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Conserved domains on  [gi|2282741847|sp|U6BLN5|]
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RecName: Full=Venom metalloproteinase BumaMPs1; Short=MPs1; AltName: Full=Acid trehalase; Flags: Precursor

Protein Classification

zinc metalloprotease( domain architecture ID 1881)

zinc metalloprotease may be a member of the astacin-like protease family or the adamalysin/reprolysin-like protease family

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ZnMc super family cl00064
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 179-377 8.14e-29

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.


The actual alignment was detected with superfamily member cd04272:

Pssm-ID: 469599  Cd Length: 220  Bit Score: 111.67  E-value: 8.14e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282741847 179 SSFTKSFQISSmetYLANMMNMVKIMFDSL-DLGIEVAIIGIIkLTKENEAKlaPYI-PLCSREMDSRETLDDMAEFYCN 256
Cdd:cd04272    15 SEFFSNEQLIR---YLAVMVNAANLRYRDLkSPRIRLLLVGIT-ISKDPDFE--PYIhPINYGYIDAAETLENFNEYVKK 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282741847 257 SADKLiqNADIVTLITTRPLGTFDeNGYFFNIHLGIAFLDNICVYcYKYAIVKEDTGIYQLANTVAHESAHLLGCDHDG- 335
Cdd:cd04272    89 KRDYF--NPDVVFLVTGLDMSTYS-GGSLQTGTGGYAYVGGACTE-NRVAMGEDTPGSYYGVYTMTHELAHLLGAPHDGs 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2282741847 336 --------EKGSLDCSARDGYIMSWNNEKIGK-KFSPCCKKRVEELITRRK 377
Cdd:cd04272   165 pppswvkgHPGSLDCPWDDGYIMSYVVNGERQyRFSQCSQRQIRNVFRRLG 215
 
Name Accession Description Interval E-value
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 179-377 8.14e-29

Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary glands of arthropods.


Pssm-ID: 239800  Cd Length: 220  Bit Score: 111.67  E-value: 8.14e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282741847 179 SSFTKSFQISSmetYLANMMNMVKIMFDSL-DLGIEVAIIGIIkLTKENEAKlaPYI-PLCSREMDSRETLDDMAEFYCN 256
Cdd:cd04272    15 SEFFSNEQLIR---YLAVMVNAANLRYRDLkSPRIRLLLVGIT-ISKDPDFE--PYIhPINYGYIDAAETLENFNEYVKK 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282741847 257 SADKLiqNADIVTLITTRPLGTFDeNGYFFNIHLGIAFLDNICVYcYKYAIVKEDTGIYQLANTVAHESAHLLGCDHDG- 335
Cdd:cd04272    89 KRDYF--NPDVVFLVTGLDMSTYS-GGSLQTGTGGYAYVGGACTE-NRVAMGEDTPGSYYGVYTMTHELAHLLGAPHDGs 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2282741847 336 --------EKGSLDCSARDGYIMSWNNEKIGK-KFSPCCKKRVEELITRRK 377
Cdd:cd04272   165 pppswvkgHPGSLDCPWDDGYIMSYVVNGERQyRFSQCSQRQIRNVFRRLG 215
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
170-362 7.70e-11

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 60.90  E-value: 7.70e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282741847 170 KIEYVFVTESSFTKSFQISSMETYLANMMNMVK-IMFDSLDLGIEVAIIGIikLTKENeaklaPYIPLCSREMDSRETLD 248
Cdd:pfam13688   4 TVALLVAADCSYVAAFGGDAAQANIINMVNTASnVYERDFNISLGLVNLTI--SDSTC-----PYTPPACSTGDSSDRLS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282741847 249 DMAEFycnSADKLIQNADIVTLITTRPLGtfdeNGyffnihlGIAFLDNIC------VYCYKYAIVKEDTGIYQLANTVA 322
Cdd:pfam13688  77 EFQDF---SAWRGTQNDDLAYLFLMTNCS----GG-------GLAWLGQLCnsgsagSVSTRVSGNNVVVSTATEWQVFA 142

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2282741847 323 HESAHLLGCDHDGEKGSLD---------CSARDGYIMSWNNEKIGKKFS 362
Cdd:pfam13688 143 HEIGHNFGAVHDCDSSTSSqccppsnstCPAGGRYIMNPSSSPNSTDFS 191
 
Name Accession Description Interval E-value
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 179-377 8.14e-29

Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary glands of arthropods.


Pssm-ID: 239800  Cd Length: 220  Bit Score: 111.67  E-value: 8.14e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282741847 179 SSFTKSFQISSmetYLANMMNMVKIMFDSL-DLGIEVAIIGIIkLTKENEAKlaPYI-PLCSREMDSRETLDDMAEFYCN 256
Cdd:cd04272    15 SEFFSNEQLIR---YLAVMVNAANLRYRDLkSPRIRLLLVGIT-ISKDPDFE--PYIhPINYGYIDAAETLENFNEYVKK 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282741847 257 SADKLiqNADIVTLITTRPLGTFDeNGYFFNIHLGIAFLDNICVYcYKYAIVKEDTGIYQLANTVAHESAHLLGCDHDG- 335
Cdd:cd04272    89 KRDYF--NPDVVFLVTGLDMSTYS-GGSLQTGTGGYAYVGGACTE-NRVAMGEDTPGSYYGVYTMTHELAHLLGAPHDGs 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2282741847 336 --------EKGSLDCSARDGYIMSWNNEKIGK-KFSPCCKKRVEELITRRK 377
Cdd:cd04272   165 pppswvkgHPGSLDCPWDDGYIMSYVVNGERQyRFSQCSQRQIRNVFRRLG 215
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 173-382 1.24e-14

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: 71.88  E-value: 1.24e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282741847 173 YVFVTESSFTKSFQ-ISSMETYLANMMNMVKIMFDSLDlgIEVAIIGIIKLTKENeaklapyipLCSREMDSRETLDDMA 251
Cdd:cd04269     6 VVVVDNSLYKKYGSnLSKVRQRVIEIVNIVDSIYRPLN--IRVVLVGLEIWTDKD---------KISVSGDAGETLNRFL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282741847 252 EFYCNSADKLIQNaDIVTLITTRplgtfdengYFFNIHLGIAFLDNICVYCYKYAIVKEDTGIYQL-ANTVAHESAHLLG 330
Cdd:cd04269    75 DWKRSNLLPRKPH-DNAQLLTGR---------DFDGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLfAVTMAHELGHNLG 144

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2282741847 331 CDHDGEkgslDCS-ARDGYIMSWNNEKIGKKFSPCCKKRVEELITRRKInHCI 382
Cdd:cd04269   145 MEHDDG----GCTcGRSTCIMAPSPSSLTDAFSNCSYEDYQKFLSRGGG-QCL 192
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 188-381 3.13e-13

Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions. This particular subfamily represents domain architectures that combine ADAM-like metalloproteinases with thrombospondin type-1 repeats. ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) proteinases are inhibited by TIMPs (tissue inhibitors of metalloproteinases), and they play roles in coagulation, angiogenesis, development and progression of arthritis. They hydrolyze the von Willebrand factor precursor and various components of the extracellular matrix.


Pssm-ID: 239801  Cd Length: 207  Bit Score: 68.03  E-value: 3.13e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282741847 188 SSMETYLANMMNMVKIMF--DSLDLGIEVAIIGIIKLTKENEAklapyiPLCSREMDSreTLDDMAEF---YCNSADKLI 262
Cdd:cd04273    20 EDLEHYILTLMNIVASLYkdPSLGNSINIVVVRLIVLEDEESG------LLISGNAQK--SLKSFCRWqkkLNPPNDSDP 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282741847 263 QNADIVTLITTRPLGTFDENGYFfnihLGIAFLDNICVYCYKYAIVkEDTGIyQLANTVAHESAHLLGCDHDGEKGSLDC 342
Cdd:cd04273    92 EHHDHAILLTRQDICRSNGNCDT----LGLAPVGGMCSPSRSCSIN-EDTGL-SSAFTIAHELGHVLGMPHDGDGNSCGP 165

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2282741847 343 SARDGYIMSWNNEKIGKKF--SPCCKKRVEELItRRKINHC 381
Cdd:cd04273   166 EGKDGHIMSPTLGANTGPFtwSKCSRRYLTSFL-DTGDGNC 205
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
170-362 7.70e-11

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 60.90  E-value: 7.70e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282741847 170 KIEYVFVTESSFTKSFQISSMETYLANMMNMVK-IMFDSLDLGIEVAIIGIikLTKENeaklaPYIPLCSREMDSRETLD 248
Cdd:pfam13688   4 TVALLVAADCSYVAAFGGDAAQANIINMVNTASnVYERDFNISLGLVNLTI--SDSTC-----PYTPPACSTGDSSDRLS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282741847 249 DMAEFycnSADKLIQNADIVTLITTRPLGtfdeNGyffnihlGIAFLDNIC------VYCYKYAIVKEDTGIYQLANTVA 322
Cdd:pfam13688  77 EFQDF---SAWRGTQNDDLAYLFLMTNCS----GG-------GLAWLGQLCnsgsagSVSTRVSGNNVVVSTATEWQVFA 142

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2282741847 323 HESAHLLGCDHDGEKGSLD---------CSARDGYIMSWNNEKIGKKFS 362
Cdd:pfam13688 143 HEIGHNFGAVHDCDSSTSSqccppsnstCPAGGRYIMNPSSSPNSTDFS 191
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 197-377 5.45e-10

Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis. Members of this family are also known as adamalysins. Most members of this family are snake venom endopeptidases, but there are also some mammalian proteins such as Swiss:P78325, and fertilin. Fertilin and closely related proteins appear to not have some active site residues and may not be active enzymes.


Pssm-ID: 426256 [Multi-domain]  Cd Length: 200  Bit Score: 58.47  E-value: 5.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282741847 197 MMNMVKIMFDSLDlgIEVAIIGIIKLTKENEAKLAPyiplcsremDSRETLDdmaEFYCNSADKLIQNA--DIVTLITTR 274
Cdd:pfam01421  31 VVNLVNSIYKELN--IRVVLVGLEIWTDEDKIDVSG---------DANDTLR---NFLKWRQEYLKKRKphDVAQLLSGV 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282741847 275 plgtfdengYFFNIHLGIAFLDNICVYCYKYAIV---KEDTGIyqLANTVAHESAHLLGCDHDGEKGSLDCSARDGYIMs 351
Cdd:pfam01421  97 ---------EFGGTTVGAAYVGGMCSLEYSGGVNedhSKNLES--FAVTMAHELGHNLGMQHDDFNGGCKCPPGGGCIM- 164

                         170       180       190
                  ....*....|....*....|....*....|
gi 2282741847 352 wnNEKIG----KKFSPCCKKRVEELITRRK 377
Cdd:pfam01421 165 --NPSAGssfpRKFSNCSQEDFEQFLTKQK 192
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 169-373 6.12e-10

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: 58.20  E-value: 6.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282741847 169 VKIEYVFVTESSFTKSFQ--ISSMETYLANMMNMV-KIMFD-SLDLGIEVAIIGIIKLTKENEAKlapyiplcSREMDSR 244
Cdd:cd04267     1 REIELVVVADHRMVSYFNsdENILQAYITELINIAnSIYRStNLRLGIRISLEGLQILKGEQFAP--------PIDSDAS 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282741847 245 ETLDdmaEFYCNSADKLIqNADIVTLITTRPLGTFDENGYffnihlgiAFLDNICvYCYKYAIVKEDTGI-YQLANTVAH 323
Cdd:cd04267    73 NTLN---SFSFWRAEGPI-RHDNAVLLTAQDFIEGDILGL--------AYVGSMC-NPYSSVGVVEDTGFtLLTALTMAH 139

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2282741847 324 ESAHLLGCDHDGE-KGSLDCSARDGYIMSWNNEKIGKK-FSPCCKKRVEELI 373
Cdd:cd04267   140 ELGHNLGAEHDGGdELAFECDGGGNYIMAPVDSGLNSYrFSQCSIGSIREFL 191
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 192-334 5.75e-08

Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the characteriztic binding motif HExxGHxxGxxH of Reprolysin-like peptidases of family M12B.


Pssm-ID: 463926 [Multi-domain]  Cd Length: 122  Bit Score: 50.83  E-value: 5.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282741847 192 TYLANMMNMVKIMFDSlDLGIEVAIIGIIKLTKENEaklaPYIplcsrEMDSRETLDDMAEFYCNSADKliQNADIVTLI 271
Cdd:pfam13582   1 ARIVSLVNRANTIYER-DLGIRLQLAAIIITTSADT----PYT-----SSDALEILDELQEVNDTRIGQ--YGYDLGHLF 68

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2282741847 272 TTRPlgtFDENGyffnihlGIAFLDNICVYCYKYAIVKEDTGIYQL-ANTVAHESAHLLGCDHD 334
Cdd:pfam13582  69 TGRD---GGGGG-------GIAYVGGVCNSGSKFGVNSGSGPVGDTgADTFAHEIGHNFGLNHT 122
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 192-367 2.05e-06

Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the characteriztic binding motif HExxGHxxGxxH of Reprolysin-like peptidases of family M12B.


Pssm-ID: 372637  Cd Length: 193  Bit Score: 48.01  E-value: 2.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282741847 192 TYLANMMNMVKIMFDSLDLGIEVAIIGIIKLTKENEAKlAPYIPLCSREMDSRETLDDMAEFYCNsadkliQNADIVTLI 271
Cdd:pfam13574   5 ENLVNVVNRVNQIYEPDDININGGLVNPGEIPATTSAS-DSGNNYCNSPTTIVRRLNFLSQWRGE------QDYCLAHLV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282741847 272 TtrpLGTFDENgyffniHLGIAFLDNICVYcyKYAIVKEDTGIYQLANT------------VAHESAHLLGCDHD----- 334
Cdd:pfam13574  78 T---MGTFSGG------ELGLAYVGQICQK--GASSPKTNTGLSTTTNYgsfnyptqewdvVAHEVGHNFGATHDcdgsq 146

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2282741847 335 -------GEKGSLDCSARDGYIMSWNNEKIGKKFSPCCKK 367
Cdd:pfam13574 147 yassgceRNAATSVCSANGSFIMNPASKSNNDLFSPCSIS 186
Reprolysin_4 pfam13583
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 263-364 2.05e-05

Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the characteriztic binding motif HExxGHxxGxxH of Reprolysin-like peptidases of family M12B.


Pssm-ID: 404471  Cd Length: 203  Bit Score: 45.30  E-value: 2.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282741847 263 QNADIVTLIttRPLGTFDENGyffnihlGIAFLDNICVYCY---KYAIVKEDTGIYQlanTVAHESAHLLGCDHDGEKGS 339
Cdd:pfam13583  90 LNYDLAYLT--LMTGPSGQNV-------GVAWVGALCSSARqnaKASGVARSRDEWD---IFAHEIGHTFGAVHDCSSQG 157

                          90       100       110
                  ....*....|....*....|....*....|
gi 2282741847 340 LD-----CSARDGYIMSWNNEKIGKKFSPC 364
Cdd:pfam13583 158 EGlssstEDGSGQTIMSYASTASQTAFSPC 187
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
 320-384 1.13e-03

Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha converting enzyme, releases soluble TNF-alpha from transmembrane pro-TNF-alpha.


Pssm-ID: 239798 [Multi-domain]  Cd Length: 244  Bit Score: 40.05  E-value: 1.13e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2282741847 320 TVAHESAHLLGCDHDgeKGSLDCS---ARDG-YIMS--------WNNekigKKFSPCCKKRVEELItRRKINHCIVE 384
Cdd:cd04270   170 VTAHELGHNFGSPHD--PDIAECApgeSQGGnYIMYaratsgdkENN----KKFSPCSKKSISKVL-EVKSNSCFVE 239
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 290-373 2.15e-03

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: 38.66  E-value: 2.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2282741847 290 LGIAFLDNICVyCYKYAIVKEDT--GIYQLANTVAHESAHLLGCDHDGEKGSLD-----------CSARDGYIMS--WNN 354
Cdd:cd00203    68 GGWAYLGRVCD-SLRGVGVLQDNqsGTKEGAQTIAHELGHALGFYHDHDRKDRDdyptiddtlnaEDDDYYSVMSytKGS 146

                          90       100
                  ....*....|....*....|.
gi 2282741847 355 EKIG--KKFSPCCKKRVEELI 373
Cdd:cd00203   147 FSDGqrKDFSQCDIDQINKLY 167
 
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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