|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11649 |
PRK11649 |
putative peptidase; Provisional |
4-410 |
8.58e-95 |
|
putative peptidase; Provisional
Pssm-ID: 236946 [Multi-domain] Cd Length: 439 Bit Score: 291.95 E-value: 8.58e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808955 4 KIFSSPFAELSPVKKVaILGLPLIAAIGVAL------QSSQSNLTKTIELDLPDstvIESILSPSSVTVIEPP------- 70
Cdd:PRK11649 6 RSIALAFNNLPRPHRV-MLGSLTVLTLAVAVwrpyvyHPESAPIVKTIELEKSE---IRSLLPEASEPIDQAAqedeaip 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808955 71 -------------TFEYQIQSGDNLSSIFTQLGFSyksmMSvmetDLNFLA-----LDTLRPGNTLRfWRDEATSDLSKM 132
Cdd:PRK11649 82 qdelddkiageagVHEYVVSTGDTLSSILNQYGID----MS----DISQLAaqdkeLRNLKIGQQLS-WTLTADGDLQRL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808955 133 ELQFSVADKVVYRLLDDGsYEFEDISIPGEWKQKPLVGDIQGSFSMSANKVGLNSLEIDHIVTLLKDKLNFsRDLRAGDQ 212
Cdd:PRK11649 153 TWEVSRRETRTYDRTGNG-FKETSEMQQGEWVNSVLKGTVGGSFVASAKNAGLTSAEISAVIKALQWQMDF-RKLKKGDE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808955 213 FEVLQKAQYVDGvatgKRE---IEAIKIMNRNRVVSAYLHTDGQYYDANGDSLQRAFQRYPVSSGWRQSSQFNPKRLHPV 289
Cdd:PRK11649 231 FSVLMSREMLDG----KSEqsqLLGVRLRSGGKDYYAIRAEDGKFYDRNGSGLAKGFLRFPTAKQFRISSNFNPRRLNPV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808955 290 TGRISPHNGTDFATPVGTPVQATGDGKVIMTRKHPYAGNYVVIQHGSTYKTRYLHLSKILVRKGQTVSRGQRIGLSGKTG 369
Cdd:PRK11649 307 TGRVAPHRGVDFAMPVGTPVLAVGDGEVVVAKRSGAAGNYVAIRHGRQYTTRYMHLRKLLVKPGQKVKRGDRIALSGNTG 386
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 880808955 370 RVTGAHLHYELIERGRPVNAMTANIPMADSVPKKEKATFVA 410
Cdd:PRK11649 387 RSTGPHLHYEVWINQQAVNPLTAKLPRTEGLTGKDRREYLA 427
|
|
| NlpD |
COG0739 |
Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell ... |
204-391 |
1.05e-53 |
|
Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440502 [Multi-domain] Cd Length: 196 Bit Score: 177.47 E-value: 1.05e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808955 204 SRDLRAGDQFEVLQKAQYVDGVATGKREIEAIKIMNRNRVVSAYLHTDGQYYDANGDSLQRAFQRYPVSSgwRQSSQFNP 283
Cdd:COG0739 8 AAALLALALLASAAGAAAAVAAAAAAAAAAAALAAAALAAAVSAAASAAAAAAAAAAAIALGSGAWPVKG--RITSGFGY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808955 284 kRLHPVTGRISPHNGTDFATPVGTPVQATGDGKVIMTRKHPYAGNYVVIQHGSTYKTRYLHLSKILVRKGQTVSRGQRIG 363
Cdd:COG0739 86 -RRHPVTGRRRFHKGIDIAAPTGTPVYAAADGTVVFAGWNGGYGNLVIIDHGNGYTTLYAHLSSILVKVGQRVKAGQVIG 164
|
170 180
....*....|....*....|....*...
gi 880808955 364 LSGKTGRVTGAHLHYELIERGRPVNAMT 391
Cdd:COG0739 165 YVGNTGRSTGPHLHFEVRVNGKPVDPLP 192
|
|
| Peptidase_M23 |
pfam01551 |
Peptidase family M23; Members of this family are zinc metallopeptidases with a range of ... |
294-388 |
4.55e-44 |
|
Peptidase family M23; Members of this family are zinc metallopeptidases with a range of specificities. The peptidase family M23 is included in this family, these are Gly-Gly endopeptidases. Peptidase family M23 are also endopeptidases. This family also includes some bacterial lipoproteins such as Swiss:P33648 for which no proteolytic activity has been demonstrated. This family also includes leukocyte cell-derived chemotaxin 2 (LECT2) proteins. LECT2 is a liver-specific protein which is thought to be linked to hepatocyte growth although the exact function of this protein is unknown.
Pssm-ID: 460250 [Multi-domain] Cd Length: 96 Bit Score: 148.85 E-value: 4.55e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808955 294 SPHNGTDFATPVGTPVQATGDGKVIMTRKHPYAGNYVVIQHGSTYKTRYLHLSKILVRKGQTVSRGQRIGLSGKTGRVTG 373
Cdd:pfam01551 1 RFHKGIDIAAPTGTPVYAAADGVVVFAGWLGGYGNLVIIDHGNGYSTLYAHLSSILVKVGQRVKAGQVIGTVGSTGRSTG 80
|
90
....*....|....*
gi 880808955 374 AHLHYELIERGRPVN 388
Cdd:pfam01551 81 PHLHFEIRKNGKPVD 95
|
|
| M23_peptidase |
cd12797 |
M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; ... |
296-380 |
1.19e-40 |
|
M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; This model describes the metallopeptidase M23 family, which includes beta-lytic metallopeptidase and lysostaphin. Members of this family are zinc endopeptidases that lyse bacterial cell wall peptidoglycans; they cleave either the N-acylmuramoyl-Ala bond between the cell wall peptidoglycan and the cross-linking peptide (e.g. beta-lytic endopeptidase) or a bond within the cross-linking peptide (e.g. stapholysin, and lysostaphin). Beta-lytic metallopeptidase, formerly known as beta-lytic protease, has a preference for cleavage of Gly-X bonds and favors hydrophobic or apolar residues on either side. It inhibits growth of sensitive organisms and may potentially serve as an antimicrobial agent. Lysostaphin, produced by Staphylococcus genus, cleaves pentaglycine cross-bridges of cell wall peptidoglycan, acting as autolysins to maintain cell wall metabolism or as toxins and weapons against competing strains. Staphylolysin (also known as LasA) is implicated in a range of processes related to Pseudomonas virulence, including stimulating shedding of the ectodomain of cell surface heparan sulphate proteoglycan syndecan-1, and elastin degradation in connective tissue. Its active site is less constricted and contains a five-coordinate zinc ion with trigonal bipyramidal geometry and two metal-bound water molecules, possibly contributing to its activity against a wider range of substrates than those used by related lytic enzymes, consistent with its multiple roles in Pseudomonas virulence. The family includes members that do not appear to have the conserved zinc-binding site and might be lipoproteins lacking proteolytic activity.
Pssm-ID: 410984 [Multi-domain] Cd Length: 85 Bit Score: 139.65 E-value: 1.19e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808955 296 HNGTDFATPVGTPVQATGDGKVIMTRKHPYAGNYVVIQHGSTYKTRYLHLSKILVRKGQTVSRGQRIGLSGKTGRVTGAH 375
Cdd:cd12797 1 HNGIDIAAPEGTPVYAAADGTVVFAGWDGGYGNYVIIDHGNGYYTLYAHLSSILVKVGQRVKKGQVIGTVGNTGRSTGPH 80
|
....*
gi 880808955 376 LHYEL 380
Cdd:cd12797 81 LHFEI 85
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11649 |
PRK11649 |
putative peptidase; Provisional |
4-410 |
8.58e-95 |
|
putative peptidase; Provisional
Pssm-ID: 236946 [Multi-domain] Cd Length: 439 Bit Score: 291.95 E-value: 8.58e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808955 4 KIFSSPFAELSPVKKVaILGLPLIAAIGVAL------QSSQSNLTKTIELDLPDstvIESILSPSSVTVIEPP------- 70
Cdd:PRK11649 6 RSIALAFNNLPRPHRV-MLGSLTVLTLAVAVwrpyvyHPESAPIVKTIELEKSE---IRSLLPEASEPIDQAAqedeaip 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808955 71 -------------TFEYQIQSGDNLSSIFTQLGFSyksmMSvmetDLNFLA-----LDTLRPGNTLRfWRDEATSDLSKM 132
Cdd:PRK11649 82 qdelddkiageagVHEYVVSTGDTLSSILNQYGID----MS----DISQLAaqdkeLRNLKIGQQLS-WTLTADGDLQRL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808955 133 ELQFSVADKVVYRLLDDGsYEFEDISIPGEWKQKPLVGDIQGSFSMSANKVGLNSLEIDHIVTLLKDKLNFsRDLRAGDQ 212
Cdd:PRK11649 153 TWEVSRRETRTYDRTGNG-FKETSEMQQGEWVNSVLKGTVGGSFVASAKNAGLTSAEISAVIKALQWQMDF-RKLKKGDE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808955 213 FEVLQKAQYVDGvatgKRE---IEAIKIMNRNRVVSAYLHTDGQYYDANGDSLQRAFQRYPVSSGWRQSSQFNPKRLHPV 289
Cdd:PRK11649 231 FSVLMSREMLDG----KSEqsqLLGVRLRSGGKDYYAIRAEDGKFYDRNGSGLAKGFLRFPTAKQFRISSNFNPRRLNPV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808955 290 TGRISPHNGTDFATPVGTPVQATGDGKVIMTRKHPYAGNYVVIQHGSTYKTRYLHLSKILVRKGQTVSRGQRIGLSGKTG 369
Cdd:PRK11649 307 TGRVAPHRGVDFAMPVGTPVLAVGDGEVVVAKRSGAAGNYVAIRHGRQYTTRYMHLRKLLVKPGQKVKRGDRIALSGNTG 386
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 880808955 370 RVTGAHLHYELIERGRPVNAMTANIPMADSVPKKEKATFVA 410
Cdd:PRK11649 387 RSTGPHLHYEVWINQQAVNPLTAKLPRTEGLTGKDRREYLA 427
|
|
| NlpD |
COG0739 |
Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell ... |
204-391 |
1.05e-53 |
|
Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440502 [Multi-domain] Cd Length: 196 Bit Score: 177.47 E-value: 1.05e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808955 204 SRDLRAGDQFEVLQKAQYVDGVATGKREIEAIKIMNRNRVVSAYLHTDGQYYDANGDSLQRAFQRYPVSSgwRQSSQFNP 283
Cdd:COG0739 8 AAALLALALLASAAGAAAAVAAAAAAAAAAAALAAAALAAAVSAAASAAAAAAAAAAAIALGSGAWPVKG--RITSGFGY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808955 284 kRLHPVTGRISPHNGTDFATPVGTPVQATGDGKVIMTRKHPYAGNYVVIQHGSTYKTRYLHLSKILVRKGQTVSRGQRIG 363
Cdd:COG0739 86 -RRHPVTGRRRFHKGIDIAAPTGTPVYAAADGTVVFAGWNGGYGNLVIIDHGNGYTTLYAHLSSILVKVGQRVKAGQVIG 164
|
170 180
....*....|....*....|....*...
gi 880808955 364 LSGKTGRVTGAHLHYELIERGRPVNAMT 391
Cdd:COG0739 165 YVGNTGRSTGPHLHFEVRVNGKPVDPLP 192
|
|
| OapA |
COG3061 |
Cell division protein YtfB/OapA (opacity-associated protein A) [Cell cycle control, cell ... |
13-411 |
8.70e-48 |
|
Cell division protein YtfB/OapA (opacity-associated protein A) [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442295 [Multi-domain] Cd Length: 425 Bit Score: 169.08 E-value: 8.70e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808955 13 LSPVKKVAILGLPLIAAIGVALQSSQSNLTKTIELDLPDSTVIESIL----SPSSVTVIEPPTFEYQIQSGDNLSSIFTQ 88
Cdd:COG3061 7 LPRKHRRLLGLLSALLLLALLLPSPDASASRVSQPLVPLALTAEADApaaaAPAAPAAPEGEWQEYTVQSGDTLSQIFRR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808955 89 LGFSYKSMMSVMETDLNFLALDTLRPGNTLRFWRDeATSDLSKMELQFSVADKVVYRLLDDGsyefedisipgeWKQKPL 168
Cdd:COG3061 87 LGLSASDLYALLAAEGDAKPLSRLKPGQELRFQLD-ADGQLQALRYEVSRLETLLFTRQGDG------------FQRKRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808955 169 VGDIQGSFSMSANKVGLNSLEIDHIVTLLKDKLNFSRDLRAGDQFEVLQKAQYVDGVATGKREIEAIKIMNRNRVVSAYL 248
Cdd:COG3061 154 TELSDGSFSADAALASLETLELAAAAGILSDFIAAALDAGAGDAGLVELEIILDDDIDFADLLFAADRFTGDYFRVYAEG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808955 249 HTDGQYYDANGDSLQRAFQRYPVSSGWRQSSQFNP-----------------------------KRLHPVTGRISPHNGT 299
Cdd:COG3061 234 EGGDGGYIGAGGFRAAKFRRRAVRFRRSSSSSSYRrrphrlsrrrrlrrgpdaaapsgssnaagGGGHKITRRGGGGGGA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808955 300 DFATPVGTPVQATGDGKVIMTRKHPYAGNYVVIQHGSTYKTRYLHLSKILVRKGQTVSRGQRIGLSGKTGRVTGAHLHYE 379
Cdd:COG3061 314 AVGVGTGTPTTGAGLGVVRGGRGGGGGVVVGQIGRGGTYGGTGLHLHKHGHKGGGVVGQGVTIGTLGGTGPTTGPHLHYE 393
|
410 420 430
....*....|....*....|....*....|..
gi 880808955 380 LIERGRPVNAMTANIPMADSVPKKEKATFVAA 411
Cdd:COG3061 394 FVQNGVRVAPLTVKLPAAPPLAAAAAAAFKAL 425
|
|
| Peptidase_M23 |
pfam01551 |
Peptidase family M23; Members of this family are zinc metallopeptidases with a range of ... |
294-388 |
4.55e-44 |
|
Peptidase family M23; Members of this family are zinc metallopeptidases with a range of specificities. The peptidase family M23 is included in this family, these are Gly-Gly endopeptidases. Peptidase family M23 are also endopeptidases. This family also includes some bacterial lipoproteins such as Swiss:P33648 for which no proteolytic activity has been demonstrated. This family also includes leukocyte cell-derived chemotaxin 2 (LECT2) proteins. LECT2 is a liver-specific protein which is thought to be linked to hepatocyte growth although the exact function of this protein is unknown.
Pssm-ID: 460250 [Multi-domain] Cd Length: 96 Bit Score: 148.85 E-value: 4.55e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808955 294 SPHNGTDFATPVGTPVQATGDGKVIMTRKHPYAGNYVVIQHGSTYKTRYLHLSKILVRKGQTVSRGQRIGLSGKTGRVTG 373
Cdd:pfam01551 1 RFHKGIDIAAPTGTPVYAAADGVVVFAGWLGGYGNLVIIDHGNGYSTLYAHLSSILVKVGQRVKAGQVIGTVGSTGRSTG 80
|
90
....*....|....*
gi 880808955 374 AHLHYELIERGRPVN 388
Cdd:pfam01551 81 PHLHFEIRKNGKPVD 95
|
|
| M23_peptidase |
cd12797 |
M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; ... |
296-380 |
1.19e-40 |
|
M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; This model describes the metallopeptidase M23 family, which includes beta-lytic metallopeptidase and lysostaphin. Members of this family are zinc endopeptidases that lyse bacterial cell wall peptidoglycans; they cleave either the N-acylmuramoyl-Ala bond between the cell wall peptidoglycan and the cross-linking peptide (e.g. beta-lytic endopeptidase) or a bond within the cross-linking peptide (e.g. stapholysin, and lysostaphin). Beta-lytic metallopeptidase, formerly known as beta-lytic protease, has a preference for cleavage of Gly-X bonds and favors hydrophobic or apolar residues on either side. It inhibits growth of sensitive organisms and may potentially serve as an antimicrobial agent. Lysostaphin, produced by Staphylococcus genus, cleaves pentaglycine cross-bridges of cell wall peptidoglycan, acting as autolysins to maintain cell wall metabolism or as toxins and weapons against competing strains. Staphylolysin (also known as LasA) is implicated in a range of processes related to Pseudomonas virulence, including stimulating shedding of the ectodomain of cell surface heparan sulphate proteoglycan syndecan-1, and elastin degradation in connective tissue. Its active site is less constricted and contains a five-coordinate zinc ion with trigonal bipyramidal geometry and two metal-bound water molecules, possibly contributing to its activity against a wider range of substrates than those used by related lytic enzymes, consistent with its multiple roles in Pseudomonas virulence. The family includes members that do not appear to have the conserved zinc-binding site and might be lipoproteins lacking proteolytic activity.
Pssm-ID: 410984 [Multi-domain] Cd Length: 85 Bit Score: 139.65 E-value: 1.19e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808955 296 HNGTDFATPVGTPVQATGDGKVIMTRKHPYAGNYVVIQHGSTYKTRYLHLSKILVRKGQTVSRGQRIGLSGKTGRVTGAH 375
Cdd:cd12797 1 HNGIDIAAPEGTPVYAAADGTVVFAGWDGGYGNYVIIDHGNGYYTLYAHLSSILVKVGQRVKKGQVIGTVGNTGRSTGPH 80
|
....*
gi 880808955 376 LHYEL 380
Cdd:cd12797 81 LHFEI 85
|
|
| SpoIIQ2 |
COG5821 |
Stage II sporulation protein SpoIIQ, clostridial version, metallopeptidase M23 family [Cell ... |
285-391 |
6.05e-33 |
|
Stage II sporulation protein SpoIIQ, clostridial version, metallopeptidase M23 family [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444523 [Multi-domain] Cd Length: 200 Bit Score: 123.21 E-value: 6.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808955 285 RLHPVTGRISPHNGTDFATPVGTPVQATGDGKVIMTRKHPYAGNYVVIQHGSTYKTRYLHL-SKILVRKGQTVSRGQRIG 363
Cdd:COG5821 86 VYSKTLNEWRTHTGIDIAAKEGTPVKAAADGVVVEVGKDPKYGITVVIDHGNGIKTVYANLdSKIKVKVGQKVKKGQVIG 165
|
90 100 110
....*....|....*....|....*....|.
gi 880808955 364 LSGKTGRV---TGAHLHYELIERGRPVNAMT 391
Cdd:COG5821 166 KVGSTALFessEGPHLHFEVLKNGKPVDPMK 196
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
288-388 |
3.04e-28 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 114.48 E-value: 3.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808955 288 PVTGRIS-----------PHNGTDFATPVGTPVQATGDGKVIMTRKHPYAGNYVVIQHGSTYKTRYLHLSKILVRKGQTV 356
Cdd:COG4942 258 PVSGRVVrrfgerdggggRNKGIDIAAPPGAPVRAVADGTVVYAGWLRGYGNLVIIDHGGGYLTLYAHLSSLLVKVGQRV 337
|
90 100 110
....*....|....*....|....*....|..
gi 880808955 357 SRGQRIGLSGKTGRVTGAHLHYELIERGRPVN 388
Cdd:COG4942 338 KAGQPIGTVGSSGGQGGPTLYFELRKNGKPVD 369
|
|
| Csd3_N2 |
pfam19425 |
Csd3 second domain; This entry represents the second domain from the Csd3 peptidase. This ... |
161-283 |
1.18e-25 |
|
Csd3 second domain; This entry represents the second domain from the Csd3 peptidase. This domain has a similar structure to pfam18059 despite low sequence similarity.
Pssm-ID: 437257 [Multi-domain] Cd Length: 122 Bit Score: 100.94 E-value: 1.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808955 161 GEWKQKPLVGDIQGSFSMSANKVGLNSLEIDHIVTLLKDKLNFsRDLRAGDQFEVLQKAQYVDGvatgKRE---IEAIKI 237
Cdd:pfam19425 2 GEWQNSVLKGRVDGSFVASARKAGLTSNEISAVIKALQWQLDF-RKLKKGDKFSVLMSREMLDG----KREqsqLLGVRL 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 880808955 238 MNRNRVVSAYLHTDGQYYDANGDSLQRAFQRYPVSSGWRQSSQFNP 283
Cdd:pfam19425 77 RSGGKDYYAIRAEDGKFYDRNGSGLARGFLRFPTAKQFRVSSNFNP 122
|
|
| SpoIVFA |
COG5833 |
Stage IV sporulation protein SpoIVFA, regulates SpoIVFB [Cell cycle control, cell division, ... |
288-363 |
1.83e-11 |
|
Stage IV sporulation protein SpoIVFA, regulates SpoIVFB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444535 [Multi-domain] Cd Length: 219 Bit Score: 63.47 E-value: 1.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808955 288 PVTGRISP-----HNGTDFATPVGTPVQATGDGKVIMTRKHPYAGNYVVIQHGSTYKTRYLHLSKILVRKGQTVSRGQRI 362
Cdd:COG5833 107 PVSGKVVEsfqenGKGVDIETPGGANVKAVKEGYVIFAGKDEETGKTVIIQHADGSESWYGNLSSIDVKLYDFVEAGQKI 186
|
.
gi 880808955 363 G 363
Cdd:COG5833 187 G 187
|
|
| nlpD |
PRK10871 |
murein hydrolase activator NlpD; |
298-388 |
1.84e-10 |
|
murein hydrolase activator NlpD;
Pssm-ID: 236782 [Multi-domain] Cd Length: 319 Bit Score: 61.77 E-value: 1.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808955 298 GTDFATPVGTPVQATGDGKVImtrkhpYAGN-------YVVIQHGSTYKTRYLHLSKILVRKGQTVSRGQRIGLSGKTGr 370
Cdd:PRK10871 221 GIDIAGSKGQAIIATADGRVV------YAGNalrgygnLIIIKHNDDYLSAYAHNDTMLVREQQEVKAGQKIATMGSTG- 293
|
90
....*....|....*...
gi 880808955 371 VTGAHLHYELIERGRPVN 388
Cdd:PRK10871 294 TSSTRLHFEIRYKGKSVN 311
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
302-388 |
5.82e-06 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 48.15 E-value: 5.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808955 302 ATPVGTPVQATGDGKVIMTRKHPYAGNYVVIQHGSTYKTRYLHLSKILVRKGQTVSRGQRIGLSGKTGRVTGAHLHYELI 381
Cdd:PRK11637 335 GASEGTEVKAIADGRVLLADWLQGYGLVVVVEHGKGDMSLYGYNQSALVSVGAQVRAGQPIALVGSSGGQGRPSLYFEIR 414
|
....*..
gi 880808955 382 ERGRPVN 388
Cdd:PRK11637 415 RQGQAVN 421
|
|
| PRK06148 |
PRK06148 |
hypothetical protein; Provisional |
287-381 |
1.51e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 180426 [Multi-domain] Cd Length: 1013 Bit Score: 47.33 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880808955 287 HPVTGRISPHNGTDFATPVGTPVQATGDGKV--IMTRKHPYA-GNYVVIQH----GSTYKTRYLHLSKILV---RKGQTV 356
Cdd:PRK06148 432 FIEGERRTVHLGVDLFAPAGTPVYAPLAGTVrsVEIEAVPLGyGGLVALEHetpgGDPFYTLYGHLAHEAVsrlKPGDRL 511
|
90 100
....*....|....*....|....*..
gi 880808955 357 SRGQRIGLSGKTGRVTG--AHLHYELI 381
Cdd:PRK06148 512 AAGELFGAMGDAHENGGwaPHLHFQLS 538
|
|
| LysM |
COG1388 |
LysM repeat [Cell wall/membrane/envelope biogenesis]; |
69-119 |
7.90e-03 |
|
LysM repeat [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440998 [Multi-domain] Cd Length: 156 Bit Score: 37.00 E-value: 7.90e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 880808955 69 PPTFEYQIQSGDNLSSIFTQLGFSYKSMMSvmetdLNFLALDTLRPGNTLR 119
Cdd:COG1388 107 PSPVTYTVKKGDTLWSIARRYGVSVEELKR-----WNGLSSDTIRPGQKLK 152
|
|
| LysM |
pfam01476 |
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ... |
74-119 |
8.04e-03 |
|
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: 34.29 E-value: 8.04e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 880808955 74 YQIQSGDNLSSIFTQLGFSYKSMMSvmetdLNFLALDTLRPGNTLR 119
Cdd:pfam01476 1 YTVKKGDTLSSIAKRYGITVEQLAE-----LNGLSSPNLYVGQKLK 41
|
|
| |
