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Conserved domains on  [gi|1581859898|gb|TAW43253|]
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LysM peptidoglycan-binding domain-containing protein [Rhizobium leguminosarum]

Protein Classification

M23 family metallopeptidase( domain architecture ID 11432770)

M23 family metallopeptidase lyses bacterial cell wall peptidoglycans

EC:  3.4.24.-
Gene Ontology:  GO:0046872|GO:0008237
MEROPS:  M23
PubMed:  36386627

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 394-533 1.17e-43

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: 159.16  E-value: 1.17e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859898 394 DAEKKSDVSSAAPESTGIGKYRWPVRGQVIASYGANVNGS-RNDGIDISVPQGTPIKAAENGVVIYAGnGLKELGNTVLV 472
Cdd:COG4942   235 EAAAAAERTPAAGFAALKGKLPWPVSGRVVRRFGERDGGGgRNKGIDIAAPPGAPVRAVADGTVVYAG-WLRGYGNLVII 313

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1581859898 473 RHDDGTVTVYGNADTLSVTRGQKIQRGQTVAVSGMSGDVKQPQVHFEVRKDASPVNPMTFL 533
Cdd:COG4942   314 DHGGGYLTLYAHLSSLLVKVGQRVKAGQPIGTVGSSGGQGGPTLYFELRKNGKPVDPLPWL 374
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
204-347 1.69e-15

LysM repeat [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 73.97  E-value: 1.69e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859898 204 GVPEKEILRVNALKTASAAQPGQAILIPTFNGGNAAKAASQAADLSKPGKMPEAPKAPEQNVAVVPGANSARDKTLASAD 283
Cdd:COG1388    13 LAAVLTLLAALLLLAAALAAVALLLLAALAPAGLSLAAALNGEALLLLLPAAAAAAKAALAAAPEAAAAAAARYTVKSGD 92

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1581859898 284 VTGKLPTGAGKDPKAPAGTYVVKQGDSLAKIAKATGSNVDDLKAANNLSASSLRIGQALKIPNG 347
Cdd:COG1388    93 TLSGIARRYGAAAAPSPVTYTVKKGDTLWSIARRYGVSVEELKRWNGLSSDTIRPGQKLKIPAS 156
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
88-232 9.42e-07

LysM repeat [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 48.94  E-value: 9.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859898  88 ALNQPYPARQGYDPTRTSSSSARLASAPVSVQRSELAAPSAVAPSRQREKEVALAQPFPTAPQAERPRLVAPTAPKMTPD 167
Cdd:COG1388    12 LLAAVLTLLAALLLLAAALAAVALLLLAALAPAGLSLAAALNGEALLLLLPAAAAAAKAALAAAPEAAAAAAARYTVKSG 91

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1581859898 168 TLTTGATPKVSGWSATNAPSVTLRPGESIATLSRRFGVPEKEILRVNALKTaSAAQPGQAILIPT 232
Cdd:COG1388    92 DTLSGIARRYGAAAAPSPVTYTVKKGDTLWSIARRYGVSVEELKRWNGLSS-DTIRPGQKLKIPA 155
 
Name Accession Description Interval E-value
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 394-533 1.17e-43

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: 159.16  E-value: 1.17e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859898 394 DAEKKSDVSSAAPESTGIGKYRWPVRGQVIASYGANVNGS-RNDGIDISVPQGTPIKAAENGVVIYAGnGLKELGNTVLV 472
Cdd:COG4942   235 EAAAAAERTPAAGFAALKGKLPWPVSGRVVRRFGERDGGGgRNKGIDIAAPPGAPVRAVADGTVVYAG-WLRGYGNLVII 313

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1581859898 473 RHDDGTVTVYGNADTLSVTRGQKIQRGQTVAVSGMSGDVKQPQVHFEVRKDASPVNPMTFL 533
Cdd:COG4942   314 DHGGGYLTLYAHLSSLLVKVGQRVKAGQPIGTVGSSGGQGGPTLYFELRKNGKPVDPLPWL 374
Peptidase_M23 pfam01551
Peptidase family M23; Members of this family are zinc metallopeptidases with a range of ...
 433-529 5.45e-33

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: 121.11  E-value: 5.45e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859898 433 SRNDGIDISVPQGTPIKAAENGVVIYAGNgLKELGNTVLVRHDDGTVTVYGNADTLSVTRGQKIQRGQTVAVSGMSGDVK 512
Cdd:pfam01551   1 RFHKGIDIAAPTGTPVYAAADGVVVFAGW-LGGYGNLVIIDHGNGYSTLYAHLSSILVKVGQRVKAGQVIGTVGSTGRST 79

                          90
                  ....*....|....*..
gi 1581859898 513 QPQVHFEVRKDASPVNP 529
Cdd:pfam01551  80 GPHLHFEIRKNGKPVDP 96
nlpD PRK10871
murein hydrolase activator NlpD;
302-533 1.89e-30

murein hydrolase activator NlpD;


Pssm-ID: 236782 [Multi-domain]  Cd Length: 319  Bit Score: 121.10  E-value: 1.89e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859898 302 TYVVKQGDSLAKIAKATGSNVDDLKAANNLSAS-SLRIGQALKIPNGTADNIK--------------TASIPAEK----V 362
Cdd:PRK10871   62 TYTVKKGDTLFYIAWITGNDFRDLAQRNNIQAPySLNVGQTLQVGNASGTPITggnaitqadaaeqgVVIKPAQNstvaV 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859898 363 D--PKPTQPAAAQQTASAQPAPYKAPAATQ-----TVDDAEKKSDVSSAAPESTGIGKYRWPVRGQVIASYGANVNGsrN 435
Cdd:PRK10871  142 AsqPTITYSESSGEQSANKMLPNNKPAATTvtapvTAPTASTTEPTASSTSTSTPISTWRWPTDGKVIENFSASEGG--N 219

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859898 436 DGIDISVPQGTPIKAAENGVVIYAGNGLKELGNTVLVRHDDGTVTVYGNADTLSVTRGQKIQRGQTVAVSGMSGdVKQPQ 515
Cdd:PRK10871  220 KGIDIAGSKGQAIIATADGRVVYAGNALRGYGNLIIIKHNDDYLSAYAHNDTMLVREQQEVKAGQKIATMGSTG-TSSTR 298

                         250
                  ....*....|....*...
gi 1581859898 516 VHFEVRKDASPVNPMTFL 533
Cdd:PRK10871  299 LHFEIRYKGKSVNPLRYL 316
M23_peptidase cd12797
M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; ...
 435-520 2.75e-28

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: 107.68  E-value: 2.75e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859898 435 NDGIDISVPQGTPIKAAENGVVIYAGNGlKELGNTVLVRHDDGTVTVYGNADTLSVTRGQKIQRGQTVAVSGMSGDVKQP 514
Cdd:cd12797     1 HNGIDIAAPEGTPVYAAADGTVVFAGWD-GGYGNYVIIDHGNGYYTLYAHLSSILVKVGQRVKKGQVIGTVGNTGRSTGP 79


                  ....*.
gi 1581859898 515 QVHFEV 520
Cdd:cd12797    80 HLHFEI 85
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
204-347 1.69e-15

LysM repeat [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 73.97  E-value: 1.69e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859898 204 GVPEKEILRVNALKTASAAQPGQAILIPTFNGGNAAKAASQAADLSKPGKMPEAPKAPEQNVAVVPGANSARDKTLASAD 283
Cdd:COG1388    13 LAAVLTLLAALLLLAAALAAVALLLLAALAPAGLSLAAALNGEALLLLLPAAAAAAKAALAAAPEAAAAAAARYTVKSGD 92

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1581859898 284 VTGKLPTGAGKDPKAPAGTYVVKQGDSLAKIAKATGSNVDDLKAANNLSASSLRIGQALKIPNG 347
Cdd:COG1388    93 TLSGIARRYGAAAAPSPVTYTVKKGDTLWSIARRYGVSVEELKRWNGLSSDTIRPGQKLKIPAS 156
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 303-345 1.51e-13

LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. The structure of this domain is known.


Pssm-ID: 396179 [Multi-domain]  Cd Length: 43  Bit Score: 64.72  E-value: 1.51e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1581859898 303 YVVKQGDSLAKIAKATGSNVDDLKAANNLSASSLRIGQALKIP 345
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSPNLYVGQKLKIP 43
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 257-356 1.48e-11

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 66.68  E-value: 1.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859898 257 APKAPEqnVAVVPGANSARDKT-LASADVTGKLPTGAGKDPKAPAGTYVVKQGDSLAKIAKATGSNVDDLKAANNLSASS 335
Cdd:PRK10783  301 APSGPH--YIMVPKKHADQLREsLASGEIAAVQSTLVADNTPLNSRSYKVRSGDTLSGIASRLNVSTKDLQQWNNLRGSK 378

                          90       100
                  ....*....|....*....|.
gi 1581859898 336 LRIGQALKIPNGTADNIKTAS 356
Cdd:PRK10783  379 LKVGQTLTIGAGSSAQRLANN 399
LysM smart00257
Lysin motif;
302-344 7.46e-11

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 57.07  E-value: 7.46e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1581859898  302 TYVVKQGDSLAKIAKATGSNVDDLKAANN-LSASSLRIGQALKI 344
Cdd:smart00257   1 TYTVKKGDTLSSIARRYGISVSDLLELNNiLDPDNLQVGQKLKI 44
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 302-344 7.87e-11

Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.


Pssm-ID: 212030 [Multi-domain]  Cd Length: 45  Bit Score: 57.11  E-value: 7.87e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1581859898 302 TYVVKQGDSLAKIAKATGSNVDDLKAANNL-SASSLRIGQALKI 344
Cdd:cd00118     2 TYTVKPGDTLWSIAKKYGVTVEELAAANPLiNPDCIYPGQKLKI 45
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
88-232 9.42e-07

LysM repeat [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 48.94  E-value: 9.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859898  88 ALNQPYPARQGYDPTRTSSSSARLASAPVSVQRSELAAPSAVAPSRQREKEVALAQPFPTAPQAERPRLVAPTAPKMTPD 167
Cdd:COG1388    12 LLAAVLTLLAALLLLAAALAAVALLLLAALAPAGLSLAAALNGEALLLLLPAAAAAAKAALAAAPEAAAAAAARYTVKSG 91

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1581859898 168 TLTTGATPKVSGWSATNAPSVTLRPGESIATLSRRFGVPEKEILRVNALKTaSAAQPGQAILIPT 232
Cdd:COG1388    92 DTLSGIARRYGAAAAPSPVTYTVKKGDTLWSIARRYGVSVEELKRWNGLSS-DTIRPGQKLKIPA 155
 
Name Accession Description Interval E-value
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 394-533 1.17e-43

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: 159.16  E-value: 1.17e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859898 394 DAEKKSDVSSAAPESTGIGKYRWPVRGQVIASYGANVNGS-RNDGIDISVPQGTPIKAAENGVVIYAGnGLKELGNTVLV 472
Cdd:COG4942   235 EAAAAAERTPAAGFAALKGKLPWPVSGRVVRRFGERDGGGgRNKGIDIAAPPGAPVRAVADGTVVYAG-WLRGYGNLVII 313

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1581859898 473 RHDDGTVTVYGNADTLSVTRGQKIQRGQTVAVSGMSGDVKQPQVHFEVRKDASPVNPMTFL 533
Cdd:COG4942   314 DHGGGYLTLYAHLSSLLVKVGQRVKAGQPIGTVGSSGGQGGPTLYFELRKNGKPVDPLPWL 374
NlpD COG0739
Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell ...
 385-533 2.14e-40

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: 144.73  E-value: 2.14e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859898 385 APAATQTVDDAEKKSDVSSAAPESTGIGKYRWPVRGQVIASYGANVN-----GSRNDGIDISVPQGTPIKAAENGVVIYA 459
Cdd:COG0739    42 AAALAAAVSAAASAAAAAAAAAAAIALGSGAWPVKGRITSGFGYRRHpvtgrRRFHKGIDIAAPTGTPVYAAADGTVVFA 121

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1581859898 460 GNGlKELGNTVLVRHDDGTVTVYGNADTLSVTRGQKIQRGQTVAVSGMSGDVKQPQVHFEVRKDASPVNPMTFL 533
Cdd:COG0739   122 GWN-GGYGNLVIIDHGNGYTTLYAHLSSILVKVGQRVKAGQVIGYVGNTGRSTGPHLHFEVRVNGKPVDPLPFL 194
Peptidase_M23 pfam01551
Peptidase family M23; Members of this family are zinc metallopeptidases with a range of ...
 433-529 5.45e-33

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: 121.11  E-value: 5.45e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859898 433 SRNDGIDISVPQGTPIKAAENGVVIYAGNgLKELGNTVLVRHDDGTVTVYGNADTLSVTRGQKIQRGQTVAVSGMSGDVK 512
Cdd:pfam01551   1 RFHKGIDIAAPTGTPVYAAADGVVVFAGW-LGGYGNLVIIDHGNGYSTLYAHLSSILVKVGQRVKAGQVIGTVGSTGRST 79

                          90
                  ....*....|....*..
gi 1581859898 513 QPQVHFEVRKDASPVNP 529
Cdd:pfam01551  80 GPHLHFEIRKNGKPVDP 96
SpoIIQ2 COG5821
Stage II sporulation protein SpoIIQ, clostridial version, metallopeptidase M23 family [Cell ...
 384-534 8.43e-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: 121.29  E-value: 8.43e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859898 384 KAPAATQTVDDAEKKSdvSSAAPESTGIGKYRWPVRGQVIASYGANVNGSR-------NDGIDISVPQGTPIKAAENGVV 456
Cdd:COG5821    41 KLEEETVKNKSESNEK--SKSKVTASTSNKFLKPVSGKITREFGEDLVYSKtlnewrtHTGIDIAAKEGTPVKAAADGVV 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859898 457 IYAGNGlKELGNTVLVRHDDGTVTVYGNADT-LSVTRGQKIQRGQTVAVSGMSGDVK---QPQVHFEVRKDASPVNPMTF 532
Cdd:COG5821   119 VEVGKD-PKYGITVVIDHGNGIKTVYANLDSkIKVKVGQKVKKGQVIGKVGSTALFEsseGPHLHFEVLKNGKPVDPMKY 197


                  ..
gi 1581859898 533 LE 534
Cdd:COG5821   198 LK 199
nlpD PRK10871
murein hydrolase activator NlpD;
302-533 1.89e-30

murein hydrolase activator NlpD;


Pssm-ID: 236782 [Multi-domain]  Cd Length: 319  Bit Score: 121.10  E-value: 1.89e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859898 302 TYVVKQGDSLAKIAKATGSNVDDLKAANNLSAS-SLRIGQALKIPNGTADNIK--------------TASIPAEK----V 362
Cdd:PRK10871   62 TYTVKKGDTLFYIAWITGNDFRDLAQRNNIQAPySLNVGQTLQVGNASGTPITggnaitqadaaeqgVVIKPAQNstvaV 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859898 363 D--PKPTQPAAAQQTASAQPAPYKAPAATQ-----TVDDAEKKSDVSSAAPESTGIGKYRWPVRGQVIASYGANVNGsrN 435
Cdd:PRK10871  142 AsqPTITYSESSGEQSANKMLPNNKPAATTvtapvTAPTASTTEPTASSTSTSTPISTWRWPTDGKVIENFSASEGG--N 219

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859898 436 DGIDISVPQGTPIKAAENGVVIYAGNGLKELGNTVLVRHDDGTVTVYGNADTLSVTRGQKIQRGQTVAVSGMSGdVKQPQ 515
Cdd:PRK10871  220 KGIDIAGSKGQAIIATADGRVVYAGNALRGYGNLIIIKHNDDYLSAYAHNDTMLVREQQEVKAGQKIATMGSTG-TSSTR 298

                         250
                  ....*....|....*...
gi 1581859898 516 VHFEVRKDASPVNPMTFL 533
Cdd:PRK10871  299 LHFEIRYKGKSVNPLRYL 316
M23_peptidase cd12797
M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; ...
 435-520 2.75e-28

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: 107.68  E-value: 2.75e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859898 435 NDGIDISVPQGTPIKAAENGVVIYAGNGlKELGNTVLVRHDDGTVTVYGNADTLSVTRGQKIQRGQTVAVSGMSGDVKQP 514
Cdd:cd12797     1 HNGIDIAAPEGTPVYAAADGTVVFAGWD-GGYGNYVIIDHGNGYYTLYAHLSSILVKVGQRVKKGQVIGTVGNTGRSTGP 79


                  ....*.
gi 1581859898 515 QVHFEV 520
Cdd:cd12797    80 HLHFEI 85
SpoIVFA COG5833
Stage IV sporulation protein SpoIVFA, regulates SpoIVFB [Cell cycle control, cell division, ...
 384-529 2.12e-21

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


Pssm-ID: 444535 [Multi-domain]  Cd Length: 219  Bit Score: 92.75  E-value: 2.12e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859898 384 KAPAATQTVDDAEKKSDVSSAapestgigkYRWPVRGQVIASYGanVNGSrndGIDISVPQGTPIKAAENGVVIYAGNGl 463
Cdd:COG5833    83 GPLAFLPPFGKEEETVEQGEA---------FALPVSGKVVESFQ--ENGK---GVDIETPGGANVKAVKEGYVIFAGKD- 147

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1581859898 464 KELGNTVLVRHDDGTVTVYGNADTLSVTRGQKIQRGQTVAVSGmSGDVKQPQVHFEVRKDASPVNP 529
Cdd:COG5833   148 EETGKTVIIQHADGSESWYGNLSSIDVKLYDFVEAGQKIGTVP-ATEGEEGTFYFAIKKGGKFIDP 212
PRK11637 PRK11637
AmiB activator; Provisional
 412-533 1.53e-17

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 84.74  E-value: 1.53e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859898 412 GKYRWPVRGQVIASYGANVNGS-RNDGIDISVPQGTPIKAAENGVVIYAgNGLKELGNTVLVRHDDGTVTVYG-NADTLs 489
Cdd:PRK11637  305 GQAFWPVRGPTLHRFGEQLQGElRWKGMVIGASEGTEVKAIADGRVLLA-DWLQGYGLVVVVEHGKGDMSLYGyNQSAL- 382

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1581859898 490 VTRGQKIQRGQTVAVSGMSGDVKQPQVHFEVRKDASPVNPMTFL 533
Cdd:PRK11637  383 VSVGAQVRAGQPIALVGSSGGQGRPSLYFEIRRQGQAVNPQPWL 426
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
204-347 1.69e-15

LysM repeat [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 73.97  E-value: 1.69e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859898 204 GVPEKEILRVNALKTASAAQPGQAILIPTFNGGNAAKAASQAADLSKPGKMPEAPKAPEQNVAVVPGANSARDKTLASAD 283
Cdd:COG1388    13 LAAVLTLLAALLLLAAALAAVALLLLAALAPAGLSLAAALNGEALLLLLPAAAAAAKAALAAAPEAAAAAAARYTVKSGD 92

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1581859898 284 VTGKLPTGAGKDPKAPAGTYVVKQGDSLAKIAKATGSNVDDLKAANNLSASSLRIGQALKIPNG 347
Cdd:COG1388    93 TLSGIARRYGAAAAPSPVTYTVKKGDTLWSIARRYGVSVEELKRWNGLSSDTIRPGQKLKIPAS 156
PRK11649 PRK11649
putative peptidase; Provisional
 437-531 8.58e-14

putative peptidase; Provisional


Pssm-ID: 236946 [Multi-domain]  Cd Length: 439  Bit Score: 73.55  E-value: 8.58e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859898 437 GIDISVPQGTPIKAAENGVVIYAGNGlKELGNTVLVRHDDGTVTVYGNADTLSVTRGQKIQRGQTVAVSGMSGDVKQPQV 516
Cdd:PRK11649  315 GVDFAMPVGTPVLAVGDGEVVVAKRS-GAAGNYVAIRHGRQYTTRYMHLRKLLVKPGQKVKRGDRIALSGNTGRSTGPHL 393

                          90
                  ....*....|....*
gi 1581859898 517 HFEVRKDASPVNPMT 531
Cdd:PRK11649  394 HYEVWINQQAVNPLT 408
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 303-345 1.51e-13

LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. The structure of this domain is known.


Pssm-ID: 396179 [Multi-domain]  Cd Length: 43  Bit Score: 64.72  E-value: 1.51e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1581859898 303 YVVKQGDSLAKIAKATGSNVDDLKAANNLSASSLRIGQALKIP 345
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSPNLYVGQKLKIP 43
SpoIIQ COG5820
Stage II sporulation protein SpoIIQ, required for engulfement [Cell cycle control, cell ...
 435-533 2.04e-12

Stage II sporulation protein SpoIIQ, required for engulfement [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444522 [Multi-domain]  Cd Length: 224  Bit Score: 66.87  E-value: 2.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859898 435 NDGIDISVPQGTP--IKAAENGVVIYAgnglKE---LGNTVLVRHDDGTVTVYGNADTLSVTRGQKIQRGQTVAVSGMS- 508
Cdd:COG5820   120 STGIDIAAKDGESfdVLAALSGTVTEV----EEdplLGYVVEIKHDNGVSTVYQSLSDVKVKAGDEVKQGQVIGTAGRNl 195

                          90       100
                  ....*....|....*....|....*.
gi 1581859898 509 -GDVKQPQVHFEVRKDASPVNPMTFL 533
Cdd:COG5820   196 fNKDAGVHLHFEVRKDGKAVNPESYL 221
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 257-356 1.48e-11

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 66.68  E-value: 1.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859898 257 APKAPEqnVAVVPGANSARDKT-LASADVTGKLPTGAGKDPKAPAGTYVVKQGDSLAKIAKATGSNVDDLKAANNLSASS 335
Cdd:PRK10783  301 APSGPH--YIMVPKKHADQLREsLASGEIAAVQSTLVADNTPLNSRSYKVRSGDTLSGIASRLNVSTKDLQQWNNLRGSK 378

                          90       100
                  ....*....|....*....|.
gi 1581859898 336 LRIGQALKIPNGTADNIKTAS 356
Cdd:PRK10783  379 LKVGQTLTIGAGSSAQRLANN 399
LysM smart00257
Lysin motif;
302-344 7.46e-11

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 57.07  E-value: 7.46e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1581859898  302 TYVVKQGDSLAKIAKATGSNVDDLKAANN-LSASSLRIGQALKI 344
Cdd:smart00257   1 TYTVKKGDTLSSIARRYGISVSDLLELNNiLDPDNLQVGQKLKI 44
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 302-344 7.87e-11

Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.


Pssm-ID: 212030 [Multi-domain]  Cd Length: 45  Bit Score: 57.11  E-value: 7.87e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1581859898 302 TYVVKQGDSLAKIAKATGSNVDDLKAANNL-SASSLRIGQALKI 344
Cdd:cd00118     2 TYTVKPGDTLWSIAKKYGVTVEELAAANPLiNPDCIYPGQKLKI 45
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
261-359 5.29e-07

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 52.39  E-value: 5.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859898 261 PEQNVAVVPGANSARDKTLASADVTGKLPTgagKDPKAPAGTYVVKQGDSLAKIAKATGSNVDDLKAANNLSASSLRIGQ 340
Cdd:PRK06347  443 PGQKLKVSAGSTSNTNTSKPSTNTNTSKPS---TNTNTNAKVYTVAKGDSLWRIANNNKVTIANLKSWNNLKSDFIYPGQ 519

                          90
                  ....*....|....*....
gi 1581859898 341 ALKIPNGTADNIKTASIPA 359
Cdd:PRK06347  520 KLKVSAGSTTNNTNTAKPS 538
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
88-232 9.42e-07

LysM repeat [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 48.94  E-value: 9.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859898  88 ALNQPYPARQGYDPTRTSSSSARLASAPVSVQRSELAAPSAVAPSRQREKEVALAQPFPTAPQAERPRLVAPTAPKMTPD 167
Cdd:COG1388    12 LLAAVLTLLAALLLLAAALAAVALLLLAALAPAGLSLAAALNGEALLLLLPAAAAAAKAALAAAPEAAAAAAARYTVKSG 91

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1581859898 168 TLTTGATPKVSGWSATNAPSVTLRPGESIATLSRRFGVPEKEILRVNALKTaSAAQPGQAILIPT 232
Cdd:COG1388    92 DTLSGIARRYGAAAAPSPVTYTVKKGDTLWSIARRYGVSVEELKRWNGLSS-DTIRPGQKLKIPA 155
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
261-355 4.01e-06

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 49.69  E-value: 4.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859898 261 PEQNVAVVPGANSARDKTlaSADVTGKLPTGAGKDPKAPAGTYVVKQGDSLAKIAKATGSNVDDLKAANNLSASSLRIGQ 340
Cdd:PRK06347  368 PGQKLKVSAGSTTSDTNT--SKPSTGTSTSKPSTGTSTNAKVYTVVKGDSLWRIANNNKVTIANLKSWNNLKSDFIYPGQ 445

                          90
                  ....*....|....*
gi 1581859898 341 ALKIPNGTADNIKTA 355
Cdd:PRK06347  446 KLKVSAGSTSNTNTS 460
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 181-342 6.69e-06

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 48.58  E-value: 6.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859898 181 SATNAPSVTLRPGESIATLSRRFGVPEKEILRVNALKTaSAAQPGQAIliptfnggnaakaasqaadlskpgkmpeapka 260
Cdd:PRK10783  339 TPLNSRSYKVRSGDTLSGIASRLNVSTKDLQQWNNLRG-SKLKVGQTL-------------------------------- 385

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859898 261 peqnvavvpgansardkTLASADVTGKLPTGAGkdpkapAGTYVVKQGDSLAKIAKATGSNVDDLKAANNLSASSLRIGQ 340
Cdd:PRK10783  386 -----------------TIGAGSSAQRLANNSD------SITYRVRKGDSLSSIAKRHGVNIKDVMRWNSDTAKNLQPGD 442


                  ..
gi 1581859898 341 AL 342
Cdd:PRK10783  443 KL 444
PRK13914 PRK13914
invasion associated endopeptidase;
124-359 9.22e-06

invasion associated endopeptidase;


Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 48.26  E-value: 9.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859898 124 AAPSAVAPSRQREKEVALAQpfpTAPQAERPRLVAPTAPKMT--PDTLTTGATPKVSgwsaTNAPSVTLRPGESIATLSR 201
Cdd:PRK13914  143 VTSTPVAPTQEVKKETTTQQ---AAPAAETKTEVKQTTQATTpaPKVAETKETPVVD----QNATTHAVKSGDTIWALSV 215

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859898 202 RFGVPEKEILRVNALKTASaaqpgqailipTFNGGNAAKAASQAADLSKPGKMPEAPKAPEQNVAVV------PGANSAR 275
Cdd:PRK13914  216 KYGVSVQDIMSWNNLSSSS-----------IYVGQKLAIKQTANTATPKAEVKTEAPAAEKQAAPVVkentntNTATTEK 284

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859898 276 DKTLASADVTGKLPTGAGKDPKAPAGTYVVKQGDSLAKIAKATGSNVDDLKAANNLSASSLRIGQALKIPNGTADNIKTA 355
Cdd:PRK13914  285 KETTTQQQTAPKAPTEAAKPAPAPSTNTNANKTNTNTNTNTNNTNTSTPSKNTNTNTNSNTNTNSNTNANQGSSNNNSNS 364


                  ....
gi 1581859898 356 SIPA 359
Cdd:PRK13914  365 SASA 368
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 188-231 1.70e-05

LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. The structure of this domain is known.


Pssm-ID: 396179 [Multi-domain]  Cd Length: 43  Bit Score: 42.00  E-value: 1.70e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1581859898 188 VTLRPGESIATLSRRFGVPEKEILRVNALKTaSAAQPGQAILIP 231
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSS-PNLYVGQKLKIP 43
LysM smart00257
Lysin motif;
189-230 4.95e-05

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 40.51  E-value: 4.95e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1581859898  189 TLRPGESIATLSRRFGVPEKEILRVNALKTASAAQPGQAILI 230
Cdd:smart00257   3 TVKKGDTLSSIARRYGISVSDLLELNNILDPDNLQVGQKLKI 44
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
271-344 2.91e-04

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 43.53  E-value: 2.91e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1581859898 271 ANSARDKTLASADVTGKLPTGAGKdpkapagTYVVKQGDSLAKIAKATGSNVDDLKAANNLSASSLRIGQALKI 344
Cdd:PRK06347  525 AGSTTNNTNTAKPSTNKPSNSTVK-------TYTVKKGDSLWAISRQYKTTVDNIKAWNKLTSNMIHVGQKLTI 591
PRK13914 PRK13914
invasion associated endopeptidase;
298-344 3.86e-04

invasion associated endopeptidase;


Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 43.25  E-value: 3.86e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1581859898 298 APAGTYVVKQGDSLAKIAKATGSNVDDLKAANNLSASSLRIGQALKI 344
Cdd:PRK13914   25 ASASTVVVEAGDTLWGIAQSKGTTVDAIKKANNLTTDKIVPGQKLQV 71
PRK13914 PRK13914
invasion associated endopeptidase;
253-361 6.66e-04

invasion associated endopeptidase;


Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 42.48  E-value: 6.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859898 253 KMPEAPKAPEQNV----AVVPGANSARDKTLASADVTGKLPTGAGKDPK-AP-----AGTYVVKQGDSLAKIAKATGSNV 322
Cdd:PRK13914  142 KVTSTPVAPTQEVkketTTQQAAPAAETKTEVKQTTQATTPAPKVAETKeTPvvdqnATTHAVKSGDTIWALSVKYGVSV 221

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1581859898 323 DDLKAANNLSASSLRIGQ--ALKIPNGTAD---NIKTASIPAEK 361
Cdd:PRK13914  222 QDIMSWNNLSSSSIYVGQklAIKQTANTATpkaEVKTEAPAAEK 265
PRK06148 PRK06148
hypothetical protein; Provisional
 437-520 2.40e-03

hypothetical protein; Provisional


Pssm-ID: 180426 [Multi-domain]  Cd Length: 1013  Bit Score: 40.78  E-value: 2.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581859898  437 GIDISVPQGTPIKAAENGVVIYAGNGLKEL--GNTVLVRHD----DGTVTVYGNADTLSVTR---GQKIQRGQTVAVSGM 507
Cdd:PRK06148   443 GVDLFAPAGTPVYAPLAGTVRSVEIEAVPLgyGGLVALEHEtpggDPFYTLYGHLAHEAVSRlkpGDRLAAGELFGAMGD 522

                           90
                   ....*....|....*
gi 1581859898  508 SGDVK--QPQVHFEV 520
Cdd:PRK06148   523 AHENGgwAPHLHFQL 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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