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Conserved domains on  [gi|401782598|ref|NP_001257925|]
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disintegrin and metalloproteinase domain-containing protein 9 isoform 1 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 9.31e-94

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: 293.05  E-value: 9.31e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401782598  212 RYVELFIVVDKERYDMMGRNQTAVREEMIRLANYLDSMYIMLNIRIVLVGLEIWTDRNPINIIGGAGDVLGNFVQWREKF 291
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401782598  292 LITRWRHDSAQLVLKKGFGG-TAGMAFVGTVCSRSHAGGINVFGQITVETFASIVAHELGHNLGMNHDDG-RECFCG-AK 368
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFGGtTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFnGGCKCPpGG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 401782598  369 SCIMNS--GASGSRNFSSCSAEDFEKLTLNKGGSCLLNIP 406
Cdd:pfam01421 161 GCIMNPsaGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
ACR smart00608
ADAM Cysteine-Rich Domain;
500-636 3.94e-59

ADAM Cysteine-Rich Domain;


:

Pssm-ID: 214743  Cd Length: 137  Bit Score: 197.58  E-value: 3.94e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401782598   500 QNGYPCQNSKAYCYNGMCQYYDAQCQVIFGSKAKAAPRDCFIEVNSKGDRFGNCGFSGSEYKKCATGNALCGKLQCENVQ 579
Cdd:smart00608   1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 401782598   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 1.37e-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: 1.37e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401782598   44 EIITPWRLT--RERREALGPSSQ--QISYVIQAQGKQHIIHLERNTDLLPNDFVVYTYDKEGSLLSDHPNVQSHCHYRGY 119
Cdd:pfam01562   1 EVVIPVRLDpsRRRRSLASESTYldTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 401782598  120 VEGVQNSAVAVSACFGLRGLLHLENASFGIEPLHN----SSHFEHIFY 163
Cdd:pfam01562  81 VEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEKysreEGGHPHVVY 128
Disintegrin pfam00200
Disintegrin;
423-496 1.08e-36

Disintegrin;


:

Pssm-ID: 459709  Cd Length: 74  Bit Score: 132.36  E-value: 1.08e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 401782598  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) ...
 747-820 4.76e-12

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: 64.89  E-value: 4.76e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401782598  747 PGDPSISRPP---GGPNVSRPP---GGPGVSRPP---GGPGVSRPP----GGPGVSRPP----GGPGVSRP---PGGPGV 806
Cdd:pfam06346  52 PGGTSIPPPPplpGAASIPPPPplpGSTGIPPPPplpGGAGIPPPPpplpGGAGVPPPPpplpGGPGIPPPppfPGGPGI 131

                          90
                  ....*....|....
gi 401782598  807 SRPPPGHGNRFPVP 820
Cdd:pfam06346 132 PPPPPGMGMPPPPP 145
EGF_2 pfam07974
EGF-like domain; This family contains EGF domains found in a variety of extracellular proteins.
 650-673 7.63e-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: 7.63e-03
                          10        20
                  ....*....|....*....|....*
gi 401782598  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 9.31e-94

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: 293.05  E-value: 9.31e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401782598  212 RYVELFIVVDKERYDMMGRNQTAVREEMIRLANYLDSMYIMLNIRIVLVGLEIWTDRNPINIIGGAGDVLGNFVQWREKF 291
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401782598  292 LITRWRHDSAQLVLKKGFGG-TAGMAFVGTVCSRSHAGGINVFGQITVETFASIVAHELGHNLGMNHDDG-RECFCG-AK 368
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFGGtTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFnGGCKCPpGG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 401782598  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 2.26e-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: 291.83  E-value: 2.26e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401782598 212 RYVELFIVVDKERYDMMGRNQTAVREEMIRLANYLDSMYIMLNIRIVLVGLEIWTDRNPINIIGGAGDVLGNFVQWREKF 291
Cdd:cd04269    1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401782598 292 LITRWRHDSAQLVLKKGF-GGTAGMAFVGTVCSRSHAGGINVFGQITVETFASIVAHELGHNLGMNHDDGrECFCGAKSC 370
Cdd:cd04269   81 LLPRKPHDNAQLLTGRDFdGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDG-GCTCGRSTC 159

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 401782598 371 IMNSGAS-GSRNFSSCSAEDFEKLTLNKGGSCLLN 404
Cdd:cd04269  160 IMAPSPSsLTDAFSNCSYEDYQKFLSRGGGQCLLN 194
ACR smart00608
ADAM Cysteine-Rich Domain;
500-636 3.94e-59

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 197.58  E-value: 3.94e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401782598   500 QNGYPCQNSKAYCYNGMCQYYDAQCQVIFGSKAKAAPRDCFIEVNSKGDRFGNCGFSGSEYKKCATGNALCGKLQCENVQ 579
Cdd:smart00608   1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 401782598   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 8.64e-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: 164.71  E-value: 8.64e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401782598  501 NGYPCQNSKAYCYNGMCQYYDAQCQVIFGSKAKAAPRDCFIEVNSKGDRFGNCGFSGSEYKKCATGNALCGKLQCENVQD 580
Cdd:pfam08516   1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQCTNVKE 80

                          90       100
                  ....*....|....*....|....*
gi 401782598  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 1.37e-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: 1.37e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401782598   44 EIITPWRLT--RERREALGPSSQ--QISYVIQAQGKQHIIHLERNTDLLPNDFVVYTYDKEGSLLSDHPNVQSHCHYRGY 119
Cdd:pfam01562   1 EVVIPVRLDpsRRRRSLASESTYldTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 401782598  120 VEGVQNSAVAVSACFGLRGLLHLENASFGIEPLHN----SSHFEHIFY 163
Cdd:pfam01562  81 VEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEKysreEGGHPHVVY 128
Disintegrin pfam00200
Disintegrin;
423-496 1.08e-36

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 132.36  E-value: 1.08e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 401782598  423 DPGEECDCGTAKECEVDPCCEGSTCKLKSFAECAYGDCCKDCQFLPGGSMCRGKTSECDVPEYCNGSSQFCPPD 496
Cdd:pfam00200   1 EEGEECDCGSLEECTNDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 423-498 2.34e-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: 128.58  E-value: 2.34e-35
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 401782598   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) ...
 747-820 4.76e-12

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: 64.89  E-value: 4.76e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401782598  747 PGDPSISRPP---GGPNVSRPP---GGPGVSRPP---GGPGVSRPP----GGPGVSRPP----GGPGVSRP---PGGPGV 806
Cdd:pfam06346  52 PGGTSIPPPPplpGAASIPPPPplpGSTGIPPPPplpGGAGIPPPPpplpGGAGVPPPPpplpGGPGIPPPppfPGGPGI 131

                          90
                  ....*....|....
gi 401782598  807 SRPPPGHGNRFPVP 820
Cdd:pfam06346 132 PPPPPGMGMPPPPP 145
PHA03378 PHA03378
EBNA-3B; Provisional
 741-828 3.84e-10

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 63.93  E-value: 3.84e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401782598 741 ANVSRQPG-DPSISRPPG-GPNVSRPPGGPGVS--RPPGGPGVSRPP-GGPGVSRPP-GGPGVSRPP-GGPGVSRPPPGH 813
Cdd:PHA03378 681 ANTMLPIQwAPGTMQPPPrAPTPMRPPAAPPGRaqRPAAATGRARPPaAAPGRARPPaAAPGRARPPaAAPGRARPPAAA 760

                         90
                 ....*....|....*
gi 401782598 814 GNRFPVPTYAAKQPA 828
Cdd:PHA03378 761 PGRARPPAAAPGAPT 775
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
750-829 1.88e-09

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 61.20  E-value: 1.88e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401782598 750 PSISRPPGGPNVSRPPGGPGVSRPPGGPGVSRPPGGPGVSRPPGGPGVSRPPGGPGVSRPPPGHGNRFPVPTYAAKQPAQ 829
Cdd:COG5164    6 PGKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQ 85
SAV_2336_NTERM NF041121
SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 ...
 741-824 2.11e-05

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


Pssm-ID: 469044 [Multi-domain]  Cd Length: 473  Bit Score: 48.07  E-value: 2.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401782598 741 ANVSRQPGDPSISRPPGGPNVSRPPGGPGVSRPPGGPGVSRPPGGPGVSRPPG-GPGVSRPPGGPGVSRPPPGHGNRFPV 819
Cdd:NF041121  12 AAQMGRAAAPPSPEGPAPTAASQPATPPPPAAPPSPPGDPPEPPAPEPAPLPApYPGSLAPPPPPPPGPAGAAPGAALPV 91


                 ....*
gi 401782598 820 PTYAA 824
Cdd:NF041121  92 RVPAP 96
SAV_2336_NTERM NF041121
SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 ...
 745-812 4.42e-03

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


Pssm-ID: 469044 [Multi-domain]  Cd Length: 473  Bit Score: 40.37  E-value: 4.42e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 401782598 745 RQPGDPSISRPPGGPnvSRPPGGPGVSRPPGGPGVSRPPGGPGVSRPPGGPGVSRPPGGPGVsRPPPG 812
Cdd:NF041121  37 TPPPPAAPPSPPGDP--PEPPAPEPAPLPAPYPGSLAPPPPPPPGPAGAAPGAALPVRVPAP-PALPN 101
EGF_2 pfam07974
EGF-like domain; This family contains EGF domains found in a variety of extracellular proteins.
 650-673 7.63e-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: 7.63e-03
                          10        20
                  ....*....|....*....|....*
gi 401782598  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 9.31e-94

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: 293.05  E-value: 9.31e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401782598  212 RYVELFIVVDKERYDMMGRNQTAVREEMIRLANYLDSMYIMLNIRIVLVGLEIWTDRNPINIIGGAGDVLGNFVQWREKF 291
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIDVSGDANDTLRNFLKWRQEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401782598  292 LITRWRHDSAQLVLKKGFGG-TAGMAFVGTVCSRSHAGGINVFGQITVETFASIVAHELGHNLGMNHDDG-RECFCG-AK 368
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFGGtTVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFnGGCKCPpGG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 401782598  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 2.26e-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: 291.83  E-value: 2.26e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401782598 212 RYVELFIVVDKERYDMMGRNQTAVREEMIRLANYLDSMYIMLNIRIVLVGLEIWTDRNPINIIGGAGDVLGNFVQWREKF 291
Cdd:cd04269    1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKISVSGDAGETLNRFLDWKRSN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401782598 292 LITRWRHDSAQLVLKKGF-GGTAGMAFVGTVCSRSHAGGINVFGQITVETFASIVAHELGHNLGMNHDDGrECFCGAKSC 370
Cdd:cd04269   81 LLPRKPHDNAQLLTGRDFdGNTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDG-GCTCGRSTC 159

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 401782598 371 IMNSGAS-GSRNFSSCSAEDFEKLTLNKGGSCLLN 404
Cdd:cd04269  160 IMAPSPSsLTDAFSNCSYEDYQKFLSRGGGQCLLN 194
ACR smart00608
ADAM Cysteine-Rich Domain;
500-636 3.94e-59

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 197.58  E-value: 3.94e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401782598   500 QNGYPCQNSKAYCYNGMCQYYDAQCQVIFGSKAKAAPRDCFIEVNSKGDRFGNCGFSGSEYKKCATGNALCGKLQCENVQ 579
Cdd:smart00608   1 QDGTPCDNGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 401782598   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 8.64e-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: 164.71  E-value: 8.64e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401782598  501 NGYPCQNSKAYCYNGMCQYYDAQCQVIFGSKAKAAPRDCFIEVNSKGDRFGNCGFSGSEYKKCATGNALCGKLQCENVQD 580
Cdd:pfam08516   1 DGTPCNNGQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQCTNVKE 80

                          90       100
                  ....*....|....*....|....*
gi 401782598  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 1.37e-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: 1.37e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401782598   44 EIITPWRLT--RERREALGPSSQ--QISYVIQAQGKQHIIHLERNTDLLPNDFVVYTYDKEGSLLSDHPNVQSHCHYRGY 119
Cdd:pfam01562   1 EVVIPVRLDpsRRRRSLASESTYldTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 401782598  120 VEGVQNSAVAVSACFGLRGLLHLENASFGIEPLHN----SSHFEHIFY 163
Cdd:pfam01562  81 VEGHPDSSVALSTCSGLRGFIRTENEEYLIEPLEKysreEGGHPHVVY 128
Disintegrin pfam00200
Disintegrin;
423-496 1.08e-36

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 132.36  E-value: 1.08e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 401782598  423 DPGEECDCGTAKECEVDPCCEGSTCKLKSFAECAYGDCCKDCQFLPGGSMCRGKTSECDVPEYCNGSSQFCPPD 496
Cdd:pfam00200   1 EEGEECDCGSLEECTNDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 423-498 2.34e-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: 128.58  E-value: 2.34e-35
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 401782598   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 7.42e-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: 7.42e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401782598 212 RYVELFIVVDKERYDMMGRNQTAVREEMIRLANYLDSMY----IMLNIRIVLVGLEIWTDRNPINIIG-GAGDVLGNFVQ 286
Cdd:cd04267    1 REIELVVVADHRMVSYFNSDENILQAYITELINIANSIYrstnLRLGIRISLEGLQILKGEQFAPPIDsDASNTLNSFSF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401782598 287 WREKFLItrwRHDSAQLVLKKGF--GGTAGMAFVGTVCSRSHAGGINVFGQITVETfASIVAHELGHNLGMNHDDGRECF 364
Cdd:cd04267   81 WRAEGPI---RHDNAVLLTAQDFieGDILGLAYVGSMCNPYSSVGVVEDTGFTLLT-ALTMAHELGHNLGAEHDGGDELA 156

                        170       180
                 ....*....|....*....|....*...
gi 401782598 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 1.24e-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: 111.18  E-value: 1.24e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401782598 212 RYVELFIVVDKERYDMMGRNQTavrEEMI-RLANYLDSMY----IMLNIRIVLVGLEIWTDRNP-INIIGGAGDVLGNFV 285
Cdd:cd04273    1 RYVETLVVADSKMVEFHHGEDL---EHYIlTLMNIVASLYkdpsLGNSINIVVVRLIVLEDEESgLLISGNAQKSLKSFC 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401782598 286 QWREK---------------FLITRwrHDsaqLVLKKGFGGTAGMAFVGTVCSRSHAGGINvfgQITVETFASIVAHELG 350
Cdd:cd04273   78 RWQKKlnppndsdpehhdhaILLTR--QD---ICRSNGNCDTLGLAPVGGMCSPSRSCSIN---EDTGLSSAFTIAHELG 149

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 401782598 351 HNLGMNHDD-GREC-FCGAKSCIMNS-GASGSRNF--SSCSAEDFEKLTLNKGGSCLL 403
Cdd:cd04273  150 HVLGMPHDGdGNSCgPEGKDGHIMSPtLGANTGPFtwSKCSRRYLTSFLDTGDGNCLL 207
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
211-383 1.04e-18

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 84.78  E-value: 1.04e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401782598  211 TRYVELFIVVDKERYDMMGRNqtAVREEMIRLANYLDS-MYIMLNIRIVLVGLEIWTDRNPINIIGG----AGDVLGNFV 285
Cdd:pfam13688   2 TRTVALLVAADCSYVAAFGGD--AAQANIINMVNTASNvYERDFNISLGLVNLTISDSTCPYTPPACstgdSSDRLSEFQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401782598  286 QWREkfLITRWRHDSAQLVLKKGFGGTaGMAFVGTVCSRSHAGGINVFGQITVE-----TFASIVAHELGHNLGMNHD-- 358
Cdd:pfam13688  80 DFSA--WRGTQNDDLAYLFLMTNCSGG-GLAWLGQLCNSGSAGSVSTRVSGNNVvvstaTEWQVFAHEIGHNFGAVHDcd 156

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 401782598  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 1.50e-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: 1.50e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401782598  237 EEMIRLANYLDSMY-IMLNIRIVLVGLEIWTDRNPINIIGGAGDVLGNFVQWrekfLITRWRH---DSAQLVLKKGFGGT 312
Cdd:pfam13582   1 ARIVSLVNRANTIYeRDLGIRLQLAAIIITTSADTPYTSSDALEILDELQEV----NDTRIGQygyDLGHLFTGRDGGGG 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 401782598  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 5.18e-15

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


Pssm-ID: 239800  Cd Length: 220  Bit Score: 75.08  E-value: 5.18e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401782598 213 YVELFIVVDKERYDMMGRNQtAVREEMIRLANYLDSMYIMLN---IRIVLVGLEIWTDRNPINIIGGAGD-------VLG 282
Cdd:cd04272    2 YPELFVVVDYDHQSEFFSNE-QLIRYLAVMVNAANLRYRDLKsprIRLLLVGITISKDPDFEPYIHPINYgyidaaeTLE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401782598 283 NFVQW-REK---------FLITR-----WRHDSAQLvlkkgfgGTAGMAFVGTVCSRSHAGginvFGQITVETFASI--V 345
Cdd:cd04272   81 NFNEYvKKKrdyfnpdvvFLVTGldmstYSGGSLQT-------GTGGYAYVGGACTENRVA----MGEDTPGSYYGVytM 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401782598 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 5.98e-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: 70.63  E-value: 5.98e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401782598 212 RYVELFIVVDKERYDmmgrnQTAVREEMIRLANYLDSMY-IMLNIRIVLVGLEIWTDRNpiniiggagdvlgnfvqwreK 290
Cdd:cd00203    1 KVIPYVVVADDRDVE-----EENLSAQIQSLILIAMQIWrDYLNIRFVLVGVEIDKADI--------------------A 55

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401782598 291 FLITRWRHDsaqlvlkkgfGGTAGMAFVGTVCSRSHAGGINVFGQITVETFASIVAHELGHNLGMNHDDGRECFCG---- 366
Cdd:cd00203   56 ILVTRQDFD----------GGTGGWAYLGRVCDSLRGVGVLQDNQSGTKEGAQTIAHELGHALGFYHDHDRKDRDDypti 125

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 401782598 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) ...
 747-820 4.76e-12

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: 64.89  E-value: 4.76e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401782598  747 PGDPSISRPP---GGPNVSRPP---GGPGVSRPP---GGPGVSRPP----GGPGVSRPP----GGPGVSRP---PGGPGV 806
Cdd:pfam06346  52 PGGTSIPPPPplpGAASIPPPPplpGSTGIPPPPplpGGAGIPPPPpplpGGAGVPPPPpplpGGPGIPPPppfPGGPGI 131

                          90
                  ....*....|....
gi 401782598  807 SRPPPGHGNRFPVP 820
Cdd:pfam06346 132 PPPPPGMGMPPPPP 145
PHA03378 PHA03378
EBNA-3B; Provisional
 741-828 3.84e-10

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 63.93  E-value: 3.84e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401782598 741 ANVSRQPG-DPSISRPPG-GPNVSRPPGGPGVS--RPPGGPGVSRPP-GGPGVSRPP-GGPGVSRPP-GGPGVSRPPPGH 813
Cdd:PHA03378 681 ANTMLPIQwAPGTMQPPPrAPTPMRPPAAPPGRaqRPAAATGRARPPaAAPGRARPPaAAPGRARPPaAAPGRARPPAAA 760

                         90
                 ....*....|....*
gi 401782598 814 GNRFPVPTYAAKQPA 828
Cdd:PHA03378 761 PGRARPPAAAPGAPT 775
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
750-829 1.88e-09

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 61.20  E-value: 1.88e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401782598 750 PSISRPPGGPNVSRPPGGPGVSRPPGGPGVSRPPGGPGVSRPPGGPGVSRPPGGPGVSRPPPGHGNRFPVPTYAAKQPAQ 829
Cdd:COG5164    6 PGKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQ 85
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
747-829 1.93e-09

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 60.81  E-value: 1.93e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401782598 747 PGDPSISRPPGGPNVSRPPGGPGVSRPPGGPGVSRPPGGPGVSRPPGGPGVSRPPGGPGVSRPPPGHGNRFPVPTYAAKQ 826
Cdd:COG5164   12 SDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQGGTR 91


                 ...
gi 401782598 827 PAQ 829
Cdd:COG5164   92 PAG 94
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
742-828 2.01e-09

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 60.81  E-value: 2.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401782598 742 NVSRQPGDPSISRPPGGPNVSRPPGGPGVSRPPGGPGVSRPPGGPGVSRPPGGPGVSRPPGGPGVSRPPPGHGNRFPVPT 821
Cdd:COG5164   16 GVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQGGTRPAGN 95


                 ....*..
gi 401782598 822 YAAKQPA 828
Cdd:COG5164   96 TGGTTPA 102
Reprolysin_2 pfam13574
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 234-386 3.64e-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: 57.25  E-value: 3.64e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401782598  234 AVREEMIRLANYLDSMYIM--LNIRIVLVGLEIWTDRNPINIIGGAGDVLGNFVQWREKFLiTRWR----HDSAQLVLKK 307
Cdd:pfam13574   2 NVTENLVNVVNRVNQIYEPddININGGLVNPGEIPATTSASDSGNNYCNSPTTIVRRLNFL-SQWRgeqdYCLAHLVTMG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401782598  308 GF-GGTAGMAFVGTVC-----SRSHAGGINV---FGQITVETFA-SIVAHELGHNLGMNHDDGRECFC--------GAKS 369
Cdd:pfam13574  81 TFsGGELGLAYVGQICqkgasSPKTNTGLSTttnYGSFNYPTQEwDVVAHEVGHNFGATHDCDGSQYAssgcernaATSV 160

                         170       180
                  ....*....|....*....|....
gi 401782598  370 C------IMN-SGASGSRNFSSCS 386
Cdd:pfam13574 161 CsangsfIMNpASKSNNDLFSPCS 184
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
744-827 3.79e-09

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 60.04  E-value: 3.79e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401782598 744 SRQPGDPSISRPPGGPNVSRPPGGPGVSRPPGGPGVSRPPGGPGVSRPPGGPGVSRPPGGPGVSRPPPGHGNRFPVPTYA 823
Cdd:COG5164   54 TTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGS 133


                 ....
gi 401782598 824 AKQP 827
Cdd:COG5164  134 TTPP 137
Reprolysin_4 pfam13583
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 212-390 6.36e-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: 6.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401782598  212 RYVELFIVVDKERYDMMGrNQTAVREEMIRLANYLDSMY-IMLNIRIVLVGLE--IWTDRNP----INIIGGAgdvLGNF 284
Cdd:pfam13583   3 RVYRVAVATDCTYSASFG-SVDELRANINATVTTANEVYgRDFNVSLALISDRdvIYTDSSTdsfnADCSGGD---LGNW 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401782598  285 VQWRekflITRWR----HDSAQLVLKKG-FGGTAGMAFVGTVCSRSH--AGGiNVFGQITVETfaSIVAHELGHNLGMNH 357
Cdd:pfam13583  79 RLAT----LTSWRdslnYDLAYLTLMTGpSGQNVGVAWVGALCSSARqnAKA-SGVARSRDEW--DIFAHEIGHTFGAVH 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 401782598  358 DDGRECfCGAK--------SCIMNSGASGSR-NFSSCSAEDF 390
Cdd:pfam13583 152 DCSSQG-EGLSsstedgsgQTIMSYASTASQtAFSPCTIRNI 192
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
744-828 8.25e-09

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 58.89  E-value: 8.25e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401782598 744 SRQPGDPSISRPPGGPNVSRPPGGPGVSRPPGGPGVSRPPGGPGVSRPPGGPGVSRPPGGPGVSRPPPGHGNRFPVPTYA 823
Cdd:COG5164   45 TRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGG 124


                 ....*
gi 401782598 824 AKQPA 828
Cdd:COG5164  125 STTPP 129
PHA03378 PHA03378
EBNA-3B; Provisional
 748-820 1.65e-07

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 55.07  E-value: 1.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401782598 748 GDPSISRPP-GGPNVSRPP-GGPGVSRPP-GGPGVSRPP-GGPGVSRPP-GGPGVSRPP-GGPGVSRP-PPGHGNrfPVP 820
Cdd:PHA03378 709 APPGRAQRPaAATGRARPPaAAPGRARPPaAAPGRARPPaAAPGRARPPaAAPGRARPPaAAPGAPTPqPPPQAP--PAP 786
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
 733-828 2.19e-07

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


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 51.58  E-value: 2.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401782598  733 QMSDGRNQANVSRQPGDPSISRPPGGPNVSRPPGGPGVSRPPGGPGVSRPPGGPGVSRP-PGGPGVSRPPGGPGVSRPPP 811
Cdd:pfam15240  38 QSQQGGQGPQGPPPGGFPPQPPASDDPPGPPPPGGPQQPPPQGGKQKPQGPPPQGGPRPpPGKPQGPPPQGGNQQQGPPP 117

                          90
                  ....*....|....*..
gi 401782598  812 GHGNRFPVPTYAAKQPA 828
Cdd:pfam15240 118 PGKPQGPPPQGGGPPPQ 134
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
 747-828 2.67e-07

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


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 51.19  E-value: 2.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401782598  747 PGDPSISRPPGGPNVSRPPGGPGVSRPPGGPGVSRP-PGGPGVSRPPGGPGVSRPPGGPGVSRPPPGHGNRFPVPTYAAK 825
Cdd:pfam15240  61 SDDPPGPPPPGGPQQPPPQGGKQKPQGPPPQGGPRPpPGKPQGPPPQGGNQQQGPPPPGKPQGPPPQGGGPPPQGGNQQG 140


                  ...
gi 401782598  826 QPA 828
Cdd:pfam15240 141 PPP 143
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 755-805 3.01e-07

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: 47.87  E-value: 3.01e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 401782598  755 PPGGPNVSRPPGGPGVSRPPGGPGVSRPPGGPGVSRPPGGPGVSRPPGGPG 805
Cdd:pfam01391   5 PPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
756-829 3.14e-07

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 53.88  E-value: 3.14e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 401782598 756 PGGPNVSRPPGGPGVSRPPGGPGVSRPPGGPGVSRPPGGPGVSRPPGGPGVSRPP-PGHGNRfPVPTYAAKQPAQ 829
Cdd:COG5164    3 LYGPGKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAgNTGGTR-PAGNQGATGPAQ 76
PBP1 COG5180
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ...
 723-830 4.12e-07

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


Pssm-ID: 444064 [Multi-domain]  Cd Length: 548  Bit Score: 53.53  E-value: 4.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401782598 723 LRKTFRKKRSQMSDGRNQANVSRQPGDPSISRPPGGPNVSRPPGG--PGVSRPPGGPGVSR--PPGGPGVSRPPGGPGVS 798
Cdd:COG5180  310 APPATRPVRPPGGARDPGTPRPGQPTERPAGVPEAASDAGQPPSAypPAEEAVPGKPLEQGapRPGSSGGDGAPFQPPNG 389

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 401782598 799 RP---PGGPGVSRPPPGHGNRF------PVPTYAAKQPAQF 830
Cdd:COG5180  390 APqpgLGRRGAPGPPMGAGDLVqaaldgGGRETASLGGAAG 430
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 755-810 5.69e-07

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: 47.10  E-value: 5.69e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 401782598  755 PPGGPNVSRPPGGPGVSRPPGGPGvsrPPGGPGVSRPPGGPGVSRPPGGPGVSRPP 810
Cdd:pfam01391   2 PPGPPGPPGPPGPPGPPGPPGPPG---PPGPPGEPGPPGPPGPPGPPGPPGAPGAP 54
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 747-804 1.96e-06

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: 45.56  E-value: 1.96e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 401782598  747 PGDPSISRPPGGPNVSRPPGGPGvsrPPGGPGvsrPPGGPGVSRPPGGPGVSRPPGGP 804
Cdd:pfam01391   6 PGPPGPPGPPGPPGPPGPPGPPG---PPGEPG---PPGPPGPPGPPGPPGAPGAPGPP 57
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
 216-401 2.12e-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: 2.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401782598 216 LFIVVDKERYDMMGRNQT-AVREEMIRLANYLDSMY--------IMLNIRIVLVGLEIWTDRNPINiiGGAGDVLGNFVQ 286
Cdd:cd04270    5 LLLVADHRFYKYMGRGEEeTTINYLISHIDRVDDIYrntdwdggGFKGIGFQIKRIRIHTTPDEVD--PGNKFYNKSFPN 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401782598 287 W-REKFLITRWRHDS------AQLVLKKGF-GGTAGMAFVGTVCSRSHaGGI---------------NVfGQITVETFAS 343
Cdd:cd04270   83 WgVEKFLVKLLLEQFsddvclAHLFTYRDFdMGTLGLAYVGSPRDNSA-GGIcekayyysngkkkylNT-GLTTTVNYGK 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 401782598 344 ---------IVAHELGHNLGMNHD-DGRECFCGAK---SCIMNSGA-SGS----RNFSSCSAEDFEKLTLNKGGSC 401
Cdd:cd04270  161 rvptkesdlVTAHELGHNFGSPHDpDIAECAPGESqggNYIMYARAtSGDkennKKFSPCSKKSISKVLEVKSNSC 236
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
742-829 2.51e-06

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 50.80  E-value: 2.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401782598 742 NVSRQPGDPSISRPPGgPNVSRPPGGPGvsrPPGGPGVSRPPGGPGVSRPPGGPGVSRPPGGPGVSRPPPGHGNRFPVPT 821
Cdd:COG5164  131 GGSTTPPGDGGSTPPG-PGSTGPGGSTT---PPGDGGSTTPPGPGGSTTPPDDGGSTTPPNKGETGTDIPTGGTPRQGPD 206


                 ....*...
gi 401782598 822 YAAKQPAQ 829
Cdd:COG5164  207 GPVKKDDK 214
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 730-824 3.37e-06

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 50.94  E-value: 3.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401782598  730 KRSQMSDGRNQANVSRQPGDPSISRPPGGPNVSRPPGGPgvsRPPGGPGVSRPPGGPGVSRPPGGPGV--SRPPGGP--- 804
Cdd:PHA03307  848 ARSSESSKSKPAAAGGRARGKNGRRRPRPPEPRARPGAA---APPKAAAAAPPAGAPAPRPRPAPRVKlgPMPPGGPdpr 924

                          90       100
                  ....*....|....*....|...
gi 401782598  805 -GVSRPPPG--HGnrfPVPTYAA 824
Cdd:PHA03307  925 gGFRRVPPGdlHT---PAPSAAA 944
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
 735-820 3.41e-06

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


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 48.11  E-value: 3.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401782598  735 SDGRNQANVSRQPGDPSISRPPGGPNVSRPPGGPGVSRPP--GGPGVSRPPGGPGVSRPPGGPGVSRPPGGPGVSRPPPG 812
Cdd:pfam15240  20 SEDVSQEDSPSLISEEEGQSQQGGQGPQGPPPGGFPPQPPasDDPPGPPPPGGPQQPPPQGGKQKPQGPPPQGGPRPPPG 99


                  ....*...
gi 401782598  813 HGNRFPVP 820
Cdd:pfam15240 100 KPQGPPPQ 107
PBP1 COG5180
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ...
 738-830 6.73e-06

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


Pssm-ID: 444064 [Multi-domain]  Cd Length: 548  Bit Score: 49.68  E-value: 6.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401782598 738 RNQANVSRQPGDPSIsRPPGG---------PNVSR-----PPGGPGVSRPPGG--PGVSRPPGGPGVSR--PPGGPGVSR 799
Cdd:COG5180  303 DVKGVASAPPATRPV-RPPGGardpgtprpGQPTErpagvPEAASDAGQPPSAypPAEEAVPGKPLEQGapRPGSSGGDG 381

                         90       100       110
                 ....*....|....*....|....*....|.
gi 401782598 800 PPGGPGVSRPPPGHGNRfPVPTYAAKQPAQF 830
Cdd:COG5180  382 APFQPPNGAPQPGLGRR-GAPGPPMGAGDLV 411
PHA03378 PHA03378
EBNA-3B; Provisional
 743-823 6.84e-06

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 50.07  E-value: 6.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401782598 743 VSRQPGDPSISRPPGGPNVSRPPGGPGVSRPPGGPGVSRPPG-GPGVSRPPGGPGVS--RPPGGPGVSRPPPGHGNRFPV 819
Cdd:PHA03378 657 VEITPYKPTWTQIGHIPYQPSPTGANTMLPIQWAPGTMQPPPrAPTPMRPPAAPPGRaqRPAAATGRARPPAAAPGRARP 736


                 ....
gi 401782598 820 PTYA 823
Cdd:PHA03378 737 PAAA 740
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 764-812 7.67e-06

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: 44.02  E-value: 7.67e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 401782598  764 PPGGPGvsrPPGGPGvsrPPGGPGVSRPPGGPGVSRPPGGPGvSRPPPG 812
Cdd:pfam01391   2 PPGPPG---PPGPPG---PPGPPGPPGPPGPPGPPGEPGPPG-PPGPPG 43
PHA03381 PHA03381
tegument protein VP22; Provisional
 701-829 1.10e-05

tegument protein VP22; Provisional


Pssm-ID: 177618 [Multi-domain]  Cd Length: 290  Bit Score: 48.08  E-value: 1.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401782598 701 VFFFLIVPLVAAAIFLFikrDELRKTFRKKRSQMSdGRNQANVSRQPGDPSISRPPGGPNVS----RPPGGPGVSRPPGG 776
Cdd:PHA03381  21 VYYDFISPDASPARVSF---EEPADRARRGAGQAR-GRSQAERRFHHYDEARADYPYYTGSSsedeRPADPRPSRRPHAQ 96

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 401782598 777 PGVSrppgGPGVSRPPGGPGVSRPPGGPGVSRPPPGHGNRFPVPTYAAKQPAQ 829
Cdd:PHA03381  97 PEAS----GPGPARGARGPAGSRGRGRRAESPSPRDPPNPKGASAPRGRKSAC 145
Drf_FH1 pfam06346
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs) ...
 747-811 1.33e-05

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


Pssm-ID: 461881 [Multi-domain]  Cd Length: 157  Bit Score: 46.02  E-value: 1.33e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 401782598  747 PGDPSISRPPGGPNVSRP--PGGPGVSRPP---GGPGVSRPP---GGPGVSRPP---GGPGVSRPP---GGPGVSRPPP 811
Cdd:pfam06346  20 CIPTPPPLPGGGGPPPPPplPGSAAIPPPPplpGGTSIPPPPplpGAASIPPPPplpGSTGIPPPPplpGGAGIPPPPP 98
SAV_2336_NTERM NF041121
SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 ...
 741-824 2.11e-05

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


Pssm-ID: 469044 [Multi-domain]  Cd Length: 473  Bit Score: 48.07  E-value: 2.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401782598 741 ANVSRQPGDPSISRPPGGPNVSRPPGGPGVSRPPGGPGVSRPPGGPGVSRPPG-GPGVSRPPGGPGVSRPPPGHGNRFPV 819
Cdd:NF041121  12 AAQMGRAAAPPSPEGPAPTAASQPATPPPPAAPPSPPGDPPEPPAPEPAPLPApYPGSLAPPPPPPPGPAGAAPGAALPV 91


                 ....*
gi 401782598 820 PTYAA 824
Cdd:NF041121  92 RVPAP 96
PHA03378 PHA03378
EBNA-3B; Provisional
 726-813 2.62e-05

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 48.14  E-value: 2.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401782598 726 TFRKKRSQMSDGRNQanvsRQPGDPSISRPP-GGPNVSRPP-GGPGVSRPP----GGPGVSRPPGGPGVS--RPPGGPGV 797
Cdd:PHA03378 721 TGRARPPAAAPGRAR----PPAAAPGRARPPaAAPGRARPPaAAPGRARPPaaapGAPTPQPPPQAPPAPqqRPRGAPTP 796

                         90       100
                 ....*....|....*....|.
gi 401782598 798 SRPPGGPGVS-----RPPPGH 813
Cdd:PHA03378 797 QPPPQAGPTSmqlmpRAAPGQ 817
ZnMc_ADAM_fungal cd04271
Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A ...
 310-386 3.10e-05

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


Pssm-ID: 239799 [Multi-domain]  Cd Length: 228  Bit Score: 46.26  E-value: 3.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401782598 310 GGTAGMAFVGTVCSRSHAG-------GINVFGQITVETfaSIVAHELGHNLGMNHD----------DGRECFC--GAKSC 370
Cdd:cd04271  109 GSEVGVAWLGQLCRTGASDqgnetvaGTNVVVRTSNEW--QVFAHEIGHTFGAVHDctsgtcsdgsVGSQQCCplSTSTC 186

                         90       100
                 ....*....|....*....|...
gi 401782598 371 ------IMN-SGASGSRNFSSCS 386
Cdd:cd04271  187 dangqyIMNpSSSSGITEFSPCT 209
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
744-814 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 401782598 744 SRQPGDPSISRPPGGPNVSRPPGGPGVSRPPGGPGVSRPPG----------------GPGVSRPPG----GPGVSRPPGG 803
Cdd:COG5164   81 TTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDdggsttppsggsttppGDGGSTPPGpgstGPGGSTTPPG 160

                         90
                 ....*....|.
gi 401782598 804 PGVSRPPPGHG 814
Cdd:COG5164  161 DGGSTTPPGPG 171
PHA03247 PHA03247
large tegument protein UL36; Provisional
 724-829 5.14e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.24  E-value: 5.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401782598  724 RKTFRKKRSQMSDGRNQANVSRQPGDPSISRPPGGPNVSRPPGGPGVSRPPGGPGVSRPPGGPGVSRPPGGPGVSRPPGG 803
Cdd:PHA03247 2781 RRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGG 2860

                          90       100
                  ....*....|....*....|....*.
gi 401782598  804 PGVSRPPPGHGNrfPVPTYAAKQPAQ 829
Cdd:PHA03247 2861 DVRRRPPSRSPA--AKPAAPARPPVR 2884
PHA03247 PHA03247
large tegument protein UL36; Provisional
 731-828 6.57e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.86  E-value: 6.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401782598  731 RSQMSDGRNQANVSRQPGDPSISrPPGGPNVSRPPGGPGVSRPPGGPGVSRP--PGGPGVSRPPGGPGVSRPPGGPGVSR 808
Cdd:PHA03247 2585 RARRPDAPPQSARPRAPVDDRGD-PRGPAPPSPLPPDTHAPDPPPPSPSPAAnePDPHPPPTVPPPERPRDDPAPGRVSR 2663

                          90       100
                  ....*....|....*....|....
gi 401782598  809 P----PPGHGNRFPVPTYAAKQPA 828
Cdd:PHA03247 2664 PrrarRLGRAAQASSPPQRPRRRA 2687
PBP1 COG5180
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ...
 744-828 9.56e-05

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


Pssm-ID: 444064 [Multi-domain]  Cd Length: 548  Bit Score: 45.82  E-value: 9.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401782598 744 SRQPGDPSISR--PPGGPNVSRPPGGPGVSRP---PGGPGVSRPPGGPGVSRPPGGPGVSR------PPGGPGVSRPPPG 812
Cdd:COG5180  360 EAVPGKPLEQGapRPGSSGGDGAPFQPPNGAPqpgLGRRGAPGPPMGAGDLVQAALDGGGRetaslgGAAGGAGQGPKAD 439

                         90
                 ....*....|....*.
gi 401782598 813 HGNRFPVPTYAAKQPA 828
Cdd:COG5180  440 FVPGDAESVSGPAGLA 455
Drf_FH1 pfam06346
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs) ...
 747-811 1.37e-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: 43.32  E-value: 1.37e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 401782598  747 PGDPS-ISRPPG--GPNVSRPPGGPGVSRPP---GGPGVSRPPGGPGVSRPPGGPGVsrpPGGPGVSRPPP 811
Cdd:pfam06346   7 PGDSStIPLPPGacIPTPPPLPGGGGPPPPPplpGSAAIPPPPPLPGGTSIPPPPPL---PGAASIPPPPP 74
PHA03247 PHA03247
large tegument protein UL36; Provisional
 734-828 3.75e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.54  E-value: 3.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401782598  734 MSDGRNQANVSRQPGDPSISRPPGGPNVSRPPGGPGVSRP----PGGPGVSRPPGGP-GVSRPPGGPGVSRPPGGPGVSR 808
Cdd:PHA03247  368 LSAGRHHPKRASLPTRKRRSARHAATPFARGPGGDDQTRPaapvPASVPTPAPTPVPaSAPPPPATPLPSAEPGSDDGPA 447

                          90       100
                  ....*....|....*....|
gi 401782598  809 PPPghGNRFPVPTYAAKQPA 828
Cdd:PHA03247  448 PPP--ERQPPAPATEPAPDD 465
DUF3729 pfam12526
Protein of unknown function (DUF3729); This family of proteins is found in viruses. Proteins ...
 747-812 4.94e-04

Protein of unknown function (DUF3729); This family of proteins is found in viruses. Proteins in this family are typically between 145 and 1707 amino acids in length. The family is found in association with pfam01443, pfam01661, pfam05417, pfam01660, pfam00978. There is a single completely conserved residue L that may be functionally important.


Pssm-ID: 372164 [Multi-domain]  Cd Length: 115  Bit Score: 40.45  E-value: 4.94e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 401782598  747 PGDPSISRPPGGP----NVSRPPGGPGVSRPPGGPGVSRPPGGPGVSRPPGGPGVSR--PPGGPGVSRPPPG 812
Cdd:pfam12526  34 SAHPDPPPPVGDPrppvVDTPPPVSAVWVLPPPSEPAAPEPDLVPPVTGPAGPPSPLapPAPAQKPPLPPPR 105
PHA03264 PHA03264
envelope glycoprotein D; Provisional
 745-811 5.65e-04

envelope glycoprotein D; Provisional


Pssm-ID: 223029 [Multi-domain]  Cd Length: 416  Bit Score: 43.46  E-value: 5.65e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 401782598 745 RQPGDPSI-SRPPGGPNVSRPPGGPGVSRPPGgPGVSRPPGGPG---VSRPPG-GPGVSRP---PGGPGVSRPPP 811
Cdd:PHA03264 276 APPGDDRPeAKPEPGPVEDGAPGRETGGEGEG-PEPAGRDGAAGgepKPGPPRpAPDADRPegwPSLEAITFPPP 349
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 750-812 6.58e-04

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 43.60  E-value: 6.58e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 401782598  750 PSISRPPGGPNVSRPPGGPGVSRP--PGGPGVSRPPGGPGVSRPPGGPGVSRPPGGP-GVSRPPPG 812
Cdd:pfam03154 443 PAASHPPTSGLHQVPSQSPFPQHPfvPGGPPPITPPSGPPTSTSSAMPGIQPPSSASvSSSGPVPA 508
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 744-829 6.81e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.44  E-value: 6.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401782598 744 SRQPGDPSISRPPGGPNVSRPPGGPGVSRPPGGPGVSRPPGGPGVSRPPGGPGVSRPPGGPGVSRPPPGHGNRFPVPTYA 823
Cdd:PRK07764 618 PAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAA 697


                 ....*.
gi 401782598 824 AKQPAQ 829
Cdd:PRK07764 698 PAQPAP 703
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 732-829 8.29e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.05  E-value: 8.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401782598 732 SQMSDGRNQANVSRQPGDPSISRPPGGPnvsrPPGGPGVSRPPGGPGVSRPPGGPGVSRPPGGPGVSRPPGGPGVSRPPP 811
Cdd:PRK07764 592 PGAAGGEGPPAPASSGPPEEAARPAAPA----APAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGD 667

                         90
                 ....*....|....*...
gi 401782598 812 GHGNRFPVPTYAAKQPAQ 829
Cdd:PRK07764 668 GWPAKAGGAAPAAPPPAP 685
MISS pfam15822
MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic ...
 755-828 9.92e-04

MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic MAPK-interacting and spindle-stabilising protein-like proteins. MISS is rich in prolines and has four potential MAPK-phosphorylation sites, a MAPK-docking site, a PEST sequence (PEST motif) and a bipartite nuclear localization signal. The endogenous protein accumulates during mouse meiotic maturation and is found as discrete dots on the MII spindle. MISS is the first example of a physiological MAPK-substrate that is stabilized in MII that specifically regulates MII spindle integrity during the CSF arrest.


Pssm-ID: 318115 [Multi-domain]  Cd Length: 238  Bit Score: 41.90  E-value: 9.92e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 401782598  755 PPGGPNVSRPPGGPgvsrPPGGPGvSRPPGGPGVSrPPGGPG---VSRPPGGPGVSRPPPGHGNRFPVPTYAAKQPA 828
Cdd:pfam15822  63 APTGMYPSIPLTGP----SPGPPA-PFPPSGPSCP-PPGGPYpapTVPGPGPIGPYPTPNMPFPELPRPYGAPTDPA 133
FAP pfam07174
Fibronectin-attachment protein (FAP); This family contains bacterial fibronectin-attachment ...
 755-827 1.26e-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: 41.84  E-value: 1.26e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 401782598  755 PPGGPNVSRPPGGPGVSRPPGGPGVSRPPGgpgvsrPPGGPGVSRPPGGPGVSRPPPGHGNRFPVPtyaAKQP 827
Cdd:pfam07174  45 PPPPSTATAPPAPPPPPPAPAAPAPPPPPA------APNAPNAPPPPADPNAPPPPPADPNAPPPP---AVDP 108
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 735-829 1.47e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 42.28  E-value: 1.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401782598 735 SDGRNQANVSRQPGDPSISRPPGGPNVSRPPGGPGVSRPPGGPGVSRPPGGPGVSRPPGGPGVSRPPGGPGVSRPPPGHG 814
Cdd:PRK07764 618 PAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAA 697

                         90
                 ....*....|....*
gi 401782598 815 NRFPVPTYAAKQPAQ 829
Cdd:PRK07764 698 PAQPAPAPAATPPAG 712
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 773-813 1.64e-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: 37.47  E-value: 1.64e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 401782598  773 PPGGPGvsrPPGGPGvsrPPGGPGVSRPPGGPGVSRP--PPGH 813
Cdd:pfam01391   2 PPGPPG---PPGPPG---PPGPPGPPGPPGPPGPPGEpgPPGP 38
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 731-844 1.89e-03

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 42.06  E-value: 1.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401782598  731 RSQMSDGRNQANVSRQPGDPSISRPPGGPNVSRPPGGPGVSR------PPGGPGVSrPPGGPGVSRPPGGPgvsRPPGGP 804
Cdd:pfam03154 152 QDNESDSDSSAQQQILQTQPPVLQAQSGAASPPSPPPPGTTQaatagpTPSAPSVP-PQGSPATSQPPNQT---QSTAAP 227

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 401782598  805 G--VSRPPPGHGNRFPVPtYAAKQPAqfpsRPPPPQPKISSQ 844
Cdd:pfam03154 228 HtlIQQTPTLHPQRLPSP-HPPLQPM----TQPPPPSQVSPQ 264
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 744-828 3.26e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.12  E-value: 3.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401782598 744 SRQPGDPSISRPPGGPNVSRPPGGPGVSRPPGGPGVSRPPGGPGVSRPPGGPgvSRPPGGPGVSRPPPGHGNRFPVPTYA 823
Cdd:PRK07764 694 AGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEP--DDPPDPAGAPAQPPPPPAPAPAAAPA 771


                 ....*
gi 401782598 824 AKQPA 828
Cdd:PRK07764 772 AAPPP 776
ZnMc_MMP_like cd04268
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ...
 331-357 3.29e-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: 3.29e-03
                         10        20
                 ....*....|....*....|....*..
gi 401782598 331 NVFGQITVETFASIVAHELGHNLGMNH 357
Cdd:cd04268   84 SSFVEYSGARLRNTAEHELGHALGLRH 110
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 741-828 4.36e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 40.74  E-value: 4.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401782598 741 ANVSRQPGDPSISRPPGGPNVSRPPGGPGVSRPPGGPGVSRPPGGPgvSRPPGGPGVSRPPGGPGVSRPPPGHGNRFPVP 820
Cdd:PRK07764 700 QPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEP--DDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPS 777


                 ....*...
gi 401782598 821 TYAAKQPA 828
Cdd:PRK07764 778 PPSEEEEM 785
SAV_2336_NTERM NF041121
SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 ...
 745-812 4.42e-03

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


Pssm-ID: 469044 [Multi-domain]  Cd Length: 473  Bit Score: 40.37  E-value: 4.42e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 401782598 745 RQPGDPSISRPPGGPnvSRPPGGPGVSRPPGGPGVSRPPGGPGVSRPPGGPGVSRPPGGPGVsRPPPG 812
Cdd:NF041121  37 TPPPPAAPPSPPGDP--PEPPAPEPAPLPAPYPGSLAPPPPPPPGPAGAAPGAALPVRVPAP-PALPN 101
Peptidase_M54 cd11375
Peptidase family M54, also called archaemetzincins or archaelysins; Peptidase M54 ...
 345-392 5.32e-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: 5.32e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 401782598 345 VAHELGHNLGMNHddgrecfCGAKSCIMnsgasgsrNFSSCSAEDFEK 392
Cdd:cd11375  127 AVHELGHLFGLDH-------CPYYACVM--------NFSNSLEETDRK 159
PHA03264 PHA03264
envelope glycoprotein D; Provisional
 749-827 5.84e-03

envelope glycoprotein D; Provisional


Pssm-ID: 223029 [Multi-domain]  Cd Length: 416  Bit Score: 39.99  E-value: 5.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401782598 749 DPSIS----RPPGGPNV-SRPPGGPGVSRPPGGPGVSRPPGgPGVSRPPGGPG---VSRPPG-GPGVSRP---PPGHGNR 816
Cdd:PHA03264 267 PPAPSggspAPPGDDRPeAKPEPGPVEDGAPGRETGGEGEG-PEPAGRDGAAGgepKPGPPRpAPDADRPegwPSLEAIT 345

                         90
                 ....*....|.
gi 401782598 817 FPVPTYAAKQP 827
Cdd:PHA03264 346 FPPPTPATPAV 356
EGF_2 pfam07974
EGF-like domain; This family contains EGF domains found in a variety of extracellular proteins.
 650-673 7.63e-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: 7.63e-03
                          10        20
                  ....*....|....*....|....*
gi 401782598  650 CHGHGVCNS-NKNCHCEDGWAPPHC 673
Cdd:pfam07974   2 CSGRGTCVNqCGKCVCDSGYQGATC 26
MISS pfam15822
MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic ...
 741-820 8.15e-03

MAPK-interacting and spindle-stabilising protein-like; MISS is a family of eukaryotic MAPK-interacting and spindle-stabilising protein-like proteins. MISS is rich in prolines and has four potential MAPK-phosphorylation sites, a MAPK-docking site, a PEST sequence (PEST motif) and a bipartite nuclear localization signal. The endogenous protein accumulates during mouse meiotic maturation and is found as discrete dots on the MII spindle. MISS is the first example of a physiological MAPK-substrate that is stabilized in MII that specifically regulates MII spindle integrity during the CSF arrest.


Pssm-ID: 318115 [Multi-domain]  Cd Length: 238  Bit Score: 38.81  E-value: 8.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401782598  741 ANVSRQPGDPSISRPPGG--PNVSRPPGGPG--VSRPPGGPGVSRPPG--GPGVSRPPGGPGVSRPPGGPGVSRPPP-GH 813
Cdd:pfam15822 100 APTVPGPGPIGPYPTPNMpfPELPRPYGAPTdpAAAAPSGPWGSMSSGpwAPGMGGQYPAPNMPYPSPGPYPAVPPPqSP 179


                  ....*..
gi 401782598  814 GNRFPVP 820
Cdd:pfam15822 180 GAAPPVP 186
PHA03247 PHA03247
large tegument protein UL36; Provisional
 747-832 9.28e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 39.92  E-value: 9.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401782598  747 PGDPSISRPPGGPnVSRPPGgPGVS----RPPGGPGVSRP--PGGPGVSRPPGGPGVSRPPGGPGVSRPPPG---HGNRF 817
Cdd:PHA03247 2561 PAAPDRSVPPPRP-APRPSE-PAVTsrarRPDAPPQSARPraPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSpspAANEP 2638

                          90
                  ....*....|....*
gi 401782598  818 PVPTYAAKQPAQFPS 832
Cdd:PHA03247 2639 DPHPPPTVPPPERPR 2653
 
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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