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Conserved domains on  [gi|446334119|ref|WP_000411974|]
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MULTISPECIES: EF-P 5-aminopentanol modification-associated protein YfmH [Bacillus]

Protein Classification

M16 family metallopeptidase( domain architecture ID 11427472)

M16 family metallopeptidase is a zinc-binding protein that may act as a peptidase cleaving small peptides close to a terminus, often including bonds on the amino side of basic residues such as arginine; similar to Escherichia coli zinc protease PqqL

CATH:  3.30.830.10
Gene Ontology:  GO:0046872|GO:0008237
MEROPS:  M16
PubMed:  1570301
SCOP:  3001831

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
PqqL COG0612
Predicted Zn-dependent peptidase, M16 family [General function prediction only];
8-428 7.41e-100

Predicted Zn-dependent peptidase, M16 family [General function prediction only];


:

Pssm-ID: 440377 [Multi-domain]  Cd Length: 427  Bit Score: 304.54  E-value: 7.41e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446334119   8 QLKETLYYEKLPNGLDVYVLPKQGFNKTFATFTTKYGSVDNtfvPLGKEemirvpdGIAHFLEHKLFEKEDH----DAFQ 83
Cdd:COG0612   10 AAAPDVEEFTLPNGLRVILVPDPEAPVVSVRLWVRVGSRDE---PPGKT-------GLAHFLEHMLFKGTKKrsagEIAE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446334119  84 LFSKQGASANAFTSFTRTAYLFSCTS-NVEQNLNTLLNFVQEPYFSEKTVEKEKGIIGQEIQMYQDNPDWRLYFGLIDSL 162
Cdd:COG0612   80 ELEALGGSLNAFTSFDYTVYYLSVLSeDLELALELLADRLLNPTFDEEELERERGVVLEEIRRYEDDPDGLAFEALLAAL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446334119 163 FVKHPIKIDIAGTIESISKITKDLLYECYETFYHPSNMLLFVVGAIDPEKTMDLVRENQAkkDYKNQPEIVRSFEEEPNE 242
Cdd:COG0612  160 YGDHPYGRPIIGTEESIEAITREDLRAFYKRYYRPNNAVLVVVGDVDPEEVLALVEKYFG--DLPAGPAPPRPDPAEPPQ 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446334119 243 VNEKKKIIS-MPVQTPKCLVGIKATNLKEkgqallKQEIALTLLLDYLF-GKSSVHYEALYNE-GLIDDSFSYdYTEENN 319
Cdd:COG0612  238 TGPRRVVVDdPDAEQAHILLGYPGPARDD------PDYYALDVLNEILGgGFSSRLFQELREKkGLAYSVGSS-FSPYRD 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446334119 320 FGFAMVGGDTK--QPDELADRLKDILLKTDYDQLDAVALERVKKKKIGGFLRSLNSPEYIANQFTRYAF---NESSLFDA 394
Cdd:COG0612  311 AGLFTIYAGTApdKLEEALAAILEELERLAKEGVTEEELERAKNQLLGSLALSLESNSGLASQLGRYELyggDLDYLEEY 390
                        410       420       430
                 ....*....|....*....|....*....|....
gi 446334119 395 LTVLEGLTVQDLQEVAKLLLSEEKMSVCQVLPKK 428
Cdd:COG0612  391 LERIEAVTAEDVQAVARKYLDPDNLVVVVVGPKK 424
 
Name Accession Description Interval E-value
PqqL COG0612
Predicted Zn-dependent peptidase, M16 family [General function prediction only];
8-428 7.41e-100

Predicted Zn-dependent peptidase, M16 family [General function prediction only];


Pssm-ID: 440377 [Multi-domain]  Cd Length: 427  Bit Score: 304.54  E-value: 7.41e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446334119   8 QLKETLYYEKLPNGLDVYVLPKQGFNKTFATFTTKYGSVDNtfvPLGKEemirvpdGIAHFLEHKLFEKEDH----DAFQ 83
Cdd:COG0612   10 AAAPDVEEFTLPNGLRVILVPDPEAPVVSVRLWVRVGSRDE---PPGKT-------GLAHFLEHMLFKGTKKrsagEIAE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446334119  84 LFSKQGASANAFTSFTRTAYLFSCTS-NVEQNLNTLLNFVQEPYFSEKTVEKEKGIIGQEIQMYQDNPDWRLYFGLIDSL 162
Cdd:COG0612   80 ELEALGGSLNAFTSFDYTVYYLSVLSeDLELALELLADRLLNPTFDEEELERERGVVLEEIRRYEDDPDGLAFEALLAAL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446334119 163 FVKHPIKIDIAGTIESISKITKDLLYECYETFYHPSNMLLFVVGAIDPEKTMDLVRENQAkkDYKNQPEIVRSFEEEPNE 242
Cdd:COG0612  160 YGDHPYGRPIIGTEESIEAITREDLRAFYKRYYRPNNAVLVVVGDVDPEEVLALVEKYFG--DLPAGPAPPRPDPAEPPQ 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446334119 243 VNEKKKIIS-MPVQTPKCLVGIKATNLKEkgqallKQEIALTLLLDYLF-GKSSVHYEALYNE-GLIDDSFSYdYTEENN 319
Cdd:COG0612  238 TGPRRVVVDdPDAEQAHILLGYPGPARDD------PDYYALDVLNEILGgGFSSRLFQELREKkGLAYSVGSS-FSPYRD 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446334119 320 FGFAMVGGDTK--QPDELADRLKDILLKTDYDQLDAVALERVKKKKIGGFLRSLNSPEYIANQFTRYAF---NESSLFDA 394
Cdd:COG0612  311 AGLFTIYAGTApdKLEEALAAILEELERLAKEGVTEEELERAKNQLLGSLALSLESNSGLASQLGRYELyggDLDYLEEY 390
                        410       420       430
                 ....*....|....*....|....*....|....
gi 446334119 395 LTVLEGLTVQDLQEVAKLLLSEEKMSVCQVLPKK 428
Cdd:COG0612  391 LERIEAVTAEDVQAVARKYLDPDNLVVVVVGPKK 424
Peptidase_M16_C pfam05193
Peptidase M16 inactive domain; Peptidase M16 consists of two structurally related domains. One ...
181-362 1.16e-19

Peptidase M16 inactive domain; Peptidase M16 consists of two structurally related domains. One is the active peptidase, whereas the other is inactive. The two domains hold the substrate like a clamp.


Pssm-ID: 428362 [Multi-domain]  Cd Length: 181  Bit Score: 85.91  E-value: 1.16e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446334119  181 KITKDLLYECYETFYHPSNMLLFVVGAIDPEKTMDLVRENQAKKDYKNQPEIVRSFEEEPNEVNEKKKIISMPVQTPKCL 260
Cdd:pfam05193   1 SLTREDLRDFYKKHYSPDNMVLVIVGDVDHEELLDLAEKYFGDLPASPKGKPRPPPLEPAKLKGREVVVPKKDEPQAHLA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446334119  261 VGikatnLKEKGQALLKQEIALTLLLDYLFG-KSSVHYEALYNE-GLIDD--SFSYDYTEENNFGFaMVGGDTKQPDELA 336
Cdd:pfam05193  81 LA-----FPGPPLNNDEDSLALDVLNELLGGgMSSRLFQELREKeGLAYSvsSFNDSYSDSGLFGI-YATVDPENVDEVI 154
                         170       180
                  ....*....|....*....|....*.
gi 446334119  337 DRLKDILLKTDYDQLDAVALERVKKK 362
Cdd:pfam05193 155 ELILEELEKLAQEGVTEEELERAKNQ 180
PQQ_syn_pqqF TIGR02110
coenzyme PQQ biosynthesis probable peptidase PqqF; In a subset of species that make coenzyme ...
18-206 2.07e-10

coenzyme PQQ biosynthesis probable peptidase PqqF; In a subset of species that make coenzyme PQQ (pyrrolo-quinoline-quinone), this probable peptidase is found in the PQQ biosynthesis region and is thought to act as a protease on PqqA (TIGR02107), a probable peptide precursor of the coenzyme. PQQ is required for some glucose dehydrogenases and alcohol dehydrogenases. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 273978 [Multi-domain]  Cd Length: 697  Bit Score: 62.58  E-value: 2.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446334119   18 LPNGLDVYVLPKQGFNKTFATFTTKYGSVDntfVPLgkeemiRVPdGIAHFLEHKLFEKEdhDAFQ-------LFSKQGA 90
Cdd:TIGR02110   5 LPNGLRVHLYHQPDAKRAAALLRVAAGSHD---EPS------AWP-GLAHFLEHLLFLGG--ERFQgddrlmpWVQRQGG 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446334119   91 SANAFTSFTRTAYLFSCT-SNVEQNLNTLLNFVQEPYFSEKTVEKEKGIIGQEIQMYQDNPDWRLYFGLIDSLFVKHPIK 169
Cdd:TIGR02110  73 QVNATTLERTTAFFFELPaAALAAGLARLCDMLARPLLTAEDQQREREVLEAEYIAWQNDADTLREAALLDALQAGHPLR 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 446334119  170 IDIAGTIESISKITKDL---LYECYETFYHPSNMLLFVVG 206
Cdd:TIGR02110 153 RFHAGSRDSLALPNTAFqqaLRDFHRRHYQAGNMQLWLQG 192
PRK15101 PRK15101
protease3; Provisional
17-145 3.47e-04

protease3; Provisional


Pssm-ID: 185056 [Multi-domain]  Cd Length: 961  Bit Score: 43.04  E-value: 3.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446334119  17 KLPNGLDVYVLPKQGFNKTFATFTTKYGSVDNtfvplgkeemirvPD---GIAHFLEHKLF-------EKEDHDAFqlFS 86
Cdd:PRK15101  48 RLDNGMTVLLVSDPQAVKSLAALALPVGSLED-------------PDaqqGLAHYLEHMVLmgskkypQPDSLAEF--LK 112
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446334119  87 KQGASANAFTSFTRTA-YLFSCTSNVEQNLNTLLNFVQEPYFSEKTVEKEKGIIGQEIQM 145
Cdd:PRK15101 113 KHGGSHNASTASYRTAfYLEVENDALPPAVDRLADAIAEPLLDPKNADRERNAVNAELTM 172
 
Name Accession Description Interval E-value
PqqL COG0612
Predicted Zn-dependent peptidase, M16 family [General function prediction only];
8-428 7.41e-100

Predicted Zn-dependent peptidase, M16 family [General function prediction only];


Pssm-ID: 440377 [Multi-domain]  Cd Length: 427  Bit Score: 304.54  E-value: 7.41e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446334119   8 QLKETLYYEKLPNGLDVYVLPKQGFNKTFATFTTKYGSVDNtfvPLGKEemirvpdGIAHFLEHKLFEKEDH----DAFQ 83
Cdd:COG0612   10 AAAPDVEEFTLPNGLRVILVPDPEAPVVSVRLWVRVGSRDE---PPGKT-------GLAHFLEHMLFKGTKKrsagEIAE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446334119  84 LFSKQGASANAFTSFTRTAYLFSCTS-NVEQNLNTLLNFVQEPYFSEKTVEKEKGIIGQEIQMYQDNPDWRLYFGLIDSL 162
Cdd:COG0612   80 ELEALGGSLNAFTSFDYTVYYLSVLSeDLELALELLADRLLNPTFDEEELERERGVVLEEIRRYEDDPDGLAFEALLAAL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446334119 163 FVKHPIKIDIAGTIESISKITKDLLYECYETFYHPSNMLLFVVGAIDPEKTMDLVRENQAkkDYKNQPEIVRSFEEEPNE 242
Cdd:COG0612  160 YGDHPYGRPIIGTEESIEAITREDLRAFYKRYYRPNNAVLVVVGDVDPEEVLALVEKYFG--DLPAGPAPPRPDPAEPPQ 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446334119 243 VNEKKKIIS-MPVQTPKCLVGIKATNLKEkgqallKQEIALTLLLDYLF-GKSSVHYEALYNE-GLIDDSFSYdYTEENN 319
Cdd:COG0612  238 TGPRRVVVDdPDAEQAHILLGYPGPARDD------PDYYALDVLNEILGgGFSSRLFQELREKkGLAYSVGSS-FSPYRD 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446334119 320 FGFAMVGGDTK--QPDELADRLKDILLKTDYDQLDAVALERVKKKKIGGFLRSLNSPEYIANQFTRYAF---NESSLFDA 394
Cdd:COG0612  311 AGLFTIYAGTApdKLEEALAAILEELERLAKEGVTEEELERAKNQLLGSLALSLESNSGLASQLGRYELyggDLDYLEEY 390
                        410       420       430
                 ....*....|....*....|....*....|....
gi 446334119 395 LTVLEGLTVQDLQEVAKLLLSEEKMSVCQVLPKK 428
Cdd:COG0612  391 LERIEAVTAEDVQAVARKYLDPDNLVVVVVGPKK 424
Peptidase_M16_C pfam05193
Peptidase M16 inactive domain; Peptidase M16 consists of two structurally related domains. One ...
181-362 1.16e-19

Peptidase M16 inactive domain; Peptidase M16 consists of two structurally related domains. One is the active peptidase, whereas the other is inactive. The two domains hold the substrate like a clamp.


Pssm-ID: 428362 [Multi-domain]  Cd Length: 181  Bit Score: 85.91  E-value: 1.16e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446334119  181 KITKDLLYECYETFYHPSNMLLFVVGAIDPEKTMDLVRENQAKKDYKNQPEIVRSFEEEPNEVNEKKKIISMPVQTPKCL 260
Cdd:pfam05193   1 SLTREDLRDFYKKHYSPDNMVLVIVGDVDHEELLDLAEKYFGDLPASPKGKPRPPPLEPAKLKGREVVVPKKDEPQAHLA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446334119  261 VGikatnLKEKGQALLKQEIALTLLLDYLFG-KSSVHYEALYNE-GLIDD--SFSYDYTEENNFGFaMVGGDTKQPDELA 336
Cdd:pfam05193  81 LA-----FPGPPLNNDEDSLALDVLNELLGGgMSSRLFQELREKeGLAYSvsSFNDSYSDSGLFGI-YATVDPENVDEVI 154
                         170       180
                  ....*....|....*....|....*.
gi 446334119  337 DRLKDILLKTDYDQLDAVALERVKKK 362
Cdd:pfam05193 155 ELILEELEKLAQEGVTEEELERAKNQ 180
Peptidase_M16 pfam00675
Insulinase (Peptidase family M16);
64-154 1.22e-16

Insulinase (Peptidase family M16);


Pssm-ID: 425812 [Multi-domain]  Cd Length: 149  Bit Score: 76.58  E-value: 1.22e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446334119   64 GIAHFLEHKLF---EKEDHDAF-QLFSKQGASANAFTSFTRTAYLFSCTS-NVEQNLNTLLNFVQEPYFSEKTVEKEKGI 138
Cdd:pfam00675  32 GLAHFLEHMAFkgtKKYPSNELeEELEKLGGSLNAFTSRENTVYYAEVLNdDLPKAVDRLADFFRNPLFTESEIERERLV 111
                          90
                  ....*....|....*.
gi 446334119  139 IGQEIQMYQDNPDWRL 154
Cdd:pfam00675 112 VLYEVEAVDSEPQLVV 127
Ptr COG1025
Secreted/periplasmic Zn-dependent peptidases, insulinase-like [Posttranslational modification, ...
64-258 3.30e-11

Secreted/periplasmic Zn-dependent peptidases, insulinase-like [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440648 [Multi-domain]  Cd Length: 956  Bit Score: 65.26  E-value: 3.30e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446334119  64 GIAHFLEHKLF---EK-EDHDAFQLF-SKQGASANAFTSFTRTAYLFSCTSNV-EQNLNTLLNFVQEPYFSEKTVEKEKG 137
Cdd:COG1025   86 GLAHFLEHMLFlgtKKyPEPGEYQEFiSKHGGSHNASTATERTNYYFEVENDAlEEALDRFADFFAAPLFDPEYVDRERN 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446334119 138 IIGQEIQMYQDNpDW-RLYFGLIDSLFVKHPIKIDIAGTIESI-----SKITKDLLyECYETFYHPSNMLLFVVGaidpe 211
Cdd:COG1025  166 AVNAEYTLKRSD-DGrRIYQVHKETLNPAHPFSRFSVGNLETLsdkpgSKLRDELL-AFYQRYYSANLMKLVLYS----- 238
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446334119 212 ktmdlvrenqakkdykNQP-----EIVRS-FEEEPNEvNEKKKIISMPVQTPK 258
Cdd:COG1025  239 ----------------NQSldeleKLARQtFGAIPNR-NLSVPPITVPLYTPE 274
PQQ_syn_pqqF TIGR02110
coenzyme PQQ biosynthesis probable peptidase PqqF; In a subset of species that make coenzyme ...
18-206 2.07e-10

coenzyme PQQ biosynthesis probable peptidase PqqF; In a subset of species that make coenzyme PQQ (pyrrolo-quinoline-quinone), this probable peptidase is found in the PQQ biosynthesis region and is thought to act as a protease on PqqA (TIGR02107), a probable peptide precursor of the coenzyme. PQQ is required for some glucose dehydrogenases and alcohol dehydrogenases. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 273978 [Multi-domain]  Cd Length: 697  Bit Score: 62.58  E-value: 2.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446334119   18 LPNGLDVYVLPKQGFNKTFATFTTKYGSVDntfVPLgkeemiRVPdGIAHFLEHKLFEKEdhDAFQ-------LFSKQGA 90
Cdd:TIGR02110   5 LPNGLRVHLYHQPDAKRAAALLRVAAGSHD---EPS------AWP-GLAHFLEHLLFLGG--ERFQgddrlmpWVQRQGG 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446334119   91 SANAFTSFTRTAYLFSCT-SNVEQNLNTLLNFVQEPYFSEKTVEKEKGIIGQEIQMYQDNPDWRLYFGLIDSLFVKHPIK 169
Cdd:TIGR02110  73 QVNATTLERTTAFFFELPaAALAAGLARLCDMLARPLLTAEDQQREREVLEAEYIAWQNDADTLREAALLDALQAGHPLR 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 446334119  170 IDIAGTIESISKITKDL---LYECYETFYHPSNMLLFVVG 206
Cdd:TIGR02110 153 RFHAGSRDSLALPNTAFqqaLRDFHRRHYQAGNMQLWLQG 192
Cym1 COG1026
Zn-dependent peptidase, M16 (insulinase) family [Posttranslational modification, protein ...
93-354 2.70e-05

Zn-dependent peptidase, M16 (insulinase) family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440649 [Multi-domain]  Cd Length: 974  Bit Score: 46.72  E-value: 2.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446334119  93 NAFTSFTRTAYLFSctSNVEQNLNTLLN---------------FVQEPY---FSEKTVEKE-KGIIGQEIQMYQDNPDWR 153
Cdd:COG1026   99 NAMTYSDKTAYPVA--SRNEKDFYNLMDvyldavffpnldpliFAQEGWryeLEEPDSPLTyKGVVYNEMKGAMSSPDSV 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446334119 154 LYFGLIDSLFVKHPIKIDIAGTIESIskitKDLLYE----CYETFYHPSNMLLFVVGAIDPEKTMDLVREN-----QAKK 224
Cdd:COG1026  177 LWRALQKSLFPDTTYGYNSGGDPEVI----PDLTYEqflaFHKKYYHPSNAYIYLYGDIDAEEHLAFLDEEylsrfERLE 252
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446334119 225 ---DYKNQP------EIVRSFEEEPNEVNEKKKIISMPVqtpkcLVGiKATNLKEKgqallkqeIALTLLLDYLFGKS-S 294
Cdd:COG1026  253 vdsEVPDQKrfsaprEVEETYPVAEEEDTENKTYLSLNW-----LLG-ESTDLEES--------LALQLLSYVLLGNSaS 318
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446334119 295 VHYEALYNEGLIDDSFSY--DYTEENNFGFAMVGGDTKQpdelADRLKDILLKT---------DYDQLDAV 354
Cdd:COG1026  319 PLKKALLDSGLGKDVSGGleDSLRQPVFSIGLKGSEPEK----AEAFEKLILETleklveegiDKELLEAA 385
PRK15101 PRK15101
protease3; Provisional
17-145 3.47e-04

protease3; Provisional


Pssm-ID: 185056 [Multi-domain]  Cd Length: 961  Bit Score: 43.04  E-value: 3.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446334119  17 KLPNGLDVYVLPKQGFNKTFATFTTKYGSVDNtfvplgkeemirvPD---GIAHFLEHKLF-------EKEDHDAFqlFS 86
Cdd:PRK15101  48 RLDNGMTVLLVSDPQAVKSLAALALPVGSLED-------------PDaqqGLAHYLEHMVLmgskkypQPDSLAEF--LK 112
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446334119  87 KQGASANAFTSFTRTA-YLFSCTSNVEQNLNTLLNFVQEPYFSEKTVEKEKGIIGQEIQM 145
Cdd:PRK15101 113 KHGGSHNASTASYRTAfYLEVENDALPPAVDRLADAIAEPLLDPKNADRERNAVNAELTM 172
 
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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