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Conserved domains on  [gi|6573493]
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Protein Classification

ZnMc_MMP domain-containing protein (domain architecture ID 11995183)

ZnMc_MMP domain-containing protein

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 ...
4-158 1.64e-91

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


:

Pssm-ID: 334067  Cd Length: 159  Bit Score: 262.55  E-value: 1.64e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6573493      4 KWDKNQITYRIIGYTPDLDPETVDDAFARAFQVWSDVTPLRFSRIHDGEADIMINFGRWEHGDGYPFDGKDGLLAHAFAP 83
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFARGDHGDGYPFDGPGGVLAHAFFP 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6573493     84 GTGVGGDSHFDDDELWSLG--KGVGYSLFLVAAHEFGHAMGLEHSQDPGALMAPIYTY--TKNFRLSQDDIKGIQELYG 158
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGssAPNGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPldPKKFRLSQDDIKGIQQLYG 159
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
4-158 1.64e-91

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


Pssm-ID: 334067  Cd Length: 159  Bit Score: 262.55  E-value: 1.64e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6573493      4 KWDKNQITYRIIGYTPDLDPETVDDAFARAFQVWSDVTPLRFSRIHDGEADIMINFGRWEHGDGYPFDGKDGLLAHAFAP 83
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFARGDHGDGYPFDGPGGVLAHAFFP 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6573493     84 GTGVGGDSHFDDDELWSLG--KGVGYSLFLVAAHEFGHAMGLEHSQDPGALMAPIYTY--TKNFRLSQDDIKGIQELYG 158
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGssAPNGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPldPKKFRLSQDDIKGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
4-158 1.14e-85

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: 247.89  E-value: 1.14e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6573493    4 KWDKNQITYRIIGYTPDLDPETVDDAFARAFQVWSDVTPLRFSRIHDG-EADIMINFGRWEHGDGYPFDGKDGLLAHAFA 82
Cdd:cd04278   1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGqEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6573493   83 PGtGVGGDSHFDDDELWSLGKGV-GYSLFLVAAHEFGHAMGLEHSQDPGALMAPIYT-YTKNFRLSQDDIKGIQELYG 158
Cdd:cd04278  81 PG-GIGGDIHFDDDEQWTLGSDSgGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQgPVPKFKLSQDDIRGIQALYG 157
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
1-159 3.79e-41

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: 134.40  E-value: 3.79e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6573493       1 RKPKWDKNQITYRIigYTPDLDPEtVDDAFARAFQVWSDVTPLRFSRIhDGEADIMINFGRWEHGdgypfdgkdGLLAHA 80
Cdd:smart00235   1 GSKKWPKGTVPYVI--DSSSLSPE-EREAIAKALAEWSDVTCIRFVER-TGTADIYISFGSGDSG---------CTLSHA 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6573493      81 FAPGtgvgGDSHFDDdELWSLGKGVgyslflvAAHEFGHAMGLEHSQDPGA---LMAPIYTY--TKNFRLSQDDIKGIQE 155
Cdd:smart00235  68 GRPG----GDQHLSL-GNGCINTGV-------AAHELGHALGLYHEQSRSDrdnYMYINYTNidTRNFDLSEDDSLGIPY 135

                   ....
gi 6573493     156 LYGA 159
Cdd:smart00235 136 DYGS 139
 
Name Accession Description Interval E-value
Peptidase_M10 pfam00413
Matrixin; The members of this family are enzymes that cleave peptides. These proteases require ...
4-158 1.64e-91

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


Pssm-ID: 334067  Cd Length: 159  Bit Score: 262.55  E-value: 1.64e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6573493      4 KWDKNQITYRIIGYTPDLDPETVDDAFARAFQVWSDVTPLRFSRIHDGEADIMINFGRWEHGDGYPFDGKDGLLAHAFAP 83
Cdd:pfam00413   1 KWRKKNLTYRILNYTPDLPRAEVRRAIRRAFKVWSEVTPLTFTEVSTGEADIMIGFARGDHGDGYPFDGPGGVLAHAFFP 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6573493     84 GTGVGGDSHFDDDELWSLG--KGVGYSLFLVAAHEFGHAMGLEHSQDPGALMAPIYTY--TKNFRLSQDDIKGIQELYG 158
Cdd:pfam00413  81 GPGLGGDIHFDDDETWTVGssAPNGINLFLVAAHEIGHALGLGHSSDPGAIMYPTYSPldPKKFRLSQDDIKGIQQLYG 159
ZnMc_MMP cd04278
Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are ...
4-158 1.14e-85

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: 247.89  E-value: 1.14e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6573493    4 KWDKNQITYRIIGYTPDLDPETVDDAFARAFQVWSDVTPLRFSRIHDG-EADIMINFGRWEHGDGYPFDGKDGLLAHAFA 82
Cdd:cd04278   1 KWSKTNLTYRILNYPPDLPRDDVRRAIARAFRVWSDVTPLTFREVTSGqEADIRISFARGNHGDGYPFDGPGGTLAHAFF 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6573493   83 PGtGVGGDSHFDDDELWSLGKGV-GYSLFLVAAHEFGHAMGLEHSQDPGALMAPIYT-YTKNFRLSQDDIKGIQELYG 158
Cdd:cd04278  81 PG-GIGGDIHFDDDEQWTLGSDSgGTDLFSVAAHEIGHALGLGHSSDPDSIMYPYYQgPVPKFKLSQDDIRGIQALYG 157
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
1-159 3.79e-41

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: 134.40  E-value: 3.79e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6573493       1 RKPKWDKNQITYRIigYTPDLDPEtVDDAFARAFQVWSDVTPLRFSRIhDGEADIMINFGRWEHGdgypfdgkdGLLAHA 80
Cdd:smart00235   1 GSKKWPKGTVPYVI--DSSSLSPE-EREAIAKALAEWSDVTCIRFVER-TGTADIYISFGSGDSG---------CTLSHA 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6573493      81 FAPGtgvgGDSHFDDdELWSLGKGVgyslflvAAHEFGHAMGLEHSQDPGA---LMAPIYTY--TKNFRLSQDDIKGIQE 155
Cdd:smart00235  68 GRPG----GDQHLSL-GNGCINTGV-------AAHELGHALGLYHEQSRSDrdnYMYINYTNidTRNFDLSEDDSLGIPY 135

                   ....
gi 6573493     156 LYGA 159
Cdd:smart00235 136 DYGS 139
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
10-157 3.20e-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: 68.70  E-value: 3.20e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6573493   10 ITYRIIGYTPDLD----PETVDDAFARAFQVWSDVTPLRF--SRIHDGEADIMINFGRWehgdgypfDGKDGLLAHAFAP 83
Cdd:cd00203   3 IPYVVVADDRDVEeenlSAQIQSLILIAMQIWRDYLNIRFvlVGVEIDKADIAILVTRQ--------DFDGGTGGWAYLG 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6573493   84 GT--GVGGDSHFDDDELWslgkgvGYSLFLVAAHEFGHAMGLEHSQD--------------------PGALMAPI---YT 138
Cdd:cd00203  75 RVcdSLRGVGVLQDNQSG------TKEGAQTIAHELGHALGFYHDHDrkdrddyptiddtlnaedddYYSVMSYTkgsFS 148
                       170
                ....*....|....*....
gi 6573493  139 YTKNFRLSQDDIKGIQELY 157
Cdd:cd00203 149 DGQRKDFSQCDIDQINKLY 167
ZnMc_MMP_like_1 cd04279
Zinc-dependent metalloprotease; MMP_like sub-family 1. A group of bacterial, archaeal, and ...
19-158 2.36e-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  Cd Length: 156  Bit Score: 65.94  E-value: 2.36e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6573493   19 PDLDPETVDDAFARAFQVWSDVTPLRFSRI--HDGEADIMINFGRWEHGDGYpfdgkDGLLAHAFAPGTGVG--GDSHFD 94
Cdd:cd04279  15 PDSRAQSWLQAVKQAAAEWENVGPLKFVYNpeEDNDADIVIFFDRPPPVGGA-----GGGLARAGFPLISDGnrKLFNRT 89
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6573493   95 DDELWSLGKGVGYSLFLVAAHEFGHAMGLEHSQD-PGALMAPIYTY--TKNFRLSQDDIKGIQELYG 158
Cdd:cd04279  90 DINLGPGQPRGAENLQAIALHELGHALGLWHHSDrPEDAMYPSQGQgpDGNPTLSARDVATLKRLYG 156
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
7-157 2.06e-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: 61.36  E-value: 2.06e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6573493    7 KNQITYRIIGYTPDldpeTVDDAFARAFQVWSDVTPLRFSRIHDG-EADIMINFGRWEHGDGYPFdgkdGLLAHAFAPGT 85
Cdd:cd04268   1 KKPITYYIDDSVPD----KLRAAILDAIEAWNKAFAIGFKNANDVdPADIRYSVIRWIPYNDGTW----SYGPSQVDPLT 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6573493   86 GVggdSHFDDDELWSLGKG-VGYSLFLVAAHEFGHAMGLEHSQDPGALMAPIYTYTK----------------------- 141
Cdd:cd04268  73 GE---ILLARVYLYSSFVEySGARLRNTAEHELGHALGLRHNFAASDRDDNVDLLAEkgdtssvmdyapsnfsiqlgdgq 149
                       170
                ....*....|....*.
gi 6573493  142 NFRLSQDDIKGIQELY 157
Cdd:cd04268 150 KYTIGPYDIAAIKKLY 165
ZnMc_serralysin_like cd04277
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ...
28-158 1.16e-11

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


Pssm-ID: 239804  Cd Length: 186  Bit Score: 59.74  E-value: 1.16e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6573493   28 DAFARAFQVWSDVTPLRFSRIHDGE-ADIMINFGRWEHGDGYpfdgkdgllAHAFAPGTG----VGGDSHFDDDELWSLG 102
Cdd:cd04277  37 AAARDALEAWEDVADIDFVEVSDNSgADIRFGNSSDPDGNTA---------GYAYYPGSGsgtaYGGDIWFNSSYDTNSD 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6573493  103 KGVGYSlFLVAAHEFGHAMGLEHSQDPGA----------------LMA----PIYTYTKNFRLSQ----DDIKGIQELYG 158
Cdd:cd04277 108 SPGSYG-YQTIIHEIGHALGLEHPGDYNGgdpvpptyaldsreytVMSynsgYGNGASAGGGYPQtpmlLDIAALQYLYG 186
ZnMc_MMP_like_3 cd04327
Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal ...
23-125 4.82e-07

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: 46.99  E-value: 4.82e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6573493   23 PETVDDAFARAFQVWSDVTPLRFSRIHDGEADIMINFgrwEHGDGY-PFDGKDGLLAHAFAPGTGVGGDSHFDDDELWSL 101
Cdd:cd04327  18 DAFLKDKVRAAAREWLPYANLKFKFVTDADADIRISF---TPGDGYwSYVGTDALLIGADAPTMNLGWFTDDTPDPEFSR 94
                        90       100
                ....*....|....*....|....
gi 6573493  102 gkgvgyslflVAAHEFGHAMGLEH 125
Cdd:cd04327  95 ----------VVLHEFGHALGFIH 108
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
111-158 1.61e-04

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: 40.10  E-value: 1.61e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 6573493  111 LVAAHEFGHAMGLEHS----------QDPGALMAPIYTYTKNFRLSQDDIKGIQELYG 158
Cdd:cd04267 135 LTMAHELGHNLGAEHDggdelafecdGGGNYIMAPVDSGLNSYRFSQCSIGSIREFLD 192
Astacin pfam01400
Astacin (Peptidase family M12A); The members of this family are enzymes that cleave peptides. ...
4-127 5.86e-04

Astacin (Peptidase family M12A); The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis. Members of this family contain two conserved disulphide bridges, these are joined 1-4 and 2-3. Members of this family have an amino terminal propeptide which is cleaved to give the active protease domain. All other linked domains are found to the carboxyl terminus of this domain. This family includes: Astacin, a digestive enzyme from Crayfish. Meprin, a multiple domain membrane component that is constructed from a homologous alpha and beta chain. Proteins involved in morphogenesis and Tolloid from drosophila.


Pssm-ID: 279708 [Multi-domain]  Cd Length: 192  Bit Score: 38.42  E-value: 5.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6573493      4 KWDKNQITYRIIGYTPDLDPEtvddAFARAFQVWSDVTPLRFSRIHDGEADIMINFGRwehGDG-YPFDGKDGllahafa 82
Cdd:pfam01400   2 KWPNGPIPYVIDGSLTGLARA----LIRQAMRHWENKTCIRFVERTSAPDINYLFFFK---GDGcYSYVGRRG------- 67
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 6573493     83 PGTGVggdshfdddelwSLGKGVGYslFLVAAHEFGHAMGLEHSQ 127
Cdd:pfam01400  68 GRQPV------------SIGDGCDK--FGIIVHELGHALGFFHEQ 98
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
102-135 6.07e-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: 35.35  E-value: 6.07e-03
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 6573493  102 GKGVGYSLFL-----VAAHEFGHAMGLEHSQDPGALMAP 135
Cdd:cd11375 111 GLPPDEGLFLerllkEAVHELGHLFGLDHCPYYACVMNF 149
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.17
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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