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Conserved domains on  [gi|446670944|ref|WP_000748290|]
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serine hydrolase [Vibrio cholerae]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10793 super family cl32580
D-alanyl-D-alanine carboxypeptidase fraction A; Provisional
 10-391 1.06e-180

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


The actual alignment was detected with superfamily member PRK10793:

Pssm-ID: 182736 [Multi-domain]  Cd Length: 403  Bit Score: 507.85  E-value: 1.06e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446670944  10 LASSITLSITLSSTAFASPI----VTPDAPQIAAKGYVLMDYHSGKVLAEKEMDTKLSPASLTKMMTSYVIGQEVKRGNI 85
Cdd:PRK10793  13 LALTTALCTAFISAAHADDLniktMIPGVPQIDAESYILIDYNSGKVLAEQNADVRRDPASLTKMMTSYVIGQAMKAGKF 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446670944  86 SLNDDVVISKNAWAKNFPD---SSKMFVEVGTTVKVSDLNRGIIIQSGNDACVAMAEHVAGTEDAFVDLMNAWASSLGMK 162
Cdd:PRK10793  93 KETDLVTVGNDAWATGNPVfkgSSLMFLKPGMQVPVSQLIRGINLQSGNDACVAMADYVAGSQDAFVGLMNSYVNALGLK 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446670944 163 NSHFTNSHGLDDPNLYSTPYDLALLGQALIRDVPEEYAIYSEQKFTYNGITQYNRNGLLWDKSMNVDGIKTGHTSGAGYN 242
Cdd:PRK10793 173 NTHFQTVHGLDADGQYSSARDMALIGQALIRDVPNEYAIYKEKEFTFNGIRQLNRNGLLWDNSLNVDGIKTGHTDKAGYN 252

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446670944 243 LVSSATEGNMRLVAVVMGTDNENARKAESKKLLSYGFRFFETVAPHKAGETFVNETIWMGDKDTIALGVDKDTYVTLPRG 322
Cdd:PRK10793 253 LVASATEGQMRLISAVMGGRTFKGRETESKKLLTWGFRFFETVNPLKVGKEFASEPVWFGDSDRASLGVDKDVYLTIPRG 332

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446670944 323 QAKDLTASFVLEK-QLKAPLKKGDIVGTLYYQLAGNDIAQYPLLALEDVQEGSLFSRLWDYLVLLFKSWF 391
Cdd:PRK10793 333 RMKDLKASYVLNTsELHAPLQKNQVVGTINFQLDGKTIEQRPLVVLQEIPEGNFFGKIIDYIKLMFHHWF 402
 
Name Accession Description Interval E-value
PRK10793 PRK10793
D-alanyl-D-alanine carboxypeptidase fraction A; Provisional
 10-391 1.06e-180

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


Pssm-ID: 182736 [Multi-domain]  Cd Length: 403  Bit Score: 507.85  E-value: 1.06e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446670944  10 LASSITLSITLSSTAFASPI----VTPDAPQIAAKGYVLMDYHSGKVLAEKEMDTKLSPASLTKMMTSYVIGQEVKRGNI 85
Cdd:PRK10793  13 LALTTALCTAFISAAHADDLniktMIPGVPQIDAESYILIDYNSGKVLAEQNADVRRDPASLTKMMTSYVIGQAMKAGKF 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446670944  86 SLNDDVVISKNAWAKNFPD---SSKMFVEVGTTVKVSDLNRGIIIQSGNDACVAMAEHVAGTEDAFVDLMNAWASSLGMK 162
Cdd:PRK10793  93 KETDLVTVGNDAWATGNPVfkgSSLMFLKPGMQVPVSQLIRGINLQSGNDACVAMADYVAGSQDAFVGLMNSYVNALGLK 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446670944 163 NSHFTNSHGLDDPNLYSTPYDLALLGQALIRDVPEEYAIYSEQKFTYNGITQYNRNGLLWDKSMNVDGIKTGHTSGAGYN 242
Cdd:PRK10793 173 NTHFQTVHGLDADGQYSSARDMALIGQALIRDVPNEYAIYKEKEFTFNGIRQLNRNGLLWDNSLNVDGIKTGHTDKAGYN 252

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446670944 243 LVSSATEGNMRLVAVVMGTDNENARKAESKKLLSYGFRFFETVAPHKAGETFVNETIWMGDKDTIALGVDKDTYVTLPRG 322
Cdd:PRK10793 253 LVASATEGQMRLISAVMGGRTFKGRETESKKLLTWGFRFFETVNPLKVGKEFASEPVWFGDSDRASLGVDKDVYLTIPRG 332

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446670944 323 QAKDLTASFVLEK-QLKAPLKKGDIVGTLYYQLAGNDIAQYPLLALEDVQEGSLFSRLWDYLVLLFKSWF 391
Cdd:PRK10793 333 RMKDLKASYVLNTsELHAPLQKNQVVGTINFQLDGKTIEQRPLVVLQEIPEGNFFGKIIDYIKLMFHHWF 402
DacC COG1686
D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis];
16-378 3.97e-146

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


Pssm-ID: 441292 [Multi-domain]  Cd Length: 324  Bit Score: 416.93  E-value: 3.97e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446670944  16 LSITLSSTAFASPIVTPDAPQIAAKGYVLMDYHSGKVLAEKEMDTKLSPASLTKMMTSYVIGQEVKRGNISLNDDVVISK 95
Cdd:COG1686    5 LLLALLLLLAAAAAAPAAPPDIAAKSAILIDADTGQVLYEKNADERLPPASLTKLMTAYVVLEALKAGKISLDDKVTVSE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446670944  96 NAWAKnfpDSSKMFVEVGTTVKVSDLNRGIIIQSGNDACVAMAEHVAGTEDAFVDLMNAWASSLGMKNSHFTNSHGLDDP 175
Cdd:COG1686   85 EAART---GGSKMGLKPGEQVTVEDLLKGLLLQSGNDAAVALAEHIAGSEEAFVALMNAKAKELGMTNTHFVNPTGLPDP 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446670944 176 NLYSTPYDLALLGQALIRDVPEEYAIYSEQKFTYN---GITQYNRNGLLWdKSMNVDGIKTGHTSGAGYNLVSSATEGNM 252
Cdd:COG1686  162 GHYSTARDLALLARAAIKDYPEFYEIFSTKEFTFPngrGITLRNTNRLLG-RYPGVDGLKTGYTDAAGYCLVASAKRGGR 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446670944 253 RLVAVVMGTDNENARKAESKKLLSYGFrffetvaphkagetfvnetiwmgdkdtialgvdkdtyvtlPRGQAkdLTASFV 332
Cdd:COG1686  241 RLIAVVLGAPSEKARFADAAKLLDYGF----------------------------------------PKGEA--LKAEVV 278

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 446670944 333 LEKQLKAPLKKGDIVGTLYYQLAGNDIAQYPLLALEDVQEGSLFSR 378
Cdd:COG1686  279 LDGPLKAPVKKGQVVGTLVVTLDGKTIAEVPLVAAEDVEKAGFFSR 324
Peptidase_S11 pfam00768
D-alanyl-D-alanine carboxypeptidase;
32-262 2.83e-111

D-alanyl-D-alanine carboxypeptidase;


Pssm-ID: 425859 [Multi-domain]  Cd Length: 234  Bit Score: 325.11  E-value: 2.83e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446670944   32 PDAPQIAAKGYVLMDYHSGKVLAEKEMDTKLSPASLTKMMTSYVIGQEVKRGNISLNDDVVISKNAWAKNFPDSSKMFVE 111
Cdd:pfam00768   1 VSAPEIAAKSAILVDYNTGKVLYEKNPDQVRPIASITKLMTAYVVLEALKAGKIKEDDMVTISEDAWATGNPGSSNIFLK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446670944  112 VGTTVKVSDLNRGIIIQSGNDACVAMAEHVAGTEDAFVDLMNAWASSLGMKNSHFTNSHGLDDPNLYSTPYDLALLGQAL 191
Cdd:pfam00768  81 PGSQVSVKDLLRGALVSSGNDAAVALAEHIAGSEKAFVK*MNAKAKELGLKNTRFVNPTGLDAHGQYSSARDMAILAKAL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446670944  192 IRDVPEEYAIYSEQKFTY---NGITQYNRNGLLWDKSMNVDGIKTGHTSGAGYNLVSSATEGNMRLVAVVMGTD 262
Cdd:pfam00768 161 IKDLPEELSITKEKSFTFrgiNKINQRNRNGLLWDKTWNVDGLKTGYTNEAGYCLVASATKGGMRLISVVMGAF 234
PBP4_Staph NF038258
penicillin-binding protein PBP4; Members of this family penicillin-binding protein 4 (PBP4), ...
 37-272 1.60e-39

penicillin-binding protein PBP4; Members of this family penicillin-binding protein 4 (PBP4), as the name is used in Staphylococcus aureus and related species from the same genus. PBP4 is not essential. It has transpeptidase activity, provides low level beta-lactam resistance, and in mutant strains can contribute to high level beta-lactam resistance.


Pssm-ID: 468436 [Multi-domain]  Cd Length: 365  Bit Score: 144.35  E-value: 1.60e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446670944  37 IAAKGYVLMDYHsgkvlaekeMDTKLSPASLTKMMTSYVIGQEVKRGNISLNDDVVISkNAWAK--NFPDSSKMFVEVGT 114
Cdd:NF038258  46 TTQTGQILYDYH---------GNKKWDPASMTKLMTMYLTLEAIKKGKLSLNDKVKIT-SDYEKmsTLPNLSTFPLKPGQ 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446670944 115 TVKVSDLNRGIIIQSGNDACVAMAEHVAGTEDAFVDLMNAWASSLGMKNSHFTNSHGL--------------DDPNLYST 180
Cdd:NF038258 116 TYTIKELLKQTALASSNAAALILAEKVSGNTSKFTDRMNEKAKALGMKHTHFTNPSGAdnnllkpyapkkykDETKSKST 195

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446670944 181 PYDLALLGQALIRDVPEEYAIYSEQKFTYNGITQYNRNGLLWDKSM---NVDGIKTGhTSGAGYNLVSSATEGNMRLVAV 257
Cdd:NF038258 196 AKDMAILSQHLIKKHPKILKYTKLTADTQHGVTLYTTNLSLPGQPMslkGTDGLKTG-TSDEGYNLALTTKRDGLRINQV 274

                        250
                 ....*....|....*...
gi 446670944 258 VMGT---DNENARKAESK 272
Cdd:NF038258 275 IMNVgpyPSEGAKHARNK 292
PBP5_C smart00936
Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. ...
 282-372 1.08e-30

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: 112.69  E-value: 1.08e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446670944   282 FETVAPHKAGETFVNETIWMGDKDTIALGVDKDTYVTLPRGQAKDLTASFVL-EKQLKAPLKKGDIVGTLYYQLAGNDIA 360
Cdd:smart00936   1 FETVKLYKKGQVVGTVKVWKGKEKTVKLGAKEDVYVTLPKGEKKKLKAKVVLdKPELEAPIKKGQVVGTLVVTLDGKLIG 80

                           90
                   ....*....|..
gi 446670944   361 QYPLLALEDVQE 372
Cdd:smart00936  81 EVPLVALEDVEK 92
 
Name Accession Description Interval E-value
PRK10793 PRK10793
D-alanyl-D-alanine carboxypeptidase fraction A; Provisional
 10-391 1.06e-180

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


Pssm-ID: 182736 [Multi-domain]  Cd Length: 403  Bit Score: 507.85  E-value: 1.06e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446670944  10 LASSITLSITLSSTAFASPI----VTPDAPQIAAKGYVLMDYHSGKVLAEKEMDTKLSPASLTKMMTSYVIGQEVKRGNI 85
Cdd:PRK10793  13 LALTTALCTAFISAAHADDLniktMIPGVPQIDAESYILIDYNSGKVLAEQNADVRRDPASLTKMMTSYVIGQAMKAGKF 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446670944  86 SLNDDVVISKNAWAKNFPD---SSKMFVEVGTTVKVSDLNRGIIIQSGNDACVAMAEHVAGTEDAFVDLMNAWASSLGMK 162
Cdd:PRK10793  93 KETDLVTVGNDAWATGNPVfkgSSLMFLKPGMQVPVSQLIRGINLQSGNDACVAMADYVAGSQDAFVGLMNSYVNALGLK 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446670944 163 NSHFTNSHGLDDPNLYSTPYDLALLGQALIRDVPEEYAIYSEQKFTYNGITQYNRNGLLWDKSMNVDGIKTGHTSGAGYN 242
Cdd:PRK10793 173 NTHFQTVHGLDADGQYSSARDMALIGQALIRDVPNEYAIYKEKEFTFNGIRQLNRNGLLWDNSLNVDGIKTGHTDKAGYN 252

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446670944 243 LVSSATEGNMRLVAVVMGTDNENARKAESKKLLSYGFRFFETVAPHKAGETFVNETIWMGDKDTIALGVDKDTYVTLPRG 322
Cdd:PRK10793 253 LVASATEGQMRLISAVMGGRTFKGRETESKKLLTWGFRFFETVNPLKVGKEFASEPVWFGDSDRASLGVDKDVYLTIPRG 332

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446670944 323 QAKDLTASFVLEK-QLKAPLKKGDIVGTLYYQLAGNDIAQYPLLALEDVQEGSLFSRLWDYLVLLFKSWF 391
Cdd:PRK10793 333 RMKDLKASYVLNTsELHAPLQKNQVVGTINFQLDGKTIEQRPLVVLQEIPEGNFFGKIIDYIKLMFHHWF 402
PRK10001 PRK10001
serine-type D-Ala-D-Ala carboxypeptidase;
4-391 2.52e-168

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


Pssm-ID: 182189 [Multi-domain]  Cd Length: 400  Bit Score: 476.41  E-value: 2.52e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446670944   4 SILKSVLASSITLSITLSSTAFASPivTPDAPQIAAKGYVLMDYHSGKVLAEKEMDTKLSPASLTKMMTSYVIGQEVKRG 83
Cdd:PRK10001   6 SLLRGLAAGSAFLFLFAPTAFAAEQ--TVEAPSVDARAWILMDYASGKVLAEGNADEKLDPASLTKIMTSYVVGQALKAD 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446670944  84 NISLNDDVVISKNAWAKNFP---DSSKMFVEVGTTVKVSDLNRGIIIQSGNDACVAMAEHVAGTEDAFVDLMNAWASSLG 160
Cdd:PRK10001  84 KIKLTDMVTVGKDAWATGNPalrGSSVMFLKPGDQVSVADLNKGVIIQSGNDACIALADYVAGSQESFIGLMNGYAKKLG 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446670944 161 MKNSHFTNSHGLDDPNLYSTPYDLALLGQALIRDVPEEYAIYSEQKFTYNGITQYNRNGLLWDKSMNVDGIKTGHTSGAG 240
Cdd:PRK10001 164 LTNTTFQTVHGLDAPGQFSTARDMALLGKALIHDVPEEYAIHKEKEFTFNKIRQPNRNRLLWSSNLNVDGMKTGTTAGAG 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446670944 241 YNLVSSATEGNMRLVAVVMGTDNENARKAESKKLLSYGFRFFETVAPHKAGETFVNETIWMGDKDTIALGVDKDTYVTLP 320
Cdd:PRK10001 244 YNLVASATQGDMRLISVVLGAKTDRIRFNESEKLLTWGFRFFETVTPIKPDATFVTQRVWFGDKSEVNLGAGEAGSVTIP 323

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446670944 321 RGQAKDLTASFVL-EKQLKAPLKKGDIVGTLYYQLAGNDIAQYPLLALEDVQEGSLFSRLWDYLVLLFKSWF 391
Cdd:PRK10001 324 RGQLKNLKASYTLtEPQLTAPLKKGQVVGTIDFQLNGKSIEQRPLIVMENVEEGGFFSRMWDFVMMKFHQWF 395
DacC COG1686
D-alanyl-D-alanine carboxypeptidase [Cell wall/membrane/envelope biogenesis];
16-378 3.97e-146

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


Pssm-ID: 441292 [Multi-domain]  Cd Length: 324  Bit Score: 416.93  E-value: 3.97e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446670944  16 LSITLSSTAFASPIVTPDAPQIAAKGYVLMDYHSGKVLAEKEMDTKLSPASLTKMMTSYVIGQEVKRGNISLNDDVVISK 95
Cdd:COG1686    5 LLLALLLLLAAAAAAPAAPPDIAAKSAILIDADTGQVLYEKNADERLPPASLTKLMTAYVVLEALKAGKISLDDKVTVSE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446670944  96 NAWAKnfpDSSKMFVEVGTTVKVSDLNRGIIIQSGNDACVAMAEHVAGTEDAFVDLMNAWASSLGMKNSHFTNSHGLDDP 175
Cdd:COG1686   85 EAART---GGSKMGLKPGEQVTVEDLLKGLLLQSGNDAAVALAEHIAGSEEAFVALMNAKAKELGMTNTHFVNPTGLPDP 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446670944 176 NLYSTPYDLALLGQALIRDVPEEYAIYSEQKFTYN---GITQYNRNGLLWdKSMNVDGIKTGHTSGAGYNLVSSATEGNM 252
Cdd:COG1686  162 GHYSTARDLALLARAAIKDYPEFYEIFSTKEFTFPngrGITLRNTNRLLG-RYPGVDGLKTGYTDAAGYCLVASAKRGGR 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446670944 253 RLVAVVMGTDNENARKAESKKLLSYGFrffetvaphkagetfvnetiwmgdkdtialgvdkdtyvtlPRGQAkdLTASFV 332
Cdd:COG1686  241 RLIAVVLGAPSEKARFADAAKLLDYGF----------------------------------------PKGEA--LKAEVV 278

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 446670944 333 LEKQLKAPLKKGDIVGTLYYQLAGNDIAQYPLLALEDVQEGSLFSR 378
Cdd:COG1686  279 LDGPLKAPVKKGQVVGTLVVTLDGKTIAEVPLVAAEDVEKAGFFSR 324
dacD PRK11397
serine-type D-Ala-D-Ala carboxypeptidase DacD;
6-383 4.44e-144

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


Pssm-ID: 183117 [Multi-domain]  Cd Length: 388  Bit Score: 414.60  E-value: 4.44e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446670944   6 LKSVLASSITLSITLSSTAFASPIV--TPDAPQIAAKGYVLMDYHSGKVLAEKEMDTKLSPASLTKMMTSYVIGQEVKRG 83
Cdd:PRK11397   1 LKRRLIIAASLFAFNLSSAFAAENIpfSPQPPAIDAGSWVLMDYTTGQILTAGNEHQQRNPASLTKLMTGYVVDRAIDSH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446670944  84 NISLNDDVVISKNAWAKN---FPDSSKMFVEVGTTVKVSDLNRGIIIQSGNDACVAMAEHVAGTEDAFVDLMNAWASSLG 160
Cdd:PRK11397  81 RITPDDIVTVGRDAWAKDnpvFVGSSLMFLKEGDRVSVRDLSRGLIVDSGNDACVALADYIAGGQRQFVEMMNNYVEKLH 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446670944 161 MKNSHFTNSHGLDDPNLYSTPYDLALLGQALIRDVPEEYAIYSEQKFTYNGITQYNRNGLLWDKSMNVDGIKTGHTSGAG 240
Cdd:PRK11397 161 LKDTHFETVHGLDAPGQHSSAYDLAVLSRAIIHGEPEFYHMYSEKSLTWNGITQQNRNGLLWDKTMNVDGLKTGHTSGAG 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446670944 241 YNLVSSATEGNMRLVAVVMGTDNENARKAESKKLLSYGFRFFETVAPHKAGETFVNETIWMGDKDTIALGVDKDTYVTLP 320
Cdd:PRK11397 241 FNLIASAVDGQRRLIAVVMGADSAKGREEQARKLLRWGQQNFTTVQILHRGKKVGTERIWYGDKENIALGTEQDFWMVLP 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446670944 321 RGQAKDLTASFVLE-KQLKAPLKKGDIVGTLyyQLAGND--IAQYPLLALEDVQEGSLFSRLWDYL 383
Cdd:PRK11397 321 KAEIPHIKAKYVLDgKELEAPISAHQRVGEI--ELYDRDkqVAHWPLVTLESVGEGGMFSRLSDYF 384
Peptidase_S11 pfam00768
D-alanyl-D-alanine carboxypeptidase;
32-262 2.83e-111

D-alanyl-D-alanine carboxypeptidase;


Pssm-ID: 425859 [Multi-domain]  Cd Length: 234  Bit Score: 325.11  E-value: 2.83e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446670944   32 PDAPQIAAKGYVLMDYHSGKVLAEKEMDTKLSPASLTKMMTSYVIGQEVKRGNISLNDDVVISKNAWAKNFPDSSKMFVE 111
Cdd:pfam00768   1 VSAPEIAAKSAILVDYNTGKVLYEKNPDQVRPIASITKLMTAYVVLEALKAGKIKEDDMVTISEDAWATGNPGSSNIFLK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446670944  112 VGTTVKVSDLNRGIIIQSGNDACVAMAEHVAGTEDAFVDLMNAWASSLGMKNSHFTNSHGLDDPNLYSTPYDLALLGQAL 191
Cdd:pfam00768  81 PGSQVSVKDLLRGALVSSGNDAAVALAEHIAGSEKAFVK*MNAKAKELGLKNTRFVNPTGLDAHGQYSSARDMAILAKAL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446670944  192 IRDVPEEYAIYSEQKFTY---NGITQYNRNGLLWDKSMNVDGIKTGHTSGAGYNLVSSATEGNMRLVAVVMGTD 262
Cdd:pfam00768 161 IKDLPEELSITKEKSFTFrgiNKINQRNRNGLLWDKTWNVDGLKTGYTNEAGYCLVASATKGGMRLISVVMGAF 234
PBP4_Staph NF038258
penicillin-binding protein PBP4; Members of this family penicillin-binding protein 4 (PBP4), ...
 37-272 1.60e-39

penicillin-binding protein PBP4; Members of this family penicillin-binding protein 4 (PBP4), as the name is used in Staphylococcus aureus and related species from the same genus. PBP4 is not essential. It has transpeptidase activity, provides low level beta-lactam resistance, and in mutant strains can contribute to high level beta-lactam resistance.


Pssm-ID: 468436 [Multi-domain]  Cd Length: 365  Bit Score: 144.35  E-value: 1.60e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446670944  37 IAAKGYVLMDYHsgkvlaekeMDTKLSPASLTKMMTSYVIGQEVKRGNISLNDDVVISkNAWAK--NFPDSSKMFVEVGT 114
Cdd:NF038258  46 TTQTGQILYDYH---------GNKKWDPASMTKLMTMYLTLEAIKKGKLSLNDKVKIT-SDYEKmsTLPNLSTFPLKPGQ 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446670944 115 TVKVSDLNRGIIIQSGNDACVAMAEHVAGTEDAFVDLMNAWASSLGMKNSHFTNSHGL--------------DDPNLYST 180
Cdd:NF038258 116 TYTIKELLKQTALASSNAAALILAEKVSGNTSKFTDRMNEKAKALGMKHTHFTNPSGAdnnllkpyapkkykDETKSKST 195

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446670944 181 PYDLALLGQALIRDVPEEYAIYSEQKFTYNGITQYNRNGLLWDKSM---NVDGIKTGhTSGAGYNLVSSATEGNMRLVAV 257
Cdd:NF038258 196 AKDMAILSQHLIKKHPKILKYTKLTADTQHGVTLYTTNLSLPGQPMslkGTDGLKTG-TSDEGYNLALTTKRDGLRINQV 274

                        250
                 ....*....|....*...
gi 446670944 258 VMGT---DNENARKAESK 272
Cdd:NF038258 275 IMNVgpyPSEGAKHARNK 292
PBP5_C pfam07943
Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. ...
 282-372 5.61e-32

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: 116.15  E-value: 5.61e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446670944  282 FETVAPHKAGETFVNETIWMGDKDTIALGVDKDTYVTLPRGQAKDLTASFVLEKQLKAPLKKGDIVGTLYYQLAGNDIAQ 361
Cdd:pfam07943   1 FETKKLYKKGDVVKKVKVWKGKKKTVPLGAKEDVYVTVPKGEKKKLKAKVTLKKPLEAPIKKGQVVGKLEVYLDGKLIGE 80

                          90
                  ....*....|.
gi 446670944  362 YPLLALEDVQE 372
Cdd:pfam07943  81 VPLVAKEDVEE 91
PBP5_C smart00936
Penicillin-binding protein 5, C-terminal domain; Penicillin-binding protein 5 expressed by E. ...
 282-372 1.08e-30

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: 112.69  E-value: 1.08e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446670944   282 FETVAPHKAGETFVNETIWMGDKDTIALGVDKDTYVTLPRGQAKDLTASFVL-EKQLKAPLKKGDIVGTLYYQLAGNDIA 360
Cdd:smart00936   1 FETVKLYKKGQVVGTVKVWKGKEKTVKLGAKEDVYVTLPKGEKKKLKAKVVLdKPELEAPIKKGQVVGTLVVTLDGKLIG 80

                           90
                   ....*....|..
gi 446670944   361 QYPLLALEDVQE 372
Cdd:smart00936  81 EVPLVALEDVEK 92
pbpG PRK11669
D-alanyl-D-alanine endopeptidase; Provisional
 4-258 8.69e-19

D-alanyl-D-alanine endopeptidase; Provisional


Pssm-ID: 236952  Cd Length: 306  Bit Score: 85.89  E-value: 8.69e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446670944   4 SILKSVLASSITLSITLSSTAFASPIVTPDAPQIAAKGYVLMDYHSGKVLAEKEMDTKLSPASLTKMMTSYVigqeVKRG 83
Cdd:PRK11669   6 SLLSLLLLLAGVPFAPQAVAKTAAATTASQPQEIASGSAMVVDLNTNKVIYSSNPDLVVPIASITKLMTAMV----VLDA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446670944  84 NISLND--DVVISKNAWAKNfpdsskmfveVGTTVKV-SDLNRG-----IIIQSGNDACVAMAEHVAGTEDAFVDLMNAW 155
Cdd:PRK11669  82 KLPLDEklKVDISQTPEMKG----------VYSRVRLnSEISRKdmlllALMSSENRAAASLAHHYPGGYKAFIKAMNAK 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446670944 156 ASSLGMKNSHFTNSHGLDDPNLySTPYDLA----------LLGQalIRDVPEEYAIYSEQKFTyngITQYNRNGLLWDKS 225
Cdd:PRK11669 152 AKALGMTNTRYVEPTGLSIHNV-STARDLTklliaskqypLIGQ--LSTTREKTATFRKPNYT---LPFRNTNHLVYRDN 225

                        250       260       270
                 ....*....|....*....|....*....|...
gi 446670944 226 MNVDGIKTGHTSGAGYNLVSSaTEGNMRLVAVV 258
Cdd:PRK11669 226 WNIQLTKTGFTNAAGHCLVMR-TVINNRPVALV 257
PenP COG2367
Beta-lactamase class A [Defense mechanisms];
41-194 1.12e-06

Beta-lactamase class A [Defense mechanisms];


Pssm-ID: 441934 [Multi-domain]  Cd Length: 276  Bit Score: 49.51  E-value: 1.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446670944  41 GYVLMDYHSGKVLAEKEmDTKLSPASLTKMMTSYVIGQEVKRGNISLNDDVVISKNAWAKNFPDSSKMfvEVGTTVKVSD 120
Cdd:COG2367   36 GVYVLDLDTGETVGINA-DERFPAASTFKLPVLAAVLRQVDAGKLSLDERVTLTPEDLVGGSGILQKL--PDGTGLTLRE 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446670944 121 LNRGIIIQSGNDACVAMAEHVaGTEDafvdlMNAWASSLGMKNSHFTnsHGLDDPNLY-------STPYDLALLGQALIR 193
Cdd:COG2367  113 LAELMITVSDNTATNLLLRLL-GPDA-----VNAFLRSLGLTDTRLD--RKEPDLNELpgdgrntTTPRDMARLLAALYR 184


                 .
gi 446670944 194 D 194
Cdd:COG2367  185 G 185
Beta-lactamase2 pfam13354
Beta-lactamase enzyme family; This is the catalytic domain of class A beta-lactamases. It is ...
 41-259 3.04e-05

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: 44.57  E-value: 3.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446670944   41 GYVLMDYHSGKVLAEKEmDTKLSPASLTKMMTSYVIGQEVKRGNISLNDDVVISKNAWAKNFPDSSKMfvEVGTTVKVSD 120
Cdd:pfam13354   1 GIYVRDLDTGEELGING-DRSFPAASTIKVPILLAVLEQVDEGKLSLDERLTVTAEDKVGGSGILQYL--PDGSQLSLRD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446670944  121 LNRGIIIQSGNDACVAMAEHVaGTEDafvdlMNAWASSLGMKNSHFTN-----SHGLDDPNLYSTPYDLALLGQALIRD- 194
Cdd:pfam13354  78 LLTLMIAVSDNTATNLLIDRL-GLEA-----VNARLRALGLRDTRLRRklpdlRAADKGGTNTTTARDMAKLLEALYRGe 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446670944  195 -VPEE-----YAIYSEQKFTyNGITQYNRngllwdksmnvDGIKTGHTSGAGYNLVSSA----TEGNMRLVAVVM 259
Cdd:pfam13354 152 lLSPEstdrlLDILSRQQFR-DRLPAGLP-----------KGARVAHKTGDLGGVRHDVgivyAPDGRPYVLAVF 214
Beta-lactamase pfam00144
Beta-lactamase; This family appears to be distantly related to pfam00905 and PF00768 ...
 41-91 7.74e-04

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: 40.95  E-value: 7.74e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446670944   41 GYVLMDYHSGKVL-------AEKEMDTKLSP------ASLTKMMTSYVIGQEVKRGNISLNDDV 91
Cdd:pfam00144  16 GVAVAVTRDGKVVvdrgggvADLEGGRPVTAdtlfriASVTKTFTAAAVLQLVERGKLDLDDPV 79
AmpC COG1680
CubicO group peptidase, beta-lactamase class C family [Defense mechanisms];
37-91 1.50e-03

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


Pssm-ID: 441286 [Multi-domain]  Cd Length: 355  Bit Score: 40.44  E-value: 1.50e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446670944  37 IAAKGYVLMDYHSGKVLAEkemDTKLSPASLTKMMTSYVIGQEVKRGNISLNDDV 91
Cdd:COG1680   46 VYEKAYGVADLETGRPVTP---DTLFRIASVTKSFTATAVLQLVEEGKLDLDDPV 97
 
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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