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Conserved domains on  [gi|148233994|ref|NP_001085262|]
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matrix metallopeptidase 16 (membrane-inserted) precursor [Xenopus laevis]

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List of domain hits

Name Accession Description Interval E-value
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
130-295 1.37e-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: 260.99  E-value: 1.37e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148233994 130 KWHHKHITYSIKNVTPKVGDLETRKAIRRAFDVWQNVTPLTFEEVPYcelengKRDVDITIIFASGFHGDSSPFDGEGGF 209
Cdd:cd04278    1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTS------GQEADIRISFARGNHGDGYPFDGPGGT 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148233994 210 LAHAYFPGpGIGGDTHFDSDEPWTLGNpNHDGNDLFLVAVHELGHALGLEHSNDPTAIMAPFYQYMETdNFKLPTDDLQG 289
Cdd:cd04278   75 LAHAFFPG-GIGGDIHFDDDEQWTLGS-DSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVP-KFKLSQDDIRG 151

                 ....*.
gi 148233994 290 IQKIYG 295
Cdd:cd04278  152 IQALYG 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
346-538 7.02e-76

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: 242.22  E-value: 7.02e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148233994 346 PNICDG-NFNTLAILRREMFVFKDQWFWRVRNNKvMDGYPMQITYFWRGLPPGIDAVYENG-EGNFVFFKGNKYWVFKDT 423
Cdd:cd00094    1 PDACDPlSFDAVTTLRGELYFFKGRYFWRLSPGK-PPGSPFLISSFWPSLPSPVDAAFERPdTGKIYFFKGDKYWVYTGK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148233994 424 TLQPGYPYDLMHLGHGIPPHGIDTAVWWEDVGKTYFFKGDRYWRYNEEMRAMDPGYPKLI-TVWKGIPESPQGAFvDKEN 502
Cdd:cd00094   80 NLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIeTDFPGVPDKVDAAF-RWLD 158
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 148233994 503 GYTYFYKGKEYWKFQNLNLRVEPGYPRSILKDFMGC 538
Cdd:cd00094  159 GYYYFFKGDQYWRFDPRSKEVRVGYPLKISSDWLGC 194
DUF3377 pfam11857
Domain of unknown function (DUF3377); This domain is functionally uncharacterized. This domain ...
540-613 1.16e-41

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: 256677  Cd Length: 74  Bit Score: 145.12  E-value: 1.16e-41
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148233994  540 SSTDGDKERTSPQDDVDIVIKLDNTASTVKAIAIVIPCILALCLLVLVYTVFQFKRKGTPRHILYCKRSMQEWV 613
Cdd:pfam11857   1 GPSDERRDRGRPEDDVDIVVEVDEVPGTVNAAAVVIPLVLLLCILVLLYTIVQFKRKGTPRHLLYCKRSLQEWV 74
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
42-93 2.48e-07

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: 250643  Cd Length: 57  Bit Score: 48.30  E-value: 2.48e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 148233994   42 AEMWLQKYGYLPPT-DprmsvLRSSETMQSAIAAMQQFYGINVTGKIDKNTID 93
Cdd:pfam01471   8 LQRYLKRLGYYPGPvD-----GVFGPSTEAAVKAFQRFFGLPVTGIVDPETLA 55
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
130-295 2.58e-83

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


:

Pssm-ID: 249842 [Multi-domain]  Cd Length: 158  Bit Score: 260.26  E-value: 2.58e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148233994  130 KWHHKHITYSIKNVTPKVGDLETRKAIRRAFDVWQNVTPLTFEEVPycelengKRDVDITIIFASGFHGDSSPFDGEGGF 209
Cdd:pfam00413   1 KWPKKNLTYRIVNYTPDLPRAEVRKAIRRAFKVWSEVTPLTFTEVT-------EGTADIMIGFGRGDHGDGYPFDGPGGV 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148233994  210 LAHAYFPGPgIGGDTHFDSDEPWTLGNPNHDGNDLFLVAVHELGHALGLEHSNDPTAIMAPFYQYMETDNFKLPTDDLQG 289
Cdd:pfam00413  74 LAHAFPPGP-IGGDIHFDDDETWTVGSDAPNGINLFLVAAHEIGHALGLGHSSDPDAIMYPYYSPYVKPVFRLDQDDIKG 152

                  ....*.
gi 148233994  290 IQKIYG 295
Cdd:pfam00413 153 IQQLYG 158
 
Name Accession Description Interval E-value
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
130-295 1.37e-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: 260.99  E-value: 1.37e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148233994 130 KWHHKHITYSIKNVTPKVGDLETRKAIRRAFDVWQNVTPLTFEEVPYcelengKRDVDITIIFASGFHGDSSPFDGEGGF 209
Cdd:cd04278    1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTS------GQEADIRISFARGNHGDGYPFDGPGGT 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148233994 210 LAHAYFPGpGIGGDTHFDSDEPWTLGNpNHDGNDLFLVAVHELGHALGLEHSNDPTAIMAPFYQYMETdNFKLPTDDLQG 289
Cdd:cd04278   75 LAHAFFPG-GIGGDIHFDDDEQWTLGS-DSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVP-KFKLSQDDIRG 151

                 ....*.
gi 148233994 290 IQKIYG 295
Cdd:cd04278  152 IQALYG 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
346-538 7.02e-76

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: 242.22  E-value: 7.02e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148233994 346 PNICDG-NFNTLAILRREMFVFKDQWFWRVRNNKvMDGYPMQITYFWRGLPPGIDAVYENG-EGNFVFFKGNKYWVFKDT 423
Cdd:cd00094    1 PDACDPlSFDAVTTLRGELYFFKGRYFWRLSPGK-PPGSPFLISSFWPSLPSPVDAAFERPdTGKIYFFKGDKYWVYTGK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148233994 424 TLQPGYPYDLMHLGHGIPPHGIDTAVWWEDVGKTYFFKGDRYWRYNEEMRAMDPGYPKLI-TVWKGIPESPQGAFvDKEN 502
Cdd:cd00094   80 NLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIeTDFPGVPDKVDAAF-RWLD 158
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 148233994 503 GYTYFYKGKEYWKFQNLNLRVEPGYPRSILKDFMGC 538
Cdd:cd00094  159 GYYYFFKGDQYWRFDPRSKEVRVGYPLKISSDWLGC 194
DUF3377 pfam11857
Domain of unknown function (DUF3377); This domain is functionally uncharacterized. This domain ...
540-613 1.16e-41

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: 256677  Cd Length: 74  Bit Score: 145.12  E-value: 1.16e-41
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148233994  540 SSTDGDKERTSPQDDVDIVIKLDNTASTVKAIAIVIPCILALCLLVLVYTVFQFKRKGTPRHILYCKRSMQEWV 613
Cdd:pfam11857   1 GPSDERRDRGRPEDDVDIVVEVDEVPGTVNAAAVVIPLVLLLCILVLLYTIVQFKRKGTPRHLLYCKRSLQEWV 74
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
445-490 4.00e-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  Cd Length: 45  Bit Score: 61.88  E-value: 4.00e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 148233994   445 IDTAVWWEDvGKTYFFKGDRYWRYNEEmrAMDPGYPKLIT-VWKGIP 490
Cdd:smart00120   1 IDAAFELRD-GKTYFFKGDKYWRFDPK--RVDPGYPKLISsFFPGLP 44
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
445-490 1.15e-11

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: 249537  Cd Length: 45  Bit Score: 60.68  E-value: 1.15e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 148233994  445 IDTAVWWEDvGKTYFFKGDRYWRYNEEMraMDPGYPKLITV-WKGIP 490
Cdd:pfam00045   1 IDAAFEDRD-GKTYFFKGRKYWRFDPQR--VEPGYPKLISDfWPGLP 44
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
42-93 2.48e-07

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: 250643  Cd Length: 57  Bit Score: 48.30  E-value: 2.48e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 148233994   42 AEMWLQKYGYLPPT-DprmsvLRSSETMQSAIAAMQQFYGINVTGKIDKNTID 93
Cdd:pfam01471   8 LQRYLKRLGYYPGPvD-----GVFGPSTEAAVKAFQRFFGLPVTGIVDPETLA 55
PRK13267 PRK13267
archaemetzincin-like protein; Reviewed
248-268 1.80e-03

archaemetzincin-like protein; Reviewed


Pssm-ID: 237325  Cd Length: 179  Bit Score: 38.46  E-value: 1.80e-03
                         10        20
                 ....*....|....*....|.
gi 148233994 248 AVHELGHALGLEHSNDPTAIM 268
Cdd:PRK13267 129 VTHELGHTLGLEHCDNPRCVM 149
COG1913 COG1913
Predicted Zn-dependent proteases [General function prediction only]
238-278 1.86e-03

Predicted Zn-dependent proteases [General function prediction only]


Pssm-ID: 224825  Cd Length: 181  Bit Score: 38.51  E-value: 1.86e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 148233994 238 NHDGNDLFLV-----AVHELGHALGLEHSNDPTAIMAPFYQYMETD 278
Cdd:COG1913  113 YTPDRELFKErvvkeVLHELGHLLGLSHCPNPRCVMNFSNSLRDVD 158
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
130-295 2.58e-83

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


Pssm-ID: 249842 [Multi-domain]  Cd Length: 158  Bit Score: 260.26  E-value: 2.58e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148233994  130 KWHHKHITYSIKNVTPKVGDLETRKAIRRAFDVWQNVTPLTFEEVPycelengKRDVDITIIFASGFHGDSSPFDGEGGF 209
Cdd:pfam00413   1 KWPKKNLTYRIVNYTPDLPRAEVRKAIRRAFKVWSEVTPLTFTEVT-------EGTADIMIGFGRGDHGDGYPFDGPGGV 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148233994  210 LAHAYFPGPgIGGDTHFDSDEPWTLGNPNHDGNDLFLVAVHELGHALGLEHSNDPTAIMAPFYQYMETDNFKLPTDDLQG 289
Cdd:pfam00413  74 LAHAFPPGP-IGGDIHFDDDETWTVGSDAPNGINLFLVAAHEIGHALGLGHSSDPDAIMYPYYSPYVKPVFRLDQDDIKG 152

                  ....*.
gi 148233994  290 IQKIYG 295
Cdd:pfam00413 153 IQQLYG 158
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
129-296 5.71e-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: 126.31  E-value: 5.71e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148233994   129 QKWHHKHITYSIKnvTPKVGDlETRKAIRRAFDVWQNVTPLTFEEVPYcelengkrDVDITIIFASGFHGdsspfdgegG 208
Cdd:smart00235   3 KKWPKGTVPYVID--SSSLSP-EEREAIAKALAEWSDVTCIRFVERTG--------TADIYISFGSGDSG---------C 62
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148233994   209 FLAHAYFPGpgigGDTHFDsDEPWTLGnpnhdgndlFLVAVHELGHALGLEHSNDPTA---IMAPFYQYMETDNFKLPTD 285
Cdd:smart00235  63 TLSHAGRPG----GDQHLS-LGNGCIN---------TGVAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFDLSED 128
                          170
                   ....*....|.
gi 148233994   286 DLQGIQKIYGP 296
Cdd:smart00235 129 DSLGIPYDYGS 139
PHA03247 PHA03247
large tegument protein UL36; Provisional
277-357 5.18e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 45.31  E-value: 5.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148233994  277 TDNFKLPTDDLQgiqkiygPPEKAPAPTKPLPTVPPHRSVPPVDPRKNDRQPKPPRPPTGDKPSYPGAKPNICDGNFNTL 356
Cdd:PHA03247 2895 TESFALPPDQPE-------RPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGAL 2967

                  .
gi 148233994  357 A 357
Cdd:PHA03247 2968 V 2968
PHA03247 PHA03247
large tegument protein UL36; Provisional
202-346 7.10e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.93  E-value: 7.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148233994  202 PFDGEGGFLAHAYfPGPGIGGDTHFDS-------------DEPwtLGNPNHDgndLFLVAVHELgHALGLEHSNDPTAIM 268
Cdd:PHA03247 2483 PAEARFPFAAGAA-PDPGGGGPPDPDAppapsrlapailpDEP--VGEPVHP---RMLTWIRGL-EELASDDAGDPPPPL 2555
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148233994  269 APFYQYMETDNfKLPtddlqgiqkiygPPEKAPAPTKPL-------PTVPPHRSVP--PVDPRKNDRQPKPPRPPTGD-- 337
Cdd:PHA03247 2556 PPAAPPAAPDR-SVP------------PPRPAPRPSEPAvtsrarrPDAPPQSARPraPVDDRGDPRGPAPPSPLPPDth 2622
                         170
                  ....*....|.
gi 148233994  338 --KPSYPGAKP 346
Cdd:PHA03247 2623 apDPPPPSPSP 2633
PRK14950 PRK14950
DNA polymerase III subunits gamma and tau; Provisional
301-346 8.25e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 40.95  E-value: 8.25e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 148233994 301 PAPTKPlPTVPPHRSVPPVDPrKNDRQPKPPRPPTGDKPSYPGAKP 346
Cdd:PRK14950 383 PAPSTR-PKAAAAANIPPKEP-VRETATPPPVPPRPVAPPVPHTPE 426
FAP pfam07174
Fibronectin-attachment protein (FAP); This family contains bacterial fibronectin-attachment ...
296-347 9.80e-04

Fibronectin-attachment protein (FAP); This family contains bacterial fibronectin-attachment proteins (FAP). Family members are rich in alanine and proline, are approximately 300 long, and seem to be restricted to mycobacteria. These proteins contain a fibronectin-binding motif that allows mycobacteria to bind to fibronectin in the extracellular matrix.


Pssm-ID: 254090 [Multi-domain]  Cd Length: 297  Bit Score: 40.26  E-value: 9.80e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 148233994  296 PPEKAPAPTKPLPTVPPHRSVPPVDPRKNDRQPKPPRPP-TGDKPSYPGAKPN 347
Cdd:pfam07174  47 PPSTAAAAPAPAAPPPPPPPAAPPAPQPDDPNAAPPPPPaDPNAPPPPPVDPN 99
 
Name Accession Description Interval E-value
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
130-295 1.37e-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: 260.99  E-value: 1.37e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148233994 130 KWHHKHITYSIKNVTPKVGDLETRKAIRRAFDVWQNVTPLTFEEVPYcelengKRDVDITIIFASGFHGDSSPFDGEGGF 209
Cdd:cd04278    1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTS------GQEADIRISFARGNHGDGYPFDGPGGT 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148233994 210 LAHAYFPGpGIGGDTHFDSDEPWTLGNpNHDGNDLFLVAVHELGHALGLEHSNDPTAIMAPFYQYMETdNFKLPTDDLQG 289
Cdd:cd04278   75 LAHAFFPG-GIGGDIHFDDDEQWTLGS-DSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVP-KFKLSQDDIRG 151

                 ....*.
gi 148233994 290 IQKIYG 295
Cdd:cd04278  152 IQALYG 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
346-538 7.02e-76

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: 242.22  E-value: 7.02e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148233994 346 PNICDG-NFNTLAILRREMFVFKDQWFWRVRNNKvMDGYPMQITYFWRGLPPGIDAVYENG-EGNFVFFKGNKYWVFKDT 423
Cdd:cd00094    1 PDACDPlSFDAVTTLRGELYFFKGRYFWRLSPGK-PPGSPFLISSFWPSLPSPVDAAFERPdTGKIYFFKGDKYWVYTGK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148233994 424 TLQPGYPYDLMHLGHGIPPHGIDTAVWWEDVGKTYFFKGDRYWRYNEEMRAMDPGYPKLI-TVWKGIPESPQGAFvDKEN 502
Cdd:cd00094   80 NLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKLIeTDFPGVPDKVDAAF-RWLD 158
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 148233994 503 GYTYFYKGKEYWKFQNLNLRVEPGYPRSILKDFMGC 538
Cdd:cd00094  159 GYYYFFKGDQYWRFDPRSKEVRVGYPLKISSDWLGC 194
DUF3377 pfam11857
Domain of unknown function (DUF3377); This domain is functionally uncharacterized. This domain ...
540-613 1.16e-41

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: 256677  Cd Length: 74  Bit Score: 145.12  E-value: 1.16e-41
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148233994  540 SSTDGDKERTSPQDDVDIVIKLDNTASTVKAIAIVIPCILALCLLVLVYTVFQFKRKGTPRHILYCKRSMQEWV 613
Cdd:pfam11857   1 GPSDERRDRGRPEDDVDIVVEVDEVPGTVNAAAVVIPLVLLLCILVLLYTIVQFKRKGTPRHLLYCKRSLQEWV 74
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
136-295 5.20e-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  Cd Length: 156  Bit Score: 84.43  E-value: 5.20e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148233994 136 ITYSIKNVTPKVGDLETR--KAIRRAFDVWQNVTPLTFEEVPyceleNGKRDVDITIifasgFHGDSSPFDGEGGFLAHA 213
Cdd:cd04279    4 IRVYIDPTPAPPDSRAQSwlQAVKQAAAEWENVGPLKFVYNP-----EEDNDADIVI-----FFDRPPPVGGAGGGLARA 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148233994 214 YFPGPGIGGDTHFDSDEPWTLGNPNHDGNDLFLVAVHELGHALGLEHSND-PTAIMAPFYQYMETDNFKLPTDDLQGIQK 292
Cdd:cd04279   74 GFPLISDGNRKLFNRTDINLGPGQPRGAENLQAIALHELGHALGLWHHSDrPEDAMYPSQGQGPDGNPTLSARDVATLKR 153

                 ...
gi 148233994 293 IYG 295
Cdd:cd04279  154 LYG 156
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
151-295 5.08e-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  Cd Length: 186  Bit Score: 79.38  E-value: 5.08e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148233994 151 ETRKAIRRAFDVWQNVTPLTFEEVPYcelengKRDVDITIIFASGFHGDSspfdgeggfLAHAYFPGPGI----GGDTHF 226
Cdd:cd04277   34 AQQAAARDALEAWEDVADIDFVEVSD------NSGADIRFGNSSDPDGNT---------AGYAYYPGSGSgtayGGDIWF 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148233994 227 DSDEpwtLGNPNHDGNDLFLVAVHELGHALGLEHSND-----PTAIMAPFYQYMET-------------DNFKLPT---- 284
Cdd:cd04277   99 NSSY---DTNSDSPGSYGYQTIIHEIGHALGLEHPGDynggdPVPPTYALDSREYTvmsynsgygngasAGGGYPQtpml 175
                        170
                 ....*....|.
gi 148233994 285 DDLQGIQKIYG 295
Cdd:cd04277  176 LDIAALQYLYG 186
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
445-490 4.00e-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  Cd Length: 45  Bit Score: 61.88  E-value: 4.00e-12
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 148233994   445 IDTAVWWEDvGKTYFFKGDRYWRYNEEmrAMDPGYPKLIT-VWKGIP 490
Cdd:smart00120   1 IDAAFELRD-GKTYFFKGDKYWRFDPK--RVDPGYPKLISsFFPGLP 44
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
445-490 1.15e-11

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: 249537  Cd Length: 45  Bit Score: 60.68  E-value: 1.15e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 148233994  445 IDTAVWWEDvGKTYFFKGDRYWRYNEEMraMDPGYPKLITV-WKGIP 490
Cdd:pfam00045   1 IDAAFEDRD-GKTYFFKGRKYWRFDPQR--VEPGYPKLISDfWPGLP 44
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
153-294 7.15e-11

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  Cd Length: 167  Bit Score: 60.61  E-value: 7.15e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148233994 153 RKAIRRAFDVWQNVTPLTFEEVPYcelenGKRDVDITIIFASGfhgdsspfDGEGGFLAHAYFPG--PGIGGDTHFDSDE 230
Cdd:cd00203   24 QSLILIAMQIWRDYLNIRFVLVGV-----EIDKADIAILVTRQ--------DFDGGTGGWAYLGRvcDSLRGVGVLQDNQ 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148233994 231 PWTlgnpnhdgNDLFLVAVHELGHALGLEHSNDPTA--------------------IMAPFY-QYMETDNFKLPTDDLQG 289
Cdd:cd00203   91 SGT--------KEGAQTIAHELGHALGFYHDHDRKDrddyptiddtlnaedddyysVMSYTKgSFSDGQRKDFSQCDIDQ 162

                 ....*
gi 148233994 290 IQKIY 294
Cdd:cd00203  163 INKLY 167
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
136-294 1.06e-09

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


Pssm-ID: 239796  Cd Length: 165  Bit Score: 57.12  E-value: 1.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148233994 136 ITYSIKNVTPKvgdlETRKAIRRAFDVWQNVTPLTFEEVpyceleNGKRDVDITIIFASGFHGDsspfDGEGGFLAHAYF 215
Cdd:cd04268    4 ITYYIDDSVPD----KLRAAILDAIEAWNKAFAIGFKNA------NDVDPADIRYSVIRWIPYN----DGTWSYGPSQVD 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148233994 216 PGPG--IGGDTHFDSDEPWTLGNPNHDgndlflVAVHELGHALGLEHSN----------------DPTAIM--APFYQYM 275
Cdd:cd04268   70 PLTGeiLLARVYLYSSFVEYSGARLRN------TAEHELGHALGLRHNFaasdrddnvdllaekgDTSSVMdyAPSNFSI 143
                        170       180
                 ....*....|....*....|..
gi 148233994 276 ETDNFKLPT---DDLQGIQKIY 294
Cdd:cd04268  144 QLGDGQKYTigpYDIAAIKKLY 165
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
398-442 4.45e-09

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  Cd Length: 45  Bit Score: 53.02  E-value: 4.45e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 148233994   398 IDAVYENGEGNFVFFKGNKYWVFKDTTLQPGYPYDLMHLGHGIPP 442
Cdd:smart00120   1 IDAAFELRDGKTYFFKGDKYWRFDPKRVDPGYPKLISSFFPGLPC 45
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
398-442 6.85e-09

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: 249537  Cd Length: 45  Bit Score: 52.59  E-value: 6.85e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 148233994  398 IDAVYENGEGNFVFFKGNKYWVFKDTTLQPGYPYDLMHLGHGIPP 442
Cdd:pfam00045   1 IDAAFEDRDGKTYFFKGRKYWRFDPQRVEPGYPKLISDFWPGLPC 45
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
360-396 1.37e-08

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: 249537  Cd Length: 45  Bit Score: 51.82  E-value: 1.37e-08
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 148233994  360 RREMFVFKDQWFWRVRNNKVMDGYPMQITYFWRGLPP 396
Cdd:pfam00045   9 DGKTYFFKGRKYWRFDPQRVEPGYPKLISDFWPGLPC 45
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
42-93 2.48e-07

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: 250643  Cd Length: 57  Bit Score: 48.30  E-value: 2.48e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 148233994   42 AEMWLQKYGYLPPT-DprmsvLRSSETMQSAIAAMQQFYGINVTGKIDKNTID 93
Cdd:pfam01471   8 LQRYLKRLGYYPGPvD-----GVFGPSTEAAVKAFQRFFGLPVTGIVDPETLA 55
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
360-396 3.31e-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  Cd Length: 45  Bit Score: 47.62  E-value: 3.31e-07
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 148233994   360 RREMFVFKDQWFWRVRNNKVMDGYPMQITYFWRGLPP 396
Cdd:smart00120   9 DGKTYFFKGDKYWRFDPKRVDPGYPKLISSFFPGLPC 45
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
496-537 2.77e-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: 249537  Cd Length: 45  Bit Score: 44.89  E-value: 2.77e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 148233994  496 AFVDKENGYTYFYKGKEYWKFQnlNLRVEPGYPRSILKDFMG 537
Cdd:pfam00045   3 AAFEDRDGKTYFFKGRKYWRFD--PQRVEPGYPKLISDFWPG 42
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
501-537 9.88e-06

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  Cd Length: 45  Bit Score: 43.39  E-value: 9.88e-06
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 148233994   501 ENGYTYFYKGKEYWKFQnlNLRVEPGYPRSILKDFMG 537
Cdd:smart00120   8 RDGKTYFFKGDKYWRFD--PKRVDPGYPKLISSFFPG 42
ZnMc_MMP_like_3 cd04327
Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal ...
148-260 1.25e-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  Cd Length: 198  Bit Score: 41.98  E-value: 1.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148233994 148 GDLETRKAIRRAFDVWQNVTPLTFEEVpycelenGKRDVDITIIFASGfHGDSSpFDGEGGFLAHAYFPGPGIGGDTHFD 227
Cdd:cd04327   17 PDAFLKDKVRAAAREWLPYANLKFKFV-------TDADADIRISFTPG-DGYWS-YVGTDALLIGADAPTMNLGWFTDDT 87
                         90       100       110
                 ....*....|....*....|....*....|...
gi 148233994 228 SDepwtlgnpnhdgNDLFLVAVHELGHALGLEH 260
Cdd:cd04327   88 PD------------PEFSRVVLHEFGHALGFIH 108
ZnMc_pappalysin_like cd04275
Zinc-dependent metalloprotease, pappalysin_like subfamily. The pregnancy-associated plasma ...
204-260 1.04e-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  Cd Length: 225  Bit Score: 39.63  E-value: 1.04e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 148233994 204 DGEGGFLAHAYFPGPGIGGDTHFD--SDEPWTLGNPNHDGNDLFLVAVHELGHALGLEH 260
Cdd:cd04275   95 FLGGGLLGYATFPDSLVSLAFITDgvVINPSSLPGGSAAPYNLGDTATHEVGHWLGLYH 153
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
240-270 1.64e-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: 1.64e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 148233994 240 DGNDLFL-----VAVHELGHALGLEHSNDPTAIMAP 270
Cdd:cd11375  114 PDEGLFLerllkEAVHELGHLFGLDHCPYYACVMNF 149
PRK13267 PRK13267
archaemetzincin-like protein; Reviewed
248-268 1.80e-03

archaemetzincin-like protein; Reviewed


Pssm-ID: 237325  Cd Length: 179  Bit Score: 38.46  E-value: 1.80e-03
                         10        20
                 ....*....|....*....|.
gi 148233994 248 AVHELGHALGLEHSNDPTAIM 268
Cdd:PRK13267 129 VTHELGHTLGLEHCDNPRCVM 149
COG1913 COG1913
Predicted Zn-dependent proteases [General function prediction only]
238-278 1.86e-03

Predicted Zn-dependent proteases [General function prediction only]


Pssm-ID: 224825  Cd Length: 181  Bit Score: 38.51  E-value: 1.86e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 148233994 238 NHDGNDLFLV-----AVHELGHALGLEHSNDPTAIMAPFYQYMETD 278
Cdd:COG1913  113 YTPDRELFKErvvkeVLHELGHLLGLSHCPNPRCVMNFSNSLRDVD 158
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
239-271 3.59e-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  Cd Length: 194  Bit Score: 37.59  E-value: 3.59e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 148233994 239 HDGNDLFLVAV---HELGHALGLEHSN------DPTAIMAPF 271
Cdd:cd04269  123 DHSRNLLLFAVtmaHELGHNLGMEHDDggctcgRSTCIMAPS 164
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
130-295 2.58e-83

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


Pssm-ID: 249842 [Multi-domain]  Cd Length: 158  Bit Score: 260.26  E-value: 2.58e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148233994  130 KWHHKHITYSIKNVTPKVGDLETRKAIRRAFDVWQNVTPLTFEEVPycelengKRDVDITIIFASGFHGDSSPFDGEGGF 209
Cdd:pfam00413   1 KWPKKNLTYRIVNYTPDLPRAEVRKAIRRAFKVWSEVTPLTFTEVT-------EGTADIMIGFGRGDHGDGYPFDGPGGV 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148233994  210 LAHAYFPGPgIGGDTHFDSDEPWTLGNPNHDGNDLFLVAVHELGHALGLEHSNDPTAIMAPFYQYMETDNFKLPTDDLQG 289
Cdd:pfam00413  74 LAHAFPPGP-IGGDIHFDDDETWTVGSDAPNGINLFLVAAHEIGHALGLGHSSDPDAIMYPYYSPYVKPVFRLDQDDIKG 152

                  ....*.
gi 148233994  290 IQKIYG 295
Cdd:pfam00413 153 IQQLYG 158
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
129-296 5.71e-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: 126.31  E-value: 5.71e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148233994   129 QKWHHKHITYSIKnvTPKVGDlETRKAIRRAFDVWQNVTPLTFEEVPYcelengkrDVDITIIFASGFHGdsspfdgegG 208
Cdd:smart00235   3 KKWPKGTVPYVID--SSSLSP-EEREAIAKALAEWSDVTCIRFVERTG--------TADIYISFGSGDSG---------C 62
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148233994   209 FLAHAYFPGpgigGDTHFDsDEPWTLGnpnhdgndlFLVAVHELGHALGLEHSNDPTA---IMAPFYQYMETDNFKLPTD 285
Cdd:smart00235  63 TLSHAGRPG----GDQHLS-LGNGCIN---------TGVAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFDLSED 128
                          170
                   ....*....|.
gi 148233994   286 DLQGIQKIYGP 296
Cdd:smart00235 129 DSLGIPYDYGS 139
PHA03247 PHA03247
large tegument protein UL36; Provisional
277-357 5.18e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 45.31  E-value: 5.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148233994  277 TDNFKLPTDDLQgiqkiygPPEKAPAPTKPLPTVPPHRSVPPVDPRKNDRQPKPPRPPTGDKPSYPGAKPNICDGNFNTL 356
Cdd:PHA03247 2895 TESFALPPDQPE-------RPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGAL 2967

                  .
gi 148233994  357 A 357
Cdd:PHA03247 2968 V 2968
PHA03247 PHA03247
large tegument protein UL36; Provisional
202-346 7.10e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.93  E-value: 7.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148233994  202 PFDGEGGFLAHAYfPGPGIGGDTHFDS-------------DEPwtLGNPNHDgndLFLVAVHELgHALGLEHSNDPTAIM 268
Cdd:PHA03247 2483 PAEARFPFAAGAA-PDPGGGGPPDPDAppapsrlapailpDEP--VGEPVHP---RMLTWIRGL-EELASDDAGDPPPPL 2555
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148233994  269 APFYQYMETDNfKLPtddlqgiqkiygPPEKAPAPTKPL-------PTVPPHRSVP--PVDPRKNDRQPKPPRPPTGD-- 337
Cdd:PHA03247 2556 PPAAPPAAPDR-SVP------------PPRPAPRPSEPAvtsrarrPDAPPQSARPraPVDDRGDPRGPAPPSPLPPDth 2622
                         170
                  ....*....|.
gi 148233994  338 --KPSYPGAKP 346
Cdd:PHA03247 2623 apDPPPPSPSP 2633
PHA03247 PHA03247
large tegument protein UL36; Provisional
296-346 3.36e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.62  E-value: 3.36e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 148233994  296 PPEKAPAPTKPLPTVPPHRSVP-PVDPRKNDRQPKPP----RPPTGDKPSYPGAKP 346
Cdd:PHA03247 2866 PPSRSPAAKPAAPARPPVRRLArPAVSRSTESFALPPdqpeRPPQPQAPPPPQPQP 2921
PRK14950 PRK14950
DNA polymerase III subunits gamma and tau; Provisional
301-346 8.25e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 40.95  E-value: 8.25e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 148233994 301 PAPTKPlPTVPPHRSVPPVDPrKNDRQPKPPRPPTGDKPSYPGAKP 346
Cdd:PRK14950 383 PAPSTR-PKAAAAANIPPKEP-VRETATPPPVPPRPVAPPVPHTPE 426
FAP pfam07174
Fibronectin-attachment protein (FAP); This family contains bacterial fibronectin-attachment ...
296-347 9.80e-04

Fibronectin-attachment protein (FAP); This family contains bacterial fibronectin-attachment proteins (FAP). Family members are rich in alanine and proline, are approximately 300 long, and seem to be restricted to mycobacteria. These proteins contain a fibronectin-binding motif that allows mycobacteria to bind to fibronectin in the extracellular matrix.


Pssm-ID: 254090 [Multi-domain]  Cd Length: 297  Bit Score: 40.26  E-value: 9.80e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 148233994  296 PPEKAPAPTKPLPTVPPHRSVPPVDPRKNDRQPKPPRPP-TGDKPSYPGAKPN 347
Cdd:pfam07174  47 PPSTAAAAPAPAAPPPPPPPAAPPAPQPDDPNAAPPPPPaDPNAPPPPPVDPN 99
SOBP pfam15279
Sine oculis-binding protein; SOBP is associated with syndromic and nonsyndromic intellectual ...
296-347 7.54e-03

Sine oculis-binding protein; SOBP is associated with syndromic and nonsyndromic intellectual disability. It carries a zinc-finger of the zf-C2H2 type at the N-terminus, and a highly characteristic C-terminal PhPhPhPhPhPh motif. The deduced 873-amino acid protein contains an N-terminal nuclear localisation signal (NLS), followed by 2 FCS-type zinc finger motifs, a proline-rich region (PR1), a putative RNA-binding motif region, and a C-terminal NLS embedded in a second proline-rich motif. SOBP is expressed in various human tissues, including developing mouse brain at embryonic day 14. In postnatal and adult mouse brain SOBP is expressed in all neurons, with intense staining in the limbic system. Highest expression is in layer V cortical neurons, hippocampus, pyriform cortex, dorsomedial nucleus of thalamus, amygdala, and hypothalamus. Postnatal expression of SOBP in the limbic system corresponds to a time of active synaptogenesis. the family is also referred to as Jackson circler, JXC1. In seven affected siblings from a consanguineous Israeli Arab family with mental retardation, anterior maxillary protrusion, and strabismus mutations were found in this protein.


Pssm-ID: 259412 [Multi-domain]  Cd Length: 237  Bit Score: 37.11  E-value: 7.54e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 148233994  296 PPEKAPAPTKPLPTVPPHRSVPPVD-------PRKNDRQPKPPRPPTGDKPSYPGAKPN 347
Cdd:pfam15279 102 PSSSPPSPSKPLISVAPPSKLLSVNsppsqphLPPKGVPPLNPQRPPGSRPPCPASNPM 160
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.11
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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