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Conserved domains on  [gi|1232327387|gb|OYW06726|]
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hypothetical protein B7Z61_01430 [Acidobacteria bacterium 37-71-11]

Protein Classification

M23 family metallopeptidase( domain architecture ID 11432770)

M23 family metallopeptidase lyses bacterial cell wall peptidoglycans

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NlpD COG0739
Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell ...
 93-288 2.07e-58

Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 440502 [Multi-domain]  Cd Length: 196  Bit Score: 185.56  E-value: 2.07e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327387  93 QRTKALAIAAGVANLFSDTSNPGLGVVGSGGPLNKLAAEPGTLLRRQDQLDKELAKVEQRLSDQAMMLShtPVVAPVVGV 172
Cdd:COG0739     1 AALALALAAALLALALLASAAGAAAAVAAAAAAAAAAAALAAAALAAAVSAAASAAAAAAAAAAAIALG--SGAWPVKGR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327387 173 ITDGFGPRMDPITHKPAFHDGLDISVAYGTVVTAPADGVVVYAARDAGYGRLLKINHGYGYTTMYGHLDRFLVKEGAHVT 252
Cdd:COG0739    79 ITSGFGYRRHPVTGRRRFHKGIDIAAPTGTPVYAAADGTVVFAGWNGGYGNLVIIDHGNGYTTLYAHLSSILVKVGQRVK 158

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1232327387 253 RGEPIGKVGMSGRTTGPHLHYEVWKDGEKENPLYYI 288
Cdd:COG0739   159 AGQVIGYVGNTGRSTGPHLHFEVRVNGKPVDPLPFL 194
 
Name Accession Description Interval E-value
NlpD COG0739
Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell ...
 93-288 2.07e-58

Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440502 [Multi-domain]  Cd Length: 196  Bit Score: 185.56  E-value: 2.07e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327387  93 QRTKALAIAAGVANLFSDTSNPGLGVVGSGGPLNKLAAEPGTLLRRQDQLDKELAKVEQRLSDQAMMLShtPVVAPVVGV 172
Cdd:COG0739     1 AALALALAAALLALALLASAAGAAAAVAAAAAAAAAAAALAAAALAAAVSAAASAAAAAAAAAAAIALG--SGAWPVKGR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327387 173 ITDGFGPRMDPITHKPAFHDGLDISVAYGTVVTAPADGVVVYAARDAGYGRLLKINHGYGYTTMYGHLDRFLVKEGAHVT 252
Cdd:COG0739    79 ITSGFGYRRHPVTGRRRFHKGIDIAAPTGTPVYAAADGTVVFAGWNGGYGNLVIIDHGNGYTTLYAHLSSILVKVGQRVK 158

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1232327387 253 RGEPIGKVGMSGRTTGPHLHYEVWKDGEKENPLYYI 288
Cdd:COG0739   159 AGQVIGYVGNTGRSTGPHLHFEVRVNGKPVDPLPFL 194
Peptidase_M23 pfam01551
Peptidase family M23; Members of this family are zinc metallopeptidases with a range of ...
 190-284 5.64e-43

Peptidase family M23; Members of this family are zinc metallopeptidases with a range of specificities. The peptidase family M23 is included in this family, these are Gly-Gly endopeptidases. Peptidase family M23 are also endopeptidases. This family also includes some bacterial lipoproteins such as Swiss:P33648 for which no proteolytic activity has been demonstrated. This family also includes leukocyte cell-derived chemotaxin 2 (LECT2) proteins. LECT2 is a liver-specific protein which is thought to be linked to hepatocyte growth although the exact function of this protein is unknown.


Pssm-ID: 460250 [Multi-domain]  Cd Length: 96  Bit Score: 142.30  E-value: 5.64e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327387 190 FHDGLDISVAYGTVVTAPADGVVVYAARDAGYGRLLKINHGYGYTTMYGHLDRFLVKEGAHVTRGEPIGKVGMSGRTTGP 269
Cdd:pfam01551   2 FHKGIDIAAPTGTPVYAAADGVVVFAGWLGGYGNLVIIDHGNGYSTLYAHLSSILVKVGQRVKAGQVIGTVGSTGRSTGP 81

                          90
                  ....*....|....*
gi 1232327387 270 HLHYEVWKDGEKENP 284
Cdd:pfam01551  82 HLHFEIRKNGKPVDP 96
M23_peptidase cd12797
M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; ...
 191-275 3.09e-38

M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; This model describes the metallopeptidase M23 family, which includes beta-lytic metallopeptidase and lysostaphin. Members of this family are zinc endopeptidases that lyse bacterial cell wall peptidoglycans; they cleave either the N-acylmuramoyl-Ala bond between the cell wall peptidoglycan and the cross-linking peptide (e.g. beta-lytic endopeptidase) or a bond within the cross-linking peptide (e.g. stapholysin, and lysostaphin). Beta-lytic metallopeptidase, formerly known as beta-lytic protease, has a preference for cleavage of Gly-X bonds and favors hydrophobic or apolar residues on either side. It inhibits growth of sensitive organisms and may potentially serve as an antimicrobial agent. Lysostaphin, produced by Staphylococcus genus, cleaves pentaglycine cross-bridges of cell wall peptidoglycan, acting as autolysins to maintain cell wall metabolism or as toxins and weapons against competing strains. Staphylolysin (also known as LasA) is implicated in a range of processes related to Pseudomonas virulence, including stimulating shedding of the ectodomain of cell surface heparan sulphate proteoglycan syndecan-1, and elastin degradation in connective tissue. Its active site is less constricted and contains a five-coordinate zinc ion with trigonal bipyramidal geometry and two metal-bound water molecules, possibly contributing to its activity against a wider range of substrates than those used by related lytic enzymes, consistent with its multiple roles in Pseudomonas virulence. The family includes members that do not appear to have the conserved zinc-binding site and might be lipoproteins lacking proteolytic activity.


Pssm-ID: 410984 [Multi-domain]  Cd Length: 85  Bit Score: 129.63  E-value: 3.09e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327387 191 HDGLDISVAYGTVVTAPADGVVVYAARDAGYGRLLKINHGYGYTTMYGHLDRFLVKEGAHVTRGEPIGKVGMSGRTTGPH 270
Cdd:cd12797     1 HNGIDIAAPEGTPVYAAADGTVVFAGWDGGYGNYVIIDHGNGYYTLYAHLSSILVKVGQRVKKGQVIGTVGNTGRSTGPH 80


                  ....*
gi 1232327387 271 LHYEV 275
Cdd:cd12797    81 LHFEI 85
PRK11649 PRK11649
putative peptidase; Provisional
 173-285 2.33e-29

putative peptidase; Provisional


Pssm-ID: 236946 [Multi-domain]  Cd Length: 439  Bit Score: 115.53  E-value: 2.33e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327387 173 ITDGFGP-RMDPITHKPAFHDGLDISVAYGTVVTAPADGVVVYAARDAGYGRLLKINHGYGYTTMYGHLDRFLVKEGAHV 251
Cdd:PRK11649  294 ISSNFNPrRLNPVTGRVAPHRGVDFAMPVGTPVLAVGDGEVVVAKRSGAAGNYVAIRHGRQYTTRYMHLRKLLVKPGQKV 373

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1232327387 252 TRGEPIGKVGMSGRTTGPHLHYEVWKDGEKENPL 285
Cdd:PRK11649  374 KRGDRIALSGNTGRSTGPHLHYEVWINQQAVNPL 407
 
Name Accession Description Interval E-value
NlpD COG0739
Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell ...
 93-288 2.07e-58

Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440502 [Multi-domain]  Cd Length: 196  Bit Score: 185.56  E-value: 2.07e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327387  93 QRTKALAIAAGVANLFSDTSNPGLGVVGSGGPLNKLAAEPGTLLRRQDQLDKELAKVEQRLSDQAMMLShtPVVAPVVGV 172
Cdd:COG0739     1 AALALALAAALLALALLASAAGAAAAVAAAAAAAAAAAALAAAALAAAVSAAASAAAAAAAAAAAIALG--SGAWPVKGR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327387 173 ITDGFGPRMDPITHKPAFHDGLDISVAYGTVVTAPADGVVVYAARDAGYGRLLKINHGYGYTTMYGHLDRFLVKEGAHVT 252
Cdd:COG0739    79 ITSGFGYRRHPVTGRRRFHKGIDIAAPTGTPVYAAADGTVVFAGWNGGYGNLVIIDHGNGYTTLYAHLSSILVKVGQRVK 158

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1232327387 253 RGEPIGKVGMSGRTTGPHLHYEVWKDGEKENPLYYI 288
Cdd:COG0739   159 AGQVIGYVGNTGRSTGPHLHFEVRVNGKPVDPLPFL 194
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 43-288 6.56e-50

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 169.17  E-value: 6.56e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327387  43 AIVSLVASGSFLRQR-AMYRSLQSENKQLKKNNQRLEETVGQVQVRLTQFEQRTKALAIA-----AGVANLFSDtsnpgl 116
Cdd:COG4942   134 AVRRLQYLKYLAPARrEQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALkaerqKLLARLEKE------ 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327387 117 gvvgsggpLNKLAAEPGTLLRRQDQLDKELAKVEQRLSDQAMMLSHTPVVA-------PVVGVITDGFGPRmDPITHkpa 189
Cdd:COG4942   208 --------LAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAAlkgklpwPVSGRVVRRFGER-DGGGG--- 275

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327387 190 FHDGLDISVAYGTVVTAPADGVVVYAARDAGYGRLLKINHGYGYTTMYGHLDRFLVKEGAHVTRGEPIGKVGMSGRTTGP 269
Cdd:COG4942   276 RNKGIDIAAPPGAPVRAVADGTVVYAGWLRGYGNLVIIDHGGGYLTLYAHLSSLLVKVGQRVKAGQPIGTVGSSGGQGGP 355

                         250
                  ....*....|....*....
gi 1232327387 270 HLHYEVWKDGEKENPLYYI 288
Cdd:COG4942   356 TLYFELRKNGKPVDPLPWL 374
Peptidase_M23 pfam01551
Peptidase family M23; Members of this family are zinc metallopeptidases with a range of ...
 190-284 5.64e-43

Peptidase family M23; Members of this family are zinc metallopeptidases with a range of specificities. The peptidase family M23 is included in this family, these are Gly-Gly endopeptidases. Peptidase family M23 are also endopeptidases. This family also includes some bacterial lipoproteins such as Swiss:P33648 for which no proteolytic activity has been demonstrated. This family also includes leukocyte cell-derived chemotaxin 2 (LECT2) proteins. LECT2 is a liver-specific protein which is thought to be linked to hepatocyte growth although the exact function of this protein is unknown.


Pssm-ID: 460250 [Multi-domain]  Cd Length: 96  Bit Score: 142.30  E-value: 5.64e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327387 190 FHDGLDISVAYGTVVTAPADGVVVYAARDAGYGRLLKINHGYGYTTMYGHLDRFLVKEGAHVTRGEPIGKVGMSGRTTGP 269
Cdd:pfam01551   2 FHKGIDIAAPTGTPVYAAADGVVVFAGWLGGYGNLVIIDHGNGYSTLYAHLSSILVKVGQRVKAGQVIGTVGSTGRSTGP 81

                          90
                  ....*....|....*
gi 1232327387 270 HLHYEVWKDGEKENP 284
Cdd:pfam01551  82 HLHFEIRKNGKPVDP 96
M23_peptidase cd12797
M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; ...
 191-275 3.09e-38

M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; This model describes the metallopeptidase M23 family, which includes beta-lytic metallopeptidase and lysostaphin. Members of this family are zinc endopeptidases that lyse bacterial cell wall peptidoglycans; they cleave either the N-acylmuramoyl-Ala bond between the cell wall peptidoglycan and the cross-linking peptide (e.g. beta-lytic endopeptidase) or a bond within the cross-linking peptide (e.g. stapholysin, and lysostaphin). Beta-lytic metallopeptidase, formerly known as beta-lytic protease, has a preference for cleavage of Gly-X bonds and favors hydrophobic or apolar residues on either side. It inhibits growth of sensitive organisms and may potentially serve as an antimicrobial agent. Lysostaphin, produced by Staphylococcus genus, cleaves pentaglycine cross-bridges of cell wall peptidoglycan, acting as autolysins to maintain cell wall metabolism or as toxins and weapons against competing strains. Staphylolysin (also known as LasA) is implicated in a range of processes related to Pseudomonas virulence, including stimulating shedding of the ectodomain of cell surface heparan sulphate proteoglycan syndecan-1, and elastin degradation in connective tissue. Its active site is less constricted and contains a five-coordinate zinc ion with trigonal bipyramidal geometry and two metal-bound water molecules, possibly contributing to its activity against a wider range of substrates than those used by related lytic enzymes, consistent with its multiple roles in Pseudomonas virulence. The family includes members that do not appear to have the conserved zinc-binding site and might be lipoproteins lacking proteolytic activity.


Pssm-ID: 410984 [Multi-domain]  Cd Length: 85  Bit Score: 129.63  E-value: 3.09e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327387 191 HDGLDISVAYGTVVTAPADGVVVYAARDAGYGRLLKINHGYGYTTMYGHLDRFLVKEGAHVTRGEPIGKVGMSGRTTGPH 270
Cdd:cd12797     1 HNGIDIAAPEGTPVYAAADGTVVFAGWDGGYGNYVIIDHGNGYYTLYAHLSSILVKVGQRVKKGQVIGTVGNTGRSTGPH 80


                  ....*
gi 1232327387 271 LHYEV 275
Cdd:cd12797    81 LHFEI 85
SpoIIQ2 COG5821
Stage II sporulation protein SpoIIQ, clostridial version, metallopeptidase M23 family [Cell ...
 166-288 3.80e-34

Stage II sporulation protein SpoIIQ, clostridial version, metallopeptidase M23 family [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444523 [Multi-domain]  Cd Length: 200  Bit Score: 122.83  E-value: 3.80e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327387 166 VAPVVGVITDGFGPRM--DPITHKPAFHDGLDISVAYGTVVTAPADGVVVYAARDAGYGRLLKINHGYGYTTMYGHLD-R 242
Cdd:COG5821    70 LKPVSGKITREFGEDLvySKTLNEWRTHTGIDIAAKEGTPVKAAADGVVVEVGKDPKYGITVVIDHGNGIKTVYANLDsK 149

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1232327387 243 FLVKEGAHVTRGEPIGKVGMSGRT---TGPHLHYEVWKDGEKENPLYYI 288
Cdd:COG5821   150 IKVKVGQKVKKGQVIGKVGSTALFessEGPHLHFEVLKNGKPVDPMKYL 198
PRK11649 PRK11649
putative peptidase; Provisional
 173-285 2.33e-29

putative peptidase; Provisional


Pssm-ID: 236946 [Multi-domain]  Cd Length: 439  Bit Score: 115.53  E-value: 2.33e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327387 173 ITDGFGP-RMDPITHKPAFHDGLDISVAYGTVVTAPADGVVVYAARDAGYGRLLKINHGYGYTTMYGHLDRFLVKEGAHV 251
Cdd:PRK11649  294 ISSNFNPrRLNPVTGRVAPHRGVDFAMPVGTPVLAVGDGEVVVAKRSGAAGNYVAIRHGRQYTTRYMHLRKLLVKPGQKV 373

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1232327387 252 TRGEPIGKVGMSGRTTGPHLHYEVWKDGEKENPL 285
Cdd:PRK11649  374 KRGDRIALSGNTGRSTGPHLHYEVWINQQAVNPL 407
nlpD PRK10871
murein hydrolase activator NlpD;
193-288 3.89e-14

murein hydrolase activator NlpD;


Pssm-ID: 236782 [Multi-domain]  Cd Length: 319  Bit Score: 71.40  E-value: 3.89e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327387 193 GLDISVAYGTVVTAPADGVVVYAARD-AGYGRLLKINHGYGYTTMYGHLDRFLVKEGAHVTRGEPIGKVGMSGrTTGPHL 271
Cdd:PRK10871  221 GIDIAGSKGQAIIATADGRVVYAGNAlRGYGNLIIIKHNDDYLSAYAHNDTMLVREQQEVKAGQKIATMGSTG-TSSTRL 299

                          90
                  ....*....|....*..
gi 1232327387 272 HYEVWKDGEKENPLYYI 288
Cdd:PRK10871  300 HFEIRYKGKSVNPLRYL 316
SpoIVFA COG5833
Stage IV sporulation protein SpoIVFA, regulates SpoIVFB [Cell cycle control, cell division, ...
 163-280 1.20e-13

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


Pssm-ID: 444535 [Multi-domain]  Cd Length: 219  Bit Score: 68.48  E-value: 1.20e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327387 163 TPVVAPVVGVITDGFGprMDpithkpafHDGLDISVAYGTVVTAPADGVVVYAARDAGYGRLLKINHGYGYTTMYGHLDR 242
Cdd:COG5833   102 EAFALPVSGKVVESFQ--EN--------GKGVDIETPGGANVKAVKEGYVIFAGKDEETGKTVIIQHADGSESWYGNLSS 171

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1232327387 243 FLVKEGAHVTRGEPIGKVGMSGRTTGpHLHYEVWKDGE 280
Cdd:COG5833   172 IDVKLYDFVEAGQKIGTVPATEGEEG-TFYFAIKKGGK 208
PRK11637 PRK11637
AmiB activator; Provisional
 193-285 4.85e-13

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 68.57  E-value: 4.85e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327387 193 GLDISVAYGTVVTAPADGVVVYAARDAGYGRLLKINHGYGYTTMYGHLDRFLVKEGAHVTRGEPIGKVGMSGRTTGPHLH 272
Cdd:PRK11637  331 GMVIGASEGTEVKAIADGRVLLADWLQGYGLVVVVEHGKGDMSLYGYNQSALVSVGAQVRAGQPIALVGSSGGQGRPSLY 410

                          90
                  ....*....|...
gi 1232327387 273 YEVWKDGEKENPL 285
Cdd:PRK11637  411 FEIRRQGQAVNPQ 423
PRK06148 PRK06148
hypothetical protein; Provisional
 191-275 1.49e-10

hypothetical protein; Provisional


Pssm-ID: 180426 [Multi-domain]  Cd Length: 1013  Bit Score: 61.58  E-value: 1.49e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327387  191 HDGLDISVAYGTVVTAPADGVVVYAARDA---GYGRLLKINH----GYGYTTMYGHLDRFLV---KEGAHVTRGEPIGKV 260
Cdd:PRK06148   441 HLGVDLFAPAGTPVYAPLAGTVRSVEIEAvplGYGGLVALEHetpgGDPFYTLYGHLAHEAVsrlKPGDRLAAGELFGAM 520

                           90
                   ....*....|....*..
gi 1232327387  261 GMSGRTTG--PHLHYEV 275
Cdd:PRK06148   521 GDAHENGGwaPHLHFQL 537
OapA COG3061
Cell division protein YtfB/OapA (opacity-associated protein A) [Cell cycle control, cell ...
 162-274 3.66e-07

Cell division protein YtfB/OapA (opacity-associated protein A) [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442295 [Multi-domain]  Cd Length: 425  Bit Score: 50.82  E-value: 3.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232327387 162 HTPVVAPVVGVITDGFGPRMDPITHKPAFHDGLDISVAYGTVVTAPADGVVVYAARDAGYGRLLKINHGYGYTTMYGHLD 241
Cdd:COG3061   281 RRGPDAAAPSGSSNAAGGGGHKITRRGGGGGGAAVGVGTGTPTTGAGLGVVRGGRGGGGGVVVGQIGRGGTYGGTGLHLH 360

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1232327387 242 RFLVKEGAHVTRGEPIGKVGMSGRTTGPHLHYE 274
Cdd:COG3061   361 KHGHKGGGVVGQGVTIGTLGGTGPTTGPHLHYE 393
 
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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