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Conserved domains on  [gi|194037087|ref|XP_001926652|]
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PREDICTED: matrix metalloproteinase-16 [Sus scrofa]

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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 ...
126-291 9.99e-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: 258.67  E-value: 9.99e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194037087 126 KWQHKHITYSIKNVTPKVGDPETRKAIRRAFDVWQNVTPLTFEEVPYSElengkrDVDITIIFASGFHGDSSPFDGEGGF 205
Cdd:cd04278    1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGQ------EADIRISFARGNHGDGYPFDGPGGT 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194037087 206 LAHAYFPGpGIGGDTHFDSDEPWTLGNpNHDGNDLFLVAVHELGHALGLEHSNDPTAIMAPFYQYMETdNFKLPNDDLQG 285
Cdd:cd04278   75 LAHAFFPG-GIGGDIHFDDDEQWTLGS-DSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVP-KFKLSQDDIRG 151

                 ....*.
gi 194037087 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 5.17e-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: 242.60  E-value: 5.17e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194037087 340 PNICDG-NFNTLAILRREMFVFKDQWFWRVRNNRvMDGYPMQITYFWRGLPPSIDAVYENSD-GNFVFFKGNKYWVFKDT 417
Cdd:cd00094    1 PDACDPlSFDAVTTLRGELYFFKGRYFWRLSPGK-PPGSPFLISSFWPSLPSPVDAAFERPDtGKIYFFKGDKYWVYTGK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194037087 418 TLQPGYPHDLMTLGSGIPPHGIDSAIWWEDVGKTYFFKGDRYWRYSEEMKTMDPGYPK-PITVWKGIPESPQGAFvHKEN 496
Cdd:cd00094   80 NLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKlIETDFPGVPDKVDAAF-RWLD 158
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 194037087 497 GFTYFYKGKEYWKFNNQILKVEPGYPRSILKDFMGC 532
Cdd:cd00094  159 GYYYFFKGDQYWRFDPRSKEVRVGYPLKISSDWLGC 194
DUF3377 pfam11857
Domain of unknown function (DUF3377); This domain is functionally uncharacterized. This domain ...
534-607 2.61e-42

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: 146.67  E-value: 2.61e-42
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 194037087  534 GPTDRDKEGHSPPDDVDIVIKLDNTASTVKAIAIVIPCILALCLLVLVYTVFQFKRKGTPRHILYCKRSMQEWV 607
Cdd:pfam11857   1 GPSDERRDRGRPEDDVDIVVEVDEVPGTVNAAAVVIPLVLLLCILVLLYTIVQFKRKGTPRHLLYCKRSLQEWV 74
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
43-96 2.66e-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: 2.66e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 194037087   43 VEVWLQKYGYLPPT-DprmsvLRSAETMQSALAAMQQFYGINMTGKVDRNTIDWM 96
Cdd:pfam01471   8 LQRYLKRLGYYPGPvD-----GVFGPSTEAAVKAFQRFFGLPVTGIVDPETLAAL 57
Gag_MA super family cl03116
Matrix protein (MA), p15; The matrix protein, p15, is encoded by the gag gene. MA is involved ...
287-335 5.45e-03

Matrix protein (MA), p15; The matrix protein, p15, is encoded by the gag gene. MA is involved in pathogenicity.


The actual alignment was detected with superfamily member pfam01140:

Pssm-ID: 250394  Cd Length: 129  Bit Score: 35.95  E-value: 5.45e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 194037087  287 QKIYGPPDKIP-----------PPTRPLPTVPPHRSIPPVDPRKNDRPKPPRPPTGRPSY 335
Cdd:pfam01140  70 PGPHGHPDQVPyivtwedlafePPPWVKPFVDPPKVLLPSSTPKPVSPSPSAPPRPSSLY 129
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
126-291 5.20e-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: 259.49  E-value: 5.20e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194037087  126 KWQHKHITYSIKNVTPKVGDPETRKAIRRAFDVWQNVTPLTFEEVPyselengKRDVDITIIFASGFHGDSSPFDGEGGF 205
Cdd:pfam00413   1 KWPKKNLTYRIVNYTPDLPRAEVRKAIRRAFKVWSEVTPLTFTEVT-------EGTADIMIGFGRGDHGDGYPFDGPGGV 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194037087  206 LAHAYFPGPgIGGDTHFDSDEPWTLGNPNHDGNDLFLVAVHELGHALGLEHSNDPTAIMAPFYQYMETDNFKLPNDDLQG 285
Cdd:pfam00413  74 LAHAFPPGP-IGGDIHFDDDETWTVGSDAPNGINLFLVAAHEIGHALGLGHSSDPDAIMYPYYSPYVKPVFRLDQDDIKG 152

                  ....*.
gi 194037087  286 IQKIYG 291
Cdd:pfam00413 153 IQQLYG 158
 
Name Accession Description Interval E-value
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
126-291 9.99e-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: 258.67  E-value: 9.99e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194037087 126 KWQHKHITYSIKNVTPKVGDPETRKAIRRAFDVWQNVTPLTFEEVPYSElengkrDVDITIIFASGFHGDSSPFDGEGGF 205
Cdd:cd04278    1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGQ------EADIRISFARGNHGDGYPFDGPGGT 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194037087 206 LAHAYFPGpGIGGDTHFDSDEPWTLGNpNHDGNDLFLVAVHELGHALGLEHSNDPTAIMAPFYQYMETdNFKLPNDDLQG 285
Cdd:cd04278   75 LAHAFFPG-GIGGDIHFDDDEQWTLGS-DSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVP-KFKLSQDDIRG 151

                 ....*.
gi 194037087 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 5.17e-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: 242.60  E-value: 5.17e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194037087 340 PNICDG-NFNTLAILRREMFVFKDQWFWRVRNNRvMDGYPMQITYFWRGLPPSIDAVYENSD-GNFVFFKGNKYWVFKDT 417
Cdd:cd00094    1 PDACDPlSFDAVTTLRGELYFFKGRYFWRLSPGK-PPGSPFLISSFWPSLPSPVDAAFERPDtGKIYFFKGDKYWVYTGK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194037087 418 TLQPGYPHDLMTLGSGIPPHGIDSAIWWEDVGKTYFFKGDRYWRYSEEMKTMDPGYPK-PITVWKGIPESPQGAFvHKEN 496
Cdd:cd00094   80 NLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKlIETDFPGVPDKVDAAF-RWLD 158
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 194037087 497 GFTYFYKGKEYWKFNNQILKVEPGYPRSILKDFMGC 532
Cdd:cd00094  159 GYYYFFKGDQYWRFDPRSKEVRVGYPLKISSDWLGC 194
DUF3377 pfam11857
Domain of unknown function (DUF3377); This domain is functionally uncharacterized. This domain ...
534-607 2.61e-42

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: 146.67  E-value: 2.61e-42
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 194037087  534 GPTDRDKEGHSPPDDVDIVIKLDNTASTVKAIAIVIPCILALCLLVLVYTVFQFKRKGTPRHILYCKRSMQEWV 607
Cdd:pfam11857   1 GPSDERRDRGRPEDDVDIVVEVDEVPGTVNAAAVVIPLVLLLCILVLLYTIVQFKRKGTPRHLLYCKRSLQEWV 74
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
439-484 1.59e-11

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: 60.33  E-value: 1.59e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 194037087   439 IDSAIWWEDvGKTYFFKGDRYWRYSEemKTMDPGYPKPIT-VWKGIP 484
Cdd:smart00120   1 IDAAFELRD-GKTYFFKGDKYWRFDP--KRVDPGYPKLISsFFPGLP 44
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
439-484 8.68e-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: 57.98  E-value: 8.68e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 194037087  439 IDSAIWWEDvGKTYFFKGDRYWRYSEEmkTMDPGYPKPITV-WKGIP 484
Cdd:pfam00045   1 IDAAFEDRD-GKTYFFKGRKYWRFDPQ--RVEPGYPKLISDfWPGLP 44
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
43-96 2.66e-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: 2.66e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 194037087   43 VEVWLQKYGYLPPT-DprmsvLRSAETMQSALAAMQQFYGINMTGKVDRNTIDWM 96
Cdd:pfam01471   8 LQRYLKRLGYYPGPvD-----GVFGPSTEAAVKAFQRFFGLPVTGIVDPETLAAL 57
PRK13267 PRK13267
archaemetzincin-like protein; Reviewed
244-264 1.76e-03

archaemetzincin-like protein; Reviewed


Pssm-ID: 237325  Cd Length: 179  Bit Score: 38.46  E-value: 1.76e-03
                         10        20
                 ....*....|....*....|.
gi 194037087 244 AVHELGHALGLEHSNDPTAIM 264
Cdd:PRK13267 129 VTHELGHTLGLEHCDNPRCVM 149
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
234-274 1.95e-03

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


Pssm-ID: 224825  Cd Length: 181  Bit Score: 38.51  E-value: 1.95e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 194037087 234 NHDGNDLFLV-----AVHELGHALGLEHSNDPTAIMAPFYQYMETD 274
Cdd:COG1913  113 YTPDRELFKErvvkeVLHELGHLLGLSHCPNPRCVMNFSNSLRDVD 158
Gag_MA pfam01140
Matrix protein (MA), p15; The matrix protein, p15, is encoded by the gag gene. MA is involved ...
287-335 5.45e-03

Matrix protein (MA), p15; The matrix protein, p15, is encoded by the gag gene. MA is involved in pathogenicity.


Pssm-ID: 250394  Cd Length: 129  Bit Score: 35.95  E-value: 5.45e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 194037087  287 QKIYGPPDKIP-----------PPTRPLPTVPPHRSIPPVDPRKNDRPKPPRPPTGRPSY 335
Cdd:pfam01140  70 PGPHGHPDQVPyivtwedlafePPPWVKPFVDPPKVLLPSSTPKPVSPSPSAPPRPSSLY 129
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
126-291 5.20e-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: 259.49  E-value: 5.20e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194037087  126 KWQHKHITYSIKNVTPKVGDPETRKAIRRAFDVWQNVTPLTFEEVPyselengKRDVDITIIFASGFHGDSSPFDGEGGF 205
Cdd:pfam00413   1 KWPKKNLTYRIVNYTPDLPRAEVRKAIRRAFKVWSEVTPLTFTEVT-------EGTADIMIGFGRGDHGDGYPFDGPGGV 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194037087  206 LAHAYFPGPgIGGDTHFDSDEPWTLGNPNHDGNDLFLVAVHELGHALGLEHSNDPTAIMAPFYQYMETDNFKLPNDDLQG 285
Cdd:pfam00413  74 LAHAFPPGP-IGGDIHFDDDETWTVGSDAPNGINLFLVAAHEIGHALGLGHSSDPDAIMYPYYSPYVKPVFRLDQDDIKG 152

                  ....*.
gi 194037087  286 IQKIYG 291
Cdd:pfam00413 153 IQQLYG 158
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
125-292 3.09e-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: 3.09e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194037087   125 QKWQHKHITYSIKnvTPKVgDPETRKAIRRAFDVWQNVTPLTFEEVPYSElengkrdvDITIIFASGFHgdsspfdgeGG 204
Cdd:smart00235   3 KKWPKGTVPYVID--SSSL-SPEEREAIAKALAEWSDVTCIRFVERTGTA--------DIYISFGSGDS---------GC 62
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194037087   205 FLAHAYFPgpgiGGDTHFDsDEPWTLGnpnhdgndlFLVAVHELGHALGLEHSNDPTA---IMAPFYQYMETDNFKLPND 281
Cdd:smart00235  63 TLSHAGRP----GGDQHLS-LGNGCIN---------TGVAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFDLSED 128
                          170
                   ....*....|.
gi 194037087   282 DLQGIQKIYGP 292
Cdd:smart00235 129 DSLGIPYDYGS 139
LELP1 pfam15042
Late cornified envelope-like proline-rich protein 1; This family of uncharacterized proteins ...
292-340 2.05e-04

Late cornified envelope-like proline-rich protein 1; This family of uncharacterized proteins is found in mammals.


Pssm-ID: 259179 [Multi-domain]  Cd Length: 111  Bit Score: 40.10  E-value: 2.05e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 194037087  292 PPDKIPPPTR--PLPTVPPHRSIPPVDPRKNDRPKPPRPPTGRPSYPGAKP 340
Cdd:pfam15042  48 SLDKCPPPPKcpPCPPCPPSTPTSPLCPPLCSPPCPGPCPPSCPPKPCVKP 98
PHA03247 PHA03247
large tegument protein UL36; Provisional
292-338 3.61e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.23  E-value: 3.61e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 194037087  292 PPDKIPPPTRPLPTVPPhrsIPPVDPRKNDRPKPPRPPTGRPSYPGA 338
Cdd:PHA03247 2901 PPDQPERPPQPQAPPPP---QPQPQPPPPPQPQPPPPPPPRPQPPLA 2944
 
Name Accession Description Interval E-value
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
126-291 9.99e-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: 258.67  E-value: 9.99e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194037087 126 KWQHKHITYSIKNVTPKVGDPETRKAIRRAFDVWQNVTPLTFEEVPYSElengkrDVDITIIFASGFHGDSSPFDGEGGF 205
Cdd:cd04278    1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGQ------EADIRISFARGNHGDGYPFDGPGGT 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194037087 206 LAHAYFPGpGIGGDTHFDSDEPWTLGNpNHDGNDLFLVAVHELGHALGLEHSNDPTAIMAPFYQYMETdNFKLPNDDLQG 285
Cdd:cd04278   75 LAHAFFPG-GIGGDIHFDDDEQWTLGS-DSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPVP-KFKLSQDDIRG 151

                 ....*.
gi 194037087 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 5.17e-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: 242.60  E-value: 5.17e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194037087 340 PNICDG-NFNTLAILRREMFVFKDQWFWRVRNNRvMDGYPMQITYFWRGLPPSIDAVYENSD-GNFVFFKGNKYWVFKDT 417
Cdd:cd00094    1 PDACDPlSFDAVTTLRGELYFFKGRYFWRLSPGK-PPGSPFLISSFWPSLPSPVDAAFERPDtGKIYFFKGDKYWVYTGK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194037087 418 TLQPGYPHDLMTLGSGIPPHGIDSAIWWEDVGKTYFFKGDRYWRYSEEMKTMDPGYPK-PITVWKGIPESPQGAFvHKEN 496
Cdd:cd00094   80 NLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKlIETDFPGVPDKVDAAF-RWLD 158
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 194037087 497 GFTYFYKGKEYWKFNNQILKVEPGYPRSILKDFMGC 532
Cdd:cd00094  159 GYYYFFKGDQYWRFDPRSKEVRVGYPLKISSDWLGC 194
DUF3377 pfam11857
Domain of unknown function (DUF3377); This domain is functionally uncharacterized. This domain ...
534-607 2.61e-42

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: 146.67  E-value: 2.61e-42
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 194037087  534 GPTDRDKEGHSPPDDVDIVIKLDNTASTVKAIAIVIPCILALCLLVLVYTVFQFKRKGTPRHILYCKRSMQEWV 607
Cdd:pfam11857   1 GPSDERRDRGRPEDDVDIVVEVDEVPGTVNAAAVVIPLVLLLCILVLLYTIVQFKRKGTPRHLLYCKRSLQEWV 74
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
132-291 6.83e-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: 6.83e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194037087 132 ITYSIKNVTPKVGDPETR--KAIRRAFDVWQNVTPLTFEEVPyseleNGKRDVDITIifasgFHGDSSPFDGEGGFLAHA 209
Cdd:cd04279    4 IRVYIDPTPAPPDSRAQSwlQAVKQAAAEWENVGPLKFVYNP-----EEDNDADIVI-----FFDRPPPVGGAGGGLARA 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194037087 210 YFPGPGIGGDTHFDSDEPWTLGNPNHDGNDLFLVAVHELGHALGLEHSND-PTAIMAPFYQYMETDNFKLPNDDLQGIQK 288
Cdd:cd04279   74 GFPLISDGNRKLFNRTDINLGPGQPRGAENLQAIALHELGHALGLWHHSDrPEDAMYPSQGQGPDGNPTLSARDVATLKR 153

                 ...
gi 194037087 289 IYG 291
Cdd:cd04279  154 LYG 156
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
146-291 1.46e-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: 80.92  E-value: 1.46e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194037087 146 PETRKAIRRAFDVWQNVTPLTFEEVPYSElengkrDVDITIIFASGFHGDSspfdgeggfLAHAYFPGPGI----GGDTH 221
Cdd:cd04277   33 AAQQAAARDALEAWEDVADIDFVEVSDNS------GADIRFGNSSDPDGNT---------AGYAYYPGSGSgtayGGDIW 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194037087 222 FDSDEpwtLGNPNHDGNDLFLVAVHELGHALGLEHSND-----PTAIMAPFYQYMET-----DNFKLPND---------- 281
Cdd:cd04277   98 FNSSY---DTNSDSPGSYGYQTIIHEIGHALGLEHPGDynggdPVPPTYALDSREYTvmsynSGYGNGASagggypqtpm 174
                        170
                 ....*....|..
gi 194037087 282 --DLQGIQKIYG 291
Cdd:cd04277  175 llDIAALQYLYG 186
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
439-484 1.59e-11

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: 60.33  E-value: 1.59e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 194037087   439 IDSAIWWEDvGKTYFFKGDRYWRYSEemKTMDPGYPKPIT-VWKGIP 484
Cdd:smart00120   1 IDAAFELRD-GKTYFFKGDKYWRFDP--KRVDPGYPKLISsFFPGLP 44
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
439-484 8.68e-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: 57.98  E-value: 8.68e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 194037087  439 IDSAIWWEDvGKTYFFKGDRYWRYSEEmkTMDPGYPKPITV-WKGIP 484
Cdd:pfam00045   1 IDAAFEDRD-GKTYFFKGRKYWRFDPQ--RVEPGYPKLISDfWPGLP 44
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
149-290 9.05e-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 [Multi-domain]  Cd Length: 167  Bit Score: 60.23  E-value: 9.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194037087 149 RKAIRRAFDVWQNVTPLTFEEVPYselenGKRDVDITIIFASGfhgdsspfDGEGGFLAHAYFPG--PGIGGDTHFDSDE 226
Cdd:cd00203   24 QSLILIAMQIWRDYLNIRFVLVGV-----EIDKADIAILVTRQ--------DFDGGTGGWAYLGRvcDSLRGVGVLQDNQ 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194037087 227 PWTlgnpnhdgNDLFLVAVHELGHALGLEHSNDPTA--------------------IMAPFY-QYMETDNFKLPNDDLQG 285
Cdd:cd00203   91 SGT--------KEGAQTIAHELGHALGFYHDHDRKDrddyptiddtlnaedddyysVMSYTKgSFSDGQRKDFSQCDIDQ 162

                 ....*
gi 194037087 286 IQKIY 290
Cdd:cd00203  163 INKLY 167
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
392-436 5.86e-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: 249537  Cd Length: 45  Bit Score: 55.67  E-value: 5.86e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 194037087  392 IDAVYENSDGNFVFFKGNKYWVFKDTTLQPGYPHDLMTLGSGIPP 436
Cdd:pfam00045   1 IDAAFEDRDGKTYFFKGRKYWRFDPQRVEPGYPKLISDFWPGLPC 45
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
392-436 1.79e-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: 54.17  E-value: 1.79e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 194037087   392 IDAVYENSDGNFVFFKGNKYWVFKDTTLQPGYPHDLMTLGSGIPP 436
Cdd:smart00120   1 IDAAFELRDGKTYFFKGDKYWRFDPKRVDPGYPKLISSFFPGLPC 45
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
132-274 4.33e-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: 55.20  E-value: 4.33e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194037087 132 ITYSIKNVTPKvgdpETRKAIRRAFDVWQNVTPLTFEEVpyseleNGKRDVDITIIFASGFHGDsspfDGEGGFLAHAYF 211
Cdd:cd04268    4 ITYYIDDSVPD----KLRAAILDAIEAWNKAFAIGFKNA------NDVDPADIRYSVIRWIPYN----DGTWSYGPSQVD 69
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 194037087 212 PGPG--IGGDTHFDSDEPWTLGNPNHDgndlflVAVHELGHALGLEHSNDPTAIMAPFYQYMETD 274
Cdd:cd04268   70 PLTGeiLLARVYLYSSFVEYSGARLRN------TAEHELGHALGLRHNFAASDRDDNVDLLAEKG 128
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
354-390 2.09e-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: 51.05  E-value: 2.09e-08
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 194037087  354 RREMFVFKDQWFWRVRNNRVMDGYPMQITYFWRGLPP 390
Cdd:pfam00045   9 DGKTYFFKGRKYWRFDPQRVEPGYPKLISDFWPGLPC 45
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
43-96 2.66e-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: 2.66e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 194037087   43 VEVWLQKYGYLPPT-DprmsvLRSAETMQSALAAMQQFYGINMTGKVDRNTIDWM 96
Cdd:pfam01471   8 LQRYLKRLGYYPGPvD-----GVFGPSTEAAVKAFQRFFGLPVTGIVDPETLAAL 57
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
354-390 4.35e-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: 47.24  E-value: 4.35e-07
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 194037087   354 RREMFVFKDQWFWRVRNNRVMDGYPMQITYFWRGLPP 390
Cdd:smart00120   9 DGKTYFFKGDKYWRFDPKRVDPGYPKLISSFFPGLPC 45
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
490-531 9.06e-07

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: 46.43  E-value: 9.06e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 194037087  490 AFVHKENGFTYFYKGKEYWKFNNQilKVEPGYPRSILKDFMG 531
Cdd:pfam00045   3 AAFEDRDGKTYFFKGRKYWRFDPQ--RVEPGYPKLISDFWPG 42
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
490-531 1.67e-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: 45.70  E-value: 1.67e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 194037087   490 AFVHKENGFTYFYKGKEYWKFNNQilKVEPGYPRSILKDFMG 531
Cdd:smart00120   3 AAFELRDGKTYFFKGDKYWRFDPK--RVDPGYPKLISSFFPG 42
ZnMc_MMP_like_3 cd04327
Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal ...
144-256 1.10e-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: 42.37  E-value: 1.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194037087 144 GDPETRKAIRRAFDVWQNVTPLTFEEVpyselenGKRDVDITIIFASGfHGDSSpFDGEGGFLAHAYFPGPGIGGDTHFD 223
Cdd:cd04327   17 PDAFLKDKVRAAAREWLPYANLKFKFV-------TDADADIRISFTPG-DGYWS-YVGTDALLIGADAPTMNLGWFTDDT 87
                         90       100       110
                 ....*....|....*....|....*....|...
gi 194037087 224 SDepwtlgnpnhdgNDLFLVAVHELGHALGLEH 256
Cdd:cd04327   88 PD------------PEFSRVVLHEFGHALGFIH 108
ZnMc_pappalysin_like cd04275
Zinc-dependent metalloprotease, pappalysin_like subfamily. The pregnancy-associated plasma ...
200-256 1.30e-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: 39.25  E-value: 1.30e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 194037087 200 DGEGGFLAHAYFPGPGIGGDTHFD--SDEPWTLGNPNHDGNDLFLVAVHELGHALGLEH 256
Cdd:cd04275   95 FLGGGLLGYATFPDSLVSLAFITDgvVINPSSLPGGSAAPYNLGDTATHEVGHWLGLYH 153
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
236-266 1.56e-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: 1.56e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 194037087 236 DGNDLFL-----VAVHELGHALGLEHSNDPTAIMAP 266
Cdd:cd11375  114 PDEGLFLerllkEAVHELGHLFGLDHCPYYACVMNF 149
PRK13267 PRK13267
archaemetzincin-like protein; Reviewed
244-264 1.76e-03

archaemetzincin-like protein; Reviewed


Pssm-ID: 237325  Cd Length: 179  Bit Score: 38.46  E-value: 1.76e-03
                         10        20
                 ....*....|....*....|.
gi 194037087 244 AVHELGHALGLEHSNDPTAIM 264
Cdd:PRK13267 129 VTHELGHTLGLEHCDNPRCVM 149
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
234-274 1.95e-03

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


Pssm-ID: 224825  Cd Length: 181  Bit Score: 38.51  E-value: 1.95e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 194037087 234 NHDGNDLFLV-----AVHELGHALGLEHSNDPTAIMAPFYQYMETD 274
Cdd:COG1913  113 YTPDRELFKErvvkeVLHELGHLLGLSHCPNPRCVMNFSNSLRDVD 158
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
235-267 3.55e-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: 3.55e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 194037087 235 HDGNDLFLVAV---HELGHALGLEHSN------DPTAIMAPF 267
Cdd:cd04269  123 DHSRNLLLFAVtmaHELGHNLGMEHDDggctcgRSTCIMAPS 164
Gag_MA pfam01140
Matrix protein (MA), p15; The matrix protein, p15, is encoded by the gag gene. MA is involved ...
287-335 5.45e-03

Matrix protein (MA), p15; The matrix protein, p15, is encoded by the gag gene. MA is involved in pathogenicity.


Pssm-ID: 250394  Cd Length: 129  Bit Score: 35.95  E-value: 5.45e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 194037087  287 QKIYGPPDKIP-----------PPTRPLPTVPPHRSIPPVDPRKNDRPKPPRPPTGRPSY 335
Cdd:pfam01140  70 PGPHGHPDQVPyivtwedlafePPPWVKPFVDPPKVLLPSSTPKPVSPSPSAPPRPSSLY 129
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
126-291 5.20e-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: 259.49  E-value: 5.20e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194037087  126 KWQHKHITYSIKNVTPKVGDPETRKAIRRAFDVWQNVTPLTFEEVPyselengKRDVDITIIFASGFHGDSSPFDGEGGF 205
Cdd:pfam00413   1 KWPKKNLTYRIVNYTPDLPRAEVRKAIRRAFKVWSEVTPLTFTEVT-------EGTADIMIGFGRGDHGDGYPFDGPGGV 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194037087  206 LAHAYFPGPgIGGDTHFDSDEPWTLGNPNHDGNDLFLVAVHELGHALGLEHSNDPTAIMAPFYQYMETDNFKLPNDDLQG 285
Cdd:pfam00413  74 LAHAFPPGP-IGGDIHFDDDETWTVGSDAPNGINLFLVAAHEIGHALGLGHSSDPDAIMYPYYSPYVKPVFRLDQDDIKG 152

                  ....*.
gi 194037087  286 IQKIYG 291
Cdd:pfam00413 153 IQQLYG 158
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
125-292 3.09e-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: 3.09e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194037087   125 QKWQHKHITYSIKnvTPKVgDPETRKAIRRAFDVWQNVTPLTFEEVPYSElengkrdvDITIIFASGFHgdsspfdgeGG 204
Cdd:smart00235   3 KKWPKGTVPYVID--SSSL-SPEEREAIAKALAEWSDVTCIRFVERTGTA--------DIYISFGSGDS---------GC 62
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194037087   205 FLAHAYFPgpgiGGDTHFDsDEPWTLGnpnhdgndlFLVAVHELGHALGLEHSNDPTA---IMAPFYQYMETDNFKLPND 281
Cdd:smart00235  63 TLSHAGRP----GGDQHLS-LGNGCIN---------TGVAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFDLSED 128
                          170
                   ....*....|.
gi 194037087   282 DLQGIQKIYGP 292
Cdd:smart00235 129 DSLGIPYDYGS 139
LELP1 pfam15042
Late cornified envelope-like proline-rich protein 1; This family of uncharacterized proteins ...
292-340 2.05e-04

Late cornified envelope-like proline-rich protein 1; This family of uncharacterized proteins is found in mammals.


Pssm-ID: 259179 [Multi-domain]  Cd Length: 111  Bit Score: 40.10  E-value: 2.05e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 194037087  292 PPDKIPPPTR--PLPTVPPHRSIPPVDPRKNDRPKPPRPPTGRPSYPGAKP 340
Cdd:pfam15042  48 SLDKCPPPPKcpPCPPCPPSTPTSPLCPPLCSPPCPGPCPPSCPPKPCVKP 98
PHA03247 PHA03247
large tegument protein UL36; Provisional
292-338 3.61e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.23  E-value: 3.61e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 194037087  292 PPDKIPPPTRPLPTVPPhrsIPPVDPRKNDRPKPPRPPTGRPSYPGA 338
Cdd:PHA03247 2901 PPDQPERPPQPQAPPPP---QPQPQPPPPPQPQPPPPPPPRPQPPLA 2944
PHA03247 PHA03247
large tegument protein UL36; Provisional
273-345 9.34e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.08  E-value: 9.34e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 194037087  273 TDNFKLPNDDLQgiqkiygPPDKIPPPTRPLPT-VPPHRSIPPVDPRKNDRPKPPRPPT----GRPSYPGAKPNICDG 345
Cdd:PHA03247 2895 TESFALPPDQPE-------RPPQPQAPPPPQPQpQPPPPPQPQPPPPPPPRPQPPLAPTtdpaGAGEPSGAVPQPWLG 2965
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.14
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • 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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