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Conserved domains on  [gi|835513023|ref|WP_047535318|]
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MULTISPECIES: monofunctional biosynthetic peptidoglycan transglycosylase [Shewanella]

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
 30-247 8.27e-94

glycosyltransferase; Provisional


The actual alignment was detected with superfamily member TIGR02070:

Pssm-ID: 475222 [Multi-domain]  Cd Length: 224  Bit Score: 275.11  E-value: 8.27e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835513023   30 KRVFIWLAKLVLGLFFASILSVVLLRFIDPPMWSWRIERAL---FPPAPITEVRHRWRSLEQISPELQLAVIAAEDQKFA 106
Cdd:TIGR02070   1 GYVIGCLVAGVLLFNLAVFAALASWRFVPPPSTAFMVAEKLalwGQGDPTCGIQHRWRPYDQISPNLKRAVIASEDAKFV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835513023  107 GHSGFDLDAISSAIEYNQK-GKKVRGASTLSQQAAKNLFMWSSRSFIRKGIEAWFTLLMELFWDKARILEVYLNIVEFGP 185
Cdd:TIGR02070  81 EHHGFDWEAIQDALEKNEKsGKVVRGGSTISQQLAKNLFLWSGRSYLRKGLEAWATWMLETWWSKQRILEVYLNSVEWGN 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 835513023  186 GIYGAEAAAKHYFGKSAAKLTRYEASLLAAVLPNPWRYKVSPPSSYVEQRSAWIRKQMRQLG 247
Cdd:TIGR02070 161 GVFGAEAAARYYFKRSASNLTRGQAARLAAVLPNPKYYDENRPGPYVRRKATWILKQMGYLG 222
 
Name Accession Description Interval E-value
mono_pep_trsgly TIGR02070
monofunctional biosynthetic peptidoglycan transglycosylase; This family is one of the ...
 30-247 8.27e-94

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: 275.11  E-value: 8.27e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835513023   30 KRVFIWLAKLVLGLFFASILSVVLLRFIDPPMWSWRIERAL---FPPAPITEVRHRWRSLEQISPELQLAVIAAEDQKFA 106
Cdd:TIGR02070   1 GYVIGCLVAGVLLFNLAVFAALASWRFVPPPSTAFMVAEKLalwGQGDPTCGIQHRWRPYDQISPNLKRAVIASEDAKFV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835513023  107 GHSGFDLDAISSAIEYNQK-GKKVRGASTLSQQAAKNLFMWSSRSFIRKGIEAWFTLLMELFWDKARILEVYLNIVEFGP 185
Cdd:TIGR02070  81 EHHGFDWEAIQDALEKNEKsGKVVRGGSTISQQLAKNLFLWSGRSYLRKGLEAWATWMLETWWSKQRILEVYLNSVEWGN 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 835513023  186 GIYGAEAAAKHYFGKSAAKLTRYEASLLAAVLPNPWRYKVSPPSSYVEQRSAWIRKQMRQLG 247
Cdd:TIGR02070 161 GVFGAEAAARYYFKRSASNLTRGQAARLAAVLPNPKYYDENRPGPYVRRKATWILKQMGYLG 222
MrcB COG0744
Penicillin-binding protein 1B/1F, peptidoglycan transglycosylase/transpeptidase [Cell wall ...
 20-250 1.07e-68

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


Pssm-ID: 440507 [Multi-domain]  Cd Length: 630  Bit Score: 222.87  E-value: 1.07e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835513023  20 PTPKPKMRGVKRVFIWLAKLVLGLFFASILSVVLLRFIDPPMWSWRIERALFPP-----------APITEVRHRWRSLEQ 88
Cdd:COG0744    2 AKPRRGKRLLRRLLGLLLLLLAVLVLAALAGLVALYVADLPDPEELEDLALPQTstiydrdgtliATLGDENREWVPLDQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835513023  89 ISPELQLAVIAAEDQKFAGHSGFDLDAISSAIEYN-QKGKKVRGASTLSQQAAKNLFMWSSRSFIRKGIEAWFTLLMELF 167
Cdd:COG0744   82 IPPHLKDAVVAIEDRRFYEHGGVDPKGIARALVANlTAGGVVQGGSTITQQLVKNLFLSNERTLSRKLKEALLALKLERK 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835513023 168 WDKARILEVYLNIVEFGPGIYGAEAAAKHYFGKSAAKLTRYEASLLAAVLPNPWRYKVSPPSSYVEQRSAWIRKQMRQLG 247
Cdd:COG0744  162 YSKDEILELYLNTVYFGRGAYGIEAAAQYYFGKSASDLTLAEAALLAGLVKAPSYYDPYRNPEAAKERRNLVLDRMVEQG 241


                 ...
gi 835513023 248 EVT 250
Cdd:COG0744  242 YIT 244
Transgly pfam00912
Transglycosylase; The penicillin-binding proteins are bifunctional proteins consisting of ...
 74-243 3.58e-66

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: 203.14  E-value: 3.58e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835513023   74 APITEVRHRWRSLEQISPELQLAVIAAEDQKFAGHSGFDLDAISSAIEYN-QKGKKVRGASTLSQQAAKNLFMWSSRSFI 152
Cdd:pfam00912   6 AELGEENREYVPLDDIPPALKNAVLAIEDRRFYEHGGVDPKGIARALLSNlRSGRIVQGGSTITQQLAKNLFLTPERTLT 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835513023  153 RKGIEAWFTLLMELFWDKARILEVYLNIVEFGPGIYGAEAAAKHYFGKSAAKLTRYEASLLAAVLPNPWRYKVSPPSSYV 232
Cdd:pfam00912  86 RKLKEAVLALKLERRYSKDEILEAYLNTVYFGRGAYGIEAAARAYFGKDASDLTLAEAALLAGLPQAPSRYNPLRNPERA 165

                         170
                  ....*....|.
gi 835513023  233 EQRSAWIRKQM 243
Cdd:pfam00912 166 KRRRNLVLDRM 176
PRK13481 PRK13481
glycosyltransferase; Provisional
 96-257 2.28e-24

glycosyltransferase; Provisional


Pssm-ID: 184078 [Multi-domain]  Cd Length: 232  Bit Score: 97.18  E-value: 2.28e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835513023  96 AVIAAEDQKFAGHSGFDLDAISSAIEYNQKGKKVRGASTLSQQAAKNLFMWSSRSFIRKGIEAWFTLLMELFWDKARILE 175
Cdd:PRK13481  60 AFISMEDERFYKHHGFDLKGTTRALFSTISDRDVQGGSTITQQVVKNYFYDNERSFTRKVKELFVAHRVEKQYSKNEILS 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835513023 176 VYLNIVEFGPGIYGAEAAAKHYFGKSAAK-------LTRYEASLLAAVLPNPWRYKVSPPSSYVEQRSAWIRKQMRQLGE 248
Cdd:PRK13481 140 FYLNNIYFGDNQYTLEGAANHYFGTTVNKnsttmshITVLQSAILASKVNAPSVYNINDMSENFTQRVSTNLEKMKQQNY 219


                 ....*....
gi 835513023 249 VTLKKVGEA 257
Cdd:PRK13481 220 INETQYQQA 228
 
Name Accession Description Interval E-value
mono_pep_trsgly TIGR02070
monofunctional biosynthetic peptidoglycan transglycosylase; This family is one of the ...
 30-247 8.27e-94

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: 275.11  E-value: 8.27e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835513023   30 KRVFIWLAKLVLGLFFASILSVVLLRFIDPPMWSWRIERAL---FPPAPITEVRHRWRSLEQISPELQLAVIAAEDQKFA 106
Cdd:TIGR02070   1 GYVIGCLVAGVLLFNLAVFAALASWRFVPPPSTAFMVAEKLalwGQGDPTCGIQHRWRPYDQISPNLKRAVIASEDAKFV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835513023  107 GHSGFDLDAISSAIEYNQK-GKKVRGASTLSQQAAKNLFMWSSRSFIRKGIEAWFTLLMELFWDKARILEVYLNIVEFGP 185
Cdd:TIGR02070  81 EHHGFDWEAIQDALEKNEKsGKVVRGGSTISQQLAKNLFLWSGRSYLRKGLEAWATWMLETWWSKQRILEVYLNSVEWGN 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 835513023  186 GIYGAEAAAKHYFGKSAAKLTRYEASLLAAVLPNPWRYKVSPPSSYVEQRSAWIRKQMRQLG 247
Cdd:TIGR02070 161 GVFGAEAAARYYFKRSASNLTRGQAARLAAVLPNPKYYDENRPGPYVRRKATWILKQMGYLG 222
MrcB COG0744
Penicillin-binding protein 1B/1F, peptidoglycan transglycosylase/transpeptidase [Cell wall ...
 20-250 1.07e-68

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


Pssm-ID: 440507 [Multi-domain]  Cd Length: 630  Bit Score: 222.87  E-value: 1.07e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835513023  20 PTPKPKMRGVKRVFIWLAKLVLGLFFASILSVVLLRFIDPPMWSWRIERALFPP-----------APITEVRHRWRSLEQ 88
Cdd:COG0744    2 AKPRRGKRLLRRLLGLLLLLLAVLVLAALAGLVALYVADLPDPEELEDLALPQTstiydrdgtliATLGDENREWVPLDQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835513023  89 ISPELQLAVIAAEDQKFAGHSGFDLDAISSAIEYN-QKGKKVRGASTLSQQAAKNLFMWSSRSFIRKGIEAWFTLLMELF 167
Cdd:COG0744   82 IPPHLKDAVVAIEDRRFYEHGGVDPKGIARALVANlTAGGVVQGGSTITQQLVKNLFLSNERTLSRKLKEALLALKLERK 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835513023 168 WDKARILEVYLNIVEFGPGIYGAEAAAKHYFGKSAAKLTRYEASLLAAVLPNPWRYKVSPPSSYVEQRSAWIRKQMRQLG 247
Cdd:COG0744  162 YSKDEILELYLNTVYFGRGAYGIEAAAQYYFGKSASDLTLAEAALLAGLVKAPSYYDPYRNPEAAKERRNLVLDRMVEQG 241


                 ...
gi 835513023 248 EVT 250
Cdd:COG0744  242 YIT 244
Transgly pfam00912
Transglycosylase; The penicillin-binding proteins are bifunctional proteins consisting of ...
 74-243 3.58e-66

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: 203.14  E-value: 3.58e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835513023   74 APITEVRHRWRSLEQISPELQLAVIAAEDQKFAGHSGFDLDAISSAIEYN-QKGKKVRGASTLSQQAAKNLFMWSSRSFI 152
Cdd:pfam00912   6 AELGEENREYVPLDDIPPALKNAVLAIEDRRFYEHGGVDPKGIARALLSNlRSGRIVQGGSTITQQLAKNLFLTPERTLT 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835513023  153 RKGIEAWFTLLMELFWDKARILEVYLNIVEFGPGIYGAEAAAKHYFGKSAAKLTRYEASLLAAVLPNPWRYKVSPPSSYV 232
Cdd:pfam00912  86 RKLKEAVLALKLERRYSKDEILEAYLNTVYFGRGAYGIEAAARAYFGKDASDLTLAEAALLAGLPQAPSRYNPLRNPERA 165

                         170
                  ....*....|.
gi 835513023  233 EQRSAWIRKQM 243
Cdd:pfam00912 166 KRRRNLVLDRM 176
PBP_1a_fam TIGR02074
penicillin-binding protein, 1A family; Bacterial that synthesize a cell wall of peptidoglycan ...
 85-250 3.05e-44

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: 156.27  E-value: 3.05e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835513023   85 SLEQISPELQLAVIAAEDQKFAGHSGFDLDAISSAIEYN-QKGKKVRGASTLSQQAAKNLFMWSSRSFIRKGIEAWFTLL 163
Cdd:TIGR02074   6 PIDDIPENLINAFLAIEDRRFYDHFGIDLKGIGRAAVANiTSGRVLEGGSTITQQLAKNLYLTNERTITRKIQEALLALK 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835513023  164 MELFWDKARILEVYLNIVEFGPGIYGAEAAAKHYFGKSAAKLTRYEASLLAAVLPNPWRYkvSPPS--SYVEQRSAWIRK 241
Cdd:TIGR02074  86 LEQKLSKDEILELYLNRIYFGNGAYGIEAAAQFYFGKSVNDLTLAEAAMLAGLPKAPSAY--NPFKnpERAKDRRNLVLS 163


                  ....*....
gi 835513023  242 QMRQLGEVT 250
Cdd:TIGR02074 164 NMVENGYIT 172
MrcA COG5009
Membrane carboxypeptidase/penicillin-binding protein [Cell wall/membrane/envelope biogenesis];
30-250 1.61e-41

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


Pssm-ID: 444033 [Multi-domain]  Cd Length: 785  Bit Score: 151.08  E-value: 1.61e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835513023  30 KRVFIWLAKLVLGLFFASILSV-VLLRFIDPPMWSWRIERALFPPAP----------ITEVRHRWR---SLEQISPELQL 95
Cdd:COG5009    1 MRLLKILLILLLLLLLLGALAVaGLYLYLSPDLPDVETLKDYQPPTPsrvysadgklIAEFGEERRipvPIEEIPPLLIN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835513023  96 AVIAAEDQKFAGHSGFDLDAISSA-IEYNQKGKKVRGASTLSQQAAKNLFMWSSRSFIRKGIEAWFTLLMELFWDKARIL 174
Cdd:COG5009   81 AFLAAEDKRFYEHPGVDPIGIARAaVVNLRTGRRVQGGSTITQQVAKNFLLSPERTLTRKIKEAILALRIEQELSKDEIL 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 835513023 175 EVYLNIVEFGPGIYGAEAAAKHYFGKSAAKLTRYEASLLAAVLPNPWRYkvSPPSSYV--EQRSAWIRKQMRQLGEVT 250
Cdd:COG5009  161 ELYLNKIYLGHRAYGVAAAAQTYFGKSLDELTLAEAAMLAGLPKAPSRY--NPIRNPEraLERRNYVLGRMLELGYIT 236
PbpC COG4953
Membrane carboxypeptidase/penicillin-binding protein PbpC [Cell wall/membrane/envelope ...
 26-219 5.59e-36

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


Pssm-ID: 443980 [Multi-domain]  Cd Length: 773  Bit Score: 135.34  E-value: 5.59e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835513023  26 MRGVKRVFIWLAKLVLGLFFASILSVVLLRFIDPPmwswrierALFPPAPITEVR--------------HRWR---SLEQ 88
Cdd:COG4953    1 MKRARLRRRRLLALLLALLLLALALWALDRLFPLP--------LLFAVPYSTVVLdrdgtllraflaadGQWRlpvPLDE 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835513023  89 ISPELQLAVIAAEDQKFAGHSGFDLDAISSAIEYN-QKGKKVRGASTLSQQAAKNLFMwSSRSFIRKGIEAWFTLLMELF 167
Cdd:COG4953   73 VSPRYLQALLAYEDRRFYYHPGVNPLALLRAAWQNlRSGRIVSGGSTLTMQVARLLEP-RPRTLSGKLRQILRALQLERR 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 835513023 168 WDKARILEVYLNIVEFGPGIYGAEAAAKHYFGKSAAKLTRYEASLLaAVLPN 219
Cdd:COG4953  152 YSKDEILELYLNLAPYGGNIEGVEAASLAYFGKPPSRLSLAEAALL-AVLPQ 202
PBP_1c TIGR02073
penicillin-binding protein 1C; This subfamily of the penicillin binding proteins includes the ...
 78-223 4.11e-28

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: 112.51  E-value: 4.11e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835513023   78 EVRHRWRSLEQISPELQLAVIAAEDQKFAGHSGFDLDAISSAIEYNQKGKKVR-GASTLSQQAAKNLFMWSSRSFIRKGI 156
Cdd:TIGR02073  30 GQWRLPVPLEDISPKFLQALLLYEDKRFYWHPGVNPLALLRAAWQNLTNGRRVsGGSTLTMQLARLLDPELSRTLTGKLR 109

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 835513023  157 EAWFTLLMELFWDKARILEVYLNIVEFGPGIYGAEAAAKHYFGKSAAKLTRYEASLLAAVLPNPWRY 223
Cdd:TIGR02073 110 QMWRAIQLEARYSKREILEAYLNLAPYGGNLEGLRAASLIYFGKEPSSLSLAEAALLAALPQAPSAR 176
PRK13481 PRK13481
glycosyltransferase; Provisional
 96-257 2.28e-24

glycosyltransferase; Provisional


Pssm-ID: 184078 [Multi-domain]  Cd Length: 232  Bit Score: 97.18  E-value: 2.28e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835513023  96 AVIAAEDQKFAGHSGFDLDAISSAIEYNQKGKKVRGASTLSQQAAKNLFMWSSRSFIRKGIEAWFTLLMELFWDKARILE 175
Cdd:PRK13481  60 AFISMEDERFYKHHGFDLKGTTRALFSTISDRDVQGGSTITQQVVKNYFYDNERSFTRKVKELFVAHRVEKQYSKNEILS 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835513023 176 VYLNIVEFGPGIYGAEAAAKHYFGKSAAK-------LTRYEASLLAAVLPNPWRYKVSPPSSYVEQRSAWIRKQMRQLGE 248
Cdd:PRK13481 140 FYLNNIYFGDNQYTLEGAANHYFGTTVNKnsttmshITVLQSAILASKVNAPSVYNINDMSENFTQRVSTNLEKMKQQNY 219


                 ....*....
gi 835513023 249 VTLKKVGEA 257
Cdd:PRK13481 220 INETQYQQA 228
mrcB PRK09506
bifunctional glycosyl transferase/transpeptidase; Reviewed
 98-222 4.18e-23

bifunctional glycosyl transferase/transpeptidase; Reviewed


Pssm-ID: 236544 [Multi-domain]  Cd Length: 830  Bit Score: 97.92  E-value: 4.18e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835513023  98 IAAEDQKFAGHSGFDLDAISSAIEYN-QKGKKVRGASTLSQQAAKNLFMWSSRSFIRKGIEAWFTLLMELFWDKARILEV 176
Cdd:PRK09506 228 LATEDRHFYEHDGISLYSIGRAVLANlTAGRTVQGGSTLTQQLVKNLFLSNERSLWRKANEAYMALIMDARYSKDRILEL 307

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 835513023 177 YLNIVEFGPG----IYGAEAAAKHYFGKSAAKLTRYEASLL-----AAVLPNPWR 222
Cdd:PRK09506 308 YLNEVYLGQSgddqIRGFPLASLYYFGRPVEELSLDQQALLvgmvkGASLYNPWR 362
mrcA PRK11636
penicillin-binding protein 1a; Provisional
 26-218 5.36e-22

penicillin-binding protein 1a; Provisional


Pssm-ID: 183248 [Multi-domain]  Cd Length: 850  Bit Score: 94.81  E-value: 5.36e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835513023  26 MRGVKRVFIwLAKLVLGLFFASILSvvLLRFIDP---------------PMWSWRIERALFppAPITEVRHRWRSLEQIS 90
Cdd:PRK11636   1 MKFVKYLLI-LAVCCILLGAGSIYG--LYRYIEPqlpdvatlkdvrlqtPMQVYSADGELI--AQYGEKRRIPLTLDQIP 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835513023  91 PELQLAVIAAEDQKFAGHSGFD----LDAISSAIeynQKGKKVRGASTLSQQAAKNLFMWSSRSFIRKGIEAWFTLLMEL 166
Cdd:PRK11636  76 PEMVKAFIATEDSRFYEHHGVDpvgiFRAASVAL---FSGHASQGASTITQQLARNFFLSPERTLMRKIKEAFLAIRIEQ 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 835513023 167 FWDKARILEVYLNIVEFGPGIYGAEAAAKHYFGKSAAKLTRYEASLLAAvLP 218
Cdd:PRK11636 153 LLTKDEILELYLNKIYLGYRAYGVGAAAQVYFGKTVDQLTLSEMAVIAG-LP 203
PRK14850 PRK14850
penicillin-binding protein 1b; Provisional
 97-222 8.43e-19

penicillin-binding protein 1b; Provisional


Pssm-ID: 237835 [Multi-domain]  Cd Length: 764  Bit Score: 85.28  E-value: 8.43e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835513023  97 VIAAEDQKFAGHSGFDLDAISSAIEYN-QKGKKVRGASTLSQQAAKNLFMWSSRSFIRKGIEAWFTLLMELFWDKARILE 175
Cdd:PRK14850 173 LLAIEDKYFYEHDGIHLSSIGRAFLVNlMSGHTIQGGSTLTQQLVKNLFLTNTRSLWRKINEIYMALILDRFYSKDRILE 252

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 835513023 176 VYLNIVEFGPG----IYGAEAAAKHYFGKSAAKLTRYEASLL-----AAVLPNPWR 222
Cdd:PRK14850 253 LYLNEVYLGQDgneqIRGFPLASIYYFGRPINELNLDQYALLvgmvkGASLYNPWT 308
PRK11240 PRK11240
penicillin-binding protein 1C; Provisional
 83-248 1.99e-17

penicillin-binding protein 1C; Provisional


Pssm-ID: 183049 [Multi-domain]  Cd Length: 772  Bit Score: 81.28  E-value: 1.99e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835513023  83 WR---SLEQISPELQLAVIAAEDQKFAGHSGFDLDAISSAIEYN-QKGKKVRGASTLSQQAAKnLFMWSSRSFIRKGIEA 158
Cdd:PRK11240  61 WRypvTIEDVSPRYLEALINYEDRWFWKHPGVNPFSVARAAWQDlTSGRVISGGSTLTMQVAR-LLDPHPRTFGGKIRQL 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835513023 159 WFTLLMELFWDKARILEVYLNIVEFGPGIYGAEAAAKHYFGKSAAKLTRYEASLLaAVLPN-PWRYKvspPSSYVEQRSA 237
Cdd:PRK11240 140 WRALQLEWHLSKREILTLYLNRAPFGGTLQGIGAASWAYLGKSPANLSYAEAALL-AVLPQaPSRLR---PDRWPERAEA 215

                        170
                 ....*....|.
gi 835513023 238 WIRKQMRQLGE 248
Cdd:PRK11240 216 ARNKVLERMAE 226
 
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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