.09e-186 1 593 1 566
ACR72247.1 2.11e-182 12 590 16 576

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3VMV_A 1.86e-24 181 407 20 248
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 4.84e-20 243 405 133 330
Structureof the thermostable pectate lyase PL 47 [Bacillus sp. TS-47]
1AIR_A 4.29e-19 212 433 63 290
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 1.04e-18 212 433 63 290
ChainA, Pectate lyase C [Dickeya chrysanthemi]
3ZSC_A 2.56e-14 245 390 71 221
Catalyticfunction and substrate recognition of the pectate lyase from Thermotoga maritima [Thermotoga maritima]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q8GCB2 2.44e-26 181 414 57 281
Pectate trisaccharide-lyase OS=Bacillus licheniformis OX=1402 GN=pelA PE=1 SV=1
Q65DC2 2.44e-26 181 414 57 281
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
B1B6T1 2.44e-26 181 414 57 281
Pectate trisaccharide-lyase OS=Bacillus sp. OX=1409 GN=pel PE=1 SV=1
Q5AVN4 1.86e-20 243 428 99 287
Pectate lyase A OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=plyA PE=1 SV=1
P0C1C1 1.21e-19 212 432 84 310
Pectate lyase 2 OS=Pectobacterium carotovorum OX=554 GN=pel2 PE=3 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
0.000329 0.999001 0.000158 0.000207 0.000159 0.000142

TMHMM  Annotations      download full data without filtering help

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