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Conserved domains on  [gi|1356626822|gb|AVL06963|]
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L,D-transpeptidase [Bacillus subtilis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ErfK COG1376
Lipoprotein-anchoring transpeptidase ErfK/SrfK [Cell wall/membrane/envelope biogenesis];
58-162 2.67e-43

Lipoprotein-anchoring transpeptidase ErfK/SrfK [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 440986 [Multi-domain]  Cd Length: 121  Bit Score: 139.61  E-value: 2.67e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356626822  58 IAVSIGAKTLTLFLNNRVMKTYPIAVGKILTQTPTGEFYIINRQRNP----------------GGPFGAYWLSLSKQHYG 121
Cdd:COG1376     1 IVVDLSEQRLYVYEDGGLVRTYPVSVGRPGFPTPTGTFRVLRKAENPtwtppaempagmpggpDNPLGPYALYLSDGGYG 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1356626822 122 IHGTNNPASIGKAVSKGCIRMHNKDVIELASIVPNGTRVTI 162
Cdd:COG1376    81 IHGTPWPSSIGRNVSHGCIRLSNEDAKWLYDRVPVGTPVVV 121
LysM smart00257
Lysin motif;
3-45 9.63e-11

Lysin motif;


:

Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 53.99  E-value: 9.63e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1356626822    3 TYQVKQGDTLNSIAADFRISTAALLQANPSLQAG-LTAGQSIVI 45
Cdd:smart00257   1 TYTVKKGDTLSSIARRYGISVSDLLELNNILDPDnLQVGQKLKI 44
 
Name Accession Description Interval E-value
ErfK COG1376
Lipoprotein-anchoring transpeptidase ErfK/SrfK [Cell wall/membrane/envelope biogenesis];
58-162 2.67e-43

Lipoprotein-anchoring transpeptidase ErfK/SrfK [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440986 [Multi-domain]  Cd Length: 121  Bit Score: 139.61  E-value: 2.67e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356626822  58 IAVSIGAKTLTLFLNNRVMKTYPIAVGKILTQTPTGEFYIINRQRNP----------------GGPFGAYWLSLSKQHYG 121
Cdd:COG1376     1 IVVDLSEQRLYVYEDGGLVRTYPVSVGRPGFPTPTGTFRVLRKAENPtwtppaempagmpggpDNPLGPYALYLSDGGYG 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1356626822 122 IHGTNNPASIGKAVSKGCIRMHNKDVIELASIVPNGTRVTI 162
Cdd:COG1376    81 IHGTPWPSSIGRNVSHGCIRLSNEDAKWLYDRVPVGTPVVV 121
YkuD_like cd16913
L,D-transpeptidases/carboxypeptidases similar to Bacillus YkuD; Members of the YkuD-like ...
 57-162 1.90e-38

L,D-transpeptidases/carboxypeptidases similar to Bacillus YkuD; Members of the YkuD-like family of proteins are found in a range of bacteria. The best studied member Bacillus YkuD has been shown to act as an L,D-transpeptidase that gives rise to an alternative pathway for peptidoglycan cross-linking. Another member Helicobacter pylori Csd6 functions as an L,D-carboxypeptidase and regulates helical cell shape and motility. The conserved region contains a conserved histidine and cysteine, with the cysteine thought to be an active site residue.


Pssm-ID: 341130 [Multi-domain]  Cd Length: 121  Bit Score: 127.04  E-value: 1.90e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356626822  57 HIAVSIGAKTLTLFLNNRVMKTYPIAVGKILTQTPTGEFYIINRQRNP------------GGPFGAYWLSLS--KQHYGI 122
Cdd:cd16913     1 YIVVDLSEQRLYLYENGKLVKTYPVSTGKPGTPTPTGTFRITRKVKNPtwtgppsippgpYNPLGPYALRLSgpGSGIGI 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1356626822 123 HGTNNPASIGKAVSKGCIRMHNKDVIELASIVPNGTRVTI 162
Cdd:cd16913    81 HGTPWPSSIGRPASHGCIRLSNEDAKELYDWVPVGTPVVI 120
YkuD pfam03734
L,D-transpeptidase catalytic domain; This family of proteins are found in a range of bacteria. ...
 55-162 4.49e-21

L,D-transpeptidase catalytic domain; This family of proteins are found in a range of bacteria. It has been shown that this domain can act as an L,D-transpeptidase that gives rise to an alternative pathway for peptidoglycan cross-linking. This gives bacteria resistance to beta-lactam antibiotics that inhibit PBPs which usually carry out the cross-linking reaction. The conserved region contains a conserved histidine and cysteine, with the cysteine thought to be an active site residue. Several members of this family contain peptidoglycan binding domains. The molecular structure of YkuD protein shows this domain has a novel tertiary fold consisting of a beta-sandwich with two mixed sheets, one containing five strands and the other, six strands. The two beta-sheets form a cradle capped by an alpha-helix. This family was formerly called the ErfK/YbiS/YcfS/YnhG family, but is now named after the first protein of known structure.


Pssm-ID: 461031 [Multi-domain]  Cd Length: 89  Bit Score: 82.01  E-value: 4.49e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356626822  55 PYHIAVSIGAKTLT-LFLNNRVMKTYPIAVGKILTQTPTGEFYIInrqrnpggpfgaywlslskqhyGIHGTNNP--ASI 131
Cdd:pfam03734   1 DRYIVVDLSEQRLLyLYENGGLVLRYPVSVGRGDGPTPTGTFRII----------------------YIHDTGTPdlFGL 58

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1356626822 132 GKAVSKGCIRMHNKDVIELASIVPNGTRVTI 162
Cdd:pfam03734  59 GRRRSHGCIRLSNEDAKELYDRVLVGTPVVI 89
PRK10260 PRK10260
L,D-transpeptidase; Provisional
 6-160 2.87e-14

L,D-transpeptidase; Provisional


Pssm-ID: 182341 [Multi-domain]  Cd Length: 306  Bit Score: 68.52  E-value: 2.87e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356626822   6 VKQGDT--LNSIAADFRISTAALLQANPSLQAGLTAGQSIV-IPG---LPDPYtipyHIAVSIGAKTLTLFL----NNRV 75
Cdd:PRK10260   45 IPEGNTqpLEYFAAEYQMGLSNMMEANPGVDTFLPKGGTVLnIPQqliLPDTV----HEGIVINSAEMRLYYypkgTNTV 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356626822  76 MkTYPIAVGKILTQTPTGEFYIINRQR----------------------------NPGGPFGAYWLSLSKQhYGIHGTNN 127
Cdd:PRK10260  121 I-VLPIGIGQLGKDTPINWTTKVERKKagptwtptakmhaeyraageplpavvpaGPDNPMGLYALYIGRL-YAIHGTNA 198

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1356626822 128 PASIGKAVSKGCIRMHNKDVIELASIVPNGTRV 160
Cdd:PRK10260  199 NFGIGLRVSHGCVRLRNEDIKFLFEKVPVGTRV 231
LysM smart00257
Lysin motif;
3-45 9.63e-11

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 53.99  E-value: 9.63e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1356626822    3 TYQVKQGDTLNSIAADFRISTAALLQANPSLQAG-LTAGQSIVI 45
Cdd:smart00257   1 TYTVKKGDTLSSIARRYGISVSDLLELNNILDPDnLQVGQKLKI 44
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 3-45 1.02e-08

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: 48.64  E-value: 1.02e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1356626822   3 TYQVKQGDTLNSIAADFRISTAALLQANPSLQAG-LTAGQSIVI 45
Cdd:cd00118     2 TYTVKPGDTLWSIAKKYGVTVEELAAANPLINPDcIYPGQKLKI 45
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
3-47 1.05e-08

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


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 51.63  E-value: 1.05e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1356626822   3 TYQVKQGDTLNSIAADFRISTAALLQANPSLQAGLTAGQSIVIPG 47
Cdd:COG1388   111 TYTVKKGDTLWSIARRYGVSVEELKRWNGLSSDTIRPGQKLKIPA 155
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 4-46 1.01e-07

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: 45.85  E-value: 1.01e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1356626822   4 YQVKQGDTLNSIAADFRISTAALLQAN----PSLQagltAGQSIVIP 46
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNglssPNLY----VGQKLKIP 43
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 3-45 2.19e-04

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 40.49  E-value: 2.19e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1356626822   3 TYQVKQGDTLNSIAADFRISTAALLQANPSLQAGLTAGQSIVI 45
Cdd:PRK10783  345 SYKVRSGDTLSGIASRLNVSTKDLQQWNNLRGSKLKVGQTLTI 387
 
Name Accession Description Interval E-value
ErfK COG1376
Lipoprotein-anchoring transpeptidase ErfK/SrfK [Cell wall/membrane/envelope biogenesis];
58-162 2.67e-43

Lipoprotein-anchoring transpeptidase ErfK/SrfK [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440986 [Multi-domain]  Cd Length: 121  Bit Score: 139.61  E-value: 2.67e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356626822  58 IAVSIGAKTLTLFLNNRVMKTYPIAVGKILTQTPTGEFYIINRQRNP----------------GGPFGAYWLSLSKQHYG 121
Cdd:COG1376     1 IVVDLSEQRLYVYEDGGLVRTYPVSVGRPGFPTPTGTFRVLRKAENPtwtppaempagmpggpDNPLGPYALYLSDGGYG 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1356626822 122 IHGTNNPASIGKAVSKGCIRMHNKDVIELASIVPNGTRVTI 162
Cdd:COG1376    81 IHGTPWPSSIGRNVSHGCIRLSNEDAKWLYDRVPVGTPVVV 121
YkuD_like cd16913
L,D-transpeptidases/carboxypeptidases similar to Bacillus YkuD; Members of the YkuD-like ...
 57-162 1.90e-38

L,D-transpeptidases/carboxypeptidases similar to Bacillus YkuD; Members of the YkuD-like family of proteins are found in a range of bacteria. The best studied member Bacillus YkuD has been shown to act as an L,D-transpeptidase that gives rise to an alternative pathway for peptidoglycan cross-linking. Another member Helicobacter pylori Csd6 functions as an L,D-carboxypeptidase and regulates helical cell shape and motility. The conserved region contains a conserved histidine and cysteine, with the cysteine thought to be an active site residue.


Pssm-ID: 341130 [Multi-domain]  Cd Length: 121  Bit Score: 127.04  E-value: 1.90e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356626822  57 HIAVSIGAKTLTLFLNNRVMKTYPIAVGKILTQTPTGEFYIINRQRNP------------GGPFGAYWLSLS--KQHYGI 122
Cdd:cd16913     1 YIVVDLSEQRLYLYENGKLVKTYPVSTGKPGTPTPTGTFRITRKVKNPtwtgppsippgpYNPLGPYALRLSgpGSGIGI 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1356626822 123 HGTNNPASIGKAVSKGCIRMHNKDVIELASIVPNGTRVTI 162
Cdd:cd16913    81 HGTPWPSSIGRPASHGCIRLSNEDAKELYDWVPVGTPVVI 120
YkuD pfam03734
L,D-transpeptidase catalytic domain; This family of proteins are found in a range of bacteria. ...
 55-162 4.49e-21

L,D-transpeptidase catalytic domain; This family of proteins are found in a range of bacteria. It has been shown that this domain can act as an L,D-transpeptidase that gives rise to an alternative pathway for peptidoglycan cross-linking. This gives bacteria resistance to beta-lactam antibiotics that inhibit PBPs which usually carry out the cross-linking reaction. The conserved region contains a conserved histidine and cysteine, with the cysteine thought to be an active site residue. Several members of this family contain peptidoglycan binding domains. The molecular structure of YkuD protein shows this domain has a novel tertiary fold consisting of a beta-sandwich with two mixed sheets, one containing five strands and the other, six strands. The two beta-sheets form a cradle capped by an alpha-helix. This family was formerly called the ErfK/YbiS/YcfS/YnhG family, but is now named after the first protein of known structure.


Pssm-ID: 461031 [Multi-domain]  Cd Length: 89  Bit Score: 82.01  E-value: 4.49e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356626822  55 PYHIAVSIGAKTLT-LFLNNRVMKTYPIAVGKILTQTPTGEFYIInrqrnpggpfgaywlslskqhyGIHGTNNP--ASI 131
Cdd:pfam03734   1 DRYIVVDLSEQRLLyLYENGGLVLRYPVSVGRGDGPTPTGTFRII----------------------YIHDTGTPdlFGL 58

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1356626822 132 GKAVSKGCIRMHNKDVIELASIVPNGTRVTI 162
Cdd:pfam03734  59 GRRRSHGCIRLSNEDAKELYDRVLVGTPVVI 89
PRK10260 PRK10260
L,D-transpeptidase; Provisional
 6-160 2.87e-14

L,D-transpeptidase; Provisional


Pssm-ID: 182341 [Multi-domain]  Cd Length: 306  Bit Score: 68.52  E-value: 2.87e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356626822   6 VKQGDT--LNSIAADFRISTAALLQANPSLQAGLTAGQSIV-IPG---LPDPYtipyHIAVSIGAKTLTLFL----NNRV 75
Cdd:PRK10260   45 IPEGNTqpLEYFAAEYQMGLSNMMEANPGVDTFLPKGGTVLnIPQqliLPDTV----HEGIVINSAEMRLYYypkgTNTV 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356626822  76 MkTYPIAVGKILTQTPTGEFYIINRQR----------------------------NPGGPFGAYWLSLSKQhYGIHGTNN 127
Cdd:PRK10260  121 I-VLPIGIGQLGKDTPINWTTKVERKKagptwtptakmhaeyraageplpavvpaGPDNPMGLYALYIGRL-YAIHGTNA 198

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1356626822 128 PASIGKAVSKGCIRMHNKDVIELASIVPNGTRV 160
Cdd:PRK10260  199 NFGIGLRVSHGCVRLRNEDIKFLFEKVPVGTRV 231
PRK10190 PRK10190
L,D-transpeptidase; Provisional
 2-162 6.36e-12

L,D-transpeptidase; Provisional


Pssm-ID: 182294 [Multi-domain]  Cd Length: 310  Bit Score: 61.80  E-value: 6.36e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356626822   2 LTYQVKQGDT--LNSIAADFRISTAALLQANPSLQAGL-TAGQSIVIPG---LPDpyTIPYHIAVSIGAKTLTLF--LNN 73
Cdd:PRK10190   38 LTVTVPDHNTqpLETFAAQYGQGLSNMLEANPGADVFLpKSGSQLTIPQqliLPD--TVRKGIVVNVAEMRLYYYppDSN 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1356626822  74 RVmKTYPIAVGKILTQTPTGEFYIINRQRN----------------------------PGGPFGAYWLSLSKQhYGIHGT 125
Cdd:PRK10190  116 TV-EVFPIGIGQAGRETPRNWVTTVERKQEaptwtptpntrreyakrgeslpafvpagPDNPMGLYAIYIGRL-YAIHGT 193

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1356626822 126 NNPASIGKAVSKGCIRMHNKDVIELASIVPNGTRVTI 162
Cdd:PRK10190  194 NANFGIGLRVSQGCIRLRNDDIKYLFDNVPVGTRVQI 230
LysM smart00257
Lysin motif;
3-45 9.63e-11

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 53.99  E-value: 9.63e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1356626822    3 TYQVKQGDTLNSIAADFRISTAALLQANPSLQAG-LTAGQSIVI 45
Cdd:smart00257   1 TYTVKKGDTLSSIARRYGISVSDLLELNNILDPDnLQVGQKLKI 44
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 3-45 1.02e-08

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: 48.64  E-value: 1.02e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1356626822   3 TYQVKQGDTLNSIAADFRISTAALLQANPSLQAG-LTAGQSIVI 45
Cdd:cd00118     2 TYTVKPGDTLWSIAKKYGVTVEELAAANPLINPDcIYPGQKLKI 45
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
3-47 1.05e-08

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


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 51.63  E-value: 1.05e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1356626822   3 TYQVKQGDTLNSIAADFRISTAALLQANPSLQAGLTAGQSIVIPG 47
Cdd:COG1388   111 TYTVKKGDTLWSIARRYGVSVEELKRWNGLSSDTIRPGQKLKIPA 155
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 4-46 1.01e-07

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: 45.85  E-value: 1.01e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1356626822   4 YQVKQGDTLNSIAADFRISTAALLQAN----PSLQagltAGQSIVIP 46
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNglssPNLY----VGQKLKIP 43
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 3-45 2.19e-04

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 40.49  E-value: 2.19e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1356626822   3 TYQVKQGDTLNSIAADFRISTAALLQANPSLQAGLTAGQSIVI 45
Cdd:PRK10783  345 SYKVRSGDTLSGIASRLNVSTKDLQQWNNLRGSKLKVGQTLTI 387
gpX COG5004
P2-like prophage tail protein X [Mobilome: prophages, transposons];
1-55 1.54e-03

P2-like prophage tail protein X [Mobilome: prophages, transposons];


Pssm-ID: 444028  Cd Length: 69  Bit Score: 35.62  E-value: 1.54e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1356626822   1 MLTYQVKQGDTLNSIAADF--RIS--TAALLQANP---SLQAGLTAGQSIVIPGLPDPYTIP 55
Cdd:COG5004     2 AMTYRTRQGDTLDALCWRYygRTAgvVEAVLAANPglaALGPVLPAGTVVTLPDIPAAPTVE 63
 
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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