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Conserved domains on  [gi|13027802|ref|NP_005932|]
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matrix metalloproteinase-16 precursor [Homo sapiens]

Protein Classification

M10A family metallopeptidase( domain architecture ID 12021161)

M10A family metallopeptidase similar to matrix metalloproteinases with a C-terminal hemopexin repeat-containing domain that may be endopeptidases that degrade various components of the extracellular matrix; also contains a possible peptidoglycan binding domain at the N-terminus and a DUF3377 domain at the C-terminal end

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 126-291 9.23e-90

Matrixin; The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis.


:

Pssm-ID: 425668 [Multi-domain]  Cd Length: 159  Bit Score: 274.49  E-value: 9.23e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13027802   126 KWQHKHITYSIKNVTPKVGDPETRKAIRRAFDVWQNVTPLTFEEVPYSElengkrdVDITIIFASGFHGDSSPFDGEGGF 205
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGE-------ADIMIGFGRGDHGDGYPFDGPGGV 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13027802   206 LAHAYFPGPGIGGDTHFDSDEPWTLGNPNHDGNDLFLVAVHELGHALGLEHSNDPTAIMAPFYQYMETDNFKLPNDDLQG 285
Cdd:pfam00413  74 LAHAFFPGPGLGGDIHFDDDETWTVGSDPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKG 153


                  ....*.
gi 13027802   286 IQKIYG 291
Cdd:pfam00413 154 IQQLYG 159
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 340-532 3.17e-77

Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metalloproteinases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metalloproteinases (TIMPs). This CD contains 4 instances of the repeat.


:

Pssm-ID: 238046 [Multi-domain]  Cd Length: 194  Bit Score: 243.37  E-value: 3.17e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13027802 340 PNICDG-NFNTLAILRREMFVFKDQWFWRVRNNRvMDGYPMQITYFWRGLPPSIDAVYENSD-GNFVFFKGNKYWVFKDT 417
Cdd:cd00094   1 PDACDPlSFDAVTTLRGELYFFKGRYFWRLSPGK-PPGSPFLISSFWPSLPSPVDAAFERPDtGKIYFFKGDKYWVYTGK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13027802 418 TLQPGYPHDLITLGSGIPPHGIDSAIWWEDVGKTYFFKGDRYWRYSEEMKTMDPGYPK-PITVWKGIPESPQGAFvHKEN 496
Cdd:cd00094  80 NLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKlIETDFPGVPDKVDAAF-RWLD 158

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 13027802 497 GFTYFYKGKEYWKFNNQILKVEPGYPRSILKDFMGC 532
Cdd:cd00094 159 GYYYFFKGDQYWRFDPRSKEVRVGYPLKISSDWLGC 194
DUF3377 pfam11857
Domain of unknown function (DUF3377); This domain is functionally uncharacterized. This domain ...
 537-607 4.73e-32

Domain of unknown function (DUF3377); This domain is functionally uncharacterized. This domain is found in eukaryotes. This presumed domain is about 70 amino acids in length.


:

Pssm-ID: 463374  Cd Length: 72  Bit Score: 118.19  E-value: 4.73e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13027802   537 DRVKEGHSPPDDVDIVIKLDNTAS-TVKAIAIVIPCILALCLLVLVYTVFQFKRKGTPRHILYCKRSMQEWV 607
Cdd:pfam11857   1 DREEDRHEEEDEVDIVVVIDDVASgTVNAIAVVVPLVLLLCILVLIYAIVQFQRKGTPRRLLYCKRSLQDWV 72
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 46-96 3.26e-06

Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This domain is found at the N or C terminus of a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. This family is found N-terminal to the catalytic domain of matrixins. The domain is found to bind peptidoglycan experimentally.


:

Pssm-ID: 460223 [Multi-domain]  Cd Length: 57  Bit Score: 44.43  E-value: 3.26e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 13027802    46 WLQKYGYLPPTdprmSVLRSAETMQSALAAMQQFYGINMTGKVDRNTIDWM 96
Cdd:pfam01471  11 YLNRLGYYPGP----VDGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 292-338 4.03e-04

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.77  E-value: 4.03e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 13027802   292 PPDKIPPPTRPLPTVPPhrsIPPADPRKNDRPKPPRPPTGRPSYPGA 338
Cdd:PHA03247 2901 PPDQPERPPQPQAPPPP---QPQPQPPPPPQPQPPPPPPPRPQPPLA 2944
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 126-291 9.23e-90

Matrixin; The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis.


Pssm-ID: 425668 [Multi-domain]  Cd Length: 159  Bit Score: 274.49  E-value: 9.23e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13027802   126 KWQHKHITYSIKNVTPKVGDPETRKAIRRAFDVWQNVTPLTFEEVPYSElengkrdVDITIIFASGFHGDSSPFDGEGGF 205
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGE-------ADIMIGFGRGDHGDGYPFDGPGGV 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13027802   206 LAHAYFPGPGIGGDTHFDSDEPWTLGNPNHDGNDLFLVAVHELGHALGLEHSNDPTAIMAPFYQYMETDNFKLPNDDLQG 285
Cdd:pfam00413  74 LAHAFFPGPGLGGDIHFDDDETWTVGSDPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKG 153


                  ....*.
gi 13027802   286 IQKIYG 291
Cdd:pfam00413 154 IQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 126-291 1.75e-83

Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are responsible for a great deal of pericellular proteolysis of extracellular matrix and cell surface molecules, playing crucial roles in morphogenesis, cell fate specification, cell migration, tissue repair, tumorigenesis, gain or loss of tissue-specific functions, and apoptosis. In many instances, they are anchored to cell membranes via trans-membrane domains, and their activity is controlled via TIMPs (tissue inhibitors of metalloproteinases).


Pssm-ID: 239805 [Multi-domain]  Cd Length: 157  Bit Score: 258.29  E-value: 1.75e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13027802 126 KWQHKHITYSIKNVTPKVGDPETRKAIRRAFDVWQNVTPLTFEEVPYSElengkrDVDITIIFASGFHGDSSPFDGEGGF 205
Cdd:cd04278   1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGQ------EADIRISFARGNHGDGYPFDGPGGT 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13027802 206 LAHAYFPGpGIGGDTHFDSDEPWTLGNpNHDGNDLFLVAVHELGHALGLEHSNDPTAIMAPFYQYMETdNFKLPNDDLQG 285
Cdd:cd04278  75 LAHAFFPG-GIGGDIHFDDDEQWTLGS-DSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVP-KFKLSQDDIRG 151


                ....*.
gi 13027802 286 IQKIYG 291
Cdd:cd04278 152 IQALYG 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 340-532 3.17e-77

Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metalloproteinases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metalloproteinases (TIMPs). This CD contains 4 instances of the repeat.


Pssm-ID: 238046 [Multi-domain]  Cd Length: 194  Bit Score: 243.37  E-value: 3.17e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13027802 340 PNICDG-NFNTLAILRREMFVFKDQWFWRVRNNRvMDGYPMQITYFWRGLPPSIDAVYENSD-GNFVFFKGNKYWVFKDT 417
Cdd:cd00094   1 PDACDPlSFDAVTTLRGELYFFKGRYFWRLSPGK-PPGSPFLISSFWPSLPSPVDAAFERPDtGKIYFFKGDKYWVYTGK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13027802 418 TLQPGYPHDLITLGSGIPPHGIDSAIWWEDVGKTYFFKGDRYWRYSEEMKTMDPGYPK-PITVWKGIPESPQGAFvHKEN 496
Cdd:cd00094  80 NLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKlIETDFPGVPDKVDAAF-RWLD 158

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 13027802 497 GFTYFYKGKEYWKFNNQILKVEPGYPRSILKDFMGC 532
Cdd:cd00094 159 GYYYFFKGDQYWRFDPRSKEVRVGYPLKISSDWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 125-292 3.62e-34

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: 126.70  E-value: 3.62e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13027802    125 QKWQHKHITYSIKnvTPKVgDPETRKAIRRAFDVWQNVTPLTFEEVPYSElengkrdvDITIIFASGFHGdsspfdgegG 204
Cdd:smart00235   3 KKWPKGTVPYVID--SSSL-SPEEREAIAKALAEWSDVTCIRFVERTGTA--------DIYISFGSGDSG---------C 62

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13027802    205 FLAHAYFPGpgigGDTHFDsDEPWTLGnpnhdgndlFLVAVHELGHALGLEHSNDPTA---IMAPFYQYMETDNFKLPND 281
Cdd:smart00235  63 TLSHAGRPG----GDQHLS-LGNGCIN---------TGVAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFDLSED 128

                          170
                   ....*....|.
gi 13027802    282 DLQGIQKIYGP 292
Cdd:smart00235 129 DSLGIPYDYGS 139
DUF3377 pfam11857
Domain of unknown function (DUF3377); This domain is functionally uncharacterized. This domain ...
 537-607 4.73e-32

Domain of unknown function (DUF3377); This domain is functionally uncharacterized. This domain is found in eukaryotes. This presumed domain is about 70 amino acids in length.


Pssm-ID: 463374  Cd Length: 72  Bit Score: 118.19  E-value: 4.73e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13027802   537 DRVKEGHSPPDDVDIVIKLDNTAS-TVKAIAIVIPCILALCLLVLVYTVFQFKRKGTPRHILYCKRSMQEWV 607
Cdd:pfam11857   1 DREEDRHEEEDEVDIVVVIDDVASgTVNAIAVVVPLVLLLCILVLIYAIVQFQRKGTPRRLLYCKRSLQDWV 72
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 439-484 1.74e-12

Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metallopeptidases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metallopeptidases (TIMPs).


Pssm-ID: 395000 [Multi-domain]  Cd Length: 44  Bit Score: 61.81  E-value: 1.74e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 13027802   439 IDSAIWWEDvGKTYFFKGDRYWRYSEEmkTMDPGYPKPITVWKGIP 484
Cdd:pfam00045   1 IDAAFEDRD-GKTYFFKGRKYWRFDPQ--RVEPGYPKLISDFPGLP 43
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 439-484 7.32e-12

Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metalloproteinases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metalloproteinases (TIMPs).


Pssm-ID: 214524 [Multi-domain]  Cd Length: 45  Bit Score: 60.33  E-value: 7.32e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 13027802    439 IDSAIWWEDvGKTYFFKGDRYWRYSEemKTMDPGYPKPIT-VWKGIP 484
Cdd:smart00120   1 IDAAFELRD-GKTYFFKGDKYWRFDP--KRVDPGYPKLISsFFPGLP 44
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 146-266 2.92e-06

Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 48.91  E-value: 2.92e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13027802 146 PETRKAIRRAFDVWQNVtpLTFEEVpyselENGKRdVDITIIFAS---GFHGDSSP----------FDGEGGFLAHAYfp 212
Cdd:COG5549 100 QQWVAAVLQAIAEWNAY--LPLEVV-----ENPEN-ADIIIVRSNpplTASPNPETgarsaettyeFYDTGNILSHRF-- 169

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 13027802 213 gpgiggdthfdsdepwTLG-NPNHDGNDLFLVAVHELGHALGLE-HSNDPTAIMAP 266
Cdd:COG5549 170 ----------------TILlSPNQTGKYLLATARHELGHALGIWgHSPSPTDAMYF 209
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 46-96 3.26e-06

Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This domain is found at the N or C terminus of a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. This family is found N-terminal to the catalytic domain of matrixins. The domain is found to bind peptidoglycan experimentally.


Pssm-ID: 460223 [Multi-domain]  Cd Length: 57  Bit Score: 44.43  E-value: 3.26e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 13027802    46 WLQKYGYLPPTdprmSVLRSAETMQSALAAMQQFYGINMTGKVDRNTIDWM 96
Cdd:pfam01471  11 YLNRLGYYPGP----VDGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
archmetzin NF033823
archaemetzincin family Zn-dependent metalloprotease;
236-264 1.30e-04

archaemetzincin family Zn-dependent metalloprotease;


Pssm-ID: 468195  Cd Length: 170  Bit Score: 42.99  E-value: 1.30e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 13027802  236 DGNDLFL-----VAVHELGHALGLEHSNDPTAIM 264
Cdd:NF033823 113 PDEDLFLerlakEAVHELGHLLGLGHCPNPRCVM 146
PHA03247 PHA03247
large tegument protein UL36; Provisional
 292-338 4.03e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.77  E-value: 4.03e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 13027802   292 PPDKIPPPTRPLPTVPPhrsIPPADPRKNDRPKPPRPPTGRPSYPGA 338
Cdd:PHA03247 2901 PPDQPERPPQPQAPPPP---QPQPQPPPPPQPQPPPPPPPRPQPPLA 2944
PRK13267 PRK13267
archaemetzincin-like protein; Reviewed
 244-264 4.69e-03

archaemetzincin-like protein; Reviewed


Pssm-ID: 237325  Cd Length: 179  Bit Score: 38.46  E-value: 4.69e-03
                         10        20
                 ....*....|....*....|.
gi 13027802  244 AVHELGHALGLEHSNDPTAIM 264
Cdd:PRK13267 129 VTHELGHTLGLEHCDNPRCVM 149
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 126-291 9.23e-90

Matrixin; The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis.


Pssm-ID: 425668 [Multi-domain]  Cd Length: 159  Bit Score: 274.49  E-value: 9.23e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13027802   126 KWQHKHITYSIKNVTPKVGDPETRKAIRRAFDVWQNVTPLTFEEVPYSElengkrdVDITIIFASGFHGDSSPFDGEGGF 205
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGE-------ADIMIGFGRGDHGDGYPFDGPGGV 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13027802   206 LAHAYFPGPGIGGDTHFDSDEPWTLGNPNHDGNDLFLVAVHELGHALGLEHSNDPTAIMAPFYQYMETDNFKLPNDDLQG 285
Cdd:pfam00413  74 LAHAFFPGPGLGGDIHFDDDETWTVGSDPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKG 153


                  ....*.
gi 13027802   286 IQKIYG 291
Cdd:pfam00413 154 IQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 126-291 1.75e-83

Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are responsible for a great deal of pericellular proteolysis of extracellular matrix and cell surface molecules, playing crucial roles in morphogenesis, cell fate specification, cell migration, tissue repair, tumorigenesis, gain or loss of tissue-specific functions, and apoptosis. In many instances, they are anchored to cell membranes via trans-membrane domains, and their activity is controlled via TIMPs (tissue inhibitors of metalloproteinases).


Pssm-ID: 239805 [Multi-domain]  Cd Length: 157  Bit Score: 258.29  E-value: 1.75e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13027802 126 KWQHKHITYSIKNVTPKVGDPETRKAIRRAFDVWQNVTPLTFEEVPYSElengkrDVDITIIFASGFHGDSSPFDGEGGF 205
Cdd:cd04278   1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGQ------EADIRISFARGNHGDGYPFDGPGGT 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13027802 206 LAHAYFPGpGIGGDTHFDSDEPWTLGNpNHDGNDLFLVAVHELGHALGLEHSNDPTAIMAPFYQYMETdNFKLPNDDLQG 285
Cdd:cd04278  75 LAHAFFPG-GIGGDIHFDDDEQWTLGS-DSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVP-KFKLSQDDIRG 151


                ....*.
gi 13027802 286 IQKIYG 291
Cdd:cd04278 152 IQALYG 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 340-532 3.17e-77

Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metalloproteinases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metalloproteinases (TIMPs). This CD contains 4 instances of the repeat.


Pssm-ID: 238046 [Multi-domain]  Cd Length: 194  Bit Score: 243.37  E-value: 3.17e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13027802 340 PNICDG-NFNTLAILRREMFVFKDQWFWRVRNNRvMDGYPMQITYFWRGLPPSIDAVYENSD-GNFVFFKGNKYWVFKDT 417
Cdd:cd00094   1 PDACDPlSFDAVTTLRGELYFFKGRYFWRLSPGK-PPGSPFLISSFWPSLPSPVDAAFERPDtGKIYFFKGDKYWVYTGK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13027802 418 TLQPGYPHDLITLGSGIPPHGIDSAIWWEDVGKTYFFKGDRYWRYSEEMKTMDPGYPK-PITVWKGIPESPQGAFvHKEN 496
Cdd:cd00094  80 NLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKlIETDFPGVPDKVDAAF-RWLD 158

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 13027802 497 GFTYFYKGKEYWKFNNQILKVEPGYPRSILKDFMGC 532
Cdd:cd00094 159 GYYYFFKGDQYWRFDPRSKEVRVGYPLKISSDWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 125-292 3.62e-34

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: 126.70  E-value: 3.62e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13027802    125 QKWQHKHITYSIKnvTPKVgDPETRKAIRRAFDVWQNVTPLTFEEVPYSElengkrdvDITIIFASGFHGdsspfdgegG 204
Cdd:smart00235   3 KKWPKGTVPYVID--SSSL-SPEEREAIAKALAEWSDVTCIRFVERTGTA--------DIYISFGSGDSG---------C 62

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13027802    205 FLAHAYFPGpgigGDTHFDsDEPWTLGnpnhdgndlFLVAVHELGHALGLEHSNDPTA---IMAPFYQYMETDNFKLPND 281
Cdd:smart00235  63 TLSHAGRPG----GDQHLS-LGNGCIN---------TGVAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFDLSED 128

                          170
                   ....*....|.
gi 13027802    282 DLQGIQKIYGP 292
Cdd:smart00235 129 DSLGIPYDYGS 139
DUF3377 pfam11857
Domain of unknown function (DUF3377); This domain is functionally uncharacterized. This domain ...
 537-607 4.73e-32

Domain of unknown function (DUF3377); This domain is functionally uncharacterized. This domain is found in eukaryotes. This presumed domain is about 70 amino acids in length.


Pssm-ID: 463374  Cd Length: 72  Bit Score: 118.19  E-value: 4.73e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13027802   537 DRVKEGHSPPDDVDIVIKLDNTAS-TVKAIAIVIPCILALCLLVLVYTVFQFKRKGTPRHILYCKRSMQEWV 607
Cdd:pfam11857   1 DREEDRHEEEDEVDIVVVIDDVASgTVNAIAVVVPLVLLLCILVLIYAIVQFQRKGTPRRLLYCKRSLQDWV 72
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 132-291 5.37e-19

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: 84.05  E-value: 5.37e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13027802 132 ITYSIKNVTPKVGDPETR--KAIRRAFDVWQNVTPLTFEEVPyseleNGKRDVDITIifasgFHGDSSPFDGEGGFLAHA 209
Cdd:cd04279   4 IRVYIDPTPAPPDSRAQSwlQAVKQAAAEWENVGPLKFVYNP-----EEDNDADIVI-----FFDRPPPVGGAGGGLARA 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13027802 210 YFPGPGIGGDTHFDSDEPWTLGNPNHDGNDLFLVAVHELGHALGLEHSND-PTAIMAPFYQYMETDNFKLPNDDLQGIQK 288
Cdd:cd04279  74 GFPLISDGNRKLFNRTDINLGPGQPRGAENLQAIALHELGHALGLWHHSDrPEDAMYPSQGQGPDGNPTLSARDVATLKR 153


                ...
gi 13027802 289 IYG 291
Cdd:cd04279 154 LYG 156
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 146-291 1.18e-17

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: 81.31  E-value: 1.18e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13027802 146 PETRKAIRRAFDVWQNVTPLTFEEVPYSElengkrDVDITIIFASGFHGDSspfdgeggfLAHAYFPGPGI----GGDTH 221
Cdd:cd04277  33 AAQQAAARDALEAWEDVADIDFVEVSDNS------GADIRFGNSSDPDGNT---------AGYAYYPGSGSgtayGGDIW 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13027802 222 FDSDEpwtLGNPNHDGNDLFLVAVHELGHALGLEHSND-----PTAIMAPFYQYMET-----DNFKLPND---------- 281
Cdd:cd04277  98 FNSSY---DTNSDSPGSYGYQTIIHEIGHALGLEHPGDynggdPVPPTYALDSREYTvmsynSGYGNGASagggypqtpm 174

                       170
                ....*....|..
gi 13027802 282 --DLQGIQKIYG 291
Cdd:cd04277 175 llDIAALQYLYG 186
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 439-484 1.74e-12

Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metallopeptidases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metallopeptidases (TIMPs).


Pssm-ID: 395000 [Multi-domain]  Cd Length: 44  Bit Score: 61.81  E-value: 1.74e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 13027802   439 IDSAIWWEDvGKTYFFKGDRYWRYSEEmkTMDPGYPKPITVWKGIP 484
Cdd:pfam00045   1 IDAAFEDRD-GKTYFFKGRKYWRFDPQ--RVEPGYPKLISDFPGLP 43
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 439-484 7.32e-12

Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metalloproteinases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metalloproteinases (TIMPs).


Pssm-ID: 214524 [Multi-domain]  Cd Length: 45  Bit Score: 60.33  E-value: 7.32e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 13027802    439 IDSAIWWEDvGKTYFFKGDRYWRYSEemKTMDPGYPKPIT-VWKGIP 484
Cdd:smart00120   1 IDAAFELRD-GKTYFFKGDKYWRFDP--KRVDPGYPKLISsFFPGLP 44
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 149-290 1.41e-10

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: 60.23  E-value: 1.41e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13027802 149 RKAIRRAFDVWQNVTPLTFEEVPYselenGKRDVDITIIFASGfhgdsspfDGEGGFLAHAYFPG--PGIGGDTHFDSDE 226
Cdd:cd00203  24 QSLILIAMQIWRDYLNIRFVLVGV-----EIDKADIAILVTRQ--------DFDGGTGGWAYLGRvcDSLRGVGVLQDNQ 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13027802 227 PWTlgnpnhdgNDLFLVAVHELGHALGLEHSNDPTA--------------------IMAPFY-QYMETDNFKLPNDDLQG 285
Cdd:cd00203  91 SGT--------KEGAQTIAHELGHALGFYHDHDRKDrddyptiddtlnaedddyysVMSYTKgSFSDGQRKDFSQCDIDQ 162


                ....*
gi 13027802 286 IQKIY 290
Cdd:cd00203 163 INKLY 167
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 392-436 2.24e-10

Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metalloproteinases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metalloproteinases (TIMPs).


Pssm-ID: 214524 [Multi-domain]  Cd Length: 45  Bit Score: 56.10  E-value: 2.24e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 13027802    392 IDAVYENSDGNFVFFKGNKYWVFKDTTLQPGYPHDLITLGSGIPP 436
Cdd:smart00120   1 IDAAFELRDGKTYFFKGDKYWRFDPKRVDPGYPKLISSFFPGLPC 45
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 392-436 3.95e-10

Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metallopeptidases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metallopeptidases (TIMPs).


Pssm-ID: 395000 [Multi-domain]  Cd Length: 44  Bit Score: 55.27  E-value: 3.95e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 13027802   392 IDAVYENSDGNFVFFKGNKYWVFKDTTLQPGYPHdLITLGSGIPP 436
Cdd:pfam00045   1 IDAAFEDRDGKTYFFKGRKYWRFDPQRVEPGYPK-LISDFPGLPC 44
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 132-274 8.84e-09

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: 54.81  E-value: 8.84e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13027802 132 ITYSIKNVTPKvgdpETRKAIRRAFDVWQNVTPLTFEEVpyseleNGKRDVDITIIFASGFHGDsspfDGEGGFLAHAYF 211
Cdd:cd04268   4 ITYYIDDSVPD----KLRAAILDAIEAWNKAFAIGFKNA------NDVDPADIRYSVIRWIPYN----DGTWSYGPSQVD 69

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13027802 212 PGPG--IGGDTHFDSDEPWTLGNPNHDgndlflVAVHELGHALGLEHSNDPTAIMAPFYQYMETD 274
Cdd:cd04268  70 PLTGeiLLARVYLYSSFVEYSGARLRN------TAEHELGHALGLRHNFAASDRDDNVDLLAEKG 128
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 354-390 2.41e-07

Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metalloproteinases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metalloproteinases (TIMPs).


Pssm-ID: 214524 [Multi-domain]  Cd Length: 45  Bit Score: 47.24  E-value: 2.41e-07
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 13027802    354 RREMFVFKDQWFWRVRNNRVMDGYPMQITYFWRGLPP 390
Cdd:smart00120   9 DGKTYFFKGDKYWRFDPKRVDPGYPKLISSFFPGLPC 45
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 490-531 9.61e-07

Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metalloproteinases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metalloproteinases (TIMPs).


Pssm-ID: 214524 [Multi-domain]  Cd Length: 45  Bit Score: 45.70  E-value: 9.61e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 13027802    490 AFVHKENGFTYFYKGKEYWKFNNQilKVEPGYPRSILKDFMG 531
Cdd:smart00120   3 AAFELRDGKTYFFKGDKYWRFDPK--RVDPGYPKLISSFFPG 42
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 490-532 1.03e-06

Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metallopeptidases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metallopeptidases (TIMPs).


Pssm-ID: 395000 [Multi-domain]  Cd Length: 44  Bit Score: 45.64  E-value: 1.03e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 13027802   490 AFVHKENGFTYFYKGKEYWKFNNQilKVEPGYPRSILKD-FMGC 532
Cdd:pfam00045   3 AAFEDRDGKTYFFKGRKYWRFDPQ--RVEPGYPKLISDFpGLPC 44
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 354-390 2.46e-06

Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. Hemopexin-like repeats occur in vitronectin and some matrix metallopeptidases family (matrixins). The HX repeats of some matrixins bind tissue inhibitor of metallopeptidases (TIMPs).


Pssm-ID: 395000 [Multi-domain]  Cd Length: 44  Bit Score: 44.48  E-value: 2.46e-06
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 13027802   354 RREMFVFKDQWFWRVRNNRVMDGYPMQITYFwRGLPP 390
Cdd:pfam00045   9 DGKTYFFKGRKYWRFDPQRVEPGYPKLISDF-PGLPC 44
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 146-266 2.92e-06

Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 48.91  E-value: 2.92e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13027802 146 PETRKAIRRAFDVWQNVtpLTFEEVpyselENGKRdVDITIIFAS---GFHGDSSP----------FDGEGGFLAHAYfp 212
Cdd:COG5549 100 QQWVAAVLQAIAEWNAY--LPLEVV-----ENPEN-ADIIIVRSNpplTASPNPETgarsaettyeFYDTGNILSHRF-- 169

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 13027802 213 gpgiggdthfdsdepwTLG-NPNHDGNDLFLVAVHELGHALGLE-HSNDPTAIMAP 266
Cdd:COG5549 170 ----------------TILlSPNQTGKYLLATARHELGHALGIWgHSPSPTDAMYF 209
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 46-96 3.26e-06

Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This domain is found at the N or C terminus of a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. This family is found N-terminal to the catalytic domain of matrixins. The domain is found to bind peptidoglycan experimentally.


Pssm-ID: 460223 [Multi-domain]  Cd Length: 57  Bit Score: 44.43  E-value: 3.26e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 13027802    46 WLQKYGYLPPTdprmSVLRSAETMQSALAAMQQFYGINMTGKVDRNTIDWM 96
Cdd:pfam01471  11 YLNRLGYYPGP----VDGYFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
archmetzin NF033823
archaemetzincin family Zn-dependent metalloprotease;
236-264 1.30e-04

archaemetzincin family Zn-dependent metalloprotease;


Pssm-ID: 468195  Cd Length: 170  Bit Score: 42.99  E-value: 1.30e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 13027802  236 DGNDLFL-----VAVHELGHALGLEHSNDPTAIM 264
Cdd:NF033823 113 PDEDLFLerlakEAVHELGHLLGLGHCPNPRCVM 146
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
239-266 2.03e-04

Predicted Zn-dependent protease [General function prediction only];


Pssm-ID: 441517  Cd Length: 175  Bit Score: 42.25  E-value: 2.03e-04
                        10        20        30
                ....*....|....*....|....*....|...
gi 13027802 239 DLFL-----VAVHELGHALGLEHSNDPTAIMAP 266
Cdd:COG1913 117 ELFLervlkEAVHELGHLFGLGHCPNPRCVMHF 149
ZnMc_MMP_like_3 cd04327
Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal ...
 144-256 2.92e-04

Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal metalloproteinase domains similar to matrix metalloproteinases and astacin.


Pssm-ID: 239819 [Multi-domain]  Cd Length: 198  Bit Score: 42.37  E-value: 2.92e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13027802 144 GDPETRKAIRRAFDVWQNVTPLTFEEVpyselenGKRDVDITIIFASGfHGDSSpFDGEGGFLAHAYFPGPGIGGDTHFD 223
Cdd:cd04327  17 PDAFLKDKVRAAAREWLPYANLKFKFV-------TDADADIRISFTPG-DGYWS-YVGTDALLIGADAPTMNLGWFTDDT 87

                        90       100       110
                ....*....|....*....|....*....|...
gi 13027802 224 SDepwtlgnpnhdgNDLFLVAVHELGHALGLEH 256
Cdd:cd04327  88 PD------------PEFSRVVLHEFGHALGFIH 108
PHA03247 PHA03247
large tegument protein UL36; Provisional
 292-338 4.03e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.77  E-value: 4.03e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 13027802   292 PPDKIPPPTRPLPTVPPhrsIPPADPRKNDRPKPPRPPTGRPSYPGA 338
Cdd:PHA03247 2901 PPDQPERPPQPQAPPPP---QPQPQPPPPPQPQPPPPPPPRPQPPLA 2944
ZnMc_pappalysin_like cd04275
Zinc-dependent metalloprotease, pappalysin_like subfamily. The pregnancy-associated plasma ...
 200-256 3.07e-03

Zinc-dependent metalloprotease, pappalysin_like subfamily. The pregnancy-associated plasma protein A (PAPP-A or pappalysin-1) cleaves insulin-like growth factor-binding proteins 4 and 5, thereby promoting cell growth by releasing bound growth factor. This model includes pappalysins and related metalloprotease domains from all three kingdoms of life. The three-dimensional structure of an archaeal representative, ulilysin, has been solved.


Pssm-ID: 239802 [Multi-domain]  Cd Length: 225  Bit Score: 39.63  E-value: 3.07e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 13027802 200 DGEGGFLAHAYFPGPGIGGDTHFD--SDEPWTLGNPNHDGNDLFLVAVHELGHALGLEH 256
Cdd:cd04275  95 FLGGGLLGYATFPDSLVSLAFITDgvVINPSSLPGGSAAPYNLGDTATHEVGHWLGLYH 153
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
 236-266 4.33e-03

Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 (archaemetzincin or archaelysin) is a zinc-dependent aminopeptidase that contains the consensus zinc-binding sequence HEXXHXXGXXH/D and a conserved Met residue at the active site, and is thus classified as a metzincin. Archaemetzincins, first identified in archaea, are also found in bacteria and eukaryotes, including two human members, archaemetzincin-1 and -2 (AMZ1 and AMZ2). AMZ1 is mainly found in the liver and heart while AMZ2 is primarily expressed in testis and heart; both have been reported to degrade synthetic substrates and peptides. The Peptidase M54 family contains an extended metzincin concensus sequence of HEXXHXXGX3CX4CXMX17CXXC such that a second zinc ion is bound to four cysteines, thus resembling a zinc finger. Phylogenetic analysis of this family reveals a complex evolutionary process involving a series of lateral gene transfer, gene loss and genetic duplication events.


Pssm-ID: 213029  Cd Length: 173  Bit Score: 38.43  E-value: 4.33e-03
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 13027802 236 DGNDLFL-----VAVHELGHALGLEHSNDPTAIMAP 266
Cdd:cd11375 114 PDEGLFLerllkEAVHELGHLFGLDHCPYYACVMNF 149
PRK13267 PRK13267
archaemetzincin-like protein; Reviewed
 244-264 4.69e-03

archaemetzincin-like protein; Reviewed


Pssm-ID: 237325  Cd Length: 179  Bit Score: 38.46  E-value: 4.69e-03
                         10        20
                 ....*....|....*....|.
gi 13027802  244 AVHELGHALGLEHSNDPTAIM 264
Cdd:PRK13267 129 VTHELGHTLGLEHCDNPRCVM 149
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 235-267 9.31e-03

Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom zinc endopeptidase. This subfamily contains other snake venom metalloproteinases, as well as membrane-anchored metalloproteases belonging to the ADAM family. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions.


Pssm-ID: 239797 [Multi-domain]  Cd Length: 194  Bit Score: 37.59  E-value: 9.31e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 13027802 235 HDGNDLFLVAV---HELGHALGLEHSN------DPTAIMAPF 267
Cdd:cd04269 123 DHSRNLLLFAVtmaHELGHNLGMEHDDggctcgRSTCIMAPS 164
 
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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