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Conserved domains on  [gi|2538591192|ref|WP_294897137|]
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MULTISPECIES: peptidoglycan DD-metalloendopeptidase family protein [Sulfuricurvum]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NlpD COG0739
Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell ...
 218-341 6.27e-52

Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 440502 [Multi-domain]  Cd Length: 196  Bit Score: 172.08  E-value: 6.27e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538591192 218 NPRITSRFTkSRYHPVLHRYRAHLGVDFGARPGTPILSTGEGRVSFVGYSTGYGKTIKIRHNNGLTSLYAHQKAFKkgIH 297
Cdd:COG0739    76 KGRITSGFG-YRRHPVTGRRRFHKGIDIAAPTGTPVYAAADGTVVFAGWNGGYGNLVIIDHGNGYTTLYAHLSSIL--VK 152

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2538591192 298 TGMKVKQSEMIGYVGNTGLSSGPHLHFGMYRGSSAIDPLSVMKK 341
Cdd:COG0739   153 VGQRVKAGQVIGYVGNTGRSTGPHLHFEVRVNGKPVDPLPFLPA 196
Csd3_N super family cl39467
Csd3 N-terminal; Csd3 (also known as HdpA) is a bi-functional enzyme with delta, ...
 22-104 3.10e-20

Csd3 N-terminal; Csd3 (also known as HdpA) is a bi-functional enzyme with delta,delta-endopeptidase activity and delta,delta-carboxypeptidase activity. The N-terminal domain is also known as domain 1 and is composed of an alpha/beta fold consisting of a five-stranded antiparallel beta-sheet and three short alpha-helices. Domain 1 blocks the active-site cleft of the LytM domain, with the protruding helix alpha-3 contributing to the Zn2+ coordination sphere. The fold of domain 1 is very remotely related to monellin/cystatin superfamily proteins, some of which act as inhibitors of cysteine peptidases.


The actual alignment was detected with superfamily member pfam18059:

Pssm-ID: 436243  Cd Length: 83  Bit Score: 84.30  E-value: 3.10e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538591192  22 FKWKDGESFLTFLERKKLPLRVYYNLDKEDQKLTEDIPYTAKCQMVVDNQNFIHQILIPVNDELQLQIYlTPKRRYETKV 101
Cdd:pfam18059   2 FVWEKGETLLGFLQKNNIPAKLYYNLDPEDKELTSEIRAGVTYYELRDDDGTLLQALIPVGEELQIHIF-KDKGQYRFDI 80


                  ...
gi 2538591192 102 IPI 104
Cdd:pfam18059  81 IPI 83
Csd3_N2 super family cl44846
Csd3 second domain; This entry represents the second domain from the Csd3 peptidase. This ...
 131-225 1.01e-06

Csd3 second domain; This entry represents the second domain from the Csd3 peptidase. This domain has a similar structure to pfam18059 despite low sequence similarity.


The actual alignment was detected with superfamily member pfam19425:

Pssm-ID: 437257 [Multi-domain]  Cd Length: 122  Bit Score: 47.40  E-value: 1.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538591192 131 SKNLASIFVKMFKGKVDFRKgLKKGDPIiMVYTQKYRLGKPFSMPEVHGAMVEINGKRVRVYRHSDGRFYDEKGGQYEKF 210
Cdd:pfam19425  27 TSNEISAVIKALQWQLDFRK-LKKGDKF-SVLMSREMLDGKREQSQLLGVRLRSGGKDYYAIRAEDGKFYDRNGSGLARG 104

                          90
                  ....*....|....*.
gi 2538591192 211 LFKLP-MRNPRITSRF 225
Cdd:pfam19425 105 FLRFPtAKQFRVSSNF 120
 
Name Accession Description Interval E-value
NlpD COG0739
Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell ...
 218-341 6.27e-52

Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440502 [Multi-domain]  Cd Length: 196  Bit Score: 172.08  E-value: 6.27e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538591192 218 NPRITSRFTkSRYHPVLHRYRAHLGVDFGARPGTPILSTGEGRVSFVGYSTGYGKTIKIRHNNGLTSLYAHQKAFKkgIH 297
Cdd:COG0739    76 KGRITSGFG-YRRHPVTGRRRFHKGIDIAAPTGTPVYAAADGTVVFAGWNGGYGNLVIIDHGNGYTTLYAHLSSIL--VK 152

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2538591192 298 TGMKVKQSEMIGYVGNTGLSSGPHLHFGMYRGSSAIDPLSVMKK 341
Cdd:COG0739   153 VGQRVKAGQVIGYVGNTGRSTGPHLHFEVRVNGKPVDPLPFLPA 196
PRK11649 PRK11649
putative peptidase; Provisional
 135-354 1.57e-38

putative peptidase; Provisional


Pssm-ID: 236946 [Multi-domain]  Cd Length: 439  Bit Score: 143.65  E-value: 1.57e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538591192 135 ASIFVKMFKGKVDFRKgLKKGDPIIMVYTQKYRLGKPfSMPEVHGAMVEINGKRVRVYRHSDGRFYDEKGGQYEKFLFKL 214
Cdd:PRK11649  209 ISAVIKALQWQMDFRK-LKKGDEFSVLMSREMLDGKS-EQSQLLGVRLRSGGKDYYAIRAEDGKFYDRNGSGLAKGFLRF 286

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538591192 215 P-MRNPRITSRFTKSRYHPVLHRYRAHLGVDFGARPGTPILSTGEGRVSFVGYSTGYGKTIKIRHNNGLTSLYAHQKafK 293
Cdd:PRK11649  287 PtAKQFRISSNFNPRRLNPVTGRVAPHRGVDFAMPVGTPVLAVGDGEVVVAKRSGAAGNYVAIRHGRQYTTRYMHLR--K 364

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2538591192 294 KGIHTGMKVKQSEMIGYVGNTGLSSGPHLHFGMYRGSSAIDPLSVMKKKTEGFTGKERRVF 354
Cdd:PRK11649  365 LLVKPGQKVKRGDRIALSGNTGRSTGPHLHYEVWINQQAVNPLTAKLPRTEGLTGKDRREY 425
Peptidase_M23 pfam01551
Peptidase family M23; Members of this family are zinc metallopeptidases with a range of ...
 240-335 2.20e-38

Peptidase family M23; Members of this family are zinc metallopeptidases with a range of specificities. The peptidase family M23 is included in this family, these are Gly-Gly endopeptidases. Peptidase family M23 are also endopeptidases. This family also includes some bacterial lipoproteins such as Swiss:P33648 for which no proteolytic activity has been demonstrated. This family also includes leukocyte cell-derived chemotaxin 2 (LECT2) proteins. LECT2 is a liver-specific protein which is thought to be linked to hepatocyte growth although the exact function of this protein is unknown.


Pssm-ID: 460250 [Multi-domain]  Cd Length: 96  Bit Score: 133.06  E-value: 2.20e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538591192 240 HLGVDFGARPGTPILSTGEGRVSFVGYSTGYGKTIKIRHNNGLTSLYAHQKAFKkgIHTGMKVKQSEMIGYVGNTGLSSG 319
Cdd:pfam01551   3 HKGIDIAAPTGTPVYAAADGVVVFAGWLGGYGNLVIIDHGNGYSTLYAHLSSIL--VKVGQRVKAGQVIGTVGSTGRSTG 80

                          90
                  ....*....|....*.
gi 2538591192 320 PHLHFGMYRGSSAIDP 335
Cdd:pfam01551  81 PHLHFEIRKNGKPVDP 96
M23_peptidase cd12797
M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; ...
 240-326 1.98e-33

M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; This model describes the metallopeptidase M23 family, which includes beta-lytic metallopeptidase and lysostaphin. Members of this family are zinc endopeptidases that lyse bacterial cell wall peptidoglycans; they cleave either the N-acylmuramoyl-Ala bond between the cell wall peptidoglycan and the cross-linking peptide (e.g. beta-lytic endopeptidase) or a bond within the cross-linking peptide (e.g. stapholysin, and lysostaphin). Beta-lytic metallopeptidase, formerly known as beta-lytic protease, has a preference for cleavage of Gly-X bonds and favors hydrophobic or apolar residues on either side. It inhibits growth of sensitive organisms and may potentially serve as an antimicrobial agent. Lysostaphin, produced by Staphylococcus genus, cleaves pentaglycine cross-bridges of cell wall peptidoglycan, acting as autolysins to maintain cell wall metabolism or as toxins and weapons against competing strains. Staphylolysin (also known as LasA) is implicated in a range of processes related to Pseudomonas virulence, including stimulating shedding of the ectodomain of cell surface heparan sulphate proteoglycan syndecan-1, and elastin degradation in connective tissue. Its active site is less constricted and contains a five-coordinate zinc ion with trigonal bipyramidal geometry and two metal-bound water molecules, possibly contributing to its activity against a wider range of substrates than those used by related lytic enzymes, consistent with its multiple roles in Pseudomonas virulence. The family includes members that do not appear to have the conserved zinc-binding site and might be lipoproteins lacking proteolytic activity.


Pssm-ID: 410984 [Multi-domain]  Cd Length: 85  Bit Score: 120.00  E-value: 1.98e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538591192 240 HLGVDFGARPGTPILSTGEGRVSFVGYSTGYGKTIKIRHNNGLTSLYAHQKAFKkgIHTGMKVKQSEMIGYVGNTGLSSG 319
Cdd:cd12797     1 HNGIDIAAPEGTPVYAAADGTVVFAGWDGGYGNYVIIDHGNGYYTLYAHLSSIL--VKVGQRVKKGQVIGTVGNTGRSTG 78


                  ....*..
gi 2538591192 320 PHLHFGM 326
Cdd:cd12797    79 PHLHFEI 85
Csd3_N pfam18059
Csd3 N-terminal; Csd3 (also known as HdpA) is a bi-functional enzyme with delta, ...
 22-104 3.10e-20

Csd3 N-terminal; Csd3 (also known as HdpA) is a bi-functional enzyme with delta,delta-endopeptidase activity and delta,delta-carboxypeptidase activity. The N-terminal domain is also known as domain 1 and is composed of an alpha/beta fold consisting of a five-stranded antiparallel beta-sheet and three short alpha-helices. Domain 1 blocks the active-site cleft of the LytM domain, with the protruding helix alpha-3 contributing to the Zn2+ coordination sphere. The fold of domain 1 is very remotely related to monellin/cystatin superfamily proteins, some of which act as inhibitors of cysteine peptidases.


Pssm-ID: 436243  Cd Length: 83  Bit Score: 84.30  E-value: 3.10e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538591192  22 FKWKDGESFLTFLERKKLPLRVYYNLDKEDQKLTEDIPYTAKCQMVVDNQNFIHQILIPVNDELQLQIYlTPKRRYETKV 101
Cdd:pfam18059   2 FVWEKGETLLGFLQKNNIPAKLYYNLDPEDKELTSEIRAGVTYYELRDDDGTLLQALIPVGEELQIHIF-KDKGQYRFDI 80


                  ...
gi 2538591192 102 IPI 104
Cdd:pfam18059  81 IPI 83
Csd3_N2 pfam19425
Csd3 second domain; This entry represents the second domain from the Csd3 peptidase. This ...
 131-225 1.01e-06

Csd3 second domain; This entry represents the second domain from the Csd3 peptidase. This domain has a similar structure to pfam18059 despite low sequence similarity.


Pssm-ID: 437257 [Multi-domain]  Cd Length: 122  Bit Score: 47.40  E-value: 1.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538591192 131 SKNLASIFVKMFKGKVDFRKgLKKGDPIiMVYTQKYRLGKPFSMPEVHGAMVEINGKRVRVYRHSDGRFYDEKGGQYEKF 210
Cdd:pfam19425  27 TSNEISAVIKALQWQLDFRK-LKKGDKF-SVLMSREMLDGKREQSQLLGVRLRSGGKDYYAIRAEDGKFYDRNGSGLARG 104

                          90
                  ....*....|....*.
gi 2538591192 211 LFKLP-MRNPRITSRF 225
Cdd:pfam19425 105 FLRFPtAKQFRVSSNF 120
 
Name Accession Description Interval E-value
NlpD COG0739
Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell ...
 218-341 6.27e-52

Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440502 [Multi-domain]  Cd Length: 196  Bit Score: 172.08  E-value: 6.27e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538591192 218 NPRITSRFTkSRYHPVLHRYRAHLGVDFGARPGTPILSTGEGRVSFVGYSTGYGKTIKIRHNNGLTSLYAHQKAFKkgIH 297
Cdd:COG0739    76 KGRITSGFG-YRRHPVTGRRRFHKGIDIAAPTGTPVYAAADGTVVFAGWNGGYGNLVIIDHGNGYTTLYAHLSSIL--VK 152

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2538591192 298 TGMKVKQSEMIGYVGNTGLSSGPHLHFGMYRGSSAIDPLSVMKK 341
Cdd:COG0739   153 VGQRVKAGQVIGYVGNTGRSTGPHLHFEVRVNGKPVDPLPFLPA 196
PRK11649 PRK11649
putative peptidase; Provisional
 135-354 1.57e-38

putative peptidase; Provisional


Pssm-ID: 236946 [Multi-domain]  Cd Length: 439  Bit Score: 143.65  E-value: 1.57e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538591192 135 ASIFVKMFKGKVDFRKgLKKGDPIIMVYTQKYRLGKPfSMPEVHGAMVEINGKRVRVYRHSDGRFYDEKGGQYEKFLFKL 214
Cdd:PRK11649  209 ISAVIKALQWQMDFRK-LKKGDEFSVLMSREMLDGKS-EQSQLLGVRLRSGGKDYYAIRAEDGKFYDRNGSGLAKGFLRF 286

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538591192 215 P-MRNPRITSRFTKSRYHPVLHRYRAHLGVDFGARPGTPILSTGEGRVSFVGYSTGYGKTIKIRHNNGLTSLYAHQKafK 293
Cdd:PRK11649  287 PtAKQFRISSNFNPRRLNPVTGRVAPHRGVDFAMPVGTPVLAVGDGEVVVAKRSGAAGNYVAIRHGRQYTTRYMHLR--K 364

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2538591192 294 KGIHTGMKVKQSEMIGYVGNTGLSSGPHLHFGMYRGSSAIDPLSVMKKKTEGFTGKERRVF 354
Cdd:PRK11649  365 LLVKPGQKVKRGDRIALSGNTGRSTGPHLHYEVWINQQAVNPLTAKLPRTEGLTGKDRREY 425
Peptidase_M23 pfam01551
Peptidase family M23; Members of this family are zinc metallopeptidases with a range of ...
 240-335 2.20e-38

Peptidase family M23; Members of this family are zinc metallopeptidases with a range of specificities. The peptidase family M23 is included in this family, these are Gly-Gly endopeptidases. Peptidase family M23 are also endopeptidases. This family also includes some bacterial lipoproteins such as Swiss:P33648 for which no proteolytic activity has been demonstrated. This family also includes leukocyte cell-derived chemotaxin 2 (LECT2) proteins. LECT2 is a liver-specific protein which is thought to be linked to hepatocyte growth although the exact function of this protein is unknown.


Pssm-ID: 460250 [Multi-domain]  Cd Length: 96  Bit Score: 133.06  E-value: 2.20e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538591192 240 HLGVDFGARPGTPILSTGEGRVSFVGYSTGYGKTIKIRHNNGLTSLYAHQKAFKkgIHTGMKVKQSEMIGYVGNTGLSSG 319
Cdd:pfam01551   3 HKGIDIAAPTGTPVYAAADGVVVFAGWLGGYGNLVIIDHGNGYSTLYAHLSSIL--VKVGQRVKAGQVIGTVGSTGRSTG 80

                          90
                  ....*....|....*.
gi 2538591192 320 PHLHFGMYRGSSAIDP 335
Cdd:pfam01551  81 PHLHFEIRKNGKPVDP 96
M23_peptidase cd12797
M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; ...
 240-326 1.98e-33

M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; This model describes the metallopeptidase M23 family, which includes beta-lytic metallopeptidase and lysostaphin. Members of this family are zinc endopeptidases that lyse bacterial cell wall peptidoglycans; they cleave either the N-acylmuramoyl-Ala bond between the cell wall peptidoglycan and the cross-linking peptide (e.g. beta-lytic endopeptidase) or a bond within the cross-linking peptide (e.g. stapholysin, and lysostaphin). Beta-lytic metallopeptidase, formerly known as beta-lytic protease, has a preference for cleavage of Gly-X bonds and favors hydrophobic or apolar residues on either side. It inhibits growth of sensitive organisms and may potentially serve as an antimicrobial agent. Lysostaphin, produced by Staphylococcus genus, cleaves pentaglycine cross-bridges of cell wall peptidoglycan, acting as autolysins to maintain cell wall metabolism or as toxins and weapons against competing strains. Staphylolysin (also known as LasA) is implicated in a range of processes related to Pseudomonas virulence, including stimulating shedding of the ectodomain of cell surface heparan sulphate proteoglycan syndecan-1, and elastin degradation in connective tissue. Its active site is less constricted and contains a five-coordinate zinc ion with trigonal bipyramidal geometry and two metal-bound water molecules, possibly contributing to its activity against a wider range of substrates than those used by related lytic enzymes, consistent with its multiple roles in Pseudomonas virulence. The family includes members that do not appear to have the conserved zinc-binding site and might be lipoproteins lacking proteolytic activity.


Pssm-ID: 410984 [Multi-domain]  Cd Length: 85  Bit Score: 120.00  E-value: 1.98e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538591192 240 HLGVDFGARPGTPILSTGEGRVSFVGYSTGYGKTIKIRHNNGLTSLYAHQKAFKkgIHTGMKVKQSEMIGYVGNTGLSSG 319
Cdd:cd12797     1 HNGIDIAAPEGTPVYAAADGTVVFAGWDGGYGNYVIIDHGNGYYTLYAHLSSIL--VKVGQRVKKGQVIGTVGNTGRSTG 78


                  ....*..
gi 2538591192 320 PHLHFGM 326
Cdd:cd12797    79 PHLHFEI 85
SpoIIQ2 COG5821
Stage II sporulation protein SpoIIQ, clostridial version, metallopeptidase M23 family [Cell ...
 201-341 1.18e-32

Stage II sporulation protein SpoIIQ, clostridial version, metallopeptidase M23 family [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444523 [Multi-domain]  Cd Length: 200  Bit Score: 121.67  E-value: 1.18e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538591192 201 DEKGGQYEKFLFKLPMrNPRITSRF-TKSRYHPVLHRYRAHLGVDFGARPGTPILSTGEGRVSFVGYSTGYGKTIKIRHN 279
Cdd:COG5821    58 KSKVTASTSNKFLKPV-SGKITREFgEDLVYSKTLNEWRTHTGIDIAAKEGTPVKAAADGVVVEVGKDPKYGITVVIDHG 136

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2538591192 280 NGLTSLYAHQKAfKKGIHTGMKVKQSEMIGYVGNTGL---SSGPHLHFGMYRGSSAIDPLSVMKK 341
Cdd:COG5821   137 NGIKTVYANLDS-KIKVKVGQKVKKGQVIGKVGSTALfesSEGPHLHFEVLKNGKPVDPMKYLKK 200
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 220-342 2.84e-29

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 116.79  E-value: 2.84e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538591192 220 RITSRFTKSRYHPVLHRyrahlGVDFGARPGTPILSTGEGRVSFVGYSTGYGKTIKIRHNNGLTSLYAH-QKAFKKgihT 298
Cdd:COG4942   262 RVVRRFGERDGGGGRNK-----GIDIAAPPGAPVRAVADGTVVYAGWLRGYGNLVIIDHGGGYLTLYAHlSSLLVK---V 333

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2538591192 299 GMKVKQSEMIGYVGNTGLSSGPHLHFGMYRGSSAIDPLSVMKKK 342
Cdd:COG4942   334 GQRVKAGQPIGTVGSSGGQGGPTLYFELRKNGKPVDPLPWLAKR 377
Csd3_N pfam18059
Csd3 N-terminal; Csd3 (also known as HdpA) is a bi-functional enzyme with delta, ...
 22-104 3.10e-20

Csd3 N-terminal; Csd3 (also known as HdpA) is a bi-functional enzyme with delta,delta-endopeptidase activity and delta,delta-carboxypeptidase activity. The N-terminal domain is also known as domain 1 and is composed of an alpha/beta fold consisting of a five-stranded antiparallel beta-sheet and three short alpha-helices. Domain 1 blocks the active-site cleft of the LytM domain, with the protruding helix alpha-3 contributing to the Zn2+ coordination sphere. The fold of domain 1 is very remotely related to monellin/cystatin superfamily proteins, some of which act as inhibitors of cysteine peptidases.


Pssm-ID: 436243  Cd Length: 83  Bit Score: 84.30  E-value: 3.10e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538591192  22 FKWKDGESFLTFLERKKLPLRVYYNLDKEDQKLTEDIPYTAKCQMVVDNQNFIHQILIPVNDELQLQIYlTPKRRYETKV 101
Cdd:pfam18059   2 FVWEKGETLLGFLQKNNIPAKLYYNLDPEDKELTSEIRAGVTYYELRDDDGTLLQALIPVGEELQIHIF-KDKGQYRFDI 80


                  ...
gi 2538591192 102 IPI 104
Cdd:pfam18059  81 IPI 83
SpoIVFA COG5833
Stage IV sporulation protein SpoIVFA, regulates SpoIVFB [Cell cycle control, cell division, ...
 199-340 3.32e-14

Stage IV sporulation protein SpoIVFA, regulates SpoIVFB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444535 [Multi-domain]  Cd Length: 219  Bit Score: 71.18  E-value: 3.32e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538591192 199 FYDEKGGQYEKFLFKLPMrNPRITSRFTKSryhpvlhryraHLGVDFGARPGTPILSTGEGRVSFVGYSTGYGKTIKIRH 278
Cdd:COG5833    91 FGKEEETVEQGEAFALPV-SGKVVESFQEN-----------GKGVDIETPGGANVKAVKEGYVIFAGKDEETGKTVIIQH 158

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2538591192 279 NNGLTSLYAHQKAFKkgIHTGMKVKQSEMIGYVGNTgLSSGPHLHFGMYRGSSAIDPLSVMK 340
Cdd:COG5833   159 ADGSESWYGNLSSID--VKLYDFVEAGQKIGTVPAT-EGEEGTFYFAIKKGGKFIDPIQVIS 217
nlpD PRK10871
murein hydrolase activator NlpD;
242-336 5.26e-10

murein hydrolase activator NlpD;


Pssm-ID: 236782 [Multi-domain]  Cd Length: 319  Bit Score: 60.23  E-value: 5.26e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538591192 242 GVDFGARPGTPILSTGEGRVSFVGYS-TGYGKTIKIRHNNGLTSLYAHQKAFKkgIHTGMKVKQSEMIGYVGNTGLSSgP 320
Cdd:PRK10871  221 GIDIAGSKGQAIIATADGRVVYAGNAlRGYGNLIIIKHNDDYLSAYAHNDTML--VREQQEVKAGQKIATMGSTGTSS-T 297

                          90
                  ....*....|....*..
gi 2538591192 321 HLHFGM-YRGSSaIDPL 336
Cdd:PRK10871  298 RLHFEIrYKGKS-VNPL 313
PRK11637 PRK11637
AmiB activator; Provisional
 232-336 9.01e-08

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 53.93  E-value: 9.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538591192 232 PVLHRYRAHL-------GVDFGARPGTPILSTGEGRVSFVGYSTGYGKTIKIRHNNGLTSLYAH-QKAFkkgIHTGMKVK 303
Cdd:PRK11637  314 PTLHRFGEQLqgelrwkGMVIGASEGTEVKAIADGRVLLADWLQGYGLVVVVEHGKGDMSLYGYnQSAL---VSVGAQVR 390

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2538591192 304 QSEMIGYVGNTGLSSGPHLHFGMYRGSSAIDPL 336
Cdd:PRK11637  391 AGQPIALVGSSGGQGRPSLYFEIRRQGQAVNPQ 423
Csd3_N2 pfam19425
Csd3 second domain; This entry represents the second domain from the Csd3 peptidase. This ...
 131-225 1.01e-06

Csd3 second domain; This entry represents the second domain from the Csd3 peptidase. This domain has a similar structure to pfam18059 despite low sequence similarity.


Pssm-ID: 437257 [Multi-domain]  Cd Length: 122  Bit Score: 47.40  E-value: 1.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538591192 131 SKNLASIFVKMFKGKVDFRKgLKKGDPIiMVYTQKYRLGKPFSMPEVHGAMVEINGKRVRVYRHSDGRFYDEKGGQYEKF 210
Cdd:pfam19425  27 TSNEISAVIKALQWQLDFRK-LKKGDKF-SVLMSREMLDGKREQSQLLGVRLRSGGKDYYAIRAEDGKFYDRNGSGLARG 104

                          90
                  ....*....|....*.
gi 2538591192 211 LFKLP-MRNPRITSRF 225
Cdd:pfam19425 105 FLRFPtAKQFRVSSNF 120
PRK06148 PRK06148
hypothetical protein; Provisional
 222-326 1.38e-06

hypothetical protein; Provisional


Pssm-ID: 180426 [Multi-domain]  Cd Length: 1013  Bit Score: 50.41  E-value: 1.38e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538591192  222 TSRFTKSRyhpvlhRYRAHLGVDFGARPGTPILSTGEGRVSFVGYST---GYGKTIKIRHNNG-----LTsLYAH-QKAF 292
Cdd:PRK06148   429 TSRFIEGE------RRTVHLGVDLFAPAGTPVYAPLAGTVRSVEIEAvplGYGGLVALEHETPggdpfYT-LYGHlAHEA 501

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2538591192  293 KKGIHTGMKVKQSEMIGYVGNTGLSSG--PHLHFGM 326
Cdd:PRK06148   502 VSRLKPGDRLAAGELFGAMGDAHENGGwaPHLHFQL 537
 
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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