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CAZyme Information: MGYG000001304_01649
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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 | Erysipelatoclostridium spiroforme | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes; Bacilli; Erysipelotrichales; Erysipelatoclostridiaceae; Erysipelatoclostridium; Erysipelatoclostridium spiroforme | |||||||||||
| CAZyme ID | MGYG000001304_01649 | |||||||||||
| CAZy Family | CBM32 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 369505; End: 372072 Strand: + | |||||||||||
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| pfam17996 | CE2_N | 1.56e-05 | 93 | 166 | 11 | 80 | Carbohydrate esterase 2 N-terminal. This is the N-terminal beta-sheet domain with jelly roll topology found in CE2 acetyl-esterase from the bacterium Clostridium thermocellum. This enzyme displays dual activities, it catalyses the deacetylation of plant polysaccharides and also potentiates the activity of its appended cellulase catalytic module through its noncatalytic cellulose binding function. This N-terminal jelly-roll domain appears to extend the substrate/cellulose binding cleft of the catalytic domain in C.thermocellum. |
| pfam07554 | FIVAR | 2.17e-05 | 521 | 582 | 4 | 68 | FIVAR domain. This domain is found in a wide variety of contexts, but mostly occurring in cell wall associated proteins. A lack of conserved catalytic residues suggests that it is a binding domain. From context, possible substrates are hyaluronate or fibronectin (personal obs: C Yeats). This is further evidenced by. Possibly the exact substrate is N-acetyl glucosamine. Finding it in the same protein as pfam05089 further supports this proposal. It is found in the C-terminal part of Bacillus sp. Gellan lyase, which is removed during maturation. Some of the proteins it is found in are involved in methicillin resistance. The name FIVAR derives from Found In Various Architectures. |
| pfam07554 | FIVAR | 2.14e-04 | 732 | 790 | 3 | 68 | FIVAR domain. This domain is found in a wide variety of contexts, but mostly occurring in cell wall associated proteins. A lack of conserved catalytic residues suggests that it is a binding domain. From context, possible substrates are hyaluronate or fibronectin (personal obs: C Yeats). This is further evidenced by. Possibly the exact substrate is N-acetyl glucosamine. Finding it in the same protein as pfam05089 further supports this proposal. It is found in the C-terminal part of Bacillus sp. Gellan lyase, which is removed during maturation. Some of the proteins it is found in are involved in methicillin resistance. The name FIVAR derives from Found In Various Architectures. |
| TIGR02168 | SMC_prok_B | 0.001 | 506 | 788 | 748 | 1024 | chromosome segregation protein SMC, common bacterial type. SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins] |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| QHB23055.1 | 2.46e-154 | 1 | 791 | 500 | 1393 |
| QEI30547.1 | 2.46e-154 | 1 | 791 | 500 | 1393 |
| QRT29448.1 | 3.45e-154 | 1 | 791 | 500 | 1393 |
| PLT74914.1 | 4.52e-152 | 1 | 529 | 499 | 1022 |
| QPK81604.1 | 5.84e-151 | 1 | 523 | 490 | 1013 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 6TR3_A | 3.42e-20 | 1 | 93 | 461 | 552 | Ruminococcusgnavus GH29 fucosidase E1_10125 in complex with fucose [[Ruminococcus] gnavus E1] |
| 6TR4_A | 3.42e-20 | 1 | 93 | 461 | 552 | Ruminococcusgnavus GH29 fucosidase E1_10125 D221A mutant in complex with fucose [[Ruminococcus] gnavus E1],6TR4_B Ruminococcus gnavus GH29 fucosidase E1_10125 D221A mutant in complex with fucose [[Ruminococcus] gnavus E1] |
| 2JNK_A | 3.93e-06 | 728 | 788 | 2 | 70 | Solutionstructure of a dockerin-containing modular pair from a family 84 glycoside hydrolase [Clostridium perfringens],2OZN_B The Cohesin-Dockerin Complex of NagJ and NagH from Clostridium perfringens [Clostridium perfringens] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| E8MGH9 | 2.59e-13 | 577 | 841 | 1654 | 1932 | Beta-L-arabinobiosidase OS=Bifidobacterium longum subsp. longum (strain ATCC 15707 / DSM 20219 / JCM 1217 / NCTC 11818 / E194b) OX=565042 GN=hypBA2 PE=1 SV=1 |
| P26831 | 9.85e-11 | 620 | 788 | 1386 | 1566 | Hyaluronoglucosaminidase OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=nagH PE=1 SV=2 |
| P0DTR5 | 1.19e-08 | 44 | 176 | 688 | 820 | A type blood alpha-D-galactosamine galactosaminidase OS=Flavonifractor plautii OX=292800 PE=1 SV=1 |
| Q9L7Q2 | 3.48e-07 | 472 | 678 | 428 | 640 | Zinc metalloprotease ZmpB OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=zmpB PE=3 SV=2 |
| P0DTR4 | 2.48e-06 | 74 | 176 | 663 | 765 | A type blood N-acetyl-alpha-D-galactosamine deacetylase OS=Flavonifractor plautii OX=292800 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 |
|---|---|---|---|---|---|
| 1.000065 | 0.000001 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
