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Conserved domains on  [gi|1485946541|gb|RKG67019|]
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protease [Corallococcus sp. CA054B]

Protein Classification

zinc-dependent metalloprotease( domain architecture ID 10574850)

zinc-dependent metalloprotease similar to Myxococcus xanthus protease B (prtB)

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Peptidase_M57 pfam12388
Dual-action HEIGH metallo-peptidase; The catalytic triad for this family of proteases is ...
51-256 7.81e-118

Dual-action HEIGH metallo-peptidase; The catalytic triad for this family of proteases is HE-H-H, which in many members is in the sequence motif HEIGH.


:

Pssm-ID: 432518  Cd Length: 212  Bit Score: 335.64  E-value: 7.81e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485946541  51 VYVGRDAHVTLEASREMLQpATKETQEQYRTTNLVGTS--ITKICVNPTSGFNSYSRLSQGLDLAIQNYNQRGLS--FTM 126
Cdd:pfam12388   1 VYVGRDAVVTLEASREMLQ-TDSDTAEQYRTTNLVGTSvtVIKICVNPTSNFNSYSRLSTGLDLAIANYNRLGLRftFRL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485946541 127 ARGPTTGCS----ANITATTMSGTGGSAGFPSGGRPYGTINIGTGLQSYSVDVNEHVITHELGHAIGFRHTDYYNRNISC 202
Cdd:pfam12388  80 TFGPNTGNSdmvtYDNTANTPSGTGGSAGFPSGGLPYGTIQIGTGLQSYSTDVNEHVITHELGHSIGFRHSDYYNRSISC 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1485946541 203 GSGGNEGTAGVGAIHIPGTPTTATvGGSIMNSCFRSTETGEFTSSDITALNYLY 256
Cdd:pfam12388 160 GSGGNEGTAGVGAILIPGTPTTAT-GGSIMNSCFSSNETGEFTSSDITALTYLY 212
 
Name Accession Description Interval E-value
Peptidase_M57 pfam12388
Dual-action HEIGH metallo-peptidase; The catalytic triad for this family of proteases is ...
51-256 7.81e-118

Dual-action HEIGH metallo-peptidase; The catalytic triad for this family of proteases is HE-H-H, which in many members is in the sequence motif HEIGH.


Pssm-ID: 432518  Cd Length: 212  Bit Score: 335.64  E-value: 7.81e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485946541  51 VYVGRDAHVTLEASREMLQpATKETQEQYRTTNLVGTS--ITKICVNPTSGFNSYSRLSQGLDLAIQNYNQRGLS--FTM 126
Cdd:pfam12388   1 VYVGRDAVVTLEASREMLQ-TDSDTAEQYRTTNLVGTSvtVIKICVNPTSNFNSYSRLSTGLDLAIANYNRLGLRftFRL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485946541 127 ARGPTTGCS----ANITATTMSGTGGSAGFPSGGRPYGTINIGTGLQSYSVDVNEHVITHELGHAIGFRHTDYYNRNISC 202
Cdd:pfam12388  80 TFGPNTGNSdmvtYDNTANTPSGTGGSAGFPSGGLPYGTIQIGTGLQSYSTDVNEHVITHELGHSIGFRHSDYYNRSISC 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1485946541 203 GSGGNEGTAGVGAIHIPGTPTTATvGGSIMNSCFRSTETGEFTSSDITALNYLY 256
Cdd:pfam12388 160 GSGGNEGTAGVGAILIPGTPTTAT-GGSIMNSCFSSNETGEFTSSDITALTYLY 212
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
113-256 5.44e-08

Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix metalloproteinases (MMPs), serralysins, and the astacin_like family of proteases.


Pssm-ID: 239796 [Multi-domain]  Cd Length: 165  Bit Score: 50.96  E-value: 5.44e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485946541 113 AIQNYNQRG-LSFTMARGpttGCSANITATTMSGTGGSAGF----PSGGRP------YGTINIGTGLQSYSVDVNEHVIT 181
Cdd:cd04268    23 AIEAWNKAFaIGFKNAND---VDPADIRYSVIRWIPYNDGTwsygPSQVDPltgeilLARVYLYSSFVEYSGARLRNTAE 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485946541 182 HELGHAIGFRHTDyynrniscgsggnegtAGVGAIHIPGTPTTATVGGSIMNSC-------FRSTETGEFTSSDITALNY 254
Cdd:cd04268   100 HELGHALGLRHNF----------------AASDRDDNVDLLAEKGDTSSVMDYApsnfsiqLGDGQKYTIGPYDIAAIKK 163

                  ..
gi 1485946541 255 LY 256
Cdd:cd04268   164 LY 165
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
144-197 1.29e-04

Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a subset of known subfamilies. Highest similarity occurs in the HExxH zinc-binding site/ active site.


Pssm-ID: 214576 [Multi-domain]  Cd Length: 139  Bit Score: 40.80  E-value: 1.29e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1485946541  144 SGTGGS-AGFPSGGrpyGTINIGTGlqsysvDVNEHVITHELGHAIGFRHTDYYN 197
Cdd:smart00235  60 SGCTLShAGRPGGD---QHLSLGNG------CINTGVAAHELGHALGLYHEQSRS 105
 
Name Accession Description Interval E-value
Peptidase_M57 pfam12388
Dual-action HEIGH metallo-peptidase; The catalytic triad for this family of proteases is ...
51-256 7.81e-118

Dual-action HEIGH metallo-peptidase; The catalytic triad for this family of proteases is HE-H-H, which in many members is in the sequence motif HEIGH.


Pssm-ID: 432518  Cd Length: 212  Bit Score: 335.64  E-value: 7.81e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485946541  51 VYVGRDAHVTLEASREMLQpATKETQEQYRTTNLVGTS--ITKICVNPTSGFNSYSRLSQGLDLAIQNYNQRGLS--FTM 126
Cdd:pfam12388   1 VYVGRDAVVTLEASREMLQ-TDSDTAEQYRTTNLVGTSvtVIKICVNPTSNFNSYSRLSTGLDLAIANYNRLGLRftFRL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485946541 127 ARGPTTGCS----ANITATTMSGTGGSAGFPSGGRPYGTINIGTGLQSYSVDVNEHVITHELGHAIGFRHTDYYNRNISC 202
Cdd:pfam12388  80 TFGPNTGNSdmvtYDNTANTPSGTGGSAGFPSGGLPYGTIQIGTGLQSYSTDVNEHVITHELGHSIGFRHSDYYNRSISC 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1485946541 203 GSGGNEGTAGVGAIHIPGTPTTATvGGSIMNSCFRSTETGEFTSSDITALNYLY 256
Cdd:pfam12388 160 GSGGNEGTAGVGAILIPGTPTTAT-GGSIMNSCFSSNETGEFTSSDITALTYLY 212
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
113-256 5.44e-08

Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix metalloproteinases (MMPs), serralysins, and the astacin_like family of proteases.


Pssm-ID: 239796 [Multi-domain]  Cd Length: 165  Bit Score: 50.96  E-value: 5.44e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485946541 113 AIQNYNQRG-LSFTMARGpttGCSANITATTMSGTGGSAGF----PSGGRP------YGTINIGTGLQSYSVDVNEHVIT 181
Cdd:cd04268    23 AIEAWNKAFaIGFKNAND---VDPADIRYSVIRWIPYNDGTwsygPSQVDPltgeilLARVYLYSSFVEYSGARLRNTAE 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485946541 182 HELGHAIGFRHTDyynrniscgsggnegtAGVGAIHIPGTPTTATVGGSIMNSC-------FRSTETGEFTSSDITALNY 254
Cdd:cd04268   100 HELGHALGLRHNF----------------AASDRDDNVDLLAEKGDTSSVMDYApsnfsiqLGDGQKYTIGPYDIAAIKK 163

                  ..
gi 1485946541 255 LY 256
Cdd:cd04268   164 LY 165
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
87-193 1.30e-05

Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and fungal metalloproteinase domains similar to matrix metalloproteinases and astacin.


Pssm-ID: 239806 [Multi-domain]  Cd Length: 156  Bit Score: 43.98  E-value: 1.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485946541  87 TSITKICVNPTSGFNS--YSRLSQGLDLAIQNYNQrGLSFTMARGPTTGCSANIT---ATTMSGTGGSAGFPSGGRPYG- 160
Cdd:cd04279     1 KSPIRVYIDPTPAPPDsrAQSWLQAVKQAAAEWEN-VGPLKFVYNPEEDNDADIViffDRPPPVGGAGGGLARAGFPLIs 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1485946541 161 ----------TINIGTGLQSYSVDVnEHVITHELGHAIGFRHT 193
Cdd:cd04279    80 dgnrklfnrtDINLGPGQPRGAENL-QAIALHELGHALGLWHH 121
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
144-197 1.29e-04

Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a subset of known subfamilies. Highest similarity occurs in the HExxH zinc-binding site/ active site.


Pssm-ID: 214576 [Multi-domain]  Cd Length: 139  Bit Score: 40.80  E-value: 1.29e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1485946541  144 SGTGGS-AGFPSGGrpyGTINIGTGlqsysvDVNEHVITHELGHAIGFRHTDYYN 197
Cdd:smart00235  60 SGCTLShAGRPGGD---QHLSLGNG------CINTGVAAHELGHALGLYHEQSRS 105
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
145-256 5.29e-04

Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major branches, the astacin-like proteases and the adamalysin/reprolysin-like proteases. Both branches have wide phylogenetic distribution, and contain sub-families, which are involved in vertebrate development and disease.


Pssm-ID: 238124 [Multi-domain]  Cd Length: 167  Bit Score: 39.81  E-value: 5.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485946541 145 GTGGSAGFPSGGRPY-GTINIGTGlqSYSVDVNEHVITHELGHAIGFRHTDYYNrniscgsggnegtAGVGAIHIPGT-P 222
Cdd:cd00203    66 GTGGWAYLGRVCDSLrGVGVLQDN--QSGTKEGAQTIAHELGHALGFYHDHDRK-------------DRDDYPTIDDTlN 130
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1485946541 223 TTATVGGSIMnSCFRSTETGE----FTSSDITALNYLY 256
Cdd:cd00203   131 AEDDDYYSVM-SYTKGSFSDGqrkdFSQCDIDQINKLY 167
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
121-199 6.20e-04

Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases are important virulence factors in pathogenic bacteria. They may be secreted into the medium via a mechanism found in gram-negative bacteria, that does not require n-terminal signal sequences which are cleaved after the transmembrane translocation. A calcium-binding domain c-terminal to the metalloprotease domain, which contains multiple tandem repeats of a nine-residue motif including the pattern GGxGxD, and which forms a parallel beta roll may be involved in the translocation mechanism and/or substrate binding. Serralysin family members may have a broad spectrum of substrates each, including host immunoglobulins, complement proteins, cell matrix and cytoskeletal proteins, as well as antimicrobial peptides.


Pssm-ID: 239804 [Multi-domain]  Cd Length: 186  Bit Score: 39.71  E-value: 6.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1485946541 121 GLSFTMARGPTtgcSANIT----ATTMSGTGGSAGFP---SGGRPYGTINIGTGLQSYSVDVNEH---VITHELGHAIGF 190
Cdd:cd04277    51 DIDFVEVSDNS---GADIRfgnsSDPDGNTAGYAYYPgsgSGTAYGGDIWFNSSYDTNSDSPGSYgyqTIIHEIGHALGL 127

                  ....*....
gi 1485946541 191 RHTDYYNRN 199
Cdd:cd04277   128 EHPGDYNGG 136
 
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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