NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|612905346|gb|EZV17024|]
View 

monofunctional glycosyltransferase [Staphylococcus aureus 12S00881]

Protein Classification

peptidoglycan glycosyltransferase( domain architecture ID 10014251)

peptidoglycan glycosyltransferase is a polymerase that catalyzes glycan chain elongation using lipid-linked disaccharide-pentapeptide as the substrate

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PRK13481 PRK13481
glycosyltransferase; Provisional
36-267 2.76e-152

glycosyltransferase; Provisional


:

Pssm-ID: 184078 [Multi-domain]  Cd Length: 232  Bit Score: 424.22  E-value: 2.76e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905346  36 KKKSKRILLKILLTILIIIALFIGIMYFLSTRDNVDELRKIENKSSFVSADNMPEYVKGAFISMEDERFYNHHGFDLKGT 115
Cdd:PRK13481   1 KKKSKRILLKILLTILIIIALFIGIMYFLSTRDNVDELRKIENKSSFVSADNMPEYVKGAFISMEDERFYKHHGFDLKGT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905346 116 TRALFSTISDRDVQGGSTITQQVVKNYFYDNDRSFTRKVKELFVAHRVEKQYNKNEILSFYLNNIYFGDNQYTLEGAANH 195
Cdd:PRK13481  81 TRALFSTISDRDVQGGSTITQQVVKNYFYDNERSFTRKVKELFVAHRVEKQYSKNEILSFYLNNIYFGDNQYTLEGAANH 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 612905346 196 YFGTTVNKNSTTMSHITVLQSAILASKVNAPSVYNINNMSENFTQRVSTNLEKMKQQNYINETQYQQAMSQL 267
Cdd:PRK13481 161 YFGTTVNKNSTTMSHITVLQSAILASKVNAPSVYNINDMSENFTQRVSTNLEKMKQQNYINETQYQQAMSQL 232
 
Name Accession Description Interval E-value
PRK13481 PRK13481
glycosyltransferase; Provisional
36-267 2.76e-152

glycosyltransferase; Provisional


Pssm-ID: 184078 [Multi-domain]  Cd Length: 232  Bit Score: 424.22  E-value: 2.76e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905346  36 KKKSKRILLKILLTILIIIALFIGIMYFLSTRDNVDELRKIENKSSFVSADNMPEYVKGAFISMEDERFYNHHGFDLKGT 115
Cdd:PRK13481   1 KKKSKRILLKILLTILIIIALFIGIMYFLSTRDNVDELRKIENKSSFVSADNMPEYVKGAFISMEDERFYKHHGFDLKGT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905346 116 TRALFSTISDRDVQGGSTITQQVVKNYFYDNDRSFTRKVKELFVAHRVEKQYNKNEILSFYLNNIYFGDNQYTLEGAANH 195
Cdd:PRK13481  81 TRALFSTISDRDVQGGSTITQQVVKNYFYDNERSFTRKVKELFVAHRVEKQYSKNEILSFYLNNIYFGDNQYTLEGAANH 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 612905346 196 YFGTTVNKNSTTMSHITVLQSAILASKVNAPSVYNINNMSENFTQRVSTNLEKMKQQNYINETQYQQAMSQL 267
Cdd:PRK13481 161 YFGTTVNKNSTTMSHITVLQSAILASKVNAPSVYNINDMSENFTQRVSTNLEKMKQQNYINETQYQQAMSQL 232
Transgly pfam00912
Transglycosylase; The penicillin-binding proteins are bifunctional proteins consisting of ...
77-250 5.65e-74

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: 223.55  E-value: 5.65e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905346   77 ENKSSFVSADNMPEYVKGAFISMEDERFYNHHGFDLKGTTRALFSTI-SDRDVQGGSTITQQVVKNYFYDNDRSFTRKVK 155
Cdd:pfam00912  10 EENREYVPLDDIPPALKNAVLAIEDRRFYEHGGVDPKGIARALLSNLrSGRIVQGGSTITQQLAKNLFLTPERTLTRKLK 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905346  156 ELFVAHRVEKQYNKNEILSFYLNNIYFGDNQYTLEGAANHYFGTTVnknsttmSHITVLQSAILASKVNAPSVYNINNMS 235
Cdd:pfam00912  90 EAVLALKLERRYSKDEILEAYLNTVYFGRGAYGIEAAARAYFGKDA-------SDLTLAEAALLAGLPQAPSRYNPLRNP 162
                         170
                  ....*....|....*
gi 612905346  236 ENFTQRVSTNLEKMK 250
Cdd:pfam00912 163 ERAKRRRNLVLDRMV 177
MrcB COG0744
Penicillin-binding protein 1B/1F, peptidoglycan transglycosylase/transpeptidase [Cell wall ...
82-266 1.50e-70

Penicillin-binding protein 1B/1F, peptidoglycan transglycosylase/transpeptidase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440507 [Multi-domain]  Cd Length: 630  Bit Score: 228.27  E-value: 1.50e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905346  82 FVSADNMPEYVKGAFISMEDERFYNHHGFDLKGTTRALFSTI-SDRDVQGGSTITQQVVKNYFYDNDRSFTRKVKELFVA 160
Cdd:COG0744   76 WVPLDQIPPHLKDAVVAIEDRRFYEHGGVDPKGIARALVANLtAGGVVQGGSTITQQLVKNLFLSNERTLSRKLKEALLA 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905346 161 HRVEKQYNKNEILSFYLNNIYFGDNQYTLEGAANHYFGTTVNKnsttmshITVLQSAILASKVNAPSVYNINNMSENFTQ 240
Cdd:COG0744  156 LKLERKYSKDEILELYLNTVYFGRGAYGIEAAAQYYFGKSASD-------LTLAEAALLAGLVKAPSYYDPYRNPEAAKE 228
                        170       180
                 ....*....|....*....|....*.
gi 612905346 241 RVSTNLEKMKQQNYINETQYQQAMSQ 266
Cdd:COG0744  229 RRNLVLDRMVEQGYITQAEADAAKAE 254
PBP_1a_fam TIGR02074
penicillin-binding protein, 1A family; Bacterial that synthesize a cell wall of peptidoglycan ...
82-264 8.61e-59

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: 195.17  E-value: 8.61e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905346   82 FVSADNMPEYVKGAFISMEDERFYNHHGFDLKGTTRALFSTI-SDRDVQGGSTITQQVVKNYFYDNDRSFTRKVKELFVA 160
Cdd:TIGR02074   4 YVPIDDIPENLINAFLAIEDRRFYDHFGIDLKGIGRAAVANItSGRVLEGGSTITQQLAKNLYLTNERTITRKIQEALLA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905346  161 HRVEKQYNKNEILSFYLNNIYFGDNQYTLEGAANHYFGTTVNKnsttmshITVLQSAILASKVNAPSVYN-INNMsENFT 239
Cdd:TIGR02074  84 LKLEQKLSKDEILELYLNRIYFGNGAYGIEAAAQFYFGKSVND-------LTLAEAAMLAGLPKAPSAYNpFKNP-ERAK 155
                         170       180
                  ....*....|....*....|....*
gi 612905346  240 QRVSTNLEKMKQQNYINETQYQQAM 264
Cdd:TIGR02074 156 DRRNLVLSNMVENGYITAEEAEEAI 180
 
Name Accession Description Interval E-value
PRK13481 PRK13481
glycosyltransferase; Provisional
36-267 2.76e-152

glycosyltransferase; Provisional


Pssm-ID: 184078 [Multi-domain]  Cd Length: 232  Bit Score: 424.22  E-value: 2.76e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905346  36 KKKSKRILLKILLTILIIIALFIGIMYFLSTRDNVDELRKIENKSSFVSADNMPEYVKGAFISMEDERFYNHHGFDLKGT 115
Cdd:PRK13481   1 KKKSKRILLKILLTILIIIALFIGIMYFLSTRDNVDELRKIENKSSFVSADNMPEYVKGAFISMEDERFYKHHGFDLKGT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905346 116 TRALFSTISDRDVQGGSTITQQVVKNYFYDNDRSFTRKVKELFVAHRVEKQYNKNEILSFYLNNIYFGDNQYTLEGAANH 195
Cdd:PRK13481  81 TRALFSTISDRDVQGGSTITQQVVKNYFYDNERSFTRKVKELFVAHRVEKQYSKNEILSFYLNNIYFGDNQYTLEGAANH 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 612905346 196 YFGTTVNKNSTTMSHITVLQSAILASKVNAPSVYNINNMSENFTQRVSTNLEKMKQQNYINETQYQQAMSQL 267
Cdd:PRK13481 161 YFGTTVNKNSTTMSHITVLQSAILASKVNAPSVYNINDMSENFTQRVSTNLEKMKQQNYINETQYQQAMSQL 232
Transgly pfam00912
Transglycosylase; The penicillin-binding proteins are bifunctional proteins consisting of ...
77-250 5.65e-74

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: 223.55  E-value: 5.65e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905346   77 ENKSSFVSADNMPEYVKGAFISMEDERFYNHHGFDLKGTTRALFSTI-SDRDVQGGSTITQQVVKNYFYDNDRSFTRKVK 155
Cdd:pfam00912  10 EENREYVPLDDIPPALKNAVLAIEDRRFYEHGGVDPKGIARALLSNLrSGRIVQGGSTITQQLAKNLFLTPERTLTRKLK 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905346  156 ELFVAHRVEKQYNKNEILSFYLNNIYFGDNQYTLEGAANHYFGTTVnknsttmSHITVLQSAILASKVNAPSVYNINNMS 235
Cdd:pfam00912  90 EAVLALKLERRYSKDEILEAYLNTVYFGRGAYGIEAAARAYFGKDA-------SDLTLAEAALLAGLPQAPSRYNPLRNP 162
                         170
                  ....*....|....*
gi 612905346  236 ENFTQRVSTNLEKMK 250
Cdd:pfam00912 163 ERAKRRRNLVLDRMV 177
MrcB COG0744
Penicillin-binding protein 1B/1F, peptidoglycan transglycosylase/transpeptidase [Cell wall ...
82-266 1.50e-70

Penicillin-binding protein 1B/1F, peptidoglycan transglycosylase/transpeptidase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440507 [Multi-domain]  Cd Length: 630  Bit Score: 228.27  E-value: 1.50e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905346  82 FVSADNMPEYVKGAFISMEDERFYNHHGFDLKGTTRALFSTI-SDRDVQGGSTITQQVVKNYFYDNDRSFTRKVKELFVA 160
Cdd:COG0744   76 WVPLDQIPPHLKDAVVAIEDRRFYEHGGVDPKGIARALVANLtAGGVVQGGSTITQQLVKNLFLSNERTLSRKLKEALLA 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905346 161 HRVEKQYNKNEILSFYLNNIYFGDNQYTLEGAANHYFGTTVNKnsttmshITVLQSAILASKVNAPSVYNINNMSENFTQ 240
Cdd:COG0744  156 LKLERKYSKDEILELYLNTVYFGRGAYGIEAAAQYYFGKSASD-------LTLAEAALLAGLVKAPSYYDPYRNPEAAKE 228
                        170       180
                 ....*....|....*....|....*.
gi 612905346 241 RVSTNLEKMKQQNYINETQYQQAMSQ 266
Cdd:COG0744  229 RRNLVLDRMVEQGYITQAEADAAKAE 254
MrcA COG5009
Membrane carboxypeptidase/penicillin-binding protein [Cell wall/membrane/envelope biogenesis];
82-266 1.25e-63

Membrane carboxypeptidase/penicillin-binding protein [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 444033 [Multi-domain]  Cd Length: 785  Bit Score: 212.71  E-value: 1.25e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905346  82 FVSADNMPEYVKGAFISMEDERFYNHHGFDLKGTTRALFSTI-SDRDVQGGSTITQQVVKNYFYDNDRSFTRKVKELFVA 160
Cdd:COG5009   68 PVPIEEIPPLLINAFLAAEDKRFYEHPGVDPIGIARAAVVNLrTGRRVQGGSTITQQVAKNFLLSPERTLTRKIKEAILA 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905346 161 HRVEKQYNKNEILSFYLNNIYFGDNQYTLEGAANHYFGTTVNKnsttmshITVLQSAILASKVNAPSVYN-INNMsENFT 239
Cdd:COG5009  148 LRIEQELSKDEILELYLNKIYLGHRAYGVAAAAQTYFGKSLDE-------LTLAEAAMLAGLPKAPSRYNpIRNP-ERAL 219
                        170       180
                 ....*....|....*....|....*..
gi 612905346 240 QRVSTNLEKMKQQNYINETQYQQAMSQ 266
Cdd:COG5009  220 ERRNYVLGRMLELGYITQAEYEAAKAE 246
PBP_1a_fam TIGR02074
penicillin-binding protein, 1A family; Bacterial that synthesize a cell wall of peptidoglycan ...
82-264 8.61e-59

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: 195.17  E-value: 8.61e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905346   82 FVSADNMPEYVKGAFISMEDERFYNHHGFDLKGTTRALFSTI-SDRDVQGGSTITQQVVKNYFYDNDRSFTRKVKELFVA 160
Cdd:TIGR02074   4 YVPIDDIPENLINAFLAIEDRRFYDHFGIDLKGIGRAAVANItSGRVLEGGSTITQQLAKNLYLTNERTITRKIQEALLA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905346  161 HRVEKQYNKNEILSFYLNNIYFGDNQYTLEGAANHYFGTTVNKnsttmshITVLQSAILASKVNAPSVYN-INNMsENFT 239
Cdd:TIGR02074  84 LKLEQKLSKDEILELYLNRIYFGNGAYGIEAAAQFYFGKSVND-------LTLAEAAMLAGLPKAPSAYNpFKNP-ERAK 155
                         170       180
                  ....*....|....*....|....*
gi 612905346  240 QRVSTNLEKMKQQNYINETQYQQAM 264
Cdd:TIGR02074 156 DRRNLVLSNMVENGYITAEEAEEAI 180
mrcA PRK11636
penicillin-binding protein 1a; Provisional
89-266 1.80e-41

penicillin-binding protein 1a; Provisional


Pssm-ID: 183248 [Multi-domain]  Cd Length: 850  Bit Score: 151.44  E-value: 1.80e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905346  89 PEYVKgAFISMEDERFYNHHGFDLKGTTRAL-FSTISDRDVQGGSTITQQVVKNYFYDNDRSFTRKVKELFVAHRVEKQY 167
Cdd:PRK11636  76 PEMVK-AFIATEDSRFYEHHGVDPVGIFRAAsVALFSGHASQGASTITQQLARNFFLSPERTLMRKIKEAFLAIRIEQLL 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905346 168 NKNEILSFYLNNIYFGDNQYTLEGAANHYFGTTVNKnsttmshITVLQSAILASKVNAPSVYNINNMSENFTQRVSTNLE 247
Cdd:PRK11636 155 TKDEILELYLNKIYLGYRAYGVGAAAQVYFGKTVDQ-------LTLSEMAVIAGLPKAPSTFNPLYSMDRAVARRNVVLS 227
                        170
                 ....*....|....*....
gi 612905346 248 KMKQQNYINETQYQQAMSQ 266
Cdd:PRK11636 228 RMLDEGYITQAQYDQARSE 246
mono_pep_trsgly TIGR02070
monofunctional biosynthetic peptidoglycan transglycosylase; This family is one of the ...
82-251 1.27e-31

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: 116.41  E-value: 1.27e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905346   82 FVSADNMPEYVKGAFISMEDERFYNHHGFDLKGTTRAL-FSTISDRDVQGGSTITQQVVKNYFYDNDRSFTRKVKELFVA 160
Cdd:TIGR02070  57 WRPYDQISPNLKRAVIASEDAKFVEHHGFDWEAIQDALeKNEKSGKVVRGGSTISQQLAKNLFLWSGRSYLRKGLEAWAT 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905346  161 HRVEKQYNKNEILSFYLNNIYFGDNQYTLEGAANHYFGTTVnknsttmSHITVLQSAILASKVNAPSVYNINNMSENFTQ 240
Cdd:TIGR02070 137 WMLETWWSKQRILEVYLNSVEWGNGVFGAEAAARYYFKRSA-------SNLTRGQAARLAAVLPNPKYYDENRPGPYVRR 209
                         170
                  ....*....|.
gi 612905346  241 RVSTNLEKMKQ 251
Cdd:TIGR02070 210 KATWILKQMGY 220
PbpC COG4953
Membrane carboxypeptidase/penicillin-binding protein PbpC [Cell wall/membrane/envelope ...
83-264 9.62e-31

Membrane carboxypeptidase/penicillin-binding protein PbpC [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443980 [Multi-domain]  Cd Length: 773  Bit Score: 120.71  E-value: 9.62e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905346  83 VSADNMPEYVKGAFISMEDERFYNHHGFDLKGTTRALFSTI-SDRDVQGGSTITQQVVKnYFYDNDRSFTRKVKELFVAH 161
Cdd:COG4953   68 VPLDEVSPRYLQALLAYEDRRFYYHPGVNPLALLRAAWQNLrSGRIVSGGSTLTMQVAR-LLEPRPRTLSGKLRQILRAL 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905346 162 RVEKQYNKNEILSFYLNNIYFGDNQYTLEGAANHYFGTTVnknsttmSHITVLQSAILASKVNAPSVYNINNMSENFTQ- 240
Cdd:COG4953  147 QLERRYSKDEILELYLNLAPYGGNIEGVEAASLAYFGKPP-------SRLSLAEAALLAVLPQAPSRRRPDRNPERARAa 219
                        170       180
                 ....*....|....*....|....*.
gi 612905346 241 --RVstnLEKMKQQNYINETQYQQAM 264
Cdd:COG4953  220 rdRV---LARLAEAGVIDAEEAALAL 242
PRK14850 PRK14850
penicillin-binding protein 1b; Provisional
79-266 1.13e-26

penicillin-binding protein 1b; Provisional


Pssm-ID: 237835 [Multi-domain]  Cd Length: 764  Bit Score: 108.78  E-value: 1.13e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905346  79 KSSFVSADNMPEYVKGAFISMEDERFYNHHGFDLKGTTRALF-STISDRDVQGGSTITQQVVKNYFYDNDRSFTRKVKEL 157
Cdd:PRK14850 156 KRLFIPRNQYPEMLIKTLLAIEDKYFYEHDGIHLSSIGRAFLvNLMSGHTIQGGSTLTQQLVKNLFLTNTRSLWRKINEI 235
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905346 158 FVAHRVEKQYNKNEILSFYLNNIYFG-DNQYTLEG---AANHYFGTTVNKnsttmshITVLQSAILASKVNAPSVYNINN 233
Cdd:PRK14850 236 YMALILDRFYSKDRILELYLNEVYLGqDGNEQIRGfplASIYYFGRPINE-------LNLDQYALLVGMVKGASLYNPWT 308
                        170       180       190
                 ....*....|....*....|....*....|...
gi 612905346 234 MSENFTQRVSTNLEKMKQQNYINETQYQQAMSQ 266
Cdd:PRK14850 309 NPNLTLKRRNLVLFLLYKQKVITRKLYKDLCSR 341
mrcB PRK09506
bifunctional glycosyl transferase/transpeptidase; Reviewed
82-260 1.46e-26

bifunctional glycosyl transferase/transpeptidase; Reviewed


Pssm-ID: 236544 [Multi-domain]  Cd Length: 830  Bit Score: 108.32  E-value: 1.46e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905346  82 FVSADNMPEYVKGAFISMEDERFYNHHGFDLKGTTRALFSTI-SDRDVQGGSTITQQVVKNYFYDNDRSFTRKVKELFVA 160
Cdd:PRK09506 213 FVPRSGFPDLLVDTLLATEDRHFYEHDGISLYSIGRAVLANLtAGRTVQGGSTLTQQLVKNLFLSNERSLWRKANEAYMA 292
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905346 161 HRVEKQYNKNEILSFYLNNIYF---GDNQytLEG---AANHYFGTTVNKnsttmshITVLQSAILASKVNAPSVYNINNM 234
Cdd:PRK09506 293 LIMDARYSKDRILELYLNEVYLgqsGDDQ--IRGfplASLYYFGRPVEE-------LSLDQQALLVGMVKGASLYNPWRN 363
                        170       180
                 ....*....|....*....|....*.
gi 612905346 235 SENFTQRVSTNLEKMKQQNYINETQY 260
Cdd:PRK09506 364 PKLALERRNLVLRLLQQQQIIDQELY 389
PBP_1c TIGR02073
penicillin-binding protein 1C; This subfamily of the penicillin binding proteins includes the ...
83-269 2.38e-26

penicillin-binding protein 1C; This subfamily of the penicillin binding proteins includes the member from E. coli designated penicillin-binding protein 1C. Members have both transglycosylase and transpeptidase domains and are involved in forming cross-links in the late stages of peptidoglycan biosynthesis. All members of this subfamily are presumed to have the same basic function. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


Pssm-ID: 273954 [Multi-domain]  Cd Length: 727  Bit Score: 107.89  E-value: 2.38e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905346   83 VSADNMPEYVKGAFISMEDERFYNHHGFDLKGTTRALFST-ISDRDVQGGSTITQQVVKNYFYDNDRSFTRKVKELFVAH 161
Cdd:TIGR02073  36 VPLEDISPKFLQALLLYEDKRFYWHPGVNPLALLRAAWQNlTNGRRVSGGSTLTMQLARLLDPELSRTLTGKLRQMWRAI 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905346  162 RVEKQYNKNEILSFYLNNIYFGDNQYTLEGAANHYFGttvnKNSTTMSHItvlQSAILASKVNAPSVYNINNMSENFTQR 241
Cdd:TIGR02073 116 QLEARYSKREILEAYLNLAPYGGNLEGLRAASLIYFG----KEPSSLSLA---EAALLAALPQAPSARRLDRLPKAAKAA 188
                         170       180
                  ....*....|....*....|....*....
gi 612905346  242 VSTNLEKMKQQNYIN-ETQYQQAMSQLNR 269
Cdd:TIGR02073 189 RDRLLDRMVEQGPDDsEQVALAALEPLPA 217
PRK11240 PRK11240
penicillin-binding protein 1C; Provisional
89-227 6.24e-13

penicillin-binding protein 1C; Provisional


Pssm-ID: 183049 [Multi-domain]  Cd Length: 772  Bit Score: 68.19  E-value: 6.24e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905346  89 PEYVKgAFISMEDERFYNHHGFDLKGTTRALFSTI-SDRDVQGGSTITQQVVKnyFYD-NDRSFTRKVKELFVAHRVEKQ 166
Cdd:PRK11240  72 PRYLE-ALINYEDRWFWKHPGVNPFSVARAAWQDLtSGRVISGGSTLTMQVAR--LLDpHPRTFGGKIRQLWRALQLEWH 148
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 612905346 167 YNKNEILSFYLNNIYFGDnqyTLEG---AANHYFGTTVnknsttmSHITVLQSAILASKVNAPS 227
Cdd:PRK11240 149 LSKREILTLYLNRAPFGG---TLQGigaASWAYLGKSP-------ANLSYAEAALLAVLPQAPS 202
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH