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Conserved domains on  [gi|951185154|ref|WP_057662870|]
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M15 family metallopeptidase [Stenotrophomonas koreensis]

Protein Classification

M15 family metallopeptidase( domain architecture ID 13000460)

M15 family metallopeptidase of the zinc-binding metallopeptidase family, which contains mostly carboxypeptidases and dipeptidases, is involved in bacterial cell wall biosynthesis and metabolism

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
D-Ala-D-Ala_dipeptidase_VanX cd14817
D-Ala-D-Ala dipeptidase VanX; D-Ala-D-Ala dipeptidase (also known as D-alanyl-D-alanine ...
34-233 4.55e-109

D-Ala-D-Ala dipeptidase VanX; D-Ala-D-Ala dipeptidase (also known as D-alanyl-D-alanine dipeptidase vanX; VanX; EC 3.4.13.22) is a Zn2+-dependent enzyme that mediates resistance to the antibiotic vancomycin in Enterococci and other bacteria (both Gram-positive and Gram-negative). It is part of a gene cluster that affects cell-wall biosynthesis. The operon triggers the termination of peptidoglycan precursors by D-Ala-(R)-lactate instead of D-Ala-D-Ala dipeptides. The enzyme is stereospecific, as L-Ala-L-Ala, D-Ala-L-Ala and L-Ala-D-Ala are not substrates. It belongs in the MEROPS peptidase family M15, subfamily D.


:

Pssm-ID: 350616  Cd Length: 199  Bit Score: 311.73  E-value: 4.55e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951185154  34 AGLVDVAGLAPDITVDMRYLGSNNFTGAPVPGYQANRCYLRAPAAQALARVQQAVAQQGYRLQVFDCYRPVRAVQAFVRW 113
Cdd:cd14817    1 AGFVYLADVIPDIVQDIRYAGSDNFVGRPIDGYEAPRCILTREAAEALAKVQAELAKQGLGLKVYDCYRPQRAVDHFVRW 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951185154 114 AHAPADPAAKAAYFPQIDKPDLL-NGYISATSGHSLGHTVDLTLLDCRSGacQPLDMGTPFDFFDPRANLGHPAVTPAQV 192
Cdd:cd14817   81 AKDPDDTRMKAEFYPDVDKKDLFeLGYIAEKSGHSRGSTVDLTLVDLDTG--EELDMGTPFDFFDPLSHTDSPGITAQQR 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 951185154 193 ANRNLLQQAMQAQGFEPYAMEWWHFSHPEQRSEATRLDVPV 233
Cdd:cd14817  159 ANRLLLRSLMEKHGFKPYPKEWWHFTLKDEPYPDTYFDFPV 199
 
Name Accession Description Interval E-value
D-Ala-D-Ala_dipeptidase_VanX cd14817
D-Ala-D-Ala dipeptidase VanX; D-Ala-D-Ala dipeptidase (also known as D-alanyl-D-alanine ...
34-233 4.55e-109

D-Ala-D-Ala dipeptidase VanX; D-Ala-D-Ala dipeptidase (also known as D-alanyl-D-alanine dipeptidase vanX; VanX; EC 3.4.13.22) is a Zn2+-dependent enzyme that mediates resistance to the antibiotic vancomycin in Enterococci and other bacteria (both Gram-positive and Gram-negative). It is part of a gene cluster that affects cell-wall biosynthesis. The operon triggers the termination of peptidoglycan precursors by D-Ala-(R)-lactate instead of D-Ala-D-Ala dipeptides. The enzyme is stereospecific, as L-Ala-L-Ala, D-Ala-L-Ala and L-Ala-D-Ala are not substrates. It belongs in the MEROPS peptidase family M15, subfamily D.


Pssm-ID: 350616  Cd Length: 199  Bit Score: 311.73  E-value: 4.55e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951185154  34 AGLVDVAGLAPDITVDMRYLGSNNFTGAPVPGYQANRCYLRAPAAQALARVQQAVAQQGYRLQVFDCYRPVRAVQAFVRW 113
Cdd:cd14817    1 AGFVYLADVIPDIVQDIRYAGSDNFVGRPIDGYEAPRCILTREAAEALAKVQAELAKQGLGLKVYDCYRPQRAVDHFVRW 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951185154 114 AHAPADPAAKAAYFPQIDKPDLL-NGYISATSGHSLGHTVDLTLLDCRSGacQPLDMGTPFDFFDPRANLGHPAVTPAQV 192
Cdd:cd14817   81 AKDPDDTRMKAEFYPDVDKKDLFeLGYIAEKSGHSRGSTVDLTLVDLDTG--EELDMGTPFDFFDPLSHTDSPGITAQQR 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 951185154 193 ANRNLLQQAMQAQGFEPYAMEWWHFSHPEQRSEATRLDVPV 233
Cdd:cd14817  159 ANRLLLRSLMEKHGFKPYPKEWWHFTLKDEPYPDTYFDFPV 199
DdpX COG2173
D-alanyl-D-alanine dipeptidase [Cell wall/membrane/envelope biogenesis];
29-234 2.21e-81

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


Pssm-ID: 441776  Cd Length: 207  Bit Score: 242.10  E-value: 2.21e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951185154  29 TTAAEAGLVDVAGLAPDITVDMRYLGSNNFTGAPVPgYQANRCYLRAPAAQALARVQQAVAQQGYRLQVFDCYRPVRAVQ 108
Cdd:COG2173    8 QAECPEGLVDIADVDPGIRLDLRYATPDNFTGRPVP-YGAPRCYLRRPAAEALAKAQAELAAQGLRLKIFDAYRPQSAQQ 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951185154 109 AFVRwahapADPAAKAAYFPQIDKPDLLN-GYISA---TSGHSLGHTVDLTLLDcRSGacQPLDMGTPFDFFDPRANLGH 184
Cdd:COG2173   87 HFWD-----ALPDDLRMKYPDVDKAELFVrGYVADparGSPHSRGAAVDLTLVD-ATG--KELDMGTGFDEFSPRSHPDY 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 951185154 185 PAVTPAQVANRNLLQQAMQAQGFEPYAMEWWHFSHPEQRSEATrLDVPVR 234
Cdd:COG2173  159 PGLTAEARANRRLLREAMEAAGFTNYPTEWWHFDLGDEMPYPV-LDFPVE 207
Peptidase_M15 pfam01427
D-ala-D-ala dipeptidase;
33-233 3.22e-43

D-ala-D-ala dipeptidase;


Pssm-ID: 279735  Cd Length: 199  Bit Score: 144.68  E-value: 3.22e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951185154   33 EAGLVDVAGLAPDITVDMRYLGSNNFTGAPVpGYQANRCYLRAPAAQALARVQQAVAQQGYRLQVFDCYRPVRAVQAFVR 112
Cdd:pfam01427   2 SLGLVDLAQVGPDYQIDLKYATADNFTGKQL-LYQAARCLAHKEPAWALAVADAYAPIAGQQLVVWDTYRPIVAQDGLQG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951185154  113 WAHAPADPAAKAAYFPQIDKPDLLNgyISATSGHSLGHTVDLTLLdcRSGACQPLDMGTPFDFFDPRANLGHP-AVTPAQ 191
Cdd:pfam01427  81 WVATPEPKEVIYHQVYQIWAVPNNN--PLTPSPHSRGAAIDLTLR--RDDLGQLVDMGGEFDEMSERSHANAYqTVEPAA 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 951185154  192 VANRNLLQQAMQAQGFEPYAMEWWHFSHPEQRSEATRLDVPV 233
Cdd:pfam01427 157 QRNRKLLRAIMESGGFLRYSGEWWHFSLPDALYNDRHPDFQV 198
PRK10178 PRK10178
D-alanyl-D-alanine dipeptidase; Provisional
36-224 7.65e-39

D-alanyl-D-alanine dipeptidase; Provisional


Pssm-ID: 236662  Cd Length: 184  Bit Score: 132.84  E-value: 7.65e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951185154  36 LVDVAGLAPDITVDMRYLGSNNFTGAPVpgYQANRCYLRAPAAQALARVQQAVAQQGYRLQVFDCYRPVRAVQafVRWAH 115
Cdd:PRK10178   7 LVEITVAFHGVEIDLKYATADNLTGKPI--YREARCLLHKDAEAALRKAVSIAQLAGLTLRIYDAYRPQQAQQ--VLWDA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951185154 116 ApadpaakaayfpqidkPDllNGYISAT---SGHSLGHTVDLTLLDcRSGacQPLDMGTPFDFFDPRANLGHPAVTPAQV 192
Cdd:PRK10178  83 C----------------PD--PQYVADLgrgSNHSRGTAIDLTLVD-AHG--NILDMGTGFDEMHARSHHFHPGVPPAAQ 141
                        170       180       190
                 ....*....|....*....|....*....|..
gi 951185154 193 ANRNLLQQAMQAQGFEPYAMEWWHFSHPEQRS 224
Cdd:PRK10178 142 RNRLLLLGIMHAAGFVHIASEWWHYELPGAAA 173
 
Name Accession Description Interval E-value
D-Ala-D-Ala_dipeptidase_VanX cd14817
D-Ala-D-Ala dipeptidase VanX; D-Ala-D-Ala dipeptidase (also known as D-alanyl-D-alanine ...
34-233 4.55e-109

D-Ala-D-Ala dipeptidase VanX; D-Ala-D-Ala dipeptidase (also known as D-alanyl-D-alanine dipeptidase vanX; VanX; EC 3.4.13.22) is a Zn2+-dependent enzyme that mediates resistance to the antibiotic vancomycin in Enterococci and other bacteria (both Gram-positive and Gram-negative). It is part of a gene cluster that affects cell-wall biosynthesis. The operon triggers the termination of peptidoglycan precursors by D-Ala-(R)-lactate instead of D-Ala-D-Ala dipeptides. The enzyme is stereospecific, as L-Ala-L-Ala, D-Ala-L-Ala and L-Ala-D-Ala are not substrates. It belongs in the MEROPS peptidase family M15, subfamily D.


Pssm-ID: 350616  Cd Length: 199  Bit Score: 311.73  E-value: 4.55e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951185154  34 AGLVDVAGLAPDITVDMRYLGSNNFTGAPVPGYQANRCYLRAPAAQALARVQQAVAQQGYRLQVFDCYRPVRAVQAFVRW 113
Cdd:cd14817    1 AGFVYLADVIPDIVQDIRYAGSDNFVGRPIDGYEAPRCILTREAAEALAKVQAELAKQGLGLKVYDCYRPQRAVDHFVRW 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951185154 114 AHAPADPAAKAAYFPQIDKPDLL-NGYISATSGHSLGHTVDLTLLDCRSGacQPLDMGTPFDFFDPRANLGHPAVTPAQV 192
Cdd:cd14817   81 AKDPDDTRMKAEFYPDVDKKDLFeLGYIAEKSGHSRGSTVDLTLVDLDTG--EELDMGTPFDFFDPLSHTDSPGITAQQR 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 951185154 193 ANRNLLQQAMQAQGFEPYAMEWWHFSHPEQRSEATRLDVPV 233
Cdd:cd14817  159 ANRLLLRSLMEKHGFKPYPKEWWHFTLKDEPYPDTYFDFPV 199
DdpX COG2173
D-alanyl-D-alanine dipeptidase [Cell wall/membrane/envelope biogenesis];
29-234 2.21e-81

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


Pssm-ID: 441776  Cd Length: 207  Bit Score: 242.10  E-value: 2.21e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951185154  29 TTAAEAGLVDVAGLAPDITVDMRYLGSNNFTGAPVPgYQANRCYLRAPAAQALARVQQAVAQQGYRLQVFDCYRPVRAVQ 108
Cdd:COG2173    8 QAECPEGLVDIADVDPGIRLDLRYATPDNFTGRPVP-YGAPRCYLRRPAAEALAKAQAELAAQGLRLKIFDAYRPQSAQQ 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951185154 109 AFVRwahapADPAAKAAYFPQIDKPDLLN-GYISA---TSGHSLGHTVDLTLLDcRSGacQPLDMGTPFDFFDPRANLGH 184
Cdd:COG2173   87 HFWD-----ALPDDLRMKYPDVDKAELFVrGYVADparGSPHSRGAAVDLTLVD-ATG--KELDMGTGFDEFSPRSHPDY 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 951185154 185 PAVTPAQVANRNLLQQAMQAQGFEPYAMEWWHFSHPEQRSEATrLDVPVR 234
Cdd:COG2173  159 PGLTAEARANRRLLREAMEAAGFTNYPTEWWHFDLGDEMPYPV-LDFPVE 207
D-Ala-D-Ala_dipeptidase_Aad cd14840
D-Ala-D-Ala dipeptidase (includes Lactobacillus plantarum Aad peptidase); D-Ala-D-Ala ...
49-224 1.41e-58

D-Ala-D-Ala dipeptidase (includes Lactobacillus plantarum Aad peptidase); D-Ala-D-Ala dipeptidase (also known as D-alanyl-D-alanine dipeptidase vanX; VanX; EC 3.4.13.22) is a Zn2+-dependent enzyme that mediates resistance to the antibiotic vancomycin in Enterococci and other bacteria (both Gram-positive and Gram-negative). It is part of a gene cluster that affects cell-wall biosynthesis. The operon triggers the termination of peptidoglycan precursors by D-Ala-(R)-lactate instead of D-Ala-D-Ala dipeptides. The enzyme is stereospecific, as L-Ala-L-Ala, D-Ala-L-Ala and L-Ala-D-Ala are not substrates. This subfamily includes Lactobacillus Aad peptidase and belongs in the MEROPS peptidase family M15, subfamily D.


Pssm-ID: 350617 [Multi-domain]  Cd Length: 158  Bit Score: 182.24  E-value: 1.41e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951185154  49 DMRYLGSNNFTGAPVpgYQANRCYLRAPAAQALARVQQAVAQQGYRLQVFDCYRPVRAVQAFvrWahapadpaakaayfp 128
Cdd:cd14840    1 DLRYATTDNFTGKKL--YPSARAYLRKEAAEKLAKAQKELKKPGYRLKIFDAYRPLSVQKKL--W--------------- 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951185154 129 qiDK-PDllNGYISA---TSGHSLGHTVDLTLLDCRSGacqPLDMGTPFDFFDPRANLGHPAVTPAQVANRNLLQQAMQA 204
Cdd:cd14840   62 --EAvPD--PRYVANpakGSRHNRGAAVDLTLVDLKGG---ELDMGTGFDDFSERAHHDYEGLSEEALKNRLLLREVMEK 134
                        170       180
                 ....*....|....*....|
gi 951185154 205 QGFEPYAMEWWHFSHPEQRS 224
Cdd:cd14840  135 AGFKPIPTEWWHFDDPDWKK 154
Peptidase_M15 pfam01427
D-ala-D-ala dipeptidase;
33-233 3.22e-43

D-ala-D-ala dipeptidase;


Pssm-ID: 279735  Cd Length: 199  Bit Score: 144.68  E-value: 3.22e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951185154   33 EAGLVDVAGLAPDITVDMRYLGSNNFTGAPVpGYQANRCYLRAPAAQALARVQQAVAQQGYRLQVFDCYRPVRAVQAFVR 112
Cdd:pfam01427   2 SLGLVDLAQVGPDYQIDLKYATADNFTGKQL-LYQAARCLAHKEPAWALAVADAYAPIAGQQLVVWDTYRPIVAQDGLQG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951185154  113 WAHAPADPAAKAAYFPQIDKPDLLNgyISATSGHSLGHTVDLTLLdcRSGACQPLDMGTPFDFFDPRANLGHP-AVTPAQ 191
Cdd:pfam01427  81 WVATPEPKEVIYHQVYQIWAVPNNN--PLTPSPHSRGAAIDLTLR--RDDLGQLVDMGGEFDEMSERSHANAYqTVEPAA 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 951185154  192 VANRNLLQQAMQAQGFEPYAMEWWHFSHPEQRSEATRLDVPV 233
Cdd:pfam01427 157 QRNRKLLRAIMESGGFLRYSGEWWHFSLPDALYNDRHPDFQV 198
PRK10178 PRK10178
D-alanyl-D-alanine dipeptidase; Provisional
36-224 7.65e-39

D-alanyl-D-alanine dipeptidase; Provisional


Pssm-ID: 236662  Cd Length: 184  Bit Score: 132.84  E-value: 7.65e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951185154  36 LVDVAGLAPDITVDMRYLGSNNFTGAPVpgYQANRCYLRAPAAQALARVQQAVAQQGYRLQVFDCYRPVRAVQafVRWAH 115
Cdd:PRK10178   7 LVEITVAFHGVEIDLKYATADNLTGKPI--YREARCLLHKDAEAALRKAVSIAQLAGLTLRIYDAYRPQQAQQ--VLWDA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951185154 116 ApadpaakaayfpqidkPDllNGYISAT---SGHSLGHTVDLTLLDcRSGacQPLDMGTPFDFFDPRANLGHPAVTPAQV 192
Cdd:PRK10178  83 C----------------PD--PQYVADLgrgSNHSRGTAIDLTLVD-AHG--NILDMGTGFDEMHARSHHFHPGVPPAAQ 141
                        170       180       190
                 ....*....|....*....|....*....|..
gi 951185154 193 ANRNLLQQAMQAQGFEPYAMEWWHFSHPEQRS 224
Cdd:PRK10178 142 RNRLLLLGIMHAAGFVHIASEWWHYELPGAAA 173
D-Ala-D-Ala_dipeptidase_like cd14843
D-Ala-D-Ala dipeptidase, includes uncharacterized enzymes; This subfamily of D-Ala-D-Ala ...
73-222 1.23e-21

D-Ala-D-Ala dipeptidase, includes uncharacterized enzymes; This subfamily of D-Ala-D-Ala dipeptidase (also known as D-alanyl-D-alanine dipeptidase vanX; VanX; EC 3.4.13.22) also includes several uncharacterized proteins. This is a Zn2+-dependent enzyme that mediates resistance to the antibiotic vancomycin in Enterococci and other bacteria (both Gram-positive and Gram-negative). It is part of a gene cluster that affects cell-wall biosynthesis. The operon triggers the termination of peptidoglycan precursors by D-Ala-(R)-lactate instead of D-Ala-D-Ala dipeptides. The enzyme is stereospecific, as L-Ala-L-Ala, D-Ala-L-Ala and L-Ala-D-Ala are not substrates. It belongs in the MEROPS peptidase family M15, subfamily D.


Pssm-ID: 350618 [Multi-domain]  Cd Length: 160  Bit Score: 87.35  E-value: 1.23e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951185154  73 LRAPAAQALARVQQAVAQqGYRLQVFDCYRPVrAVQAFVRwahapadpaakAAYFPQIDK----PDLLNGYISAT----- 143
Cdd:cd14843    1 LRESVAERLLQAQSLLPK-GLRLLIFDGYRPL-AVQKFLF-----------ERYYQKIRKrhpgRSPEELIEEVRkfvap 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951185154 144 --------SGHSLGHTVDLTLLDCRSgacQPLDMGTPFDFFDPRANLGHPAVTPA----QVA--NRNLLQQAMQAQGFEP 209
Cdd:cd14843   68 pskdpltpPPHSTGGAVDLTLADEDG---KELDMGGPIDDDTEASEAYEEALTDStgisEEArnNRRLLYDAMESAGFVN 144
                        170
                 ....*....|...
gi 951185154 210 YAMEWWHFSHPEQ 222
Cdd:cd14843  145 YPTEWWHFSYGDQ 157
D-Ala-D-Ala_dipeptidase cd17880
D-Ala-D-Ala_dipeptidase; This family contains D-Ala-D-Ala dipeptidase enzymes which include ...
77-220 2.74e-17

D-Ala-D-Ala_dipeptidase; This family contains D-Ala-D-Ala dipeptidase enzymes which include D-alanyl-D-alanine dipeptidase vanX and Aad, among others. VanX is a Zn2+-dependent enzyme that mediates resistance to the antibiotic vancomycin in Enterococci and other bacteria (both Gram-positive and Gram-negative). It is part of a gene cluster that affects cell-wall biosynthesis. The operon triggers the termination of peptidoglycan precursors by D-Ala-(R)-lactate instead of D-Ala-D-Ala dipeptides. The enzyme is stereospecific, as L-Ala-L-Ala, D-Ala-L-Ala and L-Ala-D-Ala are not substrates. It fasmily includes Lactobacillus Aad peptidase and belongs in the MEROPS peptidase family M15, subfamily D.


Pssm-ID: 350625 [Multi-domain]  Cd Length: 110  Bit Score: 74.68  E-value: 2.74e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951185154  77 AAQALARVQQAVAQQGYRLQVFDCYRPVRAVQAFVRWAHAPADPAAKAAYFPQIDKPDLL-NGYISATSGHSLGHTVDLT 155
Cdd:cd17880    3 VLKRLDKARLTAADIGWELLVFDAYRPIAAQQFMVQHTFAPIVARDGLQGQHQVYQIWAVpNNNVLTPSPHSRGAAIDLT 82
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 951185154 156 LldcrsgacqpldmgtpfdffdpranlghpavtpaqvaNRNLLQQAMQAQGFEPYAMEWWHFSHP 220
Cdd:cd17880   83 L-------------------------------------RRELLNTIMESGGFLRHSGEWWHFSLG 110
Peptidase_M15 cd14814
Metalloproteases including zinc D-Ala-D-Ala carboxypeptidase, L-Ala-D-Glu peptidase, L, ...
75-220 3.26e-03

Metalloproteases including zinc D-Ala-D-Ala carboxypeptidase, L-Ala-D-Glu peptidase, L,D-carboxypeptidase, bacteriophage endolysins, and related proteins; This family summarizes zinc-binding metallopeptidases which are mostly carboxypeptidases and dipeptidases, and includes zinc-dependent D-Ala-D-Ala carboxypeptidases, VanX, L-Ala-D-Glu peptidase, L,D-carboxypeptidase and bacteriophage endolysins, amongst other family members. These peptidases belong to MEROPS family M15 which are involved in bacterial cell wall biosynthesis and metabolism.


Pssm-ID: 350615 [Multi-domain]  Cd Length: 111  Bit Score: 36.26  E-value: 3.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951185154  75 APAAQALARVQQAVAQQGYRLQVFDCYRPVRAVQAFVRWahapadpaakaayfpqidKPDLLNGYISA----TSGHSLGH 150
Cdd:cd14814    1 PDAAEALARMIAAAGAEGRTLTINSGYRTYAQQLRLFAA------------------KGKGSGGRRWAappgTSNHQWGL 62
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 951185154 151 TVDLtlldcrsGACQPLDMGTPFDFF---DPRANLGHPAVTPAQVANRnllqqamqaqgfepyamEWWHFSHP 220
Cdd:cd14814   63 AIDL-------GDGGGWRETQGYRWLkanAPRYGFDNPGGARRGGAFQ-----------------EPWHWEYV 111
LdcB COG1876
LD-carboxypeptidase LdcB, LAS superfamily [Cell wall/membrane/envelope biogenesis];
51-102 4.88e-03

LD-carboxypeptidase LdcB, LAS superfamily [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441480  Cd Length: 168  Bit Score: 36.78  E-value: 4.88e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 951185154  51 RYLGSNNFTGAPVPGYqanrcYLRAPAAQALARVQQAVAQQGYRLQVFDCYR 102
Cdd:COG1876    6 HPLPADDLVPLPGGGH-----RLRKEAAAAFEAMQAAAKKDGIDLVIVSGYR 52
 
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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