|
Name |
Accession |
Description |
Interval |
E-value |
| MrcB |
COG0744 |
Penicillin-binding protein 1B/1F, peptidoglycan transglycosylase/transpeptidase [Cell wall ... |
42-239 |
3.78e-98 |
|
Penicillin-binding protein 1B/1F, peptidoglycan transglycosylase/transpeptidase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440507 [Multi-domain] Cd Length: 630 Bit Score: 299.53 E-value: 3.78e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587372 42 GNVMIEQSDISKLHVPAKlEVPESLTHAFIATEDKRFYHHNGLDYIAIIRASVENIKAGGVVQGGSTITQQLSKNAFLTN 121
Cdd:COG0744 63 GTLIATLGDENREWVPLD-QIPPHLKDAVVAIEDRRFYEHGGVDPKGIARALVANLTAGGVVQGGSTITQQLVKNLFLSN 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587372 122 ERTFSRKWKEIFYTKKIERTFTKDEILKLYVSNIYYGEGAWGIEKAANLYFGKKVNQLTLAESAMMAAVVKAPAYYSPAQ 201
Cdd:COG0744 142 ERTLSRKLKEALLALKLERKYSKDEILELYLNTVYFGRGAYGIEAAAQYYFGKSASDLTLAEAALLAGLVKAPSYYDPYR 221
|
170 180 190
....*....|....*....|....*....|....*...
gi 446587372 202 NYDKAVERRNVVLRLMEKEGYISHDEYVQAVSEKLVIR 239
Cdd:COG0744 222 NPEAAKERRNLVLDRMVEQGYITQAEADAAKAEPLTLV 259
|
|
| PBP_1a_fam |
TIGR02074 |
penicillin-binding protein, 1A family; Bacterial that synthesize a cell wall of peptidoglycan ... |
61-237 |
1.88e-84 |
|
penicillin-binding protein, 1A family; Bacterial that synthesize a cell wall of peptidoglycan (murein) generally have several transglycosylases and transpeptidases for the task. This family consists of bifunctional transglycosylase/transpeptidase penicillin-binding proteins (PBP). In the Proteobacteria, this family includes PBP 1A but not the paralogous PBP 1B (TIGR02071). This family also includes related proteins, often designated PBP 1A, from other bacterial lineages. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 273955 [Multi-domain] Cd Length: 531 Bit Score: 261.43 E-value: 1.88e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587372 61 EVPESLTHAFIATEDKRFYHHNGLDYIAIIRASVENIKAGGVVQGGSTITQQLSKNAFLTNERTFSRKWKEIFYTKKIER 140
Cdd:TIGR02074 9 DIPENLINAFLAIEDRRFYDHFGIDLKGIGRAAVANITSGRVLEGGSTITQQLAKNLYLTNERTITRKIQEALLALKLEQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587372 141 TFTKDEILKLYVSNIYYGEGAWGIEKAANLYFGKKVNQLTLAESAMMAAVVKAPAYYSPAQNYDKAVERRNVVLRLMEKE 220
Cdd:TIGR02074 89 KLSKDEILELYLNRIYFGNGAYGIEAAAQFYFGKSVNDLTLAEAAMLAGLPKAPSAYNPFKNPERAKDRRNLVLSNMVEN 168
|
170
....*....|....*..
gi 446587372 221 GYISHDEYVQAVSEKLV 237
Cdd:TIGR02074 169 GYITAEEAEEAINEPIQ 185
|
|
| Transgly |
pfam00912 |
Transglycosylase; The penicillin-binding proteins are bifunctional proteins consisting of ... |
42-218 |
1.26e-83 |
|
Transglycosylase; The penicillin-binding proteins are bifunctional proteins consisting of transglycosylase and transpeptidase in the N- and C-terminus respectively. The transglycosylase domain catalyzes the polymerization of murein glycan chains.
Pssm-ID: 459993 [Multi-domain] Cd Length: 177 Bit Score: 247.44 E-value: 1.26e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587372 42 GNVMIEQSDISKLHVPAKlEVPESLTHAFIATEDKRFYHHNGLDYIAIIRASVENIKAGGVVQGGSTITQQLSKNAFLTN 121
Cdd:pfam00912 2 GTLLAELGEENREYVPLD-DIPPALKNAVLAIEDRRFYEHGGVDPKGIARALLSNLRSGRIVQGGSTITQQLAKNLFLTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587372 122 ERTFSRKWKEIFYTKKIERTFTKDEILKLYVSNIYYGEGAWGIEKAANLYFGKKVNQLTLAESAMMAAVVKAPAYYSPAQ 201
Cdd:pfam00912 81 ERTLTRKLKEAVLALKLERRYSKDEILEAYLNTVYFGRGAYGIEAAARAYFGKDASDLTLAEAALLAGLPQAPSRYNPLR 160
|
170
....*....|....*..
gi 446587372 202 NYDKAVERRNVVLRLME 218
Cdd:pfam00912 161 NPERAKRRRNLVLDRMV 177
|
|
| mrcA |
PRK11636 |
penicillin-binding protein 1a; Provisional |
53-240 |
6.91e-68 |
|
penicillin-binding protein 1a; Provisional
Pssm-ID: 183248 [Multi-domain] Cd Length: 850 Bit Score: 224.62 E-value: 6.91e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587372 53 KLHVPAKL-EVPESLTHAFIATEDKRFYHHNGLDYIAIIRASVENIKAGGVVQGGSTITQQLSKNAFLTNERTFSRKWKE 131
Cdd:PRK11636 64 KRRIPLTLdQIPPEMVKAFIATEDSRFYEHHGVDPVGIFRAASVALFSGHASQGASTITQQLARNFFLSPERTLMRKIKE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587372 132 IFYTKKIERTFTKDEILKLYVSNIYYGEGAWGIEKAANLYFGKKVNQLTLAESAMMAAVVKAPAYYSPAQNYDKAVERRN 211
Cdd:PRK11636 144 AFLAIRIEQLLTKDEILELYLNKIYLGYRAYGVGAAAQVYFGKTVDQLTLSEMAVIAGLPKAPSTFNPLYSMDRAVARRN 223
|
170 180
....*....|....*....|....*....
gi 446587372 212 VVLRLMEKEGYISHDEYVQAVSEKLVIRH 240
Cdd:PRK11636 224 VVLSRMLDEGYITQAQYDQARSEPIVANY 252
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| MrcB |
COG0744 |
Penicillin-binding protein 1B/1F, peptidoglycan transglycosylase/transpeptidase [Cell wall ... |
42-239 |
3.78e-98 |
|
Penicillin-binding protein 1B/1F, peptidoglycan transglycosylase/transpeptidase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440507 [Multi-domain] Cd Length: 630 Bit Score: 299.53 E-value: 3.78e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587372 42 GNVMIEQSDISKLHVPAKlEVPESLTHAFIATEDKRFYHHNGLDYIAIIRASVENIKAGGVVQGGSTITQQLSKNAFLTN 121
Cdd:COG0744 63 GTLIATLGDENREWVPLD-QIPPHLKDAVVAIEDRRFYEHGGVDPKGIARALVANLTAGGVVQGGSTITQQLVKNLFLSN 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587372 122 ERTFSRKWKEIFYTKKIERTFTKDEILKLYVSNIYYGEGAWGIEKAANLYFGKKVNQLTLAESAMMAAVVKAPAYYSPAQ 201
Cdd:COG0744 142 ERTLSRKLKEALLALKLERKYSKDEILELYLNTVYFGRGAYGIEAAAQYYFGKSASDLTLAEAALLAGLVKAPSYYDPYR 221
|
170 180 190
....*....|....*....|....*....|....*...
gi 446587372 202 NYDKAVERRNVVLRLMEKEGYISHDEYVQAVSEKLVIR 239
Cdd:COG0744 222 NPEAAKERRNLVLDRMVEQGYITQAEADAAKAEPLTLV 259
|
|
| MrcA |
COG5009 |
Membrane carboxypeptidase/penicillin-binding protein [Cell wall/membrane/envelope biogenesis]; |
61-245 |
3.82e-93 |
|
Membrane carboxypeptidase/penicillin-binding protein [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 444033 [Multi-domain] Cd Length: 785 Bit Score: 290.52 E-value: 3.82e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587372 61 EVPESLTHAFIATEDKRFYHHNGLDYIAIIRASVENIKAGGVVQGGSTITQQLSKNAFLTNERTFSRKWKEIFYTKKIER 140
Cdd:COG5009 73 EIPPLLINAFLAAEDKRFYEHPGVDPIGIARAAVVNLRTGRRVQGGSTITQQVAKNFLLSPERTLTRKIKEAILALRIEQ 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587372 141 TFTKDEILKLYVSNIYYGEGAWGIEKAANLYFGKKVNQLTLAESAMMAAVVKAPAYYSPAQNYDKAVERRNVVLRLMEKE 220
Cdd:COG5009 153 ELSKDEILELYLNKIYLGHRAYGVAAAAQTYFGKSLDELTLAEAAMLAGLPKAPSRYNPIRNPERALERRNYVLGRMLEL 232
|
170 180
....*....|....*....|....*.
gi 446587372 221 GYISHDEYVQAVSEKLVIR-HDIKIE 245
Cdd:COG5009 233 GYITQAEYEAAKAEPLTARyHGASAE 258
|
|
| PBP_1a_fam |
TIGR02074 |
penicillin-binding protein, 1A family; Bacterial that synthesize a cell wall of peptidoglycan ... |
61-237 |
1.88e-84 |
|
penicillin-binding protein, 1A family; Bacterial that synthesize a cell wall of peptidoglycan (murein) generally have several transglycosylases and transpeptidases for the task. This family consists of bifunctional transglycosylase/transpeptidase penicillin-binding proteins (PBP). In the Proteobacteria, this family includes PBP 1A but not the paralogous PBP 1B (TIGR02071). This family also includes related proteins, often designated PBP 1A, from other bacterial lineages. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 273955 [Multi-domain] Cd Length: 531 Bit Score: 261.43 E-value: 1.88e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587372 61 EVPESLTHAFIATEDKRFYHHNGLDYIAIIRASVENIKAGGVVQGGSTITQQLSKNAFLTNERTFSRKWKEIFYTKKIER 140
Cdd:TIGR02074 9 DIPENLINAFLAIEDRRFYDHFGIDLKGIGRAAVANITSGRVLEGGSTITQQLAKNLYLTNERTITRKIQEALLALKLEQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587372 141 TFTKDEILKLYVSNIYYGEGAWGIEKAANLYFGKKVNQLTLAESAMMAAVVKAPAYYSPAQNYDKAVERRNVVLRLMEKE 220
Cdd:TIGR02074 89 KLSKDEILELYLNRIYFGNGAYGIEAAAQFYFGKSVNDLTLAEAAMLAGLPKAPSAYNPFKNPERAKDRRNLVLSNMVEN 168
|
170
....*....|....*..
gi 446587372 221 GYISHDEYVQAVSEKLV 237
Cdd:TIGR02074 169 GYITAEEAEEAINEPIQ 185
|
|
| Transgly |
pfam00912 |
Transglycosylase; The penicillin-binding proteins are bifunctional proteins consisting of ... |
42-218 |
1.26e-83 |
|
Transglycosylase; The penicillin-binding proteins are bifunctional proteins consisting of transglycosylase and transpeptidase in the N- and C-terminus respectively. The transglycosylase domain catalyzes the polymerization of murein glycan chains.
Pssm-ID: 459993 [Multi-domain] Cd Length: 177 Bit Score: 247.44 E-value: 1.26e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587372 42 GNVMIEQSDISKLHVPAKlEVPESLTHAFIATEDKRFYHHNGLDYIAIIRASVENIKAGGVVQGGSTITQQLSKNAFLTN 121
Cdd:pfam00912 2 GTLLAELGEENREYVPLD-DIPPALKNAVLAIEDRRFYEHGGVDPKGIARALLSNLRSGRIVQGGSTITQQLAKNLFLTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587372 122 ERTFSRKWKEIFYTKKIERTFTKDEILKLYVSNIYYGEGAWGIEKAANLYFGKKVNQLTLAESAMMAAVVKAPAYYSPAQ 201
Cdd:pfam00912 81 ERTLTRKLKEAVLALKLERRYSKDEILEAYLNTVYFGRGAYGIEAAARAYFGKDASDLTLAEAALLAGLPQAPSRYNPLR 160
|
170
....*....|....*..
gi 446587372 202 NYDKAVERRNVVLRLME 218
Cdd:pfam00912 161 NPERAKRRRNLVLDRMV 177
|
|
| mrcA |
PRK11636 |
penicillin-binding protein 1a; Provisional |
53-240 |
6.91e-68 |
|
penicillin-binding protein 1a; Provisional
Pssm-ID: 183248 [Multi-domain] Cd Length: 850 Bit Score: 224.62 E-value: 6.91e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587372 53 KLHVPAKL-EVPESLTHAFIATEDKRFYHHNGLDYIAIIRASVENIKAGGVVQGGSTITQQLSKNAFLTNERTFSRKWKE 131
Cdd:PRK11636 64 KRRIPLTLdQIPPEMVKAFIATEDSRFYEHHGVDPVGIFRAASVALFSGHASQGASTITQQLARNFFLSPERTLMRKIKE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587372 132 IFYTKKIERTFTKDEILKLYVSNIYYGEGAWGIEKAANLYFGKKVNQLTLAESAMMAAVVKAPAYYSPAQNYDKAVERRN 211
Cdd:PRK11636 144 AFLAIRIEQLLTKDEILELYLNKIYLGYRAYGVGAAAQVYFGKTVDQLTLSEMAVIAGLPKAPSTFNPLYSMDRAVARRN 223
|
170 180
....*....|....*....|....*....
gi 446587372 212 VVLRLMEKEGYISHDEYVQAVSEKLVIRH 240
Cdd:PRK11636 224 VVLSRMLDEGYITQAQYDQARSEPIVANY 252
|
|
| PBP_1b |
TIGR02071 |
penicillin-binding protein 1B; Bacterial that synthesize a cell wall of peptidoglycan (murein) ... |
61-236 |
1.18e-57 |
|
penicillin-binding protein 1B; Bacterial that synthesize a cell wall of peptidoglycan (murein) generally have several transglycosylases and transpeptidases for the task. This family consists of a particular bifunctional transglycosylase/transpeptidase in E. coli and other Proteobacteria, designated penicillin-binding protein 1B. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 273952 [Multi-domain] Cd Length: 730 Bit Score: 195.32 E-value: 1.18e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587372 61 EVPESLTHAFIATEDKRFYHHNGLDYIAIIRASVENIKAGGVVQGGSTITQQLSKNAFLTNERTFSRKWKEIFYTKKIER 140
Cdd:TIGR02071 154 QFPELLVDTLLATEDRDFYEHDGISLYSIGRAVWVNLTAGRTVQGGSTLTQQLVKNLFLSNERSLWRKANEAYMALILDA 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587372 141 TFTKDEILKLYVSNIYYG----EGAWGIEKAANLYFGKKVNQLTLAESAMMAAVVKAPAYYSPAQNYDKAVERRNVVLRL 216
Cdd:TIGR02071 234 RYSKDRILELYLNEVYLGqsgdDAIHGFPLASQYYFGRPLGELSLDQVALLVGMVKGPSYYNPWRNPDRALERRNLVLRL 313
|
170 180
....*....|....*....|
gi 446587372 217 MEKEGYISHDEYVQAVSEKL 236
Cdd:TIGR02071 314 LQEQKIIDDEEYDMLSARPL 333
|
|
| PbpC |
COG4953 |
Membrane carboxypeptidase/penicillin-binding protein PbpC [Cell wall/membrane/envelope ... |
61-239 |
7.60e-54 |
|
Membrane carboxypeptidase/penicillin-binding protein PbpC [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 443980 [Multi-domain] Cd Length: 773 Bit Score: 185.42 E-value: 7.60e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587372 61 EVPESLTHAFIATEDKRFYHHNGLDYIAIIRASVENIKAGGVVQGGSTITQQLsknAFLT--NERTFSRKWKEIFYTKKI 138
Cdd:COG4953 72 EVSPRYLQALLAYEDRRFYYHPGVNPLALLRAAWQNLRSGRIVSGGSTLTMQV---ARLLepRPRTLSGKLRQILRALQL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587372 139 ERTFTKDEILKLYVSNIYYGEGAWGIEKAANLYFGKKVNQLTLAESAMMAAVVKAPAYYSPAQNYDKAVERRNVVLRLME 218
Cdd:COG4953 149 ERRYSKDEILELYLNLAPYGGNIEGVEAASLAYFGKPPSRLSLAEAALLAVLPQAPSRRRPDRNPERARAARDRVLARLA 228
|
170 180
....*....|....*....|.
gi 446587372 219 KEGYISHDEYVQAVSEKLVIR 239
Cdd:COG4953 229 EAGVIDAEEAALALLEPVPAR 249
|
|
| mrcB |
PRK09506 |
bifunctional glycosyl transferase/transpeptidase; Reviewed |
63-228 |
7.48e-47 |
|
bifunctional glycosyl transferase/transpeptidase; Reviewed
Pssm-ID: 236544 [Multi-domain] Cd Length: 830 Bit Score: 166.48 E-value: 7.48e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587372 63 PESLTHAFIATEDKRFYHHNGLDYIAIIRASVENIKAGGVVQGGSTITQQLSKNAFLTNERTFSRKWKEIFYTKKIERTF 142
Cdd:PRK09506 220 PDLLVDTLLATEDRHFYEHDGISLYSIGRAVLANLTAGRTVQGGSTLTQQLVKNLFLSNERSLWRKANEAYMALIMDARY 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587372 143 TKDEILKLYVSNIYYGEGA----WGIEKAANLYFGKKVNQLTLAESAMMAAVVKAPAYYSPAQNYDKAVERRNVVLRLME 218
Cdd:PRK09506 300 SKDRILELYLNEVYLGQSGddqiRGFPLASLYYFGRPVEELSLDQQALLVGMVKGASLYNPWRNPKLALERRNLVLRLLQ 379
|
170
....*....|
gi 446587372 219 KEGYISHDEY 228
Cdd:PRK09506 380 QQQIIDQELY 389
|
|
| PRK13481 |
PRK13481 |
glycosyltransferase; Provisional |
62-234 |
1.66e-46 |
|
glycosyltransferase; Provisional
Pssm-ID: 184078 [Multi-domain] Cd Length: 232 Bit Score: 154.96 E-value: 1.66e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587372 62 VPESLTHAFIATEDKRFYHHNGLDYIAIIRASVENIKAGGVvQGGSTITQQLSKNAFLTNERTFSRKWKEIFYTKKIERT 141
Cdd:PRK13481 53 MPEYVKGAFISMEDERFYKHHGFDLKGTTRALFSTISDRDV-QGGSTITQQVVKNYFYDNERSFTRKVKELFVAHRVEKQ 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587372 142 FTKDEILKLYVSNIYYGEGAWGIEKAANLYFGKKVN-------QLTLAESAMMAAVVKAPAYYSPAQNYDKAVERRNVVL 214
Cdd:PRK13481 132 YSKNEILSFYLNNIYFGDNQYTLEGAANHYFGTTVNknsttmsHITVLQSAILASKVNAPSVYNINDMSENFTQRVSTNL 211
|
170 180
....*....|....*....|
gi 446587372 215 RLMEKEGYISHDEYVQAVSE 234
Cdd:PRK13481 212 EKMKQQNYINETQYQQAMSQ 231
|
|
| mono_pep_trsgly |
TIGR02070 |
monofunctional biosynthetic peptidoglycan transglycosylase; This family is one of the ... |
61-217 |
4.87e-41 |
|
monofunctional biosynthetic peptidoglycan transglycosylase; This family is one of the transglycosylases involved in the late stages of peptidoglycan biosynthesis. Members tend to be small, about 240 amino acids in length, and consist almost entirely of a domain described by pfam00912 for transglycosylases. Species with this protein will have several other transglycosylases as well. All species with this protein are Proteobacteria that produce murein (peptidoglycan). [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 273951 [Multi-domain] Cd Length: 224 Bit Score: 140.67 E-value: 4.87e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587372 61 EVPESLTHAFIATEDKRFYHHNGLDYIAIIRASVENIKAGGVVQGGSTITQQLSKNAFLTNERTFSRKWKEIFYTKKIER 140
Cdd:TIGR02070 62 QISPNLKRAVIASEDAKFVEHHGFDWEAIQDALEKNEKSGKVVRGGSTISQQLAKNLFLWSGRSYLRKGLEAWATWMLET 141
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446587372 141 TFTKDEILKLYVSNIYYGEGAWGIEKAANLYFGKKVNQLTLAESAMMAAVVKAPAYYSPAQNYDKAVERRNVVLRLM 217
Cdd:TIGR02070 142 WWSKQRILEVYLNSVEWGNGVFGAEAAARYYFKRSASNLTRGQAARLAAVLPNPKYYDENRPGPYVRRKATWILKQM 218
|
|
| PRK14850 |
PRK14850 |
penicillin-binding protein 1b; Provisional |
53-239 |
1.29e-40 |
|
penicillin-binding protein 1b; Provisional
Pssm-ID: 237835 [Multi-domain] Cd Length: 764 Bit Score: 148.45 E-value: 1.29e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587372 53 KLHVPAKlEVPESLTHAFIATEDKRFYHHNGLDYIAIIRASVENIKAGGVVQGGSTITQQLSKNAFLTNERTFSRKWKEI 132
Cdd:PRK14850 157 RLFIPRN-QYPEMLIKTLLAIEDKYFYEHDGIHLSSIGRAFLVNLMSGHTIQGGSTLTQQLVKNLFLTNTRSLWRKINEI 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587372 133 FYTKKIERTFTKDEILKLYVSNIYYG----EGAWGIEKAANLYFGKKVNQLTLAESAMMAAVVKAPAYYSPAQNYDKAVE 208
Cdd:PRK14850 236 YMALILDRFYSKDRILELYLNEVYLGqdgnEQIRGFPLASIYYFGRPINELNLDQYALLVGMVKGASLYNPWTNPNLTLK 315
|
170 180 190
....*....|....*....|....*....|.
gi 446587372 209 RRNVVLRLMEKEGYISHDEYVQAVSEKLVIR 239
Cdd:PRK14850 316 RRNLVLFLLYKQKVITRKLYKDLCSRPLNVQ 346
|
|
| PRK11240 |
PRK11240 |
penicillin-binding protein 1C; Provisional |
63-221 |
1.90e-25 |
|
penicillin-binding protein 1C; Provisional
Pssm-ID: 183049 [Multi-domain] Cd Length: 772 Bit Score: 104.78 E-value: 1.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587372 63 PESLtHAFIATEDKRFYHHNGLDYIAIIRASVENIKAGGVVQGGSTITQQLsknAFLTN--ERTFSRKWKEIFYTKKIER 140
Cdd:PRK11240 72 PRYL-EALINYEDRWFWKHPGVNPFSVARAAWQDLTSGRVISGGSTLTMQV---ARLLDphPRTFGGKIRQLWRALQLEW 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587372 141 TFTKDEILKLYVSNIYYGEGAWGIEKAANLYFGKKVNQLTLAESAMMAAVVKAPAYYSPAQNYDKAVERRNVVLRLMEKE 220
Cdd:PRK11240 148 HLSKREILTLYLNRAPFGGTLQGIGAASWAYLGKSPANLSYAEAALLAVLPQAPSRLRPDRWPERAEAARNKVLERMAEQ 227
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.
gi 446587372 221 G 221
Cdd:PRK11240 228 G 228
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