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Conserved domains on  [gi|489191617|ref|WP_003100972|]
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MULTISPECIES: monofunctional biosynthetic peptidoglycan transglycosylase [Pseudomonas]

Protein Classification

biosynthetic peptidoglycan transglycosylase( domain architecture ID 10020197)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
mono_pep_trsgly TIGR02070
monofunctional biosynthetic peptidoglycan transglycosylase; This family is one of the ...
14-235 8.63e-125

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: 352.92  E-value: 8.63e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489191617   14 RSLFRRLFKYLLWFMAASVVLVAVLRWVPPPGTMVMVERKVGSWVDGQP-IDLQRDWRSWEQLPDSLKVAVIAGEDQHFA 92
Cdd:TIGR02070   1 GYVIGCLVAGVLLFNLAVFAALASWRFVPPPSTAFMVAEKLALWGQGDPtCGIQHRWRPYDQISPNLKRAVIASEDAKFV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489191617   93 EHHGFDLPAIQQALAHNERGG-SIRGASTLSQQVAKNVFLWSGRSWLRKGLEAWFTLLIETLWTKQRILEVYLNSAEWGP 171
Cdd:TIGR02070  81 EHHGFDWEAIQDALEKNEKSGkVVRGGSTISQQLAKNLFLWSGRSYLRKGLEAWATWMLETWWSKQRILEVYLNSVEWGN 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489191617  172 GVFGAQAAARYHFGLDAERLSRTQASQLAAVLPSPLKWSAARPGPYVRQRAAWIRQQMWQLGGD 235
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 ...
14-235 8.63e-125

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: 352.92  E-value: 8.63e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489191617   14 RSLFRRLFKYLLWFMAASVVLVAVLRWVPPPGTMVMVERKVGSWVDGQP-IDLQRDWRSWEQLPDSLKVAVIAGEDQHFA 92
Cdd:TIGR02070   1 GYVIGCLVAGVLLFNLAVFAALASWRFVPPPSTAFMVAEKLALWGQGDPtCGIQHRWRPYDQISPNLKRAVIASEDAKFV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489191617   93 EHHGFDLPAIQQALAHNERGG-SIRGASTLSQQVAKNVFLWSGRSWLRKGLEAWFTLLIETLWTKQRILEVYLNSAEWGP 171
Cdd:TIGR02070  81 EHHGFDWEAIQDALEKNEKSGkVVRGGSTISQQLAKNLFLWSGRSYLRKGLEAWATWMLETWWSKQRILEVYLNSVEWGN 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489191617  172 GVFGAQAAARYHFGLDAERLSRTQASQLAAVLPSPLKWSAARPGPYVRQRAAWIRQQMWQLGGD 235
Cdd:TIGR02070 161 GVFGAEAAARYYFKRSASNLTRGQAARLAAVLPNPKYYDENRPGPYVRRKATWILKQMGYLGLP 224
MrcB COG0744
Penicillin-binding protein 1B/1F, peptidoglycan transglycosylase/transpeptidase [Cell wall ...
1-233 6.04e-68

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


Pssm-ID: 440507 [Multi-domain]  Cd Length: 630  Bit Score: 220.56  E-value: 6.04e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489191617   1 MAAPffQAKPRMLRSLFRRLFKYLLWFMAASVVLVAVLRW--VPPPGTMVMVERKVGS---WVDGQPI----DLQRDWRS 71
Cdd:COG0744    1 MAKP--RRGKRLLRRLLGLLLLLLAVLVLAALAGLVALYVadLPDPEELEDLALPQTStiyDRDGTLIatlgDENREWVP 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489191617  72 WEQLPDSLKVAVIAGEDQHFAEHHGFDLPAIQQALAHNERGGSI-RGASTLSQQVAKNVFLWSGRSWLRKGLEAWFTLLI 150
Cdd:COG0744   79 LDQIPPHLKDAVVAIEDRRFYEHGGVDPKGIARALVANLTAGGVvQGGSTITQQLVKNLFLSNERTLSRKLKEALLALKL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489191617 151 ETLWTKQRILEVYLNSAEWGPGVFGAQAAARYHFGLDAERLSRTQASQLAAVLPSPLKWSAARPGPYVRQRAAWIRQQMW 230
Cdd:COG0744  159 ERKYSKDEILELYLNTVYFGRGAYGIEAAAQYYFGKSASDLTLAEAALLAGLVKAPSYYDPYRNPEAAKERRNLVLDRMV 238

                 ...
gi 489191617 231 QLG 233
Cdd:COG0744  239 EQG 241
Transgly pfam00912
Transglycosylase; The penicillin-binding proteins are bifunctional proteins consisting of ...
59-229 3.30e-63

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: 195.05  E-value: 3.30e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489191617   59 DGQPI----DLQRDWRSWEQLPDSLKVAVIAGEDQHFAEHHGFDLPAIQQALAHNERGGSI-RGASTLSQQVAKNVFLWS 133
Cdd:pfam00912   1 DGTLLaelgEENREYVPLDDIPPALKNAVLAIEDRRFYEHGGVDPKGIARALLSNLRSGRIvQGGSTITQQLAKNLFLTP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489191617  134 GRSWLRKGLEAWFTLLIETLWTKQRILEVYLNSAEWGPGVFGAQAAARYHFGLDAERLSRTQASQLAAVLPSPLKWSAAR 213
Cdd:pfam00912  81 ERTLTRKLKEAVLALKLERRYSKDEILEAYLNTVYFGRGAYGIEAAARAYFGKDASDLTLAEAALLAGLPQAPSRYNPLR 160
                         170
                  ....*....|....*.
gi 489191617  214 PGPYVRQRAAWIRQQM 229
Cdd:pfam00912 161 NPERAKRRRNLVLDRM 176
mrcB PRK09506
bifunctional glycosyl transferase/transpeptidase; Reviewed
76-199 1.31e-20

bifunctional glycosyl transferase/transpeptidase; Reviewed


Pssm-ID: 236544 [Multi-domain]  Cd Length: 830  Bit Score: 90.21  E-value: 1.31e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489191617  76 PDSLKVAVIAGEDQHFAEHHGFDLPAIQQA-LAHNERGGSIRGASTLSQQVAKNVFLWSGRSWLRKGLEAWFTLLIETLW 154
Cdd:PRK09506 220 PDLLVDTLLATEDRHFYEHDGISLYSIGRAvLANLTAGRTVQGGSTLTQQLVKNLFLSNERSLWRKANEAYMALIMDARY 299
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 489191617 155 TKQRILEVYLNSAEWGPG----VFGAQAAARYHFGLDAERLSRTQASQL 199
Cdd:PRK09506 300 SKDRILELYLNEVYLGQSgddqIRGFPLASLYYFGRPVEELSLDQQALL 348
 
Name Accession Description Interval E-value
mono_pep_trsgly TIGR02070
monofunctional biosynthetic peptidoglycan transglycosylase; This family is one of the ...
14-235 8.63e-125

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: 352.92  E-value: 8.63e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489191617   14 RSLFRRLFKYLLWFMAASVVLVAVLRWVPPPGTMVMVERKVGSWVDGQP-IDLQRDWRSWEQLPDSLKVAVIAGEDQHFA 92
Cdd:TIGR02070   1 GYVIGCLVAGVLLFNLAVFAALASWRFVPPPSTAFMVAEKLALWGQGDPtCGIQHRWRPYDQISPNLKRAVIASEDAKFV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489191617   93 EHHGFDLPAIQQALAHNERGG-SIRGASTLSQQVAKNVFLWSGRSWLRKGLEAWFTLLIETLWTKQRILEVYLNSAEWGP 171
Cdd:TIGR02070  81 EHHGFDWEAIQDALEKNEKSGkVVRGGSTISQQLAKNLFLWSGRSYLRKGLEAWATWMLETWWSKQRILEVYLNSVEWGN 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489191617  172 GVFGAQAAARYHFGLDAERLSRTQASQLAAVLPSPLKWSAARPGPYVRQRAAWIRQQMWQLGGD 235
Cdd:TIGR02070 161 GVFGAEAAARYYFKRSASNLTRGQAARLAAVLPNPKYYDENRPGPYVRRKATWILKQMGYLGLP 224
MrcB COG0744
Penicillin-binding protein 1B/1F, peptidoglycan transglycosylase/transpeptidase [Cell wall ...
1-233 6.04e-68

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


Pssm-ID: 440507 [Multi-domain]  Cd Length: 630  Bit Score: 220.56  E-value: 6.04e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489191617   1 MAAPffQAKPRMLRSLFRRLFKYLLWFMAASVVLVAVLRW--VPPPGTMVMVERKVGS---WVDGQPI----DLQRDWRS 71
Cdd:COG0744    1 MAKP--RRGKRLLRRLLGLLLLLLAVLVLAALAGLVALYVadLPDPEELEDLALPQTStiyDRDGTLIatlgDENREWVP 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489191617  72 WEQLPDSLKVAVIAGEDQHFAEHHGFDLPAIQQALAHNERGGSI-RGASTLSQQVAKNVFLWSGRSWLRKGLEAWFTLLI 150
Cdd:COG0744   79 LDQIPPHLKDAVVAIEDRRFYEHGGVDPKGIARALVANLTAGGVvQGGSTITQQLVKNLFLSNERTLSRKLKEALLALKL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489191617 151 ETLWTKQRILEVYLNSAEWGPGVFGAQAAARYHFGLDAERLSRTQASQLAAVLPSPLKWSAARPGPYVRQRAAWIRQQMW 230
Cdd:COG0744  159 ERKYSKDEILELYLNTVYFGRGAYGIEAAAQYYFGKSASDLTLAEAALLAGLVKAPSYYDPYRNPEAAKERRNLVLDRMV 238

                 ...
gi 489191617 231 QLG 233
Cdd:COG0744  239 EQG 241
Transgly pfam00912
Transglycosylase; The penicillin-binding proteins are bifunctional proteins consisting of ...
59-229 3.30e-63

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: 195.05  E-value: 3.30e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489191617   59 DGQPI----DLQRDWRSWEQLPDSLKVAVIAGEDQHFAEHHGFDLPAIQQALAHNERGGSI-RGASTLSQQVAKNVFLWS 133
Cdd:pfam00912   1 DGTLLaelgEENREYVPLDDIPPALKNAVLAIEDRRFYEHGGVDPKGIARALLSNLRSGRIvQGGSTITQQLAKNLFLTP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489191617  134 GRSWLRKGLEAWFTLLIETLWTKQRILEVYLNSAEWGPGVFGAQAAARYHFGLDAERLSRTQASQLAAVLPSPLKWSAAR 213
Cdd:pfam00912  81 ERTLTRKLKEAVLALKLERRYSKDEILEAYLNTVYFGRGAYGIEAAARAYFGKDASDLTLAEAALLAGLPQAPSRYNPLR 160
                         170
                  ....*....|....*.
gi 489191617  214 PGPYVRQRAAWIRQQM 229
Cdd:pfam00912 161 NPERAKRRRNLVLDRM 176
MrcA COG5009
Membrane carboxypeptidase/penicillin-binding protein [Cell wall/membrane/envelope biogenesis];
18-233 1.48e-37

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


Pssm-ID: 444033 [Multi-domain]  Cd Length: 785  Bit Score: 139.14  E-value: 1.48e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489191617  18 RRLFKYLLWFMAASVVLVAVLRWV---------PPPGTMVMVERKVGSWV---DGQPID---LQRdwRSW---EQLPDSL 79
Cdd:COG5009    1 MRLLKILLILLLLLLLLGALAVAGlylylspdlPDVETLKDYQPPTPSRVysaDGKLIAefgEER--RIPvpiEEIPPLL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489191617  80 KVAVIAGEDQHFAEHHGFDLPAIQQALAHNERGGSI-RGASTLSQQVAKNVFLWSGRSWLRKGLEAWFTLLIETLWTKQR 158
Cdd:COG5009   79 INAFLAAEDKRFYEHPGVDPIGIARAAVVNLRTGRRvQGGSTITQQVAKNFLLSPERTLTRKIKEAILALRIEQELSKDE 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489191617 159 ILEVYLNSAEWGPGVFGAQAAARYHFGLDAERLSRTQASQLAAVLPSPLKWSaarpgPYVRQRAAWIRQ-----QMWQLG 233
Cdd:COG5009  159 ILELYLNKIYLGHRAYGVAAAAQTYFGKSLDELTLAEAAMLAGLPKAPSRYN-----PIRNPERALERRnyvlgRMLELG 233
PbpC COG4953
Membrane carboxypeptidase/penicillin-binding protein PbpC [Cell wall/membrane/envelope ...
13-233 5.94e-29

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


Pssm-ID: 443980 [Multi-domain]  Cd Length: 773  Bit Score: 114.54  E-value: 5.94e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489191617  13 LRSLFRRLFKYLLWFMAASVVLVAVLRWVPPPG------TMVMVERkvgswvDGQPIDLQRD----WRSW---EQLPDSL 79
Cdd:COG4953    4 ARLRRRRLLALLLALLLLALALWALDRLFPLPLlfavpySTVVLDR------DGTLLRAFLAadgqWRLPvplDEVSPRY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489191617  80 KVAVIAGEDQHFAEHHGFDLPAIQQALAHNERGGSI-RGASTLSQQVAKnvFLW-SGRSWLRKGLEAWFTLLIETLWTKQ 157
Cdd:COG4953   78 LQALLAYEDRRFYYHPGVNPLALLRAAWQNLRSGRIvSGGSTLTMQVAR--LLEpRPRTLSGKLRQILRALQLERRYSKD 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489191617 158 RILEVYLNSAEWGPGVFGAQAAARYHFGLDAERLSRTQASQLaAVLP-SPlkwSAARPGPYvRQRAAWIR----QQMWQL 232
Cdd:COG4953  156 EILELYLNLAPYGGNIEGVEAASLAYFGKPPSRLSLAEAALL-AVLPqAP---SRRRPDRN-PERARAARdrvlARLAEA 230

                 .
gi 489191617 233 G 233
Cdd:COG4953  231 G 231
mrcB PRK09506
bifunctional glycosyl transferase/transpeptidase; Reviewed
76-199 1.31e-20

bifunctional glycosyl transferase/transpeptidase; Reviewed


Pssm-ID: 236544 [Multi-domain]  Cd Length: 830  Bit Score: 90.21  E-value: 1.31e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489191617  76 PDSLKVAVIAGEDQHFAEHHGFDLPAIQQA-LAHNERGGSIRGASTLSQQVAKNVFLWSGRSWLRKGLEAWFTLLIETLW 154
Cdd:PRK09506 220 PDLLVDTLLATEDRHFYEHDGISLYSIGRAvLANLTAGRTVQGGSTLTQQLVKNLFLSNERSLWRKANEAYMALIMDARY 299
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 489191617 155 TKQRILEVYLNSAEWGPG----VFGAQAAARYHFGLDAERLSRTQASQL 199
Cdd:PRK09506 300 SKDRILELYLNEVYLGQSgddqIRGFPLASLYYFGRPVEELSLDQQALL 348
PRK13481 PRK13481
glycosyltransferase; Provisional
59-185 1.37e-20

glycosyltransferase; Provisional


Pssm-ID: 184078 [Multi-domain]  Cd Length: 232  Bit Score: 86.78  E-value: 1.37e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489191617  59 DGQPIDLQRDWRSWEQLPDSLKVAVIAGEDQHFAEHHGFDLPAIQQALAHNERGGSIRGASTLSQQVAKNVFLWSGRSWL 138
Cdd:PRK13481  37 ELRKIENKSSFVSADNMPEYVKGAFISMEDERFYKHHGFDLKGTTRALFSTISDRDVQGGSTITQQVVKNYFYDNERSFT 116
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 489191617 139 RKGLEAWFTLLIETLWTKQRILEVYLNSAEWGPGVFGAQAAARYHFG 185
Cdd:PRK13481 117 RKVKELFVAHRVEKQYSKNEILSFYLNNIYFGDNQYTLEGAANHYFG 163
mrcA PRK11636
penicillin-binding protein 1a; Provisional
73-206 3.25e-20

penicillin-binding protein 1a; Provisional


Pssm-ID: 183248 [Multi-domain]  Cd Length: 850  Bit Score: 89.03  E-value: 3.25e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489191617  73 EQLPDSLKVAVIAGEDQHFAEHHGFDLPAIQQALA-HNERGGSIRGASTLSQQVAKNVFLWSGRSWLRKGLEAWFTLLIE 151
Cdd:PRK11636  72 DQIPPEMVKAFIATEDSRFYEHHGVDPVGIFRAASvALFSGHASQGASTITQQLARNFFLSPERTLMRKIKEAFLAIRIE 151
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489191617 152 TLWTKQRILEVYLNSAEWGPGVFGAQAAARYHFGLDAERLSRTQASQLAAVLPSP 206
Cdd:PRK11636 152 QLLTKDEILELYLNKIYLGYRAYGVGAAAQVYFGKTVDQLTLSEMAVIAGLPKAP 206
PRK14850 PRK14850
penicillin-binding protein 1b; Provisional
66-199 7.08e-19

penicillin-binding protein 1b; Provisional


Pssm-ID: 237835 [Multi-domain]  Cd Length: 764  Bit Score: 85.28  E-value: 7.08e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489191617  66 QRDWRSWEQLPDSLKVAVIAGEDQHFAEHHGFDLPAIQQA-LAHNERGGSIRGASTLSQQVAKNVFLWSGRSWLRKGLEA 144
Cdd:PRK14850 156 KRLFIPRNQYPEMLIKTLLAIEDKYFYEHDGIHLSSIGRAfLVNLMSGHTIQGGSTLTQQLVKNLFLTNTRSLWRKINEI 235
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 489191617 145 WFTLLIETLWTKQRILEVYLNSAEWGPG----VFGAQAAARYHFGLDAERLSRTQASQL 199
Cdd:PRK14850 236 YMALILDRFYSKDRILELYLNEVYLGQDgneqIRGFPLASIYYFGRPINELNLDQYALL 294
PRK11240 PRK11240
penicillin-binding protein 1C; Provisional
17-230 1.29e-09

penicillin-binding protein 1C; Provisional


Pssm-ID: 183049 [Multi-domain]  Cd Length: 772  Bit Score: 57.79  E-value: 1.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489191617  17 FRRLFKYLLWFMAASVVLVAVL----RWVPPPGTMVMVERKVGSwVDGQPI----DLQRDWR---SWEQLPDSLKVAVIA 85
Cdd:PRK11240   2 LLTKRGRWLWLAAAPLLLFLALwladKLWPLPLHEVNPARVVVA-EDGTPLwrfaDADGIWRypvTIEDVSPRYLEALIN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489191617  86 GEDQHFAEHHGFDLPAIQQALAHNERGGSI-RGASTLSQQVAKnVFLWSGRSWLRKGLEAWFTLLIETLWTKQRILEVYL 164
Cdd:PRK11240  81 YEDRWFWKHPGVNPFSVARAAWQDLTSGRViSGGSTLTMQVAR-LLDPHPRTFGGKIRQLWRALQLEWHLSKREILTLYL 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489191617 165 NSAEWGPGVFGAQAAARYHFGLDAERLSRTQASqLAAVLPS----------PLKWSAARPGpyVRQRAAwiRQQMW 230
Cdd:PRK11240 160 NRAPFGGTLQGIGAASWAYLGKSPANLSYAEAA-LLAVLPQapsrlrpdrwPERAEAARNK--VLERMA--EQGVW 230
 
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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