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Conserved domains on  [gi|16131098|ref|NP_417675|]
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peptidoglycan glycosyltransferase MtgA [Escherichia coli str. K-12 substr. MG1655]

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
 14-233 3.32e-96

glycosyltransferase; Provisional


The actual alignment was detected with superfamily member TIGR02070:

Pssm-ID: 475222 [Multi-domain]  Cd Length: 224  Bit Score: 280.50  E-value: 3.32e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131098    14 RFLLRLMvvLAVFwgGGIALFSVAPVPFSAVMVERQVSAWLHGNFRYVAHSDWVSMDQISPWMGLAVIAAEDQKFPEHWG 93
Cdd:TIGR02070   9 AGVLLFN--LAVF--AALASWRFVPPPSTAFMVAEKLALWGQGDPTCGIQHRWRPYDQISPNLKRAVIASEDAKFVEHHG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131098    94 FDVASIEKALAHNERNENRIRGASTISQQTAKNLFLWDGRSWVRKGLEAGLTLGIETVWSKKRILTVYLNIAEFGDGVFG 173
Cdd:TIGR02070  85 FDWEAIQDALEKNEKSGKVVRGGSTISQQLAKNLFLWSGRSYLRKGLEAWATWMLETWWSKQRILEVYLNSVEWGNGVFG 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131098   174 VEAAAQRYFHKPASKLTRSEAALLAAVLPNPLRFKVSSPSGYVRSRQAWILRQMYQLGGE 233
Cdd:TIGR02070 165 AEAAARYYFKRSASNLTRGQAARLAAVLPNPKYYDENRPGPYVRRKATWILKQMGYLGLP 224
 
Name Accession Description Interval E-value
mono_pep_trsgly TIGR02070
monofunctional biosynthetic peptidoglycan transglycosylase; This family is one of the ...
 14-233 3.32e-96

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: 280.50  E-value: 3.32e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131098    14 RFLLRLMvvLAVFwgGGIALFSVAPVPFSAVMVERQVSAWLHGNFRYVAHSDWVSMDQISPWMGLAVIAAEDQKFPEHWG 93
Cdd:TIGR02070   9 AGVLLFN--LAVF--AALASWRFVPPPSTAFMVAEKLALWGQGDPTCGIQHRWRPYDQISPNLKRAVIASEDAKFVEHHG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131098    94 FDVASIEKALAHNERNENRIRGASTISQQTAKNLFLWDGRSWVRKGLEAGLTLGIETVWSKKRILTVYLNIAEFGDGVFG 173
Cdd:TIGR02070  85 FDWEAIQDALEKNEKSGKVVRGGSTISQQLAKNLFLWSGRSYLRKGLEAWATWMLETWWSKQRILEVYLNSVEWGNGVFG 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131098   174 VEAAAQRYFHKPASKLTRSEAALLAAVLPNPLRFKVSSPSGYVRSRQAWILRQMYQLGGE 233
Cdd:TIGR02070 165 AEAAARYYFKRSASNLTRGQAARLAAVLPNPKYYDENRPGPYVRRKATWILKQMGYLGLP 224
MrcB COG0744
Penicillin-binding protein 1B/1F, peptidoglycan transglycosylase/transpeptidase [Cell wall ...
 1-231 1.85e-76

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


Pssm-ID: 440507 [Multi-domain]  Cd Length: 630  Bit Score: 242.52  E-value: 1.85e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131098   1 MSKSRLTvFSFVRRFLLRLMVVLAVF---WGGGIALFSVAPVPFSAVMVERQVSA-----WLHGNF---RYVAHSDWVSM 69
Cdd:COG0744   1 MAKPRRG-KRLLRRLLGLLLLLLAVLvlaALAGLVALYVADLPDPEELEDLALPQtstiyDRDGTLiatLGDENREWVPL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131098  70 DQISPWMGLAVIAAEDQKFPEHWGFDVASIEKALAHNERNENRIRGASTISQQTAKNLFLWDGRSWVRKGLEAGLTLGIE 149
Cdd:COG0744  80 DQIPPHLKDAVVAIEDRRFYEHGGVDPKGIARALVANLTAGGVVQGGSTITQQLVKNLFLSNERTLSRKLKEALLALKLE 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131098 150 TVWSKKRILTVYLNIAEFGDGVFGVEAAAQRYFHKPASKLTRSEAALLAAVLPNPLRFKVSSPSGYVRSRQAWILRQMYQ 229
Cdd:COG0744 160 RKYSKDEILELYLNTVYFGRGAYGIEAAAQYYFGKSASDLTLAEAALLAGLVKAPSYYDPYRNPEAAKERRNLVLDRMVE 239


                ..
gi 16131098 230 LG 231
Cdd:COG0744 240 QG 241
Transgly pfam00912
Transglycosylase; The penicillin-binding proteins are bifunctional proteins consisting of ...
 60-228 4.81e-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: 222.78  E-value: 4.81e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131098    60 YVAHSDWVSMDQISPWMGLAVIAAEDQKFPEHWGFDVASIEKALAHNERNENRIRGASTISQQTAKNLFLWDGRSWVRKG 139
Cdd:pfam00912   9 GEENREYVPLDDIPPALKNAVLAIEDRRFYEHGGVDPKGIARALLSNLRSGRIVQGGSTITQQLAKNLFLTPERTLTRKL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131098   140 LEAGLTLGIETVWSKKRILTVYLNIAEFGDGVFGVEAAAQRYFHKPASKLTRSEAALLAAVLPNPLRFKVSSPSGYVRSR 219
Cdd:pfam00912  89 KEAVLALKLERRYSKDEILEAYLNTVYFGRGAYGIEAAARAYFGKDASDLTLAEAALLAGLPQAPSRYNPLRNPERAKRR 168


                  ....*....
gi 16131098   220 QAWILRQMY 228
Cdd:pfam00912 169 RNLVLDRMV 177
mrcA PRK11636
penicillin-binding protein 1a; Provisional
 67-205 2.94e-26

penicillin-binding protein 1a; Provisional


Pssm-ID: 183248 [Multi-domain]  Cd Length: 850  Bit Score: 106.75  E-value: 2.94e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131098   67 VSMDQISPWMGLAVIAAEDQKFPEHWGFDVASIEKALAHNERNENRIRGASTISQQTAKNLFLWDGRSWVRKGLEAGLTL 146
Cdd:PRK11636  69 LTLDQIPPEMVKAFIATEDSRFYEHHGVDPVGIFRAASVALFSGHASQGASTITQQLARNFFLSPERTLMRKIKEAFLAI 148

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131098  147 GIETVWSKKRILTVYLNIAEFGDGVFGVEAAAQRYFHKPASKLTRSEAALLAAvLP------NPL 205
Cdd:PRK11636 149 RIEQLLTKDEILELYLNKIYLGYRAYGVGAAAQVYFGKTVDQLTLSEMAVIAG-LPkapstfNPL 212
 
Name Accession Description Interval E-value
mono_pep_trsgly TIGR02070
monofunctional biosynthetic peptidoglycan transglycosylase; This family is one of the ...
 14-233 3.32e-96

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: 280.50  E-value: 3.32e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131098    14 RFLLRLMvvLAVFwgGGIALFSVAPVPFSAVMVERQVSAWLHGNFRYVAHSDWVSMDQISPWMGLAVIAAEDQKFPEHWG 93
Cdd:TIGR02070   9 AGVLLFN--LAVF--AALASWRFVPPPSTAFMVAEKLALWGQGDPTCGIQHRWRPYDQISPNLKRAVIASEDAKFVEHHG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131098    94 FDVASIEKALAHNERNENRIRGASTISQQTAKNLFLWDGRSWVRKGLEAGLTLGIETVWSKKRILTVYLNIAEFGDGVFG 173
Cdd:TIGR02070  85 FDWEAIQDALEKNEKSGKVVRGGSTISQQLAKNLFLWSGRSYLRKGLEAWATWMLETWWSKQRILEVYLNSVEWGNGVFG 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131098   174 VEAAAQRYFHKPASKLTRSEAALLAAVLPNPLRFKVSSPSGYVRSRQAWILRQMYQLGGE 233
Cdd:TIGR02070 165 AEAAARYYFKRSASNLTRGQAARLAAVLPNPKYYDENRPGPYVRRKATWILKQMGYLGLP 224
MrcB COG0744
Penicillin-binding protein 1B/1F, peptidoglycan transglycosylase/transpeptidase [Cell wall ...
 1-231 1.85e-76

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


Pssm-ID: 440507 [Multi-domain]  Cd Length: 630  Bit Score: 242.52  E-value: 1.85e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131098   1 MSKSRLTvFSFVRRFLLRLMVVLAVF---WGGGIALFSVAPVPFSAVMVERQVSA-----WLHGNF---RYVAHSDWVSM 69
Cdd:COG0744   1 MAKPRRG-KRLLRRLLGLLLLLLAVLvlaALAGLVALYVADLPDPEELEDLALPQtstiyDRDGTLiatLGDENREWVPL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131098  70 DQISPWMGLAVIAAEDQKFPEHWGFDVASIEKALAHNERNENRIRGASTISQQTAKNLFLWDGRSWVRKGLEAGLTLGIE 149
Cdd:COG0744  80 DQIPPHLKDAVVAIEDRRFYEHGGVDPKGIARALVANLTAGGVVQGGSTITQQLVKNLFLSNERTLSRKLKEALLALKLE 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131098 150 TVWSKKRILTVYLNIAEFGDGVFGVEAAAQRYFHKPASKLTRSEAALLAAVLPNPLRFKVSSPSGYVRSRQAWILRQMYQ 229
Cdd:COG0744 160 RKYSKDEILELYLNTVYFGRGAYGIEAAAQYYFGKSASDLTLAEAALLAGLVKAPSYYDPYRNPEAAKERRNLVLDRMVE 239


                ..
gi 16131098 230 LG 231
Cdd:COG0744 240 QG 241
Transgly pfam00912
Transglycosylase; The penicillin-binding proteins are bifunctional proteins consisting of ...
 60-228 4.81e-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: 222.78  E-value: 4.81e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131098    60 YVAHSDWVSMDQISPWMGLAVIAAEDQKFPEHWGFDVASIEKALAHNERNENRIRGASTISQQTAKNLFLWDGRSWVRKG 139
Cdd:pfam00912   9 GEENREYVPLDDIPPALKNAVLAIEDRRFYEHGGVDPKGIARALLSNLRSGRIVQGGSTITQQLAKNLFLTPERTLTRKL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131098   140 LEAGLTLGIETVWSKKRILTVYLNIAEFGDGVFGVEAAAQRYFHKPASKLTRSEAALLAAVLPNPLRFKVSSPSGYVRSR 219
Cdd:pfam00912  89 KEAVLALKLERRYSKDEILEAYLNTVYFGRGAYGIEAAARAYFGKDASDLTLAEAALLAGLPQAPSRYNPLRNPERAKRR 168


                  ....*....
gi 16131098   220 QAWILRQMY 228
Cdd:pfam00912 169 RNLVLDRMV 177
PBP_1a_fam TIGR02074
penicillin-binding protein, 1A family; Bacterial that synthesize a cell wall of peptidoglycan ...
 66-231 1.40e-49

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: 169.75  E-value: 1.40e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131098    66 WVSMDQISPWMGLAVIAAEDQKFPEHWGFDVASIEKALAHNERNENRIRGASTISQQTAKNLFLWDGRSWVRKGLEAGLT 145
Cdd:TIGR02074   4 YVPIDDIPENLINAFLAIEDRRFYDHFGIDLKGIGRAAVANITSGRVLEGGSTITQQLAKNLYLTNERTITRKIQEALLA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131098   146 LGIETVWSKKRILTVYLNIAEFGDGVFGVEAAAQRYFHKPASKLTRSEAALLAAVLPNPLRFK-VSSPSgYVRSRQAWIL 224
Cdd:TIGR02074  84 LKLEQKLSKDEILELYLNRIYFGNGAYGIEAAAQFYFGKSVNDLTLAEAAMLAGLPKAPSAYNpFKNPE-RAKDRRNLVL 162


                  ....*..
gi 16131098   225 RQMYQLG 231
Cdd:TIGR02074 163 SNMVENG 169
MrcA COG5009
Membrane carboxypeptidase/penicillin-binding protein [Cell wall/membrane/envelope biogenesis];
66-231 1.14e-46

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


Pssm-ID: 444033 [Multi-domain]  Cd Length: 785  Bit Score: 164.95  E-value: 1.14e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131098  66 WVSMDQISPWMGLAVIAAEDQKFPEHWGFDVASIEKALAHNERNENRIRGASTISQQTAKNLFLWDGRSWVRKGLEAGLT 145
Cdd:COG5009  68 PVPIEEIPPLLINAFLAAEDKRFYEHPGVDPIGIARAAVVNLRTGRRVQGGSTITQQVAKNFLLSPERTLTRKIKEAILA 147

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131098 146 LGIETVWSKKRILTVYLNIAEFGDGVFGVEAAAQRYFHKPASKLTRSEAALLAAVLPNPLRFkvsSP-SGYVRS--RQAW 222
Cdd:COG5009 148 LRIEQELSKDEILELYLNKIYLGHRAYGVAAAAQTYFGKSLDELTLAEAAMLAGLPKAPSRY---NPiRNPERAleRRNY 224


                ....*....
gi 16131098 223 ILRQMYQLG 231
Cdd:COG5009 225 VLGRMLELG 233
PbpC COG4953
Membrane carboxypeptidase/penicillin-binding protein PbpC [Cell wall/membrane/envelope ...
 13-231 5.95e-39

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


Pssm-ID: 443980 [Multi-domain]  Cd Length: 773  Bit Score: 143.05  E-value: 5.95e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131098  13 RRFLLRLMVVLAVFWGGGIALFSVAP------VPFSAVMVERQ---VSAWL--HGNFRYvahsdWVSMDQISPWMGLAVI 81
Cdd:COG4953   8 RRRLLALLLALLLLALALWALDRLFPlpllfaVPYSTVVLDRDgtlLRAFLaaDGQWRL-----PVPLDEVSPRYLQALL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131098  82 AAEDQKFPEHWGFDVASIEKALAHNERNENRIRGASTISQQTAKnlFLWDG-RSWVRKGLEAGLTLGIETVWSKKRILTV 160
Cdd:COG4953  83 AYEDRRFYYHPGVNPLALLRAAWQNLRSGRIVSGGSTLTMQVAR--LLEPRpRTLSGKLRQILRALQLERRYSKDEILEL 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131098 161 YLNIAEFGDGVFGVEAAAQRYFHKPASKLTRSEAALLaAVLPNplrfkvsSPSGYV--------RSRQAWILRQMYQLG 231
Cdd:COG4953 161 YLNLAPYGGNIEGVEAASLAYFGKPPSRLSLAEAALL-AVLPQ-------APSRRRpdrnperaRAARDRVLARLAEAG 231
mrcA PRK11636
penicillin-binding protein 1a; Provisional
 67-205 2.94e-26

penicillin-binding protein 1a; Provisional


Pssm-ID: 183248 [Multi-domain]  Cd Length: 850  Bit Score: 106.75  E-value: 2.94e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131098   67 VSMDQISPWMGLAVIAAEDQKFPEHWGFDVASIEKALAHNERNENRIRGASTISQQTAKNLFLWDGRSWVRKGLEAGLTL 146
Cdd:PRK11636  69 LTLDQIPPEMVKAFIATEDSRFYEHHGVDPVGIFRAASVALFSGHASQGASTITQQLARNFFLSPERTLMRKIKEAFLAI 148

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131098  147 GIETVWSKKRILTVYLNIAEFGDGVFGVEAAAQRYFHKPASKLTRSEAALLAAvLP------NPL 205
Cdd:PRK11636 149 RIEQLLTKDEILELYLNKIYLGYRAYGVGAAAQVYFGKTVDQLTLSEMAVIAG-LPkapstfNPL 212
PRK13481 PRK13481
glycosyltransferase; Provisional
 64-231 2.86e-22

glycosyltransferase; Provisional


Pssm-ID: 184078 [Multi-domain]  Cd Length: 232  Bit Score: 91.40  E-value: 2.86e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131098   64 SDWVSMDQISPWMGLAVIAAEDQKFPEHWGFDVASIEKALAHNERNENrIRGASTISQQTAKNLFLWDGRSWVRKGLEAG 143
Cdd:PRK13481  45 SSFVSADNMPEYVKGAFISMEDERFYKHHGFDLKGTTRALFSTISDRD-VQGGSTITQQVVKNYFYDNERSFTRKVKELF 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131098  144 LTLGIETVWSKKRILTVYLNIAEFGDGVFGVEAAAQRYF----HKPA---SKLTRSEAALLAAVLPNPLRFKVSSPSGYV 216
Cdd:PRK13481 124 VAHRVEKQYSKNEILSFYLNNIYFGDNQYTLEGAANHYFgttvNKNSttmSHITVLQSAILASKVNAPSVYNINDMSENF 203

                        170
                 ....*....|....*
gi 16131098  217 RSRQAWILRQMYQLG 231
Cdd:PRK13481 204 TQRVSTNLEKMKQQN 218
PRK11240 PRK11240
penicillin-binding protein 1C; Provisional
 8-202 3.23e-19

penicillin-binding protein 1C; Provisional


Pssm-ID: 183049 [Multi-domain]  Cd Length: 772  Bit Score: 86.29  E-value: 3.23e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131098    8 VFSFVRRFLLRLMVVLAVFWGGGIALFSVAPVPFSAVMVERQVSA------W----LHGNFRYVahsdwVSMDQISPWMG 77
Cdd:PRK11240   1 RLLTKRGRWLWLAAAPLLLFLALWLADKLWPLPLHEVNPARVVVAedgtplWrfadADGIWRYP-----VTIEDVSPRYL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131098   78 LAVIAAEDQKFPEHWGFDVASIEKALAHNERNENRIRGASTISQQTAKnlfLWD--GRSWVRKGLEAGLTLGIETVWSKK 155
Cdd:PRK11240  76 EALINYEDRWFWKHPGVNPFSVARAAWQDLTSGRVISGGSTLTMQVAR---LLDphPRTFGGKIRQLWRALQLEWHLSKR 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 16131098  156 RILTVYLNIAEFGDGVFGVEAAAQRYFHKPASKLTRSEAALLaAVLP 202
Cdd:PRK11240 153 EILTLYLNRAPFGGTLQGIGAASWAYLGKSPANLSYAEAALL-AVLP 198
mrcB PRK09506
bifunctional glycosyl transferase/transpeptidase; Reviewed
 81-206 4.63e-19

bifunctional glycosyl transferase/transpeptidase; Reviewed


Pssm-ID: 236544 [Multi-domain]  Cd Length: 830  Bit Score: 85.59  E-value: 4.63e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131098   81 IAAEDQKFPEHWGFDVASIEKALAHNERNENRIRGASTISQQTAKNLFLWDGRSWVRKGLEAGLTLGIETVWSKKRILTV 160
Cdd:PRK09506 228 LATEDRHFYEHDGISLYSIGRAVLANLTAGRTVQGGSTLTQQLVKNLFLSNERSLWRKANEAYMALIMDARYSKDRILEL 307

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 16131098  161 YLNIAEFG----DGVFGVEAAAQRYFHKPASKLTRSEAALL-----AAVLPNPLR 206
Cdd:PRK09506 308 YLNEVYLGqsgdDQIRGFPLASLYYFGRPVEELSLDQQALLvgmvkGASLYNPWR 362
PRK14850 PRK14850
penicillin-binding protein 1b; Provisional
 80-204 2.90e-16

penicillin-binding protein 1b; Provisional


Pssm-ID: 237835 [Multi-domain]  Cd Length: 764  Bit Score: 77.58  E-value: 2.90e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131098   80 VIAAEDQKFPEHWGFDVASIEKALAHNERNENRIRGASTISQQTAKNLFLWDGRSWVRKGLEAGLTLGIETVWSKKRILT 159
Cdd:PRK14850 173 LLAIEDKYFYEHDGIHLSSIGRAFLVNLMSGHTIQGGSTLTQQLVKNLFLTNTRSLWRKINEIYMALILDRFYSKDRILE 252

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 16131098  160 VYLNIAEFG----DGVFGVEAAAQRYFHKPASKLTRSEAALL-----AAVLPNP 204
Cdd:PRK14850 253 LYLNEVYLGqdgnEQIRGFPLASIYYFGRPINELNLDQYALLvgmvkGASLYNP 306
 
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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