|
Name |
Accession |
Description |
Interval |
E-value |
| GH25_AtlA-like |
cd06522 |
AtlA is an autolysin found in Gram-positive lactic acid bacteria that degrades bacterial cell ... |
44-237 |
2.03e-84 |
|
AtlA is an autolysin found in Gram-positive lactic acid bacteria that degrades bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues. This family includes the AtlA and Aml autolysins from Streptococcus mutans which have a C-terminal glycosyl hydrolase family 25 (GH25) catalytic domain as well as six tandem N-terminal repeats of the GBS (group B Streptococcus) Bsp-like peptidoglycan-binding domain. Other members of this family have one or more C-terminal peptidoglycan-binding domain(s) (SH3 or LysM) in addition to the GH25 domain.
Pssm-ID: 119382 Cd Length: 192 Bit Score: 257.30 E-value: 2.03e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506462997 44 MDVVDVSSNNGTISVADYKKMQEYGVKAVIVKLSEADSYKNPYAKVQIANAKEAGLKVGAYHYSWYASTADAQAEAKYFT 123
Cdd:cd06522 1 KDVVDVSSNNGIMSVADYNKLKNYGVKAVIVKLTEGTTYRNPYAASQIANAKAAGLKVSAYHYAHYTSAADAQAEARYFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506462997 124 DYATSLNLPKDTLMVDDLEETYTKNNsVTVNATAFSTQVKAAGYKNTSTYTYVSYVNETqLNFSYIGNNRVWIAQYPYQP 203
Cdd:cd06522 81 NTAKSLGLSKNTVMVADMEDSSSSGN-ATANVNAFWQTMKAAGYKNTDVYTSASWLNSR-ADTSTLGAKRVWVAQYPYNP 158
|
170 180 190
....*....|....*....|....*....|....
gi 2506462997 204 SDSGLWNNGYGMWQWNSNTSFPGISGTFDVSIDY 237
Cdd:cd06522 159 SSNNLWNTNYGAWQWTSQAHFPGRSGGFDVSIDY 192
|
|
| Glyco_hydro_25 |
pfam01183 |
Glycosyl hydrolases family 25; |
47-227 |
3.71e-41 |
|
Glycosyl hydrolases family 25;
Pssm-ID: 426105 Cd Length: 180 Bit Score: 144.81 E-value: 3.71e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506462997 47 VDVSSNNGTIsvaDYKKMQEYGVKAVIVKLSEADSYKNPYAKVQIANAKEAGLKVGAYHYSWYASTADAQAEAKYFTDYA 126
Cdd:pfam01183 1 IDVSSYQGDI---DWQKVKASGVSFVFIKATEGTDYVDPYFTTQYANARAAGLKVGAYHFARPCNSSTAAAQADYFLSNV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506462997 127 TSLNLPKDTLM-VDDLEETYTKNNSVTV-NATAFSTQVK-AAGYKNTsTYTYVSYVNETQLNFSYIGNNRVWIAQYPYQP 203
Cdd:pfam01183 78 QGLGLDAGTLPpVLDVEVTTGLTKAAATsNILRFLDRVKkQTGYKPV-IYTGTSFWTNNLLYGQFIADYPLWIASYAVTP 156
|
170 180
....*....|....*....|....
gi 2506462997 204 SDSGLWNNGYGMWQWNSNTSFPGI 227
Cdd:pfam01183 157 PKDYPGWTKWTFWQYTSSGSIPGV 180
|
|
| Acm |
COG3757 |
Lyzozyme M1 (1,4-beta-N-acetylmuramidase), GH25 family [Cell wall/membrane/envelope biogenesis] ... |
34-240 |
2.58e-33 |
|
Lyzozyme M1 (1,4-beta-N-acetylmuramidase), GH25 family [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442971 Cd Length: 208 Bit Score: 124.62 E-value: 2.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506462997 34 ITAGTSGLPRMDVVDVSSNNGTIsvaDYKKMQEYGVKAVIVKLSEADSYKNPYAKVQIANAKEAGLKVGAYHYSWYASTA 113
Cdd:COG3757 1 LLALGGAAYPVHGIDVSHYQGDI---DWAAVKAAGIDFAYIKATEGTDYVDPKFARNWAGARAAGLPRGAYHFFRPCSDA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506462997 114 DAQAEakYFTDYATslNLPKDTLMVDDLEETYTKNNS---VTVNATAFSTQVKAAGYKNTSTYTYVSYVNeTQLNFSYIG 190
Cdd:COG3757 78 AAQAD--NFISTVP--RDPGDLPPVLDLEENGYYGLSpaqLRAWLKAFLDEVEAHTGRKPIIYTSPSFYN-DYLGNSDFS 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2506462997 191 NNRVWIAQYPYQPSDSGlwNNGYGMWQWNSNTSFPGISGTFDVSIDYKNL 240
Cdd:COG3757 153 DYPLWIARYGSSPGYLP--GRNWTFWQYTSSGRVPGISGNVDLNVFNGSR 200
|
|
| COG5263 |
COG5263 |
Glucan-binding domain (YG repeat) [Carbohydrate transport and metabolism]; |
48-444 |
3.35e-11 |
|
Glucan-binding domain (YG repeat) [Carbohydrate transport and metabolism];
Pssm-ID: 444077 [Multi-domain] Cd Length: 486 Bit Score: 64.89 E-value: 3.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506462997 48 DVSSNNGTISVADYKKMQEYGVKAVIVKLSEADSYKNPYAKVQIANAKEAGLKVGAYHYSWYASTADAQAEAKYFTDYAT 127
Cdd:COG5263 89 SGNSSAGNNNDVYDVYVVYEGGSVKDYGGGVSDDGDDVVDKTNVAAGGGGKTKKGDTNSANTGYLGDDLGGGTADKGGSA 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506462997 128 SLNLPKDTLMVDDLEETYTKNNSVTVNATAFSTQVKAAGYKNTSTYTYVSYVNETQLNFSYIGNNRVWIAQYPYQPSDSG 207
Cdd:COG5263 169 GYGAGKDGATAAAKELVGSAADTYYGGASTYLTGDAGAYGALGLAAGSGAGAKKTGSTAGASGTAYGDSGGTAGSGLSSL 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506462997 208 LWNNGYGMWQWNSNTSFPGISGTFDVSIDYKNLISV--NSNGYNDGIFYQNNTPANGYYNDGTGYKWF---ENGQLYTGF 282
Cdd:COG5263 249 GGSSNALESGGENNQSLAGNGTSYDDAGAAGVDGTGttGTVGWVDGKWYYFDAGKMVTGWQTINGKWYyfdSDGAMATGW 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506462997 283 RNYMGTYYFFENGMRQDNKWETAWGMKYYVGSDGRAVQGVQVIDGNKYYFGNNTtfYLRTNTtIQSGNTILKANDSGVLE 362
Cdd:COG5263 329 QKINGKWYYFDEDGAMATGWVTDDGKWYYLGSDGAMATGWQKIDGKWYYFDSNG--AMATGW-VKVDGKWYYFDSSGAMA 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506462997 363 pwTGYIYDGSAYnggYRWYENGQLFTGFRYYTGTYYWFENGVRQNAGWRYAWNYTYWTNNEGRAVQGHQTIDGKDYYFGD 442
Cdd:COG5263 406 --TGWLKIDGKW---YYFDSDGAMATGWQKIGGKWYYFDSNGAMATGWVKVDGKWYYFDSDGAMATGWQTIDGKTYYFDS 480
|
..
gi 2506462997 443 DG 444
Cdd:COG5263 481 NG 482
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
255-440 |
4.01e-04 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 42.69 E-value: 4.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506462997 255 QNNTPANGYYND-GTGYKWFENGQLYTGFRNYMGTYYFFENGMRQDNKWETAWGMKYYVGSDGRAVQGvqvidgnkyYFG 333
Cdd:NF033838 480 QPSTPKTGWKQEnGMWYFYNTDGSMATGWLQNNGSWYYLNANGAMATGWLQNNGSWYYLNANGSMATG---------WLQ 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506462997 334 NNTT-FYLRTNTTIQSGntilkandsgvlepWTgyiydgsAYNGGyrWY---ENGQLFTGFRYYTGTYYWFENGVRQNAG 409
Cdd:NF033838 551 NNGSwYYLNANGAMATG--------------WL-------QYNGS--WYylnANGDMATGWLQYNGSWYYLNANGDMATG 607
|
170 180 190
....*....|....*....|....*....|.
gi 2506462997 410 WRYAWNYTYWTNNEGRAVQGhQTIDGKDYYF 440
Cdd:NF033838 608 WLQYNGSWYYLNANGSMATG-WVKDGDTWYY 637
|
|
| glucan_65_rpt |
TIGR04035 |
glucan-binding repeat; This model describes a region of about 63 amino acids that is composed ... |
310-335 |
6.31e-04 |
|
glucan-binding repeat; This model describes a region of about 63 amino acids that is composed of three repeats of a more broadly distributed family of shorter repeats modeled by pfam01473. While the shorter repeats are often associated with choline binding (and therefore with cell wall binding), the longer repeat described here represents a subgroup of repeat sequences associated with glucan binding, as found in a number glycosylhydrolases. Shah, et al. describe a repeat consensus, WYYFDANGKAVTGAQTINGQTLYFDQDGKQVKG, that corresponds to half of the repeat as modeled here and one and a half copies of the repeat as modeled by pfam01473.
Pssm-ID: 274933 [Multi-domain] Cd Length: 62 Bit Score: 37.88 E-value: 6.31e-04
|
| PspC_relate_1 |
NF033840 |
PspC-related protein choline-binding protein 1; Members of this family share C-terminal ... |
241-385 |
1.25e-03 |
|
PspC-related protein choline-binding protein 1; Members of this family share C-terminal homology to the choline-binding form of the pneumococcal surface antigen PspC, but not to its allelic LPXTG-anchored forms because they lack the choline-binding repeat region. Members of this family should not be confused with PspC itself, whose identity and function reflect regions N-terminal to the choline-binding region. See Iannelli, et al. (PMID: 11891047) for information about the different allelic forms of PspC.
Pssm-ID: 411409 [Multi-domain] Cd Length: 648 Bit Score: 41.22 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506462997 241 ISVNSNGYNDGIFYQNN--TPANGYYND-GTGYKWFENGQLYTGFRNYMGTYYFFENGMRQDNKWETAWGMKYYVGSDGR 317
Cdd:NF033840 488 VSVTSNQGTDAAVEPAKpvAPTTGWKQEnGMWYFYNTDGSMATGWVQVNGSWYYLNSNGSMATGWVQVNGSWYYLNSNGS 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506462997 318 AVQGVQVIDGNKYYFGNNTT------------FYLRTNTTI------QSGNTILKANDSGVLEPWTGYiydgsaynGGYR 379
Cdd:NF033840 568 MATGWVQVDGSWYYLNDNGSmetgwlqnngswYYLNSNGSMkanqwfQVGSKWYYVNASGELAVNTSI--------DGYR 639
|
....*.
gi 2506462997 380 WYENGQ 385
Cdd:NF033840 640 VNDNGE 645
|
|
| PspC_relate_1 |
NF033840 |
PspC-related protein choline-binding protein 1; Members of this family share C-terminal ... |
363-445 |
4.43e-03 |
|
PspC-related protein choline-binding protein 1; Members of this family share C-terminal homology to the choline-binding form of the pneumococcal surface antigen PspC, but not to its allelic LPXTG-anchored forms because they lack the choline-binding repeat region. Members of this family should not be confused with PspC itself, whose identity and function reflect regions N-terminal to the choline-binding region. See Iannelli, et al. (PMID: 11891047) for information about the different allelic forms of PspC.
Pssm-ID: 411409 [Multi-domain] Cd Length: 648 Bit Score: 39.29 E-value: 4.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506462997 363 PWTGYIYDgsayNGGYRWYE-NGQLFTGFRYYTGTYYWFENGVRQNAGWRYAWNYTYWTNNEGRAVQGHQTIDGKDYYFG 441
Cdd:NF033840 508 PTTGWKQE----NGMWYFYNtDGSMATGWVQVNGSWYYLNSNGSMATGWVQVNGSWYYLNSNGSMATGWVQVDGSWYYLN 583
|
....
gi 2506462997 442 DDGT 445
Cdd:NF033840 584 DNGS 587
|
|
| Glyco_25 |
smart00641 |
Glycosyl hydrolases family 25; |
47-126 |
6.91e-03 |
|
Glycosyl hydrolases family 25;
Pssm-ID: 128889 Cd Length: 109 Bit Score: 36.24 E-value: 6.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506462997 47 VDVSSNNGTISVAdykKMQEYGVKAVIVKLSEADSYKNPYAKVQIANAKEAGLKV-GAYHYSwYASTADAQAEAKYFTDY 125
Cdd:smart00641 4 IDVSDYEGGIDGA---KVRNTGASFAFMKATEGAGYTPPYYSYQYFLADNAGYILrGFYHAA-YPVSSSATAQANYFPSM 79
|
.
gi 2506462997 126 A 126
Cdd:smart00641 80 D 80
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GH25_AtlA-like |
cd06522 |
AtlA is an autolysin found in Gram-positive lactic acid bacteria that degrades bacterial cell ... |
44-237 |
2.03e-84 |
|
AtlA is an autolysin found in Gram-positive lactic acid bacteria that degrades bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues. This family includes the AtlA and Aml autolysins from Streptococcus mutans which have a C-terminal glycosyl hydrolase family 25 (GH25) catalytic domain as well as six tandem N-terminal repeats of the GBS (group B Streptococcus) Bsp-like peptidoglycan-binding domain. Other members of this family have one or more C-terminal peptidoglycan-binding domain(s) (SH3 or LysM) in addition to the GH25 domain.
Pssm-ID: 119382 Cd Length: 192 Bit Score: 257.30 E-value: 2.03e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506462997 44 MDVVDVSSNNGTISVADYKKMQEYGVKAVIVKLSEADSYKNPYAKVQIANAKEAGLKVGAYHYSWYASTADAQAEAKYFT 123
Cdd:cd06522 1 KDVVDVSSNNGIMSVADYNKLKNYGVKAVIVKLTEGTTYRNPYAASQIANAKAAGLKVSAYHYAHYTSAADAQAEARYFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506462997 124 DYATSLNLPKDTLMVDDLEETYTKNNsVTVNATAFSTQVKAAGYKNTSTYTYVSYVNETqLNFSYIGNNRVWIAQYPYQP 203
Cdd:cd06522 81 NTAKSLGLSKNTVMVADMEDSSSSGN-ATANVNAFWQTMKAAGYKNTDVYTSASWLNSR-ADTSTLGAKRVWVAQYPYNP 158
|
170 180 190
....*....|....*....|....*....|....
gi 2506462997 204 SDSGLWNNGYGMWQWNSNTSFPGISGTFDVSIDY 237
Cdd:cd06522 159 SSNNLWNTNYGAWQWTSQAHFPGRSGGFDVSIDY 192
|
|
| Glyco_hydro_25 |
pfam01183 |
Glycosyl hydrolases family 25; |
47-227 |
3.71e-41 |
|
Glycosyl hydrolases family 25;
Pssm-ID: 426105 Cd Length: 180 Bit Score: 144.81 E-value: 3.71e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506462997 47 VDVSSNNGTIsvaDYKKMQEYGVKAVIVKLSEADSYKNPYAKVQIANAKEAGLKVGAYHYSWYASTADAQAEAKYFTDYA 126
Cdd:pfam01183 1 IDVSSYQGDI---DWQKVKASGVSFVFIKATEGTDYVDPYFTTQYANARAAGLKVGAYHFARPCNSSTAAAQADYFLSNV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506462997 127 TSLNLPKDTLM-VDDLEETYTKNNSVTV-NATAFSTQVK-AAGYKNTsTYTYVSYVNETQLNFSYIGNNRVWIAQYPYQP 203
Cdd:pfam01183 78 QGLGLDAGTLPpVLDVEVTTGLTKAAATsNILRFLDRVKkQTGYKPV-IYTGTSFWTNNLLYGQFIADYPLWIASYAVTP 156
|
170 180
....*....|....*....|....
gi 2506462997 204 SDSGLWNNGYGMWQWNSNTSFPGI 227
Cdd:pfam01183 157 PKDYPGWTKWTFWQYTSSGSIPGV 180
|
|
| Acm |
COG3757 |
Lyzozyme M1 (1,4-beta-N-acetylmuramidase), GH25 family [Cell wall/membrane/envelope biogenesis] ... |
34-240 |
2.58e-33 |
|
Lyzozyme M1 (1,4-beta-N-acetylmuramidase), GH25 family [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442971 Cd Length: 208 Bit Score: 124.62 E-value: 2.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506462997 34 ITAGTSGLPRMDVVDVSSNNGTIsvaDYKKMQEYGVKAVIVKLSEADSYKNPYAKVQIANAKEAGLKVGAYHYSWYASTA 113
Cdd:COG3757 1 LLALGGAAYPVHGIDVSHYQGDI---DWAAVKAAGIDFAYIKATEGTDYVDPKFARNWAGARAAGLPRGAYHFFRPCSDA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506462997 114 DAQAEakYFTDYATslNLPKDTLMVDDLEETYTKNNS---VTVNATAFSTQVKAAGYKNTSTYTYVSYVNeTQLNFSYIG 190
Cdd:COG3757 78 AAQAD--NFISTVP--RDPGDLPPVLDLEENGYYGLSpaqLRAWLKAFLDEVEAHTGRKPIIYTSPSFYN-DYLGNSDFS 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2506462997 191 NNRVWIAQYPYQPSDSGlwNNGYGMWQWNSNTSFPGISGTFDVSIDYKNL 240
Cdd:COG3757 153 DYPLWIARYGSSPGYLP--GRNWTFWQYTSSGRVPGISGNVDLNVFNGSR 200
|
|
| GH25_muramidase |
cd00599 |
Endo-N-acetylmuramidases (muramidases) are lysozymes (also referred to as peptidoglycan ... |
46-235 |
4.83e-28 |
|
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.
Pssm-ID: 119373 [Multi-domain] Cd Length: 186 Bit Score: 109.75 E-value: 4.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506462997 46 VVDVSSNNGTIsvaDYKKMQEYGVKAVIVKLSEADSYKNPYAKVQIANAKEAGLKVGAYHYSWYASTADAQAEakYFTDY 125
Cdd:cd00599 2 GIDVSSWQGSI---DWNAVKAAGIDFVFIKATEGTTYVDPKFATNRARARAAGLLVGAYHFARPCANAEAQAD--NFVNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506462997 126 ATslNLPKDTLMVDDLEET--YTKNNSVTVNATAFSTQVKAAGYKNTSTYTYVSYVNeTQLNFSYIGNNRVWIAQYPYQP 203
Cdd:cd00599 77 VP--RDPGSLPLVLDVEDTggGCSAAALAAWLNAFLNEVEALTGKKPIIYTSPSFWD-DYLASSQLSDYPLWIAHYRGEP 153
|
170 180 190
....*....|....*....|....*....|..
gi 2506462997 204 SDSGLWNNGYGMWQWNSNTSFPGISGTFDVSI 235
Cdd:cd00599 154 PPAPGAWRPWTLWQYTSSGRVPGISGPVDLNV 185
|
|
| GH25_LytC-like |
cd06414 |
The LytC lysozyme of Streptococcus pneumoniae is a bacterial cell wall hydrolase that cleaves ... |
46-237 |
3.89e-22 |
|
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.
Pssm-ID: 119376 Cd Length: 191 Bit Score: 93.40 E-value: 3.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506462997 46 VVDVSSNNGTIsvaDYKKMQEYGVKAVIVKL---SEADSYKNPYAKVQIANAKEAGLKVGAYHYSWYASTADAQAEAKYF 122
Cdd:cd06414 3 GIDVSEWQGDI---DWKKVKASGVDFAIIRAgygGYGELQEDKYFEENIKGAKAAGIPVGVYFYSYAVTVAEAREEAEFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506462997 123 tdyatsLNLPKDTLM----VDDLEE-TYTKNNS----VTVNATAFSTQVKAAGYkNTSTYTYVSYVNeTQLNFSYIGNNR 193
Cdd:cd06414 80 ------LRLIKGYKLsypvYYDLEDeTQLGAGLskdqRTDIANAFCETIEAAGY-YPGIYANLSWLT-NKLDDERLSKYD 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2506462997 194 VWIAQYPYQPSDSGlwnnGYGMWQWNSNTSFPGISGTFDVSIDY 237
Cdd:cd06414 152 VWVAQYGNSPTYPG----NYGMWQYTSSGSVPGISGNVDLNYCY 191
|
|
| GH25_Cpl1-like |
cd06415 |
Cpl-1 lysin (also known as Cpl-9 lysozyme / muramidase) is a bacterial cell wall endolysin ... |
46-233 |
2.44e-21 |
|
Cpl-1 lysin (also known as Cpl-9 lysozyme / muramidase) is a bacterial cell wall endolysin encoded by the pneumococcal bacteriophage Cp-1, which cleaves the glycosidic N-acetylmuramoyl-(beta1,4)-N-acetylglucosamine bonds of the pneumococcal glycan chain, thus acting as an enzymatic antimicrobial agent (an enzybiotic) against streptococcal infections. Cpl-1 belongs to the CP family of lysozymes (CPL lysozymes) which includes the Cpl-7 lysin. Cpl-1 has a glycosyl hydrolase family 25 (GH25) catalytic domain with an irregular (beta/alpha)5-beta3 barrel and a C-terminal cell wall-anchoring module formed by six similar choline-binding repeats (ChBr's). The ChBr's facilitate the anchoring of Cpl-1 to the choline-containing teichoic acid of the pneumococcal cell wall. Other members of this domain family have an N-terminal CHAP (cysteine, histidine-dependent amidohydrolases/peptidases) domain similar to that of the firmicute CHAP lysins and associated with endopeptidase activity. The Cpl-7 lysin is also included here as is LysB of Lactococcus phage, and the Mur lysin of Lactobacillus phage.
Pssm-ID: 119377 Cd Length: 196 Bit Score: 91.31 E-value: 2.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506462997 46 VVDVSSNNGTiSVADYKKMqeyGVKAVIVKLSEADSYKNPYAKVQIANAKEAGLKVGAYHYSWY-ASTADAQAEAKYFTD 124
Cdd:cd06415 3 GVDVASYQGT-DLTAYGQA---GAKFAIVKISEGTNYVNPKASAQVSSAIANGKMTGGYHFARFgGSVSQAKYEADYFLN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506462997 125 YATSLNLPKDTLMVDDLEETYTKNNSVTVNA-TAFSTQVKAAGYKN---TSTYTYVSYVNETQLNFSYIgnNRVWIAQYP 200
Cdd:cd06415 79 SAQQAGLPKGSYLALDYEQGSGNSKAANTSAiLAFMDTIKDAGYKPmlySYKPLLLNNVDYSQIIAKYP--NSLWVAAYP 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 2506462997 201 -YQPSDSGLWN-----NGYGMWQWNSNTSFPGISGTFDV 233
Cdd:cd06415 157 tYGVQDTPDFNyfpsmDGVAIWQFTSNWRGGGVDGNITL 195
|
|
| GH25_Lyc-like |
cd06525 |
Lyc muramidase is an autolytic lysozyme (autolysin) from Clostridium acetobutylicum encoded by ... |
47-233 |
1.57e-19 |
|
Lyc muramidase is an autolytic lysozyme (autolysin) from Clostridium acetobutylicum encoded by the lyc gene. Lyc has a glycosyl hydrolase family 25 (GH25) catalytic domain. Endo-N-acetylmuramidases 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.
Pssm-ID: 119385 Cd Length: 184 Bit Score: 85.81 E-value: 1.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506462997 47 VDVSSNNGTIsvaDYKKMQEYGVKAVIVKLSEADSYKNPYAKVQIANAKEAGLKVGAYHYswYASTADAQAEAKYFtdYA 126
Cdd:cd06525 3 IDISNWQGNI---NFNAVKDSGVEVVYIKATEGTTFVDSYFNENYNGAKAAGLKVGFYHF--LVGTSNPEEQAENF--YN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506462997 127 TSLNLPKDTLMVDDLEETYTKNNS-VTVNATAFSTQVKAAGYKNTSTYTYVSYVNEtqLNFSYIGNNRVWIAQYPYQ-PS 204
Cdd:cd06525 76 TIKGKKMDLKPALDVEVNFGLSKDeLNDYVLRFIEEFEKLSGLKVGIYTYTSFINN--NLDSRLSSYPLWIANYGVSpPS 153
|
170 180
....*....|....*....|....*....
gi 2506462997 205 DSGLWNNGYGmWQWNSNTSFPGISGTFDV 233
Cdd:cd06525 154 SNGIWNSWVG-FQYSETGRVNGVSGSVDL 181
|
|
| GH25_PlyB-like |
cd06523 |
PlyB is a bacteriophage endolysin that displays potent lytic activity toward Bacillus ... |
46-234 |
1.67e-14 |
|
PlyB is a bacteriophage endolysin that displays potent lytic activity toward Bacillus anthracis. PlyB has an N-terminal glycosyl hydrolase family 25 (GH25) catalytic domain and a C-terminal bacterial SH3-like domain, SH3b. Both domains are required for effective catalytic activity. Endolysins are produced by bacteriophages at the end of their life cycle and participate in lysing the bacterial cell in order to release the newly formed progeny. Endolysins (also referred to as endo-N-acetylmuramidases or peptidoglycan hydrolases) degrade bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues.
Pssm-ID: 119383 Cd Length: 177 Bit Score: 71.24 E-value: 1.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506462997 46 VVDVSSNNGTISVaDYKKMQEyGVKAVIVKLSEADSYKNPYAKVQIANAKEAGLKVGAYHYSWYASTADAQAEAKYFTDY 125
Cdd:cd06523 2 IVDISEWQGPINW-DYDTLSK-QLDLVIIRVQYGSNYVDLKYKNNIKEFKKRGIPFGVYAFARGTSTADAKAEARDFYNR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506462997 126 ATslnlPKDTLMVDDLEETYTKNNSVTVNatAFSTQVKAAGYKNTSTYTYVSYVNETQLNFSYIGNnrVWIAQYPYQPSd 205
Cdd:cd06523 80 AN----KKPTFYVLDVEVTSMSDMNAGVQ--AFISELRRLGAKKVGLYIGHHFYTTFNLAVSKFDA--IWIPAYGSNPG- 150
|
170 180
....*....|....*....|....*....
gi 2506462997 206 sglwNNGYGMWQWNSNTSFPGISGTFDVS 234
Cdd:cd06523 151 ----TYPYDLWQYTDSGYLPGISGNVDLN 175
|
|
| GH25_YegX-like |
cd06524 |
YegX is an uncharacterized bacterial protein with a glycosyl hydrolase family 25 (GH25) ... |
47-235 |
1.86e-14 |
|
YegX is an uncharacterized bacterial protein with a glycosyl hydrolase family 25 (GH25) catalytic domain that is similar in sequence to the CH-type (Chalaropsis-type) lysozymes of the GH25 family of endolysins.
Pssm-ID: 119384 Cd Length: 194 Bit Score: 71.61 E-value: 1.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506462997 47 VDVSSNNGTI-SVADYKKMQEYGVKAVIVKLSEADSYKNPYAKVQIANAKEAGLKVGAYHYswYASTADAQAEAKYFTDy 125
Cdd:cd06524 3 IDVSHYQGKIdWQKVKAKVKDSPVAFVFIKATEGVDIVDPDFPTNWEGAKEAGIIRGAYHF--YRPNSDPKQQADNFLN- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506462997 126 aTSLNLPKDTLM-VDDLEETYTKNNSVTV--------NATAFSTQVKAAGYKNTSTYTyvsyvneTQLNFSYIGNNRVWI 196
Cdd:cd06524 80 -TVKLLGPGDLPpVLDVEWDGRKSSAKQIqegvlewlDAVEKATGVKPIIYTNPSFWT-------DYLTDSSFSEYPLWI 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2506462997 197 AQY-PYQPSDSGLWNNGYGMWQWNSNTSFPGISGTFDVSI 235
Cdd:cd06524 152 ADYnPRRKKVPPNESKKWLLWQYSDSGKVPGISGAVDLNV 191
|
|
| GH25_LysA-like |
cd06417 |
LysA is a cell wall endolysin produced by Lactobacillus fermentum, which degrades bacterial ... |
44-237 |
1.53e-13 |
|
LysA is a cell wall endolysin produced by Lactobacillus fermentum, which degrades bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues. The N-terminal glycosyl hydrolase family 25 (GH25) domain of LysA has sequence similarity with other murein hydrolase catalytic domains while the C-terminal domain has sequence similarity with putative bacterial cell wall-binding SH3b domains. This domain family also includes LysL of Lactococcus lactis.
Pssm-ID: 119379 Cd Length: 195 Bit Score: 69.01 E-value: 1.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506462997 44 MDVVDVSS----NNGTISVADYkkmqeygvkaVIVKLSEADSYKNPYAKVQIANAKEAGLKVGAYHyswYASTADAQAEA 119
Cdd:cd06417 1 MNGIDVSSwqsrIVTTVVPADF----------VIVKATQGTGYVNPSWRSQAAQAIAAGKLLGLYH---YANGGNAIAEA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506462997 120 KYFTDYATslNLPKDTLMVDDLEETYTKNNSVTVNATAFSTQVKAAGYKNTSTYTYVSYVNetQLNFSYIGNNRVWIAQY 199
Cdd:cd06417 68 DYFLNNIK--GYVGKAVLVLDWESYQNSAWGNSAWARQWVNRVHELTGVWPMVYVSKSVTR--QINWSVRADCGLWVAQY 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2506462997 200 PY-QP----SDSGLWN---NGYGMWQWNSNTSFPGISGTFDVSIDY 237
Cdd:cd06417 144 ASnNPtgyqSQAGPWNaawSGETIHQYTSNGSLNGYNGPLDLNLFY 189
|
|
| GH25_CH-type |
cd06412 |
CH-type (Chalaropsis-type) lysozymes represent one of four functionally-defined classes of ... |
47-236 |
6.01e-13 |
|
CH-type (Chalaropsis-type) lysozymes represent one of four functionally-defined classes of peptidoglycan hydrolases (also referred to as endo-N-acetylmuramidases) that cleave bacterial cell wall peptidoglycans. CH-type lysozymes exhibit both lysozyme (acetylmuramidase) and diacetylmuramidase activity. The first member of this family to be described was a muramidase from the fungus Chalaropsis. However, a majority of the CH-type lysozymes are found in bacteriophages and Gram-positive bacteria such as Streptomyces and Clostridium. CH-type lysozymes have a single glycosyl hydrolase family 25 (GH25) domain with an unusual beta/alpha-barrel fold in which the last strand of the barrel is antiparallel to strands beta7 and beta1. Most CH-type lysozymes appear to lack the cell wall-binding domain found in other GH25 muramidases.
Pssm-ID: 119374 Cd Length: 199 Bit Score: 67.35 E-value: 6.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506462997 47 VDVSSNNGTIsvaDYKKMQEYGVKAVIVKLSEADSYKNPYAKVQIANAKEAGLKVGAYHYSwYASTADAQAEAKYFTDYA 126
Cdd:cd06412 4 IDVSGHQGSV---DWSGAAANGARFAYVKATEGTSYTNPRFSSQYNGAYNAGLIRGAYHFA-LPDQSSGAAQADYFLDHG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506462997 127 TSLNLPKDTLM-VDDLEETYTKNNSVTVNATA-------FSTQVKAAGYKNTSTYTYVSYVNETQLNFSYIGNNRVWIAQ 198
Cdd:cd06412 80 GGWSPDGRTLPgVLDLEYNPYGATCYGLSPAQmvswikdFSDTYKARTGRDPVIYTTTSWWNQCTGNSAGFANHPLWLAR 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 2506462997 199 YPYQPSD-SGLWNNgYGMWQWNSNTSFPGISGTFDVSID 236
Cdd:cd06412 160 YGSSPGAlPAGWSA-WTFWQYSDSGPFPGDQNVFNGSRA 197
|
|
| GH25_muramidase_1 |
cd06413 |
Uncharacterized bacterial muramidase containing a glycosyl hydrolase family 25 (GH25) ... |
47-232 |
6.33e-12 |
|
Uncharacterized bacterial muramidase containing a glycosyl hydrolase family 25 (GH25) catalytic domain. Endo-N-acetylmuramidases 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.
Pssm-ID: 119375 Cd Length: 191 Bit Score: 64.22 E-value: 6.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506462997 47 VDVSSNNGTIsvaDYKKMQEYGVKAVIVKLSEADSYKNPYAKVQIANAKEAGLKVGAYHYSWYASTADAQAEakYFTDya 126
Cdd:cd06413 6 IDVSHHQGDI---DWARVRAQGVSFAYIKATEGGDHVDKRFAENWRGARAAGLPRGAYHFFTFCRSGAEQAA--NFIR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506462997 127 tslNLPKDTLM---VDDLEETYTKNN-----SVTVNATAFSTQVKAAGYKNTSTYTYVSYVNEtqlnfsYIG----NNRV 194
Cdd:cd06413 79 ---NVPKDPGAlppVVDVEWNGNSATcpsaeEVLAELQVFLDALEAHYGKRPIIYTTYDFYDD------YLKgefpDYPL 149
|
170 180 190
....*....|....*....|....*....|....*...
gi 2506462997 195 WIAQYPYQPSDSGlwNNGYGMWQWNSNTSFPGISGTFD 232
Cdd:cd06413 150 WIRSVAGHPRLYE--DRPWTFWQYTNRGRVPGIEGDVD 185
|
|
| COG5263 |
COG5263 |
Glucan-binding domain (YG repeat) [Carbohydrate transport and metabolism]; |
48-444 |
3.35e-11 |
|
Glucan-binding domain (YG repeat) [Carbohydrate transport and metabolism];
Pssm-ID: 444077 [Multi-domain] Cd Length: 486 Bit Score: 64.89 E-value: 3.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506462997 48 DVSSNNGTISVADYKKMQEYGVKAVIVKLSEADSYKNPYAKVQIANAKEAGLKVGAYHYSWYASTADAQAEAKYFTDYAT 127
Cdd:COG5263 89 SGNSSAGNNNDVYDVYVVYEGGSVKDYGGGVSDDGDDVVDKTNVAAGGGGKTKKGDTNSANTGYLGDDLGGGTADKGGSA 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506462997 128 SLNLPKDTLMVDDLEETYTKNNSVTVNATAFSTQVKAAGYKNTSTYTYVSYVNETQLNFSYIGNNRVWIAQYPYQPSDSG 207
Cdd:COG5263 169 GYGAGKDGATAAAKELVGSAADTYYGGASTYLTGDAGAYGALGLAAGSGAGAKKTGSTAGASGTAYGDSGGTAGSGLSSL 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506462997 208 LWNNGYGMWQWNSNTSFPGISGTFDVSIDYKNLISV--NSNGYNDGIFYQNNTPANGYYNDGTGYKWF---ENGQLYTGF 282
Cdd:COG5263 249 GGSSNALESGGENNQSLAGNGTSYDDAGAAGVDGTGttGTVGWVDGKWYYFDAGKMVTGWQTINGKWYyfdSDGAMATGW 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506462997 283 RNYMGTYYFFENGMRQDNKWETAWGMKYYVGSDGRAVQGVQVIDGNKYYFGNNTtfYLRTNTtIQSGNTILKANDSGVLE 362
Cdd:COG5263 329 QKINGKWYYFDEDGAMATGWVTDDGKWYYLGSDGAMATGWQKIDGKWYYFDSNG--AMATGW-VKVDGKWYYFDSSGAMA 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506462997 363 pwTGYIYDGSAYnggYRWYENGQLFTGFRYYTGTYYWFENGVRQNAGWRYAWNYTYWTNNEGRAVQGHQTIDGKDYYFGD 442
Cdd:COG5263 406 --TGWLKIDGKW---YYFDSDGAMATGWQKIGGKWYYFDSNGAMATGWVKVDGKWYYFDSDGAMATGWQTIDGKTYYFDS 480
|
..
gi 2506462997 443 DG 444
Cdd:COG5263 481 NG 482
|
|
| COG5263 |
COG5263 |
Glucan-binding domain (YG repeat) [Carbohydrate transport and metabolism]; |
82-444 |
5.71e-06 |
|
Glucan-binding domain (YG repeat) [Carbohydrate transport and metabolism];
Pssm-ID: 444077 [Multi-domain] Cd Length: 486 Bit Score: 48.71 E-value: 5.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506462997 82 YKNPYAKVQIANAKEAGLKVGAYHYSWYASTADAQAEAKYFTDYaTSLNLPKDTLMVDDLEETYTKNNSVTVNATAFSTQ 161
Cdd:COG5263 8 VNAGNNTYVASSTSVDATYVNGGYGVFAASDVDLVTENVTVENE-KTSGVNGKSKDGGAGEVSEKGDLSSDVGYVTDSAQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506462997 162 VKAAGYKNTSTYTYVSYVNETQLNFSYIGNNRVWIAQYPYQPSDSGLWNNGYGMWQWNSNTSFPGISGtfdvsidYKNLI 241
Cdd:COG5263 87 GGSGNSSAGNNNDVYDVYVVYEGGSVKDYGGGVSDDGDDVVDKTNVAAGGGGKTKKGDTNSANTGYLG-------DDLGG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506462997 242 SVNSNGYNDGIFYQNNTPANGYYNDGTGYKWFENGQLYTGFRNYMGTYYFFENGMRQDNKWETAWGMKYYVGSDGRAVQG 321
Cdd:COG5263 160 GTADKGGSAGYGAGKDGATAAAKELVGSAADTYYGGASTYLTGDAGAYGALGLAAGSGAGAKKTGSTAGASGTAYGDSGG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506462997 322 VQVIDGNKYYFGNNTTFYLRTNTTIQSGNTILKANDSGVLEPWTGYIYDGSAYNGGYRWYENGQLFTGFRYYTGTYYWFE 401
Cdd:COG5263 240 TAGSGLSSLGGSSNALESGGENNQSLAGNGTSYDDAGAAGVDGTGTTGTVGWVDGKWYYFDAGKMVTGWQTINGKWYYFD 319
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2506462997 402 NGVRQNAGWRYAWNYTYWTNNEGRAVQGHQTIDGKDYYFGDDG 444
Cdd:COG5263 320 SDGAMATGWQKINGKWYYFDEDGAMATGWVTDDGKWYYLGSDG 362
|
|
| COG5263 |
COG5263 |
Glucan-binding domain (YG repeat) [Carbohydrate transport and metabolism]; |
139-449 |
3.00e-04 |
|
Glucan-binding domain (YG repeat) [Carbohydrate transport and metabolism];
Pssm-ID: 444077 [Multi-domain] Cd Length: 486 Bit Score: 42.94 E-value: 3.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506462997 139 DDLEETYTKNNSVTVNATAFSTQVKAAGYKNTSTYTYVSYVNETQLNFSYIGNNRVWIAQYPYQPSDSGLWNNGYGMWQW 218
Cdd:COG5263 42 VTENVTVENEKTSGVNGKSKDGGAGEVSEKGDLSSDVGYVTDSAQGGSGNSSAGNNNDVYDVYVVYEGGSVKDYGGGVSD 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506462997 219 NSNTSFPGISGTFDVSIDYKNLISVNSNGYNDGIFYQNNTPANGYYNDGTGYKWFENGQLYTGFRNYMGTYYFFENGMRQ 298
Cdd:COG5263 122 DGDDVVDKTNVAAGGGGKTKKGDTNSANTGYLGDDLGGGTADKGGSAGYGAGKDGATAAAKELVGSAADTYYGGASTYLT 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506462997 299 DNKWETAWGMKYYVGSDGRAVQGVQVIDGNKYYFGNNTTFYLRTNTTIQSGNTILKANDSGVLEPWTGYIYDGSAYNGGY 378
Cdd:COG5263 202 GDAGAYGALGLAAGSGAGAKKTGSTAGASGTAYGDSGGTAGSGLSSLGGSSNALESGGENNQSLAGNGTSYDDAGAAGVD 281
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2506462997 379 RWYENGQLftgfRYYTGTYYWFENGVRQNaGWRYAWNYTYWTNNEGRAVQGHQTIDGKDYYFGDDGTYYKR 449
Cdd:COG5263 282 GTGTTGTV----GWVDGKWYYFDAGKMVT-GWQTINGKWYYFDSDGAMATGWQKINGKWYYFDEDGAMATG 347
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
255-440 |
4.01e-04 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 42.69 E-value: 4.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506462997 255 QNNTPANGYYND-GTGYKWFENGQLYTGFRNYMGTYYFFENGMRQDNKWETAWGMKYYVGSDGRAVQGvqvidgnkyYFG 333
Cdd:NF033838 480 QPSTPKTGWKQEnGMWYFYNTDGSMATGWLQNNGSWYYLNANGAMATGWLQNNGSWYYLNANGSMATG---------WLQ 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506462997 334 NNTT-FYLRTNTTIQSGntilkandsgvlepWTgyiydgsAYNGGyrWY---ENGQLFTGFRYYTGTYYWFENGVRQNAG 409
Cdd:NF033838 551 NNGSwYYLNANGAMATG--------------WL-------QYNGS--WYylnANGDMATGWLQYNGSWYYLNANGDMATG 607
|
170 180 190
....*....|....*....|....*....|.
gi 2506462997 410 WRYAWNYTYWTNNEGRAVQGhQTIDGKDYYF 440
Cdd:NF033838 608 WLQYNGSWYYLNANGSMATG-WVKDGDTWYY 637
|
|
| glucan_65_rpt |
TIGR04035 |
glucan-binding repeat; This model describes a region of about 63 amino acids that is composed ... |
310-335 |
6.31e-04 |
|
glucan-binding repeat; This model describes a region of about 63 amino acids that is composed of three repeats of a more broadly distributed family of shorter repeats modeled by pfam01473. While the shorter repeats are often associated with choline binding (and therefore with cell wall binding), the longer repeat described here represents a subgroup of repeat sequences associated with glucan binding, as found in a number glycosylhydrolases. Shah, et al. describe a repeat consensus, WYYFDANGKAVTGAQTINGQTLYFDQDGKQVKG, that corresponds to half of the repeat as modeled here and one and a half copies of the repeat as modeled by pfam01473.
Pssm-ID: 274933 [Multi-domain] Cd Length: 62 Bit Score: 37.88 E-value: 6.31e-04
|
| PspC_relate_1 |
NF033840 |
PspC-related protein choline-binding protein 1; Members of this family share C-terminal ... |
241-385 |
1.25e-03 |
|
PspC-related protein choline-binding protein 1; Members of this family share C-terminal homology to the choline-binding form of the pneumococcal surface antigen PspC, but not to its allelic LPXTG-anchored forms because they lack the choline-binding repeat region. Members of this family should not be confused with PspC itself, whose identity and function reflect regions N-terminal to the choline-binding region. See Iannelli, et al. (PMID: 11891047) for information about the different allelic forms of PspC.
Pssm-ID: 411409 [Multi-domain] Cd Length: 648 Bit Score: 41.22 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506462997 241 ISVNSNGYNDGIFYQNN--TPANGYYND-GTGYKWFENGQLYTGFRNYMGTYYFFENGMRQDNKWETAWGMKYYVGSDGR 317
Cdd:NF033840 488 VSVTSNQGTDAAVEPAKpvAPTTGWKQEnGMWYFYNTDGSMATGWVQVNGSWYYLNSNGSMATGWVQVNGSWYYLNSNGS 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506462997 318 AVQGVQVIDGNKYYFGNNTT------------FYLRTNTTI------QSGNTILKANDSGVLEPWTGYiydgsaynGGYR 379
Cdd:NF033840 568 MATGWVQVDGSWYYLNDNGSmetgwlqnngswYYLNSNGSMkanqwfQVGSKWYYVNASGELAVNTSI--------DGYR 639
|
....*.
gi 2506462997 380 WYENGQ 385
Cdd:NF033840 640 VNDNGE 645
|
|
| glucan_65_rpt |
TIGR04035 |
glucan-binding repeat; This model describes a region of about 63 amino acids that is composed ... |
418-444 |
1.28e-03 |
|
glucan-binding repeat; This model describes a region of about 63 amino acids that is composed of three repeats of a more broadly distributed family of shorter repeats modeled by pfam01473. While the shorter repeats are often associated with choline binding (and therefore with cell wall binding), the longer repeat described here represents a subgroup of repeat sequences associated with glucan binding, as found in a number glycosylhydrolases. Shah, et al. describe a repeat consensus, WYYFDANGKAVTGAQTINGQTLYFDQDGKQVKG, that corresponds to half of the repeat as modeled here and one and a half copies of the repeat as modeled by pfam01473.
Pssm-ID: 274933 [Multi-domain] Cd Length: 62 Bit Score: 37.11 E-value: 1.28e-03
10 20
....*....|....*....|....*..
gi 2506462997 418 YWTNNEGRAVQGHQTIDGKDYYFGDDG 444
Cdd:TIGR04035 1 YYFDADGKAVTGAQTIDGVTYYFDENG 27
|
|
| PspC_relate_1 |
NF033840 |
PspC-related protein choline-binding protein 1; Members of this family share C-terminal ... |
363-445 |
4.43e-03 |
|
PspC-related protein choline-binding protein 1; Members of this family share C-terminal homology to the choline-binding form of the pneumococcal surface antigen PspC, but not to its allelic LPXTG-anchored forms because they lack the choline-binding repeat region. Members of this family should not be confused with PspC itself, whose identity and function reflect regions N-terminal to the choline-binding region. See Iannelli, et al. (PMID: 11891047) for information about the different allelic forms of PspC.
Pssm-ID: 411409 [Multi-domain] Cd Length: 648 Bit Score: 39.29 E-value: 4.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506462997 363 PWTGYIYDgsayNGGYRWYE-NGQLFTGFRYYTGTYYWFENGVRQNAGWRYAWNYTYWTNNEGRAVQGHQTIDGKDYYFG 441
Cdd:NF033840 508 PTTGWKQE----NGMWYFYNtDGSMATGWVQVNGSWYYLNSNGSMATGWVQVNGSWYYLNSNGSMATGWVQVDGSWYYLN 583
|
....
gi 2506462997 442 DDGT 445
Cdd:NF033840 584 DNGS 587
|
|
| Glyco_25 |
smart00641 |
Glycosyl hydrolases family 25; |
47-126 |
6.91e-03 |
|
Glycosyl hydrolases family 25;
Pssm-ID: 128889 Cd Length: 109 Bit Score: 36.24 E-value: 6.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506462997 47 VDVSSNNGTISVAdykKMQEYGVKAVIVKLSEADSYKNPYAKVQIANAKEAGLKV-GAYHYSwYASTADAQAEAKYFTDY 125
Cdd:smart00641 4 IDVSDYEGGIDGA---KVRNTGASFAFMKATEGAGYTPPYYSYQYFLADNAGYILrGFYHAA-YPVSSSATAQANYFPSM 79
|
.
gi 2506462997 126 A 126
Cdd:smart00641 80 D 80
|
|
| |
