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Conserved domains on  [gi|28972033|dbj|BAC65470|]
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mKIAA0021 protein, partial [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 220-412 3.38e-94

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: 293.75  E-value: 3.38e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28972033 220 RYVELFIVVDKERYDMMGRNQTAVREEMIRLANYLDSMYIMLNIRIVLVGLEIWTDRNPINIIGGAGDVLGNFVQWREKF 299
Cdd:cd04269   1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28972033 300 LITRRRHDSAQLVLKKGF-GGTAGMAFVGTVCSRSHAGGINVFGQITVETFASIVAHELGHNLGMNHDDGrECFCGAKSC 378
Cdd:cd04269  81 LLPRKPHDNAQLLTGRDFdGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDG-GCTCGRSTC 159

                       170       180       190
                ....*....|....*....|....*....|....*
gi 28972033 379 IMNSGAS-GSRNFSSCSAEDFEKLTLNKGGSCLLN 412
Cdd:cd04269 160 IMAPSPSsLTDAFSNCSYEDYQKFLSRGGGQCLLN 194
ACR smart00608
ADAM Cysteine-Rich Domain;
508-644 2.60e-59

ADAM Cysteine-Rich Domain;


:

Pssm-ID: 214743  Cd Length: 137  Bit Score: 197.97  E-value: 2.60e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28972033    508 QNGYPCQNSKAYCYNGMCQYYDAQCQVIFGSKAKAAPRDCFIEVNSKGDRFGNCGFSGSEYKKCATGNALCGKLQCENVQ 587
Cdd:smart00608   1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 28972033    588 DMPVFGIVPAIIQTPSRGTKCWGVDFQLGSDvPDPGMVNEGTKCDAGKICRNFQCVN 644
Cdd:smart00608  81 ELPLLGEHATVIYSNIGGLVCWSLDYHLGTD-PDIGMVKDGTKCGPGKVCINGQCVD 136
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 52-171 1.29e-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: 1.29e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28972033    52 EIITPWRLT--RERREALGPSSQ--QISYVIQAQGKQHIIHLERNTDLLPNDFVVYTYDKEGSLLSDHPNVQSHCHYRGY 127
Cdd:pfam01562   1 EVVIPVRLDpsRRRRSLASESTYldTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 28972033   128 VEGVQNSAVAVSACFGLRGLLHLENASFGIEPLHN----SSHFEHIFY 171
Cdd:pfam01562  81 VEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEKysreEGGHPHVVY 128
Disintegrin pfam00200
Disintegrin;
431-504 1.29e-36

Disintegrin;


:

Pssm-ID: 459709  Cd Length: 74  Bit Score: 131.98  E-value: 1.29e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28972033   431 DPGEECDCGTAKECEVDPCCEGSTCKLKSFAECAYGDCCKDCQFLPGGSMCRGKTSECDVPEYCNGSSQFCPPD 504
Cdd:pfam00200   1 EEGEECDCGSLEECTNDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
Drf_FH1 pfam06346
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs) ...
 755-810 1.57e-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: 1.57e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28972033   755 PGDPSISRPP---GGPNVSRPP----GGPGVSRPP----GGPGVSRP---PGGPGVSRPPPGHGNRFPVP 810
Cdd:pfam06346  76 PGSTGIPPPPplpGGAGIPPPPpplpGGAGVPPPPpplpGGPGIPPPppfPGGPGIPPPPPGMGMPPPPP 145
EGF_2 pfam07974
EGF-like domain; This family contains EGF domains found in a variety of extracellular proteins.
 658-681 7.04e-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: 7.04e-03
                          10        20
                  ....*....|....*....|....*
gi 28972033   658 CHGHGVCNS-NKNCHCEDGWAPPHC 681
Cdd:pfam07974   2 CSGRGTCVNqCGKCVCDSGYQGATC 26
 
Name Accession Description Interval E-value
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 220-412 3.38e-94

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: 293.75  E-value: 3.38e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28972033 220 RYVELFIVVDKERYDMMGRNQTAVREEMIRLANYLDSMYIMLNIRIVLVGLEIWTDRNPINIIGGAGDVLGNFVQWREKF 299
Cdd:cd04269   1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28972033 300 LITRRRHDSAQLVLKKGF-GGTAGMAFVGTVCSRSHAGGINVFGQITVETFASIVAHELGHNLGMNHDDGrECFCGAKSC 378
Cdd:cd04269  81 LLPRKPHDNAQLLTGRDFdGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDG-GCTCGRSTC 159

                       170       180       190
                ....*....|....*....|....*....|....*
gi 28972033 379 IMNSGAS-GSRNFSSCSAEDFEKLTLNKGGSCLLN 412
Cdd:cd04269 160 IMAPSPSsLTDAFSNCSYEDYQKFLSRGGGQCLLN 194
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 220-414 1.64e-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: 1.64e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28972033   220 RYVELFIVVDKERYDMMGRNQTAVREEMIRLANYLDSMYIMLNIRIVLVGLEIWTDRNPINIIGGAGDVLGNFVQWREKF 299
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28972033   300 LITRRRHDSAQLVLKKGFGG-TAGMAFVGTVCSRSHAGGINVFGQITVETFASIVAHELGHNLGMNHDDG-RECFCG-AK 376
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFGGtTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFnGGCKCPpGG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 28972033   377 SCIMNS--GASGSRNFSSCSAEDFEKLTLNKGGSCLLNIP 414
Cdd:pfam01421 161 GCIMNPsaGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ACR smart00608
ADAM Cysteine-Rich Domain;
508-644 2.60e-59

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 197.97  E-value: 2.60e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28972033    508 QNGYPCQNSKAYCYNGMCQYYDAQCQVIFGSKAKAAPRDCFIEVNSKGDRFGNCGFSGSEYKKCATGNALCGKLQCENVQ 587
Cdd:smart00608   1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 28972033    588 DMPVFGIVPAIIQTPSRGTKCWGVDFQLGSDvPDPGMVNEGTKCDAGKICRNFQCVN 644
Cdd:smart00608  81 ELPLLGEHATVIYSNIGGLVCWSLDYHLGTD-PDIGMVKDGTKCGPGKVCINGQCVD 136
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 509-613 7.92e-48

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: 165.10  E-value: 7.92e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28972033   509 NGYPCQNSKAYCYNGMCQYYDAQCQVIFGSKAKAAPRDCFIEVNSKGDRFGNCGFSGSEYKKCATGNALCGKLQCENVQD 588
Cdd:pfam08516   1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQCTNVKE 80

                          90       100
                  ....*....|....*....|....*
gi 28972033   589 MPVFGIVPAIIQTPSRGTKCWGVDF 613
Cdd:pfam08516  81 LPLLGEHATVIYTNINGVTCWGTDY 105
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 52-171 1.29e-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: 1.29e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28972033    52 EIITPWRLT--RERREALGPSSQ--QISYVIQAQGKQHIIHLERNTDLLPNDFVVYTYDKEGSLLSDHPNVQSHCHYRGY 127
Cdd:pfam01562   1 EVVIPVRLDpsRRRRSLASESTYldTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 28972033   128 VEGVQNSAVAVSACFGLRGLLHLENASFGIEPLHN----SSHFEHIFY 171
Cdd:pfam01562  81 VEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEKysreEGGHPHVVY 128
Disintegrin pfam00200
Disintegrin;
431-504 1.29e-36

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 131.98  E-value: 1.29e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28972033   431 DPGEECDCGTAKECEVDPCCEGSTCKLKSFAECAYGDCCKDCQFLPGGSMCRGKTSECDVPEYCNGSSQFCPPD 504
Cdd:pfam00200   1 EEGEECDCGSLEECTNDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 431-506 2.65e-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: 2.65e-35
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28972033    431 DPGEECDCGTAKECeVDPCCEGSTCKLKSFAECAYGDCCKDCQFLPGGSMCRGKTSECDVPEYCNGSSQFCPPDVF 506
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) ...
 755-810 1.57e-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: 1.57e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28972033   755 PGDPSISRPP---GGPNVSRPP----GGPGVSRPP----GGPGVSRP---PGGPGVSRPPPGHGNRFPVP 810
Cdd:pfam06346  76 PGSTGIPPPPplpGGAGIPPPPpplpGGAGVPPPPpplpGGPGIPPPppfPGGPGIPPPPPGMGMPPPPP 145
PHA03378 PHA03378
EBNA-3B; Provisional
 756-818 8.70e-06

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 49.68  E-value: 8.70e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28972033  756 GDPSISRPP-GGPNVSRPP-GGPGVSRPP-GGPGVSRPP-GGPGVSRPPPGHGNRFPVPTYAAKQPA 818
Cdd:PHA03378 709 APPGRAQRPaAATGRARPPaAAPGRARPPaAAPGRARPPaAAPGRARPPAAAPGRARPPAAAPGAPT 775
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
750-819 1.05e-05

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 48.87  E-value: 1.05e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28972033 750 NVSRQPGDPSISRPPGGPNVSRPPGGPGVSRPPGGPGVSRPPGGPGVSRPPPGHGNRFPVPTYAAKQPAQ 819
Cdd:COG5164  16 GVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQ 85
EGF_2 pfam07974
EGF-like domain; This family contains EGF domains found in a variety of extracellular proteins.
 658-681 7.04e-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: 7.04e-03
                          10        20
                  ....*....|....*....|....*
gi 28972033   658 CHGHGVCNS-NKNCHCEDGWAPPHC 681
Cdd:pfam07974   2 CSGRGTCVNqCGKCVCDSGYQGATC 26
 
Name Accession Description Interval E-value
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 220-412 3.38e-94

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: 293.75  E-value: 3.38e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28972033 220 RYVELFIVVDKERYDMMGRNQTAVREEMIRLANYLDSMYIMLNIRIVLVGLEIWTDRNPINIIGGAGDVLGNFVQWREKF 299
Cdd:cd04269   1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28972033 300 LITRRRHDSAQLVLKKGF-GGTAGMAFVGTVCSRSHAGGINVFGQITVETFASIVAHELGHNLGMNHDDGrECFCGAKSC 378
Cdd:cd04269  81 LLPRKPHDNAQLLTGRDFdGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDG-GCTCGRSTC 159

                       170       180       190
                ....*....|....*....|....*....|....*
gi 28972033 379 IMNSGAS-GSRNFSSCSAEDFEKLTLNKGGSCLLN 412
Cdd:cd04269 160 IMAPSPSsLTDAFSNCSYEDYQKFLSRGGGQCLLN 194
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 220-414 1.64e-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: 1.64e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28972033   220 RYVELFIVVDKERYDMMGRNQTAVREEMIRLANYLDSMYIMLNIRIVLVGLEIWTDRNPINIIGGAGDVLGNFVQWREKF 299
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28972033   300 LITRRRHDSAQLVLKKGFGG-TAGMAFVGTVCSRSHAGGINVFGQITVETFASIVAHELGHNLGMNHDDG-RECFCG-AK 376
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFGGtTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFnGGCKCPpGG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 28972033   377 SCIMNS--GASGSRNFSSCSAEDFEKLTLNKGGSCLLNIP 414
Cdd:pfam01421 161 GCIMNPsaGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ACR smart00608
ADAM Cysteine-Rich Domain;
508-644 2.60e-59

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 197.97  E-value: 2.60e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28972033    508 QNGYPCQNSKAYCYNGMCQYYDAQCQVIFGSKAKAAPRDCFIEVNSKGDRFGNCGFSGSEYKKCATGNALCGKLQCENVQ 587
Cdd:smart00608   1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 28972033    588 DMPVFGIVPAIIQTPSRGTKCWGVDFQLGSDvPDPGMVNEGTKCDAGKICRNFQCVN 644
Cdd:smart00608  81 ELPLLGEHATVIYSNIGGLVCWSLDYHLGTD-PDIGMVKDGTKCGPGKVCINGQCVD 136
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 509-613 7.92e-48

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: 165.10  E-value: 7.92e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28972033   509 NGYPCQNSKAYCYNGMCQYYDAQCQVIFGSKAKAAPRDCFIEVNSKGDRFGNCGFSGSEYKKCATGNALCGKLQCENVQD 588
Cdd:pfam08516   1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQCTNVKE 80

                          90       100
                  ....*....|....*....|....*
gi 28972033   589 MPVFGIVPAIIQTPSRGTKCWGVDF 613
Cdd:pfam08516  81 LPLLGEHATVIYTNINGVTCWGTDY 105
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 52-171 1.29e-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: 1.29e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28972033    52 EIITPWRLT--RERREALGPSSQ--QISYVIQAQGKQHIIHLERNTDLLPNDFVVYTYDKEGSLLSDHPNVQSHCHYRGY 127
Cdd:pfam01562   1 EVVIPVRLDpsRRRRSLASESTYldTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 28972033   128 VEGVQNSAVAVSACFGLRGLLHLENASFGIEPLHN----SSHFEHIFY 171
Cdd:pfam01562  81 VEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEKysreEGGHPHVVY 128
Disintegrin pfam00200
Disintegrin;
431-504 1.29e-36

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 131.98  E-value: 1.29e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28972033   431 DPGEECDCGTAKECEVDPCCEGSTCKLKSFAECAYGDCCKDCQFLPGGSMCRGKTSECDVPEYCNGSSQFCPPD 504
Cdd:pfam00200   1 EEGEECDCGSLEECTNDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 431-506 2.65e-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: 2.65e-35
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28972033    431 DPGEECDCGTAKECeVDPCCEGSTCKLKSFAECAYGDCCKDCQFLPGGSMCRGKTSECDVPEYCNGSSQFCPPDVF 506
Cdd:smart00050   1 EEGEECDCGSPKEC-TDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 220-395 7.91e-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: 117.14  E-value: 7.91e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28972033 220 RYVELFIVVDKERYDMMGRNQTAVREEMIRLANYLDSMY----IMLNIRIVLVGLEIWTDRNPINIIG-GAGDVLGNFVQ 294
Cdd:cd04267   1 REIELVVVADHRMVSYFNSDENILQAYITELINIANSIYrstnLRLGIRISLEGLQILKGEQFAPPIDsDASNTLNSFSF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28972033 295 WREKFLItrrRHDSAQLVLKKGF--GGTAGMAFVGTVCSRSHAGGINVFGQITVETfASIVAHELGHNLGMNHDDGRECF 372
Cdd:cd04267  81 WRAEGPI---RHDNAVLLTAQDFieGDILGLAYVGSMCNPYSSVGVVEDTGFTLLT-ALTMAHELGHNLGAEHDGGDELA 156

                       170       180
                ....*....|....*....|....*...
gi 28972033 373 C---GAKSCIMNSGASGSRN--FSSCSA 395
Cdd:cd04267 157 FecdGGGNYIMAPVDSGLNSyrFSQCSI 184
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 220-411 6.28e-28

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: 111.95  E-value: 6.28e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28972033 220 RYVELFIVVDKERYDMMGRNQTavrEEMI-RLANYLDSMY----IMLNIRIVLVGLEIWTDRNP-INIIGGAGDVLGNFV 293
Cdd:cd04273   1 RYVETLVVADSKMVEFHHGEDL---EHYIlTLMNIVASLYkdpsLGNSINIVVVRLIVLEDEESgLLISGNAQKSLKSFC 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28972033 294 QWREK---------------FLITRRrhdsaQLVLKKGFGGTAGMAFVGTVCSRSHAGGINvfgQITVETFASIVAHELG 358
Cdd:cd04273  78 RWQKKlnppndsdpehhdhaILLTRQ-----DICRSNGNCDTLGLAPVGGMCSPSRSCSIN---EDTGLSSAFTIAHELG 149

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 28972033 359 HNLGMNHDD-GREC-FCGAKSCIMNS-GASGSRNF--SSCSAEDFEKLTLNKGGSCLL 411
Cdd:cd04273 150 HVLGMPHDGdGNSCgPEGKDGHIMSPtLGANTGPFtwSKCSRRYLTSFLDTGDGNCLL 207
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 245-366 6.57e-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: 6.57e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28972033   245 EEMIRLANYLDSMY-IMLNIRIVLVGLEIWTDRNPINIIGGAGDVLGNFVQWrekfLITRRRH---DSAQLVLKKGFGGT 320
Cdd:pfam13582   1 ARIVSLVNRANTIYeRDLGIRLQLAAIIITTSADTPYTSSDALEILDELQEV----NDTRIGQygyDLGHLFTGRDGGGG 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 28972033   321 AGMAFVGTVCSRSHAGGINVFGQITVETFASIVAHELGHNLGMNHD 366
Cdd:pfam13582  77 GGIAYVGGVCNSGSKFGVNSGSGPVGDTGADTFAHEIGHNFGLNHT 122
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
219-391 8.07e-18

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 82.47  E-value: 8.07e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28972033   219 TRYVELFIVVDKERYDMMGRNqtAVREEMIRLANYLDS-MYIMLNIRIVLVGLEIWTDRNPINIIGG----AGDVLGNFV 293
Cdd:pfam13688   2 TRTVALLVAADCSYVAAFGGD--AAQANIINMVNTASNvYERDFNISLGLVNLTISDSTCPYTPPACstgdSSDRLSEFQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28972033   294 QWREkfLITRRRHDSAQLVLKKGFGGTaGMAFVGTVCSRSHAGGINVFGQITVE-----TFASIVAHELGHNLGMNHD-- 366
Cdd:pfam13688  80 DFSA--WRGTQNDDLAYLFLMTNCSGG-GLAWLGQLCNSGSAGSVSTRVSGNNVvvstaTEWQVFAHEIGHNFGAVHDcd 156

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 28972033   367 ---DGRECFCGAKSC------IMN-SGASGSRNFS 391
Cdd:pfam13688 157 sstSSQCCPPSNSTCpaggryIMNpSSSPNSTDFS 191
ZnMc_salivary_gland_MPs cd04272
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ...
 221-410 2.35e-15

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 75.85  E-value: 2.35e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28972033 221 YVELFIVVDKERYDMMGRNQtAVREEMIRLANYLDSMYIMLN---IRIVLVGLEIWTDRNPINIIGGAGD-------VLG 290
Cdd:cd04272   2 YPELFVVVDYDHQSEFFSNE-QLIRYLAVMVNAANLRYRDLKsprIRLLLVGITISKDPDFEPYIHPINYgyidaaeTLE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28972033 291 NFVQW-REK---------FLITRRR-HDSAQLVLKKGfggTAGMAFVGTVCSRSHAGginvFGQITVETFASI--VAHEL 357
Cdd:cd04272  81 NFNEYvKKKrdyfnpdvvFLVTGLDmSTYSGGSLQTG---TGGYAYVGGACTENRVA----MGEDTPGSYYGVytMTHEL 153

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28972033 358 GHNLGMNHDDGREC-----FCGAKSC------IMNSGASGSRN--FSSCSAEDFEKLTLNKGGSCL 410
Cdd:cd04272 154 AHLLGAPHDGSPPPswvkgHPGSLDCpwddgyIMSYVVNGERQyrFSQCSQRQIRNVFRRLGASCL 219
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 220-401 4.79e-13

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: 67.93  E-value: 4.79e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28972033 220 RYVELFIVVDKERYDmmgrnQTAVREEMIRLANYLDSMY-IMLNIRIVLVGLEIWTDRNpiniiggagdvlgnfvqwreK 298
Cdd:cd00203   1 KVIPYVVVADDRDVE-----EENLSAQIQSLILIAMQIWrDYLNIRFVLVGVEIDKADI--------------------A 55

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28972033 299 FLITRRRHDsaqlvlkkgfGGTAGMAFVGTVCSRSHAGGINVFGQITVETFASIVAHELGHNLGMNHDDGRECFCG---- 374
Cdd:cd00203  56 ILVTRQDFD----------GGTGGWAYLGRVCDSLRGVGVLQDNQSGTKEGAQTIAHELGHALGFYHDHDRKDRDDypti 125

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 28972033 375 ---------AKSCIMNSGAS-----GSRNFSSCSAEDFEKL 401
Cdd:cd00203 126 ddtlnaeddDYYSVMSYTKGsfsdgQRKDFSQCDIDQINKL 166
Drf_FH1 pfam06346
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs) ...
 755-810 1.57e-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: 1.57e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28972033   755 PGDPSISRPP---GGPNVSRPP----GGPGVSRPP----GGPGVSRP---PGGPGVSRPPPGHGNRFPVP 810
Cdd:pfam06346  76 PGSTGIPPPPplpGGAGIPPPPpplpGGAGVPPPPpplpGGPGIPPPppfPGGPGIPPPPPGMGMPPPPP 145
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 242-394 2.46e-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: 2.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28972033   242 AVREEMIRLANYLDSMYIM--LNIRIVLVGLEIWTDRNPINIIGGAGDVLGNFVQWREKFL---ITRRRHDSAQLVLKKG 316
Cdd:pfam13574   2 NVTENLVNVVNRVNQIYEPddININGGLVNPGEIPATTSASDSGNNYCNSPTTIVRRLNFLsqwRGEQDYCLAHLVTMGT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28972033   317 F-GGTAGMAFVGTVC-----SRSHAGGINV---FGQITVETFA-SIVAHELGHNLGMNHDDGRECFC--------GAKSC 378
Cdd:pfam13574  82 FsGGELGLAYVGQICqkgasSPKTNTGLSTttnYGSFNYPTQEwDVVAHEVGHNFGATHDCDGSQYAssgcernaATSVC 161

                         170       180
                  ....*....|....*....|...
gi 28972033   379 ------IMN-SGASGSRNFSSCS 394
Cdd:pfam13574 162 sangsfIMNpASKSNNDLFSPCS 184
Reprolysin_4 pfam13583
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 220-398 1.78e-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: 55.32  E-value: 1.78e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28972033   220 RYVELFIVVDKERYDMMGrNQTAVREEMIRLANYLDSMY-IMLNIRIVLVGLE--IWTDRNP----INIIGGAgdvLGNF 292
Cdd:pfam13583   3 RVYRVAVATDCTYSASFG-SVDELRANINATVTTANEVYgRDFNVSLALISDRdvIYTDSSTdsfnADCSGGD---LGNW 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28972033   293 VQWREKFLITRRRHDSAQLVLKKG-FGGTAGMAFVGTVCSRSH--AGGiNVFGQITVETfaSIVAHELGHNLGMNHDDGR 369
Cdd:pfam13583  79 RLATLTSWRDSLNYDLAYLTLMTGpSGQNVGVAWVGALCSSARqnAKA-SGVARSRDEW--DIFAHEIGHTFGAVHDCSS 155

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 28972033   370 ECfCGAK--------SCIMNSGASGSR-NFSSCSAEDF 398
Cdd:pfam13583 156 QG-EGLSsstedgsgQTIMSYASTASQtAFSPCTIRNI 192
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
 224-409 1.84e-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: 50.06  E-value: 1.84e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28972033 224 LFIVVDKERYDMMGRNQT-AVREEMIRLANYLDSMY--------IMLNIRIVLVGLEIWTDRNPINiiGGAGDVLGNFVQ 294
Cdd:cd04270   5 LLLVADHRFYKYMGRGEEeTTINYLISHIDRVDDIYrntdwdggGFKGIGFQIKRIRIHTTPDEVD--PGNKFYNKSFPN 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28972033 295 W-REKFLITRRRHDS------AQLVLKKGF-GGTAGMAFVGTVCSRSHaGGI---------------NVfGQITVETFAS 351
Cdd:cd04270  83 WgVEKFLVKLLLEQFsddvclAHLFTYRDFdMGTLGLAYVGSPRDNSA-GGIcekayyysngkkkylNT-GLTTTVNYGK 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28972033 352 ---------IVAHELGHNLGMNHD-DGRECFCGAK---SCIMNSGA-SGS----RNFSSCSAEDFEKLTLNKGGSC 409
Cdd:cd04270 161 rvptkesdlVTAHELGHNFGSPHDpDIAECAPGESqggNYIMYARAtSGDkennKKFSPCSKKSISKVLEVKSNSC 236
PHA03378 PHA03378
EBNA-3B; Provisional
 756-818 8.70e-06

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 49.68  E-value: 8.70e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28972033  756 GDPSISRPP-GGPNVSRPP-GGPGVSRPP-GGPGVSRPP-GGPGVSRPPPGHGNRFPVPTYAAKQPA 818
Cdd:PHA03378 709 APPGRAQRPaAATGRARPPaAAPGRARPPaAAPGRARPPaAAPGRARPPAAAPGRARPPAAAPGAPT 775
ZnMc_ADAM_fungal cd04271
Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A ...
 289-394 9.27e-06

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


Pssm-ID: 239799 [Multi-domain]  Cd Length: 228  Bit Score: 47.80  E-value: 9.27e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28972033 289 LGNFVQWREKflitRRRHDSAQLVLKKGF--GGTAGMAFVGTVCSRSHAG-------GINVFGQITVETfaSIVAHELGH 359
Cdd:cd04271  82 LSIFSQWRGQ----QPDDGNAFWTLMTACpsGSEVGVAWLGQLCRTGASDqgnetvaGTNVVVRTSNEW--QVFAHEIGH 155

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 28972033 360 NLGMNHD----------DGRECFC--GAKSC------IMN-SGASGSRNFSSCS 394
Cdd:cd04271 156 TFGAVHDctsgtcsdgsVGSQQCCplSTSTCdangqyIMNpSSSSGITEFSPCT 209
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
750-819 1.05e-05

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 48.87  E-value: 1.05e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28972033 750 NVSRQPGDPSISRPPGGPNVSRPPGGPGVSRPPGGPGVSRPPGGPGVSRPPPGHGNRFPVPTYAAKQPAQ 819
Cdd:COG5164  16 GVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQ 85
PHA03378 PHA03378
EBNA-3B; Provisional
 755-813 1.95e-05

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 48.52  E-value: 1.95e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28972033  755 PGDPSISRPPGGPNVS--RPPGGPGVSRPP-GGPGVSRPP-GGPGVSRPPPGHGNRFPVPTYA 813
Cdd:PHA03378 698 PRAPTPMRPPAAPPGRaqRPAAATGRARPPaAAPGRARPPaAAPGRARPPAAAPGRARPPAAA 760
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
 740-819 2.95e-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: 2.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28972033   740 SQMSDGRNQanvsRQPGDPSISRPPGGPNVSRPP-GGPGVSRPP-GGPGVSRPPGGPGVSRPPPGHGNRFPVPTYAAKQP 817
Cdd:pfam15240  30 SLISEEEGQ----SQQGGQGPQGPPPGGFPPQPPaSDDPPGPPPpGGPQQPPPQGGKQKPQGPPPQGGPRPPPGKPQGPP 105


                  ..
gi 28972033   818 AQ 819
Cdd:pfam15240 106 PQ 107
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
740-818 3.74e-05

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 47.33  E-value: 3.74e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28972033 740 SQMSDGRNQANVSRQPGDPSIS-RPPGGPNVSRPPGGPGVSRPPGGPGVSRPPGGPGVSRPPPGHGNRFPVPTYAAKQPA 818
Cdd:COG5164  23 SQGSTKPAQNQGSTRPAGNTGGtRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQGGTRPAGNTGGTTPA 102
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
758-819 1.90e-04

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 45.02  E-value: 1.90e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28972033 758 PSISRPPGGPNVSRPPGGPGVSRPPGGPGVSRPPGGPGVSRPPPGHGNRFPVPTYAAKQPAQ 819
Cdd:COG5164   6 PGKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAG 67
PHA03378 PHA03378
EBNA-3B; Provisional
 749-822 1.94e-04

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 45.06  E-value: 1.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28972033  749 ANVSRQPG-DPSISRPPG-GPNVSRPPGGPGVS--RPPGGPGVSRPP-GGPGVSRPPPGHGNRFPVPTYA---AKQPAQF 820
Cdd:PHA03378 681 ANTMLPIQwAPGTMQPPPrAPTPMRPPAAPPGRaqRPAAATGRARPPaAAPGRARPPAAAPGRARPPAAApgrARPPAAA 760


                 ..
gi 28972033  821 PS 822
Cdd:PHA03378 761 PG 762
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
 748-805 2.78e-04

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


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 42.33  E-value: 2.78e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 28972033   748 QANVSRQPGDPSISRPPGGPNVSRPPGGPGVSRPPGGPGVSRPPGGPGVSRPPPGHGN 805
Cdd:pfam15240  91 QGGPRPPPGKPQGPPPQGGNQQQGPPPPGKPQGPPPQGGGPPPQGGNQQGPPPPPPGN 148
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
755-819 3.96e-04

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 43.87  E-value: 3.96e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28972033 755 PGDPSISRPPGGPNVSRPPGGPGVSRPPGGPGVSRPPGGPGVSRPP-PGHGNRfPVPTYAAKQPAQ 819
Cdd:COG5164  12 SDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAgNTGGTR-PAGNQGATGPAQ 76
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 755-802 5.61e-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: 5.61e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 28972033   755 PGDPSISRPPGGPNVSRPPGGPGVSRPPGGPGVSRPPGGPGvsrpPPG 802
Cdd:pfam01391   6 PGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPG----PPG 49
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 739-814 5.95e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 43.62  E-value: 5.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28972033   739 RSQMSDGRNQANVSRQPGDPSISRPPGGPNVSRPPGGPGVSRPPGGPGV--SRPPGGP----GVSRPPPG--HGnrfPVP 810
Cdd:PHA03307  864 RARGKNGRRRPRPPEPRARPGAAAPPKAAAAAPPAGAPAPRPRPAPRVKlgPMPPGGPdprgGFRRVPPGdlHT---PAP 940


                  ....
gi 28972033   811 TYAA 814
Cdd:PHA03307  941 SAAA 944
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 295-365 7.50e-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: 7.50e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28972033 295 WREKFLIT---RRRHDSAQL---VLKKGFGGTAGMAFVGTVcSRSHAGGI--------NVFGQITVETFASIVAHELGHN 360
Cdd:cd04268  27 WNKAFAIGfknANDVDPADIrysVIRWIPYNDGTWSYGPSQ-VDPLTGEIllarvylySSFVEYSGARLRNTAEHELGHA 105


                ....*
gi 28972033 361 LGMNH 365
Cdd:cd04268 106 LGLRH 110
PHA03378 PHA03378
EBNA-3B; Provisional
 736-810 8.15e-04

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 43.13  E-value: 8.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28972033  736 RKKRSQMSDGRnqanvSRQP-GDPSISRPP-GGPNVSRPP-GGPGVSRPP-GGPGVSRPP-GGPGVSRP-PPGHGNrfPV 809
Cdd:PHA03378 713 RAQRPAAATGR-----ARPPaAAPGRARPPaAAPGRARPPaAAPGRARPPaAAPGRARPPaAAPGAPTPqPPPQAP--PA 785


                 .
gi 28972033  810 P 810
Cdd:PHA03378 786 P 786
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
 755-818 8.45e-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: 8.45e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28972033   755 PGDPSISRPPGGPNVSRPPGGP----------GVSRPPGGPGVSRPPGGPGVSRPPPGHGNRFPVPTYAAKQPA 818
Cdd:pfam15240  61 SDDPPGPPPPGGPQQPPPQGGKqkpqgpppqgGPRPPPGKPQGPPPQGGNQQQGPPPPGKPQGPPPQGGGPPPQ 134
Drf_FH1 pfam06346
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs) ...
 755-817 8.56e-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: 40.62  E-value: 8.56e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28972033   755 PGDPSISRPP---GGPNVSRPP---GGPGVSRPP---GGPGVSRPP---GGPGVSRPPPghgnrfPVPTYAAKQP 817
Cdd:pfam06346  40 PGSAAIPPPPplpGGTSIPPPPplpGAASIPPPPplpGSTGIPPPPplpGGAGIPPPPP------PLPGGAGVPP 108
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
 754-818 1.06e-03

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: 1.06e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28972033   754 QPGDPSISRPPGGPNVSRPPGGPGVSRPPGGPGVSRPPGGPGVSRPPPGHGNRFPVPTYAAKQPA 818
Cdd:pfam15240  79 QGGKQKPQGPPPQGGPRPPPGKPQGPPPQGGNQQQGPPPPGKPQGPPPQGGGPPPQGGNQQGPPP 143
PBP1 COG5180
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ...
 731-819 1.64e-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: 1.64e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28972033 731 LRKTFRKKRSQMSDGRNQANVSRQPGDPSISRPPGGPNVSRPPGG--PGVSRPPGGPGVSR--PPGGPGVSRPPPGHGNR 806
Cdd:COG5180 310 APPATRPVRPPGGARDPGTPRPGQPTERPAGVPEAASDAGQPPSAypPAEEAVPGKPLEQGapRPGSSGGDGAPFQPPNG 389

                        90
                ....*....|....*.
gi 28972033 807 FPVPT---YAAKQPAQ 819
Cdd:COG5180 390 APQPGlgrRGAPGPPM 405
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 763-802 2.34e-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: 2.34e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 28972033   763 PPGGPNVSRPPGGPGVSRPPGGPGVSRPPGGPGvSRPPPG 802
Cdd:pfam01391   5 PPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPG-PPGPPG 43
PHA03247 PHA03247
large tegument protein UL36; Provisional
 738-818 3.61e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.08  E-value: 3.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28972033   738 KRSQMSDGRNQANVSRQPGDPSISRP----PGGPNVSRPPGGP-GVSRPPGGPGVSRPPGGPGVSRPPPghGNRFPVPTY 812
Cdd:PHA03247  382 TRKRRSARHAATPFARGPGGDDQTRPaapvPASVPTPAPTPVPaSAPPPPATPLPSAEPGSDDGPAPPP--ERQPPAPAT 459


                  ....*.
gi 28972033   813 AAKQPA 818
Cdd:PHA03247  460 EPAPDD 465
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
 353-400 5.46e-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: 5.46e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 28972033 353 VAHELGHNLGMNHddgrecfCGAKSCIMnsgasgsrNFSSCSAEDFEK 400
Cdd:cd11375 127 AVHELGHLFGLDH-------CPYYACVM--------NFSNSLEETDRK 159
EGF_2 pfam07974
EGF-like domain; This family contains EGF domains found in a variety of extracellular proteins.
 658-681 7.04e-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: 7.04e-03
                          10        20
                  ....*....|....*....|....*
gi 28972033   658 CHGHGVCNS-NKNCHCEDGWAPPHC 681
Cdd:pfam07974   2 CSGRGTCVNqCGKCVCDSGYQGATC 26
Drf_FH1 pfam06346
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs) ...
 755-801 8.31e-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: 37.93  E-value: 8.31e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 28972033   755 PGDPS-ISRPPG--GPNVSRPPGGPGVSRPP---GGPGVSRPP---GGPGVSRPPP 801
Cdd:pfam06346   7 PGDSStIPLPPGacIPTPPPLPGGGGPPPPPplpGSAAIPPPPplpGGTSIPPPPP 62
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 763-803 8.42e-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: 35.16  E-value: 8.42e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 28972033   763 PPGGPNVSRPPGGPGVSRPPGGPGVSRPPGGPGvsrpPPGH 803
Cdd:pfam01391   2 PPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPG----PPGP 38
FAP pfam07174
Fibronectin-attachment protein (FAP); This family contains bacterial fibronectin-attachment ...
 755-817 9.58e-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: 9.58e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28972033   755 PGDPSISRPPGGPNVSRPPGGPGVSRPPG---GPGVSRPPGGPGVSRPPPGHGNRFPVPtyaAKQP 817
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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