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Conserved domains on  [gi|160358787|ref|NP_031430|]
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disintegrin and metalloproteinase domain-containing protein 9 isoform 2 precursor [Mus musculus]

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 1.57e-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: 291.90  E-value: 1.57e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358787  212 RYVELFIVVDKERYDMMGRNQTAVREEMIRLANYLDSMYIMLNIRIVLVGLEIWTDRNPINIIGGAGDVLGNFVQWREKF 291
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358787  292 LITRWRHDSAQLVLKKGFGG-TAGMAFVGTVCSRSHAGGINVFGQITVETFASIVAHELGHNLGMNHDDG-RECFCG-AK 368
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFGGtTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFnGGCKCPpGG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 160358787  369 SCIMNS--GASGSRNFSSCSAEDFEKLTLNKGGSCLLNIP 406
Cdd:pfam01421 161 GCIMNPsaGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ACR smart00608
ADAM Cysteine-Rich Domain;
500-636 4.06e-59

ADAM Cysteine-Rich Domain;


:

Pssm-ID: 214743  Cd Length: 137  Bit Score: 197.58  E-value: 4.06e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358787   500 QNGYPCQNSKAYCYNGMCQYYDAQCQVIFGSKAKAAPRDCFIEVNSKGDRFGNCGFSGSEYKKCATGNALCGKLQCENVQ 579
Cdd:smart00608   1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 160358787   580 DMPVFGIVPAIIQTPSRGTKCWGVDFQLGSDvPDPGMVNEGTKCDAGKICRNFQCVN 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 1.26e-42

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: 150.93  E-value: 1.26e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358787   44 EIITPWRLT--RERREALGPSSQ--QISYVIQAQGKQHIIHLERNTDLLPNDFVVYTYDKEGSLLSDHPNVQSHCHYRGY 119
Cdd:pfam01562   1 EVVIPVRLDpsRRRRSLASESTYldTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 160358787  120 VEGVQNSAVAVSACFGLRGLLHLENASFGIEPLHN----SSHFEHIFY 163
Cdd:pfam01562  81 VEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEKysreEGGHPHVVY 128
Disintegrin pfam00200
Disintegrin;
423-496 1.37e-36

Disintegrin;


:

Pssm-ID: 459709  Cd Length: 74  Bit Score: 131.98  E-value: 1.37e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 160358787  423 DPGEECDCGTAKECEVDPCCEGSTCKLKSFAECAYGDCCKDCQFLPGGSMCRGKTSECDVPEYCNGSSQFCPPD 496
Cdd:pfam00200   1 EEGEECDCGSLEECTNDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
Drf_FH1 pfam06346
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs) ...
 747-802 1.24e-09

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: 57.57  E-value: 1.24e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358787  747 PGDPSISRPP---GGPNVSRPP----GGPGVSRPP----GGPGVSRP---PGGPGVSRPPPGHGNRFPVP 802
Cdd:pfam06346  76 PGSTGIPPPPplpGGAGIPPPPpplpGGAGVPPPPpplpGGPGIPPPppfPGGPGIPPPPPGMGMPPPPP 145
EGF_2 pfam07974
EGF-like domain; This family contains EGF domains found in a variety of extracellular proteins.
 650-673 7.85e-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: 7.85e-03
                          10        20
                  ....*....|....*....|....*
gi 160358787  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 1.57e-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: 291.90  E-value: 1.57e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358787  212 RYVELFIVVDKERYDMMGRNQTAVREEMIRLANYLDSMYIMLNIRIVLVGLEIWTDRNPINIIGGAGDVLGNFVQWREKF 291
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358787  292 LITRWRHDSAQLVLKKGFGG-TAGMAFVGTVCSRSHAGGINVFGQITVETFASIVAHELGHNLGMNHDDG-RECFCG-AK 368
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFGGtTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFnGGCKCPpGG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 160358787  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 5.86e-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: 290.29  E-value: 5.86e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358787 212 RYVELFIVVDKERYDMMGRNQTAVREEMIRLANYLDSMYIMLNIRIVLVGLEIWTDRNPINIIGGAGDVLGNFVQWREKF 291
Cdd:cd04269    1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358787 292 LITRWRHDSAQLVLKKGF-GGTAGMAFVGTVCSRSHAGGINVFGQITVETFASIVAHELGHNLGMNHDDGrECFCGAKSC 370
Cdd:cd04269   81 LLPRKPHDNAQLLTGRDFdGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDG-GCTCGRSTC 159

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 160358787 371 IMNSGAS-GSRNFSSCSAEDFEKLTLNKGGSCLLN 404
Cdd:cd04269  160 IMAPSPSsLTDAFSNCSYEDYQKFLSRGGGQCLLN 194
ACR smart00608
ADAM Cysteine-Rich Domain;
500-636 4.06e-59

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 197.58  E-value: 4.06e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358787   500 QNGYPCQNSKAYCYNGMCQYYDAQCQVIFGSKAKAAPRDCFIEVNSKGDRFGNCGFSGSEYKKCATGNALCGKLQCENVQ 579
Cdd:smart00608   1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 160358787   580 DMPVFGIVPAIIQTPSRGTKCWGVDFQLGSDvPDPGMVNEGTKCDAGKICRNFQCVN 636
Cdd:smart00608  81 ELPLLGEHATVIYSNIGGLVCWSLDYHLGTD-PDIGMVKDGTKCGPGKVCINGQCVD 136
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 501-605 1.14e-47

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: 164.33  E-value: 1.14e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358787  501 NGYPCQNSKAYCYNGMCQYYDAQCQVIFGSKAKAAPRDCFIEVNSKGDRFGNCGFSGSEYKKCATGNALCGKLQCENVQD 580
Cdd:pfam08516   1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQCTNVKE 80

                          90       100
                  ....*....|....*....|....*
gi 160358787  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 1.26e-42

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: 150.93  E-value: 1.26e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358787   44 EIITPWRLT--RERREALGPSSQ--QISYVIQAQGKQHIIHLERNTDLLPNDFVVYTYDKEGSLLSDHPNVQSHCHYRGY 119
Cdd:pfam01562   1 EVVIPVRLDpsRRRRSLASESTYldTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 160358787  120 VEGVQNSAVAVSACFGLRGLLHLENASFGIEPLHN----SSHFEHIFY 163
Cdd:pfam01562  81 VEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEKysreEGGHPHVVY 128
Disintegrin pfam00200
Disintegrin;
423-496 1.37e-36

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 131.98  E-value: 1.37e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 160358787  423 DPGEECDCGTAKECEVDPCCEGSTCKLKSFAECAYGDCCKDCQFLPGGSMCRGKTSECDVPEYCNGSSQFCPPD 496
Cdd:pfam00200   1 EEGEECDCGSLEECTNDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 423-498 2.95e-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: 128.19  E-value: 2.95e-35
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 160358787   423 DPGEECDCGTAKECeVDPCCEGSTCKLKSFAECAYGDCCKDCQFLPGGSMCRGKTSECDVPEYCNGSSQFCPPDVF 498
Cdd:smart00050   1 EEGEECDCGSPKEC-TDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
Drf_FH1 pfam06346
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs) ...
 747-802 1.24e-09

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: 57.57  E-value: 1.24e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358787  747 PGDPSISRPP---GGPNVSRPP----GGPGVSRPP----GGPGVSRP---PGGPGVSRPPPGHGNRFPVP 802
Cdd:pfam06346  76 PGSTGIPPPPplpGGAGIPPPPpplpGGAGVPPPPpplpGGPGIPPPppfPGGPGIPPPPPGMGMPPPPP 145
PHA03378 PHA03378
EBNA-3B; Provisional
 748-810 6.66e-06

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 50.07  E-value: 6.66e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 160358787 748 GDPSISRPP-GGPNVSRPP-GGPGVSRPP-GGPGVSRPP-GGPGVSRPPPGHGNRFPVPTYAAKQPA 810
Cdd:PHA03378 709 APPGRAQRPaAATGRARPPaAAPGRARPPaAAPGRARPPaAAPGRARPPAAAPGRARPPAAAPGAPT 775
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
742-811 9.00e-06

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 49.26  E-value: 9.00e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358787 742 NVSRQPGDPSISRPPGGPNVSRPPGGPGVSRPPGGPGVSRPPGGPGVSRPPPGHGNRFPVPTYAAKQPAQ 811
Cdd:COG5164   16 GVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQ 85
EGF_2 pfam07974
EGF-like domain; This family contains EGF domains found in a variety of extracellular proteins.
 650-673 7.85e-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: 7.85e-03
                          10        20
                  ....*....|....*....|....*
gi 160358787  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 1.57e-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: 291.90  E-value: 1.57e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358787  212 RYVELFIVVDKERYDMMGRNQTAVREEMIRLANYLDSMYIMLNIRIVLVGLEIWTDRNPINIIGGAGDVLGNFVQWREKF 291
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358787  292 LITRWRHDSAQLVLKKGFGG-TAGMAFVGTVCSRSHAGGINVFGQITVETFASIVAHELGHNLGMNHDDG-RECFCG-AK 368
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFGGtTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFnGGCKCPpGG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 160358787  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 5.86e-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: 290.29  E-value: 5.86e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358787 212 RYVELFIVVDKERYDMMGRNQTAVREEMIRLANYLDSMYIMLNIRIVLVGLEIWTDRNPINIIGGAGDVLGNFVQWREKF 291
Cdd:cd04269    1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358787 292 LITRWRHDSAQLVLKKGF-GGTAGMAFVGTVCSRSHAGGINVFGQITVETFASIVAHELGHNLGMNHDDGrECFCGAKSC 370
Cdd:cd04269   81 LLPRKPHDNAQLLTGRDFdGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDG-GCTCGRSTC 159

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 160358787 371 IMNSGAS-GSRNFSSCSAEDFEKLTLNKGGSCLLN 404
Cdd:cd04269  160 IMAPSPSsLTDAFSNCSYEDYQKFLSRGGGQCLLN 194
ACR smart00608
ADAM Cysteine-Rich Domain;
500-636 4.06e-59

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 197.58  E-value: 4.06e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358787   500 QNGYPCQNSKAYCYNGMCQYYDAQCQVIFGSKAKAAPRDCFIEVNSKGDRFGNCGFSGSEYKKCATGNALCGKLQCENVQ 579
Cdd:smart00608   1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 160358787   580 DMPVFGIVPAIIQTPSRGTKCWGVDFQLGSDvPDPGMVNEGTKCDAGKICRNFQCVN 636
Cdd:smart00608  81 ELPLLGEHATVIYSNIGGLVCWSLDYHLGTD-PDIGMVKDGTKCGPGKVCINGQCVD 136
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 501-605 1.14e-47

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: 164.33  E-value: 1.14e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358787  501 NGYPCQNSKAYCYNGMCQYYDAQCQVIFGSKAKAAPRDCFIEVNSKGDRFGNCGFSGSEYKKCATGNALCGKLQCENVQD 580
Cdd:pfam08516   1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQCTNVKE 80

                          90       100
                  ....*....|....*....|....*
gi 160358787  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 1.26e-42

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: 150.93  E-value: 1.26e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358787   44 EIITPWRLT--RERREALGPSSQ--QISYVIQAQGKQHIIHLERNTDLLPNDFVVYTYDKEGSLLSDHPNVQSHCHYRGY 119
Cdd:pfam01562   1 EVVIPVRLDpsRRRRSLASESTYldTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 160358787  120 VEGVQNSAVAVSACFGLRGLLHLENASFGIEPLHN----SSHFEHIFY 163
Cdd:pfam01562  81 VEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEKysreEGGHPHVVY 128
Disintegrin pfam00200
Disintegrin;
423-496 1.37e-36

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 131.98  E-value: 1.37e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 160358787  423 DPGEECDCGTAKECEVDPCCEGSTCKLKSFAECAYGDCCKDCQFLPGGSMCRGKTSECDVPEYCNGSSQFCPPD 496
Cdd:pfam00200   1 EEGEECDCGSLEECTNDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 423-498 2.95e-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: 128.19  E-value: 2.95e-35
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 160358787   423 DPGEECDCGTAKECeVDPCCEGSTCKLKSFAECAYGDCCKDCQFLPGGSMCRGKTSECDVPEYCNGSSQFCPPDVF 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 9.95e-30

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: 116.75  E-value: 9.95e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358787 212 RYVELFIVVDKERYDMMGRNQTAVREEMIRLANYLDSMY----IMLNIRIVLVGLEIWTDRNPINIIG-GAGDVLGNFVQ 286
Cdd:cd04267    1 REIELVVVADHRMVSYFNSDENILQAYITELINIANSIYrstnLRLGIRISLEGLQILKGEQFAPPIDsDASNTLNSFSF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358787 287 WREKFLItrwRHDSAQLVLKKGF--GGTAGMAFVGTVCSRSHAGGINVFGQITVETfASIVAHELGHNLGMNHDDGRECF 364
Cdd:cd04267   81 WRAEGPI---RHDNAVLLTAQDFieGDILGLAYVGSMCNPYSSVGVVEDTGFTLLT-ALTMAHELGHNLGAEHDGGDELA 156

                        170       180
                 ....*....|....*....|....*...
gi 160358787 365 C---GAKSCIMNSGASGSRN--FSSCSA 387
Cdd:cd04267  157 FecdGGGNYIMAPVDSGLNSyrFSQCSI 184
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 212-403 1.81e-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: 110.79  E-value: 1.81e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358787 212 RYVELFIVVDKERYDMMGRNQTavrEEMI-RLANYLDSMY----IMLNIRIVLVGLEIWTDRNP-INIIGGAGDVLGNFV 285
Cdd:cd04273    1 RYVETLVVADSKMVEFHHGEDL---EHYIlTLMNIVASLYkdpsLGNSINIVVVRLIVLEDEESgLLISGNAQKSLKSFC 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358787 286 QWREK---------------FLITRwrHDsaqLVLKKGFGGTAGMAFVGTVCSRSHAGGINvfgQITVETFASIVAHELG 350
Cdd:cd04273   78 RWQKKlnppndsdpehhdhaILLTR--QD---ICRSNGNCDTLGLAPVGGMCSPSRSCSIN---EDTGLSSAFTIAHELG 149

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 160358787 351 HNLGMNHDD-GREC-FCGAKSCIMNS-GASGSRNF--SSCSAEDFEKLTLNKGGSCLL 403
Cdd:cd04273  150 HVLGMPHDGdGNSCgPEGKDGHIMSPtLGANTGPFtwSKCSRRYLTSFLDTGDGNCLL 207
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
211-383 1.33e-18

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 84.78  E-value: 1.33e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358787  211 TRYVELFIVVDKERYDMMGRNqtAVREEMIRLANYLDS-MYIMLNIRIVLVGLEIWTDRNPINIIGG----AGDVLGNFV 285
Cdd:pfam13688   2 TRTVALLVAADCSYVAAFGGD--AAQANIINMVNTASNvYERDFNISLGLVNLTISDSTCPYTPPACstgdSSDRLSEFQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358787  286 QWREkfLITRWRHDSAQLVLKKGFGGTaGMAFVGTVCSRSHAGGINVFGQITVE-----TFASIVAHELGHNLGMNHD-- 358
Cdd:pfam13688  80 DFSA--WRGTQNDDLAYLFLMTNCSGG-GLAWLGQLCNSGSAGSVSTRVSGNNVvvstaTEWQVFAHEIGHNFGAVHDcd 156

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 160358787  359 ---DGRECFCGAKSC------IMN-SGASGSRNFS 383
Cdd:pfam13688 157 sstSSQCCPPSNSTCpaggryIMNpSSSPNSTDFS 191
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 237-358 1.47e-18

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: 82.42  E-value: 1.47e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358787  237 EEMIRLANYLDSMY-IMLNIRIVLVGLEIWTDRNPINIIGGAGDVLGNFVQWrekfLITRWRH---DSAQLVLKKGFGGT 312
Cdd:pfam13582   1 ARIVSLVNRANTIYeRDLGIRLQLAAIIITTSADTPYTSSDALEILDELQEV----NDTRIGQygyDLGHLFTGRDGGGG 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 160358787  313 AGMAFVGTVCSRSHAGGINVFGQITVETFASIVAHELGHNLGMNHD 358
Cdd:pfam13582  77 GGIAYVGGVCNSGSKFGVNSGSGPVGDTGADTFAHEIGHNFGLNHT 122
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 213-402 5.50e-15

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 74.70  E-value: 5.50e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358787 213 YVELFIVVDKERYDMMGRNQtAVREEMIRLANYLDSMYIMLN---IRIVLVGLEIWTDRNPINIIGGAGD-------VLG 282
Cdd:cd04272    2 YPELFVVVDYDHQSEFFSNE-QLIRYLAVMVNAANLRYRDLKsprIRLLLVGITISKDPDFEPYIHPINYgyidaaeTLE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358787 283 NFVQW-REK---------FLITR-----WRHDSAQlvlkkgfGGTAGMAFVGTVCSRSHAGginvFGQITVETFASI--V 345
Cdd:cd04272   81 NFNEYvKKKrdyfnpdvvFLVTGldmstYSGGSLQ-------TGTGGYAYVGGACTENRVA----MGEDTPGSYYGVytM 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358787 346 AHELGHNLGMNHDDGREC-----FCGAKSC------IMNSGASGSRN--FSSCSAEDFEKLTLNKGGSCL 402
Cdd:cd04272  150 THELAHLLGAPHDGSPPPswvkgHPGSLDCpwddgyIMSYVVNGERQyrFSQCSQRQIRNVFRRLGASCL 219
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 212-393 6.81e-14

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: 70.24  E-value: 6.81e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358787 212 RYVELFIVVDKERYDmmgrnQTAVREEMIRLANYLDSMY-IMLNIRIVLVGLEIWTDRNpiniiggagdvlgnfvqwreK 290
Cdd:cd00203    1 KVIPYVVVADDRDVE-----EENLSAQIQSLILIAMQIWrDYLNIRFVLVGVEIDKADI--------------------A 55

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358787 291 FLITRWRHDsaqlvlkkgfGGTAGMAFVGTVCSRSHAGGINVFGQITVETFASIVAHELGHNLGMNHDDGRECFCG---- 366
Cdd:cd00203   56 ILVTRQDFD----------GGTGGWAYLGRVCDSLRGVGVLQDNQSGTKEGAQTIAHELGHALGFYHDHDRKDRDDypti 125

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 160358787 367 ---------AKSCIMNSGAS-----GSRNFSSCSAEDFEKL 393
Cdd:cd00203  126 ddtlnaeddDYYSVMSYTKGsfsdgQRKDFSQCDIDQINKL 166
Drf_FH1 pfam06346
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs) ...
 747-802 1.24e-09

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: 57.57  E-value: 1.24e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358787  747 PGDPSISRPP---GGPNVSRPP----GGPGVSRPP----GGPGVSRP---PGGPGVSRPPPGHGNRFPVP 802
Cdd:pfam06346  76 PGSTGIPPPPplpGGAGIPPPPpplpGGAGVPPPPpplpGGPGIPPPppfPGGPGIPPPPPGMGMPPPPP 145
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 234-386 3.05e-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: 3.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358787  234 AVREEMIRLANYLDSMYIM--LNIRIVLVGLEIWTDRNPINIIGGAGDVLGNFVQWREKFLiTRWR----HDSAQLVLKK 307
Cdd:pfam13574   2 NVTENLVNVVNRVNQIYEPddININGGLVNPGEIPATTSASDSGNNYCNSPTTIVRRLNFL-SQWRgeqdYCLAHLVTMG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358787  308 GF-GGTAGMAFVGTVC-----SRSHAGGINV---FGQITVETFA-SIVAHELGHNLGMNHDDGRECFC--------GAKS 369
Cdd:pfam13574  81 TFsGGELGLAYVGQICqkgasSPKTNTGLSTttnYGSFNYPTQEwDVVAHEVGHNFGATHDCDGSQYAssgcernaATSV 160

                         170       180
                  ....*....|....*....|....
gi 160358787  370 C------IMN-SGASGSRNFSSCS 386
Cdd:pfam13574 161 CsangsfIMNpASKSNNDLFSPCS 184
Reprolysin_4 pfam13583
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 212-390 6.20e-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: 404471  Cd Length: 203  Bit Score: 56.86  E-value: 6.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358787  212 RYVELFIVVDKERYDMMGrNQTAVREEMIRLANYLDSMY-IMLNIRIVLVGLE--IWTDRNP----INIIGGAgdvLGNF 284
Cdd:pfam13583   3 RVYRVAVATDCTYSASFG-SVDELRANINATVTTANEVYgRDFNVSLALISDRdvIYTDSSTdsfnADCSGGD---LGNW 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358787  285 VQWRekflITRWR----HDSAQLVLKKG-FGGTAGMAFVGTVCSRSH--AGGiNVFGQITVETfaSIVAHELGHNLGMNH 357
Cdd:pfam13583  79 RLAT----LTSWRdslnYDLAYLTLMTGpSGQNVGVAWVGALCSSARqnAKA-SGVARSRDEW--DIFAHEIGHTFGAVH 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 160358787  358 DDGRECfCGAK--------SCIMNSGASGSR-NFSSCSAEDF 390
Cdd:pfam13583 152 DCSSQG-EGLSsstedgsgQTIMSYASTASQtAFSPCTIRNI 192
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
 216-401 2.24e-06

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: 49.68  E-value: 2.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358787 216 LFIVVDKERYDMMGRNQT-AVREEMIRLANYLDSMY--------IMLNIRIVLVGLEIWTDRNPINiiGGAGDVLGNFVQ 286
Cdd:cd04270    5 LLLVADHRFYKYMGRGEEeTTINYLISHIDRVDDIYrntdwdggGFKGIGFQIKRIRIHTTPDEVD--PGNKFYNKSFPN 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358787 287 W-REKFLITRWRHDS------AQLVLKKGF-GGTAGMAFVGTVCSRSHaGGI---------------NVfGQITVETFAS 343
Cdd:cd04270   83 WgVEKFLVKLLLEQFsddvclAHLFTYRDFdMGTLGLAYVGSPRDNSA-GGIcekayyysngkkkylNT-GLTTTVNYGK 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 160358787 344 ---------IVAHELGHNLGMNHD-DGRECFCGAK---SCIMNSGA-SGS----RNFSSCSAEDFEKLTLNKGGSC 401
Cdd:cd04270  161 rvptkesdlVTAHELGHNFGSPHDpDIAECAPGESqggNYIMYARAtSGDkennKKFSPCSKKSISKVLEVKSNSC 236
PHA03378 PHA03378
EBNA-3B; Provisional
 748-810 6.66e-06

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 50.07  E-value: 6.66e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 160358787 748 GDPSISRPP-GGPNVSRPP-GGPGVSRPP-GGPGVSRPP-GGPGVSRPPPGHGNRFPVPTYAAKQPA 810
Cdd:PHA03378 709 APPGRAQRPaAATGRARPPaAAPGRARPPaAAPGRARPPaAAPGRARPPAAAPGRARPPAAAPGAPT 775
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
742-811 9.00e-06

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 49.26  E-value: 9.00e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358787 742 NVSRQPGDPSISRPPGGPNVSRPPGGPGVSRPPGGPGVSRPPGGPGVSRPPPGHGNRFPVPTYAAKQPAQ 811
Cdd:COG5164   16 GVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQ 85
PHA03378 PHA03378
EBNA-3B; Provisional
 747-805 1.51e-05

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 48.91  E-value: 1.51e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 160358787 747 PGDPSISRPPGGPNVS--RPPGGPGVSRPP-GGPGVSRPP-GGPGVSRPPPGHGNRFPVPTYA 805
Cdd:PHA03378 698 PRAPTPMRPPAAPPGRaqRPAAATGRARPPaAAPGRARPPaAAPGRARPPAAAPGRARPPAAA 760
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
 732-811 2.43e-05

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


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 45.41  E-value: 2.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358787  732 SQMSDGRNQanvsRQPGDPSISRPPGGPNVSRPP-GGPGVSRPP-GGPGVSRPPGGPGVSRPPPGHGNRFPVPTYAAKQP 809
Cdd:pfam15240  30 SLISEEEGQ----SQQGGQGPQGPPPGGFPPQPPaSDDPPGPPPpGGPQQPPPQGGKQKPQGPPPQGGPRPPPGKPQGPP 105


                  ..
gi 160358787  810 AQ 811
Cdd:pfam15240 106 PQ 107
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
732-810 3.11e-05

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 47.33  E-value: 3.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358787 732 SQMSDGRNQANVSRQPGDPSIS-RPPGGPNVSRPPGGPGVSRPPGGPGVSRPPGGPGVSRPPPGHGNRFPVPTYAAKQPA 810
Cdd:COG5164   23 SQGSTKPAQNQGSTRPAGNTGGtRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQGGTRPAGNTGGTTPA 102
ZnMc_ADAM_fungal cd04271
Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A ...
 310-386 3.37e-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: 45.88  E-value: 3.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358787 310 GGTAGMAFVGTVCSRSHAG-------GINVFGQITVETfaSIVAHELGHNLGMNHD----------DGRECFC--GAKSC 370
Cdd:cd04271  109 GSEVGVAWLGQLCRTGASDqgnetvaGTNVVVRTSNEW--QVFAHEIGHTFGAVHDctsgtcsdgsVGSQQCCplSTSTC 186

                         90       100
                 ....*....|....*....|...
gi 160358787 371 ------IMN-SGASGSRNFSSCS 386
Cdd:cd04271  187 dangqyIMNpSSSSGITEFSPCT 209
PHA03378 PHA03378
EBNA-3B; Provisional
 741-814 1.47e-04

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 45.44  E-value: 1.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358787 741 ANVSRQPG-DPSISRPPG-GPNVSRPPGG-PGVSRPP-GGPGVSRPP-GGPGVSRPPPGHGNRFPVPTYA---AKQPAQF 812
Cdd:PHA03378 681 ANTMLPIQwAPGTMQPPPrAPTPMRPPAApPGRAQRPaAATGRARPPaAAPGRARPPAAAPGRARPPAAApgrARPPAAA 760


                 ..
gi 160358787 813 PS 814
Cdd:PHA03378 761 PG 762
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
750-811 1.67e-04

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 45.02  E-value: 1.67e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 160358787 750 PSISRPPGGPNVSRPPGGPGVSRPPGGPGVSRPPGGPGVSRPPPGHGNRFPVPTYAAKQPAQ 811
Cdd:COG5164    6 PGKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAG 67
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
 740-797 2.46e-04

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


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 42.72  E-value: 2.46e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 160358787  740 QANVSRQPGDPSISRPPGGPNVSRPPGGPGVSRPPGGPGVSRPPGGPGVSRPPPGHGN 797
Cdd:pfam15240  91 QGGPRPPPGKPQGPPPQGGNQQQGPPPPGKPQGPPPQGGGPPPQGGNQQGPPPPPPGN 148
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
747-811 3.32e-04

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 44.25  E-value: 3.32e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 160358787 747 PGDPSISRPPGGPNVSRPPGGPGVSRPPGGPGVSRPPGGPGVSRPP-PGHGNRfPVPTYAAKQPAQ 811
Cdd:COG5164   12 SDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAgNTGGTR-PAGNQGATGPAQ 76
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 731-806 4.60e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 44.01  E-value: 4.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358787  731 RSQMSDGRNQANVSRQPGDPSISRPPGGPNVSRPPGGPGVSRPPGGPGV--SRPPGGP----GVSRPPPG--HGnrfPVP 802
Cdd:PHA03307  864 RARGKNGRRRPRPPEPRARPGAAAPPKAAAAAPPAGAPAPRPRPAPRVKlgPMPPGGPdprgGFRRVPPGdlHT---PAP 940


                  ....
gi 160358787  803 TYAA 806
Cdd:PHA03307  941 SAAA 944
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 747-794 4.89e-04

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 38.63  E-value: 4.89e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 160358787  747 PGDPSISRPPGGPNVSRPPGGPGVSRPPGGPGVSRPPGGPGvsrpPPG 794
Cdd:pfam01391   6 PGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPG----PPG 49
PHA03378 PHA03378
EBNA-3B; Provisional
 728-802 5.88e-04

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 43.52  E-value: 5.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358787 728 RKKRSQMSDGRnqanvSRQP-GDPSISRPP-GGPNVSRPP-GGPGVSRPP-GGPGVSRPP-GGPGVSRP-PPGHGNrfPV 801
Cdd:PHA03378 713 RAQRPAAATGR-----ARPPaAAPGRARPPaAAPGRARPPaAAPGRARPPaAAPGRARPPaAAPGAPTPqPPPQAP--PA 785


                 .
gi 160358787 802 P 802
Cdd:PHA03378 786 P 786
Drf_FH1 pfam06346
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs) ...
 747-809 7.08e-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: 7.08e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 160358787  747 PGDPSISRPP---GGPNVSRPP---GGPGVSRPP---GGPGVSRPP---GGPGVSRPPPghgnrfPVPTYAAKQP 809
Cdd:pfam06346  40 PGSAAIPPPPplpGGTSIPPPPplpGAASIPPPPplpGSTGIPPPPplpGGAGIPPPPP------PLPGGAGVPP 108
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
 747-810 7.40e-04

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


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 41.18  E-value: 7.40e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 160358787  747 PGDPSISRPPGGPNVSRPPGGP----------GVSRPPGGPGVSRPPGGPGVSRPPPGHGNRFPVPTYAAKQPA 810
Cdd:pfam15240  61 SDDPPGPPPPGGPQQPPPQGGKqkpqgpppqgGPRPPPGKPQGPPPQGGNQQQGPPPPGKPQGPPPQGGGPPPQ 134
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
 746-810 9.54e-04

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


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 40.79  E-value: 9.54e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 160358787  746 QPGDPSISRPPGGPNVSRPPGGPGVSRPPGGPGVSRPPGGPGVSRPPPGHGNRFPVPTYAAKQPA 810
Cdd:pfam15240  79 QGGKQKPQGPPPQGGPRPPPGKPQGPPPQGGNQQQGPPPPGKPQGPPPQGGGPPPQGGNQQGPPP 143
PBP1 COG5180
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ...
 723-811 1.62e-03

PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification];


Pssm-ID: 444064 [Multi-domain]  Cd Length: 548  Bit Score: 41.97  E-value: 1.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358787 723 LRKTFRKKRSQMSDGRNQANVSRQPGDPSISRPPGGPNVSRPPGG--PGVSRPPGGPGVSR--PPGGPGVSRPPPGHGNR 798
Cdd:COG5180  310 APPATRPVRPPGGARDPGTPRPGQPTERPAGVPEAASDAGQPPSAypPAEEAVPGKPLEQGapRPGSSGGDGAPFQPPNG 389

                         90
                 ....*....|....*.
gi 160358787 799 FPVPT---YAAKQPAQ 811
Cdd:COG5180  390 APQPGlgrRGAPGPPM 405
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 755-794 2.06e-03

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 37.09  E-value: 2.06e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 160358787  755 PPGGPNVSRPPGGPGVSRPPGGPGVSRPPGGPGvSRPPPG 794
Cdd:pfam01391   5 PPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPG-PPGPPG 43
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 331-357 3.22e-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: 39.40  E-value: 3.22e-03
                         10        20
                 ....*....|....*....|....*..
gi 160358787 331 NVFGQITVETFASIVAHELGHNLGMNH 357
Cdd:cd04268   84 SSFVEYSGARLRNTAEHELGHALGLRH 110
PHA03247 PHA03247
large tegument protein UL36; Provisional
 730-810 3.57e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.08  E-value: 3.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160358787  730 KRSQMSDGRNQANVSRQPGDPSISRP----PGGPNVSRPPGGP-GVSRPPGGPGVSRPPGGPGVSRPPPghGNRFPVPTY 804
Cdd:PHA03247  382 TRKRRSARHAATPFARGPGGDDQTRPaapvPASVPTPAPTPVPaSAPPPPATPLPSAEPGSDDGPAPPP--ERQPPAPAT 459


                  ....*.
gi 160358787  805 AAKQPA 810
Cdd:PHA03247  460 EPAPDD 465
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
 345-392 5.45e-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: 38.82  E-value: 5.45e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 160358787 345 VAHELGHNLGMNHddgrecfCGAKSCIMnsgasgsrNFSSCSAEDFEK 392
Cdd:cd11375  127 AVHELGHLFGLDH-------CPYYACVM--------NFSNSLEETDRK 159
Drf_FH1 pfam06346
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs) ...
 747-793 6.69e-03

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: 38.31  E-value: 6.69e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 160358787  747 PGDPS-ISRPPG--GPNVSRPPGGPGVSRPP---GGPGVSRPP---GGPGVSRPPP 793
Cdd:pfam06346   7 PGDSStIPLPPGacIPTPPPLPGGGGPPPPPplpGSAAIPPPPplpGGTSIPPPPP 62
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 755-795 7.49e-03

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 35.55  E-value: 7.49e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 160358787  755 PPGGPNVSRPPGGPGVSRPPGGPGVSRPPGGPGvsrpPPGH 795
Cdd:pfam01391   2 PPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPG----PPGP 38
EGF_2 pfam07974
EGF-like domain; This family contains EGF domains found in a variety of extracellular proteins.
 650-673 7.85e-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: 7.85e-03
                          10        20
                  ....*....|....*....|....*
gi 160358787  650 CHGHGVCNS-NKNCHCEDGWAPPHC 673
Cdd:pfam07974   2 CSGRGTCVNqCGKCVCDSGYQGATC 26
FAP pfam07174
Fibronectin-attachment protein (FAP); This family contains bacterial fibronectin-attachment ...
 747-809 8.16e-03

Fibronectin-attachment protein (FAP); This family contains bacterial fibronectin-attachment proteins (FAP). Family members are rich in alanine and proline, are approximately 300 long, and seem to be restricted to mycobacteria. These proteins contain a fibronectin-binding motif that allows mycobacteria to bind to fibronectin in the extracellular matrix.


Pssm-ID: 429334  Cd Length: 301  Bit Score: 39.14  E-value: 8.16e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 160358787  747 PGDPSISRPPGGPNVSRPPGGPGVSRPPG---GPGVSRPPGGPGVSRPPPGHGNRFPVPtyaAKQP 809
Cdd:pfam07174  46 PPPSTATAPPAPPPPPPAPAAPAPPPPPAapnAPNAPPPPADPNAPPPPPADPNAPPPP---AVDP 108
 
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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