NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|937507228|ref|WP_054594428|]
View 

MULTISPECIES: murein transglycosylase A [Pseudomonas]

Protein Classification

murein transglycosylase A( domain architecture ID 11458107)

membrane-bound lytic murein transglycosylase A cleaves the beta-1,4 glycosidic linkages between N-acetylmuramic acid and N-acetylglucosamine in peptidoglycan

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
MltA COG2821
Membrane-bound lytic murein transglycosylase [Cell wall/membrane/envelope biogenesis];
13-381 6.01e-174

Membrane-bound lytic murein transglycosylase [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 442069 [Multi-domain]  Cd Length: 388  Bit Score: 490.16  E-value: 6.01e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937507228  13 LWTVPMVALLAGCNSGDTAKPQTHAIATYSSATWEALPAVSDNDLLAGFGSWRSACTRLKSDPV----------WGATCA 82
Cdd:COG2821    4 LLLLLALLLLAACATQPPPPGAAAPDARLQPVSFSDLPGWADDDLAAALPAFRRSCRRLARRPAasaygitaadWRAACA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937507228  83 AAANVP-QTADAIRDFLKEQLAVYGLRSSSGNANGLITGYYEPVYPGSLTQNPVANVPVYGVPDDMIIVSLESIypELKG 161
Cdd:COG2821   84 AARQLPaADPAAARAFFEREFQPYQVVGPDGGGNGLFTGYYEPELEGSRTRTAEYRYPLYRRPPDLVTVDLGSF--ELKG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937507228 162 KRLRGRLEGRVLKPYDDAAAIETKGV--KAPVLAWLTDPMDLQFLQIQGSGRIQLEDGRQLRIGYADQNGHPYRPIGRWL 239
Cdd:COG2821  162 KRLRGRLEGGRLVPYPTRAEIEAGALagRGLELAWVDDPVDAFFLQIQGSGRVRLPDGSLIRVGYAGKNGHPYTSIGRLL 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937507228 240 VDQGELKKEDVTMGAISAWAKAHPTRIPELLGSNPSYVFFSRNPDSNEGPRGSLNVPLTSGYSVAVDRKVIPLGSLLWLS 319
Cdd:COG2821  242 IDRGELPLEQMSMQAIRAWLRANPEELRELLNQNPSYVFFRELPGPDAGPLGALGVPLTPGRSIAVDPSLIPLGAPVWLE 321
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 937507228 320 TTRPD----GSALVRPVAAQDTGGAITGEVRADLFWGTGDAAGQLAGDMKQQGQIWMLWPKGAALP 381
Cdd:COG2821  322 TTLPDanfsGKPLRRLMIAQDTGGAIKGAVRADLFWGTGDEAGERAGRMKHPGRLWVLLPKGAAPP 387
 
Name Accession Description Interval E-value
MltA COG2821
Membrane-bound lytic murein transglycosylase [Cell wall/membrane/envelope biogenesis];
13-381 6.01e-174

Membrane-bound lytic murein transglycosylase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442069 [Multi-domain]  Cd Length: 388  Bit Score: 490.16  E-value: 6.01e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937507228  13 LWTVPMVALLAGCNSGDTAKPQTHAIATYSSATWEALPAVSDNDLLAGFGSWRSACTRLKSDPV----------WGATCA 82
Cdd:COG2821    4 LLLLLALLLLAACATQPPPPGAAAPDARLQPVSFSDLPGWADDDLAAALPAFRRSCRRLARRPAasaygitaadWRAACA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937507228  83 AAANVP-QTADAIRDFLKEQLAVYGLRSSSGNANGLITGYYEPVYPGSLTQNPVANVPVYGVPDDMIIVSLESIypELKG 161
Cdd:COG2821   84 AARQLPaADPAAARAFFEREFQPYQVVGPDGGGNGLFTGYYEPELEGSRTRTAEYRYPLYRRPPDLVTVDLGSF--ELKG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937507228 162 KRLRGRLEGRVLKPYDDAAAIETKGV--KAPVLAWLTDPMDLQFLQIQGSGRIQLEDGRQLRIGYADQNGHPYRPIGRWL 239
Cdd:COG2821  162 KRLRGRLEGGRLVPYPTRAEIEAGALagRGLELAWVDDPVDAFFLQIQGSGRVRLPDGSLIRVGYAGKNGHPYTSIGRLL 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937507228 240 VDQGELKKEDVTMGAISAWAKAHPTRIPELLGSNPSYVFFSRNPDSNEGPRGSLNVPLTSGYSVAVDRKVIPLGSLLWLS 319
Cdd:COG2821  242 IDRGELPLEQMSMQAIRAWLRANPEELRELLNQNPSYVFFRELPGPDAGPLGALGVPLTPGRSIAVDPSLIPLGAPVWLE 321
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 937507228 320 TTRPD----GSALVRPVAAQDTGGAITGEVRADLFWGTGDAAGQLAGDMKQQGQIWMLWPKGAALP 381
Cdd:COG2821  322 TTLPDanfsGKPLRRLMIAQDTGGAIKGAVRADLFWGTGDEAGERAGRMKHPGRLWVLLPKGAAPP 387
MltA pfam03562
MltA specific insert domain; This beta barrel domain is found inserted in the MltA a murein ...
53-279 3.96e-102

MltA specific insert domain; This beta barrel domain is found inserted in the MltA a murein degrading transglycosylase enzyme. This domain may be involved in peptidoglycan binding.


Pssm-ID: 460973 [Multi-domain]  Cd Length: 231  Bit Score: 301.79  E-value: 3.96e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937507228   53 SDNDLLAGFGSWRSACTRLKSD-PVWGATCAAAANVP--QTADAIRDFLKEQLAVYglRSSSGNANGLITGYYEPVYPGS 129
Cdd:pfam03562   2 QDDDLAAALPAFRRSCARLKKRaPDWLPACAAARSLPpsDSPAAARAFFEREFTPY--QVVGPGSDGLFTGYYEPELEGS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937507228  130 LTQNPVANVPVYGVPDDMIIVSLEsiYPELKGKRLRGRLEGRVLKPYDDAAAIETKGV---KAPVLAWLTDPMDLQFLQI 206
Cdd:pfam03562  80 RTRTAEYRYPLYRRPPDLVTVDLG--FFPLKGKRLRGRLVGGWLVPYPTRAEIEGKGAlsgRGLELAWLRDPVDAFFLQI 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 937507228  207 QGSGRIQLEDGRQLRIGYADQNGHPYRPIGRWLVDQGELKKEDVTMGAISAWAKAHPTRIPELLGSNPSYVFF 279
Cdd:pfam03562 158 QGSGRLRLPDGSVVRVGYAGQNGHPYTSIGRELIDRGELPLEQASMQGIRAWLRANPEELDELLNRNPSYVFF 230
mlta_B cd14668
Domain B insert of mltA_like lytic transglycosylases; Escherichia coli MltA is a ...
126-279 1.11e-78

Domain B insert of mltA_like lytic transglycosylases; Escherichia coli MltA is a membrane-bound lytic transglycosylase comprised of two domains separated by a large groove, where the peptidoglycan strand binds. Domain A is made up of an N-terminal and a C-terminal portion, which correspond to the 3D domain, named for 3 conserved aspartate residues. Domain B is inserted within the linear sequence of domain A. MltA is distinct from other bacterial lytic transglycosylases (LTs), which are similar to each other. Escherichia coli peptidoglycan lytic transglycosylase (LT) initiates cell wall recycling in response to damage, during bacterial fission, and cleaves peptidoglycan (PG) to create functional spaces in its wall. PG chains (also known as murein), the major components of the bacterial cell wall, are comprised of alternating beta-1-4-linked N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), and lytic transglycosylases cleave this beta-1-4 bond. Typically, peptidoglycan lytic transglycosylases (LT) are exolytic, releasing Metabolite 1 (GlcNAc-anhMurNAc-L-Ala-D-Glu-m-Dap-D-Ala-D-Ala) from the ends of the PG strands. In contrast, MltE is endolytic , cleaving in the middle of PG strands, with further processing to Metabolite 1 accomplished by other LTs. In E. coli, there are six membrane-bound LTs: MltA-MltF and soluble Slt70. Slt35 is a soluble fragment cleaved from MltB. Bacterial LTs are classified in 4 families: Family 1 includes slt70 MltC-MltF, Family 2 includes MltA, Family 3 includes MltB, and Family 4 of bacteriophage origin. While most of the LT family members are similar in structure and sequence with a lysozyme-like fold, Family 2 (including mltA) is distinct.


Pssm-ID: 270616  Cd Length: 159  Bit Score: 239.35  E-value: 1.11e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937507228 126 YPGSLTQNPVANVPVYGVPDDMIIVSLESIYPELKGKRLRGRLEGRVLKPYDDAAAIETKGV--KAPVLAWLTDPMDLQF 203
Cdd:cd14668    1 LEGSRTPTAEYRYPLYGRPPDLVTVDLGEFYPELKGKRLRGRVEGGRLVPYYTRAEIEAGALlgRGLELAWLDDPVDAFF 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 937507228 204 LQIQGSGRIQLEDGRQLRIGYADQNGHPYRPIGRWLVDQGELKKEDVTMGAISAWAKAHPTRIPELLGSNPSYVFF 279
Cdd:cd14668   81 LQIQGSGRLRLPDGSVVRVGYAGKNGHPYRSIGRVLIDRGELPKEQMSMQAIRAWLRANPERARELLNENPSYVFF 156
MltA smart00925
MltA specific insert domain; This beta barrel domain is found inserted in the MltA a murein ...
125-279 1.55e-76

MltA specific insert domain; This beta barrel domain is found inserted in the MltA a murein degrading transglycosylase enzyme. This domain may be involved in peptidoglycan binding.


Pssm-ID: 214916  Cd Length: 153  Bit Score: 233.61  E-value: 1.55e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937507228   125 VYPGSLTQNPVANVPVYGVPDDMIIVSLesIYPELKGKRLRGrleGRVLKPYDDAAAIETKGV--KAPVLAWLTDPMDLQ 202
Cdd:smart00925   1 VLEGSRTRTGRYRYPLYRRPDDLVVVDL--FDPELKGKRLRG---GGKLVPYPTRAEIEDGALdgRGLELAWVDDPVDLF 75
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 937507228   203 FLQIQGSGRIQLEDGRQLRIGYADQNGHPYRPIGRWLVDQGELKKEDVTMGAISAWAKAHPTRIPELLGSNPSYVFF 279
Cdd:smart00925  76 FLQIQGSGRVRLPDGRLIRVGYAGKNGHPYRSIGRLLIDRGEIPKEEASMQAIRAWLRANPERVDELLNRNPSYVFF 152
mltA PRK11162
murein transglycosylase A; Provisional
6-373 1.59e-53

murein transglycosylase A; Provisional


Pssm-ID: 236866 [Multi-domain]  Cd Length: 355  Bit Score: 180.88  E-value: 1.59e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937507228   6 KAWRNTLLWTVpMVALLAGCNSGDTAKPQTHAIATYSSA-TWEALPAVSDN-----DLLAGFGSWRSACTRLksdpvwga 79
Cdd:PRK11162   3 GRWVKYLLTGT-VLALLAGCSSKPTDRGQQYKDGKFTQPlSLVNQPNASGKpinagDFAEQVNQIRNSSPRL-------- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937507228  80 tcaAAANVPqTADAIRDFLKE-----QLAVYGL-----RSSSGNANGLITGYYEPVYPGSLTQNPVANVPVYGVPDDMI- 148
Cdd:PRK11162  74 ---YGRYSN-TYNAVQEWLLAggdtrELRQFGIqawqmEGVDNYGNVQFTGYYTPVIQARHTPQGEFQYPIYRMPPKRGr 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937507228 149 IVSLESIYpelkgkrlRGRLEGRVLkpyddaaaietkgvkapVLAWLTDPMDLQFLQIQGSGRIQLEDGRQLR-IGYADQ 227
Cdd:PRK11162 150 LPSRAEIY--------AGALSGKGL-----------------ELAYSNSLIDNFIMEVQGSGYVDFGDGRPLNfFAYAGK 204
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937507228 228 NGHPYRPIGRWLVDQGELKKEDVTMGAISAWAKAHPT-RIPELLGSNPSYVFFSRNPDsneGP-RGSLNVPLTSGYSVAV 305
Cdd:PRK11162 205 NGHAYRSIGKVLIDRGEVPKEDMSMQAIREWGEKHSEaEVRELLEQNPSFVFFKPQPF---APvKGASAVPLVAMASVAS 281
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 937507228 306 DRKVIPLGSLLWLSTTRPD------GSALVRPVAAQDTGGAITGEvRADLFWGTGDAAGQLAGDMKQQGQIWML 373
Cdd:PRK11162 282 DRSIIPPGTVLLAEVPLLDnngkftGKYELRLMVALDVGGAIKGQ-HFDIYQGIGPEAGHRAGHYNHYGRVWVL 354
 
Name Accession Description Interval E-value
MltA COG2821
Membrane-bound lytic murein transglycosylase [Cell wall/membrane/envelope biogenesis];
13-381 6.01e-174

Membrane-bound lytic murein transglycosylase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442069 [Multi-domain]  Cd Length: 388  Bit Score: 490.16  E-value: 6.01e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937507228  13 LWTVPMVALLAGCNSGDTAKPQTHAIATYSSATWEALPAVSDNDLLAGFGSWRSACTRLKSDPV----------WGATCA 82
Cdd:COG2821    4 LLLLLALLLLAACATQPPPPGAAAPDARLQPVSFSDLPGWADDDLAAALPAFRRSCRRLARRPAasaygitaadWRAACA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937507228  83 AAANVP-QTADAIRDFLKEQLAVYGLRSSSGNANGLITGYYEPVYPGSLTQNPVANVPVYGVPDDMIIVSLESIypELKG 161
Cdd:COG2821   84 AARQLPaADPAAARAFFEREFQPYQVVGPDGGGNGLFTGYYEPELEGSRTRTAEYRYPLYRRPPDLVTVDLGSF--ELKG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937507228 162 KRLRGRLEGRVLKPYDDAAAIETKGV--KAPVLAWLTDPMDLQFLQIQGSGRIQLEDGRQLRIGYADQNGHPYRPIGRWL 239
Cdd:COG2821  162 KRLRGRLEGGRLVPYPTRAEIEAGALagRGLELAWVDDPVDAFFLQIQGSGRVRLPDGSLIRVGYAGKNGHPYTSIGRLL 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937507228 240 VDQGELKKEDVTMGAISAWAKAHPTRIPELLGSNPSYVFFSRNPDSNEGPRGSLNVPLTSGYSVAVDRKVIPLGSLLWLS 319
Cdd:COG2821  242 IDRGELPLEQMSMQAIRAWLRANPEELRELLNQNPSYVFFRELPGPDAGPLGALGVPLTPGRSIAVDPSLIPLGAPVWLE 321
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 937507228 320 TTRPD----GSALVRPVAAQDTGGAITGEVRADLFWGTGDAAGQLAGDMKQQGQIWMLWPKGAALP 381
Cdd:COG2821  322 TTLPDanfsGKPLRRLMIAQDTGGAIKGAVRADLFWGTGDEAGERAGRMKHPGRLWVLLPKGAAPP 387
MltA pfam03562
MltA specific insert domain; This beta barrel domain is found inserted in the MltA a murein ...
53-279 3.96e-102

MltA specific insert domain; This beta barrel domain is found inserted in the MltA a murein degrading transglycosylase enzyme. This domain may be involved in peptidoglycan binding.


Pssm-ID: 460973 [Multi-domain]  Cd Length: 231  Bit Score: 301.79  E-value: 3.96e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937507228   53 SDNDLLAGFGSWRSACTRLKSD-PVWGATCAAAANVP--QTADAIRDFLKEQLAVYglRSSSGNANGLITGYYEPVYPGS 129
Cdd:pfam03562   2 QDDDLAAALPAFRRSCARLKKRaPDWLPACAAARSLPpsDSPAAARAFFEREFTPY--QVVGPGSDGLFTGYYEPELEGS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937507228  130 LTQNPVANVPVYGVPDDMIIVSLEsiYPELKGKRLRGRLEGRVLKPYDDAAAIETKGV---KAPVLAWLTDPMDLQFLQI 206
Cdd:pfam03562  80 RTRTAEYRYPLYRRPPDLVTVDLG--FFPLKGKRLRGRLVGGWLVPYPTRAEIEGKGAlsgRGLELAWLRDPVDAFFLQI 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 937507228  207 QGSGRIQLEDGRQLRIGYADQNGHPYRPIGRWLVDQGELKKEDVTMGAISAWAKAHPTRIPELLGSNPSYVFF 279
Cdd:pfam03562 158 QGSGRLRLPDGSVVRVGYAGQNGHPYTSIGRELIDRGELPLEQASMQGIRAWLRANPEELDELLNRNPSYVFF 230
mlta_B cd14668
Domain B insert of mltA_like lytic transglycosylases; Escherichia coli MltA is a ...
126-279 1.11e-78

Domain B insert of mltA_like lytic transglycosylases; Escherichia coli MltA is a membrane-bound lytic transglycosylase comprised of two domains separated by a large groove, where the peptidoglycan strand binds. Domain A is made up of an N-terminal and a C-terminal portion, which correspond to the 3D domain, named for 3 conserved aspartate residues. Domain B is inserted within the linear sequence of domain A. MltA is distinct from other bacterial lytic transglycosylases (LTs), which are similar to each other. Escherichia coli peptidoglycan lytic transglycosylase (LT) initiates cell wall recycling in response to damage, during bacterial fission, and cleaves peptidoglycan (PG) to create functional spaces in its wall. PG chains (also known as murein), the major components of the bacterial cell wall, are comprised of alternating beta-1-4-linked N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), and lytic transglycosylases cleave this beta-1-4 bond. Typically, peptidoglycan lytic transglycosylases (LT) are exolytic, releasing Metabolite 1 (GlcNAc-anhMurNAc-L-Ala-D-Glu-m-Dap-D-Ala-D-Ala) from the ends of the PG strands. In contrast, MltE is endolytic , cleaving in the middle of PG strands, with further processing to Metabolite 1 accomplished by other LTs. In E. coli, there are six membrane-bound LTs: MltA-MltF and soluble Slt70. Slt35 is a soluble fragment cleaved from MltB. Bacterial LTs are classified in 4 families: Family 1 includes slt70 MltC-MltF, Family 2 includes MltA, Family 3 includes MltB, and Family 4 of bacteriophage origin. While most of the LT family members are similar in structure and sequence with a lysozyme-like fold, Family 2 (including mltA) is distinct.


Pssm-ID: 270616  Cd Length: 159  Bit Score: 239.35  E-value: 1.11e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937507228 126 YPGSLTQNPVANVPVYGVPDDMIIVSLESIYPELKGKRLRGRLEGRVLKPYDDAAAIETKGV--KAPVLAWLTDPMDLQF 203
Cdd:cd14668    1 LEGSRTPTAEYRYPLYGRPPDLVTVDLGEFYPELKGKRLRGRVEGGRLVPYYTRAEIEAGALlgRGLELAWLDDPVDAFF 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 937507228 204 LQIQGSGRIQLEDGRQLRIGYADQNGHPYRPIGRWLVDQGELKKEDVTMGAISAWAKAHPTRIPELLGSNPSYVFF 279
Cdd:cd14668   81 LQIQGSGRLRLPDGSVVRVGYAGKNGHPYRSIGRVLIDRGELPKEQMSMQAIRAWLRANPERARELLNENPSYVFF 156
MltA smart00925
MltA specific insert domain; This beta barrel domain is found inserted in the MltA a murein ...
125-279 1.55e-76

MltA specific insert domain; This beta barrel domain is found inserted in the MltA a murein degrading transglycosylase enzyme. This domain may be involved in peptidoglycan binding.


Pssm-ID: 214916  Cd Length: 153  Bit Score: 233.61  E-value: 1.55e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937507228   125 VYPGSLTQNPVANVPVYGVPDDMIIVSLesIYPELKGKRLRGrleGRVLKPYDDAAAIETKGV--KAPVLAWLTDPMDLQ 202
Cdd:smart00925   1 VLEGSRTRTGRYRYPLYRRPDDLVVVDL--FDPELKGKRLRG---GGKLVPYPTRAEIEDGALdgRGLELAWVDDPVDLF 75
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 937507228   203 FLQIQGSGRIQLEDGRQLRIGYADQNGHPYRPIGRWLVDQGELKKEDVTMGAISAWAKAHPTRIPELLGSNPSYVFF 279
Cdd:smart00925  76 FLQIQGSGRVRLPDGRLIRVGYAGKNGHPYRSIGRLLIDRGEIPKEEASMQAIRAWLRANPERVDELLNRNPSYVFF 152
mltA PRK11162
murein transglycosylase A; Provisional
6-373 1.59e-53

murein transglycosylase A; Provisional


Pssm-ID: 236866 [Multi-domain]  Cd Length: 355  Bit Score: 180.88  E-value: 1.59e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937507228   6 KAWRNTLLWTVpMVALLAGCNSGDTAKPQTHAIATYSSA-TWEALPAVSDN-----DLLAGFGSWRSACTRLksdpvwga 79
Cdd:PRK11162   3 GRWVKYLLTGT-VLALLAGCSSKPTDRGQQYKDGKFTQPlSLVNQPNASGKpinagDFAEQVNQIRNSSPRL-------- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937507228  80 tcaAAANVPqTADAIRDFLKE-----QLAVYGL-----RSSSGNANGLITGYYEPVYPGSLTQNPVANVPVYGVPDDMI- 148
Cdd:PRK11162  74 ---YGRYSN-TYNAVQEWLLAggdtrELRQFGIqawqmEGVDNYGNVQFTGYYTPVIQARHTPQGEFQYPIYRMPPKRGr 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937507228 149 IVSLESIYpelkgkrlRGRLEGRVLkpyddaaaietkgvkapVLAWLTDPMDLQFLQIQGSGRIQLEDGRQLR-IGYADQ 227
Cdd:PRK11162 150 LPSRAEIY--------AGALSGKGL-----------------ELAYSNSLIDNFIMEVQGSGYVDFGDGRPLNfFAYAGK 204
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937507228 228 NGHPYRPIGRWLVDQGELKKEDVTMGAISAWAKAHPT-RIPELLGSNPSYVFFSRNPDsneGP-RGSLNVPLTSGYSVAV 305
Cdd:PRK11162 205 NGHAYRSIGKVLIDRGEVPKEDMSMQAIREWGEKHSEaEVRELLEQNPSFVFFKPQPF---APvKGASAVPLVAMASVAS 281
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 937507228 306 DRKVIPLGSLLWLSTTRPD------GSALVRPVAAQDTGGAITGEvRADLFWGTGDAAGQLAGDMKQQGQIWML 373
Cdd:PRK11162 282 DRSIIPPGTVLLAEVPLLDnngkftGKYELRLMVALDVGGAIKGQ-HFDIYQGIGPEAGHRAGHYNHYGRVWVL 354
mltA_like_LT_A cd14485
Domain A of MltA and related lytic transglycosylase; domain A is interrupted by domain B; ...
250-373 1.90e-41

Domain A of MltA and related lytic transglycosylase; domain A is interrupted by domain B; Escherichia coli MltA is a membrane-bound lytic transglycosylase comprised of two domains separated by a large groove, where the peptidoglycan strand binds. Domain A is made up of an N-terminal and a C-terminal portion, which correspond to the 3D domain, named for 3 conserved aspartate residues. Domain B is inserted within the linear sequence of domain A. MltA is distinct from other bacterial lytic transglycosylases (LTs), which are similar to each other. Escherichia coli peptidoglycan lytic transglycosylase (LT) initiates cell wall recycling in response to damage, during bacterial fission, and cleaves peptidoglycan (PG) to create functional spaces in its wall. PG chains (also known as murein), the major components of the bacterial cell wall, are comprised of alternating beta-1-4-linked N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), and lytic transglycosylases cleave this beta-1-4 bond. Typically, peptidoglycan lytic transglycosylases (LT) are exolytic, releasing Metabolite 1 (GlcNAc-anhMurNAc-L-Ala-D-Glu-m-Dap-D-Ala-D-Ala) from the ends of the PG strands. In contrast, MltE is endolytic , cleaving in the middle of PG strands, with further processing to Metabolite 1 accomplished by other LTs. In E. coli, there are six membrane-bound LTs: MltA-MltF and soluble Slt70. Slt35 is a soluble fragment cleaved from MltB. Bacterial LTs are classified in 4 families: Family 1 includes slt70 MltC-MltF, Family 2 includes MltA, Family 3 includes MltB, and Family 4 of bacteriophage origin. While most of the LT family members are similar in structure and sequence with a lysozyme-like fold, Family 2 (including mltA) is distinct.


Pssm-ID: 270618 [Multi-domain]  Cd Length: 159  Bit Score: 143.16  E-value: 1.90e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937507228 250 VTMGAISAWAKAHPTRIPELLGSNPSyVFFSRNPDSNEGPRGSL------NVPLTSGYSVAVDRKVIPLGSLLWLSTTRP 323
Cdd:cd14485   27 LTWGDLRASLEALLAFLLARLDAAPE-ALADFFQWVDGSGEGLFtgyyepGVPLTPGRSLAVDRSLIPLGAPVWLETPLP 105
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 937507228 324 D----GSALVRPVAAQDTGGAITGEVRADLFWGTGDAAGQLAGDMKQQGQIWML 373
Cdd:cd14485  106 DanggGKPLRRLVIAQDTGGAIKGPVRADLFWGSGDEAGELAGRMKHPGRLWVL 159
DPBB_MltA-like cd22785
double-psi beta-barrel fold of membrane-bound lytic murein transglycosylase A (MltA) and ...
287-373 4.90e-29

double-psi beta-barrel fold of membrane-bound lytic murein transglycosylase A (MltA) and similar proteins; MltA, also called murein hydrolase A, is a murein-degrading enzyme that may play a role in the recycling of muropeptides during cell elongation and/or cell division. It degrades murein glycan strands and insoluble, high-molecular weight murein sacculi. Bacterial lytic transglycosylases (LTs) are classified into 4 families: family 1 includes slt70 MltC-MltF, family 2 includes MltA, family 3 includes MltB, and family 4 includes proteins of bacteriophage origin. MltA is distinct from other bacterial LTs, which are similar in structure and sequence with a lysozyme-like fold. MltA is a kidney bean-shaped monomeric protein comprised of two domains separated by a large groove, where the peptidoglycan strand binds. Domain A is made up of an N-terminal and a C-terminal portion, which corresponds to a double-psi beta-barrel (DPBB) fold. Domain B also has a beta-barrel fold topology, but it is inserted within the linear sequence of domain A. This model corresponds to the DPBB fold that consists of two interlocked "psi-structure" motifs related by a pseudo-2-fold axis. It is involved in substrate binding and catalysis.


Pssm-ID: 439262 [Multi-domain]  Cd Length: 97  Bit Score: 108.50  E-value: 4.90e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937507228 287 EGPRGSLNVPLTSGYSVAVDRKVIPLGSLLWLSTTR----PDGSALVRPVAAQDTGGAITGeVRADLFWGTGDAAGQLAG 362
Cdd:cd22785    8 TPPRGALGVPLTPFRSVAVDPSVIPLGSVVYIPALDgvklPDGEPHDGLFIAQDTGGAIKG-KHIDVFTGSGDEAGELAG 86
                         90
                 ....*....|.
gi 937507228 363 DMKQQGQIWML 373
Cdd:cd22785   87 KLNHTGRVYVL 97
mlta_related_B cd14669
putative domain B insert of mltA_type lytic transglycosylases; Escherichia coli MltA is a ...
139-281 3.37e-24

putative domain B insert of mltA_type lytic transglycosylases; Escherichia coli MltA is a membrane-bound lytic transglycosylase comprised of two domains separated by a large groove, where the peptidoglycan strand binds. Domain A is made up of an N-terminal and a C-terminal portion, which correspond to the 3D domain, named for 3 conserved aspartate residues. Domain B is inserted within the linear sequence of domain A. MltA is distinct from other bacterial lytic transglycosylases (LTs), which are similar to each other. Escherichia coli peptidoglycan lytic transglycosylase (LT) initiates cell wall recycling in response to damage, during bacterial fission, and cleaves peptidoglycan (PG) to create functional spaces in its wall. PG chains (also known as murein), the major components of the bacterial cell wall, are comprised of alternating beta-1-4-linked N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), and lytic transglycosylases cleave this beta-1-4 bond. Typically, peptidoglycan lytic transglycosylases (LT) are exolytic, releasing Metabolite 1 (GlcNAc-anhMurNAc-L-Ala-D-Glu-m-Dap-D-Ala-D-Ala) from the ends of the PG strands. In contrast, MltE is endolytic , cleaving in the middle of PG strands, with further processing to Metabolite 1 accomplished by other LTs. In E. coli, there are six membrane-bound LTs: MltA-MltF and soluble Slt70. Slt35 is a soluble fragment cleaved from MltB. Bacterial LTs are classified in 4 families: Family 1 includes slt70 MltC-MltF, Family 2 includes MltA, Family 3 includes MltB, and Family 4 of bacteriophage origin. While most of the LT family members are similar in structure and sequence with a lysozyme-like fold, Family 2 (including mltA) is distinct.


Pssm-ID: 270617  Cd Length: 128  Bit Score: 96.33  E-value: 3.37e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937507228 139 PVYGVPDDMIIvslesiypelkgkrlrgrlegrvlkPYDDAAAIETKGV-KAPVLAWLTDPMDLQFLQIQGSGRIQLEDG 217
Cdd:cd14669   16 PVYGNPGDMIV-------------------------PYYTRAEIERGALwEAKVIAYVKDPTDLYLMQLQGSGKVKLPDG 70
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 937507228 218 RQLRIGYADQNGHPYRPIGRWLvdQGELK-KEDVTMGAISAWAKAhptripELLGSNPSYVFFSR 281
Cdd:cd14669   71 TVFRIAYAEQNGRPFLPPVASA--KGSLTpSEAANCIALNPPEVA------AFAISDPSYVFFRK 127
3D pfam06725
3D domain; This short presumed domain contains three conserved aspartate residues, hence the ...
301-374 4.18e-24

3D domain; This short presumed domain contains three conserved aspartate residues, hence the name 3D. It has been shown to be part of the catalytic double psi beta barrel domain of MltA.


Pssm-ID: 399598 [Multi-domain]  Cd Length: 72  Bit Score: 94.19  E-value: 4.18e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 937507228  301 YSVAVDRKVIPLGSLLWLSTTRpDGSALVRPVAAQDTGGAITGEvRADLFWGTGDAAGQLAGDMKQQGQIWMLW 374
Cdd:pfam06725   1 RSIAVDPSVIPLGTPVYVEGPL-GGKPVYRLAIAQDTGGAIKGN-RIDLYFGTGDEAGNLAGLYRKTGRVYILL 72
mltA_B_like cd14472
Domain B insert of mltA_like lytic transglycosylases; Escherichia coli MltA is a ...
153-281 3.29e-20

Domain B insert of mltA_like lytic transglycosylases; Escherichia coli MltA is a membrane-bound lytic transglycosylase comprised of two domains separated by a large groove, where the peptidoglycan strand binds. Domain A is made up of an N-terminal and a C-terminal portion, which correspond to the 3D domain, named for 3 conserved aspartate residues. Domain B is inserted within the linear sequence of domain A. MltA is distinct from other bacterial lytic transglycosylases (LTs), which are similar to each other. Escherichia coli peptidoglycan lytic transglycosylase (LT) initiates cell wall recycling in response to damage, during bacterial fission, and cleaves peptidoglycan (PG) to create functional spaces in its wall. PG chains (also known as murein), the major components of the bacterial cell wall, are comprised of alternating beta-1-4-linked N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), and lytic transglycosylases cleave this beta-1-4 bond. Typically, peptidoglycan lytic transglycosylases (LT) are exolytic, releasing Metabolite 1 (GlcNAc-anhMurNAc-L-Ala-D-Glu-m-Dap-D-Ala-D-Ala) from the ends of the PG strands. In contrast, MltE is endolytic , cleaving in the middle of PG strands, with further processing to Metabolite 1 accomplished by other LTs. In E. coli, there are six membrane-bound LTs: MltA-MltF and soluble Slt70. Slt35 is a soluble fragment cleaved from MltB. Bacterial LTs are classified in 4 families: Family 1 includes slt70 MltC-MltF, Family 2 includes MltA, Family 3 includes MltB, and Family 4 of bacteriophage origin. While most of the LT family members are similar in structure and sequence with a lysozyme-like fold, Family 2 (including mltA) is distinct.


Pssm-ID: 270615  Cd Length: 134  Bit Score: 85.87  E-value: 3.29e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937507228 153 ESIYPELKGKRLRGRLEGRvlkpyddaAAIETKGV-KAPVLAWLTDPMDLQFLQIQGSGRIQLEDGRQL-RIGYADQNGH 230
Cdd:cd14472   10 EFQYPIYRIPPKRGRLSSR--------AEIYAGALsDKYILAYSNSLVDNFIADVQGSGYIDFGDGSPLnFFSYAGKNGH 81
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 937507228 231 PYRPIGRWLVDQGELKKEDVTMGAISAWAKAHPTR-IPELLGSNPSYVFFSR 281
Cdd:cd14472   82 AYRSIGKVLIDRGEVKKEDISSQAIRHWGETHSEAeVRELLEQNPSFVFFKP 133
3D_domain cd14486
3D domain, named for 3 conserved aspartate residues, is found in mltA-like lytic ...
275-361 9.35e-10

3D domain, named for 3 conserved aspartate residues, is found in mltA-like lytic transglycosylases and numerous other contexts; This family contains the 3D domain, named for its 3 conserved aspartates. It is found in conjunction with numerous other domains such as MltA (membrane-bound lytic murein transglycosylase A). These aspartates are critical active site residues of mltA-like lytic transglycosylases. Escherichia coli peptidoglycan lytic transglycosylase (LT) initiates cell wall recycling in response to damage, during bacterial fission, and cleaves peptidoglycan (PG) to create functional spaces in its wall. MltA has 2 domains, separated by a large groove, where the peptidoglycan strand binds. The C-terminus has a double-psi beta barrel fold within the 3D domain, which forms the larger A domain along with the N-terminal region of Mlts, but is also found in various other domain architectures. Peptigoglycan (also known as murein) chains, the primary structural component of bacterial cells walls, are comprised of alternating beta-1-4-linked N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc); lytic transglycosylases (LTs) cleave this beta-1-4 bond. Typically, LTs are exolytic, releasing Metabolite 1 (GlcNAc-anhMurNAc-L-Ala-D-Glu-m-Dap-D-Ala-D-Ala) from the ends of the PG strands. In contrast, membrane-bound lytic murein transglycosylase E (MltE) is endolytic , cleaving in the middle of PG strands, with further processing to Metabolite 1 accomplished by other LTs. In E. coli, there are six membrane- bound LTs: MltA-MltF and soluble Slt70. Slt35 is a soluble fragment cleaved from MltB. Bacterial LTs are classified in 4 families: Family 1 includes slt70 MltC-MltF, Family 2 includes MltA, Family 3 includes MltB, and family 4 of bacteriophage origin. While most LTs are related members of the lysozyme-like lytic transglycosylase family, MltA represents a distinct fold and sequence conservation.


Pssm-ID: 270619 [Multi-domain]  Cd Length: 104  Bit Score: 55.46  E-value: 9.35e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937507228 275 SYVFFSRNPDSNEGPRGSLNVPLTSGYSVAVDRKVIPLGSLLWLSTTRPDGSALVRpvAAQDTGGAITGEvRADLFWGTG 354
Cdd:cd14486   12 GKRPSPPDEFSFSFRLTASGRPPVPYRTIAVDPSVIPLGSVVYIPELRGLPNDGVF--VAEDTGGAIKGN-HIDVYTGDG 88

                 ....*..
gi 937507228 355 DAAGQLA 361
Cdd:cd14486   89 PDARSNA 95
COG3584 COG3584
3D (Asp-Asp-Asp) domain, usually in lytic transglycosylases [Function unknown]; 3D ...
295-357 2.52e-08

3D (Asp-Asp-Asp) domain, usually in lytic transglycosylases [Function unknown]; 3D (Asp-Asp-Asp) domain, usually in lytic transglycosylases is part of the Pathway/BioSystem: 3D


Pssm-ID: 442803 [Multi-domain]  Cd Length: 92  Bit Score: 50.88  E-value: 2.52e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 937507228 295 VPLTSGYSVAVDRKVIPLGSLLWLSTtrpDGSALvrpvaAQDTGGAITGeVRADLFWGTGDAA 357
Cdd:COG3584   25 TRLRPGGVIAVDPDVIPLGTKVYIEG---YGYAV-----AEDTGGAIKG-NRIDIYMPSVSEA 78
DPBB_MltA_YuiC-like cd22784
double-psi beta-barrel fold of membrane-bound lytic murein transglycosylase A (MltA) and ...
291-357 8.17e-07

double-psi beta-barrel fold of membrane-bound lytic murein transglycosylase A (MltA) and YuiC-like proteins; This family includes two subfamilies of conserved double-psi beta-barrel (DPBB) domain proteins, such as membrane-bound lytic murein transglycosylase A (MltA)-like proteins and YuiC-like proteins. MltA, also called murein hydrolase A, is a murein-degrading enzyme that may play a role in the recycling of muropeptides during cell elongation and/or cell division. It degrades murein glycan strands and insoluble, high-molecular weight murein sacculi. Bacterial lytic transglycosylases (LTs) are classified into 4 families: family 1 includes slt70 MltC-MltF, family 2 includes MltA, family 3 includes MltB, and family 4 includes proteins of bacteriophage origin. MltA is distinct from other bacterial LTs, which are similar in structure and sequence with a lysozyme-like fold. MltA is a kidney bean-shaped monomeric protein comprised of two domains separated by a large groove, where the peptidoglycan strand binds. Domain A is made up of an N-terminal and a C-terminal portion, which corresponds to a double-psi beta-barrel (DPBB) fold. Domain B also has a beta-barrel fold topology, but it is inserted within the linear sequence of domain A. YuiC is a Firmicute stationary phase survival (Sps) protein that closely resembles the Barwin-like endoglucanase beta barrel of MltA. It is a DPBB fold that consists of two interlocked "psi-structure" motifs related by a pseudo-2-fold axis and may be involved in substrate binding and catalysis.


Pssm-ID: 439261 [Multi-domain]  Cd Length: 92  Bit Score: 46.87  E-value: 8.17e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 937507228 291 GSLNVPLTSGYSVAVDRKVIPLGSLLWLSTTRPDGSALVrpvaaQDTGGAITGEvRADLFWGTGDAA 357
Cdd:cd22784   20 TASGVTLRGYGTVAVDRDLIPLGTKVKIEGPGSGGEYVV-----LDRGGAIKGN-RIDIYFPSEKEA 80
3D_containing_proteins cd14667
Non-mltA associated 3D domain containing proteins, named for 3 conserved aspartate residues; ...
298-357 3.14e-06

Non-mltA associated 3D domain containing proteins, named for 3 conserved aspartate residues; This family contains the 3D domain, named for its 3 conserved aspartates, including similar uncharacterized proteins. These proteins contain the critical active site aspartate of mltA-like lytic transglycosylases where the 3D domain forms a larger domain with the N-terminal region. This domain is also found in conjunction with numerous other domains such as the Escherichia coli MltA, a membrane-bound lytic transglycosylase comprised of 2 domains separated by a large groove, where the peptidoglycan strand binds. Domain A is made up of an N-terminal and a C-terminal portion, corresponding to the 3D domain and Domain B is inserted within the linear sequence of domain A. MltA is distinct from other bacterial LTs, which are similar to each other. Escherichia coli peptidoglycan lytic transglycosylase (LT) initiates cell wall recycling in response to damage, during bacterial fission, and cleaves peptidoglycan (PG) to create functional spaces in its wall. PG chains (also known as murein), the major components of the bacterial cell wall, are comprised of alternating beta-1-4-linked N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), and lytic transglycosylases cleave this beta-1-4 bond.


Pssm-ID: 270620 [Multi-domain]  Cd Length: 90  Bit Score: 44.82  E-value: 3.14e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 937507228 298 TSGYSVAVDRKVIPLGSLLWLSTTRpdgsalvrpVA-AQDTGGAITGeVRADLFWGTGDAA 357
Cdd:cd14667   27 VGGGTIAVDPSVIPLGTKVYIEGYG---------VYvVEDTGGAIKG-NRIDIYMDSHAEA 77
DPBB_YuiC-like cd22786
double-psi beta-barrel fold of YuiC subfamily proteins; The YuiC subfamily includes a group of ...
287-359 4.58e-04

double-psi beta-barrel fold of YuiC subfamily proteins; The YuiC subfamily includes a group of conserved double-psi beta-barrel (DPBB) fold proteins, such as Bacillus subtilis protein YuiC, cell wall shaping protein YabE, cell wall-binding protein YocH, as well as Clostridium tetani phosphatase-associated protein PapQ. YuiC is a Firmicute stationary phase survival (Sps) protein that closely resembles the Barwin-like endoglucanase beta barrel of MltA. It is a double-psi beta-barrel (DPBB) fold that consists of two interlocked "psi-structure" motifs related by a pseudo-2-fold axis and may be involved in substrate binding and catalysis.


Pssm-ID: 439263 [Multi-domain]  Cd Length: 96  Bit Score: 39.12  E-value: 4.58e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 937507228 287 EGPRGSLNVPLTSGYSVAVDRKVIPLGSLLWLsttrpDGSAlvrPVAAQDTGGAITGEvRADLFWGTGDAAGQ 359
Cdd:cd22786   21 CYGITASGTPLKRKGTIAVDPSVIPLGTKVYI-----PGYG---YAVVADTGGAIKGN-RIDLYFPTHEEAIN 84
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH