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Conserved domains on  [gi|1894461557|ref|NP_001373298|]
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astacin-like metalloendopeptidase isoform 1 precursor [Danio rerio]

Protein Classification

M12 family metallopeptidase( domain architecture ID 10136691)

M12 family metallopeptidase such as astacin, a digestive enzyme isolated from crayfish, belongs to a group of zinc-dependent proteolytic enzymes with an HExxH zinc-binding site/active site

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ZnMc_astacin_like cd04280
Zinc-dependent metalloprotease, astacin_like subfamily or peptidase family M12A, a group of ...
111-281 6.66e-70

Zinc-dependent metalloprotease, astacin_like subfamily or peptidase family M12A, a group of zinc-dependent proteolytic enzymes with a HExxH zinc-binding site/active site. Members of this family may have an amino terminal propeptide, which is cleaved to yield the active protease domain, which is consequently always found at the N-terminus in multi-domain architectures. 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 (bone) morphogenesis, tolloid from drosophila, and the sea urchin SPAN protein, which may also play a role in development.


:

Pssm-ID: 239807 [Multi-domain]  Cd Length: 180  Bit Score: 213.97  E-value: 6.66e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894461557 111 VPYSIASGL-EDKTGHILAALKMVSKKTCVKFHHHTTEEDYLHFKPDRMCASLVGCAGGEQPILVGPKC-NAGNICHEIL 188
Cdd:cd04280     4 VPYVIDGSFdESDRSLILRAMREIESNTCIRFVPRTTEKDYIRIVKGSGCWSYVGRVGGRQVVSLGSGCfSLGTIVHELM 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894461557 189 HSLGLYHEHSRPDRDKYITILYDNIMPGKESNFK---VKKGNTLGLEYDLDSILHYGDDCFSRNGNHTIIPKKKGV-KIG 264
Cdd:cd04280    84 HALGFYHEQSRPDRDDYVTINWENIQPGYEHNFDkysPDTVTTYGVPYDYGSVMHYGPTAFSKNGKPTIVPKDPGYqIIG 163
                         170
                  ....*....|....*..
gi 1894461557 265 QRTHMSVLDVERLRRLY 281
Cdd:cd04280   164 QREGLSFLDIKKINKMY 180
 
Name Accession Description Interval E-value
ZnMc_astacin_like cd04280
Zinc-dependent metalloprotease, astacin_like subfamily or peptidase family M12A, a group of ...
111-281 6.66e-70

Zinc-dependent metalloprotease, astacin_like subfamily or peptidase family M12A, a group of zinc-dependent proteolytic enzymes with a HExxH zinc-binding site/active site. Members of this family may have an amino terminal propeptide, which is cleaved to yield the active protease domain, which is consequently always found at the N-terminus in multi-domain architectures. 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 (bone) morphogenesis, tolloid from drosophila, and the sea urchin SPAN protein, which may also play a role in development.


Pssm-ID: 239807 [Multi-domain]  Cd Length: 180  Bit Score: 213.97  E-value: 6.66e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894461557 111 VPYSIASGL-EDKTGHILAALKMVSKKTCVKFHHHTTEEDYLHFKPDRMCASLVGCAGGEQPILVGPKC-NAGNICHEIL 188
Cdd:cd04280     4 VPYVIDGSFdESDRSLILRAMREIESNTCIRFVPRTTEKDYIRIVKGSGCWSYVGRVGGRQVVSLGSGCfSLGTIVHELM 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894461557 189 HSLGLYHEHSRPDRDKYITILYDNIMPGKESNFK---VKKGNTLGLEYDLDSILHYGDDCFSRNGNHTIIPKKKGV-KIG 264
Cdd:cd04280    84 HALGFYHEQSRPDRDDYVTINWENIQPGYEHNFDkysPDTVTTYGVPYDYGSVMHYGPTAFSKNGKPTIVPKDPGYqIIG 163
                         170
                  ....*....|....*..
gi 1894461557 265 QRTHMSVLDVERLRRLY 281
Cdd:cd04280   164 QREGLSFLDIKKINKMY 180
Astacin pfam01400
Astacin (Peptidase family M12A); The members of this family are enzymes that cleave peptides. ...
101-283 1.60e-60

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 such as Swiss:P13497, and Tolloid from drosophila.


Pssm-ID: 426242 [Multi-domain]  Cd Length: 192  Bit Score: 190.57  E-value: 1.60e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894461557 101 LWPEKdgevSVPYSIASGLEDKT-GHILAALKMVSKKTCVKFHHHTT--EEDYLHFKPDRMCASLVGCAGGEQPILVGPK 177
Cdd:pfam01400   2 KWPNG----PIPYVIDGSLTGLArALIRQAMRHWENKTCIRFVERTPapDNNYLFFFKGDGCYSYVGRVGGRQPVSIGDG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894461557 178 C-NAGNICHEILHSLGLYHEHSRPDRDKYITILYDNIMPGKESNFKV---KKGNTLGLEYDLDSILHYGDDCFSRNGN-H 252
Cdd:pfam01400  78 CdKFGIIVHELGHALGFFHEQSRPDRDDYVSINWDNIDPGQEGNFDKydpSEVDSYGVPYDYGSIMHYGPNAFSKNGSlP 157
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1894461557 253 TIIPKKKGVK--IGQRTHMSVLDVERLRRLYHC 283
Cdd:pfam01400 158 TIVPKDNDYQatIGQRVKLSFYDIKKINKLYKC 190
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
98-237 2.65e-27

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: 103.20  E-value: 2.65e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894461557   98 GNHLWPEKDgevsVPYSIASGLEDKT--GHILAALKMVSKKTCVKFHHHTTEED-YLHF-KPDRMC-ASLVGCAGGEQPI 172
Cdd:smart00235   1 GSKKWPKGT----VPYVIDSSSLSPEerEAIAKALAEWSDVTCIRFVERTGTADiYISFgSGDSGCtLSHAGRPGGDQHL 76
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1894461557  173 LVGPKC-NAGNICHEILHSLGLYHEHSRPDRDKYITILYDNIMPGkesNFKVKKGNTLGLEYDLDS 237
Cdd:smart00235  77 SLGNGCiNTGVAAHELGHALGLYHEQSRSDRDNYMYINYTNIDTR---NFDLSEDDSLGIPYDYGS 139
 
Name Accession Description Interval E-value
ZnMc_astacin_like cd04280
Zinc-dependent metalloprotease, astacin_like subfamily or peptidase family M12A, a group of ...
111-281 6.66e-70

Zinc-dependent metalloprotease, astacin_like subfamily or peptidase family M12A, a group of zinc-dependent proteolytic enzymes with a HExxH zinc-binding site/active site. Members of this family may have an amino terminal propeptide, which is cleaved to yield the active protease domain, which is consequently always found at the N-terminus in multi-domain architectures. 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 (bone) morphogenesis, tolloid from drosophila, and the sea urchin SPAN protein, which may also play a role in development.


Pssm-ID: 239807 [Multi-domain]  Cd Length: 180  Bit Score: 213.97  E-value: 6.66e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894461557 111 VPYSIASGL-EDKTGHILAALKMVSKKTCVKFHHHTTEEDYLHFKPDRMCASLVGCAGGEQPILVGPKC-NAGNICHEIL 188
Cdd:cd04280     4 VPYVIDGSFdESDRSLILRAMREIESNTCIRFVPRTTEKDYIRIVKGSGCWSYVGRVGGRQVVSLGSGCfSLGTIVHELM 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894461557 189 HSLGLYHEHSRPDRDKYITILYDNIMPGKESNFK---VKKGNTLGLEYDLDSILHYGDDCFSRNGNHTIIPKKKGV-KIG 264
Cdd:cd04280    84 HALGFYHEQSRPDRDDYVTINWENIQPGYEHNFDkysPDTVTTYGVPYDYGSVMHYGPTAFSKNGKPTIVPKDPGYqIIG 163
                         170
                  ....*....|....*..
gi 1894461557 265 QRTHMSVLDVERLRRLY 281
Cdd:cd04280   164 QREGLSFLDIKKINKMY 180
Astacin pfam01400
Astacin (Peptidase family M12A); The members of this family are enzymes that cleave peptides. ...
101-283 1.60e-60

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 such as Swiss:P13497, and Tolloid from drosophila.


Pssm-ID: 426242 [Multi-domain]  Cd Length: 192  Bit Score: 190.57  E-value: 1.60e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894461557 101 LWPEKdgevSVPYSIASGLEDKT-GHILAALKMVSKKTCVKFHHHTT--EEDYLHFKPDRMCASLVGCAGGEQPILVGPK 177
Cdd:pfam01400   2 KWPNG----PIPYVIDGSLTGLArALIRQAMRHWENKTCIRFVERTPapDNNYLFFFKGDGCYSYVGRVGGRQPVSIGDG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894461557 178 C-NAGNICHEILHSLGLYHEHSRPDRDKYITILYDNIMPGKESNFKV---KKGNTLGLEYDLDSILHYGDDCFSRNGN-H 252
Cdd:pfam01400  78 CdKFGIIVHELGHALGFFHEQSRPDRDDYVSINWDNIDPGQEGNFDKydpSEVDSYGVPYDYGSIMHYGPNAFSKNGSlP 157
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1894461557 253 TIIPKKKGVK--IGQRTHMSVLDVERLRRLYHC 283
Cdd:pfam01400 158 TIVPKDNDYQatIGQRVKLSFYDIKKINKLYKC 190
ZnMc_hatching_enzyme cd04283
Zinc-dependent metalloprotease, hatching enzyme-like subfamily. Hatching enzymes are secreted ...
106-283 1.28e-59

Zinc-dependent metalloprotease, hatching enzyme-like subfamily. Hatching enzymes are secreted by teleost embryos to digest the egg envelope or chorion. In some teleosts, the hatching enzyme may be a system consisting of two evolutionary related metalloproteases, high choriolytic enzyme and low choriolytic enzyme (HCE and LCE), which may have different substrate specificities and cooperatively digest the chorion.


Pssm-ID: 239810 [Multi-domain]  Cd Length: 182  Bit Score: 187.85  E-value: 1.28e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894461557 106 DGEVSVPYSIASGL-EDKTGHILAALKMVSKKTCVKFHHHTTEEDYLHFKPDRMCASLVGCAGGEQPI-LVGPKC-NAGN 182
Cdd:cd04283     1 NGIVYVPYVISPQYsENERAVIEKAMQEFETLTCVRFVPRTTERDYLNIESRSGCWSYIGRQGGRQTVsLQKQGCmYKGI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894461557 183 ICHEILHSLGLYHEHSRPDRDKYITILYDNIMPGKESNFKVKKGNTLGLEYDLDSILHYGDDCFSRNGNHTIIPKKKG-V 261
Cdd:cd04283    81 IQHELLHALGFYHEQTRSDRDKYVRINWENIIPDQLYNFDKQDTNNLGTPYDYSSVMHYGRYAFSINGKPTIVPIPDPnV 160
                         170       180
                  ....*....|....*....|..
gi 1894461557 262 KIGQRTHMSVLDVERLRRLYHC 283
Cdd:cd04283   161 PIGQRQGMSNLDILRINKLYNC 182
ZnMc_BMP1_TLD cd04281
Zinc-dependent metalloprotease; BMP1/TLD-like subfamily. BMP1 (Bone morphogenetic protein 1) ...
101-283 2.56e-48

Zinc-dependent metalloprotease; BMP1/TLD-like subfamily. BMP1 (Bone morphogenetic protein 1) and TLD (tolloid)-like metalloproteases play vital roles in extracellular matrix formation, by cleaving precursor proteins such as enzymes, structural proteins, and proteins involved in the mineralization of the extracellular matrix. The drosophila protein tolloid and its Xenopus homologue xolloid cleave and inactivate Sog and chordin, respectively, which are inhibitors of Dpp (the Drosophila decapentaplegic gene product) and its homologue BMP4, involved in dorso-ventral patterning.


Pssm-ID: 239808 [Multi-domain]  Cd Length: 200  Bit Score: 159.53  E-value: 2.56e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894461557 101 LWPekDGevSVPYSIASGLedkTGH----ILAALKMVSKKTCVKFHHHTTEEDYLHFKPDRM-CASLVGCAG-GEQPILV 174
Cdd:cd04281     9 IWP--GG--VIPYVIDGNF---TGSqramFKQAMRHWENFTCVTFVERTPEENYIVFTYRPCgCCSYVGRRGnGPQAISI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894461557 175 GPKCNA-GNICHEILHSLGLYHEHSRPDRDKYITILYDNIMPGKESNF-KVKKG--NTLGLEYDLDSILHYGDDCFSRNG 250
Cdd:cd04281    82 GKNCDKfGIVVHELGHVIGFWHEHTRPDRDDHVTIIRENIQPGQEYNFlKMEPEevDSLGEPYDFDSIMHYARNTFSRGM 161
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1894461557 251 NH-TIIPKK--KGVK--IGQRTHMSVLDVERLRRLYHC 283
Cdd:cd04281   162 FLdTILPKRdpNGVRpeIGQRTRLSEGDIIQANKLYKC 199
ZnMc_meprin cd04282
Zinc-dependent metalloprotease, meprin_like subfamily. Meprins are membrane-bound or secreted ...
81-283 4.06e-37

Zinc-dependent metalloprotease, meprin_like subfamily. Meprins are membrane-bound or secreted extracellular proteases, which cleave a variety of targets, including peptides such as parathyroid hormone, gastrin, and cholecystokinin, cytokines such as osteopontin, and proteins such as collagen IV, fibronectin, casein and gelatin. Meprins may also be able to release proteins from the cell surface. Closely related meprin alpha- and beta-subunits form homo- and hetero-oligomers; these complexes are found on epithelial cells of the intestine, for example, and are also expressed in certain cancer cells.


Pssm-ID: 239809 [Multi-domain]  Cd Length: 230  Bit Score: 131.44  E-value: 4.06e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894461557  81 GYALEEEDII--PQTDRNA---GNHLWPekdgeVSVPYSIASGLE-DKTGHILAALKMVSKKTCVKFHHHTTEEDYLHFK 154
Cdd:cd04282    20 GLDLFEGDILldEGQSRNGligDTYRWP-----FPIPYILDDSLDlNAKGVILKAFEMYRLKSCVDFKPYEGESNYIFFF 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894461557 155 PDRMCASLVGCAGGEQPILVGPKCNA-GNICHEILHSLGLYHEHSRPDRDKYITILYDNIMPGKESNFKV---KKGNTLG 230
Cdd:cd04282    95 KGSGCWSMVGDQQGGQNLSIGAGCDYkATVEHEFLHALGFYHEQSRSDRDDYVKIWWDQILSGREHNFNKyddSFSTDLN 174
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1894461557 231 LEYDLDSILHYGDDCFSRNGNH----TIIPKKKGVkIGQRTHMSVLDVERLRRLYHC 283
Cdd:cd04282   175 TPYDYESVMHYSPFSFNKGASEptitTKIPEFNDI-IGQRLDFSDIDLERLNRMYNC 230
ZnMc smart00235
Zinc-dependent metalloprotease; Neutral zinc metallopeptidases. This alignment represents a ...
98-237 2.65e-27

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: 103.20  E-value: 2.65e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894461557   98 GNHLWPEKDgevsVPYSIASGLEDKT--GHILAALKMVSKKTCVKFHHHTTEED-YLHF-KPDRMC-ASLVGCAGGEQPI 172
Cdd:smart00235   1 GSKKWPKGT----VPYVIDSSSLSPEerEAIAKALAEWSDVTCIRFVERTGTADiYISFgSGDSGCtLSHAGRPGGDQHL 76
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1894461557  173 LVGPKC-NAGNICHEILHSLGLYHEHSRPDRDKYITILYDNIMPGkesNFKVKKGNTLGLEYDLDS 237
Cdd:smart00235  77 SLGNGCiNTGVAAHELGHALGLYHEQSRSDRDNYMYINYTNIDTR---NFDLSEDDSLGIPYDYGS 139
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
126-281 8.15e-12

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: 62.15  E-value: 8.15e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894461557 126 ILAALKMVSKKTCVKFHHHTTEED---------YLHFKPDRMCASLVG--CAGGEQPILVGPKC-----NAGNICHEILH 189
Cdd:cd00203    27 ILIAMQIWRDYLNIRFVLVGVEIDkadiailvtRQDFDGGTGGWAYLGrvCDSLRGVGVLQDNQsgtkeGAQTIAHELGH 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894461557 190 SLGLYHEHSRPDRDKYITILYDnimpgkesnfkvkkgnTLGLEYDLDSILHYGDDCFSrngnhtiipkkkgvkIGQRTHM 269
Cdd:cd00203   107 ALGFYHDHDRKDRDDYPTIDDT----------------LNAEDDDYYSVMSYTKGSFS---------------DGQRKDF 155
                         170
                  ....*....|..
gi 1894461557 270 SVLDVERLRRLY 281
Cdd:cd00203   156 SQCDIDQINKLY 167
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
183-281 7.30e-06

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: 45.18  E-value: 7.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894461557 183 ICHEILHSLGLYHEHSRPDRDKYITilydnimpgkesnfkvkkgnTLGLEYDLDSILHYGDDCFSRNGnhtiipkkkgvK 262
Cdd:cd04268    98 AEHELGHALGLRHNFAASDRDDNVD--------------------LLAEKGDTSSVMDYAPSNFSIQL-----------G 146
                          90
                  ....*....|....*....
gi 1894461557 263 IGQRTHMSVLDVERLRRLY 281
Cdd:cd04268   147 DGQKYTIGPYDIAAIKKLY 165
ZnMc_MMP_like_3 cd04327
Zinc-dependent metalloprotease; MMP_like sub-family 3. A group of bacterial and fungal ...
182-261 1.22e-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: 41.98  E-value: 1.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1894461557 182 NICHEILHSLGLYHEHSRPDRDkyITI----LYDNIM-PGKESNFKVKKGNTLGL---------EYDLDSILHY------ 241
Cdd:cd04327    95 VVLHEFGHALGFIHEHQSPAAN--IPWdkeaVYAYFSgPPNWDRETVINHNVFAKlddgdvaysPYDPDSIMHYpfpgsl 172
                          90       100
                  ....*....|....*....|.
gi 1894461557 242 -GDDcFSRNGNHTIIPKKKGV 261
Cdd:cd04327   173 tLDG-EEVPPNRTLSDKDKAF 192
 
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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