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Conserved domains on  [gi|1937871410|ref|NP_001014772|]
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disintegrin and metalloproteinase domain-containing protein 9 precursor [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 212-406 7.46e-93

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: 289.97  E-value: 7.46e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937871410 212 RYVELFIVVDKERYNMMGRNQTAVREEMIRLANYLDSMYIMLNIRIVLVGLEIWTDRNPINIIGGAGDVLGNFVQWREKF 291
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937871410 292 LITRRRHDSAQLVLKKGFGG-TAGMAFVGTVCSRSHAGGINVFGQITVETFASIVAHELGHNLGMNHDDG-RECFCA-AK 368
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFGGtTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFnGGCKCPpGG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1937871410 369 SCIMNS--GASGSRNFSSCSAEDFEKLTLNKGGSCLLNIP 406
Cdd:pfam01421 161 GCIMNPsaGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ACR smart00608
ADAM Cysteine-Rich Domain;
500-636 1.09e-57

ADAM Cysteine-Rich Domain;


:

Pssm-ID: 214743  Cd Length: 137  Bit Score: 193.35  E-value: 1.09e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937871410  500 QNGYPCWNSKAYCYNGVCQYYDAQCQVIFGSKAKAAPRDCFIEVNSKGDRFGNCGVSGSNYKTCATGNALCGKLQCENVQ 579
Cdd:smart00608   1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1937871410  580 EMPVFGIVPAIIQTPSRGTKCWGVDFQLGSDvPDPGMVNEGTKCDAGKICRNFQCVN 636
Cdd:smart00608  81 ELPLLGEHATVIYSNIGGLVCWSLDYHLGTD-PDIGMVKDGTKCGPGKVCINGQCVD 136
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 44-163 3.20e-43

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: 152.85  E-value: 3.20e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937871410  44 EIVTPWRL--SRERREALRPSSK--QISYVIQAQGKQHIIHLERNTDLLPNDFVVYTYDEEGSLLSDHPNVQSHCHYRGY 119
Cdd:pfam01562   1 EVVIPVRLdpSRRRRSLASESTYldTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1937871410 120 VEGVPNSTVAVSACFGLRGLLHLENASFGIEPLHN----SSHFEHVFY 163
Cdd:pfam01562  81 VEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEKysreEGGHPHVVY 128
Disintegrin pfam00200
Disintegrin;
423-496 5.99e-37

Disintegrin;


:

Pssm-ID: 459709  Cd Length: 74  Bit Score: 133.14  E-value: 5.99e-37
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1937871410 423 DPGEECDCGTPKECELDPCCEGSTCKLKSFAECAYGDCCKDCQFLPGGSMCRGKTSECDVPEYCNGSSQFCPPD 496
Cdd:pfam00200   1 EEGEECDCGSLEECTNDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
 732-802 2.68e-06

Proline-rich protein; This family includes several eukaryotic proline-rich proteins.


:

Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 48.50  E-value: 2.68e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1937871410 732 SQMSD--GRNQANASRPPGDPSVSRPPGGPSVSRPPGGPnvsrPPGGPNVSRPPGGPSVSRPPPVHGNRFPVP 802
Cdd:pfam15240  30 SLISEeeGQSQQGGQGPQGPPPGGFPPQPPASDDPPGPP----PPGGPQQPPPQGGKQKPQGPPPQGGPRPPP 98
EGF_2 pfam07974
EGF-like domain; This family contains EGF domains found in a variety of extracellular proteins.
 650-673 6.78e-03

EGF-like domain; This family contains EGF domains found in a variety of extracellular proteins.


:

Pssm-ID: 400365  Cd Length: 26  Bit Score: 34.63  E-value: 6.78e-03
                          10        20
                  ....*....|....*....|....*
gi 1937871410 650 CHGHGVCNS-NKNCHCEDGWAPPHC 673
Cdd:pfam07974   2 CSGRGTCVNqCGKCVCDSGYQGATC 26
 
Name Accession Description Interval E-value
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 212-406 7.46e-93

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: 289.97  E-value: 7.46e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937871410 212 RYVELFIVVDKERYNMMGRNQTAVREEMIRLANYLDSMYIMLNIRIVLVGLEIWTDRNPINIIGGAGDVLGNFVQWREKF 291
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937871410 292 LITRRRHDSAQLVLKKGFGG-TAGMAFVGTVCSRSHAGGINVFGQITVETFASIVAHELGHNLGMNHDDG-RECFCA-AK 368
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFGGtTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFnGGCKCPpGG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1937871410 369 SCIMNS--GASGSRNFSSCSAEDFEKLTLNKGGSCLLNIP 406
Cdd:pfam01421 161 GCIMNPsaGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 212-404 9.02e-93

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: 289.52  E-value: 9.02e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937871410 212 RYVELFIVVDKERYNMMGRNQTAVREEMIRLANYLDSMYIMLNIRIVLVGLEIWTDRNPINIIGGAGDVLGNFVQWREKF 291
Cdd:cd04269     1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937871410 292 LITRRRHDSAQLVLKKGF-GGTAGMAFVGTVCSRSHAGGINVFGQITVETFASIVAHELGHNLGMNHDDGrECFCAAKSC 370
Cdd:cd04269    81 LLPRKPHDNAQLLTGRDFdGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDG-GCTCGRSTC 159

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1937871410 371 IMNSGAS-GSRNFSSCSAEDFEKLTLNKGGSCLLN 404
Cdd:cd04269   160 IMAPSPSsLTDAFSNCSYEDYQKFLSRGGGQCLLN 194
ACR smart00608
ADAM Cysteine-Rich Domain;
500-636 1.09e-57

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 193.35  E-value: 1.09e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937871410  500 QNGYPCWNSKAYCYNGVCQYYDAQCQVIFGSKAKAAPRDCFIEVNSKGDRFGNCGVSGSNYKTCATGNALCGKLQCENVQ 579
Cdd:smart00608   1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1937871410  580 EMPVFGIVPAIIQTPSRGTKCWGVDFQLGSDvPDPGMVNEGTKCDAGKICRNFQCVN 636
Cdd:smart00608  81 ELPLLGEHATVIYSNIGGLVCWSLDYHLGTD-PDIGMVKDGTKCGPGKVCINGQCVD 136
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 501-605 1.35e-46

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: 161.24  E-value: 1.35e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937871410 501 NGYPCWNSKAYCYNGVCQYYDAQCQVIFGSKAKAAPRDCFIEVNSKGDRFGNCGVSGSNYKTCATGNALCGKLQCENVQE 580
Cdd:pfam08516   1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQCTNVKE 80

                          90       100
                  ....*....|....*....|....*
gi 1937871410 581 MPVFGIVPAIIQTPSRGTKCWGVDF 605
Cdd:pfam08516  81 LPLLGEHATVIYTNINGVTCWGTDY 105
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 44-163 3.20e-43

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: 152.85  E-value: 3.20e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937871410  44 EIVTPWRL--SRERREALRPSSK--QISYVIQAQGKQHIIHLERNTDLLPNDFVVYTYDEEGSLLSDHPNVQSHCHYRGY 119
Cdd:pfam01562   1 EVVIPVRLdpSRRRRSLASESTYldTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1937871410 120 VEGVPNSTVAVSACFGLRGLLHLENASFGIEPLHN----SSHFEHVFY 163
Cdd:pfam01562  81 VEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEKysreEGGHPHVVY 128
Disintegrin pfam00200
Disintegrin;
423-496 5.99e-37

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 133.14  E-value: 5.99e-37
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1937871410 423 DPGEECDCGTPKECELDPCCEGSTCKLKSFAECAYGDCCKDCQFLPGGSMCRGKTSECDVPEYCNGSSQFCPPD 496
Cdd:pfam00200   1 EEGEECDCGSLEECTNDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 423-498 1.42e-35

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: 128.96  E-value: 1.42e-35
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1937871410  423 DPGEECDCGTPKECeLDPCCEGSTCKLKSFAECAYGDCCKDCQFLPGGSMCRGKTSECDVPEYCNGSSQFCPPDVF 498
Cdd:smart00050   1 EEGEECDCGSPKEC-TDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
 732-802 2.68e-06

Proline-rich protein; This family includes several eukaryotic proline-rich proteins.


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 48.50  E-value: 2.68e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1937871410 732 SQMSD--GRNQANASRPPGDPSVSRPPGGPSVSRPPGGPnvsrPPGGPNVSRPPGGPSVSRPPPVHGNRFPVP 802
Cdd:pfam15240  30 SLISEeeGQSQQGGQGPQGPPPGGFPPQPPASDDPPGPP----PPGGPQQPPPQGGKQKPQGPPPQGGPRPPP 98
PHA03378 PHA03378
EBNA-3B; Provisional
 741-805 1.06e-04

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 46.21  E-value: 1.06e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1937871410 741 ANASRPPGDPSVSRPPGGPSVS--RPPGGPNVSRPP-GGPNVSRPP-GGPSVSRPPPVHGNRFPVPTYA 805
Cdd:PHA03378  692 GTMQPPPRAPTPMRPPAAPPGRaqRPAAATGRARPPaAAPGRARPPaAAPGRARPPAAAPGRARPPAAA 760
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
740-792 6.28e-04

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 43.09  E-value: 6.28e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1937871410 740 QANASRPPGDPSVSRPPGGPSVSRPPGGPNVSRPPGGPNVSRPPGGPSVSRPP 792
Cdd:COG5164    41 NTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQGGTRPA 93
EGF_2 pfam07974
EGF-like domain; This family contains EGF domains found in a variety of extracellular proteins.
 650-673 6.78e-03

EGF-like domain; This family contains EGF domains found in a variety of extracellular proteins.


Pssm-ID: 400365  Cd Length: 26  Bit Score: 34.63  E-value: 6.78e-03
                          10        20
                  ....*....|....*....|....*
gi 1937871410 650 CHGHGVCNS-NKNCHCEDGWAPPHC 673
Cdd:pfam07974   2 CSGRGTCVNqCGKCVCDSGYQGATC 26
SAV_2336_NTERM NF041121
SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 ...
 743-805 8.64e-03

SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 (BAC70047.1) whose C-terminal region suggests restriction enzyme activity (PMID: 18456708), and with other proteins with unrelated C-terminal regions. A member protein was also identified in a kanamycin biosynthetic gene cluster (PMID:16766657), while N-terminal regions of two other member proteins were named Trypco1 in a bioinformatic study (PMID:32101166) of predicted bacterial conflict systems.


Pssm-ID: 469044 [Multi-domain]  Cd Length: 473  Bit Score: 39.60  E-value: 8.64e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1937871410 743 ASRPPGDPSVSRPPGGPSVSRPPGGPNVSRPPG-GPNVSRPPGGPSVSRPPPVHGNRFPVPTYA 805
Cdd:NF041121   32 ASQPATPPPPAAPPSPPGDPPEPPAPEPAPLPApYPGSLAPPPPPPPGPAGAAPGAALPVRVPA 95
 
Name Accession Description Interval E-value
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 212-406 7.46e-93

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: 289.97  E-value: 7.46e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937871410 212 RYVELFIVVDKERYNMMGRNQTAVREEMIRLANYLDSMYIMLNIRIVLVGLEIWTDRNPINIIGGAGDVLGNFVQWREKF 291
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937871410 292 LITRRRHDSAQLVLKKGFGG-TAGMAFVGTVCSRSHAGGINVFGQITVETFASIVAHELGHNLGMNHDDG-RECFCA-AK 368
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFGGtTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFnGGCKCPpGG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1937871410 369 SCIMNS--GASGSRNFSSCSAEDFEKLTLNKGGSCLLNIP 406
Cdd:pfam01421 161 GCIMNPsaGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 212-404 9.02e-93

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: 289.52  E-value: 9.02e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937871410 212 RYVELFIVVDKERYNMMGRNQTAVREEMIRLANYLDSMYIMLNIRIVLVGLEIWTDRNPINIIGGAGDVLGNFVQWREKF 291
Cdd:cd04269     1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937871410 292 LITRRRHDSAQLVLKKGF-GGTAGMAFVGTVCSRSHAGGINVFGQITVETFASIVAHELGHNLGMNHDDGrECFCAAKSC 370
Cdd:cd04269    81 LLPRKPHDNAQLLTGRDFdGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDG-GCTCGRSTC 159

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1937871410 371 IMNSGAS-GSRNFSSCSAEDFEKLTLNKGGSCLLN 404
Cdd:cd04269   160 IMAPSPSsLTDAFSNCSYEDYQKFLSRGGGQCLLN 194
ACR smart00608
ADAM Cysteine-Rich Domain;
500-636 1.09e-57

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 193.35  E-value: 1.09e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937871410  500 QNGYPCWNSKAYCYNGVCQYYDAQCQVIFGSKAKAAPRDCFIEVNSKGDRFGNCGVSGSNYKTCATGNALCGKLQCENVQ 579
Cdd:smart00608   1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1937871410  580 EMPVFGIVPAIIQTPSRGTKCWGVDFQLGSDvPDPGMVNEGTKCDAGKICRNFQCVN 636
Cdd:smart00608  81 ELPLLGEHATVIYSNIGGLVCWSLDYHLGTD-PDIGMVKDGTKCGPGKVCINGQCVD 136
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 501-605 1.35e-46

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: 161.24  E-value: 1.35e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937871410 501 NGYPCWNSKAYCYNGVCQYYDAQCQVIFGSKAKAAPRDCFIEVNSKGDRFGNCGVSGSNYKTCATGNALCGKLQCENVQE 580
Cdd:pfam08516   1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQCTNVKE 80

                          90       100
                  ....*....|....*....|....*
gi 1937871410 581 MPVFGIVPAIIQTPSRGTKCWGVDF 605
Cdd:pfam08516  81 LPLLGEHATVIYTNINGVTCWGTDY 105
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 44-163 3.20e-43

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: 152.85  E-value: 3.20e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937871410  44 EIVTPWRL--SRERREALRPSSK--QISYVIQAQGKQHIIHLERNTDLLPNDFVVYTYDEEGSLLSDHPNVQSHCHYRGY 119
Cdd:pfam01562   1 EVVIPVRLdpSRRRRSLASESTYldTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1937871410 120 VEGVPNSTVAVSACFGLRGLLHLENASFGIEPLHN----SSHFEHVFY 163
Cdd:pfam01562  81 VEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEKysreEGGHPHVVY 128
Disintegrin pfam00200
Disintegrin;
423-496 5.99e-37

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 133.14  E-value: 5.99e-37
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1937871410 423 DPGEECDCGTPKECELDPCCEGSTCKLKSFAECAYGDCCKDCQFLPGGSMCRGKTSECDVPEYCNGSSQFCPPD 496
Cdd:pfam00200   1 EEGEECDCGSLEECTNDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 423-498 1.42e-35

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: 128.96  E-value: 1.42e-35
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1937871410  423 DPGEECDCGTPKECeLDPCCEGSTCKLKSFAECAYGDCCKDCQFLPGGSMCRGKTSECDVPEYCNGSSQFCPPDVF 498
Cdd:smart00050   1 EEGEECDCGSPKEC-TDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 212-387 1.69e-29

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: 115.98  E-value: 1.69e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937871410 212 RYVELFIVVDKERYNMMGRNQTAVREEMIRLANYLDSMY----IMLNIRIVLVGLEIWTDRNPINIIG-GAGDVLGNFVQ 286
Cdd:cd04267     1 REIELVVVADHRMVSYFNSDENILQAYITELINIANSIYrstnLRLGIRISLEGLQILKGEQFAPPIDsDASNTLNSFSF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937871410 287 WREKFLItrrRHDSAQLVLKKGF--GGTAGMAFVGTVCSRSHAGGINVFGQITVETfASIVAHELGHNLGMNHDDGRECF 364
Cdd:cd04267    81 WRAEGPI---RHDNAVLLTAQDFieGDILGLAYVGSMCNPYSSVGVVEDTGFTLLT-ALTMAHELGHNLGAEHDGGDELA 156

                         170       180
                  ....*....|....*....|....*...
gi 1937871410 365 C---AAKSCIMNSGASGSRN--FSSCSA 387
Cdd:cd04267   157 FecdGGGNYIMAPVDSGLNSyrFSQCSI 184
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 212-403 3.09e-27

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: 110.02  E-value: 3.09e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937871410 212 RYVELFIVVDKERYNMMGRNQTavrEEMI-RLANYLDSMY----IMLNIRIVLVGLEIWTDRNP-INIIGGAGDVLGNFV 285
Cdd:cd04273     1 RYVETLVVADSKMVEFHHGEDL---EHYIlTLMNIVASLYkdpsLGNSINIVVVRLIVLEDEESgLLISGNAQKSLKSFC 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937871410 286 QWREK---------------FLITRRrhdsaQLVLKKGFGGTAGMAFVGTVCSRSHAGGINvfgQITVETFASIVAHELG 350
Cdd:cd04273    78 RWQKKlnppndsdpehhdhaILLTRQ-----DICRSNGNCDTLGLAPVGGMCSPSRSCSIN---EDTGLSSAFTIAHELG 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1937871410 351 HNLGMNHDD-GREC-FCAAKSCIMNS-GASGSRNF--SSCSAEDFEKLTLNKGGSCLL 403
Cdd:cd04273   150 HVLGMPHDGdGNSCgPEGKDGHIMSPtLGANTGPFtwSKCSRRYLTSFLDTGDGNCLL 207
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 237-358 6.51e-19

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: 83.19  E-value: 6.51e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937871410 237 EEMIRLANYLDSMY-IMLNIRIVLVGLEIWTDRNPINIIGGAGDVLGNFVQWrekfLITRRRH---DSAQLVLKKGFGGT 312
Cdd:pfam13582   1 ARIVSLVNRANTIYeRDLGIRLQLAAIIITTSADTPYTSSDALEILDELQEV----NDTRIGQygyDLGHLFTGRDGGGG 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1937871410 313 AGMAFVGTVCSRSHAGGINVFGQITVETFASIVAHELGHNLGMNHD 358
Cdd:pfam13582  77 GGIAYVGGVCNSGSKFGVNSGSGPVGDTGADTFAHEIGHNFGLNHT 122
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
211-383 1.79e-17

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 81.31  E-value: 1.79e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937871410 211 TRYVELFIVVDKERYNMMGRNqtAVREEMIRLANYLDS-MYIMLNIRIVLVGLEIWTDRNPINIIGG----AGDVLGNFV 285
Cdd:pfam13688   2 TRTVALLVAADCSYVAAFGGD--AAQANIINMVNTASNvYERDFNISLGLVNLTISDSTCPYTPPACstgdSSDRLSEFQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937871410 286 QWREkfLITRRRHDSAQLVLKKGFGGTaGMAFVGTVCSRSHAGGINVFGQITVE-----TFASIVAHELGHNLGMNHD-- 358
Cdd:pfam13688  80 DFSA--WRGTQNDDLAYLFLMTNCSGG-GLAWLGQLCNSGSAGSVSTRVSGNNVvvstaTEWQVFAHEIGHNFGAVHDcd 156

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1937871410 359 ---DGRECFCAAKSC------IMN-SGASGSRNFS 383
Cdd:pfam13688 157 sstSSQCCPPSNSTCpaggryIMNpSSSPNSTDFS 191
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 213-402 1.42e-14

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 73.54  E-value: 1.42e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937871410 213 YVELFIVVDKERYNMMGRNQtAVREEMIRLANYLDSMYIMLN---IRIVLVGLEIWTDRNPINIIGGAGD-------VLG 282
Cdd:cd04272     2 YPELFVVVDYDHQSEFFSNE-QLIRYLAVMVNAANLRYRDLKsprIRLLLVGITISKDPDFEPYIHPINYgyidaaeTLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937871410 283 NFVQW-REK---------FLITRRR-HDSAQLVLKKGfggTAGMAFVGTVCSRSHAGginvFGQITVETFASI--VAHEL 349
Cdd:cd04272    81 NFNEYvKKKrdyfnpdvvFLVTGLDmSTYSGGSLQTG---TGGYAYVGGACTENRVA----MGEDTPGSYYGVytMTHEL 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1937871410 350 GHNLGMNHDDGREC-----FCAAKSC------IMNSGASGSRN--FSSCSAEDFEKLTLNKGGSCL 402
Cdd:cd04272   154 AHLLGAPHDGSPPPswvkgHPGSLDCpwddgyIMSYVVNGERQyrFSQCSQRQIRNVFRRLGASCL 219
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 212-393 1.93e-12

Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major branches, the astacin-like proteases and the adamalysin/reprolysin-like proteases. Both branches have wide phylogenetic distribution, and contain sub-families, which are involved in vertebrate development and disease.


Pssm-ID: 238124 [Multi-domain]  Cd Length: 167  Bit Score: 66.01  E-value: 1.93e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937871410 212 RYVELFIVVDKERYNmmgrnQTAVREEMIRLANYLDSMY-IMLNIRIVLVGLEIWTDRNpiniiggagdvlgnfvqwreK 290
Cdd:cd00203     1 KVIPYVVVADDRDVE-----EENLSAQIQSLILIAMQIWrDYLNIRFVLVGVEIDKADI--------------------A 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937871410 291 FLITRRRHDsaqlvlkkgfGGTAGMAFVGTVCSRSHAGGINVFGQITVETFASIVAHELGHNLGMNHDDGRECFCA---- 366
Cdd:cd00203    56 ILVTRQDFD----------GGTGGWAYLGRVCDSLRGVGVLQDNQSGTKEGAQTIAHELGHALGFYHDHDRKDRDDypti 125

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1937871410 367 ---------AKSCIMNSGAS-----GSRNFSSCSAEDFEKL 393
Cdd:cd00203   126 ddtlnaeddDYYSVMSYTKGsfsdgQRKDFSQCDIDQINKL 166
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 234-386 2.73e-09

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: 57.64  E-value: 2.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937871410 234 AVREEMIRLANYLDSMYIM--LNIRIVLVGLEIWTDRNPINIIGGAGDVLGNFVQWREKFL---ITRRRHDSAQLVLKKG 308
Cdd:pfam13574   2 NVTENLVNVVNRVNQIYEPddININGGLVNPGEIPATTSASDSGNNYCNSPTTIVRRLNFLsqwRGEQDYCLAHLVTMGT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937871410 309 F-GGTAGMAFVGTVC-----SRSHAGGINV---FGQITVETFA-SIVAHELGHNLGMNHDDGRECFC--------AAKSC 370
Cdd:pfam13574  82 FsGGELGLAYVGQICqkgasSPKTNTGLSTttnYGSFNYPTQEwDVVAHEVGHNFGATHDCDGSQYAssgcernaATSVC 161

                         170       180
                  ....*....|....*....|...
gi 1937871410 371 ------IMN-SGASGSRNFSSCS 386
Cdd:pfam13574 162 sangsfIMNpASKSNNDLFSPCS 184
Reprolysin_4 pfam13583
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 212-390 4.77e-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: 404471  Cd Length: 203  Bit Score: 54.16  E-value: 4.77e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937871410 212 RYVELFIVVDKERYNMMGrNQTAVREEMIRLANYLDSMY-IMLNIRIVLVGLE--IWTDRNP----INIIGGAgdvLGNF 284
Cdd:pfam13583   3 RVYRVAVATDCTYSASFG-SVDELRANINATVTTANEVYgRDFNVSLALISDRdvIYTDSSTdsfnADCSGGD---LGNW 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937871410 285 VQWREKFLITRRRHDSAQLVLKKG-FGGTAGMAFVGTVCSRSH--AGGiNVFGQITVETfaSIVAHELGHNLGMNHDDGR 361
Cdd:pfam13583  79 RLATLTSWRDSLNYDLAYLTLMTGpSGQNVGVAWVGALCSSARqnAKA-SGVARSRDEW--DIFAHEIGHTFGAVHDCSS 155

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1937871410 362 EC------FCAAK-SCIMNSGASGSR-NFSSCSAEDF 390
Cdd:pfam13583 156 QGeglsssTEDGSgQTIMSYASTASQtAFSPCTIRNI 192
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
 732-802 2.68e-06

Proline-rich protein; This family includes several eukaryotic proline-rich proteins.


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 48.50  E-value: 2.68e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1937871410 732 SQMSD--GRNQANASRPPGDPSVSRPPGGPSVSRPPGGPnvsrPPGGPNVSRPPGGPSVSRPPPVHGNRFPVP 802
Cdd:pfam15240  30 SLISEeeGQSQQGGQGPQGPPPGGFPPQPPASDDPPGPP----PPGGPQQPPPQGGKQKPQGPPPQGGPRPPP 98
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
 216-401 1.57e-05

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: 47.37  E-value: 1.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937871410 216 LFIVVDKERYNMMGRNQT-AVREEMIRLANYLDSMY--------IMLNIRIVLVGLEIWTDRNPINiiGGAGDVLGNFVQ 286
Cdd:cd04270     5 LLLVADHRFYKYMGRGEEeTTINYLISHIDRVDDIYrntdwdggGFKGIGFQIKRIRIHTTPDEVD--PGNKFYNKSFPN 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937871410 287 W-REKFLITRRRHDS------AQLVLKKGF-GGTAGMAFVGTVCSRSHaGGI---------------NVfGQITVETFAS 343
Cdd:cd04270    83 WgVEKFLVKLLLEQFsddvclAHLFTYRDFdMGTLGLAYVGSPRDNSA-GGIcekayyysngkkkylNT-GLTTTVNYGK 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1937871410 344 ---------IVAHELGHNLGMNHD-DGRECFCAAK---SCIMNSGA-SGS----RNFSSCSAEDFEKLTLNKGGSC 401
Cdd:cd04270   161 rvptkesdlVTAHELGHNFGSPHDpDIAECAPGESqggNYIMYARAtSGDkennKKFSPCSKKSISKVLEVKSNSC 236
Drf_FH1 pfam06346
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs) ...
 747-794 1.64e-05

Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs). It consists of low complexity repeats of around 12 residues.


Pssm-ID: 461881 [Multi-domain]  Cd Length: 157  Bit Score: 45.63  E-value: 1.64e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1937871410 747 PGDPSVSRPP----GGPSVSRPP----GGPNVSRP---PGGPNVSRPPGGPSVSRPPPV 794
Cdd:pfam06346  88 PGGAGIPPPPpplpGGAGVPPPPpplpGGPGIPPPppfPGGPGIPPPPPGMGMPPPPPF 146
ZnMc_ADAM_fungal cd04271
Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A ...
 281-386 1.98e-05

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: 46.65  E-value: 1.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937871410 281 LGNFVQWREKflitRRRHDSAQLVLKKGF--GGTAGMAFVGTVCSRSHAG-------GINVFGQITVETfaSIVAHELGH 351
Cdd:cd04271    82 LSIFSQWRGQ----QPDDGNAFWTLMTACpsGSEVGVAWLGQLCRTGASDqgnetvaGTNVVVRTSNEW--QVFAHEIGH 155

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1937871410 352 NLGMNHD----------DGRECFC--AAKSC------IMN-SGASGSRNFSSCS 386
Cdd:cd04271   156 TFGAVHDctsgtcsdgsVGSQQCCplSTSTCdangqyIMNpSSSSGITEFSPCT 209
Drf_FH1 pfam06346
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs) ...
 747-802 4.16e-05

Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs). It consists of low complexity repeats of around 12 residues.


Pssm-ID: 461881 [Multi-domain]  Cd Length: 157  Bit Score: 44.48  E-value: 4.16e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937871410 747 PGDPSVSRPP---GGPSVSRPP----GGPNVSRPP----GGPNVSRP---PGGPSVSRPPPVHGNRFPVP 802
Cdd:pfam06346  76 PGSTGIPPPPplpGGAGIPPPPpplpGGAGVPPPPpplpGGPGIPPPppfPGGPGIPPPPPGMGMPPPPP 145
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
 740-797 7.08e-05

Proline-rich protein; This family includes several eukaryotic proline-rich proteins.


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 44.26  E-value: 7.08e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1937871410 740 QANASRPPGDPSVSRPPGGPSVSRPPGGPNVSRPPGGPNVSRPPGGPSVSRPPPVHGN 797
Cdd:pfam15240  91 QGGPRPPPGKPQGPPPQGGNQQQGPPPPGKPQGPPPQGGGPPPQGGNQQGPPPPPPGN 148
PHA03378 PHA03378
EBNA-3B; Provisional
 741-805 1.06e-04

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 46.21  E-value: 1.06e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1937871410 741 ANASRPPGDPSVSRPPGGPSVS--RPPGGPNVSRPP-GGPNVSRPP-GGPSVSRPPPVHGNRFPVPTYA 805
Cdd:PHA03378  692 GTMQPPPRAPTPMRPPAAPPGRaqRPAAATGRARPPaAAPGRARPPaAAPGRARPPAAAPGRARPPAAA 760
PHA03378 PHA03378
EBNA-3B; Provisional
 745-805 3.22e-04

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 44.67  E-value: 3.22e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1937871410 745 RPPGDPSVS--RPPGGPSVSRPP-GGPNVSRPP-GGPNVSRPP-GGPSVSRPPPVHGNRFPVPTYA 805
Cdd:PHA03378  705 RPPAAPPGRaqRPAAATGRARPPaAAPGRARPPaAAPGRARPPaAAPGRARPPAAAPGRARPPAAA 770
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
740-792 6.28e-04

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 43.09  E-value: 6.28e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1937871410 740 QANASRPPGDPSVSRPPGGPSVSRPPGGPNVSRPPGGPNVSRPPGGPSVSRPP 792
Cdd:COG5164    41 NTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQGGTRPA 93
Drf_FH1 pfam06346
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs) ...
 736-796 6.75e-04

Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs). It consists of low complexity repeats of around 12 residues.


Pssm-ID: 461881 [Multi-domain]  Cd Length: 157  Bit Score: 41.01  E-value: 6.75e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1937871410 736 DGRNQANASRPPGDPSVSRPPGGPSVSRP--PGGPNVSRPP---GGPNVSRPP---GGPSVSRPPPVHG 796
Cdd:pfam06346   9 DSSTIPLPPGACIPTPPPLPGGGGPPPPPplPGSAAIPPPPplpGGTSIPPPPplpGAASIPPPPPLPG 77
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 287-357 7.42e-04

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: 40.94  E-value: 7.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937871410 287 WREKFLIT---RRRHDSAQL---VLKKGFGGTAGMAFVGTVcSRSHAGGI--------NVFGQITVETFASIVAHELGHN 352
Cdd:cd04268    27 WNKAFAIGfknANDVDPADIrysVIRWIPYNDGTWSYGPSQ-VDPLTGEIllarvylySSFVEYSGARLRNTAEHELGHA 105


                  ....*
gi 1937871410 353 LGMNH 357
Cdd:cd04268   106 LGLRH 110
PHA03378 PHA03378
EBNA-3B; Provisional
 728-803 1.10e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 42.75  E-value: 1.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937871410 728 RKKRSQMSDGRNQ------ANASRPPGDPSVSRPP-GGPSVSRPP-GGPNVSRPP----GGPNVSRPPGGPSVSRPPPVH 795
Cdd:PHA03378  713 RAQRPAAATGRARppaaapGRARPPAAAPGRARPPaAAPGRARPPaAAPGRARPPaaapGAPTPQPPPQAPPAPQQRPRG 792


                  ....*...
gi 1937871410 796 GnrfPVPT 803
Cdd:PHA03378  793 A---PTPQ 797
PHA03378 PHA03378
EBNA-3B; Provisional
 728-794 2.22e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 41.59  E-value: 2.22e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1937871410 728 RKKRSQMSDGRnqanASRPPGDPSVSRPP-GGPSVSRP----PGGPNVSRPPGGPNVS--RPPGGPSVSRPPPV 794
Cdd:PHA03378  733 RARPPAAAPGR----ARPPAAAPGRARPPaAAPGRARPpaaaPGAPTPQPPPQAPPAPqqRPRGAPTPQPPPQA 802
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 743-807 3.19e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 41.29  E-value: 3.19e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1937871410 743 ASRPPGdPSVSRPPGGPSVSRPPGGPNVSRPPGGPNvSRPPGGPSVSRPPPVHGN-RFPVPTYAIK 807
Cdd:pfam03154 457 PSQSPF-PQHPFVPGGPPPITPPSGPPTSTSSAMPG-IQPPSSASVSSSGPVPAAvSCPLPPVQIK 520
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
 345-392 3.55e-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: 3.55e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1937871410 345 VAHELGHNLGMNHddgrecfCAAKSCIMnsgasgsrNFSSCSAEDFEK 392
Cdd:cd11375   127 AVHELGHLFGLDH-------CPYYACVM--------NFSNSLEETDRK 159
PHA03247 PHA03247
large tegument protein UL36; Provisional
 724-805 4.23e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.08  E-value: 4.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937871410  724 RKTFRKKRSQMSDGRNQANASRP----PGDPSVSRPPGGP-SVSRPPGGPNVSRPPGGPNVSRPPggPSVSRPPPVHGNR 798
Cdd:PHA03247   385 RRSARHAATPFARGPGGDDQTRPaapvPASVPTPAPTPVPaSAPPPPATPLPSAEPGSDDGPAPP--PERQPPAPATEPA 462


                   ....*..
gi 1937871410  799 FPVPTYA 805
Cdd:PHA03247   463 PDDPDDA 469
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 742-802 5.41e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 40.52  E-value: 5.41e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1937871410 742 NASRPPGDPSVSRPPGGPSVSRPPGGPNVSrPPGGPNVSRPPGGPSVSRPP--------PVHGNRFPVP 802
Cdd:pfam03154 178 SGAASPPSPPPPGTTQAATAGPTPSAPSVP-PQGSPATSQPPNQTQSTAAPhtliqqtpTLHPQRLPSP 245
EGF_2 pfam07974
EGF-like domain; This family contains EGF domains found in a variety of extracellular proteins.
 650-673 6.78e-03

EGF-like domain; This family contains EGF domains found in a variety of extracellular proteins.


Pssm-ID: 400365  Cd Length: 26  Bit Score: 34.63  E-value: 6.78e-03
                          10        20
                  ....*....|....*....|....*
gi 1937871410 650 CHGHGVCNS-NKNCHCEDGWAPPHC 673
Cdd:pfam07974   2 CSGRGTCVNqCGKCVCDSGYQGATC 26
SAV_2336_NTERM NF041121
SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 ...
 743-805 8.64e-03

SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 (BAC70047.1) whose C-terminal region suggests restriction enzyme activity (PMID: 18456708), and with other proteins with unrelated C-terminal regions. A member protein was also identified in a kanamycin biosynthetic gene cluster (PMID:16766657), while N-terminal regions of two other member proteins were named Trypco1 in a bioinformatic study (PMID:32101166) of predicted bacterial conflict systems.


Pssm-ID: 469044 [Multi-domain]  Cd Length: 473  Bit Score: 39.60  E-value: 8.64e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1937871410 743 ASRPPGDPSVSRPPGGPSVSRPPGGPNVSRPPG-GPNVSRPPGGPSVSRPPPVHGNRFPVPTYA 805
Cdd:NF041121   32 ASQPATPPPPAAPPSPPGDPPEPPAPEPAPLPApYPGSLAPPPPPPPGPAGAAPGAALPVRVPA 95
PHA03378 PHA03378
EBNA-3B; Provisional
 733-793 9.16e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 39.67  E-value: 9.16e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937871410 733 QMSDGRNQANASRPPGDPSVSRPPGGPSVSRPPGGPNVSRPPG-GPNVSRPPGGPSVSRPPP 793
Cdd:PHA03378  656 QVEITPYKPTWTQIGHIPYQPSPTGANTMLPIQWAPGTMQPPPrAPTPMRPPAAPPGRAQRP 717
 
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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