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CAZyme Information: EPrPIT00000017681-p1

You are here: Home > Sequence: EPrPIT00000017681-p1

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 Globisporangium irregulare
Lineage Oomycota; NA; ; Pythiaceae; Globisporangium; Globisporangium irregulare
CAZyme ID EPrPIT00000017681-p1
CAZy Family GH1
CAZyme Description Glycoside hydrolase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
546 PirrDAOMBR486_SC0252|CGC1 57506.64 4.2701
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_GirregulareDAOMBR486 13869 1223557 65 13804
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in EPrPIT00000017681-p1.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH5 49 361 2.3e-84 0.9903225806451613

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
225344 BglC 1.56e-34 52 369 44 378
Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism].
395098 Cellulase 3.34e-28 46 354 1 270
Cellulase (glycosyl hydrolase family 5).
225789 LacZ 0.002 37 96 281 339
Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism].
411343 exchanger_TraA 0.009 397 497 489 575
outer membrane exchange protein TraA. TraA, together with its partner TraB, mediates a large scale exchange of outer membrane lipoproteins, and lipids, between closely related strains or clonally identical cells, certain delta-proteobacterial species such as Myxococcus xanthus. The exchange mechanism is likely to involve fusion of outer membrane, probably done to coordinate the social behaviors these bacteria display.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
8.26e-240 35 540 21 521
3.00e-71 35 386 3 367
1.59e-68 48 405 48 408
1.68e-68 48 378 49 378
1.92e-68 52 407 53 407

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
8.43e-62 48 383 23 377
Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],3W6M_B Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],3W6M_C Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],4DM2_A Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],4DM2_B Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],4DM2_C Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3]
1.65e-61 48 383 23 377
The Crystal Structure of Cellulase-Inhibitor Complex. [Pyrococcus horikoshii OT3],3VVG_B The Crystal Structure of Cellulase-Inhibitor Complex. [Pyrococcus horikoshii OT3],3VVG_C The Crystal Structure of Cellulase-Inhibitor Complex. [Pyrococcus horikoshii OT3],3W6L_A Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],3W6L_B Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],3W6L_C Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],4DM1_A Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],4DM1_B Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3],4DM1_C Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase [Pyrococcus horikoshii OT3]
1.72e-61 48 384 56 411
Crystal analysis of the complex structure, E342A-cellotetraose, of endocellulase from pyrococcus horikoshii [Pyrococcus horikoshii],3QHM_B Crystal analysis of the complex structure, E342A-cellotetraose, of endocellulase from pyrococcus horikoshii [Pyrococcus horikoshii],3QHM_C Crystal analysis of the complex structure, E342A-cellotetraose, of endocellulase from pyrococcus horikoshii [Pyrococcus horikoshii]
1.93e-61 48 387 16 356
Acidothermus Cellulolyticus Endocellulase E1 Catalytic Domain In Complex With A Cellotetraose [Acidothermus cellulolyticus],1ECE_B Acidothermus Cellulolyticus Endocellulase E1 Catalytic Domain In Complex With A Cellotetraose [Acidothermus cellulolyticus]
1.93e-61 48 387 16 356
Chain A, ENDOCELLULASE E1 FROM A. CELLULOLYTICUS [Acidothermus cellulolyticus],1VRX_B Chain B, ENDOCELLULASE E1 FROM A. CELLULOLYTICUS [Acidothermus cellulolyticus]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.74e-63 56 382 57 382
Endoglucanase OS=Paenibacillus polymyxa OX=1406 PE=3 SV=2
1.20e-58 48 387 57 397
Endoglucanase E1 OS=Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B) OX=351607 GN=Acel_0614 PE=1 SV=1
9.11e-50 55 389 44 376
Major extracellular endoglucanase OS=Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25) OX=190485 GN=engXCA PE=1 SV=2
1.19e-37 52 382 644 997
Endoglucanase/exoglucanase B OS=Caldicellulosiruptor saccharolyticus OX=44001 GN=celB PE=3 SV=1
2.78e-35 54 382 61 444
Endoglucanase G OS=Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) OX=203119 GN=celG PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000062 0.000000

TMHMM  Annotations      download full data without filtering help

Start End
523 545