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Conserved domains on  [gi|1035685929|ref|WP_064529513|]
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MULTISPECIES: monofunctional biosynthetic peptidoglycan transglycosylase [Escherichia]

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
 13-233 7.90e-95

glycosyltransferase; Provisional


The actual alignment was detected with superfamily member TIGR02070:

Pssm-ID: 475222 [Multi-domain]  Cd Length: 224  Bit Score: 277.04  E-value: 7.90e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035685929  13 RRFILRLLSVLVVFWGG---GIALFSIAPVPFSAVMVERQLSAWLHGNFRYMAHSDWVSMDQISPWMGLAVIAAEDQKFP 89
Cdd:TIGR02070   1 GYVIGCLVAGVLLFNLAvfaALASWRFVPPPSTAFMVAEKLALWGQGDPTCGIQHRWRPYDQISPNLKRAVIASEDAKFV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035685929  90 EHWGFDVASIEKALAHNERNENRIRGASTISQQTAKNLFLWDGRSWVRKGLEAGLTLGIETVWSKKRILTVYLNIAEFGD 169
Cdd:TIGR02070  81 EHHGFDWEAIQDALEKNEKSGKVVRGGSTISQQLAKNLFLWSGRSYLRKGLEAWATWMLETWWSKQRILEVYLNSVEWGN 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1035685929 170 GVFGVEAAAQRYFHKPASKLTQSEAALLAAVLPSPLRFKASAPSGYVRSRQAWILRQMHQLGGE 233
Cdd:TIGR02070 161 GVFGAEAAARYYFKRSASNLTRGQAARLAAVLPNPKYYDENRPGPYVRRKATWILKQMGYLGLP 224
 
Name Accession Description Interval E-value
mono_pep_trsgly TIGR02070
monofunctional biosynthetic peptidoglycan transglycosylase; This family is one of the ...
 13-233 7.90e-95

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: 277.04  E-value: 7.90e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035685929  13 RRFILRLLSVLVVFWGG---GIALFSIAPVPFSAVMVERQLSAWLHGNFRYMAHSDWVSMDQISPWMGLAVIAAEDQKFP 89
Cdd:TIGR02070   1 GYVIGCLVAGVLLFNLAvfaALASWRFVPPPSTAFMVAEKLALWGQGDPTCGIQHRWRPYDQISPNLKRAVIASEDAKFV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035685929  90 EHWGFDVASIEKALAHNERNENRIRGASTISQQTAKNLFLWDGRSWVRKGLEAGLTLGIETVWSKKRILTVYLNIAEFGD 169
Cdd:TIGR02070  81 EHHGFDWEAIQDALEKNEKSGKVVRGGSTISQQLAKNLFLWSGRSYLRKGLEAWATWMLETWWSKQRILEVYLNSVEWGN 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1035685929 170 GVFGVEAAAQRYFHKPASKLTQSEAALLAAVLPSPLRFKASAPSGYVRSRQAWILRQMHQLGGE 233
Cdd:TIGR02070 161 GVFGAEAAARYYFKRSASNLTRGQAARLAAVLPNPKYYDENRPGPYVRRKATWILKQMGYLGLP 224
MrcB COG0744
Penicillin-binding protein 1B/1F, peptidoglycan transglycosylase/transpeptidase [Cell wall ...
 1-231 1.35e-77

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


Pssm-ID: 440507 [Multi-domain]  Cd Length: 630  Bit Score: 245.60  E-value: 1.35e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035685929   1 MSKRRVTAFGFVR--RFILRLLSVLVVFWGGGIALFSIAPVPFSAVMVERQLS-------------AWLHGNFRymahsD 65
Cdd:COG0744     1 MAKPRRGKRLLRRllGLLLLLLAVLVLAALAGLVALYVADLPDPEELEDLALPqtstiydrdgtliATLGDENR-----E 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035685929  66 WVSMDQISPWMGLAVIAAEDQKFPEHWGFDVASIEKALAHNERNENRIRGASTISQQTAKNLFLWDGRSWVRKGLEAGLT 145
Cdd:COG0744    76 WVPLDQIPPHLKDAVVAIEDRRFYEHGGVDPKGIARALVANLTAGGVVQGGSTITQQLVKNLFLSNERTLSRKLKEALLA 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035685929 146 LGIETVWSKKRILTVYLNIAEFGDGVFGVEAAAQRYFHKPASKLTQSEAALLAAVLPSPLRFKASAPSGYVRSRQAWILR 225
Cdd:COG0744   156 LKLERKYSKDEILELYLNTVYFGRGAYGIEAAAQYYFGKSASDLTLAEAALLAGLVKAPSYYDPYRNPEAAKERRNLVLD 235


                  ....*.
gi 1035685929 226 QMHQLG 231
Cdd:COG0744   236 RMVEQG 241
Transgly pfam00912
Transglycosylase; The penicillin-binding proteins are bifunctional proteins consisting of ...
 63-228 1.58e-72

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: 218.93  E-value: 1.58e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035685929  63 HSDWVSMDQISPWMGLAVIAAEDQKFPEHWGFDVASIEKALAHNERNENRIRGASTISQQTAKNLFLWDGRSWVRKGLEA 142
Cdd:pfam00912  12 NREYVPLDDIPPALKNAVLAIEDRRFYEHGGVDPKGIARALLSNLRSGRIVQGGSTITQQLAKNLFLTPERTLTRKLKEA 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035685929 143 GLTLGIETVWSKKRILTVYLNIAEFGDGVFGVEAAAQRYFHKPASKLTQSEAALLAAVLPSPLRFKASAPSGYVRSRQAW 222
Cdd:pfam00912  92 VLALKLERRYSKDEILEAYLNTVYFGRGAYGIEAAARAYFGKDASDLTLAEAALLAGLPQAPSRYNPLRNPERAKRRRNL 171


                  ....*.
gi 1035685929 223 ILRQMH 228
Cdd:pfam00912 172 VLDRMV 177
mrcA PRK11636
penicillin-binding protein 1a; Provisional
 67-207 4.27e-26

penicillin-binding protein 1a; Provisional


Pssm-ID: 183248 [Multi-domain]  Cd Length: 850  Bit Score: 106.37  E-value: 4.27e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035685929  67 VSMDQISPWMGLAVIAAEDQKFPEHWGFDVASIEKALAHNERNENRIRGASTISQQTAKNLFLWDGRSWVRKGLEAGLTL 146
Cdd:PRK11636   69 LTLDQIPPEMVKAFIATEDSRFYEHHGVDPVGIFRAASVALFSGHASQGASTITQQLARNFFLSPERTLMRKIKEAFLAI 148

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1035685929 147 GIETVWSKKRILTVYLNIAEFGDGVFGVEAAAQRYFHKPASKLTQSEAALLAAVLPSPLRF 207
Cdd:PRK11636  149 RIEQLLTKDEILELYLNKIYLGYRAYGVGAAAQVYFGKTVDQLTLSEMAVIAGLPKAPSTF 209
 
Name Accession Description Interval E-value
mono_pep_trsgly TIGR02070
monofunctional biosynthetic peptidoglycan transglycosylase; This family is one of the ...
 13-233 7.90e-95

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: 277.04  E-value: 7.90e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035685929  13 RRFILRLLSVLVVFWGG---GIALFSIAPVPFSAVMVERQLSAWLHGNFRYMAHSDWVSMDQISPWMGLAVIAAEDQKFP 89
Cdd:TIGR02070   1 GYVIGCLVAGVLLFNLAvfaALASWRFVPPPSTAFMVAEKLALWGQGDPTCGIQHRWRPYDQISPNLKRAVIASEDAKFV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035685929  90 EHWGFDVASIEKALAHNERNENRIRGASTISQQTAKNLFLWDGRSWVRKGLEAGLTLGIETVWSKKRILTVYLNIAEFGD 169
Cdd:TIGR02070  81 EHHGFDWEAIQDALEKNEKSGKVVRGGSTISQQLAKNLFLWSGRSYLRKGLEAWATWMLETWWSKQRILEVYLNSVEWGN 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1035685929 170 GVFGVEAAAQRYFHKPASKLTQSEAALLAAVLPSPLRFKASAPSGYVRSRQAWILRQMHQLGGE 233
Cdd:TIGR02070 161 GVFGAEAAARYYFKRSASNLTRGQAARLAAVLPNPKYYDENRPGPYVRRKATWILKQMGYLGLP 224
MrcB COG0744
Penicillin-binding protein 1B/1F, peptidoglycan transglycosylase/transpeptidase [Cell wall ...
 1-231 1.35e-77

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


Pssm-ID: 440507 [Multi-domain]  Cd Length: 630  Bit Score: 245.60  E-value: 1.35e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035685929   1 MSKRRVTAFGFVR--RFILRLLSVLVVFWGGGIALFSIAPVPFSAVMVERQLS-------------AWLHGNFRymahsD 65
Cdd:COG0744     1 MAKPRRGKRLLRRllGLLLLLLAVLVLAALAGLVALYVADLPDPEELEDLALPqtstiydrdgtliATLGDENR-----E 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035685929  66 WVSMDQISPWMGLAVIAAEDQKFPEHWGFDVASIEKALAHNERNENRIRGASTISQQTAKNLFLWDGRSWVRKGLEAGLT 145
Cdd:COG0744    76 WVPLDQIPPHLKDAVVAIEDRRFYEHGGVDPKGIARALVANLTAGGVVQGGSTITQQLVKNLFLSNERTLSRKLKEALLA 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035685929 146 LGIETVWSKKRILTVYLNIAEFGDGVFGVEAAAQRYFHKPASKLTQSEAALLAAVLPSPLRFKASAPSGYVRSRQAWILR 225
Cdd:COG0744   156 LKLERKYSKDEILELYLNTVYFGRGAYGIEAAAQYYFGKSASDLTLAEAALLAGLVKAPSYYDPYRNPEAAKERRNLVLD 235


                  ....*.
gi 1035685929 226 QMHQLG 231
Cdd:COG0744   236 RMVEQG 241
Transgly pfam00912
Transglycosylase; The penicillin-binding proteins are bifunctional proteins consisting of ...
 63-228 1.58e-72

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: 218.93  E-value: 1.58e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035685929  63 HSDWVSMDQISPWMGLAVIAAEDQKFPEHWGFDVASIEKALAHNERNENRIRGASTISQQTAKNLFLWDGRSWVRKGLEA 142
Cdd:pfam00912  12 NREYVPLDDIPPALKNAVLAIEDRRFYEHGGVDPKGIARALLSNLRSGRIVQGGSTITQQLAKNLFLTPERTLTRKLKEA 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035685929 143 GLTLGIETVWSKKRILTVYLNIAEFGDGVFGVEAAAQRYFHKPASKLTQSEAALLAAVLPSPLRFKASAPSGYVRSRQAW 222
Cdd:pfam00912  92 VLALKLERRYSKDEILEAYLNTVYFGRGAYGIEAAARAYFGKDASDLTLAEAALLAGLPQAPSRYNPLRNPERAKRRRNL 171


                  ....*.
gi 1035685929 223 ILRQMH 228
Cdd:pfam00912 172 VLDRMV 177
PBP_1a_fam TIGR02074
penicillin-binding protein, 1A family; Bacterial that synthesize a cell wall of peptidoglycan ...
 66-231 9.74e-48

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: 165.13  E-value: 9.74e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035685929  66 WVSMDQISPWMGLAVIAAEDQKFPEHWGFDVASIEKALAHNERNENRIRGASTISQQTAKNLFLWDGRSWVRKGLEAGLT 145
Cdd:TIGR02074   4 YVPIDDIPENLINAFLAIEDRRFYDHFGIDLKGIGRAAVANITSGRVLEGGSTITQQLAKNLYLTNERTITRKIQEALLA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035685929 146 LGIETVWSKKRILTVYLNIAEFGDGVFGVEAAAQRYFHKPASKLTQSEAALLAAVLPSPLRFKA-SAPSgYVRSRQAWIL 224
Cdd:TIGR02074  84 LKLEQKLSKDEILELYLNRIYFGNGAYGIEAAAQFYFGKSVNDLTLAEAAMLAGLPKAPSAYNPfKNPE-RAKDRRNLVL 162


                  ....*..
gi 1035685929 225 RQMHQLG 231
Cdd:TIGR02074 163 SNMVENG 169
MrcA COG5009
Membrane carboxypeptidase/penicillin-binding protein [Cell wall/membrane/envelope biogenesis];
66-231 3.39e-47

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


Pssm-ID: 444033 [Multi-domain]  Cd Length: 785  Bit Score: 166.49  E-value: 3.39e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035685929  66 WVSMDQISPWMGLAVIAAEDQKFPEHWGFDVASIEKALAHNERNENRIRGASTISQQTAKNLFLWDGRSWVRKGLEAGLT 145
Cdd:COG5009    68 PVPIEEIPPLLINAFLAAEDKRFYEHPGVDPIGIARAAVVNLRTGRRVQGGSTITQQVAKNFLLSPERTLTRKIKEAILA 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035685929 146 LGIETVWSKKRILTVYLNIAEFGDGVFGVEAAAQRYFHKPASKLTQSEAALLAAVL--PS---PLRFKASApsgyvRSRQ 220
Cdd:COG5009   148 LRIEQELSKDEILELYLNKIYLGHRAYGVAAAAQTYFGKSLDELTLAEAAMLAGLPkaPSrynPIRNPERA-----LERR 222

                         170
                  ....*....|.
gi 1035685929 221 AWILRQMHQLG 231
Cdd:COG5009   223 NYVLGRMLELG 233
PbpC COG4953
Membrane carboxypeptidase/penicillin-binding protein PbpC [Cell wall/membrane/envelope ...
 13-231 4.71e-39

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


Pssm-ID: 443980 [Multi-domain]  Cd Length: 773  Bit Score: 143.43  E-value: 4.71e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035685929  13 RRFILRLLSVLVVFWGGGIALFSIAP------VPFSAVMVERQ---LSAWL--HGNFRYmahsdWVSMDQISPWMGLAVI 81
Cdd:COG4953     8 RRRLLALLLALLLLALALWALDRLFPlpllfaVPYSTVVLDRDgtlLRAFLaaDGQWRL-----PVPLDEVSPRYLQALL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035685929  82 AAEDQKFPEHWGFDVASIEKALAHNERNENRIRGASTISQQTAKnlFLWDG-RSWVRKGLEAGLTLGIETVWSKKRILTV 160
Cdd:COG4953    83 AYEDRRFYYHPGVNPLALLRAAWQNLRSGRIVSGGSTLTMQVAR--LLEPRpRTLSGKLRQILRALQLERRYSKDEILEL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1035685929 161 YLNIAEFGDGVFGVEAAAQRYFHKPASKLTQSEAALLAAV--LPS---PLRFKASApsgyvRSRQAWILRQMHQLG 231
Cdd:COG4953   161 YLNLAPYGGNIEGVEAASLAYFGKPPSRLSLAEAALLAVLpqAPSrrrPDRNPERA-----RAARDRVLARLAEAG 231
mrcA PRK11636
penicillin-binding protein 1a; Provisional
 67-207 4.27e-26

penicillin-binding protein 1a; Provisional


Pssm-ID: 183248 [Multi-domain]  Cd Length: 850  Bit Score: 106.37  E-value: 4.27e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035685929  67 VSMDQISPWMGLAVIAAEDQKFPEHWGFDVASIEKALAHNERNENRIRGASTISQQTAKNLFLWDGRSWVRKGLEAGLTL 146
Cdd:PRK11636   69 LTLDQIPPEMVKAFIATEDSRFYEHHGVDPVGIFRAASVALFSGHASQGASTITQQLARNFFLSPERTLMRKIKEAFLAI 148

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1035685929 147 GIETVWSKKRILTVYLNIAEFGDGVFGVEAAAQRYFHKPASKLTQSEAALLAAVLPSPLRF 207
Cdd:PRK11636  149 RIEQLLTKDEILELYLNKIYLGYRAYGVGAAAQVYFGKTVDQLTLSEMAVIAGLPKAPSTF 209
PRK13481 PRK13481
glycosyltransferase; Provisional
 64-240 1.10e-22

glycosyltransferase; Provisional


Pssm-ID: 184078 [Multi-domain]  Cd Length: 232  Bit Score: 92.56  E-value: 1.10e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035685929  64 SDWVSMDQISPWMGLAVIAAEDQKFPEHWGFDVASIEKALAHNERNENrIRGASTISQQTAKNLFLWDGRSWVRKGLEAG 143
Cdd:PRK13481   45 SSFVSADNMPEYVKGAFISMEDERFYKHHGFDLKGTTRALFSTISDRD-VQGGSTITQQVVKNYFYDNERSFTRKVKELF 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035685929 144 LTLGIETVWSKKRILTVYLNIAEFGDGVFGVEAAAQRYF----HKPASKLTQS---EAALLAAVLPSPLRFKASAPSGYV 216
Cdd:PRK13481  124 VAHRVEKQYSKNEILSFYLNNIYFGDNQYTLEGAANHYFgttvNKNSTTMSHItvlQSAILASKVNAPSVYNINDMSENF 203

                         170       180
                  ....*....|....*....|....
gi 1035685929 217 RSRQAWILRQMHQLGGESFMqQYQ 240
Cdd:PRK13481  204 TQRVSTNLEKMKQQNYINET-QYQ 226
PRK11240 PRK11240
penicillin-binding protein 1C; Provisional
 12-206 9.18e-19

penicillin-binding protein 1C; Provisional


Pssm-ID: 183049 [Multi-domain]  Cd Length: 772  Bit Score: 84.75  E-value: 9.18e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035685929  12 VRRFILRLLSVLVVFWGGGIALFSIAPVPFSAVMVERQLSA------W----LHGNFRYMahsdwVSMDQISPWMGLAVI 81
Cdd:PRK11240    5 KRGRWLWLAAAPLLLFLALWLADKLWPLPLHEVNPARVVVAedgtplWrfadADGIWRYP-----VTIEDVSPRYLEALI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035685929  82 AAEDQKFPEHWGFDVASIEKALAHNERNENRIRGASTISQQTAKnlfLWD--GRSWVRKGLEAGLTLGIETVWSKKRILT 159
Cdd:PRK11240   80 NYEDRWFWKHPGVNPFSVARAAWQDLTSGRVISGGSTLTMQVAR---LLDphPRTFGGKIRQLWRALQLEWHLSKREILT 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1035685929 160 VYLNIAEFGDGVFGVEAAAQRYFHKPASKLTQSEAALLaAVL---PSPLR 206
Cdd:PRK11240  157 LYLNRAPFGGTLQGIGAASWAYLGKSPANLSYAEAALL-AVLpqaPSRLR 205
mrcB PRK09506
bifunctional glycosyl transferase/transpeptidase; Reviewed
 81-197 3.70e-18

bifunctional glycosyl transferase/transpeptidase; Reviewed


Pssm-ID: 236544 [Multi-domain]  Cd Length: 830  Bit Score: 83.28  E-value: 3.70e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035685929  81 IAAEDQKFPEHWGFDVASIEKALAHNERNENRIRGASTISQQTAKNLFLWDGRSWVRKGLEAGLTLGIETVWSKKRILTV 160
Cdd:PRK09506  228 LATEDRHFYEHDGISLYSIGRAVLANLTAGRTVQGGSTLTQQLVKNLFLSNERSLWRKANEAYMALIMDARYSKDRILEL 307

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1035685929 161 YLNIAEFG----DGVFGVEAAAQRYFHKPASKLTQSEAALL 197
Cdd:PRK09506  308 YLNEVYLGqsgdDQIRGFPLASLYYFGRPVEELSLDQQALL 348
PRK14850 PRK14850
penicillin-binding protein 1b; Provisional
 80-197 5.51e-16

penicillin-binding protein 1b; Provisional


Pssm-ID: 237835 [Multi-domain]  Cd Length: 764  Bit Score: 76.81  E-value: 5.51e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1035685929  80 VIAAEDQKFPEHWGFDVASIEKALAHNERNENRIRGASTISQQTAKNLFLWDGRSWVRKGLEAGLTLGIETVWSKKRILT 159
Cdd:PRK14850  173 LLAIEDKYFYEHDGIHLSSIGRAFLVNLMSGHTIQGGSTLTQQLVKNLFLTNTRSLWRKINEIYMALILDRFYSKDRILE 252

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1035685929 160 VYLNIAEFG----DGVFGVEAAAQRYFHKPASKLTQSEAALL 197
Cdd:PRK14850  253 LYLNEVYLGqdgnEQIRGFPLASIYYFGRPINELNLDQYALL 294
 
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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