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Conserved domains on  [gi|12585280|sp|Q9Y5R2|]
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RecName: Full=Matrix metalloproteinase-24; Short=MMP-24; AltName: Full=Membrane-type matrix metalloproteinase 5; Short=MT-MMP 5; Short=MTMMP5; AltName: Full=Membrane-type-5 matrix metalloproteinase; Short=MT5-MMP; Short=MT5MMP; Contains: RecName: Full=Processed matrix metalloproteinase-24; Flags: Precursor

Protein Classification

M10A family metallopeptidase( domain architecture ID 12021161)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 162-327 2.12e-94

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


:

Pssm-ID: 425668 [Multi-domain]  Cd Length: 159  Bit Score: 287.59  E-value: 2.12e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12585280   162 KWRQKHITYSIHNYTPKVGELDTRKAIRQAFDVWQKVTPLTFEEVPYheiksdrKEADIMIFFASGFHGDSSPFDGEGGF 241
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVST-------GEADIMIGFGRGDHGDGYPFDGPGGV 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12585280   242 LAHAYFPGPGIGGDTHFDSDEPWTLGNANHDGNDLFLVAVHELGHALGLEHSSDPSAIMAPFYQYMETHNFKLPQDDLQG 321
Cdd:pfam00413  74 LAHAFFPGPGLGGDIHFDDDETWTVGSDPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKG 153


                  ....*.
gi 12585280   322 IQKIYG 327
Cdd:pfam00413 154 IQQLYG 159
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 377-569 4.40e-72

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: 231.05  E-value: 4.40e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12585280 377 PNICDG-NFNTVALFRGEMFVFKDRWFWRLRNNRvQEGYPMQIEQFWKGLPARIDAAYERAD-GRFVFFKGDKYWVFKEV 454
Cdd:cd00094   1 PDACDPlSFDAVTTLRGELYFFKGRYFWRLSPGK-PPGSPFLISSFWPSLPSPVDAAFERPDtGKIYFFKGDKYWVYTGK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12585280 455 TVEPGYPHSLGELGSCLPREGIDTALRWEPVGKTYFFKGERYWRYSEERRATDPGYPK-PITVWKGIPQAPQGAFISKEG 533
Cdd:cd00094  80 NLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKlIETDFPGVPDKVDAAFRWLDG 159

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 12585280 534 YYtYFYKGRDYWKFDNQKLSVEPGYPRNILRDWMGC 569
Cdd:cd00094 160 YY-YFFKGDQYWRFDPRSKEVRVGYPLKISSDWLGC 194
DUF3377 pfam11857
Domain of unknown function (DUF3377); This domain is functionally uncharacterized. This domain ...
 575-645 4.31e-31

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


:

Pssm-ID: 463374  Cd Length: 72  Bit Score: 115.88  E-value: 4.31e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 12585280   575 ERRKERRLPQDDVDIMVTINDV-PGSVNAVAVVIPCILSLCILVLVYTIFQFKNKTGPQPVTYYKRPVQEWV 645
Cdd:pfam11857   1 DREEDRHEEEDEVDIVVVIDDVaSGTVNAIAVVVPLVLLLCILVLIYAIVQFQRKGTPRRLLYCKRSLQDWV 72
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 82-134 2.16e-08

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


:

Pssm-ID: 460223 [Multi-domain]  Cd Length: 57  Bit Score: 50.59  E-value: 2.16e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 12585280    82 QNWLKSYGYllpYDSRASAlHSAKALQSAVSTMQQFYGIPVTGVLDQTTIEWM 134
Cdd:pfam01471   9 QRYLNRLGY---YPGPVDG-YFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 162-327 2.12e-94

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


Pssm-ID: 425668 [Multi-domain]  Cd Length: 159  Bit Score: 287.59  E-value: 2.12e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12585280   162 KWRQKHITYSIHNYTPKVGELDTRKAIRQAFDVWQKVTPLTFEEVPYheiksdrKEADIMIFFASGFHGDSSPFDGEGGF 241
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVST-------GEADIMIGFGRGDHGDGYPFDGPGGV 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12585280   242 LAHAYFPGPGIGGDTHFDSDEPWTLGNANHDGNDLFLVAVHELGHALGLEHSSDPSAIMAPFYQYMETHNFKLPQDDLQG 321
Cdd:pfam00413  74 LAHAFFPGPGLGGDIHFDDDETWTVGSDPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKG 153


                  ....*.
gi 12585280   322 IQKIYG 327
Cdd:pfam00413 154 IQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 162-327 3.43e-88

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: 271.38  E-value: 3.43e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12585280 162 KWRQKHITYSIHNYTPKVGELDTRKAIRQAFDVWQKVTPLTFEEVPYHEiksdrkEADIMIFFASGFHGDSSPFDGEGGF 241
Cdd:cd04278   1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGQ------EADIRISFARGNHGDGYPFDGPGGT 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12585280 242 LAHAYFPGpGIGGDTHFDSDEPWTLGNaNHDGNDLFLVAVHELGHALGLEHSSDPSAIMAPFYQYMEtHNFKLPQDDLQG 321
Cdd:cd04278  75 LAHAFFPG-GIGGDIHFDDDEQWTLGS-DSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPV-PKFKLSQDDIRG 151


                ....*.
gi 12585280 322 IQKIYG 327
Cdd:cd04278 152 IQALYG 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 377-569 4.40e-72

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: 231.05  E-value: 4.40e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12585280 377 PNICDG-NFNTVALFRGEMFVFKDRWFWRLRNNRvQEGYPMQIEQFWKGLPARIDAAYERAD-GRFVFFKGDKYWVFKEV 454
Cdd:cd00094   1 PDACDPlSFDAVTTLRGELYFFKGRYFWRLSPGK-PPGSPFLISSFWPSLPSPVDAAFERPDtGKIYFFKGDKYWVYTGK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12585280 455 TVEPGYPHSLGELGSCLPREGIDTALRWEPVGKTYFFKGERYWRYSEERRATDPGYPK-PITVWKGIPQAPQGAFISKEG 533
Cdd:cd00094  80 NLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKlIETDFPGVPDKVDAAFRWLDG 159

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 12585280 534 YYtYFYKGRDYWKFDNQKLSVEPGYPRNILRDWMGC 569
Cdd:cd00094 160 YY-YFFKGDQYWRFDPRSKEVRVGYPLKISSDWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 161-328 5.22e-36

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: 132.09  E-value: 5.22e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12585280    161 QKWRQKHITYSIH--NYTPkvgelDTRKAIRQAFDVWQKVTPLTFEEVPYheiksdrkEADIMIFFASGFHGdsspfdge 238
Cdd:smart00235   3 KKWPKGTVPYVIDssSLSP-----EEREAIAKALAEWSDVTCIRFVERTG--------TADIYISFGSGDSG-------- 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12585280    239 gGFLAHAYFPGpgigGDTHFDsDEPWTLGNAnhdgndlflVAVHELGHALGLEHSSDPSA---IMAPFYQYMETHNFKLP 315
Cdd:smart00235  62 -CTLSHAGRPG----GDQHLS-LGNGCINTG---------VAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFDLS 126

                          170
                   ....*....|...
gi 12585280    316 QDDLQGIQKIYGP 328
Cdd:smart00235 127 EDDSLGIPYDYGS 139
DUF3377 pfam11857
Domain of unknown function (DUF3377); This domain is functionally uncharacterized. This domain ...
 575-645 4.31e-31

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


Pssm-ID: 463374  Cd Length: 72  Bit Score: 115.88  E-value: 4.31e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 12585280   575 ERRKERRLPQDDVDIMVTINDV-PGSVNAVAVVIPCILSLCILVLVYTIFQFKNKTGPQPVTYYKRPVQEWV 645
Cdd:pfam11857   1 DREEDRHEEEDEVDIVVVIDDVaSGTVNAIAVVVPLVLLLCILVLIYAIVQFQRKGTPRRLLYCKRSLQDWV 72
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 476-521 1.84e-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: 395000 [Multi-domain]  Cd Length: 44  Bit Score: 59.12  E-value: 1.84e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 12585280   476 IDTALRWEPvGKTYFFKGERYWRYSEERRatDPGYPKPITVWKGIP 521
Cdd:pfam00045   1 IDAAFEDRD-GKTYFFKGRKYWRFDPQRV--EPGYPKLISDFPGLP 43
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 476-521 3.49e-10

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


Pssm-ID: 214524 [Multi-domain]  Cd Length: 45  Bit Score: 55.33  E-value: 3.49e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 12585280    476 IDTALRWePVGKTYFFKGERYWRYSEERRatDPGYPKPIT-VWKGIP 521
Cdd:smart00120   1 IDAAFEL-RDGKTYFFKGDKYWRFDPKRV--DPGYPKLISsFFPGLP 44
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 82-134 2.16e-08

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


Pssm-ID: 460223 [Multi-domain]  Cd Length: 57  Bit Score: 50.59  E-value: 2.16e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 12585280    82 QNWLKSYGYllpYDSRASAlHSAKALQSAVSTMQQFYGIPVTGVLDQTTIEWM 134
Cdd:pfam01471   9 QRYLNRLGY---YPGPVDG-YFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 185-326 3.84e-05

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


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 45.45  E-value: 3.84e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12585280 185 RKAIRQAFDVWQKVtpLTFEEVpyheikSDRKEADIMIFFAS---GFHGDSSP----------FDGEGGFLAHAYfpgpg 251
Cdd:COG5549 103 VAAVLQAIAEWNAY--LPLEVV------ENPENADIIIVRSNpplTASPNPETgarsaettyeFYDTGNILSHRF----- 169

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 12585280 252 iggdthfdsdepwTLG-NANHDGNDLFLVAVHELGHALGLE-HSSDPSAIMapfyqYME-THNFKLPQD-DLQGIQKIY 326
Cdd:COG5549 170 -------------TILlSPNQTGKYLLATARHELGHALGIWgHSPSPTDAM-----YFSqVRNPPPISPrDINTLKRIY 230
archmetzin NF033823
archaemetzincin family Zn-dependent metalloprotease;
272-300 1.38e-04

archaemetzincin family Zn-dependent metalloprotease;


Pssm-ID: 468195  Cd Length: 170  Bit Score: 42.99  E-value: 1.38e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 12585280  272 DGNDLFL-----VAVHELGHALGLEHSSDPSAIM 300
Cdd:NF033823 113 PDEDLFLerlakEAVHELGHLLGLGHCPNPRCVM 146
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 162-327 2.12e-94

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


Pssm-ID: 425668 [Multi-domain]  Cd Length: 159  Bit Score: 287.59  E-value: 2.12e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12585280   162 KWRQKHITYSIHNYTPKVGELDTRKAIRQAFDVWQKVTPLTFEEVPYheiksdrKEADIMIFFASGFHGDSSPFDGEGGF 241
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVST-------GEADIMIGFGRGDHGDGYPFDGPGGV 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12585280   242 LAHAYFPGPGIGGDTHFDSDEPWTLGNANHDGNDLFLVAVHELGHALGLEHSSDPSAIMAPFYQYMETHNFKLPQDDLQG 321
Cdd:pfam00413  74 LAHAFFPGPGLGGDIHFDDDETWTVGSDPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKG 153


                  ....*.
gi 12585280   322 IQKIYG 327
Cdd:pfam00413 154 IQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 162-327 3.43e-88

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: 271.38  E-value: 3.43e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12585280 162 KWRQKHITYSIHNYTPKVGELDTRKAIRQAFDVWQKVTPLTFEEVPYHEiksdrkEADIMIFFASGFHGDSSPFDGEGGF 241
Cdd:cd04278   1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGQ------EADIRISFARGNHGDGYPFDGPGGT 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12585280 242 LAHAYFPGpGIGGDTHFDSDEPWTLGNaNHDGNDLFLVAVHELGHALGLEHSSDPSAIMAPFYQYMEtHNFKLPQDDLQG 321
Cdd:cd04278  75 LAHAFFPG-GIGGDIHFDDDEQWTLGS-DSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPV-PKFKLSQDDIRG 151


                ....*.
gi 12585280 322 IQKIYG 327
Cdd:cd04278 152 IQALYG 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 377-569 4.40e-72

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: 231.05  E-value: 4.40e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12585280 377 PNICDG-NFNTVALFRGEMFVFKDRWFWRLRNNRvQEGYPMQIEQFWKGLPARIDAAYERAD-GRFVFFKGDKYWVFKEV 454
Cdd:cd00094   1 PDACDPlSFDAVTTLRGELYFFKGRYFWRLSPGK-PPGSPFLISSFWPSLPSPVDAAFERPDtGKIYFFKGDKYWVYTGK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12585280 455 TVEPGYPHSLGELGSCLPREGIDTALRWEPVGKTYFFKGERYWRYSEERRATDPGYPK-PITVWKGIPQAPQGAFISKEG 533
Cdd:cd00094  80 NLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKlIETDFPGVPDKVDAAFRWLDG 159

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 12585280 534 YYtYFYKGRDYWKFDNQKLSVEPGYPRNILRDWMGC 569
Cdd:cd00094 160 YY-YFFKGDQYWRFDPRSKEVRVGYPLKISSDWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 161-328 5.22e-36

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: 132.09  E-value: 5.22e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12585280    161 QKWRQKHITYSIH--NYTPkvgelDTRKAIRQAFDVWQKVTPLTFEEVPYheiksdrkEADIMIFFASGFHGdsspfdge 238
Cdd:smart00235   3 KKWPKGTVPYVIDssSLSP-----EEREAIAKALAEWSDVTCIRFVERTG--------TADIYISFGSGDSG-------- 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12585280    239 gGFLAHAYFPGpgigGDTHFDsDEPWTLGNAnhdgndlflVAVHELGHALGLEHSSDPSA---IMAPFYQYMETHNFKLP 315
Cdd:smart00235  62 -CTLSHAGRPG----GDQHLS-LGNGCINTG---------VAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFDLS 126

                          170
                   ....*....|...
gi 12585280    316 QDDLQGIQKIYGP 328
Cdd:smart00235 127 EDDSLGIPYDYGS 139
DUF3377 pfam11857
Domain of unknown function (DUF3377); This domain is functionally uncharacterized. This domain ...
 575-645 4.31e-31

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


Pssm-ID: 463374  Cd Length: 72  Bit Score: 115.88  E-value: 4.31e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 12585280   575 ERRKERRLPQDDVDIMVTINDV-PGSVNAVAVVIPCILSLCILVLVYTIFQFKNKTGPQPVTYYKRPVQEWV 645
Cdd:pfam11857   1 DREEDRHEEEDEVDIVVVIDDVaSGTVNAIAVVVPLVLLLCILVLIYAIVQFQRKGTPRRLLYCKRSLQDWV 72
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 168-327 1.38e-18

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


Pssm-ID: 239804 [Multi-domain]  Cd Length: 186  Bit Score: 84.00  E-value: 1.38e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12585280 168 ITYSIHNYTPKV------GELDT---------RKAIRQAFDVWQKVTPLTFEEVPYHEiksdrkEADIMIFFASGFHGDS 232
Cdd:cd04277   4 LTYSFSNTGGPYsygygrEEDTTntaalsaaqQAAARDALEAWEDVADIDFVEVSDNS------GADIRFGNSSDPDGNT 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12585280 233 spfdgeggfLAHAYFPGPGI----GGDTHFDSDEpwtLGNANHDGNDLFLVAVHELGHALGLEHS-----SDPSAIMAPF 303
Cdd:cd04277  78 ---------AGYAYYPGSGSgtayGGDIWFNSSY---DTNSDSPGSYGYQTIIHEIGHALGLEHPgdyngGDPVPPTYAL 145

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 12585280 304 YQYMET-------------HNFKLPQD----DLQGIQKIYG 327
Cdd:cd04277 146 DSREYTvmsynsgygngasAGGGYPQTpmllDIAALQYLYG 186
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 186-327 2.15e-18

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: 82.50  E-value: 2.15e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12585280 186 KAIRQAFDVWQKVTPLTFEEVPYHEiksdrKEADIMIFFasgfhGDSSPFDGEGGFLAHAYFPGPGIGGDTHFDSDEPWT 265
Cdd:cd04279  24 QAVKQAAAEWENVGPLKFVYNPEED-----NDADIVIFF-----DRPPPVGGAGGGLARAGFPLISDGNRKLFNRTDINL 93

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 12585280 266 LGNANHDGNDLFLVAVHELGHALGLEHSSD-PSAIMAPFYQYMETHNFKLPQDDLQGIQKIYG 327
Cdd:cd04279  94 GPGQPRGAENLQAIALHELGHALGLWHHSDrPEDAMYPSQGQGPDGNPTLSARDVATLKRLYG 156
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 168-326 6.29e-15

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: 72.94  E-value: 6.29e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12585280 168 ITYSIHNYTPKVGELDT----RKAIRQAFDVWQKVTPLTFEEVPYHEIKsdrkeADIMIFFASGfhgdsspfDGEGGFLA 243
Cdd:cd00203   3 IPYVVVADDRDVEEENLsaqiQSLILIAMQIWRDYLNIRFVLVGVEIDK-----ADIAILVTRQ--------DFDGGTGG 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12585280 244 HAYFPG--PGIGGDTHFDSDEPWTlgnanhdgNDLFLVAVHELGHALGLEHSSDPSA--------------------IMA 301
Cdd:cd00203  70 WAYLGRvcDSLRGVGVLQDNQSGT--------KEGAQTIAHELGHALGFYHDHDRKDrddyptiddtlnaedddyysVMS 141

                       170       180
                ....*....|....*....|....*.
gi 12585280 302 PFY-QYMETHNFKLPQDDLQGIQKIY 326
Cdd:cd00203 142 YTKgSFSDGQRKDFSQCDIDQINKLY 167
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 165-326 1.39e-11

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


Pssm-ID: 239796 [Multi-domain]  Cd Length: 165  Bit Score: 63.28  E-value: 1.39e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12585280 165 QKHITYSIHNYTPKvgelDTRKAIRQAFDVWQKVTPLTFEEVPyheiksDRKEADIMIFFASGFHGDsspfDGEGGFLAH 244
Cdd:cd04268   1 KKPITYYIDDSVPD----KLRAAILDAIEAWNKAFAIGFKNAN------DVDPADIRYSVIRWIPYN----DGTWSYGPS 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12585280 245 AYFPGPG--IGGDTHFDSDEPWTLGNANHDgndlflVAVHELGHALGLEHSSDPSAIMAPFYQYMETH-----------N 311
Cdd:cd04268  67 QVDPLTGeiLLARVYLYSSFVEYSGARLRN------TAEHELGHALGLRHNFAASDRDDNVDLLAEKGdtssvmdyapsN 140

                       170       180
                ....*....|....*....|....*
gi 12585280 312 FKLPQ----------DDLQGIQKIY 326
Cdd:cd04268 141 FSIQLgdgqkytigpYDIAAIKKLY 165
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 476-521 1.84e-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: 395000 [Multi-domain]  Cd Length: 44  Bit Score: 59.12  E-value: 1.84e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 12585280   476 IDTALRWEPvGKTYFFKGERYWRYSEERRatDPGYPKPITVWKGIP 521
Cdd:pfam00045   1 IDAAFEDRD-GKTYFFKGRKYWRFDPQRV--EPGYPKLISDFPGLP 43
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 476-521 3.49e-10

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


Pssm-ID: 214524 [Multi-domain]  Cd Length: 45  Bit Score: 55.33  E-value: 3.49e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 12585280    476 IDTALRWePVGKTYFFKGERYWRYSEERRatDPGYPKPIT-VWKGIP 521
Cdd:smart00120   1 IDAAFEL-RDGKTYFFKGDKYWRFDPKRV--DPGYPKLISsFFPGLP 44
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 429-467 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: 395000 [Multi-domain]  Cd Length: 44  Bit Score: 54.88  E-value: 5.86e-10
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 12585280   429 IDAAYERADGRFVFFKGDKYWVFKEVTVEPGYPHSLGEL 467
Cdd:pfam00045   1 IDAAFEDRDGKTYFFKGRKYWRFDPQRVEPGYPKLISDF 39
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 429-473 3.06e-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 [Multi-domain]  Cd Length: 45  Bit Score: 53.02  E-value: 3.06e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 12585280    429 IDAAYERADGRFVFFKGDKYWVFKEVTVEPGYPHSLGELGSCLPR 473
Cdd:smart00120   1 IDAAFELRDGKTYFFKGDKYWRFDPKRVDPGYPKLISSFFPGLPC 45
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 82-134 2.16e-08

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


Pssm-ID: 460223 [Multi-domain]  Cd Length: 57  Bit Score: 50.59  E-value: 2.16e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 12585280    82 QNWLKSYGYllpYDSRASAlHSAKALQSAVSTMQQFYGIPVTGVLDQTTIEWM 134
Cdd:pfam01471   9 QRYLNRLGY---YPGPVDG-YFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 391-426 3.54e-08

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


Pssm-ID: 214524 [Multi-domain]  Cd Length: 45  Bit Score: 49.93  E-value: 3.54e-08
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 12585280    391 RGEMFVFKDRWFWRLRNNRVQEGYPMQIEQFWKGLP 426
Cdd:smart00120   9 DGKTYFFKGDKYWRFDPKRVDPGYPKLISSFFPGLP 44
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 389-426 8.47e-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: 395000 [Multi-domain]  Cd Length: 44  Bit Score: 46.02  E-value: 8.47e-07
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 12585280   389 LFRGEMFVFKDRWFWRLRNNRVQEGYPMQIEQFWkGLP 426
Cdd:pfam00045   7 DRDGKTYFFKGRKYWRFDPQRVEPGYPKLISDFP-GLP 43
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 525-569 1.32e-06

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


Pssm-ID: 395000 [Multi-domain]  Cd Length: 44  Bit Score: 45.25  E-value: 1.32e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 12585280   525 QGAFISKEGYyTYFYKGRDYWKFDNQKlsVEPGYPRNILRD-WMGC 569
Cdd:pfam00045   2 DAAFEDRDGK-TYFFKGRKYWRFDPQR--VEPGYPKLISDFpGLPC 44
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 526-568 2.01e-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 [Multi-domain]  Cd Length: 45  Bit Score: 44.93  E-value: 2.01e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 12585280    526 GAFISKEGYyTYFYKGRDYWKFDNQKlsVEPGYPRNILRDWMG 568
Cdd:smart00120   3 AAFELRDGK-TYFFKGDKYWRFDPKR--VDPGYPKLISSFFPG 42
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 185-326 3.84e-05

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


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 45.45  E-value: 3.84e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12585280 185 RKAIRQAFDVWQKVtpLTFEEVpyheikSDRKEADIMIFFAS---GFHGDSSP----------FDGEGGFLAHAYfpgpg 251
Cdd:COG5549 103 VAAVLQAIAEWNAY--LPLEVV------ENPENADIIIVRSNpplTASPNPETgarsaettyeFYDTGNILSHRF----- 169

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 12585280 252 iggdthfdsdepwTLG-NANHDGNDLFLVAVHELGHALGLE-HSSDPSAIMapfyqYME-THNFKLPQD-DLQGIQKIY 326
Cdd:COG5549 170 -------------TILlSPNQTGKYLLATARHELGHALGIWgHSPSPTDAM-----YFSqVRNPPPISPrDINTLKRIY 230
archmetzin NF033823
archaemetzincin family Zn-dependent metalloprotease;
272-300 1.38e-04

archaemetzincin family Zn-dependent metalloprotease;


Pssm-ID: 468195  Cd Length: 170  Bit Score: 42.99  E-value: 1.38e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 12585280  272 DGNDLFL-----VAVHELGHALGLEHSSDPSAIM 300
Cdd:NF033823 113 PDEDLFLerlakEAVHELGHLLGLGHCPNPRCVM 146
ZnMc_MMP_like_3 cd04327
Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal ...
 180-292 2.25e-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 [Multi-domain]  Cd Length: 198  Bit Score: 42.75  E-value: 2.25e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12585280 180 GELDTRKAIRQAFDVWQKVTPLTFEEVpyheiksDRKEADIMIFFASGfHGDSSpFDGEGGFLAHAYFPGPGIGGDTHFD 259
Cdd:cd04327  17 PDAFLKDKVRAAAREWLPYANLKFKFV-------TDADADIRISFTPG-DGYWS-YVGTDALLIGADAPTMNLGWFTDDT 87

                        90       100       110
                ....*....|....*....|....*....|...
gi 12585280 260 SDepwtlgnanhdgNDLFLVAVHELGHALGLEH 292
Cdd:cd04327  88 PD------------PEFSRVVLHEFGHALGFIH 108
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
275-302 4.28e-04

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 41.48  E-value: 4.28e-04
                        10        20        30
                ....*....|....*....|....*....|...
gi 12585280 275 DLFL-----VAVHELGHALGLEHSSDPSAIMAP 302
Cdd:COG1913 117 ELFLervlkEAVHELGHLFGLGHCPNPRCVMHF 149
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
 272-302 1.54e-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: 39.97  E-value: 1.54e-03
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 12585280 272 DGNDLFL-----VAVHELGHALGLEHSSDPSAIMAP 302
Cdd:cd11375 114 PDEGLFLerllkEAVHELGHLFGLDHCPYYACVMNF 149
ZnMc_pappalysin_like cd04275
Zinc-dependent metalloprotease, pappalysin_like subfamily. The pregnancy-associated plasma ...
 236-292 7.08e-03

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


Pssm-ID: 239802 [Multi-domain]  Cd Length: 225  Bit Score: 38.47  E-value: 7.08e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 12585280 236 DGEGGFLAHAYFPGPGIGGDTHFD--SDEPWTLGNANHDGNDLFLVAVHELGHALGLEH 292
Cdd:cd04275  95 FLGGGLLGYATFPDSLVSLAFITDgvVINPSSLPGGSAAPYNLGDTATHEVGHWLGLYH 153
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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