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Conserved domains on  [gi|221377879|ref|NP_001138008|]
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mustard, isoform S [Drosophila melanogaster]

Protein Classification

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List of domain hits

Name Accession Description Interval E-value
TLDc smart00584
domain in TBC and LysM domain containing proteins;
944-1106 3.81e-73

domain in TBC and LysM domain containing proteins;


:

Pssm-ID: 214733  Cd Length: 165  Bit Score: 239.53  E-value: 3.81e-73
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221377879    944 TEILTEEHREKLCSHLPARAEGYSWSLIFSTSQHGFALNSLYRKMARLESPVLIVIEDTEHNVFGALTSCSLHVSDHFYG 1023
Cdd:smart00584    1 SSILSEEILALINSHLPTRAEGYPWTLLYSSSQHGYSLNTLYRKVEGYRPPTLLIIKDTDGEVFGAYASQAWRVSDHFYG 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221377879   1024 TGESLLYKFNPSFKVFHWTGENM-YFIKGNMESLSIGAGDGRFGLWLDGDLNQGRSQQCSTYGNEPL-APQEDFVIKTLE 1101
Cdd:smart00584   81 TGESFLFQLNPKFVVYDWTGKNKyYYINGTPDSLPIGGGGGGFGLWIDEDLNHGSSSHCKTFGNPPLsTKQEDFLILDIE 160

                    ....*
gi 221377879   1102 CWAFV 1106
Cdd:smart00584  161 VWGFG 165
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
142-207 2.87e-13

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


:

Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 68.58  E-value: 2.87e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221377879  142 QRFESVDKLSRQKSSLPTIPTISYTVGNRDTLTSVAARFDTTPSELTHLNRLNSSFIYPGQQLLVP 207
Cdd:COG1388    89 KSGDTLSGIARRYGAAAAPSPVTYTVKKGDTLWSIARRYGVSVEELKRWNGLSSDTIRPGQKLKIP 154
 
Name Accession Description Interval E-value
TLDc smart00584
domain in TBC and LysM domain containing proteins;
944-1106 3.81e-73

domain in TBC and LysM domain containing proteins;


Pssm-ID: 214733  Cd Length: 165  Bit Score: 239.53  E-value: 3.81e-73
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221377879    944 TEILTEEHREKLCSHLPARAEGYSWSLIFSTSQHGFALNSLYRKMARLESPVLIVIEDTEHNVFGALTSCSLHVSDHFYG 1023
Cdd:smart00584    1 SSILSEEILALINSHLPTRAEGYPWTLLYSSSQHGYSLNTLYRKVEGYRPPTLLIIKDTDGEVFGAYASQAWRVSDHFYG 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221377879   1024 TGESLLYKFNPSFKVFHWTGENM-YFIKGNMESLSIGAGDGRFGLWLDGDLNQGRSQQCSTYGNEPL-APQEDFVIKTLE 1101
Cdd:smart00584   81 TGESFLFQLNPKFVVYDWTGKNKyYYINGTPDSLPIGGGGGGFGLWIDEDLNHGSSSHCKTFGNPPLsTKQEDFLILDIE 160

                    ....*
gi 221377879   1102 CWAFV 1106
Cdd:smart00584  161 VWGFG 165
TLD pfam07534
TLD; This domain is predicted to be an enzyme and is often found associated with pfam01476. It ...
970-1106 8.79e-43

TLD; This domain is predicted to be an enzyme and is often found associated with pfam01476. It's structure consists of a beta-sandwich surrounded by two helices and two one-turn helices.


Pssm-ID: 429519  Cd Length: 139  Bit Score: 152.38  E-value: 8.79e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221377879   970 LIFSTSQHGFALNSLYRKMARlESPVLIVIEDTEHNVFGALTSCSLHVSDH-FYGTGESLLYKFNPSFKVFHWTGENMYF 1048
Cdd:pfam07534    1 LLYSTSRDGSSYQTFLEKIDN-KGPTLLIIKDNDGYIFGAFASQPWKVSGKkFYGDGESFLFSLSPQFDPYKWTGKNNAY 79
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 221377879  1049 IKGNMESLSIGAGDGRFGLWLDGDLNQGRSQQCSTYGNEPLAP--QEDFVIKTLECWAFV 1106
Cdd:pfam07534   80 FNCTSDGLGFGGGQPKFDLWIDSDLEFGYSRHCETFGNGQLSGsgQERFKIDDVEVWGLG 139
OXR1 COG5142
Oxidation resistance protein [DNA replication, recombination, and repair];
922-1103 2.06e-30

Oxidation resistance protein [DNA replication, recombination, and repair];


Pssm-ID: 227471  Cd Length: 212  Bit Score: 119.61  E-value: 2.06e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221377879  922 KTSLFATGSFDLDFPIPDLIG-----KTEILTEEHREKLCSHLPARAEGY-SWSLIFSTSQHGFALNSLYRKMARLESPV 995
Cdd:COG5142     7 KDYLFDSSLPDLPELQFDLMHdgksyKASLLTEEIVTRIRESLPDRYKYStSWRLLYSLFENGFSLRTFYESFGENEWPF 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221377879  996 -----LIVIEDTEHNVFGALTSCSLHVSDHFYGTGESLLYKFNP---------SFKVFHWTGENMYFIKGNMESLSIGAG 1061
Cdd:COG5142    87 rrvgfVLACRDKDGDLFGAFFEDRIRPARHYYGRDEMFLWKAARrpadrladkEVAVYPISGGKGFGIYCTPDFLAFGCG 166
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 221377879 1062 DGRFGLWLDGDLNQGRSQQCSTYGNEPLAPQEDFV-IKTLECW 1103
Cdd:COG5142   167 GGRYGLLIDKSLLDGESHPVETFGNCLLSSKGHFFrIVYLELW 209
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
142-207 2.87e-13

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


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 68.58  E-value: 2.87e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221377879  142 QRFESVDKLSRQKSSLPTIPTISYTVGNRDTLTSVAARFDTTPSELTHLNRLNSSFIYPGQQLLVP 207
Cdd:COG1388    89 KSGDTLSGIARRYGAAAAPSPVTYTVKKGDTLWSIARRYGVSVEELKRWNGLSSDTIRPGQKLKIP 154
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
165-207 4.12e-12

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: 61.64  E-value: 4.12e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 221377879   165 YTVGNRDTLTSVAARFDTTPSELTHLNRLNSSFIYPGQQLLVP 207
Cdd:pfam01476    1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSPNLYVGQKLKIP 43
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
163-206 1.19e-07

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: 49.02  E-value: 1.19e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 221377879  163 ISYTVGNRDTLTSVAARFDTTPSELTHLNRL-NSSFIYPGQQLLV 206
Cdd:cd00118     1 KTYTVKPGDTLWSIAKKYGVTVEELAAANPLiNPDCIYPGQKLKI 45
LysM smart00257
Lysin motif;
165-206 2.84e-07

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 47.83  E-value: 2.84e-07
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 221377879    165 YTVGNRDTLTSVAARFDTTPSELTHLNR-LNSSFIYPGQQLLV 206
Cdd:smart00257    2 YTVKKGDTLSSIARRYGISVSDLLELNNiLDPDNLQVGQKLKI 44
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
164-206 3.13e-04

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 44.73  E-value: 3.13e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 221377879  164 SYTVGNRDTLTSVAARFDTTPSELTHLNRLNSSFIYPGQQLLV 206
Cdd:PRK10783  345 SYKVRSGDTLSGIASRLNVSTKDLQQWNNLRGSKLKVGQTLTI 387
 
Name Accession Description Interval E-value
TLDc smart00584
domain in TBC and LysM domain containing proteins;
944-1106 3.81e-73

domain in TBC and LysM domain containing proteins;


Pssm-ID: 214733  Cd Length: 165  Bit Score: 239.53  E-value: 3.81e-73
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221377879    944 TEILTEEHREKLCSHLPARAEGYSWSLIFSTSQHGFALNSLYRKMARLESPVLIVIEDTEHNVFGALTSCSLHVSDHFYG 1023
Cdd:smart00584    1 SSILSEEILALINSHLPTRAEGYPWTLLYSSSQHGYSLNTLYRKVEGYRPPTLLIIKDTDGEVFGAYASQAWRVSDHFYG 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221377879   1024 TGESLLYKFNPSFKVFHWTGENM-YFIKGNMESLSIGAGDGRFGLWLDGDLNQGRSQQCSTYGNEPL-APQEDFVIKTLE 1101
Cdd:smart00584   81 TGESFLFQLNPKFVVYDWTGKNKyYYINGTPDSLPIGGGGGGFGLWIDEDLNHGSSSHCKTFGNPPLsTKQEDFLILDIE 160

                    ....*
gi 221377879   1102 CWAFV 1106
Cdd:smart00584  161 VWGFG 165
TLD pfam07534
TLD; This domain is predicted to be an enzyme and is often found associated with pfam01476. It ...
970-1106 8.79e-43

TLD; This domain is predicted to be an enzyme and is often found associated with pfam01476. It's structure consists of a beta-sandwich surrounded by two helices and two one-turn helices.


Pssm-ID: 429519  Cd Length: 139  Bit Score: 152.38  E-value: 8.79e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221377879   970 LIFSTSQHGFALNSLYRKMARlESPVLIVIEDTEHNVFGALTSCSLHVSDH-FYGTGESLLYKFNPSFKVFHWTGENMYF 1048
Cdd:pfam07534    1 LLYSTSRDGSSYQTFLEKIDN-KGPTLLIIKDNDGYIFGAFASQPWKVSGKkFYGDGESFLFSLSPQFDPYKWTGKNNAY 79
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 221377879  1049 IKGNMESLSIGAGDGRFGLWLDGDLNQGRSQQCSTYGNEPLAP--QEDFVIKTLECWAFV 1106
Cdd:pfam07534   80 FNCTSDGLGFGGGQPKFDLWIDSDLEFGYSRHCETFGNGQLSGsgQERFKIDDVEVWGLG 139
OXR1 COG5142
Oxidation resistance protein [DNA replication, recombination, and repair];
922-1103 2.06e-30

Oxidation resistance protein [DNA replication, recombination, and repair];


Pssm-ID: 227471  Cd Length: 212  Bit Score: 119.61  E-value: 2.06e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221377879  922 KTSLFATGSFDLDFPIPDLIG-----KTEILTEEHREKLCSHLPARAEGY-SWSLIFSTSQHGFALNSLYRKMARLESPV 995
Cdd:COG5142     7 KDYLFDSSLPDLPELQFDLMHdgksyKASLLTEEIVTRIRESLPDRYKYStSWRLLYSLFENGFSLRTFYESFGENEWPF 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221377879  996 -----LIVIEDTEHNVFGALTSCSLHVSDHFYGTGESLLYKFNP---------SFKVFHWTGENMYFIKGNMESLSIGAG 1061
Cdd:COG5142    87 rrvgfVLACRDKDGDLFGAFFEDRIRPARHYYGRDEMFLWKAARrpadrladkEVAVYPISGGKGFGIYCTPDFLAFGCG 166
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 221377879 1062 DGRFGLWLDGDLNQGRSQQCSTYGNEPLAPQEDFV-IKTLECW 1103
Cdd:COG5142   167 GGRYGLLIDKSLLDGESHPVETFGNCLLSSKGHFFrIVYLELW 209
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
142-207 2.87e-13

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


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 68.58  E-value: 2.87e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221377879  142 QRFESVDKLSRQKSSLPTIPTISYTVGNRDTLTSVAARFDTTPSELTHLNRLNSSFIYPGQQLLVP 207
Cdd:COG1388    89 KSGDTLSGIARRYGAAAAPSPVTYTVKKGDTLWSIARRYGVSVEELKRWNGLSSDTIRPGQKLKIP 154
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
165-207 4.12e-12

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: 61.64  E-value: 4.12e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 221377879   165 YTVGNRDTLTSVAARFDTTPSELTHLNRLNSSFIYPGQQLLVP 207
Cdd:pfam01476    1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSPNLYVGQKLKIP 43
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
163-206 1.19e-07

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: 49.02  E-value: 1.19e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 221377879  163 ISYTVGNRDTLTSVAARFDTTPSELTHLNRL-NSSFIYPGQQLLV 206
Cdd:cd00118     1 KTYTVKPGDTLWSIAKKYGVTVEELAAANPLiNPDCIYPGQKLKI 45
LysM smart00257
Lysin motif;
165-206 2.84e-07

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 47.83  E-value: 2.84e-07
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 221377879    165 YTVGNRDTLTSVAARFDTTPSELTHLNR-LNSSFIYPGQQLLV 206
Cdd:smart00257    2 YTVKKGDTLSSIARRYGISVSDLLELNNiLDPDNLQVGQKLKI 44
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
164-206 3.13e-04

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 44.73  E-value: 3.13e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 221377879  164 SYTVGNRDTLTSVAARFDTTPSELTHLNRLNSSFIYPGQQLLV 206
Cdd:PRK10783  345 SYKVRSGDTLSGIASRLNVSTKDLQQWNNLRGSKLKVGQTLTI 387
XkdP COG1652
Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion ...
155-207 1.19e-03

Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion transport and metabolism];


Pssm-ID: 441258 [Multi-domain]  Cd Length: 163  Bit Score: 40.76  E-value: 1.19e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 221377879  155 SSLPTIPTISYTVGNRDTLTSVAARFDTTPS---ELTHLNRL---NSSFIYPGQQLLVP 207
Cdd:COG1652   102 AELAPDAPKTYTVKPGDTLWGIAKRFYGDPArwpEIAEANRDqikNPDLIYPGQVLRIP 160
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
146-206 1.21e-03

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 42.76  E-value: 1.21e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221377879  146 SVDKLSRQKSSLPTIPTISYTVGNRDTLTSVAARFDTTPSELTHLNRLNSSFIYPGQQLLV 206
Cdd:PRK06347  463 STNTNTSKPSTNTNTNAKVYTVAKGDSLWRIANNNKVTIANLKSWNNLKSDFIYPGQKLKV 523
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
165-206 6.22e-03

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 40.45  E-value: 6.22e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 221377879  165 YTVGNRDTLTSVAARFDTTPSELTHLNRLNSSFIYPGQQLLV 206
Cdd:PRK06347  408 YTVVKGDSLWRIANNNKVTIANLKSWNNLKSDFIYPGQKLKV 449
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
165-206 8.31e-03

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 40.06  E-value: 8.31e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 221377879  165 YTVGNRDTLTSVAARFDTTPSELTHLNRLNSSFIYPGQQLLV 206
Cdd:PRK06347  333 YTVVKGDSLWRIANNHKVTVANLKAWNNLKSDFIYPGQKLKV 374
 
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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