Species | CAG-822 sp900546055 | |||||||||||
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Lineage | Bacteria; Firmicutes; Bacilli; RF39; UBA660; CAG-822; CAG-822 sp900546055 | |||||||||||
CAZyme ID | MGYG000004120_00099 | |||||||||||
CAZy Family | CBM13 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 94503; End: 97034 Strand: + |
MKKLICLLPF LSIFFICMGS VDAAPALADG EYKIKSAVSN NMVMTIEGGD FTKPSNVNLE | 60 |
NDNNLKTQRW NVKHLGNDYY VISSSAASYA VLDVKGAGKI NKTNVQIYGY NNSSAQKWLV | 120 |
KYAGNGYYYV ISNCNNLYLD VDGAKNYNGV NLHMYQGNGT SAQMFKFVPI VDPKQSLPDG | 180 |
SYTISTALNN NSVLDLTSGR TENSTNVQLY SSNDSWAQIW DVKYLNNGYY SITSHLNSEK | 240 |
SLDVSGAKSM NSANVQLYQS NGTDAQQWIL KDLGNGYYNI VSKLDNLFLD ISGAKYTNGT | 300 |
NVQLYHTNGT SAQKFKFNKV EFNMLSDGLY MINSALNSNK VVGLDKEVSV NNANVQLETN | 360 |
ANLNSQKWWV KYIGSGYYTI QTALDDSKAI DVPGAKTYDG ANVQLYASNG SKAQKWIIKY | 420 |
LGGNQYSIVS ALDGRHVDVK SGQTAEGTNI QLYSSNGTNA QKFTFTPTEK SGQGHSYEDG | 480 |
YYTISTSINT SMVLDVSAGA KYNGVNVQLY KSNNSNAQVW YLKYLNNGFY SIASSINPDL | 540 |
VLDVASGGMV SGTNVQMYRF NNSDSQQWMI RDLGDGNVSL VSKINGLSLD VTNGTLVNGA | 600 |
NIQVANSNGG NGQKFKLSKN TNNKVYTGID VSYHQGNIDW EKIAKSDLGF VIIRAGYGGD | 660 |
WNDQDDLMFA ANVSACEKYN IPYGLYLYSY ASDIDNANGT GAVSEAKHML RLINLIKANN | 720 |
YHPNLGTKVF LDVEDKSVAN VGKEKLTLVA DKFCSTIENN GYSCGIYANK MWLTDKLDSV | 780 |
ALSKKYEIWL AEWPNGVNTF AQAMNTRPTY NLTPYKYWQF ASDGNINGIS TNVDMDLGYN | 840 |
IFE | 843 |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH25 | 629 | 829 | 1.9e-36 | 0.9943502824858758 |
CBM13 | 181 | 323 | 7.6e-24 | 0.7074468085106383 |
CBM13 | 328 | 475 | 1e-21 | 0.7340425531914894 |
CBM13 | 29 | 190 | 6.1e-18 | 0.8351063829787234 |
CBM13 | 478 | 571 | 6.5e-17 | 0.4734042553191489 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd06414 | GH25_LytC-like | 3.37e-59 | 628 | 839 | 3 | 191 | The LytC lysozyme of Streptococcus pneumoniae is a bacterial cell wall hydrolase that cleaves the beta1-4-glycosydic bond located between the N-acetylmuramoyl-N-glucosaminyl residues of the cell wall polysaccharide chains. LytC is composed of a C-terminal glycosyl hydrolase family 25 (GH25) domain and an N-terminal choline-binding module (CBM) consisting of eleven homologous repeats that specifically recognizes the choline residues of pneumococcal lipoteichoic and teichoic acids. This domain arrangement is the reverse of the major pneumococcal autolysin, LytA, and the CPL-1-like lytic enzymes of the pneumococcal bacteriophages, in which the CBM (consisting of six repeats) is at the C-terminus. This model represents the C-terminal catalytic domain of the LytC-like enzymes. |
cd00599 | GH25_muramidase | 8.23e-25 | 628 | 837 | 2 | 185 | Endo-N-acetylmuramidases (muramidases) are lysozymes (also referred to as peptidoglycan hydrolases) that degrade bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues. This family of muramidases contains a glycosyl hydrolase family 25 (GH25) catalytic domain and is found in bacteria, fungi, slime molds, round worms, protozoans and bacteriophages. The bacteriophage members are referred to as endolysins which are involved in lysing the host cell at the end of the replication cycle to allow release of mature phage particles. Endolysins are typically modular enzymes consisting of a catalytically active domain that hydrolyzes the peptidoglycan cell wall and a cell wall-binding domain that anchors the protein to the cell wall. Endolysins generally have narrow substrate specificities with either intra-species or intra-genus bacteriolytic activity. |
pfam14200 | RicinB_lectin_2 | 9.12e-23 | 217 | 305 | 2 | 89 | Ricin-type beta-trefoil lectin domain-like. |
pfam14200 | RicinB_lectin_2 | 7.73e-20 | 364 | 453 | 1 | 89 | Ricin-type beta-trefoil lectin domain-like. |
pfam14200 | RicinB_lectin_2 | 8.39e-19 | 68 | 155 | 3 | 89 | Ricin-type beta-trefoil lectin domain-like. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QCP36075.1 | 1.99e-34 | 628 | 837 | 99 | 284 |
BAK44097.1 | 6.42e-34 | 614 | 839 | 614 | 824 |
CAB1243797.1 | 5.03e-33 | 628 | 842 | 5 | 198 |
BCA89043.1 | 1.10e-32 | 628 | 842 | 213 | 419 |
QHJ73726.1 | 9.24e-32 | 627 | 842 | 3 | 193 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2WW5_A | 3.33e-16 | 629 | 839 | 272 | 468 | 3D-structureof the modular autolysin LytC from Streptococcus pneumoniae at 1.6 A resolution [Streptococcus pneumoniae R6],2WWD_A 3D-structure of the modular autolysin LytC from Streptococcus pneumoniae in complex with pneummococcal peptidoglycan fragment [Streptococcus pneumoniae R6] |
2WWC_A | 7.80e-16 | 629 | 839 | 272 | 468 | 3D-structureof the modular autolysin LytC from Streptococcus pneumoniae in complex with synthetic peptidoglycan ligand [Streptococcus pneumoniae R6] |
4KRU_A | 1.26e-07 | 628 | 836 | 22 | 205 | X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101] |
4KRT_A | 3.21e-07 | 628 | 836 | 22 | 205 | X-raystructure of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101],4KRT_B X-ray structure of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101] |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000278 | 0.999031 | 0.000234 | 0.000152 | 0.000143 | 0.000139 |
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