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Conserved domains on  [gi|1622840266|ref|XP_001100890|]
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matrix metalloproteinase-24 isoform X4 [Macaca mulatta]

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 ...
 131-296 9.65e-95

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: 9.65e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840266 131 KWRQKHITYSIHNYTPKVGELDTRKAIRQAFDVWQKVTPLTFEEVPYheiksdrKEADIMIFFASGFHGDSSPFDGEGGF 210
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVST-------GEADIMIGFGRGDHGDGYPFDGPGGV 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840266 211 LAHAYFPGPGIGGDTHFDSDEPWTLGNANHDGNDLFLVAVHELGHALGLEHSNDPSAIMAPFYQYMETHNFKLPQDDLQG 290
Cdd:pfam00413  74 LAHAFFPGPGLGGDIHFDDDETWTVGSDPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKG 153


                  ....*.
gi 1622840266 291 IQKIYG 296
Cdd:pfam00413 154 IQQLYG 159
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 346-538 4.42e-73

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: 232.59  E-value: 4.42e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840266 346 PNICDG-NFNTVALFRGEMFVFKDRWFWRLRNNRvQEGYPMQIEQFWKGLPARIDAAYERAD-GRFVFFKGDKYWVFKEV 423
Cdd:cd00094     1 PDACDPlSFDAVTTLRGELYFFKGRYFWRLSPGK-PPGSPFLISSFWPSLPSPVDAAFERPDtGKIYFFKGDKYWVYTGK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840266 424 TVEPGYPHSLGELGSCLPREGIDTALRWEPVGKTYFFKGERYWRYSEERRATDPGYPK-PITVWKGIPQAPQGAFISKEG 502
Cdd:cd00094    80 NLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKlIETDFPGVPDKVDAAFRWLDG 159

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1622840266 503 YYtYFYKGRDYWKFDNQKLSVEPGYPRNILRDWMGC 538
Cdd:cd00094   160 YY-YFFKGDQYWRFDPRSKEVRVGYPLKISSDWLGC 194
DUF3377 pfam11857
Domain of unknown function (DUF3377); This domain is functionally uncharacterized. This domain ...
 544-614 3.84e-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: 3.84e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622840266 544 ERRKERRLPQDDVDIMVTINDV-PGSVNAVAVVIPCILSLCILVLVYTIFQFKNKTGPQPVTYYKRPVQEWV 614
Cdd:pfam11857   1 DREEDRHEEEDEVDIVVVIDDVaSGTVNAIAVVVPLVLLLCILVLIYAIVQFQRKGTPRRLLYCKRSLQDWV 72
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 51-103 1.45e-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: 51.36  E-value: 1.45e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1622840266  51 KNWLKSYGYllpYDSRASAlHSGKALQSAVSTMQQFYGIPVTGVLDQTTIEWM 103
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 ...
 131-296 9.65e-95

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: 9.65e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840266 131 KWRQKHITYSIHNYTPKVGELDTRKAIRQAFDVWQKVTPLTFEEVPYheiksdrKEADIMIFFASGFHGDSSPFDGEGGF 210
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVST-------GEADIMIGFGRGDHGDGYPFDGPGGV 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840266 211 LAHAYFPGPGIGGDTHFDSDEPWTLGNANHDGNDLFLVAVHELGHALGLEHSNDPSAIMAPFYQYMETHNFKLPQDDLQG 290
Cdd:pfam00413  74 LAHAFFPGPGLGGDIHFDDDETWTVGSDPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKG 153


                  ....*.
gi 1622840266 291 IQKIYG 296
Cdd:pfam00413 154 IQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 131-296 1.32e-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: 271.77  E-value: 1.32e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840266 131 KWRQKHITYSIHNYTPKVGELDTRKAIRQAFDVWQKVTPLTFEEVPYHEiksdrkEADIMIFFASGFHGDSSPFDGEGGF 210
Cdd:cd04278     1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGQ------EADIRISFARGNHGDGYPFDGPGGT 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840266 211 LAHAYFPGpGIGGDTHFDSDEPWTLGNaNHDGNDLFLVAVHELGHALGLEHSNDPSAIMAPFYQYMEtHNFKLPQDDLQG 290
Cdd:cd04278    75 LAHAFFPG-GIGGDIHFDDDEQWTLGS-DSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPV-PKFKLSQDDIRG 151


                  ....*.
gi 1622840266 291 IQKIYG 296
Cdd:cd04278   152 IQALYG 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 346-538 4.42e-73

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: 232.59  E-value: 4.42e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840266 346 PNICDG-NFNTVALFRGEMFVFKDRWFWRLRNNRvQEGYPMQIEQFWKGLPARIDAAYERAD-GRFVFFKGDKYWVFKEV 423
Cdd:cd00094     1 PDACDPlSFDAVTTLRGELYFFKGRYFWRLSPGK-PPGSPFLISSFWPSLPSPVDAAFERPDtGKIYFFKGDKYWVYTGK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840266 424 TVEPGYPHSLGELGSCLPREGIDTALRWEPVGKTYFFKGERYWRYSEERRATDPGYPK-PITVWKGIPQAPQGAFISKEG 502
Cdd:cd00094    80 NLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKlIETDFPGVPDKVDAAFRWLDG 159

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1622840266 503 YYtYFYKGRDYWKFDNQKLSVEPGYPRNILRDWMGC 538
Cdd:cd00094   160 YY-YFFKGDQYWRFDPRSKEVRVGYPLKISSDWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 130-297 2.59e-35

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: 129.78  E-value: 2.59e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840266  130 QKWRQKHITYSIH--NYTPkvgelDTRKAIRQAFDVWQKVTPLTFEEVPYheiksdrkEADIMIFFASGFHGdsspfdge 207
Cdd:smart00235   3 KKWPKGTVPYVIDssSLSP-----EEREAIAKALAEWSDVTCIRFVERTG--------TADIYISFGSGDSG-------- 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840266  208 gGFLAHAYFPGpgigGDTHFDsDEPWTLGNAnhdgndlflVAVHELGHALGLEHSNDPSA---IMAPFYQYMETHNFKLP 284
Cdd:smart00235  62 -CTLSHAGRPG----GDQHLS-LGNGCINTG---------VAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFDLS 126

                          170
                   ....*....|...
gi 1622840266  285 QDDLQGIQKIYGP 297
Cdd:smart00235 127 EDDSLGIPYDYGS 139
DUF3377 pfam11857
Domain of unknown function (DUF3377); This domain is functionally uncharacterized. This domain ...
 544-614 3.84e-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: 3.84e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622840266 544 ERRKERRLPQDDVDIMVTINDV-PGSVNAVAVVIPCILSLCILVLVYTIFQFKNKTGPQPVTYYKRPVQEWV 614
Cdd:pfam11857   1 DREEDRHEEEDEVDIVVVIDDVaSGTVNAIAVVVPLVLLLCILVLIYAIVQFQRKGTPRRLLYCKRSLQDWV 72
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 445-490 1.17e-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: 59.50  E-value: 1.17e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1622840266 445 IDTALRWEPvGKTYFFKGERYWRYSEERRatDPGYPKPITVWKGIP 490
Cdd:pfam00045   1 IDAAFEDRD-GKTYFFKGRKYWRFDPQRV--EPGYPKLISDFPGLP 43
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 445-490 2.16e-10

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


Pssm-ID: 214524 [Multi-domain]  Cd Length: 45  Bit Score: 56.10  E-value: 2.16e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1622840266  445 IDTALRWePVGKTYFFKGERYWRYSEERRatDPGYPKPIT-VWKGIP 490
Cdd:smart00120   1 IDAAFEL-RDGKTYFFKGDKYWRFDPKRV--DPGYPKLISsFFPGLP 44
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 51-103 1.45e-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: 51.36  E-value: 1.45e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1622840266  51 KNWLKSYGYllpYDSRASAlHSGKALQSAVSTMQQFYGIPVTGVLDQTTIEWM 103
Cdd:pfam01471   9 QRYLNRLGY---YPGPVDG-YFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 154-295 1.69e-05

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


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 46.60  E-value: 1.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840266 154 RKAIRQAFDVWQKVtpLTFEEVpyheikSDRKEADIMIFFAS---GFHGDSSP----------FDGEGGFLAHAYfpgpg 220
Cdd:COG5549   103 VAAVLQAIAEWNAY--LPLEVV------ENPENADIIIVRSNpplTASPNPETgarsaettyeFYDTGNILSHRF----- 169

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622840266 221 iggdthfdsdepwTLG-NANHDGNDLFLVAVHELGHALGLE-HSNDPSAIMapfyqYME-THNFKLPQD-DLQGIQKIY 295
Cdd:COG5549   170 -------------TILlSPNQTGKYLLATARHELGHALGIWgHSPSPTDAM-----YFSqVRNPPPISPrDINTLKRIY 230
archmetzin NF033823
archaemetzincin family Zn-dependent metalloprotease;
241-269 2.16e-04

archaemetzincin family Zn-dependent metalloprotease;


Pssm-ID: 468195  Cd Length: 170  Bit Score: 42.22  E-value: 2.16e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1622840266 241 DGNDLFL-----VAVHELGHALGLEHSNDPSAIM 269
Cdd:NF033823  113 PDEDLFLerlakEAVHELGHLLGLGHCPNPRCVM 146
PRK13267 PRK13267
archaemetzincin-like protein; Reviewed
 249-269 2.28e-03

archaemetzincin-like protein; Reviewed


Pssm-ID: 237325  Cd Length: 179  Bit Score: 39.24  E-value: 2.28e-03
                          10        20
                  ....*....|....*....|.
gi 1622840266 249 AVHELGHALGLEHSNDPSAIM 269
Cdd:PRK13267  129 VTHELGHTLGLEHCDNPRCVM 149
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 131-296 9.65e-95

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: 9.65e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840266 131 KWRQKHITYSIHNYTPKVGELDTRKAIRQAFDVWQKVTPLTFEEVPYheiksdrKEADIMIFFASGFHGDSSPFDGEGGF 210
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVST-------GEADIMIGFGRGDHGDGYPFDGPGGV 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840266 211 LAHAYFPGPGIGGDTHFDSDEPWTLGNANHDGNDLFLVAVHELGHALGLEHSNDPSAIMAPFYQYMETHNFKLPQDDLQG 290
Cdd:pfam00413  74 LAHAFFPGPGLGGDIHFDDDETWTVGSDPPHGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPLDSKKFRLSQDDIKG 153


                  ....*.
gi 1622840266 291 IQKIYG 296
Cdd:pfam00413 154 IQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 131-296 1.32e-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: 271.77  E-value: 1.32e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840266 131 KWRQKHITYSIHNYTPKVGELDTRKAIRQAFDVWQKVTPLTFEEVPYHEiksdrkEADIMIFFASGFHGDSSPFDGEGGF 210
Cdd:cd04278     1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGQ------EADIRISFARGNHGDGYPFDGPGGT 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840266 211 LAHAYFPGpGIGGDTHFDSDEPWTLGNaNHDGNDLFLVAVHELGHALGLEHSNDPSAIMAPFYQYMEtHNFKLPQDDLQG 290
Cdd:cd04278    75 LAHAFFPG-GIGGDIHFDDDEQWTLGS-DSGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPV-PKFKLSQDDIRG 151


                  ....*.
gi 1622840266 291 IQKIYG 296
Cdd:cd04278   152 IQALYG 157
HX cd00094
Hemopexin-like repeats.; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 346-538 4.42e-73

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: 232.59  E-value: 4.42e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840266 346 PNICDG-NFNTVALFRGEMFVFKDRWFWRLRNNRvQEGYPMQIEQFWKGLPARIDAAYERAD-GRFVFFKGDKYWVFKEV 423
Cdd:cd00094     1 PDACDPlSFDAVTTLRGELYFFKGRYFWRLSPGK-PPGSPFLISSFWPSLPSPVDAAFERPDtGKIYFFKGDKYWVYTGK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840266 424 TVEPGYPHSLGELGSCLPREGIDTALRWEPVGKTYFFKGERYWRYSEERRATDPGYPK-PITVWKGIPQAPQGAFISKEG 502
Cdd:cd00094    80 NLEPGYPKPISDLGFPPTVKQIDAALRWPDNGKTYFFKGDKYWRYDEKTQKMDPGYPKlIETDFPGVPDKVDAAFRWLDG 159

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1622840266 503 YYtYFYKGRDYWKFDNQKLSVEPGYPRNILRDWMGC 538
Cdd:cd00094   160 YY-YFFKGDQYWRFDPRSKEVRVGYPLKISSDWLGC 194
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 130-297 2.59e-35

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: 129.78  E-value: 2.59e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840266  130 QKWRQKHITYSIH--NYTPkvgelDTRKAIRQAFDVWQKVTPLTFEEVPYheiksdrkEADIMIFFASGFHGdsspfdge 207
Cdd:smart00235   3 KKWPKGTVPYVIDssSLSP-----EEREAIAKALAEWSDVTCIRFVERTG--------TADIYISFGSGDSG-------- 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840266  208 gGFLAHAYFPGpgigGDTHFDsDEPWTLGNAnhdgndlflVAVHELGHALGLEHSNDPSA---IMAPFYQYMETHNFKLP 284
Cdd:smart00235  62 -CTLSHAGRPG----GDQHLS-LGNGCINTG---------VAAHELGHALGLYHEQSRSDrdnYMYINYTNIDTRNFDLS 126

                          170
                   ....*....|...
gi 1622840266  285 QDDLQGIQKIYGP 297
Cdd:smart00235 127 EDDSLGIPYDYGS 139
DUF3377 pfam11857
Domain of unknown function (DUF3377); This domain is functionally uncharacterized. This domain ...
 544-614 3.84e-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: 3.84e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622840266 544 ERRKERRLPQDDVDIMVTINDV-PGSVNAVAVVIPCILSLCILVLVYTIFQFKNKTGPQPVTYYKRPVQEWV 614
Cdd:pfam11857   1 DREEDRHEEEDEVDIVVVIDDVaSGTVNAIAVVVPLVLLLCILVLIYAIVQFQRKGTPRRLLYCKRSLQDWV 72
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 137-296 3.90e-19

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: 85.55  E-value: 3.90e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840266 137 ITYSIHNYTPKV------GELDT---------RKAIRQAFDVWQKVTPLTFEEVPYHEiksdrkEADIMIFFASGFHGDS 201
Cdd:cd04277     4 LTYSFSNTGGPYsygygrEEDTTntaalsaaqQAAARDALEAWEDVADIDFVEVSDNS------GADIRFGNSSDPDGNT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840266 202 spfdgeggfLAHAYFPGPGI----GGDTHFDSDEpwtLGNANHDGNDLFLVAVHELGHALGLEHSNDPSA---------- 267
Cdd:cd04277    78 ---------AGYAYYPGSGSgtayGGDIWFNSSY---DTNSDSPGSYGYQTIIHEIGHALGLEHPGDYNGgdpvpptyal 145

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1622840266 268 ------IMAPFYQY--METHNFKLPQ----DDLQGIQKIYG 296
Cdd:cd04277   146 dsreytVMSYNSGYgnGASAGGGYPQtpmlLDIAALQYLYG 186
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 155-296 1.29e-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: 83.27  E-value: 1.29e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840266 155 KAIRQAFDVWQKVTPLTFEEVPYHEiksdrKEADIMIFFasgfhGDSSPFDGEGGFLAHAYFPGPGIGGDTHFDSDEPWT 234
Cdd:cd04279    24 QAVKQAAAEWENVGPLKFVYNPEED-----NDADIVIFF-----DRPPPVGGAGGGLARAGFPLISDGNRKLFNRTDINL 93

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622840266 235 LGNANHDGNDLFLVAVHELGHALGLEHSND-PSAIMAPFYQYMETHNFKLPQDDLQGIQKIYG 296
Cdd:cd04279    94 GPGQPRGAENLQAIALHELGHALGLWHHSDrPEDAMYPSQGQGPDGNPTLSARDVATLKRLYG 156
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 137-295 3.28e-14

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: 70.63  E-value: 3.28e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840266 137 ITYSIHNYTPKVGELDT----RKAIRQAFDVWQKVTPLTFEEVPYHEIKsdrkeADIMIFFASGfhgdsspfDGEGGFLA 212
Cdd:cd00203     3 IPYVVVADDRDVEEENLsaqiQSLILIAMQIWRDYLNIRFVLVGVEIDK-----ADIAILVTRQ--------DFDGGTGG 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840266 213 HAYFPG--PGIGGDTHFDSDEPWTlgnanhdgNDLFLVAVHELGHALGLEHSNDPSA--------------------IMA 270
Cdd:cd00203    70 WAYLGRvcDSLRGVGVLQDNQSGT--------KEGAQTIAHELGHALGFYHDHDRKDrddyptiddtlnaedddyysVMS 141

                         170       180
                  ....*....|....*....|....*.
gi 1622840266 271 PFY-QYMETHNFKLPQDDLQGIQKIY 295
Cdd:cd00203   142 YTKgSFSDGQRKDFSQCDIDQINKLY 167
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 134-295 6.61e-12

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: 64.05  E-value: 6.61e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840266 134 QKHITYSIHNYTPKvgelDTRKAIRQAFDVWQKVTPLTFEEVPyheiksDRKEADIMIFFASGFHGDsspfDGEGGFLAH 213
Cdd:cd04268     1 KKPITYYIDDSVPD----KLRAAILDAIEAWNKAFAIGFKNAN------DVDPADIRYSVIRWIPYN----DGTWSYGPS 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840266 214 AYFPGPG--IGGDTHFDSDEPWTLGNANHDgndlflVAVHELGHALGLEHSNDPSAIMAPFYQYMETH-----------N 280
Cdd:cd04268    67 QVDPLTGeiLLARVYLYSSFVEYSGARLRN------TAEHELGHALGLRHNFAASDRDDNVDLLAEKGdtssvmdyapsN 140

                         170       180
                  ....*....|....*....|....*
gi 1622840266 281 FKLPQ----------DDLQGIQKIY 295
Cdd:cd04268   141 FSIQLgdgqkytigpYDIAAIKKLY 165
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 445-490 1.17e-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: 59.50  E-value: 1.17e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1622840266 445 IDTALRWEPvGKTYFFKGERYWRYSEERRatDPGYPKPITVWKGIP 490
Cdd:pfam00045   1 IDAAFEDRD-GKTYFFKGRKYWRFDPQRV--EPGYPKLISDFPGLP 43
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 445-490 2.16e-10

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


Pssm-ID: 214524 [Multi-domain]  Cd Length: 45  Bit Score: 56.10  E-value: 2.16e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1622840266  445 IDTALRWePVGKTYFFKGERYWRYSEERRatDPGYPKPIT-VWKGIP 490
Cdd:smart00120   1 IDAAFEL-RDGKTYFFKGDKYWRFDPKRV--DPGYPKLISsFFPGLP 44
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 398-436 4.04e-10

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


Pssm-ID: 395000 [Multi-domain]  Cd Length: 44  Bit Score: 55.27  E-value: 4.04e-10
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1622840266 398 IDAAYERADGRFVFFKGDKYWVFKEVTVEPGYPHSLGEL 436
Cdd:pfam00045   1 IDAAFEDRDGKTYFFKGRKYWRFDPQRVEPGYPKLISDF 39
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 398-442 2.15e-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: 2.15e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1622840266  398 IDAAYERADGRFVFFKGDKYWVFKEVTVEPGYPHSLGELGSCLPR 442
Cdd:smart00120   1 IDAAFELRDGKTYFFKGDKYWRFDPKRVDPGYPKLISSFFPGLPC 45
PG_binding_1 pfam01471
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ...
 51-103 1.45e-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: 51.36  E-value: 1.45e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1622840266  51 KNWLKSYGYllpYDSRASAlHSGKALQSAVSTMQQFYGIPVTGVLDQTTIEWM 103
Cdd:pfam01471   9 QRYLNRLGY---YPGPVDG-YFGPSTEAAVKAFQRAFGLPVDGIVDPETLAAL 57
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 360-395 2.51e-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: 50.32  E-value: 2.51e-08
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1622840266  360 RGEMFVFKDRWFWRLRNNRVQEGYPMQIEQFWKGLP 395
Cdd:smart00120   9 DGKTYFFKGDKYWRFDPKRVDPGYPKLISSFFPGLP 44
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 358-395 5.84e-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: 46.41  E-value: 5.84e-07
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1622840266 358 LFRGEMFVFKDRWFWRLRNNRVQEGYPMQIEQFWkGLP 395
Cdd:pfam00045   7 DRDGKTYFFKGRKYWRFDPQRVEPGYPKLISDFP-GLP 43
Hemopexin pfam00045
Hemopexin; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 494-538 8.98e-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: 45.64  E-value: 8.98e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1622840266 494 QGAFISKEGYyTYFYKGRDYWKFDNQKlsVEPGYPRNILRD-WMGC 538
Cdd:pfam00045   2 DAAFEDRDGK-TYFFKGRKYWRFDPQR--VEPGYPKLISDFpGLPC 44
HX smart00120
Hemopexin-like repeats; Hemopexin is a heme-binding protein that transports heme to the liver. ...
 495-537 1.32e-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: 45.31  E-value: 1.32e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1622840266  495 GAFISKEGYyTYFYKGRDYWKFDNQKlsVEPGYPRNILRDWMG 537
Cdd:smart00120   3 AAFELRDGK-TYFFKGDKYWRFDPKR--VDPGYPKLISSFFPG 42
COG5549 COG5549
Predicted Zn-dependent protease [Posttranslational modification, protein turnover, chaperones]; ...
 154-295 1.69e-05

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


Pssm-ID: 444292 [Multi-domain]  Cd Length: 234  Bit Score: 46.60  E-value: 1.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840266 154 RKAIRQAFDVWQKVtpLTFEEVpyheikSDRKEADIMIFFAS---GFHGDSSP----------FDGEGGFLAHAYfpgpg 220
Cdd:COG5549   103 VAAVLQAIAEWNAY--LPLEVV------ENPENADIIIVRSNpplTASPNPETgarsaettyeFYDTGNILSHRF----- 169

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622840266 221 iggdthfdsdepwTLG-NANHDGNDLFLVAVHELGHALGLE-HSNDPSAIMapfyqYME-THNFKLPQD-DLQGIQKIY 295
Cdd:COG5549   170 -------------TILlSPNQTGKYLLATARHELGHALGIWgHSPSPTDAM-----YFSqVRNPPPISPrDINTLKRIY 230
ZnMc_MMP_like_3 cd04327
Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal ...
 149-261 1.68e-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: 43.14  E-value: 1.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622840266 149 GELDTRKAIRQAFDVWQKVTPLTFEEVpyheiksDRKEADIMIFFASGfHGDSSpFDGEGGFLAHAYFPGPGIGGDTHFD 228
Cdd:cd04327    17 PDAFLKDKVRAAAREWLPYANLKFKFV-------TDADADIRISFTPG-DGYWS-YVGTDALLIGADAPTMNLGWFTDDT 87

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1622840266 229 SDepwtlgnanhdgNDLFLVAVHELGHALGLEH 261
Cdd:cd04327    88 PD------------PEFSRVVLHEFGHALGFIH 108
archmetzin NF033823
archaemetzincin family Zn-dependent metalloprotease;
241-269 2.16e-04

archaemetzincin family Zn-dependent metalloprotease;


Pssm-ID: 468195  Cd Length: 170  Bit Score: 42.22  E-value: 2.16e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1622840266 241 DGNDLFL-----VAVHELGHALGLEHSNDPSAIM 269
Cdd:NF033823  113 PDEDLFLerlakEAVHELGHLLGLGHCPNPRCVM 146
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
244-271 3.25e-04

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 41.87  E-value: 3.25e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1622840266 244 DLFL-----VAVHELGHALGLEHSNDPSAIMAP 271
Cdd:COG1913   117 ELFLervlkEAVHELGHLFGLGHCPNPRCVMHF 149
PRK13267 PRK13267
archaemetzincin-like protein; Reviewed
 249-269 2.28e-03

archaemetzincin-like protein; Reviewed


Pssm-ID: 237325  Cd Length: 179  Bit Score: 39.24  E-value: 2.28e-03
                          10        20
                  ....*....|....*....|.
gi 1622840266 249 AVHELGHALGLEHSNDPSAIM 269
Cdd:PRK13267  129 VTHELGHTLGLEHCDNPRCVM 149
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
 241-271 3.32e-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: 38.82  E-value: 3.32e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1622840266 241 DGNDLFL-----VAVHELGHALGLEHSNDPSAIMAP 271
Cdd:cd11375   114 PDEGLFLerllkEAVHELGHLFGLDHCPYYACVMNF 149
ZnMc_pappalysin_like cd04275
Zinc-dependent metalloprotease, pappalysin_like subfamily. The pregnancy-associated plasma ...
 205-261 7.05e-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: 7.05e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622840266 205 DGEGGFLAHAYFPGPGIGGDTHFD--SDEPWTLGNANHDGNDLFLVAVHELGHALGLEH 261
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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