NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1849023065|ref|XP_034793624|]
View 

disintegrin and metalloproteinase domain-containing protein 21 [Pan paniscus]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 208-396 1.49e-69

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: 225.96  E-value: 1.49e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849023065 208 WFLELVVVVNHDFFIYSQSNISKVQEDVFLVVNIVDSMYKQLGTYIILIGIEIWNQGNVFPMT-SIEQVLNDFSQWKQIS 286
Cdd:cd04269     1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSgDAGETLNRFLDWKRSN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849023065 287 LS-QLQHDAAHMFIKNSLI-SILGLAYVAGICRPPIDCGVDNFQGDTWSLFANTVAHELGHTLGMQHDEEFCFCGERGCI 364
Cdd:cd04269    81 LLpRKPHDNAQLLTGRDFDgNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRSTCI 160

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1849023065 365 MNTFRV-PAEKFTNCSYADFMKTTLNQ-GSCLHN 396
Cdd:cd04269   161 MAPSPSsLTDAFSNCSYEDYQKFLSRGgGQCLLN 194
ACR smart00608
ADAM Cysteine-Rich Domain;
491-627 7.46e-62

ADAM Cysteine-Rich Domain;


:

Pssm-ID: 214743  Cd Length: 137  Bit Score: 203.36  E-value: 7.46e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849023065  491 QDGIPCS-DSAYCYQKRCNNHDQHCREIFGKDAKSASQNCYKEINSQGNRFGHCGINGTTYLKCHISDVFCGRVQCENVR 569
Cdd:smart00608   1 QDGTPCDnGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1849023065  570 DIPLLQDHFTLQHTHINGVTCWGIDYHLRMNiSDIGEVKDGTVCGPGKICIHKKCVSL 627
Cdd:smart00608  81 ELPLLGEHATVIYSNIGGLVCWSLDYHLGTD-PDIGMVKDGTKCGPGKVCINGQCVDV 137
Disintegrin pfam00200
Disintegrin;
415-487 8.32e-35

Disintegrin;


:

Pssm-ID: 459709  Cd Length: 74  Bit Score: 126.59  E-value: 8.32e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1849023065 415 EREEQCDCGSVQQCEQDACCL-LNCTLRPGAACAFGLCCKDCKFMPSGELCRQEVNECDLPEWCNGTSHQCPED 487
Cdd:pfam00200   1 EEGEECDCGSLEECTNDPCCDaKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 41-159 5.43e-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: 109.33  E-value: 5.43e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849023065  41 EVVIPLKVISRGR------SAKTPGWLSYSLRFGGQKHVVHMRVKKLLVSRHLPVFTYTDEHALLEDQLFIPDDCYYHGY 114
Cdd:pfam01562   1 EVVIPVRLDPSRRrrslasESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1849023065 115 VEGAPESLVVFSACfGGFRGVLKISGLTYEIEPI----RHSATFEHLVY 159
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 ...
 208-396 1.49e-69

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: 225.96  E-value: 1.49e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849023065 208 WFLELVVVVNHDFFIYSQSNISKVQEDVFLVVNIVDSMYKQLGTYIILIGIEIWNQGNVFPMT-SIEQVLNDFSQWKQIS 286
Cdd:cd04269     1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSgDAGETLNRFLDWKRSN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849023065 287 LS-QLQHDAAHMFIKNSLI-SILGLAYVAGICRPPIDCGVDNFQGDTWSLFANTVAHELGHTLGMQHDEEFCFCGERGCI 364
Cdd:cd04269    81 LLpRKPHDNAQLLTGRDFDgNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRSTCI 160

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1849023065 365 MNTFRV-PAEKFTNCSYADFMKTTLNQ-GSCLHN 396
Cdd:cd04269   161 MAPSPSsLTDAFSNCSYEDYQKFLSRGgGQCLLN 194
ACR smart00608
ADAM Cysteine-Rich Domain;
491-627 7.46e-62

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 203.36  E-value: 7.46e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849023065  491 QDGIPCS-DSAYCYQKRCNNHDQHCREIFGKDAKSASQNCYKEINSQGNRFGHCGINGTTYLKCHISDVFCGRVQCENVR 569
Cdd:smart00608   1 QDGTPCDnGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1849023065  570 DIPLLQDHFTLQHTHINGVTCWGIDYHLRMNiSDIGEVKDGTVCGPGKICIHKKCVSL 627
Cdd:smart00608  81 ELPLLGEHATVIYSNIGGLVCWSLDYHLGTD-PDIGMVKDGTKCGPGKVCINGQCVDV 137
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 492-595 1.62e-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: 168.56  E-value: 1.62e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849023065 492 DGIPCSDS-AYCYQKRCNNHDQHCREIFGKDAKSASQNCYKEINSQGNRFGHCGINGTTYLKCHISDVFCGRVQCENVRD 570
Cdd:pfam08516   1 DGTPCNNGqAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQCTNVKE 80

                          90       100
                  ....*....|....*....|....*
gi 1849023065 571 IPLLQDHFTLQHTHINGVTCWGIDY 595
Cdd:pfam08516  81 LPLLGEHATVIYTNINGVTCWGTDY 105
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 209-398 3.71e-46

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: 162.86  E-value: 3.71e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849023065 209 FLELVVVVNHDFFIYSQSNISKVQEDVFLVVNIVDSMYKQLGTYIILIGIEIWNQGNVFPMTS-IEQVLNDFSQWKQISL 287
Cdd:pfam01421   2 YIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGdANDTLRNFLKWRQEYL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849023065 288 SQL-QHDAAHMFIKNSLISI-LGLAYVAGICRPPIDCGVDNFQGDTWSLFANTVAHELGHTLGMQHDEEF--CFCGERG- 362
Cdd:pfam01421  82 KKRkPHDVAQLLSGVEFGGTtVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFNggCKCPPGGg 161

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1849023065 363 CIMN--TFRVPAEKFTNCSYADFMKTTLNQ-GSCLHNPP 398
Cdd:pfam01421 162 CIMNpsAGSSFPRKFSNCSQEDFEQFLTKQkGACLFNKP 200
Disintegrin pfam00200
Disintegrin;
415-487 8.32e-35

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 126.59  E-value: 8.32e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1849023065 415 EREEQCDCGSVQQCEQDACCL-LNCTLRPGAACAFGLCCKDCKFMPSGELCRQEVNECDLPEWCNGTSHQCPED 487
Cdd:pfam00200   1 EEGEECDCGSLEECTNDPCCDaKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 415-489 1.12e-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: 1.12e-31
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1849023065  415 EREEQCDCGSVQQCeQDACC-LLNCTLRPGAACAFGLCCKDCKFMPSGELCRQEVNECDLPEWCNGTSHQCPEDRY 489
Cdd:smart00050   1 EEGEECDCGSPKEC-TDPCCdPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 41-159 5.43e-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: 109.33  E-value: 5.43e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849023065  41 EVVIPLKVISRGR------SAKTPGWLSYSLRFGGQKHVVHMRVKKLLVSRHLPVFTYTDEHALLEDQLFIPDDCYYHGY 114
Cdd:pfam01562   1 EVVIPVRLDPSRRrrslasESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1849023065 115 VEGAPESLVVFSACfGGFRGVLKISGLTYEIEPI----RHSATFEHLVY 159
Cdd:pfam01562  81 VEGHPDSSVALSTC-SGLRGFIRTENEEYLIEPLekysREEGGHPHVVY 128
archmetzin NF033823
archaemetzincin family Zn-dependent metalloprotease;
339-366 1.64e-03

archaemetzincin family Zn-dependent metalloprotease;


Pssm-ID: 468195  Cd Length: 170  Bit Score: 39.91  E-value: 1.64e-03
                          10        20
                  ....*....|....*....|....*...
gi 1849023065 339 VAHELGHTLGMQHdeefcfCGERGCIMN 366
Cdd:NF033823  126 AVHELGHLLGLGH------CPNPRCVMH 147
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
339-366 2.14e-03

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 39.56  E-value: 2.14e-03
                          10        20
                  ....*....|....*....|....*...
gi 1849023065 339 VAHELGHTLGMQHdeefcfCGERGCIMN 366
Cdd:COG1913   127 AVHELGHLFGLGH------CPNPRCVMH 148
SVAGG NF038115
SVAGG family GlyGly-CTERM protein; The SVAGG (Shewanella/Vibrio/Aeromonas GlyGly-CTERM protein) ...
 311-390 3.58e-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: 3.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849023065 311 YVAGICRPPIDCGVDNFQGDTWSLFAN-TVAHELGHTLGMQH---DEEFCFCGERGcIMNTfrVPAEKFTNCSYADFMKT 386
Cdd:NF038115  149 NANGVAQVGMDLQVKGYNVTLDLYVATqTLAHELGHLFGLYNghaESAECSEGGYR-LMCG--SLAENFENLFGSSELQR 225


                  ....
gi 1849023065 387 TLNQ 390
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 ...
 208-396 1.49e-69

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: 225.96  E-value: 1.49e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849023065 208 WFLELVVVVNHDFFIYSQSNISKVQEDVFLVVNIVDSMYKQLGTYIILIGIEIWNQGNVFPMT-SIEQVLNDFSQWKQIS 286
Cdd:cd04269     1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSgDAGETLNRFLDWKRSN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849023065 287 LS-QLQHDAAHMFIKNSLI-SILGLAYVAGICRPPIDCGVDNFQGDTWSLFANTVAHELGHTLGMQHDEEFCFCGERGCI 364
Cdd:cd04269    81 LLpRKPHDNAQLLTGRDFDgNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRSTCI 160

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1849023065 365 MNTFRV-PAEKFTNCSYADFMKTTLNQ-GSCLHN 396
Cdd:cd04269   161 MAPSPSsLTDAFSNCSYEDYQKFLSRGgGQCLLN 194
ACR smart00608
ADAM Cysteine-Rich Domain;
491-627 7.46e-62

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 203.36  E-value: 7.46e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849023065  491 QDGIPCS-DSAYCYQKRCNNHDQHCREIFGKDAKSASQNCYKEINSQGNRFGHCGINGTTYLKCHISDVFCGRVQCENVR 569
Cdd:smart00608   1 QDGTPCDnGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1849023065  570 DIPLLQDHFTLQHTHINGVTCWGIDYHLRMNiSDIGEVKDGTVCGPGKICIHKKCVSL 627
Cdd:smart00608  81 ELPLLGEHATVIYSNIGGLVCWSLDYHLGTD-PDIGMVKDGTKCGPGKVCINGQCVDV 137
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 492-595 1.62e-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: 168.56  E-value: 1.62e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849023065 492 DGIPCSDS-AYCYQKRCNNHDQHCREIFGKDAKSASQNCYKEINSQGNRFGHCGINGTTYLKCHISDVFCGRVQCENVRD 570
Cdd:pfam08516   1 DGTPCNNGqAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQCTNVKE 80

                          90       100
                  ....*....|....*....|....*
gi 1849023065 571 IPLLQDHFTLQHTHINGVTCWGIDY 595
Cdd:pfam08516  81 LPLLGEHATVIYTNINGVTCWGTDY 105
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 209-398 3.71e-46

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: 162.86  E-value: 3.71e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849023065 209 FLELVVVVNHDFFIYSQSNISKVQEDVFLVVNIVDSMYKQLGTYIILIGIEIWNQGNVFPMTS-IEQVLNDFSQWKQISL 287
Cdd:pfam01421   2 YIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGdANDTLRNFLKWRQEYL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849023065 288 SQL-QHDAAHMFIKNSLISI-LGLAYVAGICRPPIDCGVDNFQGDTWSLFANTVAHELGHTLGMQHDEEF--CFCGERG- 362
Cdd:pfam01421  82 KKRkPHDVAQLLSGVEFGGTtVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFNggCKCPPGGg 161

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1849023065 363 CIMN--TFRVPAEKFTNCSYADFMKTTLNQ-GSCLHNPP 398
Cdd:pfam01421 162 CIMNpsAGSSFPRKFSNCSQEDFEQFLTKQkGACLFNKP 200
Disintegrin pfam00200
Disintegrin;
415-487 8.32e-35

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 126.59  E-value: 8.32e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1849023065 415 EREEQCDCGSVQQCEQDACCL-LNCTLRPGAACAFGLCCKDCKFMPSGELCRQEVNECDLPEWCNGTSHQCPED 487
Cdd:pfam00200   1 EEGEECDCGSLEECTNDPCCDaKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 415-489 1.12e-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: 1.12e-31
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1849023065  415 EREEQCDCGSVQQCeQDACC-LLNCTLRPGAACAFGLCCKDCKFMPSGELCRQEVNECDLPEWCNGTSHQCPEDRY 489
Cdd:smart00050   1 EEGEECDCGSPKEC-TDPCCdPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 41-159 5.43e-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: 109.33  E-value: 5.43e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849023065  41 EVVIPLKVISRGR------SAKTPGWLSYSLRFGGQKHVVHMRVKKLLVSRHLPVFTYTDEHALLEDQLFIPDDCYYHGY 114
Cdd:pfam01562   1 EVVIPVRLDPSRRrrslasESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1849023065 115 VEGAPESLVVFSACfGGFRGVLKISGLTYEIEPI----RHSATFEHLVY 159
Cdd:pfam01562  81 VEGHPDSSVALSTC-SGLRGFIRTENEEYLIEPLekysREEGGHPHVVY 128
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 209-380 3.12e-24

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: 100.57  E-value: 3.12e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849023065 209 FLELVVVVNHDFFIYSQSNISKVQEDVFLVVNIVDSMYK----QLGTYIILIGIEIWNqGNVF---PMTSIEQVLNDFSQ 281
Cdd:cd04267     2 EIELVVVADHRMVSYFNSDENILQAYITELINIANSIYRstnlRLGIRISLEGLQILK-GEQFappIDSDASNTLNSFSF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849023065 282 WKQISLSQlqHDAAHMFIKNSLIS--ILGLAYVAGICRPPIDCGV---DNFQGDTWslfaNTVAHELGHTLGMQHDEEFC 356
Cdd:cd04267    81 WRAEGPIR--HDNAVLLTAQDFIEgdILGLAYVGSMCNPYSSVGVvedTGFTLLTA----LTMAHELGHNLGAEHDGGDE 154

                         170       180       190
                  ....*....|....*....|....*....|
gi 1849023065 357 FCGERG----CIMNTFRVPAEK--FTNCSY 380
Cdd:cd04267   155 LAFECDgggnYIMAPVDSGLNSyrFSQCSI 184
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 209-395 1.15e-17

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: 81.90  E-value: 1.15e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849023065 209 FLELVVVVNHDFF-IYSQSNiskVQEDVFLVVNIVDSMYKQ--LGTYI--ILIGIEIWNQGNVFPMTS--IEQVLNDFSQ 281
Cdd:cd04273     2 YVETLVVADSKMVeFHHGED---LEHYILTLMNIVASLYKDpsLGNSIniVVVRLIVLEDEESGLLISgnAQKSLKSFCR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849023065 282 WKQ-----ISLSQLQHDAAHMF------IKNSLISILGLAYVAGICRPPIDCGVDnfQGDTWSLfANTVAHELGHTLGMQ 350
Cdd:cd04273    79 WQKklnppNDSDPEHHDHAILLtrqdicRSNGNCDTLGLAPVGGMCSPSRSCSIN--EDTGLSS-AFTIAHELGHVLGMP 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1849023065 351 HDEEFCFCGER---GCIM------NTFRVPaekFTNCS---YADFMKTtlNQGSCLH 395
Cdd:cd04273   156 HDGDGNSCGPEgkdGHIMsptlgaNTGPFT---WSKCSrryLTSFLDT--GDGNCLL 207
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 238-352 5.11e-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: 63.16  E-value: 5.11e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849023065 238 VVNIVDSMY-KQLGTYIILIGIEIWNQGN-VFPMTSIEQVLNDFSQWKQISLSQLQHDAAHMFIKNSLISILGLAYVAGI 315
Cdd:pfam13582   6 LVNRANTIYeRDLGIRLQLAAIIITTSADtPYTSSDALEILDELQEVNDTRIGQYGYDLGHLFTGRDGGGGGGIAYVGGV 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1849023065 316 CRppidcgVDNFQGDTWSL------FANTVAHELGHTLGMQHD 352
Cdd:pfam13582  86 CN------SGSKFGVNSGSgpvgdtGADTFAHEIGHNFGLNHT 122
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 272-367 2.59e-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: 54.07  E-value: 2.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849023065 272 IEQVLNDFSQWKQI--SLSQLQ---HDAAHMFIKNSL-ISILGLAYVAGICRPPIDCGVDNFQGDTWSLFANTVAHELGH 345
Cdd:cd00203    27 ILIAMQIWRDYLNIrfVLVGVEidkADIAILVTRQDFdGGTGGWAYLGRVCDSLRGVGVLQDNQSGTKEGAQTIAHELGH 106

                          90       100
                  ....*....|....*....|..
gi 1849023065 346 TLGMQHDEEFCFCGERGCIMNT 367
Cdd:cd00203   107 ALGFYHDHDRKDRDDYPTIDDT 128
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
212-367 9.63e-08

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 52.81  E-value: 9.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849023065 212 LVVVVNHDFFIYSQSNisKVQEDVFLVVNIVDS-MYKQLGTYIILIGIEIWNQGNVFPMT-----SIEQVLNDF---SQW 282
Cdd:pfam13688   7 LLVAADCSYVAAFGGD--AAQANIINMVNTASNvYERDFNISLGLVNLTISDSTCPYTPPacstgDSSDRLSEFqdfSAW 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849023065 283 KqislSQLQHDAAHMFIkNSLISILGLAYVAGICRPPIDCGVDNFQGDT-----WSLFANTVAHELGHTLGMQHD----- 352
Cdd:pfam13688  85 R----GTQNDDLAYLFL-MTNCSGGGLAWLGQLCNSGSAGSVSTRVSGNnvvvsTATEWQVFAHEIGHNFGAVHDcdsst 159

                         170       180
                  ....*....|....*....|..
gi 1849023065 353 -EEFCF-----CGERG-CIMNT 367
Cdd:pfam13688 160 sSQCCPpsnstCPAGGrYIMNP 181
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 231-352 3.27e-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: 3.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849023065 231 VQEDVFLVVNIVDSMYKQ--LGTYIILIGI-------EIWNQGNVFPMTSIEQV--LNDFSQWKqislSQLQHDAAH-MF 298
Cdd:pfam13574   3 VTENLVNVVNRVNQIYEPddININGGLVNPgeipattSASDSGNNYCNSPTTIVrrLNFLSQWR----GEQDYCLAHlVT 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1849023065 299 IKNSLISILGLAYVAGICR-------------PPIDCGVDNFQGDTWSLFAntvaHELGHTLGMQHD 352
Cdd:pfam13574  79 MGTFSGGELGLAYVGQICQkgasspktntglsTTTNYGSFNYPTQEWDVVA----HEVGHNFGATHD 141
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 211-353 7.48e-07

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 50.81  E-value: 7.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849023065 211 ELVVVVNHDFFIYSQSNiSKVQEDVFLVVNIVDSMYKQL---GTYIILIGIEI------------WNQGNVFPMTSIEQv 275
Cdd:cd04272     4 ELFVVVDYDHQSEFFSN-EQLIRYLAVMVNAANLRYRDLkspRIRLLLVGITIskdpdfepyihpINYGYIDAAETLEN- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849023065 276 LNDFSQWKQIslsQLQHDAAHMFIKNSLI---------SILGLAYVAGICrppidcgVDNFQG---DTWSLF--ANTVAH 341
Cdd:cd04272    82 FNEYVKKKRD---YFNPDVVFLVTGLDMStysggslqtGTGGYAYVGGAC-------TENRVAmgeDTPGSYygVYTMTH 151

                         170
                  ....*....|..
gi 1849023065 342 ELGHTLGMQHDE 353
Cdd:cd04272   152 ELAHLLGAPHDG 163
ZnMc_ADAM_fungal cd04271
Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A ...
 231-352 2.47e-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: 49.34  E-value: 2.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849023065 231 VQEDVFLVVNIVDSMYKQlgTYIILIGI-----------------EIWNQGnVFPMTSIEQVLNDFSQWKqislSQLQHD 293
Cdd:cd04271    23 ARRNILNNVNSASQLYES--SFNISLGLrnltisdascpstavdsAPWNLP-CNSRIDIDDRLSIFSQWR----GQQPDD 95

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1849023065 294 AA---HMFIKNSLISILGLAYVAGICRPPIdcgvdNFQGDTWSLFANTV----------AHELGHTLGMQHD 352
Cdd:cd04271    96 GNafwTLMTACPSGSEVGVAWLGQLCRTGA-----SDQGNETVAGTNVVvrtsnewqvfAHEIGHTFGAVHD 162
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 326-351 1.08e-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: 1.08e-03
                          10        20
                  ....*....|....*....|....*.
gi 1849023065 326 NFQGDTWSLFANTVAHELGHTLGMQH 351
Cdd:cd04268    85 SFVEYSGARLRNTAEHELGHALGLRH 110
archmetzin NF033823
archaemetzincin family Zn-dependent metalloprotease;
339-366 1.64e-03

archaemetzincin family Zn-dependent metalloprotease;


Pssm-ID: 468195  Cd Length: 170  Bit Score: 39.91  E-value: 1.64e-03
                          10        20
                  ....*....|....*....|....*...
gi 1849023065 339 VAHELGHTLGMQHdeefcfCGERGCIMN 366
Cdd:NF033823  126 AVHELGHLLGLGH------CPNPRCVMH 147
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
339-366 2.14e-03

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 39.56  E-value: 2.14e-03
                          10        20
                  ....*....|....*....|....*...
gi 1849023065 339 VAHELGHTLGMQHdeefcfCGERGCIMN 366
Cdd:COG1913   127 AVHELGHLFGLGH------CPNPRCVMH 148
ZnMc_MMP_like_2 cd04276
Zinc-dependent metalloprotease; MMP_like sub-family 2. A group of bacterial metalloproteinase ...
 335-351 2.52e-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: 2.52e-03
                          10
                  ....*....|....*..
gi 1849023065 335 FANTVAHELGHTLGMQH 351
Cdd:cd04276   116 LRYLLAHEVGHTLGLRH 132
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
 338-366 2.91e-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: 2.91e-03
                          10        20
                  ....*....|....*....|....*....
gi 1849023065 338 TVAHELGHTLGMQHdeefcfCGERGCIMN 366
Cdd:cd11375   126 EAVHELGHLFGLDH------CPYYACVMN 148
SVAGG NF038115
SVAGG family GlyGly-CTERM protein; The SVAGG (Shewanella/Vibrio/Aeromonas GlyGly-CTERM protein) ...
 311-390 3.58e-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: 3.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1849023065 311 YVAGICRPPIDCGVDNFQGDTWSLFAN-TVAHELGHTLGMQH---DEEFCFCGERGcIMNTfrVPAEKFTNCSYADFMKT 386
Cdd:NF038115  149 NANGVAQVGMDLQVKGYNVTLDLYVATqTLAHELGHLFGLYNghaESAECSEGGYR-LMCG--SLAENFENLFGSSELQR 225


                  ....
gi 1849023065 387 TLNQ 390
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH