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Conserved domains on  [gi|1090689823|emb|SEG02192|]
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Putative cell wall binding repeat-containing protein [Lachnospira multipara]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
pneumo_PspA super family cl41532
pneumococcal surface protein A; The pneumococcal surface protein proteins, found in ...
 314-492 5.89e-73

pneumococcal surface protein A; The pneumococcal surface protein proteins, found in Streptococcus pneumoniae, are repetitive, with patterns of localized high sequence identity across pairs of proteins given different specific names that recombination may be presumed. This protein, PspA, has an N-terminal region that lacks a cross-wall-targeting YSIRK type extended signal peptide, in contrast to the closely related choline-binding protein CbpA which has a similar C-terminus but a YSIRK-containing region at the N-terminus.


The actual alignment was detected with superfamily member NF033930:

Pssm-ID: 468251 [Multi-domain]  Cd Length: 660  Bit Score: 243.28  E-value: 5.89e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090689823 314 TPTTGTWVNHGYGYWYQRfDGSYPyDQWEKIGGNWYYFNHDGYRQTGWLLDRGTWYYLNGSGAMQTGWILDKGTWYYLNG 393
Cdd:NF033930  440 APKTGWKQENGMWYFYNT-DGSMA-TGWLQNNGSWYYLNSNGAMATGWLQYNGSWYYLNANGAMATGWAKVNGSWYYLNA 517

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090689823 394 SGAMQTGWLLDRGTWYYLNGSGVMQTGWLLDNGTWYYLNDNGAMATGWIKLGETWYYLNGSGAMQTGWLLDNGSWYYLTA 473
Cdd:NF033930  518 NGAMATGWLQYNGSWYYLNANGAMATGWLKYNGSWYYLNANGAMATGWLQYNGSWYYLNANGAMATGWAKVNGSWYYLNA 597

                         170       180
                  ....*....|....*....|..
gi 1090689823 474 SGAMATNTYIDG---YYVDGSG 492
Cdd:NF033930  598 NGSMATGWVKDGdtwYYLEASG 619
GH25_muramidase super family cl10448
Endo-N-acetylmuramidases (muramidases) are lysozymes (also referred to as peptidoglycan ...
 110-295 6.68e-59

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.


The actual alignment was detected with superfamily member cd06414:

Pssm-ID: 447900  Cd Length: 191  Bit Score: 192.78  E-value: 6.68e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090689823 110 IKGIDVSRYQGSINWTEVRNEGINYVMIRVGY---SNRNLDYNYEDNISGSNLAGLHTGVYFYSTAMSVEQSIGDAQWVI 186
Cdd:cd06414     1 KKGIDVSEWQGDIDWKKVKASGVDFAIIRAGYggyGELQEDKYFEENIKGAKAAGIPVGVYFYSYAVTVAEAREEAEFVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090689823 187 NQLRGYKVDYPVAIDLESWDQ--AELGREEVTRIAKAFCDEIRAAGYTPMVYCNENWARNYVDFSKLDGVEKWIARYGYY 264
Cdd:cd06414    81 RLIKGYKLSYPVYYDLEDETQlgAGLSKDQRTDIANAFCETIEAAGYYPGIYANLSWLTNKLDDERLSKYDVWVAQYGNS 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1090689823 265 YDTSITRGMWQAGSQYRLNGISSTfVDIDFA 295
Cdd:cd06414   161 PTYPGNYGMWQYTSSGSVPGISGN-VDLNYC 190
PspC_relate_1 super family cl41464
PspC-related protein choline-binding protein 1; Members of this family share C-terminal ...
 33-96 5.62e-14

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.


The actual alignment was detected with superfamily member NF033840:

Pssm-ID: 411409 [Multi-domain]  Cd Length: 648  Bit Score: 74.35  E-value: 5.62e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1090689823  33 WEQEGDEWYYYDDNGNRITGWSEINGHWYYFDTSDCQAVkGWQKINGKWQYFQLSGDYECAWVE 96
Cdd:NF033840  512 WKQENGMWYFYNTDGSMATGWVQVNGSWYYLNSNGSMAT-GWVQVNGSWYYLNSNGSMATGWVQ 574
 
Name Accession Description Interval E-value
pneumo_PspA NF033930
pneumococcal surface protein A; The pneumococcal surface protein proteins, found in ...
 314-492 5.89e-73

pneumococcal surface protein A; The pneumococcal surface protein proteins, found in Streptococcus pneumoniae, are repetitive, with patterns of localized high sequence identity across pairs of proteins given different specific names that recombination may be presumed. This protein, PspA, has an N-terminal region that lacks a cross-wall-targeting YSIRK type extended signal peptide, in contrast to the closely related choline-binding protein CbpA which has a similar C-terminus but a YSIRK-containing region at the N-terminus.


Pssm-ID: 468251 [Multi-domain]  Cd Length: 660  Bit Score: 243.28  E-value: 5.89e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090689823 314 TPTTGTWVNHGYGYWYQRfDGSYPyDQWEKIGGNWYYFNHDGYRQTGWLLDRGTWYYLNGSGAMQTGWILDKGTWYYLNG 393
Cdd:NF033930  440 APKTGWKQENGMWYFYNT-DGSMA-TGWLQNNGSWYYLNSNGAMATGWLQYNGSWYYLNANGAMATGWAKVNGSWYYLNA 517

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090689823 394 SGAMQTGWLLDRGTWYYLNGSGVMQTGWLLDNGTWYYLNDNGAMATGWIKLGETWYYLNGSGAMQTGWLLDNGSWYYLTA 473
Cdd:NF033930  518 NGAMATGWLQYNGSWYYLNANGAMATGWLKYNGSWYYLNANGAMATGWLQYNGSWYYLNANGAMATGWAKVNGSWYYLNA 597

                         170       180
                  ....*....|....*....|..
gi 1090689823 474 SGAMATNTYIDG---YYVDGSG 492
Cdd:NF033930  598 NGSMATGWVKDGdtwYYLEASG 619
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
 309-495 3.90e-72

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: 241.84  E-value: 3.90e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090689823 309 PISSYTPTTGTWVNHGYGYWYQRfDGSYPyDQWEKIGGNWYYFNHDGYRQTGWLLDRGTWYYLNGSGAMQTGWILDKGTW 388
Cdd:NF033838  478 PAQPSTPKTGWKQENGMWYFYNT-DGSMA-TGWLQNNGSWYYLNANGAMATGWLQNNGSWYYLNANGSMATGWLQNNGSW 555

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090689823 389 YYLNGSGAMQTGWLLDRGTWYYLNGSGVMQTGWLLDNGTWYYLNDNGAMATGWIKLGETWYYLNGSGAMQTGWLLDNGSW 468
Cdd:NF033838  556 YYLNANGAMATGWLQYNGSWYYLNANGDMATGWLQYNGSWYYLNANGDMATGWLQYNGSWYYLNANGSMATGWVKDGDTW 635

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1090689823 469 YYLTASGAM---------------------ATNTYIDGYYVDGSGRWV 495
Cdd:NF033838  636 YYLEASGAMkasqwfkvsdkwyyvngsgalAVNTTVDGYGVNANGEWV 683
pneumo_PspA NF033930
pneumococcal surface protein A; The pneumococcal surface protein proteins, found in ...
 337-495 4.54e-72

pneumococcal surface protein A; The pneumococcal surface protein proteins, found in Streptococcus pneumoniae, are repetitive, with patterns of localized high sequence identity across pairs of proteins given different specific names that recombination may be presumed. This protein, PspA, has an N-terminal region that lacks a cross-wall-targeting YSIRK type extended signal peptide, in contrast to the closely related choline-binding protein CbpA which has a similar C-terminus but a YSIRK-containing region at the N-terminus.


Pssm-ID: 468251 [Multi-domain]  Cd Length: 660  Bit Score: 240.97  E-value: 4.54e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090689823 337 PYDQWEKIGGNWYYFNHDGYRQTGWLLDRGTWYYLNGSGAMQTGWILDKGTWYYLNGSGAMQTGWLLDRGTWYYLNGSGV 416
Cdd:NF033930  441 PKTGWKQENGMWYFYNTDGSMATGWLQNNGSWYYLNSNGAMATGWLQYNGSWYYLNANGAMATGWAKVNGSWYYLNANGA 520

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090689823 417 MQTGWLLDNGTWYYLNDNGAMATGWIKLGETWYYLNGSGAMQTGWLLDNGSWYYLTASGAMATN-TYIDG--YYVDGSGR 493
Cdd:NF033930  521 MATGWLQYNGSWYYLNANGAMATGWLKYNGSWYYLNANGAMATGWLQYNGSWYYLNANGAMATGwAKVNGswYYLNANGS 600


                  ....*.
gi 1090689823 494 ----WV 495
Cdd:NF033930  601 matgWV 606
pneumo_PspA NF033930
pneumococcal surface protein A; The pneumococcal surface protein proteins, found in ...
 341-495 1.70e-71

pneumococcal surface protein A; The pneumococcal surface protein proteins, found in Streptococcus pneumoniae, are repetitive, with patterns of localized high sequence identity across pairs of proteins given different specific names that recombination may be presumed. This protein, PspA, has an N-terminal region that lacks a cross-wall-targeting YSIRK type extended signal peptide, in contrast to the closely related choline-binding protein CbpA which has a similar C-terminus but a YSIRK-containing region at the N-terminus.


Pssm-ID: 468251 [Multi-domain]  Cd Length: 660  Bit Score: 239.43  E-value: 1.70e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090689823 341 WEKIGGNWYYFNHDGYRQTGWLLDRGTWYYLNGSGAMQTGWILDKGTWYYLNGSGAMQTGWLLDRGTWYYLNGSGVMQTG 420
Cdd:NF033930  485 WLQYNGSWYYLNANGAMATGWAKVNGSWYYLNANGAMATGWLQYNGSWYYLNANGAMATGWLKYNGSWYYLNANGAMATG 564

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090689823 421 WLLDNGTWYYLNDNGAMATGWIKLGETWYYLNGSGAMQTGWLLDNGSWYYLTASGAM---------------------AT 479
Cdd:NF033930  565 WLQYNGSWYYLNANGAMATGWAKVNGSWYYLNANGSMATGWVKDGDTWYYLEASGAMkasqwfkvsdkwyyvnglgalAV 644

                         170
                  ....*....|....*.
gi 1090689823 480 NTYIDGYYVDGSGRWV 495
Cdd:NF033930  645 NTTVDGYTVNANGEWV 660
GH25_LytC-like cd06414
The LytC lysozyme of Streptococcus pneumoniae is a bacterial cell wall hydrolase that cleaves ...
 110-295 6.68e-59

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: 192.78  E-value: 6.68e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090689823 110 IKGIDVSRYQGSINWTEVRNEGINYVMIRVGY---SNRNLDYNYEDNISGSNLAGLHTGVYFYSTAMSVEQSIGDAQWVI 186
Cdd:cd06414     1 KKGIDVSEWQGDIDWKKVKASGVDFAIIRAGYggyGELQEDKYFEENIKGAKAAGIPVGVYFYSYAVTVAEAREEAEFVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090689823 187 NQLRGYKVDYPVAIDLESWDQ--AELGREEVTRIAKAFCDEIRAAGYTPMVYCNENWARNYVDFSKLDGVEKWIARYGYY 264
Cdd:cd06414    81 RLIKGYKLSYPVYYDLEDETQlgAGLSKDQRTDIANAFCETIEAAGYYPGIYANLSWLTNKLDDERLSKYDVWVAQYGNS 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1090689823 265 YDTSITRGMWQAGSQYRLNGISSTfVDIDFA 295
Cdd:cd06414   161 PTYPGNYGMWQYTSSGSVPGISGN-VDLNYC 190
PspC_relate_1 NF033840
PspC-related protein choline-binding protein 1; Members of this family share C-terminal ...
 296-495 1.35e-54

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: 193.76  E-value: 1.35e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090689823 296 TKDYSKIVTARKAPISSYtPTTGTwVNHGYGYWYQRFDGSYPYDQWEKIGGNWYYFNHDGYRQTGWLLDRGTWYYLNGSG 375
Cdd:NF033840  469 TREPEKVVVPKKSSIPSY-PVSVT-SNQGTDAAVEPAKPVAPTTGWKQENGMWYFYNTDGSMATGWVQVNGSWYYLNSNG 546

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090689823 376 AMQTGWILDKGTWYYLNGSGAMQTGWLLDRGTWYYLNGSGVMQTGWLLDNGTWYYLNDNGAM-ATGWIKLGETWYYLNgs 454
Cdd:NF033840  547 SMATGWVQVNGSWYYLNSNGSMATGWVQVDGSWYYLNDNGSMETGWLQNNGSWYYLNSNGSMkANQWFQVGSKWYYVN-- 624

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1090689823 455 gamqtgwlldngswyyltASGAMATNTYIDGYYVDGSGRWV 495
Cdd:NF033840  625 ------------------ASGELAVNTSIDGYRVNDNGEWV 647
COG5263 COG5263
Glucan-binding domain (YG repeat) [Carbohydrate transport and metabolism];
57-495 4.93e-48

Glucan-binding domain (YG repeat) [Carbohydrate transport and metabolism];


Pssm-ID: 444077 [Multi-domain]  Cd Length: 486  Bit Score: 172.75  E-value: 4.93e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090689823  57 NGHWYYFDTSDCQAVKGWQKINGKWQYFQLSGDYECAWVEDRTHNGMDFEAGTIKGIDVSRYQGSINWTEVRNEGINYVM 136
Cdd:COG5263    35 AASDVDLVTENVTVENEKTSGVNGKSKDGGAGEVSEKGDLSSDVGYVTDSAQGGSGNSSAGNNNDVYDVYVVYEGGSVKD 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090689823 137 IRVGYSNRNLDYNYEDNISGSNLAGLHTGVYFYSTAMSVEQSIGDAQWVINQLRGYKVDYPVAIDLESWDQAELGREEVT 216
Cdd:COG5263   115 YGGGVSDDGDDVVDKTNVAAGGGGKTKKGDTNSANTGYLGDDLGGGTADKGGSAGYGAGKDGATAAAKELVGSAADTYYG 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090689823 217 RIAKAFCDEIRAAGYTP----MVYCNENWARNYVDFSKLDGVEKWIARYGYYYDTSITRGMWQAGSQYRLNGISSTFVDI 292
Cdd:COG5263   195 GASTYLTGDAGAYGALGlaagSGAGAKKTGSTAGASGTAYGDSGGTAGSGLSSLGGSSNALESGGENNQSLAGNGTSYDD 274

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090689823 293 DFATKDYSKIVTARKAPISS--YTPTTGTWVN---HGYGYWYQRFDGSYPYDQWEKIGGNWYYFNHDGYRQTGWLLDRGT 367
Cdd:COG5263   275 AGAAGVDGTGTTGTVGWVDGkwYYFDAGKMVTgwqTINGKWYYFDSDGAMATGWQKINGKWYYFDEDGAMATGWVTDDGK 354

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090689823 368 WYYLNGSGAMQTGWILDKGTWYYLNGSGAMQTGWLLDRGTWYYLNGSGVMQTGWLLDNGTWYYLNDNGAMATGWIKLGET 447
Cdd:COG5263   355 WYYLGSDGAMATGWQKIDGKWYYFDSNGAMATGWVKVDGKWYYFDSSGAMATGWLKIDGKWYYFDSDGAMATGWQKIGGK 434

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1090689823 448 WYYLNGSGAMQTGWLLDNGSWYYLTASGAMATNTY-IDG--YYVDGSGRWV 495
Cdd:COG5263   435 WYYFDSNGAMATGWVKVDGKWYYFDSDGAMATGWQtIDGktYYFDSNGAWV 485
Acm COG3757
Lyzozyme M1 (1,4-beta-N-acetylmuramidase), GH25 family [Cell wall/membrane/envelope biogenesis] ...
 105-293 1.70e-45

Lyzozyme M1 (1,4-beta-N-acetylmuramidase), GH25 family [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442971  Cd Length: 208  Bit Score: 158.14  E-value: 1.70e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090689823 105 FEAGTIKGIDVSRYQGSINWTEVRNEGINYVMIRVGYSNRNLDYNYEDNISGSNLAGLHTGVYFYSTAMS--VEQsigdA 182
Cdd:COG3757     6 GAAYPVHGIDVSHYQGDIDWAAVKAAGIDFAYIKATEGTDYVDPKFARNWAGARAAGLPRGAYHFFRPCSdaAAQ----A 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090689823 183 QWVINQLRGYKVDYPVAIDLESWDQAELGREEVTRIAKAFCDEIRAA-GYTPMVYCNENWARNYVDFSKLDGVEKWIARY 261
Cdd:COG3757    82 DNFISTVPRDPGDLPPVLDLEENGYYGLSPAQLRAWLKAFLDEVEAHtGRKPIIYTSPSFYNDYLGNSDFSDYPLWIARY 161

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1090689823 262 GYYYDTSITRG--MWQAGSQYRLNGIsSTFVDID 293
Cdd:COG3757   162 GSSPGYLPGRNwtFWQYTSSGRVPGI-SGNVDLN 194
Glyco_hydro_25 pfam01183
Glycosyl hydrolases family 25;
113-285 5.69e-18

Glycosyl hydrolases family 25;


Pssm-ID: 426105  Cd Length: 180  Bit Score: 81.64  E-value: 5.69e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090689823 113 IDVSRYQGSINWTEVRNEGINYVMIRVGYSNRNLDYNYEDNISGSNLAGLHTGVYFYSTAMSVEQSIGDAQWVINQLRG- 191
Cdd:pfam01183   1 IDVSSYQGDIDWQKVKASGVSFVFIKATEGTDYVDPYFTTQYANARAAGLKVGAYHFARPCNSSTAAAQADYFLSNVQGl 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090689823 192 --YKVDYPVAIDLESwdQAELGREEVTRIAKAFCDEIR-AAGYTPMVYCNENWARNYVDFSKLDGVEK-WIARYG----- 262
Cdd:pfam01183  81 glDAGTLPPVLDVEV--TTGLTKAAATSNILRFLDRVKkQTGYKPVIYTGTSFWTNNLLYGQFIADYPlWIASYAvtppk 158

                         170       180
                  ....*....|....*....|....
gi 1090689823 263 -YYYDTSITrgMWQAGSQYRLNGI 285
Cdd:pfam01183 159 dYPGWTKWT--FWQYTSSGSIPGV 180
PspC_relate_1 NF033840
PspC-related protein choline-binding protein 1; Members of this family share C-terminal ...
 33-96 5.62e-14

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: 74.35  E-value: 5.62e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1090689823  33 WEQEGDEWYYYDDNGNRITGWSEINGHWYYFDTSDCQAVkGWQKINGKWQYFQLSGDYECAWVE 96
Cdd:NF033840  512 WKQENGMWYFYNTDGSMATGWVQVNGSWYYLNSNGSMAT-GWVQVNGSWYYLNSNGSMATGWVQ 574
PspC_relate_1 NF033840
PspC-related protein choline-binding protein 1; Members of this family share C-terminal ...
 22-97 1.52e-13

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: 73.19  E-value: 1.52e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1090689823  22 FIVTKTEAAQHWEQEGDEWYYYDDNGNRITGWSEINGHWYYFDTSDCQAVkGWQKINGKWQYFQLSGDYECAWVED 97
Cdd:NF033840  521 FYNTDGSMATGWVQVNGSWYYLNSNGSMATGWVQVNGSWYYLNSNGSMAT-GWVQVDGSWYYLNDNGSMETGWLQN 595
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
 30-97 7.55e-12

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: 67.73  E-value: 7.55e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1090689823  30 AQHWEQEGDEWYYYDDNGNRITGWSEINGHWYYFDTSDCQAVkGWQKINGKWQYFQLSGDYECAWVED 97
Cdd:NF033838  565 ATGWLQYNGSWYYLNANGDMATGWLQYNGSWYYLNANGDMAT-GWLQYNGSWYYLNANGSMATGWVKD 631
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
 30-96 1.47e-11

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: 66.96  E-value: 1.47e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1090689823  30 AQHWEQEGDEWYYYDDNGNRITGWSEINGHWYYFDTSDCQAVkGWQKINGKWQYFQLSGDYECAWVE 96
Cdd:NF033838  545 ATGWLQNNGSWYYLNANGAMATGWLQYNGSWYYLNANGDMAT-GWLQYNGSWYYLNANGDMATGWLQ 610
pneumo_PspA NF033930
pneumococcal surface protein A; The pneumococcal surface protein proteins, found in ...
 30-96 3.28e-11

pneumococcal surface protein A; The pneumococcal surface protein proteins, found in Streptococcus pneumoniae, are repetitive, with patterns of localized high sequence identity across pairs of proteins given different specific names that recombination may be presumed. This protein, PspA, has an N-terminal region that lacks a cross-wall-targeting YSIRK type extended signal peptide, in contrast to the closely related choline-binding protein CbpA which has a similar C-terminus but a YSIRK-containing region at the N-terminus.


Pssm-ID: 468251 [Multi-domain]  Cd Length: 660  Bit Score: 65.71  E-value: 3.28e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1090689823  30 AQHWEQEGDEWYYYDDNGNRITGWSEINGHWYYFDTSDCQAVkGWQKINGKWQYFQLSGDYECAWVE 96
Cdd:NF033930  482 ATGWLQYNGSWYYLNANGAMATGWAKVNGSWYYLNANGAMAT-GWLQYNGSWYYLNANGAMATGWLK 547
PspC_relate_1 NF033840
PspC-related protein choline-binding protein 1; Members of this family share C-terminal ...
 30-89 1.99e-10

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: 63.18  E-value: 1.99e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090689823  30 AQHWEQEGDEWYYYDDNGNRITGWSEINGHWYYFDTSDCQAVKGWQKINGKWQYFQLSGD 89
Cdd:NF033840  569 ATGWVQVDGSWYYLNDNGSMETGWLQNNGSWYYLNSNGSMKANQWFQVGSKWYYVNASGE 628
pneumo_PspA NF033930
pneumococcal surface protein A; The pneumococcal surface protein proteins, found in ...
 30-88 3.26e-08

pneumococcal surface protein A; The pneumococcal surface protein proteins, found in Streptococcus pneumoniae, are repetitive, with patterns of localized high sequence identity across pairs of proteins given different specific names that recombination may be presumed. This protein, PspA, has an N-terminal region that lacks a cross-wall-targeting YSIRK type extended signal peptide, in contrast to the closely related choline-binding protein CbpA which has a similar C-terminus but a YSIRK-containing region at the N-terminus.


Pssm-ID: 468251 [Multi-domain]  Cd Length: 660  Bit Score: 56.08  E-value: 3.26e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1090689823  30 AQHWEQEGDEWYYYDDNGNRITGWSEINGHWYYFDTSDCQAVkGWQKINGKWQYFQLSG 88
Cdd:NF033930  562 ATGWLQYNGSWYYLNANGAMATGWAKVNGSWYYLNANGSMAT-GWVKDGDTWYYLEASG 619
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
 30-88 1.29e-07

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: 54.25  E-value: 1.29e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1090689823  30 AQHWEQEGDEWYYYDDNGNRITGWSEINGHWYYFDTSDCQAVkGWQKINGKWQYFQLSG 88
Cdd:NF033838  585 ATGWLQYNGSWYYLNANGDMATGWLQYNGSWYYLNANGSMAT-GWVKDGDTWYYLEASG 642
Choline_bind_3 pfam19127
Choline-binding repeat; Pair of presumed choline-binding repeats often found adjacent to ...
 438-482 2.68e-07

Choline-binding repeat; Pair of presumed choline-binding repeats often found adjacent to pfam01473.


Pssm-ID: 465978 [Multi-domain]  Cd Length: 47  Bit Score: 47.15  E-value: 2.68e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1090689823 438 ATGWIKLGETWYYLNGSGAMQTGWLL-DNGSWYYLTA-SGAMATNTY 482
Cdd:pfam19127   1 VTGWQTINGQTLYFDSDGKQVKGWVVtIDGKWYYFDAdSGEMVTNRF 47
PspC_relate_1 NF033840
PspC-related protein choline-binding protein 1; Members of this family share C-terminal ...
 51-96 1.14e-06

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: 51.24  E-value: 1.14e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1090689823  51 TGWSEINGHWYYFDTsDCQAVKGWQKINGKWQYFQLSGDYECAWVE 96
Cdd:NF033840  510 TGWKQENGMWYFYNT-DGSMATGWVQVNGSWYYLNSNGSMATGWVQ 554
glucan_65_rpt TIGR04035
glucan-binding repeat; This model describes a region of about 63 amino acids that is composed ...
 41-84 1.37e-06

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: 45.59  E-value: 1.37e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1090689823  41 YYYDDNGNRITGWSEINGHWYYFDTSDCQAVKGWQKINGKWQYF 84
Cdd:TIGR04035   1 YYFDADGKAVTGAQTIDGVTYYFDENGKQVKGDFVTNGGGTYYY 44
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
 30-88 3.05e-06

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: 50.01  E-value: 3.05e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1090689823  30 AQHWEQEGDEWYYYDDNGNRITGWSEINGHWYYFDTSDCQAVKGWQKINGKWQYFQLSG 88
Cdd:NF033838  605 ATGWLQYNGSWYYLNANGSMATGWVKDGDTWYYLEASGAMKASQWFKVSDKWYYVNGSG 663
Choline_bind_3 pfam19127
Choline-binding repeat; Pair of presumed choline-binding repeats often found adjacent to ...
 51-84 2.22e-05

Choline-binding repeat; Pair of presumed choline-binding repeats often found adjacent to pfam01473.


Pssm-ID: 465978 [Multi-domain]  Cd Length: 47  Bit Score: 41.76  E-value: 2.22e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1090689823  51 TGWSEINGHWYYFDtSDCQAVKGWQK-INGKWQYF 84
Cdd:pfam19127   2 TGWQTINGQTLYFD-SDGKQVKGWVVtIDGKWYYF 35
Glyco_25 smart00641
Glycosyl hydrolases family 25;
110-152 4.03e-03

Glycosyl hydrolases family 25;


Pssm-ID: 128889  Cd Length: 109  Bit Score: 37.01  E-value: 4.03e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1090689823  110 IKGIDVSRYQGSINWTEVRNEGINYVMIR----VGYSNRNLDYNYED 152
Cdd:smart00641   1 TKGIDVSDYEGGIDGAKVRNTGASFAFMKategAGYTPPYYSYQYFL 47
 
Name Accession Description Interval E-value
pneumo_PspA NF033930
pneumococcal surface protein A; The pneumococcal surface protein proteins, found in ...
 314-492 5.89e-73

pneumococcal surface protein A; The pneumococcal surface protein proteins, found in Streptococcus pneumoniae, are repetitive, with patterns of localized high sequence identity across pairs of proteins given different specific names that recombination may be presumed. This protein, PspA, has an N-terminal region that lacks a cross-wall-targeting YSIRK type extended signal peptide, in contrast to the closely related choline-binding protein CbpA which has a similar C-terminus but a YSIRK-containing region at the N-terminus.


Pssm-ID: 468251 [Multi-domain]  Cd Length: 660  Bit Score: 243.28  E-value: 5.89e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090689823 314 TPTTGTWVNHGYGYWYQRfDGSYPyDQWEKIGGNWYYFNHDGYRQTGWLLDRGTWYYLNGSGAMQTGWILDKGTWYYLNG 393
Cdd:NF033930  440 APKTGWKQENGMWYFYNT-DGSMA-TGWLQNNGSWYYLNSNGAMATGWLQYNGSWYYLNANGAMATGWAKVNGSWYYLNA 517

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090689823 394 SGAMQTGWLLDRGTWYYLNGSGVMQTGWLLDNGTWYYLNDNGAMATGWIKLGETWYYLNGSGAMQTGWLLDNGSWYYLTA 473
Cdd:NF033930  518 NGAMATGWLQYNGSWYYLNANGAMATGWLKYNGSWYYLNANGAMATGWLQYNGSWYYLNANGAMATGWAKVNGSWYYLNA 597

                         170       180
                  ....*....|....*....|..
gi 1090689823 474 SGAMATNTYIDG---YYVDGSG 492
Cdd:NF033930  598 NGSMATGWVKDGdtwYYLEASG 619
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
 309-495 3.90e-72

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: 241.84  E-value: 3.90e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090689823 309 PISSYTPTTGTWVNHGYGYWYQRfDGSYPyDQWEKIGGNWYYFNHDGYRQTGWLLDRGTWYYLNGSGAMQTGWILDKGTW 388
Cdd:NF033838  478 PAQPSTPKTGWKQENGMWYFYNT-DGSMA-TGWLQNNGSWYYLNANGAMATGWLQNNGSWYYLNANGSMATGWLQNNGSW 555

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090689823 389 YYLNGSGAMQTGWLLDRGTWYYLNGSGVMQTGWLLDNGTWYYLNDNGAMATGWIKLGETWYYLNGSGAMQTGWLLDNGSW 468
Cdd:NF033838  556 YYLNANGAMATGWLQYNGSWYYLNANGDMATGWLQYNGSWYYLNANGDMATGWLQYNGSWYYLNANGSMATGWVKDGDTW 635

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1090689823 469 YYLTASGAM---------------------ATNTYIDGYYVDGSGRWV 495
Cdd:NF033838  636 YYLEASGAMkasqwfkvsdkwyyvngsgalAVNTTVDGYGVNANGEWV 683
pneumo_PspA NF033930
pneumococcal surface protein A; The pneumococcal surface protein proteins, found in ...
 337-495 4.54e-72

pneumococcal surface protein A; The pneumococcal surface protein proteins, found in Streptococcus pneumoniae, are repetitive, with patterns of localized high sequence identity across pairs of proteins given different specific names that recombination may be presumed. This protein, PspA, has an N-terminal region that lacks a cross-wall-targeting YSIRK type extended signal peptide, in contrast to the closely related choline-binding protein CbpA which has a similar C-terminus but a YSIRK-containing region at the N-terminus.


Pssm-ID: 468251 [Multi-domain]  Cd Length: 660  Bit Score: 240.97  E-value: 4.54e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090689823 337 PYDQWEKIGGNWYYFNHDGYRQTGWLLDRGTWYYLNGSGAMQTGWILDKGTWYYLNGSGAMQTGWLLDRGTWYYLNGSGV 416
Cdd:NF033930  441 PKTGWKQENGMWYFYNTDGSMATGWLQNNGSWYYLNSNGAMATGWLQYNGSWYYLNANGAMATGWAKVNGSWYYLNANGA 520

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090689823 417 MQTGWLLDNGTWYYLNDNGAMATGWIKLGETWYYLNGSGAMQTGWLLDNGSWYYLTASGAMATN-TYIDG--YYVDGSGR 493
Cdd:NF033930  521 MATGWLQYNGSWYYLNANGAMATGWLKYNGSWYYLNANGAMATGWLQYNGSWYYLNANGAMATGwAKVNGswYYLNANGS 600


                  ....*.
gi 1090689823 494 ----WV 495
Cdd:NF033930  601 matgWV 606
pneumo_PspA NF033930
pneumococcal surface protein A; The pneumococcal surface protein proteins, found in ...
 341-495 1.70e-71

pneumococcal surface protein A; The pneumococcal surface protein proteins, found in Streptococcus pneumoniae, are repetitive, with patterns of localized high sequence identity across pairs of proteins given different specific names that recombination may be presumed. This protein, PspA, has an N-terminal region that lacks a cross-wall-targeting YSIRK type extended signal peptide, in contrast to the closely related choline-binding protein CbpA which has a similar C-terminus but a YSIRK-containing region at the N-terminus.


Pssm-ID: 468251 [Multi-domain]  Cd Length: 660  Bit Score: 239.43  E-value: 1.70e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090689823 341 WEKIGGNWYYFNHDGYRQTGWLLDRGTWYYLNGSGAMQTGWILDKGTWYYLNGSGAMQTGWLLDRGTWYYLNGSGVMQTG 420
Cdd:NF033930  485 WLQYNGSWYYLNANGAMATGWAKVNGSWYYLNANGAMATGWLQYNGSWYYLNANGAMATGWLKYNGSWYYLNANGAMATG 564

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090689823 421 WLLDNGTWYYLNDNGAMATGWIKLGETWYYLNGSGAMQTGWLLDNGSWYYLTASGAM---------------------AT 479
Cdd:NF033930  565 WLQYNGSWYYLNANGAMATGWAKVNGSWYYLNANGSMATGWVKDGDTWYYLEASGAMkasqwfkvsdkwyyvnglgalAV 644

                         170
                  ....*....|....*.
gi 1090689823 480 NTYIDGYYVDGSGRWV 495
Cdd:NF033930  645 NTTVDGYTVNANGEWV 660
GH25_LytC-like cd06414
The LytC lysozyme of Streptococcus pneumoniae is a bacterial cell wall hydrolase that cleaves ...
 110-295 6.68e-59

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: 192.78  E-value: 6.68e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090689823 110 IKGIDVSRYQGSINWTEVRNEGINYVMIRVGY---SNRNLDYNYEDNISGSNLAGLHTGVYFYSTAMSVEQSIGDAQWVI 186
Cdd:cd06414     1 KKGIDVSEWQGDIDWKKVKASGVDFAIIRAGYggyGELQEDKYFEENIKGAKAAGIPVGVYFYSYAVTVAEAREEAEFVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090689823 187 NQLRGYKVDYPVAIDLESWDQ--AELGREEVTRIAKAFCDEIRAAGYTPMVYCNENWARNYVDFSKLDGVEKWIARYGYY 264
Cdd:cd06414    81 RLIKGYKLSYPVYYDLEDETQlgAGLSKDQRTDIANAFCETIEAAGYYPGIYANLSWLTNKLDDERLSKYDVWVAQYGNS 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1090689823 265 YDTSITRGMWQAGSQYRLNGISSTfVDIDFA 295
Cdd:cd06414   161 PTYPGNYGMWQYTSSGSVPGISGN-VDLNYC 190
PspC_relate_1 NF033840
PspC-related protein choline-binding protein 1; Members of this family share C-terminal ...
 296-495 1.35e-54

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: 193.76  E-value: 1.35e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090689823 296 TKDYSKIVTARKAPISSYtPTTGTwVNHGYGYWYQRFDGSYPYDQWEKIGGNWYYFNHDGYRQTGWLLDRGTWYYLNGSG 375
Cdd:NF033840  469 TREPEKVVVPKKSSIPSY-PVSVT-SNQGTDAAVEPAKPVAPTTGWKQENGMWYFYNTDGSMATGWVQVNGSWYYLNSNG 546

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090689823 376 AMQTGWILDKGTWYYLNGSGAMQTGWLLDRGTWYYLNGSGVMQTGWLLDNGTWYYLNDNGAM-ATGWIKLGETWYYLNgs 454
Cdd:NF033840  547 SMATGWVQVNGSWYYLNSNGSMATGWVQVDGSWYYLNDNGSMETGWLQNNGSWYYLNSNGSMkANQWFQVGSKWYYVN-- 624

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1090689823 455 gamqtgwlldngswyyltASGAMATNTYIDGYYVDGSGRWV 495
Cdd:NF033840  625 ------------------ASGELAVNTSIDGYRVNDNGEWV 647
COG5263 COG5263
Glucan-binding domain (YG repeat) [Carbohydrate transport and metabolism];
57-495 4.93e-48

Glucan-binding domain (YG repeat) [Carbohydrate transport and metabolism];


Pssm-ID: 444077 [Multi-domain]  Cd Length: 486  Bit Score: 172.75  E-value: 4.93e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090689823  57 NGHWYYFDTSDCQAVKGWQKINGKWQYFQLSGDYECAWVEDRTHNGMDFEAGTIKGIDVSRYQGSINWTEVRNEGINYVM 136
Cdd:COG5263    35 AASDVDLVTENVTVENEKTSGVNGKSKDGGAGEVSEKGDLSSDVGYVTDSAQGGSGNSSAGNNNDVYDVYVVYEGGSVKD 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090689823 137 IRVGYSNRNLDYNYEDNISGSNLAGLHTGVYFYSTAMSVEQSIGDAQWVINQLRGYKVDYPVAIDLESWDQAELGREEVT 216
Cdd:COG5263   115 YGGGVSDDGDDVVDKTNVAAGGGGKTKKGDTNSANTGYLGDDLGGGTADKGGSAGYGAGKDGATAAAKELVGSAADTYYG 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090689823 217 RIAKAFCDEIRAAGYTP----MVYCNENWARNYVDFSKLDGVEKWIARYGYYYDTSITRGMWQAGSQYRLNGISSTFVDI 292
Cdd:COG5263   195 GASTYLTGDAGAYGALGlaagSGAGAKKTGSTAGASGTAYGDSGGTAGSGLSSLGGSSNALESGGENNQSLAGNGTSYDD 274

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090689823 293 DFATKDYSKIVTARKAPISS--YTPTTGTWVN---HGYGYWYQRFDGSYPYDQWEKIGGNWYYFNHDGYRQTGWLLDRGT 367
Cdd:COG5263   275 AGAAGVDGTGTTGTVGWVDGkwYYFDAGKMVTgwqTINGKWYYFDSDGAMATGWQKINGKWYYFDEDGAMATGWVTDDGK 354

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090689823 368 WYYLNGSGAMQTGWILDKGTWYYLNGSGAMQTGWLLDRGTWYYLNGSGVMQTGWLLDNGTWYYLNDNGAMATGWIKLGET 447
Cdd:COG5263   355 WYYLGSDGAMATGWQKIDGKWYYFDSNGAMATGWVKVDGKWYYFDSSGAMATGWLKIDGKWYYFDSDGAMATGWQKIGGK 434

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1090689823 448 WYYLNGSGAMQTGWLLDNGSWYYLTASGAMATNTY-IDG--YYVDGSGRWV 495
Cdd:COG5263   435 WYYFDSNGAMATGWVKVDGKWYYFDSDGAMATGWQtIDGktYYFDSNGAWV 485
Acm COG3757
Lyzozyme M1 (1,4-beta-N-acetylmuramidase), GH25 family [Cell wall/membrane/envelope biogenesis] ...
 105-293 1.70e-45

Lyzozyme M1 (1,4-beta-N-acetylmuramidase), GH25 family [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442971  Cd Length: 208  Bit Score: 158.14  E-value: 1.70e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090689823 105 FEAGTIKGIDVSRYQGSINWTEVRNEGINYVMIRVGYSNRNLDYNYEDNISGSNLAGLHTGVYFYSTAMS--VEQsigdA 182
Cdd:COG3757     6 GAAYPVHGIDVSHYQGDIDWAAVKAAGIDFAYIKATEGTDYVDPKFARNWAGARAAGLPRGAYHFFRPCSdaAAQ----A 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090689823 183 QWVINQLRGYKVDYPVAIDLESWDQAELGREEVTRIAKAFCDEIRAA-GYTPMVYCNENWARNYVDFSKLDGVEKWIARY 261
Cdd:COG3757    82 DNFISTVPRDPGDLPPVLDLEENGYYGLSPAQLRAWLKAFLDEVEAHtGRKPIIYTSPSFYNDYLGNSDFSDYPLWIARY 161

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1090689823 262 GYYYDTSITRG--MWQAGSQYRLNGIsSTFVDID 293
Cdd:COG3757   162 GSSPGYLPGRNwtFWQYTSSGRVPGI-SGNVDLN 194
GH25_muramidase cd00599
Endo-N-acetylmuramidases (muramidases) are lysozymes (also referred to as peptidoglycan ...
 111-293 8.39e-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: 109.36  E-value: 8.39e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090689823 111 KGIDVSRYQGSINWTEVRNEGINYVMIRVGYSNRNLDYNYEDNISGSNLAGLHTGVYFYSTAmsVEQSIGDAQWVINQLR 190
Cdd:cd00599     1 KGIDVSSWQGSIDWNAVKAAGIDFVFIKATEGTTYVDPKFATNRARARAAGLLVGAYHFARP--CANAEAQADNFVNTVP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090689823 191 GYKVDYPVAIDLEsWDQAELGREEVTRIAKAFCDEI-RAAGYTPMVYCNENWARNYVDFSKLDGVEKWIARYGYYYDTSI 269
Cdd:cd00599    79 RDPGSLPLVLDVE-DTGGGCSAAALAAWLNAFLNEVeALTGKKPIIYTSPSFWDDYLASSQLSDYPLWIAHYRGEPPPAP 157

                         170       180
                  ....*....|....*....|....*...
gi 1090689823 270 TRG----MWQAGSQYRLNGISSTfVDID 293
Cdd:cd00599   158 GAWrpwtLWQYTSSGRVPGISGP-VDLN 184
GH25_Lyc-like cd06525
Lyc muramidase is an autolytic lysozyme (autolysin) from Clostridium acetobutylicum encoded by ...
 111-294 2.15e-18

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: 82.73  E-value: 2.15e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090689823 111 KGIDVSRYQGSINWTEVRNEGINYVMIRVGYSNRNLDYNYEDNISGSNLAGLHTGVYFYSTAMSveQSIGDAQWVINQLR 190
Cdd:cd06525     1 KGIDISNWQGNINFNAVKDSGVEVVYIKATEGTTFVDSYFNENYNGAKAAGLKVGFYHFLVGTS--NPEEQAENFYNTIK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090689823 191 GYKVDYPVAIDLESwdQAELGREEVTRIAKAFCDEIRA-AGYTPMVYCNENWARNYVDfSKLDGVEKWIARYGYYYDTSI 269
Cdd:cd06525    79 GKKMDLKPALDVEV--NFGLSKDELNDYVLRFIEEFEKlSGLKVGIYTYTSFINNNLD-SRLSSYPLWIANYGVSPPSSN 155

                         170       180
                  ....*....|....*....|....*....
gi 1090689823 270 TRGMWQAGSQY----RLNGISSTfVDIDF 294
Cdd:cd06525   156 GIWNSWVGFQYsetgRVNGVSGS-VDLDE 183
COG5263 COG5263
Glucan-binding domain (YG repeat) [Carbohydrate transport and metabolism];
338-419 3.03e-18

Glucan-binding domain (YG repeat) [Carbohydrate transport and metabolism];


Pssm-ID: 444077 [Multi-domain]  Cd Length: 486  Bit Score: 87.23  E-value: 3.03e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090689823 338 YDQWEKIGGNWYYFNHDGYRQTGWLLDRGTWYYLNGSGAMQTGWILDKGTWYYLNGSGAMQTGWLLDRGTWYYLNGSGVM 417
Cdd:COG5263   405 ATGWLKIDGKWYYFDSDGAMATGWQKIGGKWYYFDSNGAMATGWVKVDGKWYYFDSDGAMATGWQTIDGKTYYFDSNGAW 484


                  ..
gi 1090689823 418 QT 419
Cdd:COG5263   485 VG 486
Glyco_hydro_25 pfam01183
Glycosyl hydrolases family 25;
113-285 5.69e-18

Glycosyl hydrolases family 25;


Pssm-ID: 426105  Cd Length: 180  Bit Score: 81.64  E-value: 5.69e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090689823 113 IDVSRYQGSINWTEVRNEGINYVMIRVGYSNRNLDYNYEDNISGSNLAGLHTGVYFYSTAMSVEQSIGDAQWVINQLRG- 191
Cdd:pfam01183   1 IDVSSYQGDIDWQKVKASGVSFVFIKATEGTDYVDPYFTTQYANARAAGLKVGAYHFARPCNSSTAAAQADYFLSNVQGl 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090689823 192 --YKVDYPVAIDLESwdQAELGREEVTRIAKAFCDEIR-AAGYTPMVYCNENWARNYVDFSKLDGVEK-WIARYG----- 262
Cdd:pfam01183  81 glDAGTLPPVLDVEV--TTGLTKAAATSNILRFLDRVKkQTGYKPVIYTGTSFWTNNLLYGQFIADYPlWIASYAvtppk 158

                         170       180
                  ....*....|....*....|....
gi 1090689823 263 -YYYDTSITrgMWQAGSQYRLNGI 285
Cdd:pfam01183 159 dYPGWTKWT--FWQYTSSGSIPGV 180
GH25_muramidase_1 cd06413
Uncharacterized bacterial muramidase containing a glycosyl hydrolase family 25 (GH25) ...
 109-292 7.32e-15

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: 73.08  E-value: 7.32e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090689823 109 TIKGIDVSRYQGSINWTEVRNEGINYVMIRVGYSNRNLDYNYEDNISGSNLAGLHTGVY-FYSTAMSVEQSigdAQWVIN 187
Cdd:cd06413     2 PVRGIDVSHHQGDIDWARVRAQGVSFAYIKATEGGDHVDKRFAENWRGARAAGLPRGAYhFFTFCRSGAEQ---AANFIR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090689823 188 QLRGYKVDYPVAIDLESW-DQAE-LGREEVTRIAKAFCDEIRAA-GYTPMVYCNEN---------------WARNYVDFS 249
Cdd:cd06413    79 NVPKDPGALPPVVDVEWNgNSATcPSAEEVLAELQVFLDALEAHyGKRPIIYTTYDfyddylkgefpdyplWIRSVAGHP 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1090689823 250 KLDGVEKWIarygyyydtsitrgMWQAGSQYRLNGIsSTFVDI 292
Cdd:cd06413   159 RLYEDRPWT--------------FWQYTNRGRVPGI-EGDVDL 186
GH25_PlyB-like cd06523
PlyB is a bacteriophage endolysin that displays potent lytic activity toward Bacillus ...
 113-286 1.03e-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: 72.01  E-value: 1.03e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090689823 113 IDVSRYQGSINWT-EVRNEGINYVMIRVGYSNRNLDYNYEDNISGSNLAGLHTGVYFYSTAMSVEQSIGDAQWVINqlRG 191
Cdd:cd06523     3 VDISEWQGPINWDyDTLSKQLDLVIIRVQYGSNYVDLKYKNNIKEFKKRGIPFGVYAFARGTSTADAKAEARDFYN--RA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090689823 192 YKVDYPVAIDLE--SWDQAELGreevtriAKAFCDEIRAAGYTPMV-YCNENWARNYV-DFSKLDGVekWIARYG----- 262
Cdd:cd06523    81 NKKPTFYVLDVEvtSMSDMNAG-------VQAFISELRRLGAKKVGlYIGHHFYTTFNlAVSKFDAI--WIPAYGsnpgt 151

                         170       180
                  ....*....|....*....|....
gi 1090689823 263 YYYDtsitrgMWQAGSQYRLNGIS 286
Cdd:cd06523   152 YPYD------LWQYTDSGYLPGIS 169
PspC_relate_1 NF033840
PspC-related protein choline-binding protein 1; Members of this family share C-terminal ...
 33-96 5.62e-14

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: 74.35  E-value: 5.62e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1090689823  33 WEQEGDEWYYYDDNGNRITGWSEINGHWYYFDTSDCQAVkGWQKINGKWQYFQLSGDYECAWVE 96
Cdd:NF033840  512 WKQENGMWYFYNTDGSMATGWVQVNGSWYYLNSNGSMAT-GWVQVNGSWYYLNSNGSMATGWVQ 574
PspC_relate_1 NF033840
PspC-related protein choline-binding protein 1; Members of this family share C-terminal ...
 22-97 1.52e-13

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: 73.19  E-value: 1.52e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1090689823  22 FIVTKTEAAQHWEQEGDEWYYYDDNGNRITGWSEINGHWYYFDTSDCQAVkGWQKINGKWQYFQLSGDYECAWVED 97
Cdd:NF033840  521 FYNTDGSMATGWVQVNGSWYYLNSNGSMATGWVQVNGSWYYLNSNGSMAT-GWVQVDGSWYYLNDNGSMETGWLQN 595
GH25_AtlA-like cd06522
AtlA is an autolysin found in Gram-positive lactic acid bacteria that degrades bacterial cell ...
 113-294 3.73e-12

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: 65.08  E-value: 3.73e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090689823 113 IDVSRYQGSI---NWTEVRNEGINYVMIRVGYSNRNLDYNYEDNISGSNLAGLHTGVYFYSTAMSVEQSIGDAQWVINQL 189
Cdd:cd06522     4 VDVSSNNGIMsvaDYNKLKNYGVKAVIVKLTEGTTYRNPYAASQIANAKAAGLKVSAYHYAHYTSAADAQAEARYFANTA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090689823 190 R--GYKVDYPVAIDLESwdqAELGREeVTRIAKAFCDEIRAAGYT-PMVYCNENWARNYVDFSKLDGVEKWIARYGYYYD 266
Cdd:cd06522    84 KslGLSKNTVMVADMED---SSSSGN-ATANVNAFWQTMKAAGYKnTDVYTSASWLNSRADTSTLGAKRVWVAQYPYNPS 159

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1090689823 267 TSI----TRGMWQAGSQYRLNGISSTF-VDIDF 294
Cdd:cd06522   160 SNNlwntNYGAWQWTSQAHFPGRSGGFdVSIDY 192
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
 30-97 7.55e-12

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: 67.73  E-value: 7.55e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1090689823  30 AQHWEQEGDEWYYYDDNGNRITGWSEINGHWYYFDTSDCQAVkGWQKINGKWQYFQLSGDYECAWVED 97
Cdd:NF033838  565 ATGWLQYNGSWYYLNANGDMATGWLQYNGSWYYLNANGDMAT-GWLQYNGSWYYLNANGSMATGWVKD 631
GH25_YegX-like cd06524
YegX is an uncharacterized bacterial protein with a glycosyl hydrolase family 25 (GH25) ...
 111-293 7.89e-12

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: 64.29  E-value: 7.89e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090689823 111 KGIDVSRYQGSINWTE----VRNEGINYVMIRVGYSNRNLDYNYEDNISGSNLAGLHTGVY-FYSTAMSVEQSigdAQWV 185
Cdd:cd06524     1 FGIDVSHYQGKIDWQKvkakVKDSPVAFVFIKATEGVDIVDPDFPTNWEGAKEAGIIRGAYhFYRPNSDPKQQ---ADNF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090689823 186 INQLRGYKV-DYPVAIDLEsWDQAELGREEVTRIAKAFCDEI-RAAGYTPMVYCNENWARNYVDFSKLDGVEKWIARYG- 262
Cdd:cd06524    78 LNTVKLLGPgDLPPVLDVE-WDGRKSSAKQIQEGVLEWLDAVeKATGVKPIIYTNPSFWTDYLTDSSFSEYPLWIADYNp 156

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1090689823 263 ----YYYDTSITRGMWQAGSQYRLNGISSTfVDID 293
Cdd:cd06524   157 rrkkVPPNESKKWLLWQYSDSGKVPGISGA-VDLN 190
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
 30-96 1.47e-11

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: 66.96  E-value: 1.47e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1090689823  30 AQHWEQEGDEWYYYDDNGNRITGWSEINGHWYYFDTSDCQAVkGWQKINGKWQYFQLSGDYECAWVE 96
Cdd:NF033838  545 ATGWLQNNGSWYYLNANGAMATGWLQYNGSWYYLNANGDMAT-GWLQYNGSWYYLNANGDMATGWLQ 610
pneumo_PspA NF033930
pneumococcal surface protein A; The pneumococcal surface protein proteins, found in ...
 30-96 3.28e-11

pneumococcal surface protein A; The pneumococcal surface protein proteins, found in Streptococcus pneumoniae, are repetitive, with patterns of localized high sequence identity across pairs of proteins given different specific names that recombination may be presumed. This protein, PspA, has an N-terminal region that lacks a cross-wall-targeting YSIRK type extended signal peptide, in contrast to the closely related choline-binding protein CbpA which has a similar C-terminus but a YSIRK-containing region at the N-terminus.


Pssm-ID: 468251 [Multi-domain]  Cd Length: 660  Bit Score: 65.71  E-value: 3.28e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1090689823  30 AQHWEQEGDEWYYYDDNGNRITGWSEINGHWYYFDTSDCQAVkGWQKINGKWQYFQLSGDYECAWVE 96
Cdd:NF033930  482 ATGWLQYNGSWYYLNANGAMATGWAKVNGSWYYLNANGAMAT-GWLQYNGSWYYLNANGAMATGWLK 547
PspC_relate_1 NF033840
PspC-related protein choline-binding protein 1; Members of this family share C-terminal ...
 30-89 1.99e-10

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: 63.18  E-value: 1.99e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090689823  30 AQHWEQEGDEWYYYDDNGNRITGWSEINGHWYYFDTSDCQAVKGWQKINGKWQYFQLSGD 89
Cdd:NF033840  569 ATGWVQVDGSWYYLNDNGSMETGWLQNNGSWYYLNSNGSMKANQWFQVGSKWYYVNASGE 628
GH25_Cpl1-like cd06415
Cpl-1 lysin (also known as Cpl-9 lysozyme / muramidase) is a bacterial cell wall endolysin ...
 112-264 6.00e-09

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: 55.87  E-value: 6.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090689823 112 GIDVSRYQGSiNWTEVRNEGINYVMIRVGYSNRNLDYNYEDNISGSNLAGLHTGVYFYS-TAMSVEQSIGDAQWVINQLR 190
Cdd:cd06415     3 GVDVASYQGT-DLTAYGQAGAKFAIVKISEGTNYVNPKASAQVSSAIANGKMTGGYHFArFGGSVSQAKYEADYFLNSAQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090689823 191 GY---KVDYpVAIDLESWDQAElgREEVTRIAKAFCDEIRAAGYTPMVYCNENWARNYVDFSKLdgVEK-----WIARYG 262
Cdd:cd06415    82 QAglpKGSY-LALDYEQGSGNS--KAANTSAILAFMDTIKDAGYKPMLYSYKPLLLNNVDYSQI--IAKypnslWVAAYP 156


                  ..
gi 1090689823 263 YY 264
Cdd:cd06415   157 TY 158
pneumo_PspA NF033930
pneumococcal surface protein A; The pneumococcal surface protein proteins, found in ...
 30-88 3.26e-08

pneumococcal surface protein A; The pneumococcal surface protein proteins, found in Streptococcus pneumoniae, are repetitive, with patterns of localized high sequence identity across pairs of proteins given different specific names that recombination may be presumed. This protein, PspA, has an N-terminal region that lacks a cross-wall-targeting YSIRK type extended signal peptide, in contrast to the closely related choline-binding protein CbpA which has a similar C-terminus but a YSIRK-containing region at the N-terminus.


Pssm-ID: 468251 [Multi-domain]  Cd Length: 660  Bit Score: 56.08  E-value: 3.26e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1090689823  30 AQHWEQEGDEWYYYDDNGNRITGWSEINGHWYYFDTSDCQAVkGWQKINGKWQYFQLSG 88
Cdd:NF033930  562 ATGWLQYNGSWYYLNANGAMATGWAKVNGSWYYLNANGSMAT-GWVKDGDTWYYLEASG 619
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
 30-88 1.29e-07

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: 54.25  E-value: 1.29e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1090689823  30 AQHWEQEGDEWYYYDDNGNRITGWSEINGHWYYFDTSDCQAVkGWQKINGKWQYFQLSG 88
Cdd:NF033838  585 ATGWLQYNGSWYYLNANGDMATGWLQYNGSWYYLNANGSMAT-GWVKDGDTWYYLEASG 642
Choline_bind_3 pfam19127
Choline-binding repeat; Pair of presumed choline-binding repeats often found adjacent to ...
 438-482 2.68e-07

Choline-binding repeat; Pair of presumed choline-binding repeats often found adjacent to pfam01473.


Pssm-ID: 465978 [Multi-domain]  Cd Length: 47  Bit Score: 47.15  E-value: 2.68e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1090689823 438 ATGWIKLGETWYYLNGSGAMQTGWLL-DNGSWYYLTA-SGAMATNTY 482
Cdd:pfam19127   1 VTGWQTINGQTLYFDSDGKQVKGWVVtIDGKWYYFDAdSGEMVTNRF 47
PspC_relate_1 NF033840
PspC-related protein choline-binding protein 1; Members of this family share C-terminal ...
 51-96 1.14e-06

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: 51.24  E-value: 1.14e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1090689823  51 TGWSEINGHWYYFDTsDCQAVKGWQKINGKWQYFQLSGDYECAWVE 96
Cdd:NF033840  510 TGWKQENGMWYFYNT-DGSMATGWVQVNGSWYYLNSNGSMATGWVQ 554
glucan_65_rpt TIGR04035
glucan-binding repeat; This model describes a region of about 63 amino acids that is composed ...
 41-84 1.37e-06

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: 45.59  E-value: 1.37e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1090689823  41 YYYDDNGNRITGWSEINGHWYYFDTSDCQAVKGWQKINGKWQYF 84
Cdd:TIGR04035   1 YYFDADGKAVTGAQTIDGVTYYFDENGKQVKGDFVTNGGGTYYY 44
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
 30-88 3.05e-06

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: 50.01  E-value: 3.05e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1090689823  30 AQHWEQEGDEWYYYDDNGNRITGWSEINGHWYYFDTSDCQAVKGWQKINGKWQYFQLSG 88
Cdd:NF033838  605 ATGWLQYNGSWYYLNANGSMATGWVKDGDTWYYLEASGAMKASQWFKVSDKWYYVNGSG 663
GH25_CH-type cd06412
CH-type (Chalaropsis-type) lysozymes represent one of four functionally-defined classes of ...
 110-262 3.52e-06

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: 47.70  E-value: 3.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090689823 110 IKGIDVSRYQGSINWTEVRNEGINYVMIRV--GYSNRNLdyNYEDNISGSNLAGLHTGVYFYSTAmsvEQSIGDAQ--WV 185
Cdd:cd06412     1 VPGIDVSGHQGSVDWSGAAANGARFAYVKAteGTSYTNP--RFSSQYNGAYNAGLIRGAYHFALP---DQSSGAAQadYF 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090689823 186 INQLRGYKVD---YPVAIDLESWDQAE----LGREEVTRIAKAFCDEIRAA-GYTPMVYCNENWARNYVDFSKLDGVEK- 256
Cdd:cd06412    76 LDHGGGWSPDgrtLPGVLDLEYNPYGAtcygLSPAQMVSWIKDFSDTYKARtGRDPVIYTTTSWWNQCTGNSAGFANHPl 155


                  ....*.
gi 1090689823 257 WIARYG 262
Cdd:cd06412   156 WLARYG 161
Choline_bind_3 pfam19127
Choline-binding repeat; Pair of presumed choline-binding repeats often found adjacent to ...
 341-377 6.57e-06

Choline-binding repeat; Pair of presumed choline-binding repeats often found adjacent to pfam01473.


Pssm-ID: 465978 [Multi-domain]  Cd Length: 47  Bit Score: 43.30  E-value: 6.57e-06
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1090689823 341 WEKIGGNWYYFNHDGYRQTGWLL-DRGTWYYLNG-SGAM 377
Cdd:pfam19127   4 WQTINGQTLYFDSDGKQVKGWVVtIDGKWYYFDAdSGEM 42
Choline_bind_3 pfam19127
Choline-binding repeat; Pair of presumed choline-binding repeats often found adjacent to ...
 399-439 1.31e-05

Choline-binding repeat; Pair of presumed choline-binding repeats often found adjacent to pfam01473.


Pssm-ID: 465978 [Multi-domain]  Cd Length: 47  Bit Score: 42.14  E-value: 1.31e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1090689823 399 TGWLLDRGTWYYLNGSGVMQTGWLL-DNGTWYYLN-DNGAMAT 439
Cdd:pfam19127   2 TGWQTINGQTLYFDSDGKQVKGWVVtIDGKWYYFDaDSGEMVT 44
Choline_bind_3 pfam19127
Choline-binding repeat; Pair of presumed choline-binding repeats often found adjacent to ...
 51-84 2.22e-05

Choline-binding repeat; Pair of presumed choline-binding repeats often found adjacent to pfam01473.


Pssm-ID: 465978 [Multi-domain]  Cd Length: 47  Bit Score: 41.76  E-value: 2.22e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1090689823  51 TGWSEINGHWYYFDtSDCQAVKGWQK-INGKWQYF 84
Cdd:pfam19127   2 TGWQTINGQTLYFD-SDGKQVKGWVVtIDGKWYYF 35
Choline_bind_3 pfam19127
Choline-binding repeat; Pair of presumed choline-binding repeats often found adjacent to ...
 359-397 2.59e-04

Choline-binding repeat; Pair of presumed choline-binding repeats often found adjacent to pfam01473.


Pssm-ID: 465978 [Multi-domain]  Cd Length: 47  Bit Score: 38.68  E-value: 2.59e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1090689823 359 TGWLLDRGTWYYLNGSGAMQTGWIL-DKGTWYYLNG-SGAM 397
Cdd:pfam19127   2 TGWQTINGQTLYFDSDGKQVKGWVVtIDGKWYYFDAdSGEM 42
Choline_bind_3 pfam19127
Choline-binding repeat; Pair of presumed choline-binding repeats often found adjacent to ...
 379-417 6.68e-04

Choline-binding repeat; Pair of presumed choline-binding repeats often found adjacent to pfam01473.


Pssm-ID: 465978 [Multi-domain]  Cd Length: 47  Bit Score: 37.52  E-value: 6.68e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1090689823 379 TGWILDKGTWYYLNGSGAMQTGWLL-DRGTWYYLNG-SGVM 417
Cdd:pfam19127   2 TGWQTINGQTLYFDSDGKQVKGWVVtIDGKWYYFDAdSGEM 42
GH25_LysA-like cd06417
LysA is a cell wall endolysin produced by Lactobacillus fermentum, which degrades bacterial ...
 110-267 1.19e-03

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: 40.12  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090689823 110 IKGIDVSRYQGSINWTEVRNEginYVMIRV----GYSNRNLDYNYEDNISgsnlAGLHTGVYFYSTAMSVEQsigDAQWV 185
Cdd:cd06417     1 MNGIDVSSWQSRIVTTVVPAD---FVIVKAtqgtGYVNPSWRSQAAQAIA----AGKLLGLYHYANGGNAIA---EADYF 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090689823 186 INQLRGYKVDYPVAIDLESWDQAELGREEvtrIAKAFCDEI-RAAGYTPMVYCNENWARNYvDFSKLDGVEKWIARYGYY 264
Cdd:cd06417    71 LNNIKGYVGKAVLVLDWESYQNSAWGNSA---WARQWVNRVhELTGVWPMVYVSKSVTRQI-NWSVRADCGLWVAQYASN 146


                  ...
gi 1090689823 265 YDT 267
Cdd:cd06417   147 NPT 149
Glyco_25 smart00641
Glycosyl hydrolases family 25;
110-152 4.03e-03

Glycosyl hydrolases family 25;


Pssm-ID: 128889  Cd Length: 109  Bit Score: 37.01  E-value: 4.03e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1090689823  110 IKGIDVSRYQGSINWTEVRNEGINYVMIR----VGYSNRNLDYNYED 152
Cdd:smart00641   1 TKGIDVSDYEGGIDGAKVRNTGASFAFMKategAGYTPPYYSYQYFL 47
Choline_bind_2 pfam19085
Choline-binding repeat; this entry contains a pair of presumed choline-binding repeats that ...
 469-494 4.13e-03

Choline-binding repeat; this entry contains a pair of presumed choline-binding repeats that are often found adjacent to pfam01473.


Pssm-ID: 436951 [Multi-domain]  Cd Length: 38  Bit Score: 34.96  E-value: 4.13e-03
                          10        20
                  ....*....|....*....|....*...
gi 1090689823 469 YYLTASGAMATNTYIDG--YYVDGSGRW 494
Cdd:pfam19085  11 YYLGSDGAMATNTWVDDgrYYVGADGKW 38
Choline_bind_1 pfam01473
Putative cell wall binding repeat; These repeats are characterized by conserved aromatic ...
 419-437 6.16e-03

Putative cell wall binding repeat; These repeats are characterized by conserved aromatic residues and glycines are found in multiple tandem copies in a number of proteins. The CW repeat is 20 amino acid residues long. The exact domain boundaries may not be correct. It has been suggested that these repeats in Swiss:P15057 might be responsible for the specific recognition of choline-containing cell walls. Similar but longer repeats are found in the glucosyltransferases and glucan-binding proteins of oral streptococci and shown to be involved in glucan binding as well as in the related dextransucrases of Leuconostoc mesenteroides. Repeats also occur in toxins of Clostridium difficile and other clostridia, though the ligands are not always known.


Pssm-ID: 366661 [Multi-domain]  Cd Length: 19  Bit Score: 34.28  E-value: 6.16e-03
                          10
                  ....*....|....*....
gi 1090689823 419 TGWLLDNGTWYYLNDNGAM 437
Cdd:pfam01473   1 TGWVKINGNWYYFDSNGVM 19
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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