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Conserved domains on  [gi|446645529|ref|WP_000722875|]
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MULTISPECIES: serine hydrolase [Bacillus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
strep_PBP3 super family cl45725
streptococcal D-alanyl-D-alanine carboxypeptidase PBP3; PBP3 (penicillin-binding protein 3) is ...
 43-403 1.39e-102

streptococcal D-alanyl-D-alanine carboxypeptidase PBP3; PBP3 (penicillin-binding protein 3) is the lone D-alanyl-D-alanine carboxypeptidase in Streptococcus pneumoniae. The gene is known as pbp3 or dacA.


The actual alignment was detected with superfamily member NF038273:

Pssm-ID: 468443 [Multi-domain]  Cd Length: 407  Bit Score: 310.65  E-value: 1.39e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645529  43 TGKILHEQNPDELLAIASMSKLIVVYAVLEAIKEGKITWDTKVNISDYAYEVSRNNEFSNVPFEKgRQYTVKELYHSIVI 122
Cdd:NF038273  38 TGKILYEKDATTPVPIASLTKLLTAYLVYKEIKSGKLSWDTPVKISDYPYELTTNYEISNVPLDA-RKYTVKELLEASLV 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645529 123 FSANGSSIALAELLAGSEKNFLNLANEHAKKLGLKKYKFVNATGLNNADLKGKHPEGTDPNAENSMSARDMGMLSKTMIT 202
Cdd:NF038273 117 ASANSAAIALAEKIAGSEPKFVDKMKAQLKEWGITDAKLVNASGLNNSYLGDHIYPGSKKDDENKLSAKDVAIIARHLIK 196

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645529 203 KYPEMLEDTKQRFRNFPDNhpkpiRMENWNWMLPGAAFAYEGTDGLKTGSSDTAGYGFTITAKRGDVRLISVIIKTKSMD 282
Cdd:NF038273 197 DFPEVLKITSKTSADFAGT-----TIYSYNYMLKGMPYYREGVDGLKTGTTEKAGASFVATSVENGMRVITVVLNADNAD 271

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645529 283 E----RFTESRELIEYGFNNFEKQKL----KVNKNNTISVVKGKEDQVTVAPEKEITVIAKKGSKEPYKIGTELDKSlae 354
Cdd:NF038273 272 EdeyaRFTATNQLLDYIYQNFEKVTLvkkgQAYKDSKLPVIDGKKKTVSAVAKKDLTVIQKIGTDSKPSVKFTPKKK--- 348

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446645529 355 dgHLVAPIKKDAKVGSITLESTDKYG--FLDGSKSMKVTAKttEEVEKANW 403
Cdd:NF038273 349 --ELTAPIKKGQVVGKATFKDKDLIGkgYLGEPPSVELVAK--KDVKKSFF 395
 
Name Accession Description Interval E-value
strep_PBP3 NF038273
streptococcal D-alanyl-D-alanine carboxypeptidase PBP3; PBP3 (penicillin-binding protein 3) is ...
 43-403 1.39e-102

streptococcal D-alanyl-D-alanine carboxypeptidase PBP3; PBP3 (penicillin-binding protein 3) is the lone D-alanyl-D-alanine carboxypeptidase in Streptococcus pneumoniae. The gene is known as pbp3 or dacA.


Pssm-ID: 468443 [Multi-domain]  Cd Length: 407  Bit Score: 310.65  E-value: 1.39e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645529  43 TGKILHEQNPDELLAIASMSKLIVVYAVLEAIKEGKITWDTKVNISDYAYEVSRNNEFSNVPFEKgRQYTVKELYHSIVI 122
Cdd:NF038273  38 TGKILYEKDATTPVPIASLTKLLTAYLVYKEIKSGKLSWDTPVKISDYPYELTTNYEISNVPLDA-RKYTVKELLEASLV 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645529 123 FSANGSSIALAELLAGSEKNFLNLANEHAKKLGLKKYKFVNATGLNNADLKGKHPEGTDPNAENSMSARDMGMLSKTMIT 202
Cdd:NF038273 117 ASANSAAIALAEKIAGSEPKFVDKMKAQLKEWGITDAKLVNASGLNNSYLGDHIYPGSKKDDENKLSAKDVAIIARHLIK 196

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645529 203 KYPEMLEDTKQRFRNFPDNhpkpiRMENWNWMLPGAAFAYEGTDGLKTGSSDTAGYGFTITAKRGDVRLISVIIKTKSMD 282
Cdd:NF038273 197 DFPEVLKITSKTSADFAGT-----TIYSYNYMLKGMPYYREGVDGLKTGTTEKAGASFVATSVENGMRVITVVLNADNAD 271

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645529 283 E----RFTESRELIEYGFNNFEKQKL----KVNKNNTISVVKGKEDQVTVAPEKEITVIAKKGSKEPYKIGTELDKSlae 354
Cdd:NF038273 272 EdeyaRFTATNQLLDYIYQNFEKVTLvkkgQAYKDSKLPVIDGKKKTVSAVAKKDLTVIQKIGTDSKPSVKFTPKKK--- 348

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446645529 355 dgHLVAPIKKDAKVGSITLESTDKYG--FLDGSKSMKVTAKttEEVEKANW 403
Cdd:NF038273 349 --ELTAPIKKGQVVGKATFKDKDLIGkgYLGEPPSVELVAK--KDVKKSFF 395
DacC COG1686
D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis];
43-404 1.33e-91

D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441292 [Multi-domain]  Cd Length: 324  Bit Score: 279.41  E-value: 1.33e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645529  43 TGKILHEQNPDELLAIASMSKLIVVYAVLEAIKEGKITWDTKVNISDYAYEVsrnnEFSNVPFEKGRQYTVKELYHSIVI 122
Cdd:COG1686   38 TGQVLYEKNADERLPPASLTKLMTAYVVLEALKAGKISLDDKVTVSEEAART----GGSKMGLKPGEQVTVEDLLKGLLL 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645529 123 FSANGSSIALAELLAGSEKNFLNLANEHAKKLGLKKYKFVNATGLnnadlkgkhpegtdPNAENSMSARDMGMLSKTMIT 202
Cdd:COG1686  114 QSGNDAAVALAEHIAGSEEAFVALMNAKAKELGMTNTHFVNPTGL--------------PDPGHYSTARDLALLARAAIK 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645529 203 KYPEMLEDTKQRFRNFPDnhPKPIRMENWNWMLpgaaFAYEGTDGLKTGSSDTAGYGFTITAKRGDVRLISVIIKTKSMD 282
Cdd:COG1686  180 DYPEFYEIFSTKEFTFPN--GRGITLRNTNRLL----GRYPGVDGLKTGYTDAAGYCLVASAKRGGRRLIAVVLGAPSEK 253

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645529 283 ERFTESRELIEYGFnnfekqklkvnknntisvvkgkedqvtvapekeitviakkgskepyKIGTELDKSLAEDGHLVAPI 362
Cdd:COG1686  254 ARFADAAKLLDYGF----------------------------------------------PKGEALKAEVVLDGPLKAPV 287

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 446645529 363 KKDAKVGSITLestdkygFLDGSKSMKVTAKTTEEVEKANWF 404
Cdd:COG1686  288 KKGQVVGTLVV-------TLDGKTIAEVPLVAAEDVEKAGFF 322
Peptidase_S11 pfam00768
D-alanyl-D-alanine carboxypeptidase;
43-276 1.67e-62

D-alanyl-D-alanine carboxypeptidase;


Pssm-ID: 425859 [Multi-domain]  Cd Length: 234  Bit Score: 201.46  E-value: 1.67e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645529   43 TGKILHEQNPDELLAIASMSKLIVVYAVLEAIKEGKITWDTKVNISDYAYEVSrNNEFSNVPFEKGRQYTVKELYHSIVI 122
Cdd:pfam00768  18 TGKVLYEKNPDQVRPIASITKLMTAYVVLEALKAGKIKEDDMVTISEDAWATG-NPGSSNIFLKPGSQVSVKDLLRGALV 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645529  123 FSANGSSIALAELLAGSEKNFLNLANEHAKKLGLKKYKFVNATGLNNADLKgkhpegtdpnaensMSARDMGMLSKTMIT 202
Cdd:pfam00768  97 SSGNDAAVALAEHIAGSEKAFVK*MNAKAKELGLKNTRFVNPTGLDAHGQY--------------SSARDMAILAKALIK 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446645529  203 KYPEMLEDTKQRFRNFPDnhpkpirMENWNWMLPGAAFAYEG--TDGLKTGSSDTAGYGFTITAKRGDVRLISVII 276
Cdd:pfam00768 163 DLPEELSITKEKSFTFRG-------INKINQRNRNGLLWDKTwnVDGLKTGYTNEAGYCLVASATKGGMRLISVVM 231
PRK10001 PRK10001
serine-type D-Ala-D-Ala carboxypeptidase;
43-423 3.15e-44

serine-type D-Ala-D-Ala carboxypeptidase;


Pssm-ID: 182189 [Multi-domain]  Cd Length: 400  Bit Score: 158.62  E-value: 3.15e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645529  43 TGKILHEQNPDELLAIASMSKLIVVYAVLEAIKEGKITWDTKVNISDYAYEVSRNN-EFSNVPFEK-GRQYTVKELYHSI 120
Cdd:PRK10001  49 SGKVLAEGNADEKLDPASLTKIMTSYVVGQALKADKIKLTDMVTVGKDAWATGNPAlRGSSVMFLKpGDQVSVADLNKGV 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645529 121 VIFSANGSSIALAELLAGSEKNFLNLANEHAKKLGLKKYKFVNATGLnnaDLKGKHPegtdpnaensmSARDMGMLSKTM 200
Cdd:PRK10001 129 IIQSGNDACIALADYVAGSQESFIGLMNGYAKKLGLTNTTFQTVHGL---DAPGQFS-----------TARDMALLGKAL 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645529 201 ITKYPEMLEDTKQRFRNFpdnhpKPIRMENWNWMLPGAAFayeGTDGLKTGSSDTAGYGFTITAKRGDVRLISVIIKTKS 280
Cdd:PRK10001 195 IHDVPEEYAIHKEKEFTF-----NKIRQPNRNRLLWSSNL---NVDGMKTGTTAGAGYNLVASATQGDMRLISVVLGAKT 266

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645529 281 MDERFTESRELIEYGFNNFEK-QKLKVNKN-NTISVVKGKEDQVTVAPEKEITVIAKKGSKEPYKIGTELDkslaeDGHL 358
Cdd:PRK10001 267 DRIRFNESEKLLTWGFRFFETvTPIKPDATfVTQRVWFGDKSEVNLGAGEAGSVTIPRGQLKNLKASYTLT-----EPQL 341

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446645529 359 VAPIKKDAKVGSITLESTDKygfldgsksmkvtaktteEVEKANWFVLTMRSIGDFFSNLWSKVF 423
Cdd:PRK10001 342 TAPLKKGQVVGTIDFQLNGK------------------SIEQRPLIVMENVEEGGFFSRMWDFVM 388
PBP5_C smart00936
Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. ...
 299-400 1.22e-10

Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. coli functions as a D-alanyl-D-alanine carboxypeptidase. It is composed of two domains that are oriented at approximately right angles to each other. The N-terminal domain (pfam00768) is the catalytic domain. The C-terminal domain featured in this family is organized into a sandwich of two anti-parallel beta-sheets, and has a relatively hydrophobic surface as compared to the N-terminal domain. Its precise function is unknown; it may mediate interactions with other cell wall-synthesising enzymes, thus allowing the protein to be recruited to areas of active cell wall synthesis. It may also function as a linker domain that positions the active site in the catalytic domain closer to the peptidoglycan layer, to allow it to interact with cell wall peptides.


Pssm-ID: 198004 [Multi-domain]  Cd Length: 92  Bit Score: 57.61  E-value: 1.22e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645529   299 FEKQKLkVNKN---NTISVVKGKEDQVTVAPEKEITVIAKKGSKEPYKIGTELDKSlaedgHLVAPIKKDAKVGSITLes 375
Cdd:smart00936   1 FETVKL-YKKGqvvGTVKVWKGKEKTVKLGAKEDVYVTLPKGEKKKLKAKVVLDKP-----ELEAPIKKGQVVGTLVV-- 72

                           90       100
                   ....*....|....*....|....*
gi 446645529   376 tdkygFLDGSKSMKVTAKTTEEVEK 400
Cdd:smart00936  73 -----TLDGKLIGEVPLVALEDVEK 92
 
Name Accession Description Interval E-value
strep_PBP3 NF038273
streptococcal D-alanyl-D-alanine carboxypeptidase PBP3; PBP3 (penicillin-binding protein 3) is ...
 43-403 1.39e-102

streptococcal D-alanyl-D-alanine carboxypeptidase PBP3; PBP3 (penicillin-binding protein 3) is the lone D-alanyl-D-alanine carboxypeptidase in Streptococcus pneumoniae. The gene is known as pbp3 or dacA.


Pssm-ID: 468443 [Multi-domain]  Cd Length: 407  Bit Score: 310.65  E-value: 1.39e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645529  43 TGKILHEQNPDELLAIASMSKLIVVYAVLEAIKEGKITWDTKVNISDYAYEVSRNNEFSNVPFEKgRQYTVKELYHSIVI 122
Cdd:NF038273  38 TGKILYEKDATTPVPIASLTKLLTAYLVYKEIKSGKLSWDTPVKISDYPYELTTNYEISNVPLDA-RKYTVKELLEASLV 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645529 123 FSANGSSIALAELLAGSEKNFLNLANEHAKKLGLKKYKFVNATGLNNADLKGKHPEGTDPNAENSMSARDMGMLSKTMIT 202
Cdd:NF038273 117 ASANSAAIALAEKIAGSEPKFVDKMKAQLKEWGITDAKLVNASGLNNSYLGDHIYPGSKKDDENKLSAKDVAIIARHLIK 196

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645529 203 KYPEMLEDTKQRFRNFPDNhpkpiRMENWNWMLPGAAFAYEGTDGLKTGSSDTAGYGFTITAKRGDVRLISVIIKTKSMD 282
Cdd:NF038273 197 DFPEVLKITSKTSADFAGT-----TIYSYNYMLKGMPYYREGVDGLKTGTTEKAGASFVATSVENGMRVITVVLNADNAD 271

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645529 283 E----RFTESRELIEYGFNNFEKQKL----KVNKNNTISVVKGKEDQVTVAPEKEITVIAKKGSKEPYKIGTELDKSlae 354
Cdd:NF038273 272 EdeyaRFTATNQLLDYIYQNFEKVTLvkkgQAYKDSKLPVIDGKKKTVSAVAKKDLTVIQKIGTDSKPSVKFTPKKK--- 348

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446645529 355 dgHLVAPIKKDAKVGSITLESTDKYG--FLDGSKSMKVTAKttEEVEKANW 403
Cdd:NF038273 349 --ELTAPIKKGQVVGKATFKDKDLIGkgYLGEPPSVELVAK--KDVKKSFF 395
DacC COG1686
D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis];
43-404 1.33e-91

D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441292 [Multi-domain]  Cd Length: 324  Bit Score: 279.41  E-value: 1.33e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645529  43 TGKILHEQNPDELLAIASMSKLIVVYAVLEAIKEGKITWDTKVNISDYAYEVsrnnEFSNVPFEKGRQYTVKELYHSIVI 122
Cdd:COG1686   38 TGQVLYEKNADERLPPASLTKLMTAYVVLEALKAGKISLDDKVTVSEEAART----GGSKMGLKPGEQVTVEDLLKGLLL 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645529 123 FSANGSSIALAELLAGSEKNFLNLANEHAKKLGLKKYKFVNATGLnnadlkgkhpegtdPNAENSMSARDMGMLSKTMIT 202
Cdd:COG1686  114 QSGNDAAVALAEHIAGSEEAFVALMNAKAKELGMTNTHFVNPTGL--------------PDPGHYSTARDLALLARAAIK 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645529 203 KYPEMLEDTKQRFRNFPDnhPKPIRMENWNWMLpgaaFAYEGTDGLKTGSSDTAGYGFTITAKRGDVRLISVIIKTKSMD 282
Cdd:COG1686  180 DYPEFYEIFSTKEFTFPN--GRGITLRNTNRLL----GRYPGVDGLKTGYTDAAGYCLVASAKRGGRRLIAVVLGAPSEK 253

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645529 283 ERFTESRELIEYGFnnfekqklkvnknntisvvkgkedqvtvapekeitviakkgskepyKIGTELDKSLAEDGHLVAPI 362
Cdd:COG1686  254 ARFADAAKLLDYGF----------------------------------------------PKGEALKAEVVLDGPLKAPV 287

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 446645529 363 KKDAKVGSITLestdkygFLDGSKSMKVTAKTTEEVEKANWF 404
Cdd:COG1686  288 KKGQVVGTLVV-------TLDGKTIAEVPLVAAEDVEKAGFF 322
Peptidase_S11 pfam00768
D-alanyl-D-alanine carboxypeptidase;
43-276 1.67e-62

D-alanyl-D-alanine carboxypeptidase;


Pssm-ID: 425859 [Multi-domain]  Cd Length: 234  Bit Score: 201.46  E-value: 1.67e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645529   43 TGKILHEQNPDELLAIASMSKLIVVYAVLEAIKEGKITWDTKVNISDYAYEVSrNNEFSNVPFEKGRQYTVKELYHSIVI 122
Cdd:pfam00768  18 TGKVLYEKNPDQVRPIASITKLMTAYVVLEALKAGKIKEDDMVTISEDAWATG-NPGSSNIFLKPGSQVSVKDLLRGALV 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645529  123 FSANGSSIALAELLAGSEKNFLNLANEHAKKLGLKKYKFVNATGLNNADLKgkhpegtdpnaensMSARDMGMLSKTMIT 202
Cdd:pfam00768  97 SSGNDAAVALAEHIAGSEKAFVK*MNAKAKELGLKNTRFVNPTGLDAHGQY--------------SSARDMAILAKALIK 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446645529  203 KYPEMLEDTKQRFRNFPDnhpkpirMENWNWMLPGAAFAYEG--TDGLKTGSSDTAGYGFTITAKRGDVRLISVII 276
Cdd:pfam00768 163 DLPEELSITKEKSFTFRG-------INKINQRNRNGLLWDKTwnVDGLKTGYTNEAGYCLVASATKGGMRLISVVM 231
PRK10001 PRK10001
serine-type D-Ala-D-Ala carboxypeptidase;
43-423 3.15e-44

serine-type D-Ala-D-Ala carboxypeptidase;


Pssm-ID: 182189 [Multi-domain]  Cd Length: 400  Bit Score: 158.62  E-value: 3.15e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645529  43 TGKILHEQNPDELLAIASMSKLIVVYAVLEAIKEGKITWDTKVNISDYAYEVSRNN-EFSNVPFEK-GRQYTVKELYHSI 120
Cdd:PRK10001  49 SGKVLAEGNADEKLDPASLTKIMTSYVVGQALKADKIKLTDMVTVGKDAWATGNPAlRGSSVMFLKpGDQVSVADLNKGV 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645529 121 VIFSANGSSIALAELLAGSEKNFLNLANEHAKKLGLKKYKFVNATGLnnaDLKGKHPegtdpnaensmSARDMGMLSKTM 200
Cdd:PRK10001 129 IIQSGNDACIALADYVAGSQESFIGLMNGYAKKLGLTNTTFQTVHGL---DAPGQFS-----------TARDMALLGKAL 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645529 201 ITKYPEMLEDTKQRFRNFpdnhpKPIRMENWNWMLPGAAFayeGTDGLKTGSSDTAGYGFTITAKRGDVRLISVIIKTKS 280
Cdd:PRK10001 195 IHDVPEEYAIHKEKEFTF-----NKIRQPNRNRLLWSSNL---NVDGMKTGTTAGAGYNLVASATQGDMRLISVVLGAKT 266

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645529 281 MDERFTESRELIEYGFNNFEK-QKLKVNKN-NTISVVKGKEDQVTVAPEKEITVIAKKGSKEPYKIGTELDkslaeDGHL 358
Cdd:PRK10001 267 DRIRFNESEKLLTWGFRFFETvTPIKPDATfVTQRVWFGDKSEVNLGAGEAGSVTIPRGQLKNLKASYTLT-----EPQL 341

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446645529 359 VAPIKKDAKVGSITLESTDKygfldgsksmkvtaktteEVEKANWFVLTMRSIGDFFSNLWSKVF 423
Cdd:PRK10001 342 TAPLKKGQVVGTIDFQLNGK------------------SIEQRPLIVMENVEEGGFFSRMWDFVM 388
PRK10793 PRK10793
D-alanyl-D-alanine carboxypeptidase fraction A; Provisional
 43-404 1.87e-36

D-alanyl-D-alanine carboxypeptidase fraction A; Provisional


Pssm-ID: 182736 [Multi-domain]  Cd Length: 403  Bit Score: 137.68  E-value: 1.87e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645529  43 TGKILHEQNPDELLAIASMSKLIVVYAVLEAIKEGKITWDTKVNISDYAYeVSRNNEF--SNVPFEK-GRQYTVKELYHS 119
Cdd:PRK10793  56 SGKVLAEQNADVRRDPASLTKMMTSYVIGQAMKAGKFKETDLVTVGNDAW-ATGNPVFkgSSLMFLKpGMQVPVSQLIRG 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645529 120 IVIFSANGSSIALAELLAGSEKNFLNLANEHAKKLGLKKYKFVNATGLnnaDLKGKHPegtdpnaensmSARDMGMLSKT 199
Cdd:PRK10793 135 INLQSGNDACVAMADYVAGSQDAFVGLMNSYVNALGLKNTHFQTVHGL---DADGQYS-----------SARDMALIGQA 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645529 200 MITKYPEmlEDTKQRFRNFPDNHpkpIRMENWNWMLPGAAFAyegTDGLKTGSSDTAGYGFTITAKRGDVRLISVIIKTK 279
Cdd:PRK10793 201 LIRDVPN--EYAIYKEKEFTFNG---IRQLNRNGLLWDNSLN---VDGIKTGHTDKAGYNLVASATEGQMRLISAVMGGR 272

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645529 280 SMDERFTESRELIEYGFNNFEK-QKLKVNKN-NTISVVKGKEDQVTVAPEKEITVIAKKGSKEPYKIGTELDKSlaedgH 357
Cdd:PRK10793 273 TFKGRETESKKLLTWGFRFFETvNPLKVGKEfASEPVWFGDSDRASLGVDKDVYLTIPRGRMKDLKASYVLNTS-----E 347

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 446645529 358 LVAPIKKDAKVGSITLEstdkygfLDGSKSMKVTAKTTEEVEKANWF 404
Cdd:PRK10793 348 LHAPLQKNQVVGTINFQ-------LDGKTIEQRPLVVLQEIPEGNFF 387
dacD PRK11397
serine-type D-Ala-D-Ala carboxypeptidase DacD;
43-378 1.25e-33

serine-type D-Ala-D-Ala carboxypeptidase DacD;


Pssm-ID: 183117 [Multi-domain]  Cd Length: 388  Bit Score: 129.55  E-value: 1.25e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645529  43 TGKILHEQNPDELLAIASMSKLIVVYAVLEAIKEGKITWDTKVNISDYAYeVSRNNEF--SNVPFEK-GRQYTVKELYHS 119
Cdd:PRK11397  46 TGQILTAGNEHQQRNPASLTKLMTGYVVDRAIDSHRITPDDIVTVGRDAW-AKDNPVFvgSSLMFLKeGDRVSVRDLSRG 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645529 120 IVIFSANGSSIALAELLAGSEKNFLNLANEHAKKLGLKKYKFVNATGLnnaDLKGKHPegtdpnaensmSARDMGMLSKT 199
Cdd:PRK11397 125 LIVDSGNDACVALADYIAGGQRQFVEMMNNYVEKLHLKDTHFETVHGL---DAPGQHS-----------SAYDLAVLSRA 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645529 200 MITKYPEMLEDTKQRFRNFpdnhpKPIRMENWNWMLpgaafaYEGT---DGLKTGSSDTAGYGFTITAKRGDVRLISVII 276
Cdd:PRK11397 191 IIHGEPEFYHMYSEKSLTW-----NGITQQNRNGLL------WDKTmnvDGLKTGHTSGAGFNLIASAVDGQRRLIAVVM 259

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645529 277 KTKSMDERFTESRELIEYGFNNFEKQKL--KVNKNNTISVVKGKEDQVTVAPEKEITVIAKKGSKEPYKIGTELDKSlae 354
Cdd:PRK11397 260 GADSAKGREEQARKLLRWGQQNFTTVQIlhRGKKVGTERIWYGDKENIALGTEQDFWMVLPKAEIPHIKAKYVLDGK--- 336

                        330       340
                 ....*....|....*....|....
gi 446645529 355 dgHLVAPIKKDAKVGSITLESTDK 378
Cdd:PRK11397 337 --ELEAPISAHQRVGEIELYDRDK 358
PBP5_C pfam07943
Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. ...
 299-400 1.89e-11

Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. coli functions as a D-alanyl-D-alanine carboxypeptidase. It is composed of two domains that are oriented at approximately right angles to each other. The N-terminal domain (pfam00768) is the catalytic domain. The C-terminal domain featured in this family is organized into a sandwich of two anti-parallel beta-sheets, and has a relatively hydrophobic surface as compared to the N-terminal domain. Its precise function is unknown; it may mediate interactions with other cell wall-synthesising enzymes, thus allowing the protein to be recruited to areas of active cell wall synthesis. It may also function as a linker domain that positions the active site in the catalytic domain closer to the peptidoglycan layer, to allow it to interact with cell wall peptides.


Pssm-ID: 429749 [Multi-domain]  Cd Length: 91  Bit Score: 59.92  E-value: 1.89e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645529  299 FEKQKL--KVNKNNTISVVKGKEDQVTVAPEKEITVIAKKGSKEPYKIGTELDKSlaedghLVAPIKKDAKVGSITLest 376
Cdd:pfam07943   1 FETKKLykKGDVVKKVKVWKGKKKTVPLGAKEDVYVTVPKGEKKKLKAKVTLKKP------LEAPIKKGQVVGKLEV--- 71

                          90       100
                  ....*....|....*....|....
gi 446645529  377 dkygFLDGSKSMKVTAKTTEEVEK 400
Cdd:pfam07943  72 ----YLDGKLIGEVPLVAKEDVEE 91
PBP5_C smart00936
Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. ...
 299-400 1.22e-10

Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. coli functions as a D-alanyl-D-alanine carboxypeptidase. It is composed of two domains that are oriented at approximately right angles to each other. The N-terminal domain (pfam00768) is the catalytic domain. The C-terminal domain featured in this family is organized into a sandwich of two anti-parallel beta-sheets, and has a relatively hydrophobic surface as compared to the N-terminal domain. Its precise function is unknown; it may mediate interactions with other cell wall-synthesising enzymes, thus allowing the protein to be recruited to areas of active cell wall synthesis. It may also function as a linker domain that positions the active site in the catalytic domain closer to the peptidoglycan layer, to allow it to interact with cell wall peptides.


Pssm-ID: 198004 [Multi-domain]  Cd Length: 92  Bit Score: 57.61  E-value: 1.22e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645529   299 FEKQKLkVNKN---NTISVVKGKEDQVTVAPEKEITVIAKKGSKEPYKIGTELDKSlaedgHLVAPIKKDAKVGSITLes 375
Cdd:smart00936   1 FETVKL-YKKGqvvGTVKVWKGKEKTVKLGAKEDVYVTLPKGEKKKLKAKVVLDKP-----ELEAPIKKGQVVGTLVV-- 72

                           90       100
                   ....*....|....*....|....*
gi 446645529   376 tdkygFLDGSKSMKVTAKTTEEVEK 400
Cdd:smart00936  73 -----TLDGKLIGEVPLVALEDVEK 92
pbpG PRK11669
D-alanyl-D-alanine endopeptidase; Provisional
 43-258 4.75e-10

D-alanyl-D-alanine endopeptidase; Provisional


Pssm-ID: 236952  Cd Length: 306  Bit Score: 60.46  E-value: 4.75e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645529  43 TGKILHEQNPDELLAIASMSKLIVVYAVLEAikegKITWDTK--VNISDyAYEVsrNNEFSNVPFekGRQYTVKELYHSI 120
Cdd:PRK11669  51 TNKVIYSSNPDLVVPIASITKLMTAMVVLDA----KLPLDEKlkVDISQ-TPEM--KGVYSRVRL--NSEISRKDMLLLA 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645529 121 VIFSANGSSIALAELLAGSEKNFLNLANEHAKKLGLKKYKFVNATGLnnadlkgkhpegtdpNAENSMSARDmgmLSKTM 200
Cdd:PRK11669 122 LMSSENRAAASLAHHYPGGYKAFIKAMNAKAKALGMTNTRYVEPTGL---------------SIHNVSTARD---LTKLL 183

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446645529 201 IT--KYPEM--LEDTKQR------------FRNfpDNHpkPIRMENWNWMLPgaafayegtdglKTGSSDTAGY 258
Cdd:PRK11669 184 IAskQYPLIgqLSTTREKtatfrkpnytlpFRN--TNH--LVYRDNWNIQLT------------KTGFTNAAGH 241
PenP COG2367
Beta-lactamase class A [Defense mechanisms];
43-196 1.73e-09

Beta-lactamase class A [Defense mechanisms];


Pssm-ID: 441934 [Multi-domain]  Cd Length: 276  Bit Score: 58.37  E-value: 1.73e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645529  43 TGKILhEQNPDELLAIASMSKLIVVYAVLEAIKEGKITWDTKVNISDYAYEvsrnnEFSNV--PFEKGRQYTVKELYHSI 120
Cdd:COG2367   44 TGETV-GINADERFPAASTFKLPVLAAVLRQVDAGKLSLDERVTLTPEDLV-----GGSGIlqKLPDGTGLTLRELAELM 117

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446645529 121 VIFSANGSSIALAELLaGSEKnflnlANEHAKKLGLKKYKFVNATGLNNADLKGKhpegtdpnaENSMSARDMGML 196
Cdd:COG2367  118 ITVSDNTATNLLLRLL-GPDA-----VNAFLRSLGLTDTRLDRKEPDLNELPGDG---------RNTTTPRDMARL 178
Beta-lactamase2 pfam13354
Beta-lactamase enzyme family; This is the catalytic domain of class A beta-lactamases. It is ...
 51-196 1.30e-07

Beta-lactamase enzyme family; This is the catalytic domain of class A beta-lactamases. It is closely related to Beta-lactamase, pfam00144, the serine beta-lactamase-like superfamily, which contains the distantly related pfam00905 and PF00768 D-alanyl-D-alanine carboxypeptidase.


Pssm-ID: 463854 [Multi-domain]  Cd Length: 215  Bit Score: 51.89  E-value: 1.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645529   51 NPDELLAIASMSKLIVVYAVLEAIKEGKITWDTKVNISDyayEVSRNNEFSNVPFEKGRQYTVKELYHSIVIFSANGSSI 130
Cdd:pfam13354  16 NGDRSFPAASTIKVPILLAVLEQVDEGKLSLDERLTVTA---EDKVGGSGILQYLPDGSQLSLRDLLTLMIAVSDNTATN 92

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446645529  131 ALAELLAGSEknflnlANEHAKKLGLKkykfvnATGLNNADLKgkhPEGTDPNAENSMSARDMGML 196
Cdd:pfam13354  93 LLIDRLGLEA------VNARLRALGLR------DTRLRRKLPD---LRAADKGGTNTTTARDMAKL 143
AmpC COG1680
CubicO group peptidase, beta-lactamase class C family [Defense mechanisms];
44-90 2.81e-04

CubicO group peptidase, beta-lactamase class C family [Defense mechanisms];


Pssm-ID: 441286 [Multi-domain]  Cd Length: 355  Bit Score: 42.75  E-value: 2.81e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446645529  44 GKILHEQ-------------NPDELLAIASMSKLIVVYAVLEAIKEGKITWDTKVniSDY 90
Cdd:COG1680   43 GKVVYEKaygvadletgrpvTPDTLFRIASVTKSFTATAVLQLVEEGKLDLDDPV--SKY 100
Beta-lactamase pfam00144
Beta-lactamase; This family appears to be distantly related to pfam00905 and PF00768 ...
 51-97 5.58e-03

Beta-lactamase; This family appears to be distantly related to pfam00905 and PF00768 D-alanyl-D-alanine carboxypeptidase.


Pssm-ID: 395092 [Multi-domain]  Cd Length: 327  Bit Score: 38.64  E-value: 5.58e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 446645529   51 NPDELLAIASMSKLIVVYAVLEAIKEGKITWDTKVniSDYAYEVSRN 97
Cdd:pfam00144  45 TADTLFRIASVTKTFTAAAVLQLVERGKLDLDDPV--SKYLPEFAGP 89
 
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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