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CAZyme Information: MGYG000000967_00061

You are here: Home > Sequence: MGYG000000967_00061

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 sp900543365
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; CAG-274; UMGS1441; UMGS1441 sp900543365
CAZyme ID MGYG000000967_00061
CAZy Family PL1
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1111 117378.85 4.4056
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000967 1698990 MAG Spain Europe
Gene Location Start: 15943;  End: 19278  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000967_00061.

CAZyme Signature Domains help

Family Start End Evalue family coverage
PL1 245 439 2.2e-36 0.8762376237623762
CBM77 581 681 3.3e-28 0.9223300970873787

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam18283 CBM77 8.97e-31 573 683 1 108
Carbohydrate binding module 77. This domain is the non-catalytic carbohydrate binding module 77 (CBM77) present in Ruminococcus flavefaciens. CBMs fulfil a critical targeting function in plant cell wall depolymerisation. In CBM77, a cluster of conserved basic residues (Lys1092, Lys1107 and Lys1162) confer calcium-independent recognition of homogalacturonan.
COG3866 PelB 3.80e-24 261 443 102 278
Pectate lyase [Carbohydrate transport and metabolism].
smart00656 Amb_all 3.59e-17 261 442 17 190
Amb_all domain.
cd08548 Type_I_cohesin_like 2.78e-11 912 1035 1 134
Type I cohesin domain, interaction partner of dockerin. 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 cohesins; their interactions with dockerin mediate assembly of a range of dockerin-borne enzymes to the complex.
cd14256 Dockerin_I 4.46e-11 1050 1106 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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
BBF42492.1 3.23e-150 3 538 2 502
ACR71161.1 1.32e-101 1 683 1 890
ADU23076.1 4.76e-98 44 553 762 1252
CDR31241.1 1.96e-92 44 537 334 806
ACX62589.1 1.26e-71 44 683 43 680

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5FU5_A 1.90e-20 570 686 3 114
Thecomplexity of the Ruminococcus flavefaciens cellulosome reflects an expansion in glycan recognition [Ruminococcus flavefaciens]
3VMV_A 1.53e-19 260 440 79 248
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]
1AIR_A 2.02e-15 217 448 50 267
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 4.85e-15 217 448 50 267
ChainA, Pectate lyase C [Dickeya chrysanthemi]
1VBL_A 1.89e-13 261 536 133 411
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
P0C1C3 1.26e-17 239 448 89 288
Pectate lyase 3 OS=Pectobacterium carotovorum subsp. carotovorum OX=555 GN=pel3 PE=3 SV=1
P0C1C2 4.05e-17 217 448 71 288
Pectate lyase 3 OS=Pectobacterium carotovorum OX=554 GN=pel3 PE=1 SV=1
Q6CZT2 5.43e-17 191 448 30 288
Pectate lyase 3 OS=Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) OX=218491 GN=pel3 PE=3 SV=1
Q8GCB2 8.82e-17 257 442 105 276
Pectate trisaccharide-lyase OS=Bacillus licheniformis OX=1402 GN=pelA PE=1 SV=1
Q65DC2 8.82e-17 257 442 105 276
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

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
0.000364 0.998814 0.000179 0.000246 0.000193 0.000170

TMHMM  Annotations      download full data without filtering help

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