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Conserved domains on  [gi|1753041289|ref|XP_018865443|]
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disintegrin and metalloproteinase domain-containing protein 21 isoform X1 [Gorilla gorilla gorilla]

Protein Classification

disintegrin and metalloproteinase domain-containing protein( domain architecture ID 10480592)

disintegrin and metalloproteinase domain-containing protein also contains an ADAM domain and belongs to the ADAM family of membrane-anchored metalloproteases; ADAMs (A Disintegrin And Metalloprotease) are glycoproteins that play roles in cell signaling, cell fusion, and cell-cell interactions

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 272-460 1.51e-68

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: 224.42  E-value: 1.51e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1753041289 272 WFLELVVVVNHDFFIYSQSNISKVQEDVFVVVNIVDSMYKQLGTYIILIGIEIWNQGNVFPMT-SIEQVLNDFSQWKQIS 350
Cdd:cd04269     1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSgDAGETLNRFLDWKRSN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1753041289 351 LS-QLQHDAAHMFIKNSLI-SILGLAYVAGICRPPIDCGVDNFQGDTWSLFANTVAHELGHTLGMQHDEEFCFCGERGCI 428
Cdd:cd04269    81 LLpRKPHDNAQLLTGRDFDgNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRSTCI 160

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1753041289 429 MNTFRV-PAEKFTNCSYADFMKTTLNQ-GSCLHD 460
Cdd:cd04269   161 MAPSPSsLTDAFSNCSYEDYQKFLSRGgGQCLLN 194
ACR smart00608
ADAM Cysteine-Rich Domain;
555-691 5.98e-62

ADAM Cysteine-Rich Domain;


:

Pssm-ID: 214743  Cd Length: 137  Bit Score: 204.52  E-value: 5.98e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1753041289  555 QDGIPCS-DSAYCYQKRCNNHDQHCREIFGKDAKSASQNCYKEINSQGNRFGHCGINGTTYLKCHISDVFCGRVQCENVR 633
Cdd:smart00608   1 QDGTPCDnGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1753041289  634 DIPLLQDHFTLQHTHINGVTCWGIDYHLRMNiSDIGEVKDGTVCGPGKICIHKKCVSL 691
Cdd:smart00608  81 ELPLLGEHATVIYSNIGGLVCWSLDYHLGTD-PDIGMVKDGTKCGPGKVCINGQCVDV 137
Disintegrin pfam00200
Disintegrin;
479-551 9.31e-35

Disintegrin;


:

Pssm-ID: 459709  Cd Length: 74  Bit Score: 126.59  E-value: 9.31e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1753041289 479 EREEQCDCGSVQQCEQDACCL-LNCTLRPGAACAFGLCCKDCKFMPSGELCRQEVNECDLPEWCNGTSHQCPED 551
Cdd:pfam00200   1 EEGEECDCGSLEECTNDPCCDaKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 105-223 1.22e-28

Reprolysin family propeptide; This region is the propeptide for members of peptidase family M12B. The propeptide contains a sequence motif similar to the "cysteine switch" of the matrixins. This motif is found at the C terminus of the alignment but is not well aligned.


:

Pssm-ID: 460254  Cd Length: 128  Bit Score: 111.25  E-value: 1.22e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1753041289 105 EVVIPLKVSSRGR------SAKAPGWLSYSLRFGGQKHVVHMRVKKLLVSRHLPVFTYTDERALLEDQLFIPDDCYYHGY 178
Cdd:pfam01562   1 EVVIPVRLDPSRRrrslasESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1753041289 179 VEGAPESLVVFSACfGGFRGVLKISGLTYEIEPI----RHSATFEHLVY 223
Cdd:pfam01562  81 VEGHPDSSVALSTC-SGLRGFIRTENEEYLIEPLekysREEGGHPHVVY 128
 
Name Accession Description Interval E-value
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 272-460 1.51e-68

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: 224.42  E-value: 1.51e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1753041289 272 WFLELVVVVNHDFFIYSQSNISKVQEDVFVVVNIVDSMYKQLGTYIILIGIEIWNQGNVFPMT-SIEQVLNDFSQWKQIS 350
Cdd:cd04269     1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSgDAGETLNRFLDWKRSN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1753041289 351 LS-QLQHDAAHMFIKNSLI-SILGLAYVAGICRPPIDCGVDNFQGDTWSLFANTVAHELGHTLGMQHDEEFCFCGERGCI 428
Cdd:cd04269    81 LLpRKPHDNAQLLTGRDFDgNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRSTCI 160

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1753041289 429 MNTFRV-PAEKFTNCSYADFMKTTLNQ-GSCLHD 460
Cdd:cd04269   161 MAPSPSsLTDAFSNCSYEDYQKFLSRGgGQCLLN 194
ACR smart00608
ADAM Cysteine-Rich Domain;
555-691 5.98e-62

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 204.52  E-value: 5.98e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1753041289  555 QDGIPCS-DSAYCYQKRCNNHDQHCREIFGKDAKSASQNCYKEINSQGNRFGHCGINGTTYLKCHISDVFCGRVQCENVR 633
Cdd:smart00608   1 QDGTPCDnGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1753041289  634 DIPLLQDHFTLQHTHINGVTCWGIDYHLRMNiSDIGEVKDGTVCGPGKICIHKKCVSL 691
Cdd:smart00608  81 ELPLLGEHATVIYSNIGGLVCWSLDYHLGTD-PDIGMVKDGTKCGPGKVCINGQCVDV 137
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 556-659 1.06e-49

ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell surface and extracellular matrix (ECM) in order to alter cell behaviour. It has been shown that the cysteine-rich domain of ADAM13 regulates the protein's metalloprotease activity.


Pssm-ID: 462504  Cd Length: 105  Bit Score: 169.72  E-value: 1.06e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1753041289 556 DGIPCSDS-AYCYQKRCNNHDQHCREIFGKDAKSASQNCYKEINSQGNRFGHCGINGTTYLKCHISDVFCGRVQCENVRD 634
Cdd:pfam08516   1 DGTPCNNGqAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQCTNVKE 80

                          90       100
                  ....*....|....*....|....*
gi 1753041289 635 IPLLQDHFTLQHTHINGVTCWGIDY 659
Cdd:pfam08516  81 LPLLGEHATVIYTNINGVTCWGTDY 105
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 273-462 1.08e-45

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: 162.08  E-value: 1.08e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1753041289 273 FLELVVVVNHDFFIYSQSNISKVQEDVFVVVNIVDSMYKQLGTYIILIGIEIWNQGNVFPMTS-IEQVLNDFSQWKQISL 351
Cdd:pfam01421   2 YIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGdANDTLRNFLKWRQEYL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1753041289 352 SQL-QHDAAHMFIKNSLISI-LGLAYVAGICRPPIDCGVDNFQGDTWSLFANTVAHELGHTLGMQHDEEF--CFCGERG- 426
Cdd:pfam01421  82 KKRkPHDVAQLLSGVEFGGTtVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFNggCKCPPGGg 161

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1753041289 427 CIMN--TFRVPAEKFTNCSYADFMKTTLNQ-GSCLHDPP 462
Cdd:pfam01421 162 CIMNpsAGSSFPRKFSNCSQEDFEQFLTKQkGACLFNKP 200
Disintegrin pfam00200
Disintegrin;
479-551 9.31e-35

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 126.59  E-value: 9.31e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1753041289 479 EREEQCDCGSVQQCEQDACCL-LNCTLRPGAACAFGLCCKDCKFMPSGELCRQEVNECDLPEWCNGTSHQCPED 551
Cdd:pfam00200   1 EEGEECDCGSLEECTNDPCCDaKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 479-553 1.13e-31

Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to integrin receptors. They contain a 'RGD' sequence, identical to the recognition site of many adhesion proteins. Molecules containing both disintegrin and metalloprotease domains are known as ADAMs.


Pssm-ID: 214490  Cd Length: 75  Bit Score: 117.79  E-value: 1.13e-31
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1753041289  479 EREEQCDCGSVQQCeQDACC-LLNCTLRPGAACAFGLCCKDCKFMPSGELCRQEVNECDLPEWCNGTSHQCPEDRY 553
Cdd:smart00050   1 EEGEECDCGSPKEC-TDPCCdPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 105-223 1.22e-28

Reprolysin family propeptide; This region is the propeptide for members of peptidase family M12B. The propeptide contains a sequence motif similar to the "cysteine switch" of the matrixins. This motif is found at the C terminus of the alignment but is not well aligned.


Pssm-ID: 460254  Cd Length: 128  Bit Score: 111.25  E-value: 1.22e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1753041289 105 EVVIPLKVSSRGR------SAKAPGWLSYSLRFGGQKHVVHMRVKKLLVSRHLPVFTYTDERALLEDQLFIPDDCYYHGY 178
Cdd:pfam01562   1 EVVIPVRLDPSRRrrslasESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1753041289 179 VEGAPESLVVFSACfGGFRGVLKISGLTYEIEPI----RHSATFEHLVY 223
Cdd:pfam01562  81 VEGHPDSSVALSTC-SGLRGFIRTENEEYLIEPLekysREEGGHPHVVY 128
archmetzin NF033823
archaemetzincin family Zn-dependent metalloprotease;
403-430 1.71e-03

archaemetzincin family Zn-dependent metalloprotease;


Pssm-ID: 468195  Cd Length: 170  Bit Score: 39.91  E-value: 1.71e-03
                          10        20
                  ....*....|....*....|....*...
gi 1753041289 403 VAHELGHTLGMQHdeefcfCGERGCIMN 430
Cdd:NF033823  126 AVHELGHLLGLGH------CPNPRCVMH 147
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
403-430 2.52e-03

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 39.56  E-value: 2.52e-03
                          10        20
                  ....*....|....*....|....*...
gi 1753041289 403 VAHELGHTLGMQHdeefcfCGERGCIMN 430
Cdd:COG1913   127 AVHELGHLFGLGH------CPNPRCVMH 148
SVAGG NF038115
SVAGG family GlyGly-CTERM protein; The SVAGG (Shewanella/Vibrio/Aeromonas GlyGly-CTERM protein) ...
 375-454 3.98e-03

SVAGG family GlyGly-CTERM protein; The SVAGG (Shewanella/Vibrio/Aeromonas GlyGly-CTERM protein) family (defined and named here) averages about 420 amino acids in length. Member proteins have a C-terminal GlyGly-CTERM sorting signal, which implies cleavage by rhombosortase, export by a type II secretion system (T2SS), and covalent attachment to the outer membrane.


Pssm-ID: 468358 [Multi-domain]  Cd Length: 407  Bit Score: 40.53  E-value: 3.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1753041289 375 YVAGICRPPIDCGVDNFQGDTWSLFAN-TVAHELGHTLGMQH---DEEFCFCGERGcIMNTfrVPAEKFTNCSYADFMKT 450
Cdd:NF038115  149 NANGVAQVGMDLQVKGYNVTLDLYVATqTLAHELGHLFGLYNghaESAECSEGGYR-LMCG--SLAENFENLFGSSELQR 225


                  ....
gi 1753041289 451 TLNQ 454
Cdd:NF038115  226 FYNN 229
 
Name Accession Description Interval E-value
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 272-460 1.51e-68

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: 224.42  E-value: 1.51e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1753041289 272 WFLELVVVVNHDFFIYSQSNISKVQEDVFVVVNIVDSMYKQLGTYIILIGIEIWNQGNVFPMT-SIEQVLNDFSQWKQIS 350
Cdd:cd04269     1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSgDAGETLNRFLDWKRSN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1753041289 351 LS-QLQHDAAHMFIKNSLI-SILGLAYVAGICRPPIDCGVDNFQGDTWSLFANTVAHELGHTLGMQHDEEFCFCGERGCI 428
Cdd:cd04269    81 LLpRKPHDNAQLLTGRDFDgNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRSTCI 160

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1753041289 429 MNTFRV-PAEKFTNCSYADFMKTTLNQ-GSCLHD 460
Cdd:cd04269   161 MAPSPSsLTDAFSNCSYEDYQKFLSRGgGQCLLN 194
ACR smart00608
ADAM Cysteine-Rich Domain;
555-691 5.98e-62

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 204.52  E-value: 5.98e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1753041289  555 QDGIPCS-DSAYCYQKRCNNHDQHCREIFGKDAKSASQNCYKEINSQGNRFGHCGINGTTYLKCHISDVFCGRVQCENVR 633
Cdd:smart00608   1 QDGTPCDnGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1753041289  634 DIPLLQDHFTLQHTHINGVTCWGIDYHLRMNiSDIGEVKDGTVCGPGKICIHKKCVSL 691
Cdd:smart00608  81 ELPLLGEHATVIYSNIGGLVCWSLDYHLGTD-PDIGMVKDGTKCGPGKVCINGQCVDV 137
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 556-659 1.06e-49

ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell surface and extracellular matrix (ECM) in order to alter cell behaviour. It has been shown that the cysteine-rich domain of ADAM13 regulates the protein's metalloprotease activity.


Pssm-ID: 462504  Cd Length: 105  Bit Score: 169.72  E-value: 1.06e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1753041289 556 DGIPCSDS-AYCYQKRCNNHDQHCREIFGKDAKSASQNCYKEINSQGNRFGHCGINGTTYLKCHISDVFCGRVQCENVRD 634
Cdd:pfam08516   1 DGTPCNNGqAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQCTNVKE 80

                          90       100
                  ....*....|....*....|....*
gi 1753041289 635 IPLLQDHFTLQHTHINGVTCWGIDY 659
Cdd:pfam08516  81 LPLLGEHATVIYTNINGVTCWGTDY 105
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 273-462 1.08e-45

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: 162.08  E-value: 1.08e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1753041289 273 FLELVVVVNHDFFIYSQSNISKVQEDVFVVVNIVDSMYKQLGTYIILIGIEIWNQGNVFPMTS-IEQVLNDFSQWKQISL 351
Cdd:pfam01421   2 YIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGdANDTLRNFLKWRQEYL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1753041289 352 SQL-QHDAAHMFIKNSLISI-LGLAYVAGICRPPIDCGVDNFQGDTWSLFANTVAHELGHTLGMQHDEEF--CFCGERG- 426
Cdd:pfam01421  82 KKRkPHDVAQLLSGVEFGGTtVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFNggCKCPPGGg 161

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1753041289 427 CIMN--TFRVPAEKFTNCSYADFMKTTLNQ-GSCLHDPP 462
Cdd:pfam01421 162 CIMNpsAGSSFPRKFSNCSQEDFEQFLTKQkGACLFNKP 200
Disintegrin pfam00200
Disintegrin;
479-551 9.31e-35

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 126.59  E-value: 9.31e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1753041289 479 EREEQCDCGSVQQCEQDACCL-LNCTLRPGAACAFGLCCKDCKFMPSGELCRQEVNECDLPEWCNGTSHQCPED 551
Cdd:pfam00200   1 EEGEECDCGSLEECTNDPCCDaKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 479-553 1.13e-31

Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to integrin receptors. They contain a 'RGD' sequence, identical to the recognition site of many adhesion proteins. Molecules containing both disintegrin and metalloprotease domains are known as ADAMs.


Pssm-ID: 214490  Cd Length: 75  Bit Score: 117.79  E-value: 1.13e-31
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1753041289  479 EREEQCDCGSVQQCeQDACC-LLNCTLRPGAACAFGLCCKDCKFMPSGELCRQEVNECDLPEWCNGTSHQCPEDRY 553
Cdd:smart00050   1 EEGEECDCGSPKEC-TDPCCdPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 105-223 1.22e-28

Reprolysin family propeptide; This region is the propeptide for members of peptidase family M12B. The propeptide contains a sequence motif similar to the "cysteine switch" of the matrixins. This motif is found at the C terminus of the alignment but is not well aligned.


Pssm-ID: 460254  Cd Length: 128  Bit Score: 111.25  E-value: 1.22e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1753041289 105 EVVIPLKVSSRGR------SAKAPGWLSYSLRFGGQKHVVHMRVKKLLVSRHLPVFTYTDERALLEDQLFIPDDCYYHGY 178
Cdd:pfam01562   1 EVVIPVRLDPSRRrrslasESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1753041289 179 VEGAPESLVVFSACfGGFRGVLKISGLTYEIEPI----RHSATFEHLVY 223
Cdd:pfam01562  81 VEGHPDSSVALSTC-SGLRGFIRTENEEYLIEPLekysREEGGHPHVVY 128
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 273-444 7.78e-25

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: 102.50  E-value: 7.78e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1753041289 273 FLELVVVVNHDFFIYSQSNISKVQEDVFVVVNIVDSMYK----QLGTYIILIGIEIWNqGNVF---PMTSIEQVLNDFSQ 345
Cdd:cd04267     2 EIELVVVADHRMVSYFNSDENILQAYITELINIANSIYRstnlRLGIRISLEGLQILK-GEQFappIDSDASNTLNSFSF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1753041289 346 WKQISLSQlqHDAAHMFIKNSLIS--ILGLAYVAGICRPPIDCGV---DNFQGDTWslfaNTVAHELGHTLGMQHDEEFC 420
Cdd:cd04267    81 WRAEGPIR--HDNAVLLTAQDFIEgdILGLAYVGSMCNPYSSVGVvedTGFTLLTA----LTMAHELGHNLGAEHDGGDE 154

                         170       180       190
                  ....*....|....*....|....*....|
gi 1753041289 421 FCGERG----CIMNTFRVPAEK--FTNCSY 444
Cdd:cd04267   155 LAFECDgggnYIMAPVDSGLNSyrFSQCSI 184
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 273-459 7.11e-18

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: 82.67  E-value: 7.11e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1753041289 273 FLELVVVVNHDFF-IYSQSNiskVQEDVFVVVNIVDSMYKQ--LGTYI--ILIGIEIWNQGNVFPMTS--IEQVLNDFSQ 345
Cdd:cd04273     2 YVETLVVADSKMVeFHHGED---LEHYILTLMNIVASLYKDpsLGNSIniVVVRLIVLEDEESGLLISgnAQKSLKSFCR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1753041289 346 WKQ-----ISLSQLQHDAAHMF------IKNSLISILGLAYVAGICRPPIDCGVDnfQGDTWSLfANTVAHELGHTLGMQ 414
Cdd:cd04273    79 WQKklnppNDSDPEHHDHAILLtrqdicRSNGNCDTLGLAPVGGMCSPSRSCSIN--EDTGLSS-AFTIAHELGHVLGMP 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1753041289 415 HDEEFCFCGER---GCIM------NTFRVPaekFTNCS---YADFMKTtlNQGSCLH 459
Cdd:cd04273   156 HDGDGNSCGPEgkdGHIMsptlgaNTGPFT---WSKCSrryLTSFLDT--GDGNCLL 207
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 302-416 4.75e-12

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: 63.54  E-value: 4.75e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1753041289 302 VVNIVDSMY-KQLGTYIILIGIEIWNQGN-VFPMTSIEQVLNDFSQWKQISLSQLQHDAAHMFIKNSLISILGLAYVAGI 379
Cdd:pfam13582   6 LVNRANTIYeRDLGIRLQLAAIIITTSADtPYTSSDALEILDELQEVNDTRIGQYGYDLGHLFTGRDGGGGGGIAYVGGV 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1753041289 380 CRppidcgVDNFQGDTWSL------FANTVAHELGHTLGMQHD 416
Cdd:pfam13582  86 CN------SGSKFGVNSGSgpvgdtGADTFAHEIGHNFGLNHT 122
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 273-431 2.04e-08

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: 54.45  E-value: 2.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1753041289 273 FLELVVVVNHDFFiysqsNISKVQEDVFVVVNIVDSMYKQ-LGTYIILIGIEIWNQGNVFPMTSIeqvlnDFSQwkqisl 351
Cdd:cd00203     2 VIPYVVVADDRDV-----EEENLSAQIQSLILIAMQIWRDyLNIRFVLVGVEIDKADIAILVTRQ-----DFDG------ 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1753041289 352 sqlqhdaahmfiknsliSILGLAYVAGICRPPIDCGVDNFQGDTWSLFANTVAHELGHTLGMQHDEEFCFCGERGCIMNT 431
Cdd:cd00203    66 -----------------GTGGWAYLGRVCDSLRGVGVLQDNQSGTKEGAQTIAHELGHALGFYHDHDRKDRDDYPTIDDT 128
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 275-417 1.05e-07

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 53.51  E-value: 1.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1753041289 275 ELVVVVNHDFFIYSQSNiSKVQEDVFVVVNIVDSMYKQL---GTYIILIGIEI------------WNQGNVFPMTSIEQv 339
Cdd:cd04272     4 ELFVVVDYDHQSEFFSN-EQLIRYLAVMVNAANLRYRDLkspRIRLLLVGITIskdpdfepyihpINYGYIDAAETLEN- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1753041289 340 LNDFSQWKQIslsQLQHDAAHMFIKNSLI---------SILGLAYVAGICrppidcgVDNFQG---DTWSLF--ANTVAH 405
Cdd:cd04272    82 FNEYVKKKRD---YFNPDVVFLVTGLDMStysggslqtGTGGYAYVGGAC-------TENRVAmgeDTPGSYygVYTMTH 151

                         170
                  ....*....|..
gi 1753041289 406 ELGHTLGMQHDE 417
Cdd:cd04272   152 ELAHLLGAPHDG 163
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 295-416 3.29e-07

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: 51.48  E-value: 3.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1753041289 295 VQEDVFVVVNIVDSMYKQ--LGTYIILIGI-------EIWNQGNVFPMTSIEQV--LNDFSQWKqislSQLQHDAAH-MF 362
Cdd:pfam13574   3 VTENLVNVVNRVNQIYEPddININGGLVNPgeipattSASDSGNNYCNSPTTIVrrLNFLSQWR----GEQDYCLAHlVT 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1753041289 363 IKNSLISILGLAYVAGICR-------------PPIDCGVDNFQGDTWSLFAntvaHELGHTLGMQHD 416
Cdd:pfam13574  79 MGTFSGGELGLAYVGQICQkgasspktntglsTTTNYGSFNYPTQEWDVVA----HEVGHNFGATHD 141
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
276-431 3.59e-07

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 51.27  E-value: 3.59e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1753041289 276 LVVVVNHDFFIYSQSNisKVQEDVFVVVNIVDS-MYKQLGTYIILIGIEIWNQGNVFPMT-----SIEQVLNDF---SQW 346
Cdd:pfam13688   7 LLVAADCSYVAAFGGD--AAQANIINMVNTASNvYERDFNISLGLVNLTISDSTCPYTPPacstgDSSDRLSEFqdfSAW 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1753041289 347 KqislSQLQHDAAHMFIkNSLISILGLAYVAGICRPPIDCGVDNFQGDT-----WSLFANTVAHELGHTLGMQHD----- 416
Cdd:pfam13688  85 R----GTQNDDLAYLFL-MTNCSGGGLAWLGQLCNSGSAGSVSTRVSGNnvvvsTATEWQVFAHEIGHNFGAVHDcdsst 159

                         170       180
                  ....*....|....*....|..
gi 1753041289 417 -EEFCF-----CGERG-CIMNT 431
Cdd:pfam13688 160 sSQCCPpsnstCPAGGrYIMNP 181
ZnMc_ADAM_fungal cd04271
Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A ...
 295-416 3.03e-06

Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A Disintegrin And Metalloprotease) family of metalloproteases are integral membrane proteases acting on a variety of extracellular targets. They are involved in shedding soluble peptides or proteins from the cell surface. This subfamily contains fungal ADAMs, whose precise function has yet to be determined.


Pssm-ID: 239799 [Multi-domain]  Cd Length: 228  Bit Score: 48.96  E-value: 3.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1753041289 295 VQEDVFVVVNIVDSMYKQlgTYIILIGI-----------------EIWNQGnVFPMTSIEQVLNDFSQWKqislSQLQHD 357
Cdd:cd04271    23 ARRNILNNVNSASQLYES--SFNISLGLrnltisdascpstavdsAPWNLP-CNSRIDIDDRLSIFSQWR----GQQPDD 95

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1753041289 358 AA---HMFIKNSLISILGLAYVAGICRPPIdcgvdNFQGDTWSLFANTV----------AHELGHTLGMQHD 416
Cdd:cd04271    96 GNafwTLMTACPSGSEVGVAWLGQLCRTGA-----SDQGNETVAGTNVVvrtsnewqvfAHEIGHTFGAVHD 162
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 390-415 1.19e-03

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: 40.56  E-value: 1.19e-03
                          10        20
                  ....*....|....*....|....*.
gi 1753041289 390 NFQGDTWSLFANTVAHELGHTLGMQH 415
Cdd:cd04268    85 SFVEYSGARLRNTAEHELGHALGLRH 110
archmetzin NF033823
archaemetzincin family Zn-dependent metalloprotease;
403-430 1.71e-03

archaemetzincin family Zn-dependent metalloprotease;


Pssm-ID: 468195  Cd Length: 170  Bit Score: 39.91  E-value: 1.71e-03
                          10        20
                  ....*....|....*....|....*...
gi 1753041289 403 VAHELGHTLGMQHdeefcfCGERGCIMN 430
Cdd:NF033823  126 AVHELGHLLGLGH------CPNPRCVMH 147
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
403-430 2.52e-03

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 39.56  E-value: 2.52e-03
                          10        20
                  ....*....|....*....|....*...
gi 1753041289 403 VAHELGHTLGMQHdeefcfCGERGCIMN 430
Cdd:COG1913   127 AVHELGHLFGLGH------CPNPRCVMH 148
ZnMc_MMP_like_2 cd04276
Zinc-dependent metalloprotease; MMP_like sub-family 2. A group of bacterial metalloproteinase ...
 399-415 2.78e-03

Zinc-dependent metalloprotease; MMP_like sub-family 2. A group of bacterial metalloproteinase domains similar to matrix metalloproteinases and astacin.


Pssm-ID: 239803  Cd Length: 197  Bit Score: 39.62  E-value: 2.78e-03
                          10
                  ....*....|....*..
gi 1753041289 399 FANTVAHELGHTLGMQH 415
Cdd:cd04276   116 LRYLLAHEVGHTLGLRH 132
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
 402-430 3.21e-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: 39.20  E-value: 3.21e-03
                          10        20
                  ....*....|....*....|....*....
gi 1753041289 402 TVAHELGHTLGMQHdeefcfCGERGCIMN 430
Cdd:cd11375   126 EAVHELGHLFGLDH------CPYYACVMN 148
SVAGG NF038115
SVAGG family GlyGly-CTERM protein; The SVAGG (Shewanella/Vibrio/Aeromonas GlyGly-CTERM protein) ...
 375-454 3.98e-03

SVAGG family GlyGly-CTERM protein; The SVAGG (Shewanella/Vibrio/Aeromonas GlyGly-CTERM protein) family (defined and named here) averages about 420 amino acids in length. Member proteins have a C-terminal GlyGly-CTERM sorting signal, which implies cleavage by rhombosortase, export by a type II secretion system (T2SS), and covalent attachment to the outer membrane.


Pssm-ID: 468358 [Multi-domain]  Cd Length: 407  Bit Score: 40.53  E-value: 3.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1753041289 375 YVAGICRPPIDCGVDNFQGDTWSLFAN-TVAHELGHTLGMQH---DEEFCFCGERGcIMNTfrVPAEKFTNCSYADFMKT 450
Cdd:NF038115  149 NANGVAQVGMDLQVKGYNVTLDLYVATqTLAHELGHLFGLYNghaESAECSEGGYR-LMCG--SLAENFENLFGSSELQR 225


                  ....
gi 1753041289 451 TLNQ 454
Cdd:NF038115  226 FYNN 229
 
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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