|
Name |
Accession |
Description |
Interval |
E-value |
| MrcB |
COG0744 |
Penicillin-binding protein 1B/1F, peptidoglycan transglycosylase/transpeptidase [Cell wall ... |
42-239 |
2.03e-98 |
|
Penicillin-binding protein 1B/1F, peptidoglycan transglycosylase/transpeptidase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440507 [Multi-domain] Cd Length: 630 Bit Score: 300.30 E-value: 2.03e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488019703 42 GNVMIERSDISKLHVPAKlEVPESLTHAFIATEDKRFYHHNGLDYIAIIRASIENIKAGGVVQGGSTITQQLSKNAFLSN 121
Cdd:COG0744 63 GTLIATLGDENREWVPLD-QIPPHLKDAVVAIEDRRFYEHGGVDPKGIARALVANLTAGGVVQGGSTITQQLVKNLFLSN 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488019703 122 ERTFSRKWKEIFYTKKIERTFTKDEILKLYVSNIYYGEGAWGIEKAANLYFGKKVDQLTLAESAMMAAIVKAPAYYSPAQ 201
Cdd:COG0744 142 ERTLSRKLKEALLALKLERKYSKDEILELYLNTVYFGRGAYGIEAAAQYYFGKSASDLTLAEAALLAGLVKAPSYYDPYR 221
|
170 180 190
....*....|....*....|....*....|....*...
gi 488019703 202 NYDKAVERRNVVLRLMEKEGYINHDEYVQAVSEKLVIR 239
Cdd:COG0744 222 NPEAAKERRNLVLDRMVEQGYITQAEADAAKAEPLTLV 259
|
|
| Transgly |
pfam00912 |
Transglycosylase; The penicillin-binding proteins are bifunctional proteins consisting of ... |
42-218 |
4.85e-84 |
|
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: 248.59 E-value: 4.85e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488019703 42 GNVMIERSDISKLHVPAKlEVPESLTHAFIATEDKRFYHHNGLDYIAIIRASIENIKAGGVVQGGSTITQQLSKNAFLSN 121
Cdd:pfam00912 2 GTLLAELGEENREYVPLD-DIPPALKNAVLAIEDRRFYEHGGVDPKGIARALLSNLRSGRIVQGGSTITQQLAKNLFLTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488019703 122 ERTFSRKWKEIFYTKKIERTFTKDEILKLYVSNIYYGEGAWGIEKAANLYFGKKVDQLTLAESAMMAAIVKAPAYYSPAQ 201
Cdd:pfam00912 81 ERTLTRKLKEAVLALKLERRYSKDEILEAYLNTVYFGRGAYGIEAAARAYFGKDASDLTLAEAALLAGLPQAPSRYNPLR 160
|
170
....*....|....*..
gi 488019703 202 NYDKAVERRNVVLRLME 218
Cdd:pfam00912 161 NPERAKRRRNLVLDRMV 177
|
|
| PBP_1a_fam |
TIGR02074 |
penicillin-binding protein, 1A family; Bacterial that synthesize a cell wall of peptidoglycan ... |
61-237 |
8.61e-83 |
|
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: 257.19 E-value: 8.61e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488019703 61 EVPESLTHAFIATEDKRFYHHNGLDYIAIIRASIENIKAGGVVQGGSTITQQLSKNAFLSNERTFSRKWKEIFYTKKIER 140
Cdd:TIGR02074 9 DIPENLINAFLAIEDRRFYDHFGIDLKGIGRAAVANITSGRVLEGGSTITQQLAKNLYLTNERTITRKIQEALLALKLEQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488019703 141 TFTKDEILKLYVSNIYYGEGAWGIEKAANLYFGKKVDQLTLAESAMMAAIVKAPAYYSPAQNYDKAVERRNVVLRLMEKE 220
Cdd:TIGR02074 89 KLSKDEILELYLNRIYFGNGAYGIEAAAQFYFGKSVNDLTLAEAAMLAGLPKAPSAYNPFKNPERAKDRRNLVLSNMVEN 168
|
170
....*....|....*..
gi 488019703 221 GYINHDEYVQAVSEKLV 237
Cdd:TIGR02074 169 GYITAEEAEEAINEPIQ 185
|
|
| mrcA |
PRK11636 |
penicillin-binding protein 1a; Provisional |
53-240 |
4.02e-68 |
|
penicillin-binding protein 1a; Provisional
Pssm-ID: 183248 [Multi-domain] Cd Length: 850 Bit Score: 225.40 E-value: 4.02e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488019703 53 KLHVPAKL-EVPESLTHAFIATEDKRFYHHNGLDYIAIIRASIENIKAGGVVQGGSTITQQLSKNAFLSNERTFSRKWKE 131
Cdd:PRK11636 64 KRRIPLTLdQIPPEMVKAFIATEDSRFYEHHGVDPVGIFRAASVALFSGHASQGASTITQQLARNFFLSPERTLMRKIKE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488019703 132 IFYTKKIERTFTKDEILKLYVSNIYYGEGAWGIEKAANLYFGKKVDQLTLAESAMMAAIVKAPAYYSPAQNYDKAVERRN 211
Cdd:PRK11636 144 AFLAIRIEQLLTKDEILELYLNKIYLGYRAYGVGAAAQVYFGKTVDQLTLSEMAVIAGLPKAPSTFNPLYSMDRAVARRN 223
|
170 180
....*....|....*....|....*....
gi 488019703 212 VVLRLMEKEGYINHDEYVQAVSEKLVIRH 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 |
2.03e-98 |
|
Penicillin-binding protein 1B/1F, peptidoglycan transglycosylase/transpeptidase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440507 [Multi-domain] Cd Length: 630 Bit Score: 300.30 E-value: 2.03e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488019703 42 GNVMIERSDISKLHVPAKlEVPESLTHAFIATEDKRFYHHNGLDYIAIIRASIENIKAGGVVQGGSTITQQLSKNAFLSN 121
Cdd:COG0744 63 GTLIATLGDENREWVPLD-QIPPHLKDAVVAIEDRRFYEHGGVDPKGIARALVANLTAGGVVQGGSTITQQLVKNLFLSN 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488019703 122 ERTFSRKWKEIFYTKKIERTFTKDEILKLYVSNIYYGEGAWGIEKAANLYFGKKVDQLTLAESAMMAAIVKAPAYYSPAQ 201
Cdd:COG0744 142 ERTLSRKLKEALLALKLERKYSKDEILELYLNTVYFGRGAYGIEAAAQYYFGKSASDLTLAEAALLAGLVKAPSYYDPYR 221
|
170 180 190
....*....|....*....|....*....|....*...
gi 488019703 202 NYDKAVERRNVVLRLMEKEGYINHDEYVQAVSEKLVIR 239
Cdd:COG0744 222 NPEAAKERRNLVLDRMVEQGYITQAEADAAKAEPLTLV 259
|
|
| MrcA |
COG5009 |
Membrane carboxypeptidase/penicillin-binding protein [Cell wall/membrane/envelope biogenesis]; |
61-239 |
5.31e-93 |
|
Membrane carboxypeptidase/penicillin-binding protein [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 444033 [Multi-domain] Cd Length: 785 Bit Score: 290.14 E-value: 5.31e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488019703 61 EVPESLTHAFIATEDKRFYHHNGLDYIAIIRASIENIKAGGVVQGGSTITQQLSKNAFLSNERTFSRKWKEIFYTKKIER 140
Cdd:COG5009 73 EIPPLLINAFLAAEDKRFYEHPGVDPIGIARAAVVNLRTGRRVQGGSTITQQVAKNFLLSPERTLTRKIKEAILALRIEQ 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488019703 141 TFTKDEILKLYVSNIYYGEGAWGIEKAANLYFGKKVDQLTLAESAMMAAIVKAPAYYSPAQNYDKAVERRNVVLRLMEKE 220
Cdd:COG5009 153 ELSKDEILELYLNKIYLGHRAYGVAAAAQTYFGKSLDELTLAEAAMLAGLPKAPSRYNPIRNPERALERRNYVLGRMLEL 232
|
170
....*....|....*....
gi 488019703 221 GYINHDEYVQAVSEKLVIR 239
Cdd:COG5009 233 GYITQAEYEAAKAEPLTAR 251
|
|
| Transgly |
pfam00912 |
Transglycosylase; The penicillin-binding proteins are bifunctional proteins consisting of ... |
42-218 |
4.85e-84 |
|
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: 248.59 E-value: 4.85e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488019703 42 GNVMIERSDISKLHVPAKlEVPESLTHAFIATEDKRFYHHNGLDYIAIIRASIENIKAGGVVQGGSTITQQLSKNAFLSN 121
Cdd:pfam00912 2 GTLLAELGEENREYVPLD-DIPPALKNAVLAIEDRRFYEHGGVDPKGIARALLSNLRSGRIVQGGSTITQQLAKNLFLTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488019703 122 ERTFSRKWKEIFYTKKIERTFTKDEILKLYVSNIYYGEGAWGIEKAANLYFGKKVDQLTLAESAMMAAIVKAPAYYSPAQ 201
Cdd:pfam00912 81 ERTLTRKLKEAVLALKLERRYSKDEILEAYLNTVYFGRGAYGIEAAARAYFGKDASDLTLAEAALLAGLPQAPSRYNPLR 160
|
170
....*....|....*..
gi 488019703 202 NYDKAVERRNVVLRLME 218
Cdd:pfam00912 161 NPERAKRRRNLVLDRMV 177
|
|
| PBP_1a_fam |
TIGR02074 |
penicillin-binding protein, 1A family; Bacterial that synthesize a cell wall of peptidoglycan ... |
61-237 |
8.61e-83 |
|
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: 257.19 E-value: 8.61e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488019703 61 EVPESLTHAFIATEDKRFYHHNGLDYIAIIRASIENIKAGGVVQGGSTITQQLSKNAFLSNERTFSRKWKEIFYTKKIER 140
Cdd:TIGR02074 9 DIPENLINAFLAIEDRRFYDHFGIDLKGIGRAAVANITSGRVLEGGSTITQQLAKNLYLTNERTITRKIQEALLALKLEQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488019703 141 TFTKDEILKLYVSNIYYGEGAWGIEKAANLYFGKKVDQLTLAESAMMAAIVKAPAYYSPAQNYDKAVERRNVVLRLMEKE 220
Cdd:TIGR02074 89 KLSKDEILELYLNRIYFGNGAYGIEAAAQFYFGKSVNDLTLAEAAMLAGLPKAPSAYNPFKNPERAKDRRNLVLSNMVEN 168
|
170
....*....|....*..
gi 488019703 221 GYINHDEYVQAVSEKLV 237
Cdd:TIGR02074 169 GYITAEEAEEAINEPIQ 185
|
|
| mrcA |
PRK11636 |
penicillin-binding protein 1a; Provisional |
53-240 |
4.02e-68 |
|
penicillin-binding protein 1a; Provisional
Pssm-ID: 183248 [Multi-domain] Cd Length: 850 Bit Score: 225.40 E-value: 4.02e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488019703 53 KLHVPAKL-EVPESLTHAFIATEDKRFYHHNGLDYIAIIRASIENIKAGGVVQGGSTITQQLSKNAFLSNERTFSRKWKE 131
Cdd:PRK11636 64 KRRIPLTLdQIPPEMVKAFIATEDSRFYEHHGVDPVGIFRAASVALFSGHASQGASTITQQLARNFFLSPERTLMRKIKE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488019703 132 IFYTKKIERTFTKDEILKLYVSNIYYGEGAWGIEKAANLYFGKKVDQLTLAESAMMAAIVKAPAYYSPAQNYDKAVERRN 211
Cdd:PRK11636 144 AFLAIRIEQLLTKDEILELYLNKIYLGYRAYGVGAAAQVYFGKTVDQLTLSEMAVIAGLPKAPSTFNPLYSMDRAVARRN 223
|
170 180
....*....|....*....|....*....
gi 488019703 212 VVLRLMEKEGYINHDEYVQAVSEKLVIRH 240
Cdd:PRK11636 224 VVLSRMLDEGYITQAQYDQARSEPIVANY 252
|
|
| PBP_1b |
TIGR02071 |
penicillin-binding protein 1B; Bacterial that synthesize a cell wall of peptidoglycan (murein) ... |
61-236 |
9.95e-58 |
|
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: 195.71 E-value: 9.95e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488019703 61 EVPESLTHAFIATEDKRFYHHNGLDYIAIIRASIENIKAGGVVQGGSTITQQLSKNAFLSNERTFSRKWKEIFYTKKIER 140
Cdd:TIGR02071 154 QFPELLVDTLLATEDRDFYEHDGISLYSIGRAVWVNLTAGRTVQGGSTLTQQLVKNLFLSNERSLWRKANEAYMALILDA 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488019703 141 TFTKDEILKLYVSNIYYG----EGAWGIEKAANLYFGKKVDQLTLAESAMMAAIVKAPAYYSPAQNYDKAVERRNVVLRL 216
Cdd:TIGR02071 234 RYSKDRILELYLNEVYLGqsgdDAIHGFPLASQYYFGRPLGELSLDQVALLVGMVKGPSYYNPWRNPDRALERRNLVLRL 313
|
170 180
....*....|....*....|
gi 488019703 217 MEKEGYINHDEYVQAVSEKL 236
Cdd:TIGR02071 314 LQEQKIIDDEEYDMLSARPL 333
|
|
| PbpC |
COG4953 |
Membrane carboxypeptidase/penicillin-binding protein PbpC [Cell wall/membrane/envelope ... |
61-239 |
2.71e-54 |
|
Membrane carboxypeptidase/penicillin-binding protein PbpC [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 443980 [Multi-domain] Cd Length: 773 Bit Score: 186.58 E-value: 2.71e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488019703 61 EVPESLTHAFIATEDKRFYHHNGLDYIAIIRASIENIKAGGVVQGGSTITQQLsknAFLS--NERTFSRKWKEIFYTKKI 138
Cdd:COG4953 72 EVSPRYLQALLAYEDRRFYYHPGVNPLALLRAAWQNLRSGRIVSGGSTLTMQV---ARLLepRPRTLSGKLRQILRALQL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488019703 139 ERTFTKDEILKLYVSNIYYGEGAWGIEKAANLYFGKKVDQLTLAESAMMAAIVKAPAYYSPAQNYDKAVERRNVVLRLME 218
Cdd:COG4953 149 ERRYSKDEILELYLNLAPYGGNIEGVEAASLAYFGKPPSRLSLAEAALLAVLPQAPSRRRPDRNPERARAARDRVLARLA 228
|
170 180
....*....|....*....|.
gi 488019703 219 KEGYINHDEYVQAVSEKLVIR 239
Cdd:COG4953 229 EAGVIDAEEAALALLEPVPAR 249
|
|
| mrcB |
PRK09506 |
bifunctional glycosyl transferase/transpeptidase; Reviewed |
63-228 |
5.35e-47 |
|
bifunctional glycosyl transferase/transpeptidase; Reviewed
Pssm-ID: 236544 [Multi-domain] Cd Length: 830 Bit Score: 166.87 E-value: 5.35e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488019703 63 PESLTHAFIATEDKRFYHHNGLDYIAIIRASIENIKAGGVVQGGSTITQQLSKNAFLSNERTFSRKWKEIFYTKKIERTF 142
Cdd:PRK09506 220 PDLLVDTLLATEDRHFYEHDGISLYSIGRAVLANLTAGRTVQGGSTLTQQLVKNLFLSNERSLWRKANEAYMALIMDARY 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488019703 143 TKDEILKLYVSNIYYGEGA----WGIEKAANLYFGKKVDQLTLAESAMMAAIVKAPAYYSPAQNYDKAVERRNVVLRLME 218
Cdd:PRK09506 300 SKDRILELYLNEVYLGQSGddqiRGFPLASLYYFGRPVEELSLDQQALLVGMVKGASLYNPWRNPKLALERRNLVLRLLQ 379
|
170
....*....|
gi 488019703 219 KEGYINHDEY 228
Cdd:PRK09506 380 QQQIIDQELY 389
|
|
| PRK13481 |
PRK13481 |
glycosyltransferase; Provisional |
62-234 |
9.05e-47 |
|
glycosyltransferase; Provisional
Pssm-ID: 184078 [Multi-domain] Cd Length: 232 Bit Score: 155.73 E-value: 9.05e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488019703 62 VPESLTHAFIATEDKRFYHHNGLDYIAIIRASIENIKAGGVvQGGSTITQQLSKNAFLSNERTFSRKWKEIFYTKKIERT 141
Cdd:PRK13481 53 MPEYVKGAFISMEDERFYKHHGFDLKGTTRALFSTISDRDV-QGGSTITQQVVKNYFYDNERSFTRKVKELFVAHRVEKQ 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488019703 142 FTKDEILKLYVSNIYYGEGAWGIEKAANLYFGKKVD-------QLTLAESAMMAAIVKAPAYYSPAQNYDKAVERRNVVL 214
Cdd:PRK13481 132 YSKNEILSFYLNNIYFGDNQYTLEGAANHYFGTTVNknsttmsHITVLQSAILASKVNAPSVYNINDMSENFTQRVSTNL 211
|
170 180
....*....|....*....|
gi 488019703 215 RLMEKEGYINHDEYVQAVSE 234
Cdd:PRK13481 212 EKMKQQNYINETQYQQAMSQ 231
|
|
| mono_pep_trsgly |
TIGR02070 |
monofunctional biosynthetic peptidoglycan transglycosylase; This family is one of the ... |
61-217 |
1.83e-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: 141.83 E-value: 1.83e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488019703 61 EVPESLTHAFIATEDKRFYHHNGLDYIAIIRASIENIKAGGVVQGGSTITQQLSKNAFLSNERTFSRKWKEIFYTKKIER 140
Cdd:TIGR02070 62 QISPNLKRAVIASEDAKFVEHHGFDWEAIQDALEKNEKSGKVVRGGSTISQQLAKNLFLWSGRSYLRKGLEAWATWMLET 141
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488019703 141 TFTKDEILKLYVSNIYYGEGAWGIEKAANLYFGKKVDQLTLAESAMMAAIVKAPAYYSPAQNYDKAVERRNVVLRLM 217
Cdd:TIGR02070 142 WWSKQRILEVYLNSVEWGNGVFGAEAAARYYFKRSASNLTRGQAARLAAVLPNPKYYDENRPGPYVRRKATWILKQM 218
|
|
| PRK14850 |
PRK14850 |
penicillin-binding protein 1b; Provisional |
53-239 |
4.34e-41 |
|
penicillin-binding protein 1b; Provisional
Pssm-ID: 237835 [Multi-domain] Cd Length: 764 Bit Score: 150.00 E-value: 4.34e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488019703 53 KLHVPAKlEVPESLTHAFIATEDKRFYHHNGLDYIAIIRASIENIKAGGVVQGGSTITQQLSKNAFLSNERTFSRKWKEI 132
Cdd:PRK14850 157 RLFIPRN-QYPEMLIKTLLAIEDKYFYEHDGIHLSSIGRAFLVNLMSGHTIQGGSTLTQQLVKNLFLTNTRSLWRKINEI 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488019703 133 FYTKKIERTFTKDEILKLYVSNIYYG----EGAWGIEKAANLYFGKKVDQLTLAESAMMAAIVKAPAYYSPAQNYDKAVE 208
Cdd:PRK14850 236 YMALILDRFYSKDRILELYLNEVYLGqdgnEQIRGFPLASIYYFGRPINELNLDQYALLVGMVKGASLYNPWTNPNLTLK 315
|
170 180 190
....*....|....*....|....*....|.
gi 488019703 209 RRNVVLRLMEKEGYINHDEYVQAVSEKLVIR 239
Cdd:PRK14850 316 RRNLVLFLLYKQKVITRKLYKDLCSRPLNVQ 346
|
|
| PRK11240 |
PRK11240 |
penicillin-binding protein 1C; Provisional |
63-221 |
1.64e-25 |
|
penicillin-binding protein 1C; Provisional
Pssm-ID: 183049 [Multi-domain] Cd Length: 772 Bit Score: 105.17 E-value: 1.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488019703 63 PESLtHAFIATEDKRFYHHNGLDYIAIIRASIENIKAGGVVQGGSTITQQLSKnaFLS-NERTFSRKWKEIFYTKKIERT 141
Cdd:PRK11240 72 PRYL-EALINYEDRWFWKHPGVNPFSVARAAWQDLTSGRVISGGSTLTMQVAR--LLDpHPRTFGGKIRQLWRALQLEWH 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488019703 142 FTKDEILKLYVSNIYYGEGAWGIEKAANLYFGKKVDQLTLAESAMMAAIVKAPAYYSPAQNYDKAVERRNVVLRLMEKEG 221
Cdd:PRK11240 149 LSKREILTLYLNRAPFGGTLQGIGAASWAYLGKSPANLSYAEAALLAVLPQAPSRLRPDRWPERAEAARNKVLERMAEQG 228
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