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Conserved domains on  [gi|804839927|emb|CRA31639|]
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Svh [Salmonella enterica subsp. enterica serovar Typhi]

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 ...
31-252 1.24e-131

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: 369.90  E-value: 1.24e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 804839927  31 KDFVDITTVAPDVQVDMRYFTSHNFIGRPIKGYNAPVCLLTRPAANAVKQVADRLRPFGLTLKIYDCYRPQSAVNDFIAW 110
Cdd:cd14817    1 AGFVYLADVIPDIVQDIRYAGSDNFVGRPIDGYEAPRCILTREAAEALAKVQAELAKQGLGLKVYDCYRPQRAVDHFVRW 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 804839927 111 AKDPSQNQMKNEFYPQVEKNRLFEEGYLAARSGHSRGSTLDLTIVPLDSkipiyhpgrplvnctasaaqrspDNSLDFGT 190
Cdd:cd14817   81 AKDPDDTRMKAEFYPDVDKKDLFELGYIAEKSGHSRGSTVDLTLVDLDT-----------------------GEELDMGT 137
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 804839927 191 GFDCFSPLSHPDNVMLTAQQRANRLLLQTLMRDAGFTPLDTEWWHFSLTHEPYPNTWFDFPV 252
Cdd:cd14817  138 PFDFFDPLSHTDSPGITAQQRANRLLLRSLMEKHGFKPYPKEWWHFTLKDEPYPDTYFDFPV 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 ...
31-252 1.24e-131

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: 369.90  E-value: 1.24e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 804839927  31 KDFVDITTVAPDVQVDMRYFTSHNFIGRPIKGYNAPVCLLTRPAANAVKQVADRLRPFGLTLKIYDCYRPQSAVNDFIAW 110
Cdd:cd14817    1 AGFVYLADVIPDIVQDIRYAGSDNFVGRPIDGYEAPRCILTREAAEALAKVQAELAKQGLGLKVYDCYRPQRAVDHFVRW 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 804839927 111 AKDPSQNQMKNEFYPQVEKNRLFEEGYLAARSGHSRGSTLDLTIVPLDSkipiyhpgrplvnctasaaqrspDNSLDFGT 190
Cdd:cd14817   81 AKDPDDTRMKAEFYPDVDKKDLFELGYIAEKSGHSRGSTVDLTLVDLDT-----------------------GEELDMGT 137
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 804839927 191 GFDCFSPLSHPDNVMLTAQQRANRLLLQTLMRDAGFTPLDTEWWHFSLTHEPYPNTWFDFPV 252
Cdd:cd14817  138 PFDFFDPLSHTDSPGITAQQRANRLLLRSLMEKHGFKPYPKEWWHFTLKDEPYPDTYFDFPV 199
DdpX COG2173
D-alanyl-D-alanine dipeptidase [Cell wall/membrane/envelope biogenesis];
30-253 2.89e-91

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


Pssm-ID: 441776  Cd Length: 207  Bit Score: 267.90  E-value: 2.89e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 804839927  30 PKDFVDITTVAPDVQVDMRYFTSHNFIGRPIKgYNAPVCLLTRPAANAVKQVADRLRPFGLTLKIYDCYRPQSAVNDFia 109
Cdd:COG2173   12 PEGLVDIADVDPGIRLDLRYATPDNFTGRPVP-YGAPRCYLRRPAAEALAKAQAELAAQGLRLKIFDAYRPQSAQQHF-- 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 804839927 110 WAKDPSQNQMKnefYPQVEKNRLFEEGYLAAR---SGHSRGSTLDLTIVPLDskipiyhpgrplvnctasaaqrspDNSL 186
Cdd:COG2173   89 WDALPDDLRMK---YPDVDKAELFVRGYVADPargSPHSRGAAVDLTLVDAT------------------------GKEL 141
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 804839927 187 DFGTGFDCFSPLSHPDNVMLTAQQRANRLLLQTLMRDAGFTPLDTEWWHFSLTHE-PYPNTwfDFPVK 253
Cdd:COG2173  142 DMGTGFDEFSPRSHPDYPGLTAEARANRRLLREAMEAAGFTNYPTEWWHFDLGDEmPYPVL--DFPVE 207
Peptidase_M15 pfam01427
D-ala-D-ala dipeptidase;
33-252 4.44e-41

D-ala-D-ala dipeptidase;


Pssm-ID: 279735  Cd Length: 199  Bit Score: 140.06  E-value: 4.44e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 804839927   33 FVDITTVAPDVQVDMRYFTSHNFIGRPIkGYNAPVCLLTRPAANAVKQVADRLRPFGLTLKIYDCYRPQSAVNDFIAWAK 112
Cdd:pfam01427   5 LVDLAQVGPDYQIDLKYATADNFTGKQL-LYQAARCLAHKEPAWALAVADAYAPIAGQQLVVWDTYRPIVAQDGLQGWVA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 804839927  113 DPSQNQMKNEFYPQVEKNrlfEEGYLAARSGHSRGSTLDLTIVPLDSKIPiyhpgrplvnctasaaqrspdnsLDFGTGF 192
Cdd:pfam01427  84 TPEPKEVIYHQVYQIWAV---PNNNPLTPSPHSRGAAIDLTLRRDDLGQL-----------------------VDMGGEF 137
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 804839927  193 DCFSPLSHPDNV-MLTAQQRANRLLLQTLMRDAGFTPLDTEWWHFSLTHEPYPNTWFDFPV 252
Cdd:pfam01427 138 DEMSERSHANAYqTVEPAAQRNRKLLRAIMESGGFLRYSGEWWHFSLPDALYNDRHPDFQV 198
PRK10178 PRK10178
D-alanyl-D-alanine dipeptidase; Provisional
34-238 5.53e-38

D-alanyl-D-alanine dipeptidase; Provisional


Pssm-ID: 236662  Cd Length: 184  Bit Score: 131.30  E-value: 5.53e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 804839927  34 VDITTVAPDVQVDMRYFTSHNFIGRPIkgYNAPVCLLTRPAANAVKQVADRLRPFGLTLKIYDCYRPQSAvnDFIAWAKD 113
Cdd:PRK10178   8 VEITVAFHGVEIDLKYATADNLTGKPI--YREARCLLHKDAEAALRKAVSIAQLAGLTLRIYDAYRPQQA--QQVLWDAC 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 804839927 114 PSQNqmknefypqveknrlfeegYLA--AR-SGHSRGSTLDLTIVPLDSkipiyhpgrplvnctasaaqrspdNSLDFGT 190
Cdd:PRK10178  84 PDPQ-------------------YVAdlGRgSNHSRGTAIDLTLVDAHG------------------------NILDMGT 120
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 804839927 191 GFDCFSPLSHPDNVMLTAQQRANRLLLQTLMRDAGFTPLDTEWWHFSL 238
Cdd:PRK10178 121 GFDEMHARSHHFHPGVPPAAQRNRLLLLGIMHAAGFVHIASEWWHYEL 168
 
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 ...
31-252 1.24e-131

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: 369.90  E-value: 1.24e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 804839927  31 KDFVDITTVAPDVQVDMRYFTSHNFIGRPIKGYNAPVCLLTRPAANAVKQVADRLRPFGLTLKIYDCYRPQSAVNDFIAW 110
Cdd:cd14817    1 AGFVYLADVIPDIVQDIRYAGSDNFVGRPIDGYEAPRCILTREAAEALAKVQAELAKQGLGLKVYDCYRPQRAVDHFVRW 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 804839927 111 AKDPSQNQMKNEFYPQVEKNRLFEEGYLAARSGHSRGSTLDLTIVPLDSkipiyhpgrplvnctasaaqrspDNSLDFGT 190
Cdd:cd14817   81 AKDPDDTRMKAEFYPDVDKKDLFELGYIAEKSGHSRGSTVDLTLVDLDT-----------------------GEELDMGT 137
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 804839927 191 GFDCFSPLSHPDNVMLTAQQRANRLLLQTLMRDAGFTPLDTEWWHFSLTHEPYPNTWFDFPV 252
Cdd:cd14817  138 PFDFFDPLSHTDSPGITAQQRANRLLLRSLMEKHGFKPYPKEWWHFTLKDEPYPDTYFDFPV 199
DdpX COG2173
D-alanyl-D-alanine dipeptidase [Cell wall/membrane/envelope biogenesis];
30-253 2.89e-91

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


Pssm-ID: 441776  Cd Length: 207  Bit Score: 267.90  E-value: 2.89e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 804839927  30 PKDFVDITTVAPDVQVDMRYFTSHNFIGRPIKgYNAPVCLLTRPAANAVKQVADRLRPFGLTLKIYDCYRPQSAVNDFia 109
Cdd:COG2173   12 PEGLVDIADVDPGIRLDLRYATPDNFTGRPVP-YGAPRCYLRRPAAEALAKAQAELAAQGLRLKIFDAYRPQSAQQHF-- 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 804839927 110 WAKDPSQNQMKnefYPQVEKNRLFEEGYLAAR---SGHSRGSTLDLTIVPLDskipiyhpgrplvnctasaaqrspDNSL 186
Cdd:COG2173   89 WDALPDDLRMK---YPDVDKAELFVRGYVADPargSPHSRGAAVDLTLVDAT------------------------GKEL 141
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 804839927 187 DFGTGFDCFSPLSHPDNVMLTAQQRANRLLLQTLMRDAGFTPLDTEWWHFSLTHE-PYPNTwfDFPVK 253
Cdd:COG2173  142 DMGTGFDEFSPRSHPDYPGLTAEARANRRLLREAMEAAGFTNYPTEWWHFDLGDEmPYPVL--DFPVE 207
D-Ala-D-Ala_dipeptidase_Aad cd14840
D-Ala-D-Ala dipeptidase (includes Lactobacillus plantarum Aad peptidase); D-Ala-D-Ala ...
46-239 1.24e-52

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: 167.98  E-value: 1.24e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 804839927  46 DMRYFTSHNFIGRPIkgYNAPVCLLTRPAANAVKQVADRLRPFGLTLKIYDCYRPQSAvndfiawakdpsQNQMkNEFYP 125
Cdd:cd14840    1 DLRYATTDNFTGKKL--YPSARAYLRKEAAEKLAKAQKELKKPGYRLKIFDAYRPLSV------------QKKL-WEAVP 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 804839927 126 qveknrlfEEGYLA--AR-SGHSRGSTLDLTIVplDSKipiyhpGRPLvnctasaaqrspdnslDFGTGFDCFSPLSHPD 202
Cdd:cd14840   66 --------DPRYVAnpAKgSRHNRGAAVDLTLV--DLK------GGEL----------------DMGTGFDDFSERAHHD 113
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 804839927 203 NVMLTAQQRANRLLLQTLMRDAGFTPLDTEWWHFSLT 239
Cdd:cd14840  114 YEGLSEEALKNRLLLREVMEKAGFKPIPTEWWHFDDP 150
Peptidase_M15 pfam01427
D-ala-D-ala dipeptidase;
33-252 4.44e-41

D-ala-D-ala dipeptidase;


Pssm-ID: 279735  Cd Length: 199  Bit Score: 140.06  E-value: 4.44e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 804839927   33 FVDITTVAPDVQVDMRYFTSHNFIGRPIkGYNAPVCLLTRPAANAVKQVADRLRPFGLTLKIYDCYRPQSAVNDFIAWAK 112
Cdd:pfam01427   5 LVDLAQVGPDYQIDLKYATADNFTGKQL-LYQAARCLAHKEPAWALAVADAYAPIAGQQLVVWDTYRPIVAQDGLQGWVA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 804839927  113 DPSQNQMKNEFYPQVEKNrlfEEGYLAARSGHSRGSTLDLTIVPLDSKIPiyhpgrplvnctasaaqrspdnsLDFGTGF 192
Cdd:pfam01427  84 TPEPKEVIYHQVYQIWAV---PNNNPLTPSPHSRGAAIDLTLRRDDLGQL-----------------------VDMGGEF 137
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 804839927  193 DCFSPLSHPDNV-MLTAQQRANRLLLQTLMRDAGFTPLDTEWWHFSLTHEPYPNTWFDFPV 252
Cdd:pfam01427 138 DEMSERSHANAYqTVEPAAQRNRKLLRAIMESGGFLRYSGEWWHFSLPDALYNDRHPDFQV 198
PRK10178 PRK10178
D-alanyl-D-alanine dipeptidase; Provisional
34-238 5.53e-38

D-alanyl-D-alanine dipeptidase; Provisional


Pssm-ID: 236662  Cd Length: 184  Bit Score: 131.30  E-value: 5.53e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 804839927  34 VDITTVAPDVQVDMRYFTSHNFIGRPIkgYNAPVCLLTRPAANAVKQVADRLRPFGLTLKIYDCYRPQSAvnDFIAWAKD 113
Cdd:PRK10178   8 VEITVAFHGVEIDLKYATADNLTGKPI--YREARCLLHKDAEAALRKAVSIAQLAGLTLRIYDAYRPQQA--QQVLWDAC 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 804839927 114 PSQNqmknefypqveknrlfeegYLA--AR-SGHSRGSTLDLTIVPLDSkipiyhpgrplvnctasaaqrspdNSLDFGT 190
Cdd:PRK10178  84 PDPQ-------------------YVAdlGRgSNHSRGTAIDLTLVDAHG------------------------NILDMGT 120
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 804839927 191 GFDCFSPLSHPDNVMLTAQQRANRLLLQTLMRDAGFTPLDTEWWHFSL 238
Cdd:PRK10178 121 GFDEMHARSHHFHPGVPPAAQRNRLLLLGIMHAAGFVHIASEWWHYEL 168
D-Ala-D-Ala_dipeptidase_like cd14843
D-Ala-D-Ala dipeptidase, includes uncharacterized enzymes; This subfamily of D-Ala-D-Ala ...
79-237 3.12e-18

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: 78.87  E-value: 3.12e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 804839927  79 KQVADRLR------PFGLTLKIYDCYRPQSAvndfiawakdpsQNQMKNEFYPQVEKNR----LFEEGYLAAR------- 141
Cdd:cd14843    3 ESVAERLLqaqsllPKGLRLLIFDGYRPLAV------------QKFLFERYYQKIRKRHpgrsPEELIEEVRKfvappsk 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 804839927 142 -----SGHSRGSTLDLTIVPLDSKipiyhpgrplvnctasaaqrspdnSLDFGTGFDCFSPLSHPDNVMLTA------QQ 210
Cdd:cd14843   71 dpltpPPHSTGGAVDLTLADEDGK------------------------ELDMGGPIDDDTEASEAYEEALTDstgiseEA 126
                        170       180
                 ....*....|....*....|....*..
gi 804839927 211 RANRLLLQTLMRDAGFTPLDTEWWHFS 237
Cdd:cd14843  127 RNNRRLLYDAMESAGFVNYPTEWWHFS 153
D-Ala-D-Ala_dipeptidase cd17880
D-Ala-D-Ala_dipeptidase; This family contains D-Ala-D-Ala dipeptidase enzymes which include ...
89-238 4.29e-16

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: 71.99  E-value: 4.29e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 804839927  89 GLTLKIYDCYRPQSAVNDFIAWAKDPSQNQMKNEFYPQVEKNRLFEEGYLAARSGHSRGSTLDLTIvpldskipiyhpgr 168
Cdd:cd17880   18 GWELLVFDAYRPIAAQQFMVQHTFAPIVARDGLQGQHQVYQIWAVPNNNVLTPSPHSRGAAIDLTL-------------- 83
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 804839927 169 plvnctasaaqrspdnsldfgtgfdcfsplshpdnvmltaqqraNRLLLQTLMRDAGFTPLDTEWWHFSL 238
Cdd:cd17880   84 --------------------------------------------RRELLNTIMESGGFLRHSGEWWHFSL 109
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
22-99 1.68e-03

Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte Tyrosine Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyr residues in protein substrates. ALK and LTK are orphan receptor PTKs (RTKs) whose ligands are not yet well-defined. ALK appears to play an important role in mammalian neural development as well as visceral muscle differentiation in Drosophila. ALK is aberrantly expressed as fusion proteins, due to chromosomal translocations, in about 60% of anaplastic large cell lymphomas (ALCLs). ALK fusion proteins are also found in rare cases of diffuse large B cell lymphomas (DLBCLs). LTK is mainly expressed in B lymphocytes and neuronal tissues. It is important in cell proliferation and survival. Transgenic mice expressing TLK display retarded growth and high mortality rate. In addition, a polymorphism in mouse and human LTK is implicated in the pathogenesis of systemic lupus erythematosus. RTKs contain an extracellular ligand-binding domain, a transmembrane region, and an intracellular tyr kinase domain. They are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The ALK/LTK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270632 [Multi-domain]  Cd Length: 277  Bit Score: 38.91  E-value: 1.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 804839927  22 ENHIDLHQPKDFV--DITTVAPDVQVDMRYFTSHNFIGRPIKGYNapvCLLTRPAANAVKQVADrlrpFGLTLKIY--DC 97
Cdd:cd05036  102 ENRPRPEQPSSLTmlDLLQLAQDVAKGCRYLEENHFIHRDIAARN---CLLTCKGPGRVAKIGD----FGMARDIYraDY 174

                 ..
gi 804839927  98 YR 99
Cdd:cd05036  175 YR 176
 
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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