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Conserved domains on  [gi|966513662|ref|WP_058530181|]
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septal ring lytic transglycosylase RlpA family protein [Legionella rubrilucens]

Protein Classification

septal ring lytic transglycosylase RlpA family protein( domain architecture ID 11435221)

septal ring lytic transglycosylase RlpA family protein similar to endolytic peptidoglycan transglycosylase RlpA (rare lipoprotein A), a lytic transglycosylase with a strong preference for naked glycan strands that lack stem peptides

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RlpA COG0797
Peptidoglycan lytic transglycosylase RlpA, contains C-terminal SPOR domain [Cell wall/membrane ...
 70-192 3.84e-68

Peptidoglycan lytic transglycosylase RlpA, contains C-terminal SPOR domain [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 440560 [Multi-domain]  Cd Length: 133  Bit Score: 207.01  E-value: 3.84e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966513662  70 GNPDSYAVNGRKYEVMRSASGYKTRGMASWYGTKFHSRRTSSGDDYDMYAMTAAHKTLPLPSYVRVKNLSNGREAIVKVN 149
Cdd:COG0797   11 ASGKPYTVRGKTYYPLAEASGYTETGLASWYGDKFHGRKTASGERYDPNALTAAHKTLPLGTYVRVTNLENGRSVVVRVN 90

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 966513662 150 DRGPFHADRVIDLSYAAATKLGLLPKGTAPVEIEALTVKSPGG 192
Cdd:COG0797   91 DRGPFVKGRIIDLSYAAARKLGMLGKGVAPVRVEVLGPASLAG 133
SPOR pfam05036
SPOR domain; Bacterial SPOR domains bind peptidoglycan (PG) and target proteins to the cell ...
 197-264 1.88e-11

SPOR domain; Bacterial SPOR domains bind peptidoglycan (PG) and target proteins to the cell division site by binding to denuded glycan strands that lack stem peptides. This 70 residue domain is composed of two 35 residue repeats found in proteins involved in sporulation and cell division such as FtsN, DedD, and CwlM. This domain is involved in binding peptidoglycan. Two tandem repeats fold into a pseudo-2-fold symmetric single-domain structure containing numerous contacts between the repeats. FtsN is an essential cell division protein with a simple bitopic topology, a short N-terminal cytoplasmic segment fused to a large carboxy periplasmic domain through a single transmembrane domain. These repeats lay at the periplasmic C-terminus. FtsN localizes to the septum ring complex.


:

Pssm-ID: 461531 [Multi-domain]  Cd Length: 76  Bit Score: 58.53  E-value: 1.88e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966513662  197 YYYVQAGAFNSQDLANALREKLAKL--TPSPVFIENYQHRYIVRVGPFANKAMTESLKMRLAANGVKGSF 264
Cdd:pfam05036   4 GYYVQLGAFSNEANAEALAAKLRAKgfAAYVAVTSKGGGLYRVRVGPFASREEARAALKKLKALAGLSPF 73
 
Name Accession Description Interval E-value
RlpA COG0797
Peptidoglycan lytic transglycosylase RlpA, contains C-terminal SPOR domain [Cell wall/membrane ...
 70-192 3.84e-68

Peptidoglycan lytic transglycosylase RlpA, contains C-terminal SPOR domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440560 [Multi-domain]  Cd Length: 133  Bit Score: 207.01  E-value: 3.84e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966513662  70 GNPDSYAVNGRKYEVMRSASGYKTRGMASWYGTKFHSRRTSSGDDYDMYAMTAAHKTLPLPSYVRVKNLSNGREAIVKVN 149
Cdd:COG0797   11 ASGKPYTVRGKTYYPLAEASGYTETGLASWYGDKFHGRKTASGERYDPNALTAAHKTLPLGTYVRVTNLENGRSVVVRVN 90

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 966513662 150 DRGPFHADRVIDLSYAAATKLGLLPKGTAPVEIEALTVKSPGG 192
Cdd:COG0797   91 DRGPFVKGRIIDLSYAAARKLGMLGKGVAPVRVEVLGPASLAG 133
DPBB_RlpA-like cd22268
double-psi beta-barrel fold of endolytic peptidoglycan transglycosylase RlpA and similar ...
 94-183 3.58e-52

double-psi beta-barrel fold of endolytic peptidoglycan transglycosylase RlpA and similar proteins; Endolytic peptidoglycan transglycosylase RlpA (rare lipoprotein A, RlpA) is a lytic transglycosylase with a strong preference for naked glycan strands that lack stem peptides. It adopts a double-psi beta-barrel (DPBB) fold and is one of four SPOR-domain containing proteins in Escherichia coli (including FtsN, DedA and DamX) that bind peptidoglycan (PG) and are targeted to the septum during division. It directly interacts with the divisome protein FtsK in vitro, and deletion of the rlpA gene partially bypasses the requirement for functional FtsK, a large, multi-spanning membrane protein that facilitates double-stranded DNA translocation during division and sporulation in E. coli and Bacillus subtilis, respectively. In Pseudomonas aeruginosa, RlpA contributes to rod shape maintenance and daughter cell separation. The separation of daughter cells requires extensive PG remodeling. It has been suggested that amidases and RlpA work in tandem to degrade PG in the division septum and lateral wall to facilitate daughter cell separation.


Pssm-ID: 439248 [Multi-domain]  Cd Length: 92  Bit Score: 164.93  E-value: 3.58e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966513662  94 RGMASWYGTKFHSRRTSSGDDYDMYAMTAAHKTLPLPSYVRVKNLSNGREAIVKVNDRGPFHADRVIDLSYAAATKLGLL 173
Cdd:cd22268    2 TGKASWYGPGFHGRRTASGERYDPNALTAAHKTLPFGTKVRVTNLENGKSVVVRVNDRGPFVKGRIIDLSYAAAKKLGML 81

                         90
                 ....*....|
gi 966513662 174 PKGTAPVEIE 183
Cdd:cd22268   82 GAGVAPVRIE 91
rlpA TIGR00413
rare lipoprotein A; This is a family of prokaryotic proteins with unknown function. ...
 95-245 1.66e-43

rare lipoprotein A; This is a family of prokaryotic proteins with unknown function. Lipoprotein annotation based on the presence of consensus lipoprotein signal sequence. Included in this family is the E. coli putative lipoprotein rlpA. [Cell envelope, Other]


Pssm-ID: 273065 [Multi-domain]  Cd Length: 208  Bit Score: 146.67  E-value: 1.66e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966513662   95 GMASWYGTKFHSRRTSSGDDYDMYAMTAAHKTLPLPSYVRVKNLSNGREAIVKVNDRGPFHADRVIDLSYAAATKLGLLP 174
Cdd:TIGR00413   1 GLASWYGPKFHGRKTANGEVYNMKALTAAHKTLPFNTYVKVTNLHNNRSVIVRINDRGPFSDDRIIDLSHAAAREIGLIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966513662  175 KGTAPVEIEAL----------------------------------TVKSPGGQHVA------YYYVQAGAFNSQDLANAL 214
Cdd:TIGR00413  81 RGVGQVRIEVLhvakngnlsgaatktfnkqakkqeakdrlvlesnTLFDNTKKSINalkgteFFCLQMGELRSRSQANKL 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 966513662  215 REKLAKLTPSPVfIENYQHRYIVRVGPFANK 245
Cdd:TIGR00413 161 ITQLALANLQTE-VNRSGPKYEVYIGPFDDK 190
PRK10672 PRK10672
endolytic peptidoglycan transglycosylase RlpA;
35-191 5.00e-39

endolytic peptidoglycan transglycosylase RlpA;


Pssm-ID: 236733 [Multi-domain]  Cd Length: 361  Bit Score: 139.43  E-value: 5.00e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966513662  35 PKKPFTPTQQDGAPKGPLpKTFQKVKPANEPLSRYGNPDsYAVNGRKYEVMRSASGYKTRGMASWYGTKFHSRRTSSGDD 114
Cdd:PRK10672  23 GQQQTVSAPQPAVCNGPV-VEISGAEPRYEPYNPTANQD-YQRNGKSYKIVQDPSNFSQAGLAAIYDAEAGSNLTASGER 100

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966513662 115 YDMYAMTAAHKTLPLPSYVRVKNLSNGREAIVKVNDRGPFHADRVIDLSYAAATKLGLLPkgTAPVEIEALTVKSPG 191
Cdd:PRK10672 101 FDPNALTAAHPTLPIPSYVRVTNLANGRMIVVRINDRGPYGPGRVIDLSRAAADRLNTSN--NTKVRIDPIIVAPDG 175
DPBB_1 pfam03330
Lytic transglycolase; Rare lipoprotein A (RlpA) contains a conserved region that has the ...
 93-182 7.15e-30

Lytic transglycolase; Rare lipoprotein A (RlpA) contains a conserved region that has the double-psi beta-barrel (DPBB) fold. The function of RlpA is not well understood, but it has been shown to act as a prc mutant suppressor in Escherichia coli. The DPBB fold is often an enzymatic domain. The members of this family are quite diverse, and if catalytic this family may contain several different functions. Another example of this domain is found in the N terminus of pollen allergen. Recent studies show that the full-length RlpA protein from Pseudomonas Aeruginosa is an outer membrane protein that is a lytic transglycolase with specificity for peptidoglycan lacking stem peptides. Residue D157 in UniProtKB:Q9X6V6 is critical for lytic activity.


Pssm-ID: 427248 [Multi-domain]  Cd Length: 82  Bit Score: 107.29  E-value: 7.15e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966513662   93 TRGMASWYGtkfhsRRTSSGDDYDMYAMTAAHKTLPLPSYVRVKNlsnGREAIVKVNDRGPFHADRVIDLSYAAATKLGL 172
Cdd:pfam03330   1 AAGSASLYN-----NGTACGECYDVRCLTAAHPTLPFGTYCRVLS---GRSVIVRITDRGPFPPGRHFDLSGAAFEKLAM 72

                          90
                  ....*....|
gi 966513662  173 LPKGTAPVEI 182
Cdd:pfam03330  73 PRAGIVPVQY 82
SPOR pfam05036
SPOR domain; Bacterial SPOR domains bind peptidoglycan (PG) and target proteins to the cell ...
 197-264 1.88e-11

SPOR domain; Bacterial SPOR domains bind peptidoglycan (PG) and target proteins to the cell division site by binding to denuded glycan strands that lack stem peptides. This 70 residue domain is composed of two 35 residue repeats found in proteins involved in sporulation and cell division such as FtsN, DedD, and CwlM. This domain is involved in binding peptidoglycan. Two tandem repeats fold into a pseudo-2-fold symmetric single-domain structure containing numerous contacts between the repeats. FtsN is an essential cell division protein with a simple bitopic topology, a short N-terminal cytoplasmic segment fused to a large carboxy periplasmic domain through a single transmembrane domain. These repeats lay at the periplasmic C-terminus. FtsN localizes to the septum ring complex.


Pssm-ID: 461531 [Multi-domain]  Cd Length: 76  Bit Score: 58.53  E-value: 1.88e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966513662  197 YYYVQAGAFNSQDLANALREKLAKL--TPSPVFIENYQHRYIVRVGPFANKAMTESLKMRLAANGVKGSF 264
Cdd:pfam05036   4 GYYVQLGAFSNEANAEALAAKLRAKgfAAYVAVTSKGGGLYRVRVGPFASREEARAALKKLKALAGLSPF 73
DedD COG3147
Cell division protein DedD (periplasmic protein involved in septation) [Cell cycle control, ...
 165-262 3.44e-08

Cell division protein DedD (periplasmic protein involved in septation) [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442381 [Multi-domain]  Cd Length: 140  Bit Score: 51.31  E-value: 3.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966513662 165 AAATKLGLLPKGTAPVEIEALT----VKSPGGQHvayYYVQAGAFNSQDLANALREKLAKLTpSPVFIENYQH----RYI 236
Cdd:COG3147   32 AAAPKPAAKPAAPKPAAAAAAApaakAAAPAGGG---WVVQLGAFSNEDNAKELVAKLRAAG-YPAYTEPVTTgggtLYR 107

                         90       100
                 ....*....|....*....|....*..
gi 966513662 237 VRVGPFANKAMTESLKMRL-AANGVKG 262
Cdd:COG3147  108 VRVGPFASRAEAEAALAKLkKLTGLKG 134
 
Name Accession Description Interval E-value
RlpA COG0797
Peptidoglycan lytic transglycosylase RlpA, contains C-terminal SPOR domain [Cell wall/membrane ...
 70-192 3.84e-68

Peptidoglycan lytic transglycosylase RlpA, contains C-terminal SPOR domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440560 [Multi-domain]  Cd Length: 133  Bit Score: 207.01  E-value: 3.84e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966513662  70 GNPDSYAVNGRKYEVMRSASGYKTRGMASWYGTKFHSRRTSSGDDYDMYAMTAAHKTLPLPSYVRVKNLSNGREAIVKVN 149
Cdd:COG0797   11 ASGKPYTVRGKTYYPLAEASGYTETGLASWYGDKFHGRKTASGERYDPNALTAAHKTLPLGTYVRVTNLENGRSVVVRVN 90

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 966513662 150 DRGPFHADRVIDLSYAAATKLGLLPKGTAPVEIEALTVKSPGG 192
Cdd:COG0797   91 DRGPFVKGRIIDLSYAAARKLGMLGKGVAPVRVEVLGPASLAG 133
DPBB_RlpA-like cd22268
double-psi beta-barrel fold of endolytic peptidoglycan transglycosylase RlpA and similar ...
 94-183 3.58e-52

double-psi beta-barrel fold of endolytic peptidoglycan transglycosylase RlpA and similar proteins; Endolytic peptidoglycan transglycosylase RlpA (rare lipoprotein A, RlpA) is a lytic transglycosylase with a strong preference for naked glycan strands that lack stem peptides. It adopts a double-psi beta-barrel (DPBB) fold and is one of four SPOR-domain containing proteins in Escherichia coli (including FtsN, DedA and DamX) that bind peptidoglycan (PG) and are targeted to the septum during division. It directly interacts with the divisome protein FtsK in vitro, and deletion of the rlpA gene partially bypasses the requirement for functional FtsK, a large, multi-spanning membrane protein that facilitates double-stranded DNA translocation during division and sporulation in E. coli and Bacillus subtilis, respectively. In Pseudomonas aeruginosa, RlpA contributes to rod shape maintenance and daughter cell separation. The separation of daughter cells requires extensive PG remodeling. It has been suggested that amidases and RlpA work in tandem to degrade PG in the division septum and lateral wall to facilitate daughter cell separation.


Pssm-ID: 439248 [Multi-domain]  Cd Length: 92  Bit Score: 164.93  E-value: 3.58e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966513662  94 RGMASWYGTKFHSRRTSSGDDYDMYAMTAAHKTLPLPSYVRVKNLSNGREAIVKVNDRGPFHADRVIDLSYAAATKLGLL 173
Cdd:cd22268    2 TGKASWYGPGFHGRRTASGERYDPNALTAAHKTLPFGTKVRVTNLENGKSVVVRVNDRGPFVKGRIIDLSYAAAKKLGML 81

                         90
                 ....*....|
gi 966513662 174 PKGTAPVEIE 183
Cdd:cd22268   82 GAGVAPVRIE 91
rlpA TIGR00413
rare lipoprotein A; This is a family of prokaryotic proteins with unknown function. ...
 95-245 1.66e-43

rare lipoprotein A; This is a family of prokaryotic proteins with unknown function. Lipoprotein annotation based on the presence of consensus lipoprotein signal sequence. Included in this family is the E. coli putative lipoprotein rlpA. [Cell envelope, Other]


Pssm-ID: 273065 [Multi-domain]  Cd Length: 208  Bit Score: 146.67  E-value: 1.66e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966513662   95 GMASWYGTKFHSRRTSSGDDYDMYAMTAAHKTLPLPSYVRVKNLSNGREAIVKVNDRGPFHADRVIDLSYAAATKLGLLP 174
Cdd:TIGR00413   1 GLASWYGPKFHGRKTANGEVYNMKALTAAHKTLPFNTYVKVTNLHNNRSVIVRINDRGPFSDDRIIDLSHAAAREIGLIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966513662  175 KGTAPVEIEAL----------------------------------TVKSPGGQHVA------YYYVQAGAFNSQDLANAL 214
Cdd:TIGR00413  81 RGVGQVRIEVLhvakngnlsgaatktfnkqakkqeakdrlvlesnTLFDNTKKSINalkgteFFCLQMGELRSRSQANKL 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 966513662  215 REKLAKLTPSPVfIENYQHRYIVRVGPFANK 245
Cdd:TIGR00413 161 ITQLALANLQTE-VNRSGPKYEVYIGPFDDK 190
PRK10672 PRK10672
endolytic peptidoglycan transglycosylase RlpA;
35-191 5.00e-39

endolytic peptidoglycan transglycosylase RlpA;


Pssm-ID: 236733 [Multi-domain]  Cd Length: 361  Bit Score: 139.43  E-value: 5.00e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966513662  35 PKKPFTPTQQDGAPKGPLpKTFQKVKPANEPLSRYGNPDsYAVNGRKYEVMRSASGYKTRGMASWYGTKFHSRRTSSGDD 114
Cdd:PRK10672  23 GQQQTVSAPQPAVCNGPV-VEISGAEPRYEPYNPTANQD-YQRNGKSYKIVQDPSNFSQAGLAAIYDAEAGSNLTASGER 100

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966513662 115 YDMYAMTAAHKTLPLPSYVRVKNLSNGREAIVKVNDRGPFHADRVIDLSYAAATKLGLLPkgTAPVEIEALTVKSPG 191
Cdd:PRK10672 101 FDPNALTAAHPTLPIPSYVRVTNLANGRMIVVRINDRGPYGPGRVIDLSRAAADRLNTSN--NTKVRIDPIIVAPDG 175
DPBB_1 pfam03330
Lytic transglycolase; Rare lipoprotein A (RlpA) contains a conserved region that has the ...
 93-182 7.15e-30

Lytic transglycolase; Rare lipoprotein A (RlpA) contains a conserved region that has the double-psi beta-barrel (DPBB) fold. The function of RlpA is not well understood, but it has been shown to act as a prc mutant suppressor in Escherichia coli. The DPBB fold is often an enzymatic domain. The members of this family are quite diverse, and if catalytic this family may contain several different functions. Another example of this domain is found in the N terminus of pollen allergen. Recent studies show that the full-length RlpA protein from Pseudomonas Aeruginosa is an outer membrane protein that is a lytic transglycolase with specificity for peptidoglycan lacking stem peptides. Residue D157 in UniProtKB:Q9X6V6 is critical for lytic activity.


Pssm-ID: 427248 [Multi-domain]  Cd Length: 82  Bit Score: 107.29  E-value: 7.15e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966513662   93 TRGMASWYGtkfhsRRTSSGDDYDMYAMTAAHKTLPLPSYVRVKNlsnGREAIVKVNDRGPFHADRVIDLSYAAATKLGL 172
Cdd:pfam03330   1 AAGSASLYN-----NGTACGECYDVRCLTAAHPTLPFGTYCRVLS---GRSVIVRITDRGPFPPGRHFDLSGAAFEKLAM 72

                          90
                  ....*....|
gi 966513662  173 LPKGTAPVEI 182
Cdd:pfam03330  73 PRAGIVPVQY 82
SPOR pfam05036
SPOR domain; Bacterial SPOR domains bind peptidoglycan (PG) and target proteins to the cell ...
 197-264 1.88e-11

SPOR domain; Bacterial SPOR domains bind peptidoglycan (PG) and target proteins to the cell division site by binding to denuded glycan strands that lack stem peptides. This 70 residue domain is composed of two 35 residue repeats found in proteins involved in sporulation and cell division such as FtsN, DedD, and CwlM. This domain is involved in binding peptidoglycan. Two tandem repeats fold into a pseudo-2-fold symmetric single-domain structure containing numerous contacts between the repeats. FtsN is an essential cell division protein with a simple bitopic topology, a short N-terminal cytoplasmic segment fused to a large carboxy periplasmic domain through a single transmembrane domain. These repeats lay at the periplasmic C-terminus. FtsN localizes to the septum ring complex.


Pssm-ID: 461531 [Multi-domain]  Cd Length: 76  Bit Score: 58.53  E-value: 1.88e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966513662  197 YYYVQAGAFNSQDLANALREKLAKL--TPSPVFIENYQHRYIVRVGPFANKAMTESLKMRLAANGVKGSF 264
Cdd:pfam05036   4 GYYVQLGAFSNEANAEALAAKLRAKgfAAYVAVTSKGGGLYRVRVGPFASREEARAALKKLKALAGLSPF 73
FtsN COG3087
Cell division protein FtsN [Cell cycle control, cell division, chromosome partitioning];
95-264 4.49e-11

Cell division protein FtsN [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442321 [Multi-domain]  Cd Length: 198  Bit Score: 60.80  E-value: 4.49e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966513662  95 GMASWYGTKFHSRRTSSGDDYDMYAMTAAHKTLPLPSYVRVKNLSNGREAIVKVNDRGPFHADRVIDLSYAAATKLGLLP 174
Cdd:COG3087   15 LLLELSAEAAAAASDNLRLAAGSAAAPALAEDALVASAAKAGLAETGAKAGAILAAAALAALNAAAAALAAASAAAAAAA 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966513662 175 KGTAPVEIEALTV-------KSPGGQHVAYYYVQAGAFNSQDLANALREKLAKLTpSPVFIE----NYQHRYIVRVGPFA 243
Cdd:COG3087   95 APAAAAAEAAAAPagmakkeAAAAPAAKKPYYVQVGAFRSRANAERLRARLALLG-LEARVVevevGGGTWYRVRVGPFS 173

                        170       180
                 ....*....|....*....|.
gi 966513662 244 NKAMTESLKMRLAANGVKGSF 264
Cdd:COG3087  174 SRAEAEKAREKLKAAGIDALV 194
DedD COG3147
Cell division protein DedD (periplasmic protein involved in septation) [Cell cycle control, ...
 165-262 3.44e-08

Cell division protein DedD (periplasmic protein involved in septation) [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442381 [Multi-domain]  Cd Length: 140  Bit Score: 51.31  E-value: 3.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966513662 165 AAATKLGLLPKGTAPVEIEALT----VKSPGGQHvayYYVQAGAFNSQDLANALREKLAKLTpSPVFIENYQH----RYI 236
Cdd:COG3147   32 AAAPKPAAKPAAPKPAAAAAAApaakAAAPAGGG---WVVQLGAFSNEDNAKELVAKLRAAG-YPAYTEPVTTgggtLYR 107

                         90       100
                 ....*....|....*....|....*..
gi 966513662 237 VRVGPFANKAMTESLKMRL-AANGVKG 262
Cdd:COG3147  108 VRVGPFASRAEAEAALAKLkKLTGLKG 134
 
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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