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Conserved domains on  [gi|2101302170|ref|WP_223812900|]
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MULTISPECIES: serine protease [unclassified Geobacillus]

Protein Classification

S1 family peptidase( domain architecture ID 10595581)

S1 family peptidase is a serine endopeptidase containing the catalytic triad His, Asp and Ser; such as peroxisomal leader peptide-processing protease

EC:  3.4.21.-
Gene Ontology:  GO:0008236|GO:0008233|GO:0006508|GO:0004252
MEROPS:  S1
PubMed:  9383148|25664608|29785722|31895561|9374470

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
 29-182 7.62e-27

Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational modification, protein turnover, chaperones];


:

Pssm-ID: 440035 [Multi-domain]  Cd Length: 274  Bit Score: 106.39  E-value: 7.62e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101302170  29 LKVILPGGDVLDGEVKSYGAPvnqgKDVAVLKVEGKHLPTLPLGDSDNVQNQDDIWVIGYPaaaesdylspdSSLVSSMN 108
Cdd:COG0265    27 ITVTLADGREYPAKVVGRDPL----TDLAVLKIDAKDLPAAPLGDSDKLRVGDWVLAIGNP-----------FGLGQTVT 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101302170 109 AGHVSATSKKTEQGS-----PVIQIDAAATHGNSGGPVINKRGEMIGLLTF---RGGTvnrqeVQRFNFVVPVNTVKEFV 180
Cdd:COG0265    92 AGIVSALGRSIGSSGggtydDFIQTDAAINPGNSGGPLVNLNGEVIGINTAiisRSGG-----SQGIGFAIPINLAKRVV 166


                  ..
gi 2101302170 181 KQ 182
Cdd:COG0265   167 EQ 168
BamD super family cl34714
Outer membrane protein assembly factor BamD, BamD/ComL family [Cell wall/membrane/envelope ...
 190-241 1.48e-03

Outer membrane protein assembly factor BamD, BamD/ComL family [Cell wall/membrane/envelope biogenesis];


The actual alignment was detected with superfamily member COG4105:

Pssm-ID: 443281 [Multi-domain]  Cd Length: 254  Bit Score: 39.48  E-value: 1.48e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2101302170 190 GSIDTLFREGLTLYWGGYYKDALAKFEAVERLYPGHSEIKR---FITDSQQKSGQ 241
Cdd:COG4105    30 WDAEELYEEAKEALEKGDYEKAIKLFEELEPRYPGSPYAEQaqlMLAYAYYKQGD 84
 
Name Accession Description Interval E-value
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
 29-182 7.62e-27

Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440035 [Multi-domain]  Cd Length: 274  Bit Score: 106.39  E-value: 7.62e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101302170  29 LKVILPGGDVLDGEVKSYGAPvnqgKDVAVLKVEGKHLPTLPLGDSDNVQNQDDIWVIGYPaaaesdylspdSSLVSSMN 108
Cdd:COG0265    27 ITVTLADGREYPAKVVGRDPL----TDLAVLKIDAKDLPAAPLGDSDKLRVGDWVLAIGNP-----------FGLGQTVT 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101302170 109 AGHVSATSKKTEQGS-----PVIQIDAAATHGNSGGPVINKRGEMIGLLTF---RGGTvnrqeVQRFNFVVPVNTVKEFV 180
Cdd:COG0265    92 AGIVSALGRSIGSSGggtydDFIQTDAAINPGNSGGPLVNLNGEVIGINTAiisRSGG-----SQGIGFAIPINLAKRVV 166


                  ..
gi 2101302170 181 KQ 182
Cdd:COG0265   167 EQ 168
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
 29-151 4.19e-18

Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 79.39  E-value: 4.19e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101302170  29 LKVILPGGDVLDGEVksygAPVNQGKDVAVLKV--EGKHLPTLPLGDSDNVQNQDDIWVIGYPAAAESdylspdsslvSS 106
Cdd:pfam13365  30 VSVVLADGREYPATV----VARDPDLDLALLRVsgDGRGLPPLPLGDSEPLVGGERVYAVGYPLGGEK----------LS 95

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2101302170 107 MNAGHVSATSKKTEQ--GSPVIQIDAAATHGNSGGPVINKRGEMIGL 151
Cdd:pfam13365  96 LSEGIVSGVDEGRDGgdDGRVIQTDAALSPGSSGGPVFDADGRVVGI 142
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
 54-183 1.10e-16

periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various designated DegP, heat shock protein HtrA, and protease DO. The ortholog in Pseudomonas aeruginosa is designated MucD and is found in an operon that controls mucoid phenotype. This family also includes the DegQ (HhoA) paralog in E. coli which can rescue a DegP mutant, but not the smaller DegS paralog, which cannot. Members of this family are located in the periplasm and have separable functions as both protease and chaperone. Members have a trypsin domain and two copies of a PDZ domain. This protein protects bacteria from thermal and other stresses and may be important for the survival of bacterial pathogens.// The chaperone function is dominant at low temperatures, whereas the proteolytic activity is turned on at elevated temperatures. [Protein fate, Protein folding and stabilization, Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 273938 [Multi-domain]  Cd Length: 428  Bit Score: 80.34  E-value: 1.10e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101302170  54 KDVAVLKVEGKH-LPTLPLGDSDNVQNQDdiWV--IGYPAAaesdylspdssLVSSMNAGHVSATSKKT---EQGSPVIQ 127
Cdd:TIGR02037 105 TDIAVLKIDAKKnLPVIKLGDSDKLRVGD--WVlaIGNPFG-----------LGQTVTSGIVSALGRSGlgiGDYENFIQ 171

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101302170 128 IDAAATHGNSGGPVINKRGEMIGLLTF----RGGTVNrqevqrFNFVVPVNTVKEFVKQA 183
Cdd:TIGR02037 172 TDAAINPGNSGGPLVNLRGEVIGINTAilspSGGNVG------IGFAIPSNMAKNVVDQL 225
PRK10942 PRK10942
serine endoprotease DegP;
55-182 1.27e-07

serine endoprotease DegP;


Pssm-ID: 236802 [Multi-domain]  Cd Length: 473  Bit Score: 52.85  E-value: 1.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101302170  55 DVAVLKVEG-KHLPTLPLGDSDNVQNQDDIWVIGYPAAaesdylspdssLVSSMNAGHVSATSK---KTEQGSPVIQIDA 130
Cdd:PRK10942  160 DIALIQLQNpKNLTAIKMADSDALRVGDYTVAIGNPYG-----------LGETVTSGIVSALGRsglNVENYENFIQTDA 228

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2101302170 131 AATHGNSGGPVINKRGEMIGL----LTFRGGTVNrqevqrFNFVVPVNTVKEFVKQ 182
Cdd:PRK10942  229 AINRGNSGGALVNLNGELIGIntaiLAPDGGNIG------IGFAIPSNMVKNLTSQ 278
BamD COG4105
Outer membrane protein assembly factor BamD, BamD/ComL family [Cell wall/membrane/envelope ...
 190-241 1.48e-03

Outer membrane protein assembly factor BamD, BamD/ComL family [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443281 [Multi-domain]  Cd Length: 254  Bit Score: 39.48  E-value: 1.48e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2101302170 190 GSIDTLFREGLTLYWGGYYKDALAKFEAVERLYPGHSEIKR---FITDSQQKSGQ 241
Cdd:COG4105    30 WDAEELYEEAKEALEKGDYEKAIKLFEELEPRYPGSPYAEQaqlMLAYAYYKQGD 84
OM_YfiO TIGR03302
outer membrane assembly lipoprotein YfiO; Members of this protein family include YfiO, a ...
 191-224 5.49e-03

outer membrane assembly lipoprotein YfiO; Members of this protein family include YfiO, a near-essential protein of the outer membrane, part of a complex involved in protein insertion into the bacterial outer membrane. Many proteins in this family are annotated as ComL, based on the involvement of this protein in natural transformation with exogenous DNA in Neisseria gonorrhoeae. This protein family shows sequence similarity to, but is distinct from, the tol-pal system protein YbgF (TIGR02795). [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 274513 [Multi-domain]  Cd Length: 235  Bit Score: 37.53  E-value: 5.49e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2101302170 191 SIDTLFREGLTLYWGGYYKDALAKFEAVERLYPG 224
Cdd:TIGR03302  32 PAEELYEEAKEALDSGDYTEAIKYFEALESRYPF 65
 
Name Accession Description Interval E-value
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
 29-182 7.62e-27

Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440035 [Multi-domain]  Cd Length: 274  Bit Score: 106.39  E-value: 7.62e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101302170  29 LKVILPGGDVLDGEVKSYGAPvnqgKDVAVLKVEGKHLPTLPLGDSDNVQNQDDIWVIGYPaaaesdylspdSSLVSSMN 108
Cdd:COG0265    27 ITVTLADGREYPAKVVGRDPL----TDLAVLKIDAKDLPAAPLGDSDKLRVGDWVLAIGNP-----------FGLGQTVT 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101302170 109 AGHVSATSKKTEQGS-----PVIQIDAAATHGNSGGPVINKRGEMIGLLTF---RGGTvnrqeVQRFNFVVPVNTVKEFV 180
Cdd:COG0265    92 AGIVSALGRSIGSSGggtydDFIQTDAAINPGNSGGPLVNLNGEVIGINTAiisRSGG-----SQGIGFAIPINLAKRVV 166


                  ..
gi 2101302170 181 KQ 182
Cdd:COG0265   167 EQ 168
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
 29-151 4.19e-18

Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 79.39  E-value: 4.19e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101302170  29 LKVILPGGDVLDGEVksygAPVNQGKDVAVLKV--EGKHLPTLPLGDSDNVQNQDDIWVIGYPAAAESdylspdsslvSS 106
Cdd:pfam13365  30 VSVVLADGREYPATV----VARDPDLDLALLRVsgDGRGLPPLPLGDSEPLVGGERVYAVGYPLGGEK----------LS 95

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2101302170 107 MNAGHVSATSKKTEQ--GSPVIQIDAAATHGNSGGPVINKRGEMIGL 151
Cdd:pfam13365  96 LSEGIVSGVDEGRDGgdDGRVIQTDAALSPGSSGGPVFDADGRVVGI 142
degP_htrA_DO TIGR02037
periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various ...
 54-183 1.10e-16

periplasmic serine protease, Do/DeqQ family; This family consists of a set proteins various designated DegP, heat shock protein HtrA, and protease DO. The ortholog in Pseudomonas aeruginosa is designated MucD and is found in an operon that controls mucoid phenotype. This family also includes the DegQ (HhoA) paralog in E. coli which can rescue a DegP mutant, but not the smaller DegS paralog, which cannot. Members of this family are located in the periplasm and have separable functions as both protease and chaperone. Members have a trypsin domain and two copies of a PDZ domain. This protein protects bacteria from thermal and other stresses and may be important for the survival of bacterial pathogens.// The chaperone function is dominant at low temperatures, whereas the proteolytic activity is turned on at elevated temperatures. [Protein fate, Protein folding and stabilization, Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 273938 [Multi-domain]  Cd Length: 428  Bit Score: 80.34  E-value: 1.10e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101302170  54 KDVAVLKVEGKH-LPTLPLGDSDNVQNQDdiWV--IGYPAAaesdylspdssLVSSMNAGHVSATSKKT---EQGSPVIQ 127
Cdd:TIGR02037 105 TDIAVLKIDAKKnLPVIKLGDSDKLRVGD--WVlaIGNPFG-----------LGQTVTSGIVSALGRSGlgiGDYENFIQ 171

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101302170 128 IDAAATHGNSGGPVINKRGEMIGLLTF----RGGTVNrqevqrFNFVVPVNTVKEFVKQA 183
Cdd:TIGR02037 172 TDAAINPGNSGGPLVNLRGEVIGINTAilspSGGNVG------IGFAIPSNMAKNVVDQL 225
PRK10942 PRK10942
serine endoprotease DegP;
55-182 1.27e-07

serine endoprotease DegP;


Pssm-ID: 236802 [Multi-domain]  Cd Length: 473  Bit Score: 52.85  E-value: 1.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101302170  55 DVAVLKVEG-KHLPTLPLGDSDNVQNQDDIWVIGYPAAaesdylspdssLVSSMNAGHVSATSK---KTEQGSPVIQIDA 130
Cdd:PRK10942  160 DIALIQLQNpKNLTAIKMADSDALRVGDYTVAIGNPYG-----------LGETVTSGIVSALGRsglNVENYENFIQTDA 228

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2101302170 131 AATHGNSGGPVINKRGEMIGL----LTFRGGTVNrqevqrFNFVVPVNTVKEFVKQ 182
Cdd:PRK10942  229 AINRGNSGGALVNLNGELIGIntaiLAPDGGNIG------IGFAIPSNMVKNLTSQ 278
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 43-160 5.33e-07

V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 49.29  E-value: 5.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101302170  43 VKSYGAPVNQGKDVAVLKVE---GKHLPTLPLGDSDNVQNQDDIWVIGYPAaaesdylspDSSLVSSM-NAGHVsatskk 118
Cdd:COG3591    65 PPGWVASGDAGYDYALLRLDeplGDTTGWLGLAFNDAPLAGEPVTIIGYPG---------DRPKDLSLdCSGRV------ 129

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2101302170 119 TEQGSPVIQIDAAATHGNSGGPVINK---RGEMIGLLTFRGGTVN 160
Cdd:COG3591   130 TGVQGNRLSYDCDTTGGSSGSPVLDDsdgGGRVVGVHSAGGADRA 174
Trypsin pfam00089
Trypsin;
49-180 2.19e-06

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 47.82  E-value: 2.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101302170  49 PVNQGKDVAVLKVE-----GKHLPTLPLGD-SDNVQNQDDIWVIGYPAAAESDYlspdSSLVSSMNAGHVSATSKKTEQG 122
Cdd:pfam00089  82 PDTLDNDIALLKLEspvtlGDTVRPICLPDaSSDLPVGTTCTVSGWGNTKTLGP----SDTLQEVTVPVVSRETCRSAYG 157

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2101302170 123 SPV----IQIDA---AATHGNSGGPVINKRGEMIGLLTFrGGTVNRQEvqRFNFVVPVNTVKEFV 180
Cdd:pfam00089 158 GTVtdtmICAGAggkDACQGDSGGPLVCSDGELIGIVSW-GYGCASGN--YPGVYTPVSSYLDWI 219
PRK10898 PRK10898
serine endoprotease DegS;
55-154 2.79e-06

serine endoprotease DegS;


Pssm-ID: 182820 [Multi-domain]  Cd Length: 353  Bit Score: 48.46  E-value: 2.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101302170  55 DVAVLKVEGKHLPTLPLGDSDNVQNQDDIWVIGYPaaaesdYlspdsSLVSSMNAGHVSATSKKTEqgSPV-----IQID 129
Cdd:PRK10898  126 DLAVLKINATNLPVIPINPKRVPHIGDVVLAIGNP------Y-----NLGQTITQGIISATGRIGL--SPTgrqnfLQTD 192

                          90       100
                  ....*....|....*....|....*..
gi 2101302170 130 AAATHGNSGGPVINKRGEMIGL--LTF 154
Cdd:PRK10898  193 ASINHGNSGGALVNSLGELMGIntLSF 219
PRK10139 PRK10139
serine endoprotease DegQ;
6-182 1.57e-05

serine endoprotease DegQ;


Pssm-ID: 182262 [Multi-domain]  Cd Length: 455  Bit Score: 46.48  E-value: 1.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101302170   6 GVDFDIAYDYMIEYTLYTNVTRGLKVILPGGDVLDGevKSYGApvNQGKDVAVLKVEG-KHLPTLPLGDSDNVQNQDDIW 84
Cdd:PRK10139   94 GVIIDAAKGYVLTNNHVINQAQKISIQLNDGREFDA--KLIGS--DDQSDIALLQIQNpSKLTQIAIADSDKLRVGDFAV 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2101302170  85 VIGYPAAaesdylspdssLVSSMNAGHVSATSK---KTEQGSPVIQIDAAATHGNSGGPVINKRGEMIG----LLTFRGG 157
Cdd:PRK10139  170 AVGNPFG-----------LGQTATSGIISALGRsglNLEGLENFIQTDASINRGNSGGALLNLNGELIGintaILAPGGG 238

                         170       180
                  ....*....|....*....|....*
gi 2101302170 158 TVNrqevqrFNFVVPVNTVKEFVKQ 182
Cdd:PRK10139  239 SVG------IGFAIPSNMARTLAQQ 257
BamD COG4105
Outer membrane protein assembly factor BamD, BamD/ComL family [Cell wall/membrane/envelope ...
 190-241 1.48e-03

Outer membrane protein assembly factor BamD, BamD/ComL family [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443281 [Multi-domain]  Cd Length: 254  Bit Score: 39.48  E-value: 1.48e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2101302170 190 GSIDTLFREGLTLYWGGYYKDALAKFEAVERLYPGHSEIKR---FITDSQQKSGQ 241
Cdd:COG4105    30 WDAEELYEEAKEALEKGDYEKAIKLFEELEPRYPGSPYAEQaqlMLAYAYYKQGD 84
OM_YfiO TIGR03302
outer membrane assembly lipoprotein YfiO; Members of this protein family include YfiO, a ...
 191-224 5.49e-03

outer membrane assembly lipoprotein YfiO; Members of this protein family include YfiO, a near-essential protein of the outer membrane, part of a complex involved in protein insertion into the bacterial outer membrane. Many proteins in this family are annotated as ComL, based on the involvement of this protein in natural transformation with exogenous DNA in Neisseria gonorrhoeae. This protein family shows sequence similarity to, but is distinct from, the tol-pal system protein YbgF (TIGR02795). [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 274513 [Multi-domain]  Cd Length: 235  Bit Score: 37.53  E-value: 5.49e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2101302170 191 SIDTLFREGLTLYWGGYYKDALAKFEAVERLYPG 224
Cdd:TIGR03302  32 PAEELYEEAKEALDSGDYTEAIKYFEALESRYPF 65
Peptidase_S46 pfam10459
Peptidase S46; Dipeptidyl-peptidase 7 (DPP-7) is the best characterized member of this family. ...
 133-152 8.36e-03

Peptidase S46; Dipeptidyl-peptidase 7 (DPP-7) is the best characterized member of this family. It is a serine peptidase that is located on the cell surface and is predicted to have two N-terminal transmembrane domains.


Pssm-ID: 431297  Cd Length: 695  Bit Score: 38.01  E-value: 8.36e-03
                          10        20
                  ....*....|....*....|
gi 2101302170 133 THGNSGGPVINKRGEMIGLL 152
Cdd:pfam10459 629 TGGNSGSPVLNGKGELVGLA 648
 
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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