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CAZyme Information: MGYG000003337_01195
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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 sp900765125 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Ruminococcus_C; Ruminococcus_C sp900765125 | |||||||||||
| CAZyme ID | MGYG000003337_01195 | |||||||||||
| CAZy Family | GH48 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 42; End: 2108 Strand: + | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH48 | 2 | 272 | 5e-98 | 0.4157119476268412 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| pfam02011 | Glyco_hydro_48 | 1.02e-147 | 4 | 519 | 201 | 620 | Glycosyl hydrolase family 48. Members of this family are endoglucanase EC:3.2.1.4 and exoglucanase EC:3.2.1.91 enzymes that cleave cellulose or related substrate. |
| cd14256 | Dockerin_I | 9.93e-12 | 620 | 676 | 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. |
| pfam02368 | Big_2 | 6.70e-08 | 558 | 599 | 35 | 77 | Bacterial Ig-like domain (group 2). This family consists of bacterial domains with an Ig-like fold. Members of this family are found in bacterial and phage surface proteins such as intimins. |
| pfam08428 | Rib | 1.08e-04 | 536 | 605 | 1 | 76 | Rib/alpha-like repeat. The region featured in this family is found repeated in a number of bacterial surface proteins, such as Rib and alpha. These are expressed by group B streptococci, and Rib is thought to confer protective immunity. |
| COG5492 | YjdB | 1.54e-04 | 533 | 608 | 184 | 268 | Uncharacterized conserved protein YjdB, contains Ig-like domain [General function prediction only]. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| CBL17316.1 | 4.32e-180 | 1 | 681 | 265 | 799 |
| AAR01217.1 | 4.10e-164 | 1 | 524 | 255 | 776 |
| CAS03459.1 | 1.55e-162 | 1 | 524 | 260 | 782 |
| ADX05724.1 | 1.08e-161 | 1 | 528 | 256 | 741 |
| ADU23081.1 | 1.29e-155 | 1 | 522 | 261 | 779 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 6D5D_A | 5.08e-109 | 5 | 518 | 220 | 640 | Structureof Caldicellulosiruptor danielii GH48 module of glycoside hydrolase WP_045175321 [Caldicellulosiruptor danielii] |
| 4EL8_A | 4.39e-107 | 5 | 518 | 209 | 629 | Theunliganded structure of C.bescii CelA GH48 module [Caldicellulosiruptor bescii DSM 6725] |
| 4L0G_A | 7.88e-107 | 5 | 518 | 213 | 633 | CrystalStructure of a GH48 cellobiohydrolase from Caldicellulosiruptor bescii [Caldicellulosiruptor bescii DSM 6725],4L6X_A Crystal Structure of a GH48 cellobiohydrolase from Caldicellulosiruptor bescii [Caldicellulosiruptor bescii DSM 6725],4TXT_A Crystal Structure of a GH48 cellobiohydrolase from Caldicellulosiruptor bescii [Caldicellulosiruptor bescii DSM 6725] |
| 1F9D_A | 8.77e-100 | 12 | 521 | 220 | 629 | ChainA, ENDO-1,4-BETA-GLUCANASE F [Ruminiclostridium cellulolyticum],1FBW_A Chain A, ENDO-1,4-BETA-GLUCANASE F [Ruminiclostridium cellulolyticum],2QNO_A Chain A, Endoglucanase F [Ruminiclostridium cellulolyticum] |
| 1F9O_A | 8.77e-100 | 12 | 521 | 220 | 629 | Crystalstructure of the cellulase Cel48F from C. Cellulolyticum with the thiooligosaccharide inhibitor PIPS-IG3 [Ruminiclostridium cellulolyticum],1FAE_A Crystal structure of the cellulase CEL48F from C. cellulolyticum in complex with cellobiose [Ruminiclostridium cellulolyticum],1FBO_A Crystal structure of the cellulase CEL48F from C. cellulolyticum in complex with cellobiitol [Ruminiclostridium cellulolyticum],1FCE_A PROCESSIVE ENDOCELLULASE CELF OF CLOSTRIDIUM CELLULOLYTICUM [Ruminiclostridium cellulolyticum],1G9G_A Xtal-Structure Of The Free Native Cellulase Cel48f [Ruminiclostridium cellulolyticum] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| P22534 | 2.03e-101 | 5 | 518 | 1317 | 1737 | Endoglucanase A OS=Caldicellulosiruptor saccharolyticus OX=44001 GN=celA PE=3 SV=2 |
| P37698 | 8.97e-99 | 12 | 525 | 249 | 662 | Endoglucanase F OS=Ruminiclostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 / H10) OX=394503 GN=celCCF PE=1 SV=2 |
| P50900 | 2.65e-98 | 5 | 513 | 243 | 649 | Exoglucanase-2 OS=Thermoclostridium stercorarium (strain ATCC 35414 / DSM 8532 / NCIMB 11754) OX=1121335 GN=celY PE=1 SV=2 |
| A3DH67 | 1.05e-97 | 5 | 523 | 238 | 665 | Cellulose 1,4-beta-cellobiosidase (reducing end) CelS OS=Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) OX=203119 GN=celS PE=1 SV=1 |
| P0C2S5 | 1.05e-97 | 5 | 523 | 238 | 665 | Cellulose 1,4-beta-cellobiosidase (reducing end) CelS OS=Acetivibrio thermocellus OX=1515 GN=celS PE=1 SV=1 |
SignalP and Lipop Annotations help
This protein is predicted as OTHER
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 1.000071 | 0.000007 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |