|
Name |
Accession |
Description |
Interval |
E-value |
| PRK06347 |
PRK06347 |
1,4-beta-N-acetylmuramoylhydrolase; |
108-607 |
1.44e-108 |
|
1,4-beta-N-acetylmuramoylhydrolase;
Pssm-ID: 180536 [Multi-domain] Cd Length: 592 Bit Score: 340.52 E-value: 1.44e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 108 PTTPSTEQPTADSTTPVESGTTDSSVAEITPV--APSATESEAAPAVT-----PDDEVKVPEARVASAQTFSALSPTQSP 180
Cdd:PRK06347 71 KEAPATATPENTTEPTVEPKQTETKEQTKTPEekQPAAKQVEKAPAEPatvsnPDNATSSSTPATYNLLQKSALRSGATV 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 181 SEFIAELARCAQPIAQANDLYASVMMAQAIVESGWGASTLSKAPNYNLFGIKGSYNGQSVYMDTWEYL-NGKWLVKKEPF 259
Cdd:PRK06347 151 QSFIQTIQASSSQIAAENDLYASVMIAQAILESAYGTSELGSAPNYNLFGIKGAYNGQSYTKQTLEDDgKGNYYTITAKF 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 260 RKYPSYMESFQDNAHVL-KTTSFQAGvyYYAGAWKSNTSSYRDATAWLTGRYATDPSYNAKLNNVITAYNLTQYDTPSSG 338
Cdd:PRK06347 231 RKYPSYHQSLEDYAQVIrKGPSWNPN--YYSKVWKSNTTSYKDATKALTGTYATDTAYATKLNDLISRYNLTQYDSGKTT 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 339 GNTGGGTVNPGTGGSNNQSGTNTYYTVKSGDTLNKIAAQYDVSVANLRSWNGISGDLIFVGQKLIVKKGASGNTGGSGNG 418
Cdd:PRK06347 309 GGNSGSTGNSSNSSNTGNTSNAKIYTVVKGDSLWRIANNHKVTVANLKAWNNLKSDFIYPGQKLKVSAGSTTSDTNTSKP 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 419 GSNNNQSGTNT-------YYTVKSGDTLNKIAAQYGVSVANLRSWNGISGDLIFVGQKLIVKKGASGNTGGSNNGGSNNN 491
Cdd:PRK06347 389 STGTSTSKPSTgtstnakVYTVVKGDSLWRIANNNKVTIANLKSWNNLKSDFIYPGQKLKVSAGSTSNTNTSKPSTNTNT 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 492 QSGTNTY------YTIKSGDTLNKIAAQYGVSVANLRSWNGISGDLIFAGQKIIVKKGANSGSTNTNKPTNN--GGGATT 563
Cdd:PRK06347 469 SKPSTNTntnakvYTVAKGDSLWRIANNNKVTIANLKSWNNLKSDFIYPGQKLKVSAGSTTNNTNTAKPSTNkpSNSTVK 548
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1633233584 564 SYTIKSGDTLNKISAQFGVSVANLRSWNGIKGDLIFAGQTIIVK 607
Cdd:PRK06347 549 TYTVKKGDSLWAISRQYKTTVDNIKAWNKLTSNMIHVGQKLTIK 592
|
|
| FlgJ |
COG1705 |
Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell ... |
111-331 |
4.23e-56 |
|
Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell motility];
Pssm-ID: 441311 [Multi-domain] Cd Length: 276 Bit Score: 192.11 E-value: 4.23e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 111 PSTEQPTADSTTPVESGTTDSSVAEITPVAPSATESEAAPAVTPDDEVKVPEARVASAQTFSALSPtqSPSEFIAELARC 190
Cdd:COG1705 62 ASALGGGASALSSAAALALKSAAKSATEAGGGLASANAAATSAAALAASLSGAAALAASATAAASA--SPEEFIAKIAPA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 191 AQPIAQANDLYASVMMAQAIVESGWGASTLSKAPNYNLFGIKGSYN--GQSVYMDTWEYLNGKWLVKKEPFRKYPSYMES 268
Cdd:COG1705 140 AQKAAKKYGVPASVLIAQAALESGWGKSELDGSPSNNLFGIKAGGSwqGKSVEVTTTEYVNGKAVKIKARFRAYDSYAES 219
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1633233584 269 FQDNAHVLKTTSfqagvyYYAGAWKsNTSSYRDATAWL-TGRYATDPSYNAKLNNVITAYNLTQ 331
Cdd:COG1705 220 FRDYARLLKNNP------RYAGALA-NAKDYEAFAKALqKAGYATDPKYADKLISIIESYNLTQ 276
|
|
| LYZ2 |
smart00047 |
Lysozyme subfamily 2; Eubacterial enzymes distantly related to eukaryotic lysozymes. |
177-333 |
2.39e-39 |
|
Lysozyme subfamily 2; Eubacterial enzymes distantly related to eukaryotic lysozymes.
Pssm-ID: 214488 [Multi-domain] Cd Length: 147 Bit Score: 141.80 E-value: 2.39e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 177 TQSPSEFIAELARCAQPIAQANDLYASVMMAQAIVESGWGASTLSKaPNYNLFGIKGSYNGQSVYMDTWEYLNGKWLVKK 256
Cdd:smart00047 5 GGSTLEFVGKIFNEAQKAYQINGVYPSILIAQAALESGWGTSKLAK-KYNNLFGIKGAYDGRPVRMGTLEYLNGGWVTVK 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1633233584 257 EPFRKYPSymESFQDNAHVLKTTSFqagvyYYAGAWKSNtssyrdatAWLTGRYATDPSYNAKLNNVITAYN--LTQYD 333
Cdd:smart00047 84 AAFRGYFG--EKFIDYAYVLRGQNP-----LYKKRWGSN--------ALQTAGYATDPDYAKKLIRIIALYDekLKGYD 147
|
|
| flagell_FlgJ |
TIGR02541 |
flagellar rod assembly protein/muramidase FlgJ; The N-terminal region of this protein acts ... |
127-324 |
6.03e-27 |
|
flagellar rod assembly protein/muramidase FlgJ; The N-terminal region of this protein acts directly in flagellar rod assembly. The C-terminal region is a flagellum-specific muramidase (peptidoglycan hydrolase) required for formation of the outer membrane L ring.
Pssm-ID: 274188 [Multi-domain] Cd Length: 294 Bit Score: 111.48 E-value: 6.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 127 GTTDSSVAEITPVAP----SATESEAAPAVTPDDEVKVPEARVASAQTFSALSPTQ------------SPSEFIAELARC 190
Cdd:TIGR02541 79 GLADMIVAQLTKGQGnepsEGAARGAAPSPLVYRPRLDPKPRRIVKALIESVELSRprgrshaesvpgHPKSFVNSMLPH 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 191 AQPIAQANDLYASVMMAQAIVESGWGASTLSKA---PNYNLFGIK--GSYNGQSVYMDTWEYLNGKWLVKKEPFRKYPSY 265
Cdd:TIGR02541 159 ARKAAQQLGVPPHLILAQAALESGWGQRQIRNAdgsPSYNLFGIKasGSWQGKVVTTMTTEYVDGVAQKLTAKFRSYSSY 238
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1633233584 266 MESFQDNAHVLKTTSfqagvyYYAGAWKSNtSSYRDATAWLTGRYATDPSYNAKLNNVI 324
Cdd:TIGR02541 239 EEAFSDYARLLNNNP------RYEAVLQQR-SAESFARGLQRAGYATDPRYARKLLQVI 290
|
|
| sporang_Gsm |
NF038016 |
sporangiospore maturation cell wall hydrolase GsmA; The peptidoglycan-hydrolyzing enzyme GsmA ... |
176-333 |
6.68e-22 |
|
sporangiospore maturation cell wall hydrolase GsmA; The peptidoglycan-hydrolyzing enzyme GsmA occurs in some sporangia-forming members of the Actinobacteria, such as Actinoplanes missouriensis, and is required for proper separation of spores. GsmA proteins have one or two SH3 domains N-terminal to the hydrolase domain.
Pssm-ID: 411609 [Multi-domain] Cd Length: 312 Bit Score: 96.73 E-value: 6.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 176 PTQSPSEFIAELARCAQPIAQANDLYASVMMAQAIVESGWGASTLSkAPNYNLFGIK--GSY----NGQSVYMDTWEYLN 249
Cdd:NF038016 156 PRGTPAQFIAAVAPPAQQSQRATGVPASVTIAQAILESGWGRSGLT-REDHNYFGIKcfGSPgpiaVGCRSYATFECSPT 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 250 GKWLVKKEPFRKYPSYMESFQDNAHVLKTTSfqagvyYYAGAWKSNTSSYRDATA-WLTGrYATDPSYNAKLNNVITAYN 328
Cdd:NF038016 235 GGCFDTTATFRAYASAADSFRDHGRFLSVNS------RYAPAFAYTDDPDQFAREiHKAG-YATDPTYADKLIGLMKQYN 307
|
....*
gi 1633233584 329 LTQYD 333
Cdd:NF038016 308 LYQYD 312
|
|
| Glucosaminidase |
pfam01832 |
Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase; This family includes ... |
191-271 |
1.06e-21 |
|
Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase; This family includes Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase EC:3.2.1.96. As well as the flageller protein J that has been shown to hydrolyse peptidoglycan.
Pssm-ID: 460354 [Multi-domain] Cd Length: 91 Bit Score: 89.94 E-value: 1.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 191 AQPIAQANDLYASVMMAQAIVESGWGASTLSKaPNYNLFGIKGSYNGQsVYMDTWEYlngkwlVKKEPFRKYPSYMESFQ 270
Cdd:pfam01832 4 AIEAAKKYGIPASVLLAQAALESGWGTSRLAK-ESNNLFGIKASWKGK-VAYDTDEV------TVAARFRKYDSVEESIR 75
|
.
gi 1633233584 271 D 271
Cdd:pfam01832 76 D 76
|
|
| LysM |
pfam01476 |
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ... |
627-668 |
3.60e-15 |
|
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. The structure of this domain is known.
Pssm-ID: 396179 [Multi-domain] Cd Length: 43 Bit Score: 69.73 E-value: 3.60e-15
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1633233584 627 HTVKSGDSLWGLSMQYGISIQKIKQLNGLSGDTIYIGQTLKV 668
Cdd:pfam01476 1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSPNLYVGQKLKI 42
|
|
| LysM |
COG1388 |
LysM repeat [Cell wall/membrane/envelope biogenesis]; |
602-668 |
7.92e-15 |
|
LysM repeat [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440998 [Multi-domain] Cd Length: 156 Bit Score: 72.43 E-value: 7.92e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 602 QTIIVKKGASAGGNASSTNSASG---KRHTVKSGDSLWGLSMQYGISIQKIKQLNGLSGDTIYIGQTLKV 668
Cdd:COG1388 84 ARYTVKSGDTLSGIARRYGAAAApspVTYTVKKGDTLWSIARRYGVSVEELKRWNGLSSDTIRPGQKLKI 153
|
|
| LysM |
cd00118 |
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ... |
429-472 |
3.83e-14 |
|
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.
Pssm-ID: 212030 [Multi-domain] Cd Length: 45 Bit Score: 66.74 E-value: 3.83e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1633233584 429 TYYTVKSGDTLNKIAAQYGVSVANLRSWNGI-SGDLIFVGQKLIV 472
Cdd:cd00118 1 KTYTVKPGDTLWSIAKKYGVTVEELAAANPLiNPDCIYPGQKLKI 45
|
|
| LysM |
cd00118 |
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ... |
625-668 |
2.04e-12 |
|
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.
Pssm-ID: 212030 [Multi-domain] Cd Length: 45 Bit Score: 61.73 E-value: 2.04e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1633233584 625 KRHTVKSGDSLWGLSMQYGISIQKIKQLNGL-SGDTIYIGQTLKV 668
Cdd:cd00118 1 KTYTVKPGDTLWSIAKKYGVTVEELAAANPLiNPDCIYPGQKLKI 45
|
|
| LysM |
smart00257 |
Lysin motif; |
627-668 |
2.46e-12 |
|
Lysin motif;
Pssm-ID: 197609 [Multi-domain] Cd Length: 44 Bit Score: 61.69 E-value: 2.46e-12
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1633233584 627 HTVKSGDSLWGLSMQYGISIQKIKQLNG-LSGDTIYIGQTLKV 668
Cdd:smart00257 2 YTVKKGDTLSSIARRYGISVSDLLELNNiLDPDNLQVGQKLKI 44
|
|
| PRK13914 |
PRK13914 |
invasion associated endopeptidase; |
603-668 |
6.54e-03 |
|
invasion associated endopeptidase;
Pssm-ID: 237555 [Multi-domain] Cd Length: 481 Bit Score: 39.40 E-value: 6.54e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1633233584 603 TIIVKKGASAGGNASSTnSASGKRHTVKSGDSLWGLSMQYGISIQKIKQLNGLSGDTIYIGQTLKV 668
Cdd:PRK13914 7 TIAATAGIAVTAFAAPT-IASASTVVVEAGDTLWGIAQSKGTTVDAIKKANNLTTDKIVPGQKLQV 71
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK06347 |
PRK06347 |
1,4-beta-N-acetylmuramoylhydrolase; |
108-607 |
1.44e-108 |
|
1,4-beta-N-acetylmuramoylhydrolase;
Pssm-ID: 180536 [Multi-domain] Cd Length: 592 Bit Score: 340.52 E-value: 1.44e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 108 PTTPSTEQPTADSTTPVESGTTDSSVAEITPV--APSATESEAAPAVT-----PDDEVKVPEARVASAQTFSALSPTQSP 180
Cdd:PRK06347 71 KEAPATATPENTTEPTVEPKQTETKEQTKTPEekQPAAKQVEKAPAEPatvsnPDNATSSSTPATYNLLQKSALRSGATV 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 181 SEFIAELARCAQPIAQANDLYASVMMAQAIVESGWGASTLSKAPNYNLFGIKGSYNGQSVYMDTWEYL-NGKWLVKKEPF 259
Cdd:PRK06347 151 QSFIQTIQASSSQIAAENDLYASVMIAQAILESAYGTSELGSAPNYNLFGIKGAYNGQSYTKQTLEDDgKGNYYTITAKF 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 260 RKYPSYMESFQDNAHVL-KTTSFQAGvyYYAGAWKSNTSSYRDATAWLTGRYATDPSYNAKLNNVITAYNLTQYDTPSSG 338
Cdd:PRK06347 231 RKYPSYHQSLEDYAQVIrKGPSWNPN--YYSKVWKSNTTSYKDATKALTGTYATDTAYATKLNDLISRYNLTQYDSGKTT 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 339 GNTGGGTVNPGTGGSNNQSGTNTYYTVKSGDTLNKIAAQYDVSVANLRSWNGISGDLIFVGQKLIVKKGASGNTGGSGNG 418
Cdd:PRK06347 309 GGNSGSTGNSSNSSNTGNTSNAKIYTVVKGDSLWRIANNHKVTVANLKAWNNLKSDFIYPGQKLKVSAGSTTSDTNTSKP 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 419 GSNNNQSGTNT-------YYTVKSGDTLNKIAAQYGVSVANLRSWNGISGDLIFVGQKLIVKKGASGNTGGSNNGGSNNN 491
Cdd:PRK06347 389 STGTSTSKPSTgtstnakVYTVVKGDSLWRIANNNKVTIANLKSWNNLKSDFIYPGQKLKVSAGSTSNTNTSKPSTNTNT 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 492 QSGTNTY------YTIKSGDTLNKIAAQYGVSVANLRSWNGISGDLIFAGQKIIVKKGANSGSTNTNKPTNN--GGGATT 563
Cdd:PRK06347 469 SKPSTNTntnakvYTVAKGDSLWRIANNNKVTIANLKSWNNLKSDFIYPGQKLKVSAGSTTNNTNTAKPSTNkpSNSTVK 548
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1633233584 564 SYTIKSGDTLNKISAQFGVSVANLRSWNGIKGDLIFAGQTIIVK 607
Cdd:PRK06347 549 TYTVKKGDSLWAISRQYKTTVDNIKAWNKLTSNMIHVGQKLTIK 592
|
|
| FlgJ |
COG1705 |
Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell ... |
111-331 |
4.23e-56 |
|
Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell motility];
Pssm-ID: 441311 [Multi-domain] Cd Length: 276 Bit Score: 192.11 E-value: 4.23e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 111 PSTEQPTADSTTPVESGTTDSSVAEITPVAPSATESEAAPAVTPDDEVKVPEARVASAQTFSALSPtqSPSEFIAELARC 190
Cdd:COG1705 62 ASALGGGASALSSAAALALKSAAKSATEAGGGLASANAAATSAAALAASLSGAAALAASATAAASA--SPEEFIAKIAPA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 191 AQPIAQANDLYASVMMAQAIVESGWGASTLSKAPNYNLFGIKGSYN--GQSVYMDTWEYLNGKWLVKKEPFRKYPSYMES 268
Cdd:COG1705 140 AQKAAKKYGVPASVLIAQAALESGWGKSELDGSPSNNLFGIKAGGSwqGKSVEVTTTEYVNGKAVKIKARFRAYDSYAES 219
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1633233584 269 FQDNAHVLKTTSfqagvyYYAGAWKsNTSSYRDATAWL-TGRYATDPSYNAKLNNVITAYNLTQ 331
Cdd:COG1705 220 FRDYARLLKNNP------RYAGALA-NAKDYEAFAKALqKAGYATDPKYADKLISIIESYNLTQ 276
|
|
| PRK08581 |
PRK08581 |
amidase domain-containing protein; |
131-335 |
2.18e-44 |
|
amidase domain-containing protein;
Pssm-ID: 236304 [Multi-domain] Cd Length: 619 Bit Score: 168.43 E-value: 2.18e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 131 SSVAEITPVAPSATESEAAPAVTPDDEVKVPEARVASAQTFSALS--------------PTQSPSEFIAELARCAQPIAQ 196
Cdd:PRK08581 257 ETSNTKNPQLPTQDELKHKSKPAQSFENDVNQSNTRSTSLFETGPslsnnddsgsfnvvDSKDTRQFIKSIAKDAHRIGQ 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 197 ANDLYASVMMAQAIVESGWGASTLSKAPNYNLFGIKGSYNGQSVYMDTWEYLNGKWLVKKEPFRKYPSYMESFQDNAHVL 276
Cdd:PRK08581 337 DNDIYASVMIAQAILESDSGQSALAKSPNHNLFGIKGAYEGNSVSFNTLEADGNQLYSINAGFRKYPSTKESLEDYADLI 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1633233584 277 K--TTSFQAgvyYYAGAWKSNTSSYRDATAWLTGRYATDPSYNAKLNNVITAYNLTQYDTP 335
Cdd:PRK08581 417 KngIDGNST---IYKPTWKSEAKSYKDATSHLSKTYATDPNYAKKLNSIIKHYNLTQFDDE 474
|
|
| LYZ2 |
smart00047 |
Lysozyme subfamily 2; Eubacterial enzymes distantly related to eukaryotic lysozymes. |
177-333 |
2.39e-39 |
|
Lysozyme subfamily 2; Eubacterial enzymes distantly related to eukaryotic lysozymes.
Pssm-ID: 214488 [Multi-domain] Cd Length: 147 Bit Score: 141.80 E-value: 2.39e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 177 TQSPSEFIAELARCAQPIAQANDLYASVMMAQAIVESGWGASTLSKaPNYNLFGIKGSYNGQSVYMDTWEYLNGKWLVKK 256
Cdd:smart00047 5 GGSTLEFVGKIFNEAQKAYQINGVYPSILIAQAALESGWGTSKLAK-KYNNLFGIKGAYDGRPVRMGTLEYLNGGWVTVK 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1633233584 257 EPFRKYPSymESFQDNAHVLKTTSFqagvyYYAGAWKSNtssyrdatAWLTGRYATDPSYNAKLNNVITAYN--LTQYD 333
Cdd:smart00047 84 AAFRGYFG--EKFIDYAYVLRGQNP-----LYKKRWGSN--------ALQTAGYATDPDYAKKLIRIIALYDekLKGYD 147
|
|
| flagell_FlgJ |
TIGR02541 |
flagellar rod assembly protein/muramidase FlgJ; The N-terminal region of this protein acts ... |
127-324 |
6.03e-27 |
|
flagellar rod assembly protein/muramidase FlgJ; The N-terminal region of this protein acts directly in flagellar rod assembly. The C-terminal region is a flagellum-specific muramidase (peptidoglycan hydrolase) required for formation of the outer membrane L ring.
Pssm-ID: 274188 [Multi-domain] Cd Length: 294 Bit Score: 111.48 E-value: 6.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 127 GTTDSSVAEITPVAP----SATESEAAPAVTPDDEVKVPEARVASAQTFSALSPTQ------------SPSEFIAELARC 190
Cdd:TIGR02541 79 GLADMIVAQLTKGQGnepsEGAARGAAPSPLVYRPRLDPKPRRIVKALIESVELSRprgrshaesvpgHPKSFVNSMLPH 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 191 AQPIAQANDLYASVMMAQAIVESGWGASTLSKA---PNYNLFGIK--GSYNGQSVYMDTWEYLNGKWLVKKEPFRKYPSY 265
Cdd:TIGR02541 159 ARKAAQQLGVPPHLILAQAALESGWGQRQIRNAdgsPSYNLFGIKasGSWQGKVVTTMTTEYVDGVAQKLTAKFRSYSSY 238
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1633233584 266 MESFQDNAHVLKTTSfqagvyYYAGAWKSNtSSYRDATAWLTGRYATDPSYNAKLNNVI 324
Cdd:TIGR02541 239 EEAFSDYARLLNNNP------RYEAVLQQR-SAESFARGLQRAGYATDPRYARKLLQVI 290
|
|
| sporang_Gsm |
NF038016 |
sporangiospore maturation cell wall hydrolase GsmA; The peptidoglycan-hydrolyzing enzyme GsmA ... |
176-333 |
6.68e-22 |
|
sporangiospore maturation cell wall hydrolase GsmA; The peptidoglycan-hydrolyzing enzyme GsmA occurs in some sporangia-forming members of the Actinobacteria, such as Actinoplanes missouriensis, and is required for proper separation of spores. GsmA proteins have one or two SH3 domains N-terminal to the hydrolase domain.
Pssm-ID: 411609 [Multi-domain] Cd Length: 312 Bit Score: 96.73 E-value: 6.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 176 PTQSPSEFIAELARCAQPIAQANDLYASVMMAQAIVESGWGASTLSkAPNYNLFGIK--GSY----NGQSVYMDTWEYLN 249
Cdd:NF038016 156 PRGTPAQFIAAVAPPAQQSQRATGVPASVTIAQAILESGWGRSGLT-REDHNYFGIKcfGSPgpiaVGCRSYATFECSPT 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 250 GKWLVKKEPFRKYPSYMESFQDNAHVLKTTSfqagvyYYAGAWKSNTSSYRDATA-WLTGrYATDPSYNAKLNNVITAYN 328
Cdd:NF038016 235 GGCFDTTATFRAYASAADSFRDHGRFLSVNS------RYAPAFAYTDDPDQFAREiHKAG-YATDPTYADKLIGLMKQYN 307
|
....*
gi 1633233584 329 LTQYD 333
Cdd:NF038016 308 LYQYD 312
|
|
| Glucosaminidase |
pfam01832 |
Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase; This family includes ... |
191-271 |
1.06e-21 |
|
Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase; This family includes Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase EC:3.2.1.96. As well as the flageller protein J that has been shown to hydrolyse peptidoglycan.
Pssm-ID: 460354 [Multi-domain] Cd Length: 91 Bit Score: 89.94 E-value: 1.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 191 AQPIAQANDLYASVMMAQAIVESGWGASTLSKaPNYNLFGIKGSYNGQsVYMDTWEYlngkwlVKKEPFRKYPSYMESFQ 270
Cdd:pfam01832 4 AIEAAKKYGIPASVLLAQAALESGWGTSRLAK-ESNNLFGIKASWKGK-VAYDTDEV------TVAARFRKYDSVEESIR 75
|
.
gi 1633233584 271 D 271
Cdd:pfam01832 76 D 76
|
|
| flgJ |
PRK05684 |
flagellar assembly peptidoglycan hydrolase FlgJ; |
126-324 |
3.64e-18 |
|
flagellar assembly peptidoglycan hydrolase FlgJ;
Pssm-ID: 235559 [Multi-domain] Cd Length: 312 Bit Score: 85.70 E-value: 3.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 126 SGTTDSSVAEITPVAPSATESEAAPAVTPDDEVKVPEARVASAQTFSALSPTQSPSEFIAELARCAQPIAQANDLYASVM 205
Cdd:PRK05684 98 SPEQSPAPEESAGAVPMKFDLETVQSYQNQALAQLVRKAIPQPPLASDKPLFGSSDDFVARLSPPAQKAAQQSGVPHHLL 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 206 MAQAIVESGWGASTLSKA---PNYNLFGIK--GSYNGQSVYMDTWEYLNGKWLVKKEPFRKYPSYMESFQDNAHVLKTTS 280
Cdd:PRK05684 178 LAQAALESGWGQREIRTAdgsPSHNLFGIKadGSWKGPVTEITTTEYENGVAVKVKAAFRVYDSYLESFNDYVSLLTNNP 257
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1633233584 281 FQAGVyyyagawKSNTSSYRDATAWLTGRYATDPSYNAKLNNVI 324
Cdd:PRK05684 258 RYAAV-------TQAASPEQFARALQDAGYATDPNYARKLVSVI 294
|
|
| flgJ |
PRK12713 |
flagellar rod assembly protein/muramidase FlgJ; Provisional |
182-325 |
3.71e-17 |
|
flagellar rod assembly protein/muramidase FlgJ; Provisional
Pssm-ID: 139173 [Multi-domain] Cd Length: 339 Bit Score: 83.26 E-value: 3.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 182 EFIAELARCAQPIAQANDLYASVMMAQAIVESGWGASTLSK---APNYNLFGIKG--SYNGQSVYMDTWEYLNGKWLVKK 256
Cdd:PRK12713 183 DFVSRMSRAANVAAQQSGVPARLILGQAALESGWGRRELRHedgSTSYNLFGIKAgaSWKGKVVNVMTTEYVDGVAQKLV 262
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1633233584 257 EPFRKYPSYMESFQDNAHVLKTTSFQAGVyyyAGAWKSNTSSYRDATAwltgRYATDPSYNAKLNNVIT 325
Cdd:PRK12713 263 QPFRAYSSYEESFSDYARLIGNSPRYEAV---TQAGNEIEAARRIQEA----GYATDPRYAEKLISIMG 324
|
|
| LysM |
COG1388 |
LysM repeat [Cell wall/membrane/envelope biogenesis]; |
353-543 |
8.67e-17 |
|
LysM repeat [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440998 [Multi-domain] Cd Length: 156 Bit Score: 78.21 E-value: 8.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 353 SNNQSGTNTYYTVKSGDTLNKIAAQYDVSVANLRSWNGISGDLIFVGQKLIVKKGASGNTGGSGNGGSNNNQSGTNTYYT 432
Cdd:COG1388 8 ANAALLAAVLTLLAALLLLAAALAAVALLLLAALAPAGLSLAAALNGEALLLLLPAAAAAAKAALAAAPEAAAAAAARYT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 433 VKSGDTLNKIAAQYGVSVAnlrswngisgdlifvgqklivkkgasgntggsnnggsnnnqsGTNTYYTIKSGDTLNKIAA 512
Cdd:COG1388 88 VKSGDTLSGIARRYGAAAA------------------------------------------PSPVTYTVKKGDTLWSIAR 125
|
170 180 190
....*....|....*....|....*....|.
gi 1633233584 513 QYGVSVANLRSWNGISGDLIFAGQKIIVKKG 543
Cdd:COG1388 126 RYGVSVEELKRWNGLSSDTIRPGQKLKIPAS 156
|
|
| LysM |
pfam01476 |
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ... |
431-473 |
2.54e-15 |
|
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. The structure of this domain is known.
Pssm-ID: 396179 [Multi-domain] Cd Length: 43 Bit Score: 70.12 E-value: 2.54e-15
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1633233584 431 YTVKSGDTLNKIAAQYGVSVANLRSWNGISGDLIFVGQKLIVK 473
Cdd:pfam01476 1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSPNLYVGQKLKIP 43
|
|
| LysM |
pfam01476 |
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ... |
627-668 |
3.60e-15 |
|
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. The structure of this domain is known.
Pssm-ID: 396179 [Multi-domain] Cd Length: 43 Bit Score: 69.73 E-value: 3.60e-15
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1633233584 627 HTVKSGDSLWGLSMQYGISIQKIKQLNGLSGDTIYIGQTLKV 668
Cdd:pfam01476 1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSPNLYVGQKLKI 42
|
|
| flgJ |
PRK12711 |
flagellar assembly peptidoglycan hydrolase FlgJ; |
144-320 |
4.21e-15 |
|
flagellar assembly peptidoglycan hydrolase FlgJ;
Pssm-ID: 237180 [Multi-domain] Cd Length: 392 Bit Score: 77.70 E-value: 4.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 144 TESEAAPAVTPDDevkvpearVASAQTFSALSPTQSPSEFIAELARCAQPIAQANDLYASVMMAQAIVESGWGASTLSKA 223
Cdd:PRK12711 187 AASDAADANAAVN--------ASAASTAAASLGERTPEGFVAKIWTHAQKAARELGVDPRALVAQAALETGWGRRGIGNG 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 224 PN-YNLFGIKGS-YNGQSVYMDTWEYLNGKWLVKKEPFRKYPSYMESFQDNAHVLKTTSfqagvyYYAGAWKSNTSSYRD 301
Cdd:PRK12711 259 GDsNNLFGIKATgWNGDKVTTGTHEYVNGVKTTETADFRAYGSAEESFADYVRLLKNNS------RYQQALQAGTDIKGF 332
|
170
....*....|....*....
gi 1633233584 302 ATAWLTGRYATDPSYNAKL 320
Cdd:PRK12711 333 ARGLQQAGYATDPGYAAKI 351
|
|
| LysM |
COG1388 |
LysM repeat [Cell wall/membrane/envelope biogenesis]; |
429-609 |
6.99e-15 |
|
LysM repeat [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440998 [Multi-domain] Cd Length: 156 Bit Score: 72.43 E-value: 6.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 429 TYYTVKSGDTLNKIAAQYGVSVANLRSWNGISGDLIFVGQKLIVKKGASGNTGGSNNGGSNNNQSGTNTYYTIKSGDTLN 508
Cdd:COG1388 16 VLTLLAALLLLAAALAAVALLLLAALAPAGLSLAAALNGEALLLLLPAAAAAAKAALAAAPEAAAAAAARYTVKSGDTLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 509 KIAAQYGVSVAnlrswngisgdlifagqkiivkkgansgstntnkptnnggGATTSYTIKSGDTLNKISAQFGVSVANLR 588
Cdd:COG1388 96 GIARRYGAAAA----------------------------------------PSPVTYTVKKGDTLWSIARRYGVSVEELK 135
|
170 180
....*....|....*....|.
gi 1633233584 589 SWNGIKGDLIFAGQTIIVKKG 609
Cdd:COG1388 136 RWNGLSSDTIRPGQKLKIPAS 156
|
|
| LysM |
pfam01476 |
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ... |
363-405 |
7.13e-15 |
|
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. The structure of this domain is known.
Pssm-ID: 396179 [Multi-domain] Cd Length: 43 Bit Score: 68.58 E-value: 7.13e-15
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1633233584 363 YTVKSGDTLNKIAAQYDVSVANLRSWNGISGDLIFVGQKLIVK 405
Cdd:pfam01476 1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSPNLYVGQKLKIP 43
|
|
| LysM |
COG1388 |
LysM repeat [Cell wall/membrane/envelope biogenesis]; |
602-668 |
7.92e-15 |
|
LysM repeat [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440998 [Multi-domain] Cd Length: 156 Bit Score: 72.43 E-value: 7.92e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 602 QTIIVKKGASAGGNASSTNSASG---KRHTVKSGDSLWGLSMQYGISIQKIKQLNGLSGDTIYIGQTLKV 668
Cdd:COG1388 84 ARYTVKSGDTLSGIARRYGAAAApspVTYTVKKGDTLWSIARRYGVSVEELKRWNGLSSDTIRPGQKLKI 153
|
|
| flgJ |
PRK12709 |
flagellar rod assembly protein/muramidase FlgJ; Provisional |
172-320 |
9.79e-15 |
|
flagellar rod assembly protein/muramidase FlgJ; Provisional
Pssm-ID: 237179 [Multi-domain] Cd Length: 320 Bit Score: 75.73 E-value: 9.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 172 SALSP-------TQSPSEFIAELARCAQPIAQANDLYASVMMAQAIVESGWGASTLSKA---PNYNLFGIKGS--YNGQS 239
Cdd:PRK12709 158 SALTPplkgnggSPDADAFVDKLAAPAQAASAATGIPARFIVGQAALESGWGKREIRGAdgsTSYNVFGIKATkgWTGRT 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 240 VYMDTWEYLNGKWLVKKEPFRKYPSYMESFQDNAHVLKTTSFQAGVyyyagawksnTSSYRDATAWLTGR----YATDPS 315
Cdd:PRK12709 238 VSAVTTEYVNGKPRRVVAKFRAYDSYEHAMTDYANLLKNNPRYAGV----------LNASRSVEGFAHGMqkagYATDPH 307
|
....*
gi 1633233584 316 YNAKL 320
Cdd:PRK12709 308 YAKKL 312
|
|
| mltD |
PRK10783 |
membrane-bound lytic murein transglycosylase D; Provisional |
354-470 |
2.04e-14 |
|
membrane-bound lytic murein transglycosylase D; Provisional
Pssm-ID: 182727 [Multi-domain] Cd Length: 456 Bit Score: 75.93 E-value: 2.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 354 NNQSGTNTYYTVKSGDTLNKIAAQYDVSVANLRSWNGISGDLIFVGQKLIVKKGASGNTGGSGNGGsnnnqsgtnTYYTV 433
Cdd:PRK10783 337 DNTPLNSRSYKVRSGDTLSGIASRLNVSTKDLQQWNNLRGSKLKVGQTLTIGAGSSAQRLANNSDS---------ITYRV 407
|
90 100 110
....*....|....*....|....*....|....*..
gi 1633233584 434 KSGDTLNKIAAQYGVSVANLRSWNGISGDLIFVGQKL 470
Cdd:PRK10783 408 RKGDSLSSIAKRHGVNIKDVMRWNSDTAKNLQPGDKL 444
|
|
| LysM |
pfam01476 |
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ... |
499-541 |
2.54e-14 |
|
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. The structure of this domain is known.
Pssm-ID: 396179 [Multi-domain] Cd Length: 43 Bit Score: 67.04 E-value: 2.54e-14
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1633233584 499 YTIKSGDTLNKIAAQYGVSVANLRSWNGISGDLIFAGQKIIVK 541
Cdd:pfam01476 1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSPNLYVGQKLKIP 43
|
|
| LysM |
cd00118 |
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ... |
429-472 |
3.83e-14 |
|
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.
Pssm-ID: 212030 [Multi-domain] Cd Length: 45 Bit Score: 66.74 E-value: 3.83e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1633233584 429 TYYTVKSGDTLNKIAAQYGVSVANLRSWNGI-SGDLIFVGQKLIV 472
Cdd:cd00118 1 KTYTVKPGDTLWSIAKKYGVTVEELAAANPLiNPDCIYPGQKLKI 45
|
|
| LysM |
smart00257 |
Lysin motif; |
430-472 |
8.24e-14 |
|
Lysin motif;
Pssm-ID: 197609 [Multi-domain] Cd Length: 44 Bit Score: 65.93 E-value: 8.24e-14
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1633233584 430 YYTVKSGDTLNKIAAQYGVSVANLRSWNGISG-DLIFVGQKLIV 472
Cdd:smart00257 1 TYTVKKGDTLSSIARRYGISVSDLLELNNILDpDNLQVGQKLKI 44
|
|
| mltD |
PRK10783 |
membrane-bound lytic murein transglycosylase D; Provisional |
506-666 |
9.42e-14 |
|
membrane-bound lytic murein transglycosylase D; Provisional
Pssm-ID: 182727 [Multi-domain] Cd Length: 456 Bit Score: 74.00 E-value: 9.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 506 TLNKIAAQYGVSVANLRSWN-GISGDLIFAG--QKIIV-KKGAN-------SGSTNTNKPT---NNGGGATTSYTIKSGD 571
Cdd:PRK10783 273 ELAQAAEMAGMSLTKLKTFNaGYKRSTTAPSgpHYIMVpKKHADqlreslaSGEIAAVQSTlvaDNTPLNSRSYKVRSGD 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 572 TLNKISAQFGVSVANLRSWNGIKGDLIFAGQTIIVKKGASAGGNASSTNSASGKrhtVKSGDSLWGLSMQYGISIQKIKQ 651
Cdd:PRK10783 353 TLSGIASRLNVSTKDLQQWNNLRGSKLKVGQTLTIGAGSSAQRLANNSDSITYR---VRKGDSLSSIAKRHGVNIKDVMR 429
|
170
....*....|....*
gi 1633233584 652 LNGLSGDTIYIGQTL 666
Cdd:PRK10783 430 WNSDTAKNLQPGDKL 444
|
|
| flgJ |
PRK12712 |
flagellar rod assembly protein/muramidase FlgJ; Provisional |
176-320 |
9.60e-14 |
|
flagellar rod assembly protein/muramidase FlgJ; Provisional
Pssm-ID: 139172 [Multi-domain] Cd Length: 344 Bit Score: 73.12 E-value: 9.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 176 PTQSP---SEFIAELARCAQPIAQANDLYASVMMAQAIVESGWGASTLSKA---PNYNLFGIKG--SYNGQSVYMDTWEY 247
Cdd:PRK12712 190 PDDAPahvSAFVARMAGPAEAASRASGVPARLIVGQAALESGWGRREITHAdgsTTFNVFGIKAgaNWKGRVAEVTTTEY 269
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1633233584 248 LNGKWLVKKEPFRKYPSYMESFQDNAHVLKTTSFQAGVYYYAGAWKSNTSSYRDAtawltgrYATDPSYNAKL 320
Cdd:PRK12712 270 VDGQPQKVRARFRAYGSYDEACADYARLLTSNPRYAGVVSAASADEAAHGLQRAG-------YATDPAYGHKL 335
|
|
| LysM |
cd00118 |
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ... |
361-404 |
1.43e-13 |
|
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.
Pssm-ID: 212030 [Multi-domain] Cd Length: 45 Bit Score: 65.20 E-value: 1.43e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1633233584 361 TYYTVKSGDTLNKIAAQYDVSVANLRSWNGI-SGDLIFVGQKLIV 404
Cdd:cd00118 1 KTYTVKPGDTLWSIAKKYGVTVEELAAANPLiNPDCIYPGQKLKI 45
|
|
| mltD |
PRK10783 |
membrane-bound lytic murein transglycosylase D; Provisional |
431-538 |
1.50e-13 |
|
membrane-bound lytic murein transglycosylase D; Provisional
Pssm-ID: 182727 [Multi-domain] Cd Length: 456 Bit Score: 73.23 E-value: 1.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 431 YTVKSGDTLNKIAAQYGVSVANLRSWNGISGDLIFVGQKLIVKKGASGNTGGSNNGGsnnnqsgtnTYYTIKSGDTLNKI 510
Cdd:PRK10783 346 YKVRSGDTLSGIASRLNVSTKDLQQWNNLRGSKLKVGQTLTIGAGSSAQRLANNSDS---------ITYRVRKGDSLSSI 416
|
90 100
....*....|....*....|....*...
gi 1633233584 511 AAQYGVSVANLRSWNGISGDLIFAGQKI 538
Cdd:PRK10783 417 AKRHGVNIKDVMRWNSDTAKNLQPGDKL 444
|
|
| LysM |
pfam01476 |
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ... |
565-607 |
1.91e-13 |
|
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. The structure of this domain is known.
Pssm-ID: 396179 [Multi-domain] Cd Length: 43 Bit Score: 64.72 E-value: 1.91e-13
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1633233584 565 YTIKSGDTLNKISAQFGVSVANLRSWNGIKGDLIFAGQTIIVK 607
Cdd:pfam01476 1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSPNLYVGQKLKIP 43
|
|
| LysM |
smart00257 |
Lysin motif; |
362-404 |
3.26e-13 |
|
Lysin motif;
Pssm-ID: 197609 [Multi-domain] Cd Length: 44 Bit Score: 64.00 E-value: 3.26e-13
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1633233584 362 YYTVKSGDTLNKIAAQYDVSVANLRSWNGISG-DLIFVGQKLIV 404
Cdd:smart00257 1 TYTVKKGDTLSSIARRYGISVSDLLELNNILDpDNLQVGQKLKI 44
|
|
| LysM |
smart00257 |
Lysin motif; |
498-540 |
4.97e-13 |
|
Lysin motif;
Pssm-ID: 197609 [Multi-domain] Cd Length: 44 Bit Score: 63.62 E-value: 4.97e-13
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1633233584 498 YYTIKSGDTLNKIAAQYGVSVANLRSWNGISG-DLIFAGQKIIV 540
Cdd:smart00257 1 TYTVKKGDTLSSIARRYGISVSDLLELNNILDpDNLQVGQKLKI 44
|
|
| LysM |
cd00118 |
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ... |
497-540 |
5.50e-13 |
|
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.
Pssm-ID: 212030 [Multi-domain] Cd Length: 45 Bit Score: 63.66 E-value: 5.50e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1633233584 497 TYYTIKSGDTLNKIAAQYGVSVANLRSWNGI-SGDLIFAGQKIIV 540
Cdd:cd00118 1 KTYTVKPGDTLWSIAKKYGVTVEELAAANPLiNPDCIYPGQKLKI 45
|
|
| mltD |
PRK10783 |
membrane-bound lytic murein transglycosylase D; Provisional |
499-597 |
9.34e-13 |
|
membrane-bound lytic murein transglycosylase D; Provisional
Pssm-ID: 182727 [Multi-domain] Cd Length: 456 Bit Score: 70.92 E-value: 9.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 499 YTIKSGDTLNKIAAQYGVSVANLRSWNGISGDLIFAGQKIIVKKGANSGSTNTNkptnnggGATTSYTIKSGDTLNKISA 578
Cdd:PRK10783 346 YKVRSGDTLSGIASRLNVSTKDLQQWNNLRGSKLKVGQTLTIGAGSSAQRLANN-------SDSITYRVRKGDSLSSIAK 418
|
90 100
....*....|....*....|
gi 1633233584 579 QFGVSVANLRSWN-GIKGDL 597
Cdd:PRK10783 419 RHGVNIKDVMRWNsDTAKNL 438
|
|
| LysM |
cd00118 |
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ... |
625-668 |
2.04e-12 |
|
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.
Pssm-ID: 212030 [Multi-domain] Cd Length: 45 Bit Score: 61.73 E-value: 2.04e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1633233584 625 KRHTVKSGDSLWGLSMQYGISIQKIKQLNGL-SGDTIYIGQTLKV 668
Cdd:cd00118 1 KTYTVKPGDTLWSIAKKYGVTVEELAAANPLiNPDCIYPGQKLKI 45
|
|
| LysM |
smart00257 |
Lysin motif; |
627-668 |
2.46e-12 |
|
Lysin motif;
Pssm-ID: 197609 [Multi-domain] Cd Length: 44 Bit Score: 61.69 E-value: 2.46e-12
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1633233584 627 HTVKSGDSLWGLSMQYGISIQKIKQLNG-LSGDTIYIGQTLKV 668
Cdd:smart00257 2 YTVKKGDTLSSIARRYGISVSDLLELNNiLDPDNLQVGQKLKI 44
|
|
| LysM |
smart00257 |
Lysin motif; |
565-606 |
1.15e-11 |
|
Lysin motif;
Pssm-ID: 197609 [Multi-domain] Cd Length: 44 Bit Score: 59.77 E-value: 1.15e-11
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1633233584 565 YTIKSGDTLNKISAQFGVSVANLRSWNGIKG-DLIFAGQTIIV 606
Cdd:smart00257 2 YTVKKGDTLSSIARRYGISVSDLLELNNILDpDNLQVGQKLKI 44
|
|
| LysM |
cd00118 |
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ... |
563-606 |
2.46e-11 |
|
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.
Pssm-ID: 212030 [Multi-domain] Cd Length: 45 Bit Score: 58.65 E-value: 2.46e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1633233584 563 TSYTIKSGDTLNKISAQFGVSVANLRSWNGIKG-DLIFAGQTIIV 606
Cdd:cd00118 1 KTYTVKPGDTLWSIAKKYGVTVEELAAANPLINpDCIYPGQKLKI 45
|
|
| PRK13914 |
PRK13914 |
invasion associated endopeptidase; |
433-668 |
5.25e-09 |
|
invasion associated endopeptidase;
Pssm-ID: 237555 [Multi-domain] Cd Length: 481 Bit Score: 59.04 E-value: 5.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 433 VKSGDTLNKIAAQYGVSVANLRSWNGISGDLIFVGQKLIVKKGASGNTGGSNNGGsnnnqsgtnTYYTIKSGDTLN---- 508
Cdd:PRK13914 32 VEAGDTLWGIAQSKGTTVDAIKKANNLTTDKIVPGQKLQVNEVAAAEKTEKSVSA---------TWLNVRSGAGVDnsii 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 509 ---KIAAQYGVSVANLRSWNGIS---GDLIFAGQKIIVKKGANSGSTNTNKPTNNgggATTSYTIKSGDTLNKISAQFgv 582
Cdd:PRK13914 103 tsiKGGTKVTVETTESNGWHKITyndGKTGFVNGKYLTDKVTSTPVAPTQEVKKE---TTTQQAAPAAETKTEVKQTT-- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 583 svanlrswngikgdlifAGQTIIVKKGASAGGNASSTNSASgkrHTVKSGDSLWGLSMQYGISIQKIKQLNGLSGDTIYI 662
Cdd:PRK13914 178 -----------------QATTPAPKVAETKETPVVDQNATT---HAVKSGDTIWALSVKYGVSVQDIMSWNNLSSSSIYV 237
|
....*.
gi 1633233584 663 GQTLKV 668
Cdd:PRK13914 238 GQKLAI 243
|
|
| PRK13914 |
PRK13914 |
invasion associated endopeptidase; |
429-661 |
9.91e-09 |
|
invasion associated endopeptidase;
Pssm-ID: 237555 [Multi-domain] Cd Length: 481 Bit Score: 58.27 E-value: 9.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 429 TYYTVKSGDTLNKIAAQYGVSVANLRSWNGISGDLIFVGQKLIVKKGASGNTGGSNNGGSNNNQ-----------SGTNT 497
Cdd:PRK13914 200 TTHAVKSGDTIWALSVKYGVSVQDIMSWNNLSSSSIYVGQKLAIKQTANTATPKAEVKTEAPAAekqaapvvkenTNTNT 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 498 YYTIKSGDTLNKIAAQYGVSVAnlrSWNGISGDLIFAGQKIIVKKGANSGSTNTNKPTNNGGGATTSYTIKSGDTlnkiS 577
Cdd:PRK13914 280 ATTEKKETTTQQQTAPKAPTEA---AKPAPAPSTNTNANKTNTNTNTNTNNTNTSTPSKNTNTNTNSNTNTNSNT----N 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 578 AQFGVSVANLRSwngiKGDLIFAGQTIIVKKGASAGGNASSTNSASGKRHTV--KSGDSLWGLSMQYGISIQKIKQLNGL 655
Cdd:PRK13914 353 ANQGSSNNNSNS----SASAIIAEAQKHLGKAYSWGGNGPTTFDCSGYTKYVfaKAGISLPRTSGAQYASTTRISESQAK 428
|
....*.
gi 1633233584 656 SGDTIY 661
Cdd:PRK13914 429 PGDLVF 434
|
|
| mltD |
PRK10783 |
membrane-bound lytic murein transglycosylase D; Provisional |
572-669 |
1.34e-07 |
|
membrane-bound lytic murein transglycosylase D; Provisional
Pssm-ID: 182727 [Multi-domain] Cd Length: 456 Bit Score: 54.36 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 572 TLNKISAQFGVSVANLRSWN-GIKGDLIFAG--QTIIVKKG-------ASAGGNASST--------NSASGKRHTVKSGD 633
Cdd:PRK10783 273 ELAQAAEMAGMSLTKLKTFNaGYKRSTTAPSgpHYIMVPKKhadqlreSLASGEIAAVqstlvadnTPLNSRSYKVRSGD 352
|
90 100 110
....*....|....*....|....*....|....*.
gi 1633233584 634 SLWGLSMQYGISIQKIKQLNGLSGDTIYIGQTLKVG 669
Cdd:PRK10783 353 TLSGIASRLNVSTKDLQQWNNLRGSKLKVGQTLTIG 388
|
|
| PRK13914 |
PRK13914 |
invasion associated endopeptidase; |
365-548 |
1.71e-07 |
|
invasion associated endopeptidase;
Pssm-ID: 237555 [Multi-domain] Cd Length: 481 Bit Score: 54.04 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 365 VKSGDTLNKIAAQYDVSVANLRSWNGISGDLIFVGQKLIVKKGASGNTGGSGNGGsnnnqsgtnTYYTVKSGDTLN---- 440
Cdd:PRK13914 32 VEAGDTLWGIAQSKGTTVDAIKKANNLTTDKIVPGQKLQVNEVAAAEKTEKSVSA---------TWLNVRSGAGVDnsii 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 441 ---KIAAQYGVSVANLRSWNGIS---GDLIFVGQKLI--------------VKKGASGNTGGSNNGGSNNNQSGTN---- 496
Cdd:PRK13914 103 tsiKGGTKVTVETTESNGWHKITyndGKTGFVNGKYLtdkvtstpvaptqeVKKETTTQQAAPAAETKTEVKQTTQattp 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1633233584 497 -----------------TYYTIKSGDTLNKIAAQYGVSVANLRSWNGISGDLIFAGQKIIVKKGANSGS 548
Cdd:PRK13914 183 apkvaetketpvvdqnaTTHAVKSGDTIWALSVKYGVSVQDIMSWNNLSSSSIYVGQKLAIKQTANTAT 251
|
|
| XkdP |
COG1652 |
Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion ... |
609-668 |
1.18e-06 |
|
Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion transport and metabolism];
Pssm-ID: 441258 [Multi-domain] Cd Length: 163 Bit Score: 48.85 E-value: 1.18e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1633233584 609 GASAGGNASSTNSASGKRHTVKSGDSLWGLSMQY---GISIQKIKQLNGL---SGDTIYIGQTLKV 668
Cdd:COG1652 94 AEEAAAPSAELAPDAPKTYTVKPGDTLWGIAKRFygdPARWPEIAEANRDqikNPDLIYPGQVLRI 159
|
|
| flgJ |
PRK12710 |
flagellar rod assembly protein/muramidase FlgJ; Provisional |
182-331 |
1.47e-06 |
|
flagellar rod assembly protein/muramidase FlgJ; Provisional
Pssm-ID: 139170 [Multi-domain] Cd Length: 291 Bit Score: 50.56 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 182 EFIAELARCAQPIAQANDLYASVMMAQAIVESGWGASTLSKA---PNYNLFGIK-GSYNG-QSVYMDTWEYLNGKWLVKK 256
Cdd:PRK12710 132 DFVKSVWPTAKQAASLIGLDPKLLVAQAALETGWGKFVTRDAdgsSSNNLFNIKtGSHSEvESIQVKTTEYIADTPIKIN 211
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1633233584 257 EPFRKYPSYMESFQDNAHVLKTTSfqagVYYYAGAWKSNTSSYrdATAWLTGRYATDPSYNAKLNNVITAYNLTQ 331
Cdd:PRK12710 212 ASFRKYPSIEHSFHDYVSLIKGSE----RYQMALANAENPEIY--VSELNKAGYATDPNYSNKILSIYHGDELNQ 280
|
|
| PRK13914 |
PRK13914 |
invasion associated endopeptidase; |
361-408 |
2.03e-06 |
|
invasion associated endopeptidase;
Pssm-ID: 237555 [Multi-domain] Cd Length: 481 Bit Score: 50.96 E-value: 2.03e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1633233584 361 TYYTVKSGDTLNKIAAQYDVSVANLRSWNGISGDLIFVGQKLIVKKGA 408
Cdd:PRK13914 200 TTHAVKSGDTIWALSVKYGVSVQDIMSWNNLSSSSIYVGQKLAIKQTA 247
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
43-224 |
1.13e-05 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 48.88 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 43 PVAllPVTAEATEEQPTNAEVAQAPTTETGLVETPTTETTPGTTEQPTTDSSTTTESTTESSKETPT-----------TP 111
Cdd:PRK10811 846 PVV--RPQDVQVEEQREAEEVQVQPVVAEVPVAAAVEPVVSAPVVEAVAEVVEEPVVVAEPQPEEVVvvetthpeviaAP 923
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 112 STEQP--TADSTTPVESgttdSSVAEITPVAPSATESEAAPAVTPDDEVKVPEARVASAqtfsalspTQSPSEFIAELAR 189
Cdd:PRK10811 924 VTEQPqvITESDVAVAQ----EVAEHAEPVVEPQDETADIEEAAETAEVVVAEPEVVAQ--------PAAPVVAEVAAEV 991
|
170 180 190
....*....|....*....|....*....|....*
gi 1633233584 190 CAQPIAQANDLYASVmmAQAIVESGWGASTLSKAP 224
Cdd:PRK10811 992 ETVTAVEPEVAPAQV--PEATVEHNHATAPMTRAP 1024
|
|
| XkdP |
COG1652 |
Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion ... |
511-606 |
1.29e-03 |
|
Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion transport and metabolism];
Pssm-ID: 441258 [Multi-domain] Cd Length: 163 Bit Score: 39.99 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 511 AAQYGVSVANLRSWNGISGDLIFAGQKIIVKKGANSGSTNTNKPTNNGGGATTSYTIKSGDTLNKISAQFGVSVANLRSW 590
Cdd:COG1652 58 GLAAAVAAAAAAAVLIAPVAVMRAGAAAKLSPAVTVAEEAAAPSAELAPDAPKTYTVKPGDTLWGIAKRFYGDPARWPEI 137
|
90 100
....*....|....*....|..
gi 1633233584 591 -----NGIKG-DLIFAGQTIIV 606
Cdd:COG1652 138 aeanrDQIKNpDLIYPGQVLRI 159
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
108-191 |
3.05e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 41.08 E-value: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 108 PTTPSTEQPTADSTTPVESGTTDSSVAEITPVAPSATESEAAPAVTPDDEVKVPEARVASAQTFSALSPTQSPSEFIAEL 187
Cdd:PHA03247 2733 PALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVL 2812
|
....
gi 1633233584 188 ARCA 191
Cdd:PHA03247 2813 APAA 2816
|
|
| XkdP |
COG1652 |
Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion ... |
429-472 |
3.15e-03 |
|
Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion transport and metabolism];
Pssm-ID: 441258 [Multi-domain] Cd Length: 163 Bit Score: 38.83 E-value: 3.15e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1633233584 429 TYYTVKSGDTLNKIAAQ-YGvsvaNLRSWNGI---------SGDLIFVGQKLIV 472
Cdd:COG1652 110 KTYTVKPGDTLWGIAKRfYG----DPARWPEIaeanrdqikNPDLIYPGQVLRI 159
|
|
| spore_safA |
TIGR02899 |
spore coat assembly protein SafA; SafA (YrbB) (SafA) of Bacillus subtilis is a protein found ... |
501-538 |
3.83e-03 |
|
spore coat assembly protein SafA; SafA (YrbB) (SafA) of Bacillus subtilis is a protein found at the interface of the spore cortex and spore coat, and is dependent on SpoVID for its localization. This model is based on the N-terminal LysM (lysin motif) domain (see pfamAM model pfam01476) of SafA and, from several other spore-forming species, the protein with the most similar N-terminal region. However, this set of proteins differs greatly in C-terminal of the LysM domaim; blocks of 12-residue and 13-residue repeats are found in the Bacillus cereus group, tandem LysM domains in Thermoanaerobacter tengcongensis MB4, etc. in which one of which is found in most examples of endospore-forming bacteria. [Cellular processes, Sporulation and germination]
Pssm-ID: 131945 [Multi-domain] Cd Length: 44 Bit Score: 35.54 E-value: 3.83e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1633233584 501 IKSGDTLNKIAAQYGVSVANLRSWNG-ISG-DLIFAGQKI 538
Cdd:TIGR02899 1 VQKGDTLWKIAKKYGVDFDELIQANPqLSNpNLIYPGMKI 40
|
|
| PRK11198 |
PRK11198 |
LysM domain/BON superfamily protein; Provisional |
429-470 |
5.94e-03 |
|
LysM domain/BON superfamily protein; Provisional
Pssm-ID: 236880 [Multi-domain] Cd Length: 147 Bit Score: 37.59 E-value: 5.94e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1633233584 429 TYYTVKSGDTLNKIA-AQYGvsvaNLRSWNGI---------SGDLIFVGQKL 470
Cdd:PRK11198 96 QFYTVKSGDTLSAIAkKVYG----NANKYNKIfeankpmlkSPDKIYPGQVL 143
|
|
| spore_safA |
TIGR02899 |
spore coat assembly protein SafA; SafA (YrbB) (SafA) of Bacillus subtilis is a protein found ... |
433-470 |
6.08e-03 |
|
spore coat assembly protein SafA; SafA (YrbB) (SafA) of Bacillus subtilis is a protein found at the interface of the spore cortex and spore coat, and is dependent on SpoVID for its localization. This model is based on the N-terminal LysM (lysin motif) domain (see pfamAM model pfam01476) of SafA and, from several other spore-forming species, the protein with the most similar N-terminal region. However, this set of proteins differs greatly in C-terminal of the LysM domaim; blocks of 12-residue and 13-residue repeats are found in the Bacillus cereus group, tandem LysM domains in Thermoanaerobacter tengcongensis MB4, etc. in which one of which is found in most examples of endospore-forming bacteria. [Cellular processes, Sporulation and germination]
Pssm-ID: 131945 [Multi-domain] Cd Length: 44 Bit Score: 35.16 E-value: 6.08e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1633233584 433 VKSGDTLNKIAAQYGVSVANLRSWNG-ISG-DLIFVGQKL 470
Cdd:TIGR02899 1 VQKGDTLWKIAKKYGVDFDELIQANPqLSNpNLIYPGMKI 40
|
|
| PRK13914 |
PRK13914 |
invasion associated endopeptidase; |
603-668 |
6.54e-03 |
|
invasion associated endopeptidase;
Pssm-ID: 237555 [Multi-domain] Cd Length: 481 Bit Score: 39.40 E-value: 6.54e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1633233584 603 TIIVKKGASAGGNASSTnSASGKRHTVKSGDSLWGLSMQYGISIQKIKQLNGLSGDTIYIGQTLKV 668
Cdd:PRK13914 7 TIAATAGIAVTAFAAPT-IASASTVVVEAGDTLWGIAQSKGTTVDAIKKANNLTTDKIVPGQKLQV 71
|
|
| XkdP |
COG1652 |
Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion ... |
353-404 |
6.80e-03 |
|
Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion transport and metabolism];
Pssm-ID: 441258 [Multi-domain] Cd Length: 163 Bit Score: 38.06 E-value: 6.80e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1633233584 353 SNNQSGTNTYYTVKSGDTLNKIAAQYDVSVANLRSW-----NGISG-DLIFVGQKLIV 404
Cdd:COG1652 102 AELAPDAPKTYTVKPGDTLWGIAKRFYGDPARWPEIaeanrDQIKNpDLIYPGQVLRI 159
|
|
| PRK10856 |
PRK10856 |
cytoskeleton protein RodZ; |
110-206 |
9.57e-03 |
|
cytoskeleton protein RodZ;
Pssm-ID: 236776 [Multi-domain] Cd Length: 331 Bit Score: 38.85 E-value: 9.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633233584 110 TPSTEQPTADSTTPVESGTTDSSVAEITPVAPSATESEAAPAVTPDDEVKVPEARVASAQTFSALSPTQSPsefiAELAR 189
Cdd:PRK10856 168 TTTDPATTPAPAAPVDTTPTNSQTPAVATAPAPAVDPQQNAVVAPSQANVDTAATPAPAAPATPDGAAPLP----TDQAG 243
|
90
....*....|....*..
gi 1633233584 190 CAQPIAQANDLyasVMM 206
Cdd:PRK10856 244 VSTPAADPNAL---VMN 257
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