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Conserved domains on  [gi|446587416|ref|WP_000664762|]
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EF-P 5-aminopentanol modification-associated protein YfmH [Staphylococcus aureus]

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];
10-420 1.51e-76

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


:

Pssm-ID: 440377 [Multi-domain]  Cd Length: 427  Bit Score: 244.45  E-value: 1.51e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587416  10 DERVFEQELENGLRLFIIPKPGFQKTFVTYTTQFGSLDNqfkPIGQDqfvtvpdGVAHFLEHKLFEKEE----EDLFTAF 85
Cdd:COG0612   12 APDVEEFTLPNGLRVILVPDPEAPVVSVRLWVRVGSRDE---PPGKT-------GLAHFLEHMLFKGTKkrsaGEIAEEL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587416  86 AEDNAQANAFTSFDRTSYLFSA-TDNIENNIKRLLTMVETPYFTKETVDKEKGIIAEEIKMYQEQPRYKLMFNTLRAMYQ 164
Cdd:COG0612   82 EALGGSLNAFTSFDYTVYYLSVlSEDLELALELLADRLLNPTFDEEELERERGVVLEEIRRYEDDPDGLAFEALLAALYG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587416 165 QHPIRVDIAGSVESIYDITKDDLYLCYETFYHPSNMVLFVVGDVDPETICRIVKQH-EDARNKVNQPKIDRglvDEPEDV 243
Cdd:COG0612  162 DHPYGRPIIGTEESIEAITREDLRAFYKRYYRPNNAVLVVVGDVDPEEVLALVEKYfGDLPAGPAPPRPDP---AEPPQT 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587416 244 KEAFVT-ESMKIQSPRLMLGFKnkplqeAPQKYVQRDLEMSLFFELIFGEETD-FYQNLLNE-GLIDDTFGYQFVLEPTY 320
Cdd:COG0612  239 GPRRVVvDDPDAEQAHILLGYP------GPARDDPDYYALDVLNEILGGGFSSrLFQELREKkGLAYSVGSSFSPYRDAG 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587416 321 SFSI-VTSATEEPDKLKKLLLDELCD-KKGNFQDAEaFELLKKQFIGEFISSLNSPEYIANQYTKLYFEGV---SVFDML 395
Cdd:COG0612  313 LFTIyAGTAPDKLEEALAAILEELERlAKEGVTEEE-LERAKNQLLGSLALSLESNSGLASQLGRYELYGGdldYLEEYL 391
                        410       420
                 ....*....|....*....|....*
gi 446587416 396 DIVENITLDSINETSSLYLNLDQQV 420
Cdd:COG0612  392 ERIEAVTAEDVQAVARKYLDPDNLV 416
 
Name Accession Description Interval E-value
PqqL COG0612
Predicted Zn-dependent peptidase, M16 family [General function prediction only];
10-420 1.51e-76

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


Pssm-ID: 440377 [Multi-domain]  Cd Length: 427  Bit Score: 244.45  E-value: 1.51e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587416  10 DERVFEQELENGLRLFIIPKPGFQKTFVTYTTQFGSLDNqfkPIGQDqfvtvpdGVAHFLEHKLFEKEE----EDLFTAF 85
Cdd:COG0612   12 APDVEEFTLPNGLRVILVPDPEAPVVSVRLWVRVGSRDE---PPGKT-------GLAHFLEHMLFKGTKkrsaGEIAEEL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587416  86 AEDNAQANAFTSFDRTSYLFSA-TDNIENNIKRLLTMVETPYFTKETVDKEKGIIAEEIKMYQEQPRYKLMFNTLRAMYQ 164
Cdd:COG0612   82 EALGGSLNAFTSFDYTVYYLSVlSEDLELALELLADRLLNPTFDEEELERERGVVLEEIRRYEDDPDGLAFEALLAALYG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587416 165 QHPIRVDIAGSVESIYDITKDDLYLCYETFYHPSNMVLFVVGDVDPETICRIVKQH-EDARNKVNQPKIDRglvDEPEDV 243
Cdd:COG0612  162 DHPYGRPIIGTEESIEAITREDLRAFYKRYYRPNNAVLVVVGDVDPEEVLALVEKYfGDLPAGPAPPRPDP---AEPPQT 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587416 244 KEAFVT-ESMKIQSPRLMLGFKnkplqeAPQKYVQRDLEMSLFFELIFGEETD-FYQNLLNE-GLIDDTFGYQFVLEPTY 320
Cdd:COG0612  239 GPRRVVvDDPDAEQAHILLGYP------GPARDDPDYYALDVLNEILGGGFSSrLFQELREKkGLAYSVGSSFSPYRDAG 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587416 321 SFSI-VTSATEEPDKLKKLLLDELCD-KKGNFQDAEaFELLKKQFIGEFISSLNSPEYIANQYTKLYFEGV---SVFDML 395
Cdd:COG0612  313 LFTIyAGTAPDKLEEALAAILEELERlAKEGVTEEE-LERAKNQLLGSLALSLESNSGLASQLGRYELYGGdldYLEEYL 391
                        410       420
                 ....*....|....*....|....*
gi 446587416 396 DIVENITLDSINETSSLYLNLDQQV 420
Cdd:COG0612  392 ERIEAVTAEDVQAVARKYLDPDNLV 416
Peptidase_M16_C pfam05193
Peptidase M16 inactive domain; Peptidase M16 consists of two structurally related domains. One ...
181-363 2.59e-21

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: 90.53  E-value: 2.59e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587416  181 DITKDDLYLCYETFYHPSNMVLFVVGDVDPETICRIVKQHEDARNKVNQPKIDRGLVDEPEDVKEAFVTESMKIQSPRLM 260
Cdd:pfam05193   1 SLTREDLRDFYKKHYSPDNMVLVIVGDVDHEELLDLAEKYFGDLPASPKGKPRPPPLEPAKLKGREVVVPKKDEPQAHLA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587416  261 LGFKNKPLQEAPQKYVqrdleMSLFFELIFGE-ETDFYQNLLNE-GLIDDTFGYQFVLEPTYSFSI-VTSATEEPDKLKK 337
Cdd:pfam05193  81 LAFPGPPLNNDEDSLA-----LDVLNELLGGGmSSRLFQELREKeGLAYSVSSFNDSYSDSGLFGIyATVDPENVDEVIE 155
                         170       180
                  ....*....|....*....|....*.
gi 446587416  338 LLLDELCDKKGNFQDAEAFELLKKQF 363
Cdd:pfam05193 156 LILEELEKLAQEGVTEEELERAKNQL 181
PQQ_syn_pqqF TIGR02110
coenzyme PQQ biosynthesis probable peptidase PqqF; In a subset of species that make coenzyme ...
18-206 4.95e-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: 61.42  E-value: 4.95e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587416   18 LENGLRLFIIPKPGFQKTFVTYTTQFGSLDnqfkpigqdqfvtVPD---GVAHFLEHKLFEKEE-----EDLFTAFAEDN 89
Cdd:TIGR02110   5 LPNGLRVHLYHQPDAKRAAALLRVAAGSHD-------------EPSawpGLAHFLEHLLFLGGErfqgdDRLMPWVQRQG 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587416   90 AQANAFTSFDRTSYLFS-ATDNIENNIKRLLTMVETPYFTKETVDKEKGIIAEEIKMYQEQPRYKLMFNTLRAMYQQHPI 168
Cdd:TIGR02110  72 GQVNATTLERTTAFFFElPAAALAAGLARLCDMLARPLLTAEDQQREREVLEAEYIAWQNDADTLREAALLDALQAGHPL 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 446587416  169 RVDIAGSVESI---YDITKDDLYLCYETFYHPSNMVLFVVG 206
Cdd:TIGR02110 152 RRFHAGSRDSLalpNTAFQQALRDFHRRHYQAGNMQLWLQG 192
 
Name Accession Description Interval E-value
PqqL COG0612
Predicted Zn-dependent peptidase, M16 family [General function prediction only];
10-420 1.51e-76

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


Pssm-ID: 440377 [Multi-domain]  Cd Length: 427  Bit Score: 244.45  E-value: 1.51e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587416  10 DERVFEQELENGLRLFIIPKPGFQKTFVTYTTQFGSLDNqfkPIGQDqfvtvpdGVAHFLEHKLFEKEE----EDLFTAF 85
Cdd:COG0612   12 APDVEEFTLPNGLRVILVPDPEAPVVSVRLWVRVGSRDE---PPGKT-------GLAHFLEHMLFKGTKkrsaGEIAEEL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587416  86 AEDNAQANAFTSFDRTSYLFSA-TDNIENNIKRLLTMVETPYFTKETVDKEKGIIAEEIKMYQEQPRYKLMFNTLRAMYQ 164
Cdd:COG0612   82 EALGGSLNAFTSFDYTVYYLSVlSEDLELALELLADRLLNPTFDEEELERERGVVLEEIRRYEDDPDGLAFEALLAALYG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587416 165 QHPIRVDIAGSVESIYDITKDDLYLCYETFYHPSNMVLFVVGDVDPETICRIVKQH-EDARNKVNQPKIDRglvDEPEDV 243
Cdd:COG0612  162 DHPYGRPIIGTEESIEAITREDLRAFYKRYYRPNNAVLVVVGDVDPEEVLALVEKYfGDLPAGPAPPRPDP---AEPPQT 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587416 244 KEAFVT-ESMKIQSPRLMLGFKnkplqeAPQKYVQRDLEMSLFFELIFGEETD-FYQNLLNE-GLIDDTFGYQFVLEPTY 320
Cdd:COG0612  239 GPRRVVvDDPDAEQAHILLGYP------GPARDDPDYYALDVLNEILGGGFSSrLFQELREKkGLAYSVGSSFSPYRDAG 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587416 321 SFSI-VTSATEEPDKLKKLLLDELCD-KKGNFQDAEaFELLKKQFIGEFISSLNSPEYIANQYTKLYFEGV---SVFDML 395
Cdd:COG0612  313 LFTIyAGTAPDKLEEALAAILEELERlAKEGVTEEE-LERAKNQLLGSLALSLESNSGLASQLGRYELYGGdldYLEEYL 391
                        410       420
                 ....*....|....*....|....*
gi 446587416 396 DIVENITLDSINETSSLYLNLDQQV 420
Cdd:COG0612  392 ERIEAVTAEDVQAVARKYLDPDNLV 416
Peptidase_M16_C pfam05193
Peptidase M16 inactive domain; Peptidase M16 consists of two structurally related domains. One ...
181-363 2.59e-21

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: 90.53  E-value: 2.59e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587416  181 DITKDDLYLCYETFYHPSNMVLFVVGDVDPETICRIVKQHEDARNKVNQPKIDRGLVDEPEDVKEAFVTESMKIQSPRLM 260
Cdd:pfam05193   1 SLTREDLRDFYKKHYSPDNMVLVIVGDVDHEELLDLAEKYFGDLPASPKGKPRPPPLEPAKLKGREVVVPKKDEPQAHLA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587416  261 LGFKNKPLQEAPQKYVqrdleMSLFFELIFGE-ETDFYQNLLNE-GLIDDTFGYQFVLEPTYSFSI-VTSATEEPDKLKK 337
Cdd:pfam05193  81 LAFPGPPLNNDEDSLA-----LDVLNELLGGGmSSRLFQELREKeGLAYSVSSFNDSYSDSGLFGIyATVDPENVDEVIE 155
                         170       180
                  ....*....|....*....|....*.
gi 446587416  338 LLLDELCDKKGNFQDAEAFELLKKQF 363
Cdd:pfam05193 156 LILEELEKLAQEGVTEEELERAKNQL 181
Peptidase_M16 pfam00675
Insulinase (Peptidase family M16);
64-174 7.43e-14

Insulinase (Peptidase family M16);


Pssm-ID: 425812 [Multi-domain]  Cd Length: 149  Bit Score: 68.49  E-value: 7.43e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587416   64 GVAHFLEHKLF---EKEEEDLFTAFAED-NAQANAFTSFDRTSYLFSA-TDNIENNIKRLLTMVETPYFTKETVDKEKGI 138
Cdd:pfam00675  32 GLAHFLEHMAFkgtKKYPSNELEEELEKlGGSLNAFTSRENTVYYAEVlNDDLPKAVDRLADFFRNPLFTESEIERERLV 111
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 446587416  139 IAEEIKMYQEQPRYKLMFNTLRAMYQQHPIRVDIAG 174
Cdd:pfam00675 112 VLYEVEAVDSEPQLVVLENLHAAAYRNTPLGRSLLG 147
PQQ_syn_pqqF TIGR02110
coenzyme PQQ biosynthesis probable peptidase PqqF; In a subset of species that make coenzyme ...
18-206 4.95e-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: 61.42  E-value: 4.95e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587416   18 LENGLRLFIIPKPGFQKTFVTYTTQFGSLDnqfkpigqdqfvtVPD---GVAHFLEHKLFEKEE-----EDLFTAFAEDN 89
Cdd:TIGR02110   5 LPNGLRVHLYHQPDAKRAAALLRVAAGSHD-------------EPSawpGLAHFLEHLLFLGGErfqgdDRLMPWVQRQG 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587416   90 AQANAFTSFDRTSYLFS-ATDNIENNIKRLLTMVETPYFTKETVDKEKGIIAEEIKMYQEQPRYKLMFNTLRAMYQQHPI 168
Cdd:TIGR02110  72 GQVNATTLERTTAFFFElPAAALAAGLARLCDMLARPLLTAEDQQREREVLEAEYIAWQNDADTLREAALLDALQAGHPL 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 446587416  169 RVDIAGSVESI---YDITKDDLYLCYETFYHPSNMVLFVVG 206
Cdd:TIGR02110 152 RRFHAGSRDSLalpNTAFQQALRDFHRRHYQAGNMQLWLQG 192
Ptr COG1025
Secreted/periplasmic Zn-dependent peptidases, insulinase-like [Posttranslational modification, ...
17-220 5.41e-09

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


Pssm-ID: 440648 [Multi-domain]  Cd Length: 956  Bit Score: 58.32  E-value: 5.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587416  17 ELENGLRLFIIPKPGFQKTFVTYTTQFGSLDNqfkPIGQDqfvtvpdGVAHFLEHKLF---EK-EEEDLFTAFAEDNA-Q 91
Cdd:COG1025   49 TLDNGLKVLLVSDPQADKSAAALAVPVGSFDD---PDDQQ-------GLAHFLEHMLFlgtKKyPEPGEYQEFISKHGgS 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446587416  92 ANAFTSFDRTSYLFS-ATDNIENNIKRLLTMVETPYFTKETVDKEKGIIAEEIKMYQEqpryklmfNTLRAMYQ------ 164
Cdd:COG1025  119 HNASTATERTNYYFEvENDALEEALDRFADFFAAPLFDPEYVDRERNAVNAEYTLKRS--------DDGRRIYQvhketl 190
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446587416 165 --QHPIRVDIAGSVESIYDIT----KDDLYLCYETFYHPSNMVLFVVGDVDPETICRIVKQH 220
Cdd:COG1025  191 npAHPFSRFSVGNLETLSDKPgsklRDELLAFYQRYYSANLMKLVLYSNQSLDELEKLARQT 252
 
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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