Species | Erysipelatoclostridium spiroforme | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes; Bacilli; Erysipelotrichales; Erysipelatoclostridiaceae; Erysipelatoclostridium; Erysipelatoclostridium spiroforme | |||||||||||
CAZyme ID | MGYG000001304_01643 | |||||||||||
CAZy Family | GH123 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 354072; End: 358031 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH123 | 405 | 978 | 5.2e-157 | 0.9776951672862454 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam13320 | DUF4091 | 8.06e-16 | 858 | 929 | 2 | 66 | Domain of unknown function (DUF4091). This presumed domain is functionally uncharacterized. This domain family is found in bacteria, archaea and eukaryotes, and is approximately 70 amino acids in length. There is a single completely conserved residue G that may be functionally important. |
pfam02368 | Big_2 | 1.08e-10 | 315 | 369 | 1 | 55 | 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. |
COG5492 | YjdB | 3.82e-06 | 310 | 459 | 177 | 318 | Uncharacterized conserved protein YjdB, contains Ig-like domain [General function prediction only]. |
pfam17996 | CE2_N | 7.68e-06 | 208 | 291 | 2 | 81 | 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 | 1.21e-04 | 1206 | 1264 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QUD71731.1 | 8.97e-308 | 10 | 988 | 16 | 995 |
AYE33261.1 | 4.15e-266 | 187 | 999 | 47 | 852 |
QAS61432.1 | 4.15e-266 | 187 | 999 | 47 | 852 |
QBJ76609.1 | 3.21e-231 | 401 | 988 | 6 | 580 |
ATD58699.1 | 3.21e-231 | 401 | 988 | 6 | 580 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
5FQE_A | 7.27e-217 | 402 | 995 | 30 | 610 | Thedetails of glycolipid glycan hydrolysis by the structural analysis of a family 123 glycoside hydrolase from Clostridium perfringens [Clostridium perfringens],5FQE_B The details of glycolipid glycan hydrolysis by the structural analysis of a family 123 glycoside hydrolase from Clostridium perfringens [Clostridium perfringens],5FQF_A The details of glycolipid glycan hydrolysis by the structural analysis of a family 123 glycoside hydrolase from Clostridium perfringens [Clostridium perfringens],5FQF_B The details of glycolipid glycan hydrolysis by the structural analysis of a family 123 glycoside hydrolase from Clostridium perfringens [Clostridium perfringens],5FR0_A The details of glycolipid glycan hydrolysis by the structural analysis of a family 123 glycoside hydrolase from Clostridium perfringens [Clostridium perfringens] |
5FQG_A | 1.13e-215 | 402 | 995 | 30 | 610 | Thedetails of glycolipid glycan hydrolysis by the structural analysis of a family 123 glycoside hydrolase from Clostridium perfringens [Clostridium perfringens],5FQH_A The details of glycolipid glycan hydrolysis by the structural analysis of a family 123 glycoside hydrolase from Clostridium perfringens [Clostridium perfringens] |
5L7V_A | 5.83e-79 | 433 | 938 | 56 | 526 | ChainA, glycoside hydrolase [Phocaeicola vulgatus ATCC 8482],5L7V_B Chain B, glycoside hydrolase [Phocaeicola vulgatus ATCC 8482] |
5L7R_A | 8.48e-79 | 433 | 938 | 71 | 541 | ChainA, glycoside hydrolase [Phocaeicola vulgatus ATCC 8482],5L7R_B Chain B, glycoside hydrolase [Phocaeicola vulgatus ATCC 8482],5L7U_A Chain A, Glycoside hydrolase [Phocaeicola vulgatus ATCC 8482],5L7U_B Chain B, Glycoside hydrolase [Phocaeicola vulgatus ATCC 8482] |
2JNK_A | 8.52e-06 | 1203 | 1262 | 14 | 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] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
E8MGH9 | 2.22e-17 | 1082 | 1319 | 1681 | 1933 | 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 |
P0DTR5 | 5.24e-17 | 46 | 304 | 842 | 1071 | A type blood alpha-D-galactosamine galactosaminidase OS=Flavonifractor plautii OX=292800 PE=1 SV=1 |
P26831 | 1.79e-10 | 1086 | 1262 | 1377 | 1566 | Hyaluronoglucosaminidase OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=nagH PE=1 SV=2 |
P0DTR4 | 7.35e-06 | 200 | 291 | 667 | 756 | A type blood N-acetyl-alpha-D-galactosamine deacetylase OS=Flavonifractor plautii OX=292800 PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000266 | 0.999050 | 0.000180 | 0.000181 | 0.000157 | 0.000148 |
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