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Conserved domains on  [gi|2443851657|ref|WP_273383678|]
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monofunctional biosynthetic peptidoglycan transglycosylase [Actinobacillus porcinus]

Protein Classification

biosynthetic peptidoglycan transglycosylase( domain architecture ID 1001727)

biosynthetic peptidoglycan transglycosylase is involved in the final stages of peptidoglycan synthesis

CATH:  1.10.3810.10
Gene Ontology:  GO:0071555|GO:0008955|GO:0009252|GO:0008360
PubMed:  8830253
SCOP:  4002510

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK13481 super family cl29529
glycosyltransferase; Provisional
 45-247 1.71e-103

glycosyltransferase; Provisional


The actual alignment was detected with superfamily member TIGR02070:

Pssm-ID: 475222 [Multi-domain]  Cd Length: 224  Bit Score: 299.76  E-value: 1.71e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443851657  45 LAITLFFRFVPLPFSAYMVQQKVSRLLQLNLSDEMHYNWVSLDQISPNMQLAVIAAEDQRFPTHWGFDWNAIEKALEHNE 124
Cdd:TIGR02070  19 FAALASWRFVPPPSTAFMVAEKLALWGQGDPTCGIQHRWRPYDQISPNLKRAVIASEDAKFVEHHGFDWEAIQDALEKNE 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443851657 125 KS-KRIRGGSTISQQTAKNLYLWHGQSWLRKGLEVPVTITLELLWSKKRILEVYLNIAEFGKGIFGVEAASRFYFKKAAK 203
Cdd:TIGR02070  99 KSgKVVRGGSTISQQLAKNLFLWSGRSYLRKGLEAWATWMLETWWSKQRILEVYLNSVEWGNGVFGAEAAARYYFKRSAS 178

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2443851657 204 NLTQSEAALLAAVLPNPIIYKVNAPSALVKRKQAWIMRQMNGLG 247
Cdd:TIGR02070 179 NLTRGQAARLAAVLPNPKYYDENRPGPYVRRKATWILKQMGYLG 222
 
Name Accession Description Interval E-value
mono_pep_trsgly TIGR02070
monofunctional biosynthetic peptidoglycan transglycosylase; This family is one of the ...
 45-247 1.71e-103

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: 299.76  E-value: 1.71e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443851657  45 LAITLFFRFVPLPFSAYMVQQKVSRLLQLNLSDEMHYNWVSLDQISPNMQLAVIAAEDQRFPTHWGFDWNAIEKALEHNE 124
Cdd:TIGR02070  19 FAALASWRFVPPPSTAFMVAEKLALWGQGDPTCGIQHRWRPYDQISPNLKRAVIASEDAKFVEHHGFDWEAIQDALEKNE 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443851657 125 KS-KRIRGGSTISQQTAKNLYLWHGQSWLRKGLEVPVTITLELLWSKKRILEVYLNIAEFGKGIFGVEAASRFYFKKAAK 203
Cdd:TIGR02070  99 KSgKVVRGGSTISQQLAKNLFLWSGRSYLRKGLEAWATWMLETWWSKQRILEVYLNSVEWGNGVFGAEAAARYYFKRSAS 178

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2443851657 204 NLTQSEAALLAAVLPNPIIYKVNAPSALVKRKQAWIMRQMNGLG 247
Cdd:TIGR02070 179 NLTRGQAARLAAVLPNPKYYDENRPGPYVRRKATWILKQMGYLG 222
Transgly pfam00912
Transglycosylase; The penicillin-binding proteins are bifunctional proteins consisting of ...
 83-244 4.66e-71

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: 215.46  E-value: 4.66e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443851657  83 WVSLDQISPNMQLAVIAAEDQRFPTHWGFDWNAIEKALEHNEKSKRI-RGGSTISQQTAKNLYLWHGQSWLRKGLEVPVT 161
Cdd:pfam00912  15 YVPLDDIPPALKNAVLAIEDRRFYEHGGVDPKGIARALLSNLRSGRIvQGGSTITQQLAKNLFLTPERTLTRKLKEAVLA 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443851657 162 ITLELLWSKKRILEVYLNIAEFGKGIFGVEAASRFYFKKAAKNLTQSEAALLAAVLPNPIIYKVNAPSALVKRKQAWIMR 241
Cdd:pfam00912  95 LKLERRYSKDEILEAYLNTVYFGRGAYGIEAAARAYFGKDASDLTLAEAALLAGLPQAPSRYNPLRNPERAKRRRNLVLD 174


                  ...
gi 2443851657 242 QMN 244
Cdd:pfam00912 175 RMV 177
MrcB COG0744
Penicillin-binding protein 1B/1F, peptidoglycan transglycosylase/transpeptidase [Cell wall ...
 1-248 1.97e-70

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


Pssm-ID: 440507 [Multi-domain]  Cd Length: 630  Bit Score: 227.50  E-value: 1.97e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443851657   1 MLKRKNNLFSLKILRTFFRLGrsliqrktkgkcgrfFARFFIAFLAITLFFRFVPLPFSAYM---VQQKVSRLLQLN--- 74
Cdd:COG0744     1 MAKPRRGKRLLRRLLGLLLLL---------------LAVLVLAALAGLVALYVADLPDPEELedlALPQTSTIYDRDgtl 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443851657  75 ---LSDEmHYNWVSLDQISPNMQLAVIAAEDQRFPTHWGFDWNAIEKALEHNEKSKRIR-GGSTISQQTAKNLYLWHGQS 150
Cdd:COG0744    66 iatLGDE-NREWVPLDQIPPHLKDAVVAIEDRRFYEHGGVDPKGIARALVANLTAGGVVqGGSTITQQLVKNLFLSNERT 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443851657 151 WLRKGLEVPVTITLELLWSKKRILEVYLNIAEFGKGIFGVEAASRFYFKKAAKNLTQSEAALLAAVLPNPIIYKVNAPSA 230
Cdd:COG0744   145 LSRKLKEALLALKLERKYSKDEILELYLNTVYFGRGAYGIEAAAQYYFGKSASDLTLAEAALLAGLVKAPSYYDPYRNPE 224

                         250
                  ....*....|....*...
gi 2443851657 231 LVKRKQAWIMRQMNGLGK 248
Cdd:COG0744   225 AAKERRNLVLDRMVEQGY 242
PRK13481 PRK13481
glycosyltransferase; Provisional
 82-226 3.04e-23

glycosyltransferase; Provisional


Pssm-ID: 184078 [Multi-domain]  Cd Length: 232  Bit Score: 94.10  E-value: 3.04e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443851657  82 NWVSLDQISPNMQLAVIAAEDQRFPTHWGFDWNAIEKALEHNEKSKRIRGGSTISQQTAKNLYLWHGQSWLRKGLEVPVT 161
Cdd:PRK13481   46 SFVSADNMPEYVKGAFISMEDERFYKHHGFDLKGTTRALFSTISDRDVQGGSTITQQVVKNYFYDNERSFTRKVKELFVA 125

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2443851657 162 ITLELLWSKKRILEVYLNIAEFGKGIFGVEAASRFYF----KKAAKNLTQS---EAALLAAVLPNPIIYKVN 226
Cdd:PRK13481  126 HRVEKQYSKNEILSFYLNNIYFGDNQYTLEGAANHYFgttvNKNSTTMSHItvlQSAILASKVNAPSVYNIN 197
 
Name Accession Description Interval E-value
mono_pep_trsgly TIGR02070
monofunctional biosynthetic peptidoglycan transglycosylase; This family is one of the ...
 45-247 1.71e-103

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: 299.76  E-value: 1.71e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443851657  45 LAITLFFRFVPLPFSAYMVQQKVSRLLQLNLSDEMHYNWVSLDQISPNMQLAVIAAEDQRFPTHWGFDWNAIEKALEHNE 124
Cdd:TIGR02070  19 FAALASWRFVPPPSTAFMVAEKLALWGQGDPTCGIQHRWRPYDQISPNLKRAVIASEDAKFVEHHGFDWEAIQDALEKNE 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443851657 125 KS-KRIRGGSTISQQTAKNLYLWHGQSWLRKGLEVPVTITLELLWSKKRILEVYLNIAEFGKGIFGVEAASRFYFKKAAK 203
Cdd:TIGR02070  99 KSgKVVRGGSTISQQLAKNLFLWSGRSYLRKGLEAWATWMLETWWSKQRILEVYLNSVEWGNGVFGAEAAARYYFKRSAS 178

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2443851657 204 NLTQSEAALLAAVLPNPIIYKVNAPSALVKRKQAWIMRQMNGLG 247
Cdd:TIGR02070 179 NLTRGQAARLAAVLPNPKYYDENRPGPYVRRKATWILKQMGYLG 222
Transgly pfam00912
Transglycosylase; The penicillin-binding proteins are bifunctional proteins consisting of ...
 83-244 4.66e-71

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: 215.46  E-value: 4.66e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443851657  83 WVSLDQISPNMQLAVIAAEDQRFPTHWGFDWNAIEKALEHNEKSKRI-RGGSTISQQTAKNLYLWHGQSWLRKGLEVPVT 161
Cdd:pfam00912  15 YVPLDDIPPALKNAVLAIEDRRFYEHGGVDPKGIARALLSNLRSGRIvQGGSTITQQLAKNLFLTPERTLTRKLKEAVLA 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443851657 162 ITLELLWSKKRILEVYLNIAEFGKGIFGVEAASRFYFKKAAKNLTQSEAALLAAVLPNPIIYKVNAPSALVKRKQAWIMR 241
Cdd:pfam00912  95 LKLERRYSKDEILEAYLNTVYFGRGAYGIEAAARAYFGKDASDLTLAEAALLAGLPQAPSRYNPLRNPERAKRRRNLVLD 174


                  ...
gi 2443851657 242 QMN 244
Cdd:pfam00912 175 RMV 177
MrcB COG0744
Penicillin-binding protein 1B/1F, peptidoglycan transglycosylase/transpeptidase [Cell wall ...
 1-248 1.97e-70

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


Pssm-ID: 440507 [Multi-domain]  Cd Length: 630  Bit Score: 227.50  E-value: 1.97e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443851657   1 MLKRKNNLFSLKILRTFFRLGrsliqrktkgkcgrfFARFFIAFLAITLFFRFVPLPFSAYM---VQQKVSRLLQLN--- 74
Cdd:COG0744     1 MAKPRRGKRLLRRLLGLLLLL---------------LAVLVLAALAGLVALYVADLPDPEELedlALPQTSTIYDRDgtl 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443851657  75 ---LSDEmHYNWVSLDQISPNMQLAVIAAEDQRFPTHWGFDWNAIEKALEHNEKSKRIR-GGSTISQQTAKNLYLWHGQS 150
Cdd:COG0744    66 iatLGDE-NREWVPLDQIPPHLKDAVVAIEDRRFYEHGGVDPKGIARALVANLTAGGVVqGGSTITQQLVKNLFLSNERT 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443851657 151 WLRKGLEVPVTITLELLWSKKRILEVYLNIAEFGKGIFGVEAASRFYFKKAAKNLTQSEAALLAAVLPNPIIYKVNAPSA 230
Cdd:COG0744   145 LSRKLKEALLALKLERKYSKDEILELYLNTVYFGRGAYGIEAAAQYYFGKSASDLTLAEAALLAGLVKAPSYYDPYRNPE 224

                         250
                  ....*....|....*...
gi 2443851657 231 LVKRKQAWIMRQMNGLGK 248
Cdd:COG0744   225 AAKERRNLVLDRMVEQGY 242
PBP_1a_fam TIGR02074
penicillin-binding protein, 1A family; Bacterial that synthesize a cell wall of peptidoglycan ...
 83-223 1.62e-47

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: 164.74  E-value: 1.62e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443851657  83 WVSLDQISPNMQLAVIAAEDQRFPTHWGFDWNAIEKALEHNEKSKR-IRGGSTISQQTAKNLYLWHGQSWLRKGLEVPVT 161
Cdd:TIGR02074   4 YVPIDDIPENLINAFLAIEDRRFYDHFGIDLKGIGRAAVANITSGRvLEGGSTITQQLAKNLYLTNERTITRKIQEALLA 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2443851657 162 ITLELLWSKKRILEVYLNIAEFGKGIFGVEAASRFYFKKAAKNLTQSEAALLAAVLPNPIIY 223
Cdd:TIGR02074  84 LKLEQKLSKDEILELYLNRIYFGNGAYGIEAAAQFYFGKSVNDLTLAEAAMLAGLPKAPSAY 145
MrcA COG5009
Membrane carboxypeptidase/penicillin-binding protein [Cell wall/membrane/envelope biogenesis];
83-248 1.14e-44

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


Pssm-ID: 444033 [Multi-domain]  Cd Length: 785  Bit Score: 159.94  E-value: 1.14e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443851657  83 WVSLDQISPNMQLAVIAAEDQRFPTHWGFDWNAIEKALEHNEKSKRI-RGGSTISQQTAKNLYLWHGQSWLRKGLEVPVT 161
Cdd:COG5009    68 PVPIEEIPPLLINAFLAAEDKRFYEHPGVDPIGIARAAVVNLRTGRRvQGGSTITQQVAKNFLLSPERTLTRKIKEAILA 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443851657 162 ITLELLWSKKRILEVYLNIAEFGKGIFGVEAASRFYFKKAAKNLTQSEAALLAAVLPNPIIY-KVNAPSALVKRkQAWIM 240
Cdd:COG5009   148 LRIEQELSKDEILELYLNKIYLGHRAYGVAAAAQTYFGKSLDELTLAEAAMLAGLPKAPSRYnPIRNPERALER-RNYVL 226


                  ....*...
gi 2443851657 241 RQMNGLGK 248
Cdd:COG5009   227 GRMLELGY 234
PbpC COG4953
Membrane carboxypeptidase/penicillin-binding protein PbpC [Cell wall/membrane/envelope ...
 45-231 2.71e-40

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


Pssm-ID: 443980 [Multi-domain]  Cd Length: 773  Bit Score: 147.29  E-value: 2.71e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443851657  45 LAITLFFRFVPLPFSAymvQQKVSR--------LLQLNL-SDEMHYNWVSLDQISPNMQLAVIAAEDQRFPTHWGFDWNA 115
Cdd:COG4953    23 LALWALDRLFPLPLLF---AVPYSTvvldrdgtLLRAFLaADGQWRLPVPLDEVSPRYLQALLAYEDRRFYYHPGVNPLA 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443851657 116 IEKALEHNEKSKRI-RGGSTISQQTAKnLyLW-HGQSWLRKGLEVPVTITLELLWSKKRILEVYLNIAEFGKGIFGVEAA 193
Cdd:COG4953   100 LLRAAWQNLRSGRIvSGGSTLTMQVAR-L-LEpRPRTLSGKLRQILRALQLERRYSKDEILELYLNLAPYGGNIEGVEAA 177

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2443851657 194 SRFYFKKAAKNLTQSEAALLaAVLPnpiiykvNAPSAL 231
Cdd:COG4953   178 SLAYFGKPPSRLSLAEAALL-AVLP-------QAPSRR 207
PRK13481 PRK13481
glycosyltransferase; Provisional
 82-226 3.04e-23

glycosyltransferase; Provisional


Pssm-ID: 184078 [Multi-domain]  Cd Length: 232  Bit Score: 94.10  E-value: 3.04e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443851657  82 NWVSLDQISPNMQLAVIAAEDQRFPTHWGFDWNAIEKALEHNEKSKRIRGGSTISQQTAKNLYLWHGQSWLRKGLEVPVT 161
Cdd:PRK13481   46 SFVSADNMPEYVKGAFISMEDERFYKHHGFDLKGTTRALFSTISDRDVQGGSTITQQVVKNYFYDNERSFTRKVKELFVA 125

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2443851657 162 ITLELLWSKKRILEVYLNIAEFGKGIFGVEAASRFYF----KKAAKNLTQS---EAALLAAVLPNPIIYKVN 226
Cdd:PRK13481  126 HRVEKQYSKNEILSFYLNNIYFGDNQYTLEGAANHYFgttvNKNSTTMSHItvlQSAILASKVNAPSVYNIN 197
mrcA PRK11636
penicillin-binding protein 1a; Provisional
 84-231 2.21e-22

penicillin-binding protein 1a; Provisional


Pssm-ID: 183248 [Multi-domain]  Cd Length: 850  Bit Score: 95.97  E-value: 2.21e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443851657  84 VSLDQISPNMQLAVIAAEDQRFPTHWGFD----WNAIEKALEHNEKSKrirGGSTISQQTAKNLYLWHGQSWLRKGLEVP 159
Cdd:PRK11636   69 LTLDQIPPEMVKAFIATEDSRFYEHHGVDpvgiFRAASVALFSGHASQ---GASTITQQLARNFFLSPERTLMRKIKEAF 145

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2443851657 160 VTITLELLWSKKRILEVYLNIAEFGKGIFGVEAASRFYFKKAAKNLTQSEAALLAAvLPnpiiykvNAPSAL 231
Cdd:PRK11636  146 LAIRIEQLLTKDEILELYLNKIYLGYRAYGVGAAAQVYFGKTVDQLTLSEMAVIAG-LP-------KAPSTF 209
PRK11240 PRK11240
penicillin-binding protein 1C; Provisional
 84-231 4.62e-19

penicillin-binding protein 1C; Provisional


Pssm-ID: 183049 [Multi-domain]  Cd Length: 772  Bit Score: 85.91  E-value: 4.62e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443851657  84 VSLDQISPNMQLAVIAAEDQRFPTHWGFDWNAIEKALEHNEKSKRI-RGGSTISQQTAKnLYLWHGQSWLRKGLEVPVTI 162
Cdd:PRK11240   65 VTIEDVSPRYLEALINYEDRWFWKHPGVNPFSVARAAWQDLTSGRViSGGSTLTMQVAR-LLDPHPRTFGGKIRQLWRAL 143

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2443851657 163 TLELLWSKKRILEVYLNIAEFGKGIFGVEAASRFYFKKAAKNLTQSEAALLaAVLPnpiiykvNAPSAL 231
Cdd:PRK11240  144 QLEWHLSKREILTLYLNRAPFGGTLQGIGAASWAYLGKSPANLSYAEAALL-AVLP-------QAPSRL 204
PRK14850 PRK14850
penicillin-binding protein 1b; Provisional
 97-235 4.36e-15

penicillin-binding protein 1b; Provisional


Pssm-ID: 237835 [Multi-domain]  Cd Length: 764  Bit Score: 74.50  E-value: 4.36e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443851657  97 VIAAEDQRFPTHWGFDWNAIEKALEHNEKSKR-IRGGSTISQQTAKNLYLWHGQSWLRKGLEVPVTITLELLWSKKRILE 175
Cdd:PRK14850  173 LLAIEDKYFYEHDGIHLSSIGRAFLVNLMSGHtIQGGSTLTQQLVKNLFLTNTRSLWRKINEIYMALILDRFYSKDRILE 252

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2443851657 176 VYLNIAEFGKG----IFGVEAASRFYFKKAAKNLTQSEAALLAAVLPNPIIYKV-NAPSALVKRK 235
Cdd:PRK14850  253 LYLNEVYLGQDgneqIRGFPLASIYYFGRPINELNLDQYALLVGMVKGASLYNPwTNPNLTLKRR 317
mrcB PRK09506
bifunctional glycosyl transferase/transpeptidase; Reviewed
 98-220 1.23e-14

bifunctional glycosyl transferase/transpeptidase; Reviewed


Pssm-ID: 236544 [Multi-domain]  Cd Length: 830  Bit Score: 73.27  E-value: 1.23e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443851657  98 IAAEDQRFPTHWGFDWNAIEKALEHNEKSKR-IRGGSTISQQTAKNLYLWHGQSWLRKGLEVPVTITLELLWSKKRILEV 176
Cdd:PRK09506  228 LATEDRHFYEHDGISLYSIGRAVLANLTAGRtVQGGSTLTQQLVKNLFLSNERSLWRKANEAYMALIMDARYSKDRILEL 307

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2443851657 177 YLNIAEFGKG----IFGVEAASRFYFKKAAKNLTQSEAALL-----AAVLPNP 220
Cdd:PRK09506  308 YLNEVYLGQSgddqIRGFPLASLYYFGRPVEELSLDQQALLvgmvkGASLYNP 360
 
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.
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