|
Name |
Accession |
Description |
Interval |
E-value |
| strep_PBP3 |
NF038273 |
streptococcal D-alanyl-D-alanine carboxypeptidase PBP3; PBP3 (penicillin-binding protein 3) is ... |
12-417 |
3.61e-131 |
|
streptococcal D-alanyl-D-alanine carboxypeptidase PBP3; PBP3 (penicillin-binding protein 3) is the lone D-alanyl-D-alanine carboxypeptidase in Streptococcus pneumoniae. The gene is known as pbp3 or dacA.
Pssm-ID: 468443 [Multi-domain] Cd Length: 407 Bit Score: 384.22 E-value: 3.61e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500022673 12 IMAVSLAVSGFLVSPKAAQaaaEPTVNANAAIAIEESTGKILYSKDADKLMGIASMTKMMDEYLLLEAINDGKIKWDDKV 91
Cdd:NF038273 4 ILLLLLLLAFFLATTVSAD---DFDVAAKHAIAVEANTGKILYEKDATTPVPIASLTKLLTAYLVYKEIKSGKLSWDTPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500022673 92 TISEYAYKVSQDRSLSNVPLRlGEEYTVQELYEAMAIYSANGAAIAIAEKVAGSEKAFVDLMNKKAEKLKLGEHQFVNST 171
Cdd:NF038273 81 KISDYPYELTTNYEISNVPLD-ARKYTVKELLEASLVASANSAAIALAEKIAGSEPKFVDKMKAQLKEWGITDAKLVNAS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500022673 172 GLNNEDLKGGQQVG-GPKDENKMTARGMAKLAKHLIKDYPEVLKTASTTKKEFRkGTsdqiDMTNWNWLLPGLIYGRKGV 250
Cdd:NF038273 160 GLNNSYLGDHIYPGsKKDDENKLSAKDVAIIARHLIKDFPEVLKITSKTSADFA-GT----TIYSYNYMLKGMPYYREGV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500022673 251 DGLKTGTTDYAGMCLTATAVEDGMRVITVVLHANggGAGEHTSARFDETNKMLDYSFNNFKVKEVQKAGSKVKDpSSIAV 330
Cdd:NF038273 235 DGLKTGTTEKAGASFVATSVENGMRVITVVLNAD--NADEDEYARFTATNQLLDYIYQNFEKVTLVKKGQAYKD-SKLPV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500022673 331 DKGKEDTVGLVTKDAVKLVVPKNDNApKLSTKVTLKDKTLEVPVKKNTAVGEMevSLKGGDKLG--YLDGKqtENIDVLT 408
Cdd:NF038273 312 IDGKKKTVSAVAKKDLTVIQKIGTDS-KPSVKFTPKKKELTAPIKKGQVVGKA--TFKDKDLIGkgYLGEP--PSVELVA 386
|
....*....
gi 500022673 409 ANDVEKANW 417
Cdd:NF038273 387 KKDVKKSFF 395
|
|
| DacC |
COG1686 |
D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis]; |
13-418 |
2.11e-108 |
|
D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441292 [Multi-domain] Cd Length: 324 Bit Score: 323.33 E-value: 2.11e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500022673 13 MAVSLAVSGFLVSPKAAQAAAE-PTVNANAAIAIEESTGKILYSKDADKLMGIASMTKMMDEYLLLEAINDGKIKWDDKV 91
Cdd:COG1686 1 MKKLLLLALLLLLAAAAAAPAApPDIAAKSAILIDADTGQVLYEKNADERLPPASLTKLMTAYVVLEALKAGKISLDDKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500022673 92 TISEYAYKVsqdrSLSNVPLRLGEEYTVQELYEAMAIYSANGAAIAIAEKVAGSEKAFVDLMNKKAEKLKLGEHQFVNST 171
Cdd:COG1686 81 TVSEEAART----GGSKMGLKPGEQVTVEDLLKGLLLQSGNDAAVALAEHIAGSEEAFVALMNAKAKELGMTNTHFVNPT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500022673 172 GLNNEDlkggqqvggpkdeNKMTARGMAKLAKHLIKDYPEVLKTASTTKKEFRKGtsDQIDMTNWNWLLpgliYGRKGVD 251
Cdd:COG1686 157 GLPDPG-------------HYSTARDLALLARAAIKDYPEFYEIFSTKEFTFPNG--RGITLRNTNRLL----GRYPGVD 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500022673 252 GLKTGTTDYAGMCLTATAVEDGMRVITVVLHANGggagehTSARFDETNKMLDYSFnnfkvkevqkagskvkdpssiavd 331
Cdd:COG1686 218 GLKTGYTDAAGYCLVASAKRGGRRLIAVVLGAPS------EKARFADAAKLLDYGF------------------------ 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500022673 332 kgkedtvglvtkdavklvvPKNDnapKLSTKVTLkDKTLEVPVKKNTAVGEMEVslkggdklgYLDGKQTENIDVLTAND 411
Cdd:COG1686 268 -------------------PKGE---ALKAEVVL-DGPLKAPVKKGQVVGTLVV---------TLDGKTIAEVPLVAAED 315
|
....*..
gi 500022673 412 VEKANWF 418
Cdd:COG1686 316 VEKAGFF 322
|
|
| Peptidase_S11 |
pfam00768 |
D-alanyl-D-alanine carboxypeptidase; |
32-283 |
4.18e-86 |
|
D-alanyl-D-alanine carboxypeptidase;
Pssm-ID: 425859 [Multi-domain] Cd Length: 234 Bit Score: 263.09 E-value: 4.18e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500022673 32 AAEPTVNANAAIAIEESTGKILYSKDADKLMGIASMTKMMDEYLLLEAINDGKIKWDDKVTISEYAYKVSQDRSlSNVPL 111
Cdd:pfam00768 1 VSAPEIAAKSAILVDYNTGKVLYEKNPDQVRPIASITKLMTAYVVLEALKAGKIKEDDMVTISEDAWATGNPGS-SNIFL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500022673 112 RLGEEYTVQELYEAMAIYSANGAAIAIAEKVAGSEKAFVDLMNKKAEKLKLGEHQFVNSTGLNNEDlkggqqvggpkdeN 191
Cdd:pfam00768 80 KPGSQVSVKDLLRGALVSSGNDAAVALAEHIAGSEKAFVK*MNAKAKELGLKNTRFVNPTGLDAHG-------------Q 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500022673 192 KMTARGMAKLAKHLIKDYPEVLKTASTTKKEFRkgtsdqiDMTNWNWLLPGLIYGRKG--VDGLKTGTTDYAGMCLTATA 269
Cdd:pfam00768 147 YSSARDMAILAKALIKDLPEELSITKEKSFTFR-------GINKINQRNRNGLLWDKTwnVDGLKTGYTNEAGYCLVASA 219
|
250
....*....|....
gi 500022673 270 VEDGMRVITVVLHA 283
Cdd:pfam00768 220 TKGGMRLISVVMGA 233
|
|
| PBP4_Staph |
NF038258 |
penicillin-binding protein PBP4; Members of this family penicillin-binding protein 4 (PBP4), ... |
15-368 |
8.39e-61 |
|
penicillin-binding protein PBP4; Members of this family penicillin-binding protein 4 (PBP4), as the name is used in Staphylococcus aureus and related species from the same genus. PBP4 is not essential. It has transpeptidase activity, provides low level beta-lactam resistance, and in mutant strains can contribute to high level beta-lactam resistance.
Pssm-ID: 468436 [Multi-domain] Cd Length: 365 Bit Score: 202.13 E-value: 8.39e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500022673 15 VSLAVSGFLVSPKAAQAAAEPTVNANA--------------AIAIEEsTGKILYSKDADKLMGIASMTKMMDEYLLLEAI 80
Cdd:NF038258 2 VSLLLLSTIITPPASAAAETPVEIANQegyqnlseqynpegAIVTTQ-TGQILYDYHGNKKWDPASMTKLMTMYLTLEAI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500022673 81 NDGKIKWDDKVTISEYAYKVSQDRSLSNVPLRLGEEYTVQELYEAMAIYSANGAAIAIAEKVAGSEKAFVDLMNKKAEKL 160
Cdd:NF038258 81 KKGKLSLNDKVKITSDYEKMSTLPNLSTFPLKPGQTYTIKELLKQTALASSNAAALILAEKVSGNTSKFTDRMNEKAKAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500022673 161 KLGEHQFVNSTGLNNEDLKGGQqvggPK-----DENKMTARGMAKLAKHLIKDYPEVLKtasTTKKEfrKGTSDQIDMTN 235
Cdd:NF038258 161 GMKHTHFTNPSGADNNLLKPYA----PKkykdeTKSKSTAKDMAILSQHLIKKHPKILK---YTKLT--ADTQHGVTLYT 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500022673 236 WNWLLPGLIYGRKGVDGLKTGTTDyAGMCLTATAVEDGMRVITVVLHAN--GGGAGEHtsARFDETNKMLDYSFNNFKVK 313
Cdd:NF038258 232 TNLSLPGQPMSLKGTDGLKTGTSD-EGYNLALTTKRDGLRINQVIMNVGpyPSEGAKH--ARNKIANALMERAFKQYEYK 308
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 500022673 314 EVQKAGSKVKDpssiavdkGKEDTVglvtKDAVKLVVPKNDNAPKLstKVTLKDK 368
Cdd:NF038258 309 KVLSKGEHKID--------GKTYYV----KKDLYDVVPKDKSKYDL--KINKDGK 349
|
|
| PRK10001 |
PRK10001 |
serine-type D-Ala-D-Ala carboxypeptidase; |
22-444 |
4.67e-49 |
|
serine-type D-Ala-D-Ala carboxypeptidase;
Pssm-ID: 182189 [Multi-domain] Cd Length: 400 Bit Score: 172.10 E-value: 4.67e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500022673 22 FLVSP---KAAQAAAEPTVNANAAIAIEESTGKILYSKDADKLMGIASMTKMMDEYLLLEAINDGKIKWDDKVTISEYAY 98
Cdd:PRK10001 19 FLFAPtafAAEQTVEAPSVDARAWILMDYASGKVLAEGNADEKLDPASLTKIMTSYVVGQALKADKIKLTDMVTVGKDAW 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500022673 99 KVSQD--RSLSNVPLRLGEEYTVQELYEAMAIYSANGAAIAIAEKVAGSEKAFVDLMNKKAEKLKLGEHQFVNSTGLNNE 176
Cdd:PRK10001 99 ATGNPalRGSSVMFLKPGDQVSVADLNKGVIIQSGNDACIALADYVAGSQESFIGLMNGYAKKLGLTNTTFQTVHGLDAP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500022673 177 dlkgGQQvggpkdenkMTARGMAKLAKHLIKDYPEvlKTASTTKKEFrkgTSDQIDMTNWNWLLPGliyGRKGVDGLKTG 256
Cdd:PRK10001 179 ----GQF---------STARDMALLGKALIHDVPE--EYAIHKEKEF---TFNKIRQPNRNRLLWS---SNLNVDGMKTG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500022673 257 TTDYAGMCLTATAVEDGMRVITVVLHANGGGagehtsARFDETNKMLDYSFNNFKVKEVQKagskvkdPSSIAVDK---- 332
Cdd:PRK10001 238 TTAGAGYNLVASATQGDMRLISVVLGAKTDR------IRFNESEKLLTWGFRFFETVTPIK-------PDATFVTQrvwf 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500022673 333 GKEDTVGLVTKDAVKLVVPKNdNAPKLSTKVTLKDKTLEVPVKKNTAVGEMEVSlkggdklgyLDGKQTENIDVLTANDV 412
Cdd:PRK10001 305 GDKSEVNLGAGEAGSVTIPRG-QLKNLKASYTLTEPQLTAPLKKGQVVGTIDFQ---------LNGKSIEQRPLIVMENV 374
|
410 420 430
....*....|....*....|....*....|..
gi 500022673 413 EKanwfalsaqavGSFFTSAGNYIADGVKGWF 444
Cdd:PRK10001 375 EE-----------GGFFSRMWDFVMMKFHQWF 395
|
|
| PBP5_C |
smart00936 |
Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. ... |
310-414 |
5.46e-16 |
|
Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. coli functions as a D-alanyl-D-alanine carboxypeptidase. It is composed of two domains that are oriented at approximately right angles to each other. The N-terminal domain (pfam00768) is the catalytic domain. The C-terminal domain featured in this family is organized into a sandwich of two anti-parallel beta-sheets, and has a relatively hydrophobic surface as compared to the N-terminal domain. Its precise function is unknown; it may mediate interactions with other cell wall-synthesising enzymes, thus allowing the protein to be recruited to areas of active cell wall synthesis. It may also function as a linker domain that positions the active site in the catalytic domain closer to the peptidoglycan layer, to allow it to interact with cell wall peptides.
Pssm-ID: 198004 [Multi-domain] Cd Length: 92 Bit Score: 73.02 E-value: 5.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500022673 310 FKVKEVQKAGSKVKdpsSIAVDKGKEDTVGLVTKDAVKLVVPKNDNaPKLSTKVTLKDKTLEVPVKKNTAVGEMEVslkg 389
Cdd:smart00936 1 FETVKLYKKGQVVG---TVKVWKGKEKTVKLGAKEDVYVTLPKGEK-KKLKAKVVLDKPELEAPIKKGQVVGTLVV---- 72
|
90 100
....*....|....*....|....*
gi 500022673 390 gdklgYLDGKQTENIDVLTANDVEK 414
Cdd:smart00936 73 -----TLDGKLIGEVPLVALEDVEK 92
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
12-59 |
5.27e-03 |
|
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third step in the histidine degradation pathway, the hydrolysis of (S)-3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate to N-formimidoyl-L-glutamate. In bacteria, the enzyme is part of histidine utilization (hut) operon.
Pssm-ID: 238621 [Multi-domain] Cd Length: 371 Bit Score: 38.78 E-value: 5.27e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 500022673 12 IMAVSLAVSGFLVSPKAAQAAAepTVNANAAIAIEESTGKILYSKDAD 59
Cdd:cd01296 298 PLVMHLACRLMRMTPEEALTAA--TINAAAALGLGETVGSLEVGKQAD 343
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| strep_PBP3 |
NF038273 |
streptococcal D-alanyl-D-alanine carboxypeptidase PBP3; PBP3 (penicillin-binding protein 3) is ... |
12-417 |
3.61e-131 |
|
streptococcal D-alanyl-D-alanine carboxypeptidase PBP3; PBP3 (penicillin-binding protein 3) is the lone D-alanyl-D-alanine carboxypeptidase in Streptococcus pneumoniae. The gene is known as pbp3 or dacA.
Pssm-ID: 468443 [Multi-domain] Cd Length: 407 Bit Score: 384.22 E-value: 3.61e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500022673 12 IMAVSLAVSGFLVSPKAAQaaaEPTVNANAAIAIEESTGKILYSKDADKLMGIASMTKMMDEYLLLEAINDGKIKWDDKV 91
Cdd:NF038273 4 ILLLLLLLAFFLATTVSAD---DFDVAAKHAIAVEANTGKILYEKDATTPVPIASLTKLLTAYLVYKEIKSGKLSWDTPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500022673 92 TISEYAYKVSQDRSLSNVPLRlGEEYTVQELYEAMAIYSANGAAIAIAEKVAGSEKAFVDLMNKKAEKLKLGEHQFVNST 171
Cdd:NF038273 81 KISDYPYELTTNYEISNVPLD-ARKYTVKELLEASLVASANSAAIALAEKIAGSEPKFVDKMKAQLKEWGITDAKLVNAS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500022673 172 GLNNEDLKGGQQVG-GPKDENKMTARGMAKLAKHLIKDYPEVLKTASTTKKEFRkGTsdqiDMTNWNWLLPGLIYGRKGV 250
Cdd:NF038273 160 GLNNSYLGDHIYPGsKKDDENKLSAKDVAIIARHLIKDFPEVLKITSKTSADFA-GT----TIYSYNYMLKGMPYYREGV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500022673 251 DGLKTGTTDYAGMCLTATAVEDGMRVITVVLHANggGAGEHTSARFDETNKMLDYSFNNFKVKEVQKAGSKVKDpSSIAV 330
Cdd:NF038273 235 DGLKTGTTEKAGASFVATSVENGMRVITVVLNAD--NADEDEYARFTATNQLLDYIYQNFEKVTLVKKGQAYKD-SKLPV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500022673 331 DKGKEDTVGLVTKDAVKLVVPKNDNApKLSTKVTLKDKTLEVPVKKNTAVGEMevSLKGGDKLG--YLDGKqtENIDVLT 408
Cdd:NF038273 312 IDGKKKTVSAVAKKDLTVIQKIGTDS-KPSVKFTPKKKELTAPIKKGQVVGKA--TFKDKDLIGkgYLGEP--PSVELVA 386
|
....*....
gi 500022673 409 ANDVEKANW 417
Cdd:NF038273 387 KKDVKKSFF 395
|
|
| DacC |
COG1686 |
D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis]; |
13-418 |
2.11e-108 |
|
D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441292 [Multi-domain] Cd Length: 324 Bit Score: 323.33 E-value: 2.11e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500022673 13 MAVSLAVSGFLVSPKAAQAAAE-PTVNANAAIAIEESTGKILYSKDADKLMGIASMTKMMDEYLLLEAINDGKIKWDDKV 91
Cdd:COG1686 1 MKKLLLLALLLLLAAAAAAPAApPDIAAKSAILIDADTGQVLYEKNADERLPPASLTKLMTAYVVLEALKAGKISLDDKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500022673 92 TISEYAYKVsqdrSLSNVPLRLGEEYTVQELYEAMAIYSANGAAIAIAEKVAGSEKAFVDLMNKKAEKLKLGEHQFVNST 171
Cdd:COG1686 81 TVSEEAART----GGSKMGLKPGEQVTVEDLLKGLLLQSGNDAAVALAEHIAGSEEAFVALMNAKAKELGMTNTHFVNPT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500022673 172 GLNNEDlkggqqvggpkdeNKMTARGMAKLAKHLIKDYPEVLKTASTTKKEFRKGtsDQIDMTNWNWLLpgliYGRKGVD 251
Cdd:COG1686 157 GLPDPG-------------HYSTARDLALLARAAIKDYPEFYEIFSTKEFTFPNG--RGITLRNTNRLL----GRYPGVD 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500022673 252 GLKTGTTDYAGMCLTATAVEDGMRVITVVLHANGggagehTSARFDETNKMLDYSFnnfkvkevqkagskvkdpssiavd 331
Cdd:COG1686 218 GLKTGYTDAAGYCLVASAKRGGRRLIAVVLGAPS------EKARFADAAKLLDYGF------------------------ 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500022673 332 kgkedtvglvtkdavklvvPKNDnapKLSTKVTLkDKTLEVPVKKNTAVGEMEVslkggdklgYLDGKQTENIDVLTAND 411
Cdd:COG1686 268 -------------------PKGE---ALKAEVVL-DGPLKAPVKKGQVVGTLVV---------TLDGKTIAEVPLVAAED 315
|
....*..
gi 500022673 412 VEKANWF 418
Cdd:COG1686 316 VEKAGFF 322
|
|
| Peptidase_S11 |
pfam00768 |
D-alanyl-D-alanine carboxypeptidase; |
32-283 |
4.18e-86 |
|
D-alanyl-D-alanine carboxypeptidase;
Pssm-ID: 425859 [Multi-domain] Cd Length: 234 Bit Score: 263.09 E-value: 4.18e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500022673 32 AAEPTVNANAAIAIEESTGKILYSKDADKLMGIASMTKMMDEYLLLEAINDGKIKWDDKVTISEYAYKVSQDRSlSNVPL 111
Cdd:pfam00768 1 VSAPEIAAKSAILVDYNTGKVLYEKNPDQVRPIASITKLMTAYVVLEALKAGKIKEDDMVTISEDAWATGNPGS-SNIFL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500022673 112 RLGEEYTVQELYEAMAIYSANGAAIAIAEKVAGSEKAFVDLMNKKAEKLKLGEHQFVNSTGLNNEDlkggqqvggpkdeN 191
Cdd:pfam00768 80 KPGSQVSVKDLLRGALVSSGNDAAVALAEHIAGSEKAFVK*MNAKAKELGLKNTRFVNPTGLDAHG-------------Q 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500022673 192 KMTARGMAKLAKHLIKDYPEVLKTASTTKKEFRkgtsdqiDMTNWNWLLPGLIYGRKG--VDGLKTGTTDYAGMCLTATA 269
Cdd:pfam00768 147 YSSARDMAILAKALIKDLPEELSITKEKSFTFR-------GINKINQRNRNGLLWDKTwnVDGLKTGYTNEAGYCLVASA 219
|
250
....*....|....
gi 500022673 270 VEDGMRVITVVLHA 283
Cdd:pfam00768 220 TKGGMRLISVVMGA 233
|
|
| PBP4_Staph |
NF038258 |
penicillin-binding protein PBP4; Members of this family penicillin-binding protein 4 (PBP4), ... |
15-368 |
8.39e-61 |
|
penicillin-binding protein PBP4; Members of this family penicillin-binding protein 4 (PBP4), as the name is used in Staphylococcus aureus and related species from the same genus. PBP4 is not essential. It has transpeptidase activity, provides low level beta-lactam resistance, and in mutant strains can contribute to high level beta-lactam resistance.
Pssm-ID: 468436 [Multi-domain] Cd Length: 365 Bit Score: 202.13 E-value: 8.39e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500022673 15 VSLAVSGFLVSPKAAQAAAEPTVNANA--------------AIAIEEsTGKILYSKDADKLMGIASMTKMMDEYLLLEAI 80
Cdd:NF038258 2 VSLLLLSTIITPPASAAAETPVEIANQegyqnlseqynpegAIVTTQ-TGQILYDYHGNKKWDPASMTKLMTMYLTLEAI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500022673 81 NDGKIKWDDKVTISEYAYKVSQDRSLSNVPLRLGEEYTVQELYEAMAIYSANGAAIAIAEKVAGSEKAFVDLMNKKAEKL 160
Cdd:NF038258 81 KKGKLSLNDKVKITSDYEKMSTLPNLSTFPLKPGQTYTIKELLKQTALASSNAAALILAEKVSGNTSKFTDRMNEKAKAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500022673 161 KLGEHQFVNSTGLNNEDLKGGQqvggPK-----DENKMTARGMAKLAKHLIKDYPEVLKtasTTKKEfrKGTSDQIDMTN 235
Cdd:NF038258 161 GMKHTHFTNPSGADNNLLKPYA----PKkykdeTKSKSTAKDMAILSQHLIKKHPKILK---YTKLT--ADTQHGVTLYT 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500022673 236 WNWLLPGLIYGRKGVDGLKTGTTDyAGMCLTATAVEDGMRVITVVLHAN--GGGAGEHtsARFDETNKMLDYSFNNFKVK 313
Cdd:NF038258 232 TNLSLPGQPMSLKGTDGLKTGTSD-EGYNLALTTKRDGLRINQVIMNVGpyPSEGAKH--ARNKIANALMERAFKQYEYK 308
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 500022673 314 EVQKAGSKVKDpssiavdkGKEDTVglvtKDAVKLVVPKNDNAPKLstKVTLKDK 368
Cdd:NF038258 309 KVLSKGEHKID--------GKTYYV----KKDLYDVVPKDKSKYDL--KINKDGK 349
|
|
| PRK10001 |
PRK10001 |
serine-type D-Ala-D-Ala carboxypeptidase; |
22-444 |
4.67e-49 |
|
serine-type D-Ala-D-Ala carboxypeptidase;
Pssm-ID: 182189 [Multi-domain] Cd Length: 400 Bit Score: 172.10 E-value: 4.67e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500022673 22 FLVSP---KAAQAAAEPTVNANAAIAIEESTGKILYSKDADKLMGIASMTKMMDEYLLLEAINDGKIKWDDKVTISEYAY 98
Cdd:PRK10001 19 FLFAPtafAAEQTVEAPSVDARAWILMDYASGKVLAEGNADEKLDPASLTKIMTSYVVGQALKADKIKLTDMVTVGKDAW 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500022673 99 KVSQD--RSLSNVPLRLGEEYTVQELYEAMAIYSANGAAIAIAEKVAGSEKAFVDLMNKKAEKLKLGEHQFVNSTGLNNE 176
Cdd:PRK10001 99 ATGNPalRGSSVMFLKPGDQVSVADLNKGVIIQSGNDACIALADYVAGSQESFIGLMNGYAKKLGLTNTTFQTVHGLDAP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500022673 177 dlkgGQQvggpkdenkMTARGMAKLAKHLIKDYPEvlKTASTTKKEFrkgTSDQIDMTNWNWLLPGliyGRKGVDGLKTG 256
Cdd:PRK10001 179 ----GQF---------STARDMALLGKALIHDVPE--EYAIHKEKEF---TFNKIRQPNRNRLLWS---SNLNVDGMKTG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500022673 257 TTDYAGMCLTATAVEDGMRVITVVLHANGGGagehtsARFDETNKMLDYSFNNFKVKEVQKagskvkdPSSIAVDK---- 332
Cdd:PRK10001 238 TTAGAGYNLVASATQGDMRLISVVLGAKTDR------IRFNESEKLLTWGFRFFETVTPIK-------PDATFVTQrvwf 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500022673 333 GKEDTVGLVTKDAVKLVVPKNdNAPKLSTKVTLKDKTLEVPVKKNTAVGEMEVSlkggdklgyLDGKQTENIDVLTANDV 412
Cdd:PRK10001 305 GDKSEVNLGAGEAGSVTIPRG-QLKNLKASYTLTEPQLTAPLKKGQVVGTIDFQ---------LNGKSIEQRPLIVMENV 374
|
410 420 430
....*....|....*....|....*....|..
gi 500022673 413 EKanwfalsaqavGSFFTSAGNYIADGVKGWF 444
Cdd:PRK10001 375 EE-----------GGFFSRMWDFVMMKFHQWF 395
|
|
| PRK10793 |
PRK10793 |
D-alanyl-D-alanine carboxypeptidase fraction A; Provisional |
35-419 |
2.26e-42 |
|
D-alanyl-D-alanine carboxypeptidase fraction A; Provisional
Pssm-ID: 182736 [Multi-domain] Cd Length: 403 Bit Score: 154.24 E-value: 2.26e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500022673 35 PTVNANAAIAIEESTGKILYSKDADKLMGIASMTKMMDEYLLLEAINDGKIKWDDKVTISEYAYK----VSQDRSLsnVP 110
Cdd:PRK10793 42 PQIDAESYILIDYNSGKVLAEQNADVRRDPASLTKMMTSYVIGQAMKAGKFKETDLVTVGNDAWAtgnpVFKGSSL--MF 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500022673 111 LRLGEEYTVQELYEAMAIYSANGAAIAIAEKVAGSEKAFVDLMNKKAEKLKLGEHQFVNSTGLNNEdlkgGQQvggpkde 190
Cdd:PRK10793 120 LKPGMQVPVSQLIRGINLQSGNDACVAMADYVAGSQDAFVGLMNSYVNALGLKNTHFQTVHGLDAD----GQY------- 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500022673 191 nkMTARGMAKLAKHLIKDYPEvlKTASTTKKEFrkgTSDQIDMTNWNwllpGLIYGRK-GVDGLKTGTTDYAGMCLTATA 269
Cdd:PRK10793 189 --SSARDMALIGQALIRDVPN--EYAIYKEKEF---TFNGIRQLNRN----GLLWDNSlNVDGIKTGHTDKAGYNLVASA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500022673 270 VEDGMRVITVVLhangggaGEHT-SARFDETNKMLDYSFNNFKVKEVQKAGskvKDPSSIAVDKGKEDTVGLVTKDAVKL 348
Cdd:PRK10793 258 TEGQMRLISAVM-------GGRTfKGRETESKKLLTWGFRFFETVNPLKVG---KEFASEPVWFGDSDRASLGVDKDVYL 327
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500022673 349 VVPKNdNAPKLSTKVTLKDKTLEVPVKKNTAVGEMEVSlkggdklgyLDGKQTENIDVLTANDVEKANWFA 419
Cdd:PRK10793 328 TIPRG-RMKDLKASYVLNTSELHAPLQKNQVVGTINFQ---------LDGKTIEQRPLVVLQEIPEGNFFG 388
|
|
| dacD |
PRK11397 |
serine-type D-Ala-D-Ala carboxypeptidase DacD; |
17-393 |
4.08e-42 |
|
serine-type D-Ala-D-Ala carboxypeptidase DacD;
Pssm-ID: 183117 [Multi-domain] Cd Length: 388 Bit Score: 153.44 E-value: 4.08e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500022673 17 LAVSGFLVSPKAAQAAAE-------PTVNANAAIAIEESTGKILYSKDADKLMGIASMTKMMDEYLLLEAINDGKIKWDD 89
Cdd:PRK11397 7 IAASLFAFNLSSAFAAENipfspqpPAIDAGSWVLMDYTTGQILTAGNEHQQRNPASLTKLMTGYVVDRAIDSHRITPDD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500022673 90 KVTISEYAYK----VSQDRSLsnVPLRLGEEYTVQELYEAMAIYSANGAAIAIAEKVAGSEKAFVDLMNKKAEKLKLGEH 165
Cdd:PRK11397 87 IVTVGRDAWAkdnpVFVGSSL--MFLKEGDRVSVRDLSRGLIVDSGNDACVALADYIAGGQRQFVEMMNNYVEKLHLKDT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500022673 166 QFVNSTGLNNEdlkgGQQVggpkdenkmTARGMAKLAKHLIKDYPEVLKTASTtkkefRKGTSDQIDMTNWNwllpGLIY 245
Cdd:PRK11397 165 HFETVHGLDAP----GQHS---------SAYDLAVLSRAIIHGEPEFYHMYSE-----KSLTWNGITQQNRN----GLLW 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500022673 246 GRK-GVDGLKTGTTDYAGMCLTATAVEDGMRVITVVLhangggAGEHTSARFDETNKMLDYSFNNFKVKEVQKAGSKVkd 324
Cdd:PRK11397 223 DKTmNVDGLKTGHTSGAGFNLIASAVDGQRRLIAVVM------GADSAKGREEQARKLLRWGQQNFTTVQILHRGKKV-- 294
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 500022673 325 pSSIAVDKGKEDTVGLVTKDAVKLVVPKnDNAPKLSTKVTLKDKTLEVPVKKNTAVGEMEvsLKGGDKL 393
Cdd:PRK11397 295 -GTERIWYGDKENIALGTEQDFWMVLPK-AEIPHIKAKYVLDGKELEAPISAHQRVGEIE--LYDRDKQ 359
|
|
| pbpG |
PRK11669 |
D-alanyl-D-alanine endopeptidase; Provisional |
6-285 |
1.78e-21 |
|
D-alanyl-D-alanine endopeptidase; Provisional
Pssm-ID: 236952 Cd Length: 306 Bit Score: 94.36 E-value: 1.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500022673 6 KKTGIAIMAVSLAVSGFLVSPK--AAQAAAEPT-----VNANAAIAIEESTGKILYSKDADKLMGIASMTKMMDEYLLLE 78
Cdd:PRK11669 1 MKFRVSLLSLLLLLAGVPFAPQavAKTAAATTAsqpqeIASGSAMVVDLNTNKVIYSSNPDLVVPIASITKLMTAMVVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500022673 79 AindgKIKWDDKVTIseyayKVSQDRSLSNV--PLRLGEEYTVQELYEAMAIYSANGAAIAIAEKVAGSEKAFVDLMNKK 156
Cdd:PRK11669 81 A----KLPLDEKLKV-----DISQTPEMKGVysRVRLNSEISRKDMLLLALMSSENRAAASLAHHYPGGYKAFIKAMNAK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500022673 157 AEKLKLGEHQFVNSTGLNnedlkggqqvggpkDENKMTARGMAKLAKhLIKDYPeVLKTASTTKKE---FRK-------- 225
Cdd:PRK11669 152 AKALGMTNTRYVEPTGLS--------------IHNVSTARDLTKLLI-ASKQYP-LIGQLSTTREKtatFRKpnytlpfr 215
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 500022673 226 GTSDQIDMTNWNWLLPgliygrkgvdglKTGTTDYAGMCLTATAVEDGMRVITVVLHANG 285
Cdd:PRK11669 216 NTNHLVYRDNWNIQLT------------KTGFTNAAGHCLVMRTVINNRPVALVVLDAFG 263
|
|
| PBP5_C |
smart00936 |
Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. ... |
310-414 |
5.46e-16 |
|
Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. coli functions as a D-alanyl-D-alanine carboxypeptidase. It is composed of two domains that are oriented at approximately right angles to each other. The N-terminal domain (pfam00768) is the catalytic domain. The C-terminal domain featured in this family is organized into a sandwich of two anti-parallel beta-sheets, and has a relatively hydrophobic surface as compared to the N-terminal domain. Its precise function is unknown; it may mediate interactions with other cell wall-synthesising enzymes, thus allowing the protein to be recruited to areas of active cell wall synthesis. It may also function as a linker domain that positions the active site in the catalytic domain closer to the peptidoglycan layer, to allow it to interact with cell wall peptides.
Pssm-ID: 198004 [Multi-domain] Cd Length: 92 Bit Score: 73.02 E-value: 5.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500022673 310 FKVKEVQKAGSKVKdpsSIAVDKGKEDTVGLVTKDAVKLVVPKNDNaPKLSTKVTLKDKTLEVPVKKNTAVGEMEVslkg 389
Cdd:smart00936 1 FETVKLYKKGQVVG---TVKVWKGKEKTVKLGAKEDVYVTLPKGEK-KKLKAKVVLDKPELEAPIKKGQVVGTLVV---- 72
|
90 100
....*....|....*....|....*
gi 500022673 390 gdklgYLDGKQTENIDVLTANDVEK 414
Cdd:smart00936 73 -----TLDGKLIGEVPLVALEDVEK 92
|
|
| PBP5_C |
pfam07943 |
Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. ... |
310-414 |
3.94e-12 |
|
Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. coli functions as a D-alanyl-D-alanine carboxypeptidase. It is composed of two domains that are oriented at approximately right angles to each other. The N-terminal domain (pfam00768) is the catalytic domain. The C-terminal domain featured in this family is organized into a sandwich of two anti-parallel beta-sheets, and has a relatively hydrophobic surface as compared to the N-terminal domain. Its precise function is unknown; it may mediate interactions with other cell wall-synthesising enzymes, thus allowing the protein to be recruited to areas of active cell wall synthesis. It may also function as a linker domain that positions the active site in the catalytic domain closer to the peptidoglycan layer, to allow it to interact with cell wall peptides.
Pssm-ID: 429749 [Multi-domain] Cd Length: 91 Bit Score: 61.84 E-value: 3.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500022673 310 FKVKEVQKAGSKVKdpsSIAVDKGKEDTVGLVTKDAVKLVVPKNDNApKLSTKVTLKDKtLEVPVKKNTAVGEMEVslkg 389
Cdd:pfam07943 1 FETKKLYKKGDVVK---KVKVWKGKKKTVPLGAKEDVYVTVPKGEKK-KLKAKVTLKKP-LEAPIKKGQVVGKLEV---- 71
|
90 100
....*....|....*....|....*
gi 500022673 390 gdklgYLDGKQTENIDVLTANDVEK 414
Cdd:pfam07943 72 -----YLDGKLIGEVPLVAKEDVEE 91
|
|
| Beta-lactamase2 |
pfam13354 |
Beta-lactamase enzyme family; This is the catalytic domain of class A beta-lactamases. It is ... |
48-208 |
8.21e-08 |
|
Beta-lactamase enzyme family; This is the catalytic domain of class A beta-lactamases. It is closely related to Beta-lactamase, pfam00144, the serine beta-lactamase-like superfamily, which contains the distantly related pfam00905 and PF00768 D-alanyl-D-alanine carboxypeptidase.
Pssm-ID: 463854 [Multi-domain] Cd Length: 215 Bit Score: 52.66 E-value: 8.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500022673 48 STGKiLYSKDADKLMGIASMTKMMDEYLLLEAINDGKIKWDDKVTISEyAYKVSQDRSLSnvPLRLGEEYTVQELYEAMA 127
Cdd:pfam13354 8 DTGE-ELGINGDRSFPAASTIKVPILLAVLEQVDEGKLSLDERLTVTA-EDKVGGSGILQ--YLPDGSQLSLRDLLTLMI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500022673 128 IYSANGAAIAIAEKVAGSEkafvdlMNKKAEKLKLGEHQFVNSTGLNNEDLKGGqqvggpkdENKMTARGMAKLAKHLIK 207
Cdd:pfam13354 84 AVSDNTATNLLIDRLGLEA------VNARLRALGLRDTRLRRKLPDLRAADKGG--------TNTTTARDMAKLLEALYR 149
|
.
gi 500022673 208 D 208
Cdd:pfam13354 150 G 150
|
|
| PenP |
COG2367 |
Beta-lactamase class A [Defense mechanisms]; |
10-218 |
2.24e-07 |
|
Beta-lactamase class A [Defense mechanisms];
Pssm-ID: 441934 [Multi-domain] Cd Length: 276 Bit Score: 52.21 E-value: 2.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500022673 10 IAIMAVSLAVSGFLVSPKAAQAAAEPTVNANAAIAIEESTGKILYSKDADKLMGIASMTKMMDEYLLLEAINDGKIKWDD 89
Cdd:COG2367 4 LALLLLAAAAAAPASALEAELAALEAALGGRVGVYVLDLDTGETVGINADERFPAASTFKLPVLAAVLRQVDAGKLSLDE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500022673 90 KVTISEyaykvsQDRSL-SNV--PLRLGEEYTVQELYEAMAIYSANGAAIAIAEKVaGSEKafvdlMNKKAEKLKLGEHQ 166
Cdd:COG2367 84 RVTLTP------EDLVGgSGIlqKLPDGTGLTLRELAELMITVSDNTATNLLLRLL-GPDA-----VNAFLRSLGLTDTR 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 500022673 167 FVNSTGLNNEDLKGGqqvggpkdENKMTARGMAKLAKHLIKdyPEVLKTAST 218
Cdd:COG2367 152 LDRKEPDLNELPGDG--------RNTTTPRDMARLLAALYR--GELLSPESR 193
|
|
| AmpC |
COG1680 |
CubicO group peptidase, beta-lactamase class C family [Defense mechanisms]; |
13-208 |
1.85e-05 |
|
CubicO group peptidase, beta-lactamase class C family [Defense mechanisms];
Pssm-ID: 441286 [Multi-domain] Cd Length: 355 Bit Score: 46.60 E-value: 1.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500022673 13 MAVSLAVSGFLVSPKAAQAAAEPTVNAN----AAIAIEEStGKILYSK-------------DADKLMGIASMTKMMDEYL 75
Cdd:COG1680 3 FAAAAPAAGLSADLAALDAALDAALAEGgipgAAVAVVRD-GKVVYEKaygvadletgrpvTPDTLFRIASVTKSFTATA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500022673 76 LLEAINDGKIKWDDKVT--ISEYAYKVSQDRSLS------------------NVPLRLGEEYTVQELYEAMA-------- 127
Cdd:COG1680 82 VLQLVEEGKLDLDDPVSkyLPEFKLPDDAKRDITvrhllthtsglpdyepdpYDAADVARPYTPDDLLARLAalpllfep 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500022673 128 ----IYSANGAAIA--IAEKVAGseKAFVDLMNKK-AEKLKLgehqfvNSTGLNNEDLKGGQQVGGPKDENK-------- 192
Cdd:COG1680 162 gtrfSYSNLGYDLLgeIIERVTG--QPLEDYLRERiFEPLGM------TDTGFGLPDAEAARLAPGYEADGEvhdapawl 233
|
250 260
....*....|....*....|....*.
gi 500022673 193 ----------MTARGMAKLAKHLIKD 208
Cdd:COG1680 234 gavagagglfSTARDLARFGQALLNG 259
|
|
| Beta-lactamase |
pfam00144 |
Beta-lactamase; This family appears to be distantly related to pfam00905 and PF00768 ... |
57-205 |
1.13e-03 |
|
Beta-lactamase; This family appears to be distantly related to pfam00905 and PF00768 D-alanyl-D-alanine carboxypeptidase.
Pssm-ID: 395092 [Multi-domain] Cd Length: 327 Bit Score: 40.95 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500022673 57 DADKLMGIASMTKMMDEYLLLEAINDGKIKWDDKVT--ISEYAYKVSQDRSLSNV-------------PLRLGEEYTVQE 121
Cdd:pfam00144 45 TADTLFRIASVTKTFTAAAVLQLVERGKLDLDDPVSkyLPEFAGPGKGGITLRDLlthtsglpplfapDDLEEAAADAAE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500022673 122 LYEAMA------------IYSANGAAIA--IAEKVAGseKAFVDLMNKK-AEKLKLgehqfvNSTGLNNEDLKGGQQVGG 186
Cdd:pfam00144 125 LVRALAalppvwppgtrwGYSNTAYGLLgeLLERVTG--QSYEELLGDRiLRPLGM------TDTELGVPEPGDPRDAAG 196
|
170 180 190
....*....|....*....|....*....|....*..
gi 500022673 187 PKDEN------------------KMTARGMAKLAKHL 205
Cdd:pfam00144 197 YTGEGppvrvppgplpagaygglKSTARDLARFLLAL 233
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
12-59 |
5.27e-03 |
|
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third step in the histidine degradation pathway, the hydrolysis of (S)-3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate to N-formimidoyl-L-glutamate. In bacteria, the enzyme is part of histidine utilization (hut) operon.
Pssm-ID: 238621 [Multi-domain] Cd Length: 371 Bit Score: 38.78 E-value: 5.27e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 500022673 12 IMAVSLAVSGFLVSPKAAQAAAepTVNANAAIAIEESTGKILYSKDAD 59
Cdd:cd01296 298 PLVMHLACRLMRMTPEEALTAA--TINAAAALGLGETVGSLEVGKQAD 343
|
|
| |
