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Conserved domains on  [gi|157836903]
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Chain A, STROMELYSIN-1

Protein Classification

M10 family metallopeptidase domain-containing protein( domain architecture ID 11995183)

M10 family metallopeptidase domain-containing protein is a metalloendopeptidase similar to matrix metalloproteinases that may be endopeptidases that degrade various components of the extracellular matrix

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 ...
 9-165 3.68e-96

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


:

Pssm-ID: 425668 [Multi-domain]  Cd Length: 159  Bit Score: 274.88  E-value: 3.68e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157836903    9 KWRKTHLTYRIVNYTPDLPKDAVDSAVEKALKVWEEVTPLTFSRLYEGEADIMISFAVREHGDFYPFDGPGNVLAHAYAP 88
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157836903   89 GPGINGDAHFDDDEQWTKDTT---GTNLFLVAAHEIGHSLGLFHSANTEALMYPLYhSLTDLTRFRLSQDDINGIQSLYG 165
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSDpphGINLFLVAAHEIGHALGLGHSSDPGAIMYPTY-SPLDSKKFRLSQDDIKGIQQLYG 159
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 9-165 3.68e-96

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


Pssm-ID: 425668 [Multi-domain]  Cd Length: 159  Bit Score: 274.88  E-value: 3.68e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157836903    9 KWRKTHLTYRIVNYTPDLPKDAVDSAVEKALKVWEEVTPLTFSRLYEGEADIMISFAVREHGDFYPFDGPGNVLAHAYAP 88
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157836903   89 GPGINGDAHFDDDEQWTKDTT---GTNLFLVAAHEIGHSLGLFHSANTEALMYPLYhSLTDLTRFRLSQDDINGIQSLYG 165
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSDpphGINLFLVAAHEIGHALGLGHSSDPGAIMYPTY-SPLDSKKFRLSQDDIKGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 9-165 4.98e-84

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: 244.04  E-value: 4.98e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157836903   9 KWRKTHLTYRIVNYTPDLPKDAVDSAVEKALKVWEEVTPLTFSRL-YEGEADIMISFAVREHGDFYPFDGPGNVLAHAYA 87
Cdd:cd04278    1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVtSGQEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157836903  88 PGpGINGDAHFDDDEQWTKDT--TGTNLFLVAAHEIGHSLGLFHSANTEALMYPLYHSLTdlTRFRLSQDDINGIQSLYG 165
Cdd:cd04278   81 PG-GIGGDIHFDDDEQWTLGSdsGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPV--PKFKLSQDDIRGIQALYG 157
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 6-166 6.84e-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: 118.99  E-value: 6.84e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157836903     6 GIPKWRKTHLTYRIvnYTPDLPKDAvDSAVEKALKVWEEVTPLTFSRLYeGEADIMISFAVREHGDFYpfdgpgnvlAHA 85
Cdd:smart00235   1 GSKKWPKGTVPYVI--DSSSLSPEE-REAIAKALAEWSDVTCIRFVERT-GTADIYISFGSGDSGCTL---------SHA 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157836903    86 YAPGpginGDAHFDDdEQWTKDTTgtnlflVAAHEIGHSLGLFHSANTEA---LMYPLYHSlTDLTRFRLSQDDINGIQS 162
Cdd:smart00235  68 GRPG----GDQHLSL-GNGCINTG------VAAHELGHALGLYHEQSRSDrdnYMYINYTN-IDTRNFDLSEDDSLGIPY 135


                   ....
gi 157836903   163 LYGP 166
Cdd:smart00235 136 DYGS 139
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
116-139 3.48e-03

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 36.47  E-value: 3.48e-03
                         10        20
                 ....*....|....*....|....
gi 157836903 116 VAAHEIGHSLGLFHSANTEALMYP 139
Cdd:COG1913  126 EAVHELGHLFGLGHCPNPRCVMHF 149
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
 9-165 3.68e-96

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


Pssm-ID: 425668 [Multi-domain]  Cd Length: 159  Bit Score: 274.88  E-value: 3.68e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157836903    9 KWRKTHLTYRIVNYTPDLPKDAVDSAVEKALKVWEEVTPLTFSRLYEGEADIMISFAVREHGDFYPFDGPGNVLAHAYAP 88
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFGRGDHGDGYPFDGPGGVLAHAFFP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157836903   89 GPGINGDAHFDDDEQWTKDTT---GTNLFLVAAHEIGHSLGLFHSANTEALMYPLYhSLTDLTRFRLSQDDINGIQSLYG 165
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGSDpphGINLFLVAAHEIGHALGLGHSSDPGAIMYPTY-SPLDSKKFRLSQDDIKGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
 9-165 4.98e-84

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: 244.04  E-value: 4.98e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157836903   9 KWRKTHLTYRIVNYTPDLPKDAVDSAVEKALKVWEEVTPLTFSRL-YEGEADIMISFAVREHGDFYPFDGPGNVLAHAYA 87
Cdd:cd04278    1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVtSGQEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157836903  88 PGpGINGDAHFDDDEQWTKDT--TGTNLFLVAAHEIGHSLGLFHSANTEALMYPLYHSLTdlTRFRLSQDDINGIQSLYG 165
Cdd:cd04278   81 PG-GIGGDIHFDDDEQWTLGSdsGGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQGPV--PKFKLSQDDIRGIQALYG 157
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
 6-166 6.84e-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: 118.99  E-value: 6.84e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157836903     6 GIPKWRKTHLTYRIvnYTPDLPKDAvDSAVEKALKVWEEVTPLTFSRLYeGEADIMISFAVREHGDFYpfdgpgnvlAHA 85
Cdd:smart00235   1 GSKKWPKGTVPYVI--DSSSLSPEE-REAIAKALAEWSDVTCIRFVERT-GTADIYISFGSGDSGCTL---------SHA 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157836903    86 YAPGpginGDAHFDDdEQWTKDTTgtnlflVAAHEIGHSLGLFHSANTEA---LMYPLYHSlTDLTRFRLSQDDINGIQS 162
Cdd:smart00235  68 GRPG----GDQHLSL-GNGCINTG------VAAHELGHALGLYHEQSRSDrdnYMYINYTN-IDTRNFDLSEDDSLGIPY 135


                   ....
gi 157836903   163 LYGP 166
Cdd:smart00235 136 DYGS 139
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 15-164 1.18e-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: 70.24  E-value: 1.18e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157836903  15 LTYRIVNYT----PDLPKDAVDSAVEKALKVWEEVTPLTF--SRLYEGEADIMISFAvreHGDFypfdgPGNVLAHAYAP 88
Cdd:cd00203    3 IPYVVVADDrdveEENLSAQIQSLILIAMQIWRDYLNIRFvlVGVEIDKADIAILVT---RQDF-----DGGTGGWAYLG 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157836903  89 G--PGINGDAHFDDDEQWTKDttgtnLFLVAAHEIGHSLGLFHSANTEA--------------------LMYPLYHSLTD 146
Cdd:cd00203   75 RvcDSLRGVGVLQDNQSGTKE-----GAQTIAHELGHALGFYHDHDRKDrddyptiddtlnaedddyysVMSYTKGSFSD 149

                        170
                 ....*....|....*...
gi 157836903 147 LTRFRLSQDDINGIQSLY 164
Cdd:cd00203  150 GQRKDFSQCDIDQINKLY 167
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
 20-165 1.32e-14

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: 67.10  E-value: 1.32e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157836903  20 VNYTPDLPKDAVDS---AVEKALKVWEEVTPLTF--SRLYEGEADIMISFAVREHGDfypfdGPGNVLAHAYAPGPGING 94
Cdd:cd04279    8 IDPTPAPPDSRAQSwlqAVKQAAAEWENVGPLKFvyNPEEDNDADIVIFFDRPPPVG-----GAGGGLARAGFPLISDGN 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157836903  95 DA---HFDDDEQWTKDTTGTNLFLVAAHEIGHSLGLFH-SANTEALMYPLYHSLTDLTRfRLSQDDINGIQSLYG 165
Cdd:cd04279   83 RKlfnRTDINLGPGQPRGAENLQAIALHELGHALGLWHhSDRPEDAMYPSQGQGPDGNP-TLSARDVATLKRLYG 156
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
 33-165 5.07e-13

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: 63.59  E-value: 5.07e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157836903  33 SAVEKALKVWEEVTPLTFSRLYEGE-ADIMISFavrehgdfypFDGP-GNVLAHAYAPGPGIN----GDAHFDDDEQWTK 106
Cdd:cd04277   37 AAARDALEAWEDVADIDFVEVSDNSgADIRFGN----------SSDPdGNTAGYAYYPGSGSGtaygGDIWFNSSYDTNS 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157836903 107 DTTGTNLFLVAAHEIGHSLGLFHSANTEA----------------LM-YPLYHSLTDLTRFRLSQ----DDINGIQSLYG 165
Cdd:cd04277  107 DSPGSYGYQTIIHEIGHALGLEHPGDYNGgdpvpptyaldsreytVMsYNSGYGNGASAGGGYPQtpmlLDIAALQYLYG 186
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 15-164 4.30e-09

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


Pssm-ID: 239796 [Multi-domain]  Cd Length: 165  Bit Score: 52.50  E-value: 4.30e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157836903  15 LTYRIVNYTPDlpkdAVDSAVEKALKVWEEVTPLTFSRLYEG-EADIMISFaVRehgdfypfDGPGNVLAHAYAPG--PG 91
Cdd:cd04268    4 ITYYIDDSVPD----KLRAAILDAIEAWNKAFAIGFKNANDVdPADIRYSV-IR--------WIPYNDGTWSYGPSqvDP 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157836903  92 INGDAHFDDDEQWT--KDTTGTNLFLVAAHEIGHSLGLFHS----------------ANTEALMYPLYHS----LTDLTR 149
Cdd:cd04268   71 LTGEILLARVYLYSsfVEYSGARLRNTAEHELGHALGLRHNfaasdrddnvdllaekGDTSSVMDYAPSNfsiqLGDGQK 150

                        170
                 ....*....|....*
gi 157836903 150 FRLSQDDINGIQSLY 164
Cdd:cd04268  151 YTIGPYDIAAIKKLY 165
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 79-165 2.34e-05

Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ADAM family of metalloproteases contains proteolytic domains from snake venoms, proteases from the mammalian reproductive tract, and the tumor necrosis factor alpha convertase, TACE. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions.


Pssm-ID: 239795  Cd Length: 192  Bit Score: 42.79  E-value: 2.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157836903  79 GNVLAHAYAPGPGINGDahfddDEQWTKDTTGTNL-FLVAAHEIGHSLGLFHSANTEA----------LMYPlyhSLTDL 147
Cdd:cd04267  103 GDILGLAYVGSMCNPYS-----SVGVVEDTGFTLLtALTMAHELGHNLGAEHDGGDELafecdgggnyIMAP---VDSGL 174

                         90
                 ....*....|....*...
gi 157836903 148 TRFRLSQDDINGIQSLYG 165
Cdd:cd04267  175 NSYRFSQCSIGSIREFLD 192
ZnMc_MMP_like_3 cd04327
Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal ...
 27-129 2.02e-03

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: 36.97  E-value: 2.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157836903  27 PKDAVDSAVEKALKVWEEVTPLTFSRLYEGEADIMISFavREHGDFYPFDGPGNVLAHayAPGPGINgdahFDDDEQWTK 106
Cdd:cd04327   17 PDAFLKDKVRAAAREWLPYANLKFKFVTDADADIRISF--TPGDGYWSYVGTDALLIG--ADAPTMN----LGWFTDDTP 88

                         90       100
                 ....*....|....*....|...
gi 157836903 107 DTTGTNlflVAAHEIGHSLGLFH 129
Cdd:cd04327   89 DPEFSR---VVLHEFGHALGFIH 108
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
116-139 3.48e-03

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 36.47  E-value: 3.48e-03
                         10        20
                 ....*....|....*....|....
gi 157836903 116 VAAHEIGHSLGLFHSANTEALMYP 139
Cdd:COG1913  126 EAVHELGHLFGLGHCPNPRCVMHF 149
ZnMc_pappalysin_like cd04275
Zinc-dependent metalloprotease, pappalysin_like subfamily. The pregnancy-associated plasma ...
 71-129 5.52e-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: 36.16  E-value: 5.52e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157836903  71 DFYPFDGpGNVLAHAYAPGPGINGDAHFD----DDEQWTKDTTGT-NLFLVAAHEIGHSLGLFH 129
Cdd:cd04275   91 YVANFLG-GGLLGYATFPDSLVSLAFITDgvviNPSSLPGGSAAPyNLGDTATHEVGHWLGLYH 153
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 111-129 7.17e-03

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


Pssm-ID: 239797 [Multi-domain]  Cd Length: 194  Bit Score: 35.67  E-value: 7.17e-03
                         10        20
                 ....*....|....*....|..
gi 157836903 111 TNLFLVA---AHEIGHSLGLFH 129
Cdd:cd04269  126 RNLLLFAvtmAHELGHNLGMEH 147
 
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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