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Conserved domains on  [gi|195232759|ref|NP_001124175|]
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disintegrin and metalloproteinase domain-containing protein 29 preproprotein [Homo sapiens]

Protein Classification

disintegrin and metalloproteinase domain-containing protein( domain architecture ID 10480592)

disintegrin and metalloproteinase domain-containing protein also contains an ADAM domain and belongs to the ADAM family of membrane-anchored metalloproteases; ADAMs (A Disintegrin And Metalloprotease) are glycoproteins that play roles in cell signaling, cell fusion, and cell-cell interactions

Graphical summary

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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 ...
 198-386 9.84e-67

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: 220.18  E-value: 9.84e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759 198 RIVEIVVVIDNYLYIRYERNDSKLLEDLYVIVNIVDSILDVIGVKVLLFGLEIWTNKNLI-VVDDVRKSVHLYCKWKSEN 276
Cdd:cd04269    1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKIsVSGDAGETLNRFLDWKRSN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759 277 ITPRMQHDTSHLFTTLGLRG-LSGIGAFRGMCTPHRSCAIVTFMNKTLGTFSIAVAHHLGHNLGMNHDEDTCRCSQPRCI 355
Cdd:cd04269   81 LLPRKPHDNAQLLTGRDFDGnTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRSTCI 160

                        170       180       190
                 ....*....|....*....|....*....|...
gi 195232759 356 MHEGNPPITK-FSNCSYGDFWEYTVER-TKCLL 386
Cdd:cd04269  161 MAPSPSSLTDaFSNCSYEDYQKFLSRGgGQCLL 193
ACR smart00608
ADAM Cysteine-Rich Domain;
483-618 3.43e-55

ADAM Cysteine-Rich Domain;


:

Pssm-ID: 214743  Cd Length: 137  Bit Score: 186.41  E-value: 3.43e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759   483 DGIPCK-ERGYCYEKSCHDRNEQCRRIFGAGANTASETCYKELNTLGDRVGHCGIKNATYIKCNISDVQCGRIQCENVTE 561
Cdd:smart00608   2 DGTPCDnGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVSE 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 195232759   562 IPNMSDHTTVHWARFNDIMCWSTDYHLGMKgPDIGEVKDGTECGIDHICIHRHCVHI 618
Cdd:smart00608  82 LPLLGEHATVIYSNIGGLVCWSLDYHLGTD-PDIGMVKDGTKCGPGKVCINGQCVDV 137
Disintegrin pfam00200
Disintegrin;
406-478 1.32e-35

Disintegrin;


:

Pssm-ID: 459709  Cd Length: 74  Bit Score: 128.90  E-value: 1.32e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 195232759  406 EEGEECDCGPLKHCAKDPCCL-SNCTLTDGSTCAFGLCCKDCKFLPSGKVCRKEVNECDLPEWCNGTSHKCPDD 478
Cdd:pfam00200   1 EEGEECDCGSLEECTNDPCCDaKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 32-150 1.26e-29

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: 113.95  E-value: 1.26e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759   32 DVVIPVRITG------TTRGMTPPGWLSYILPFGGQKHIIHIKVKKLLFSKHLPVFTYTDQGAILEDQPFVQNNCYYHGY 105
Cdd:pfam01562   1 EVVIPVRLDPsrrrrsLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 195232759  106 VEGDPESLVSLSTCfGGFQGILQINDFAYEIKPLAF----STTFEHLVY 150
Cdd:pfam01562  81 VEGHPDSSVALSTC-SGLRGFIRTENEEYLIEPLEKysreEGGHPHVVY 128
Atrophin-1 super family cl38111
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 701-819 8.73e-12

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.


The actual alignment was detected with superfamily member pfam03154:

Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 69.03  E-value: 8.73e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759  701 SKPIKKQQDVQTPSAKEEEKIQRRPHELP-PQSQPWVMPSQSQPPVTPSQSHPQ-VMPSQSQPPVTPSQSQPRVMP---- 774
Cdd:pfam03154 215 SQPPNQTQSTAAPHTLIQQTPTLHPQRLPsPHPPLQPMTQPPPPSQVSPQPLPQpSLHGQMPPMPHSLQTGPSHMQhpvp 294

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 195232759  775 ----------SQSQPPVMP-------SQSHPQLTPSQSQPPVTPSQRQ------PQLMPSQSQPPVTP 819
Cdd:pfam03154 295 pqpfpltpqsSQSQVPPGPspaapgqSQQRIHTPPSQSQLQSQQPPREqplppaPLSMPHIKPPPTTP 362
 
Name Accession Description Interval E-value
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 198-386 9.84e-67

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: 220.18  E-value: 9.84e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759 198 RIVEIVVVIDNYLYIRYERNDSKLLEDLYVIVNIVDSILDVIGVKVLLFGLEIWTNKNLI-VVDDVRKSVHLYCKWKSEN 276
Cdd:cd04269    1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKIsVSGDAGETLNRFLDWKRSN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759 277 ITPRMQHDTSHLFTTLGLRG-LSGIGAFRGMCTPHRSCAIVTFMNKTLGTFSIAVAHHLGHNLGMNHDEDTCRCSQPRCI 355
Cdd:cd04269   81 LLPRKPHDNAQLLTGRDFDGnTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRSTCI 160

                        170       180       190
                 ....*....|....*....|....*....|...
gi 195232759 356 MHEGNPPITK-FSNCSYGDFWEYTVER-TKCLL 386
Cdd:cd04269  161 MAPSPSSLTDaFSNCSYEDYQKFLSRGgGQCLL 193
ACR smart00608
ADAM Cysteine-Rich Domain;
483-618 3.43e-55

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 186.41  E-value: 3.43e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759   483 DGIPCK-ERGYCYEKSCHDRNEQCRRIFGAGANTASETCYKELNTLGDRVGHCGIKNATYIKCNISDVQCGRIQCENVTE 561
Cdd:smart00608   2 DGTPCDnGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVSE 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 195232759   562 IPNMSDHTTVHWARFNDIMCWSTDYHLGMKgPDIGEVKDGTECGIDHICIHRHCVHI 618
Cdd:smart00608  82 LPLLGEHATVIYSNIGGLVCWSLDYHLGTD-PDIGMVKDGTKCGPGKVCINGQCVDV 137
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 483-586 2.88e-44

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: 154.70  E-value: 2.88e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759  483 DGIPCKE-RGYCYEKSCHDRNEQCRRIFGAGANTASETCYKELNTLGDRVGHCGIKNATYIKCNISDVQCGRIQCENVTE 561
Cdd:pfam08516   1 DGTPCNNgQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQCTNVKE 80

                          90       100
                  ....*....|....*....|....*
gi 195232759  562 IPNMSDHTTVHWARFNDIMCWSTDY 586
Cdd:pfam08516  81 LPLLGEHATVIYTNINGVTCWGTDY 105
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 198-386 3.48e-40

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: 146.68  E-value: 3.48e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759  198 RIVEIVVVIDNYLYIRYERNDSKLLEDLYVIVNIVDSILDVIGVKVLLFGLEIWTNKNLI-VVDDVRKSVHLYCKWKSEN 276
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIdVSGDANDTLRNFLKWRQEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759  277 ITPRMQHDTSHLFTTLGLRGL-SGIGAFRGMCTPHRSCAIVTFMNKTLGTFSIAVAHHLGHNLGMNHDEDT--CRC-SQP 352
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFGGTtVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFNggCKCpPGG 160

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 195232759  353 RCIMHE--GNPPITKFSNCSYGDFWEYTVE-RTKCLL 386
Cdd:pfam01421 161 GCIMNPsaGSSFPRKFSNCSQEDFEQFLTKqKGACLF 197
Disintegrin pfam00200
Disintegrin;
406-478 1.32e-35

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 128.90  E-value: 1.32e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 195232759  406 EEGEECDCGPLKHCAKDPCCL-SNCTLTDGSTCAFGLCCKDCKFLPSGKVCRKEVNECDLPEWCNGTSHKCPDD 478
Cdd:pfam00200   1 EEGEECDCGSLEECTNDPCCDaKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 406-480 2.92e-32

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: 119.72  E-value: 2.92e-32
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 195232759   406 EEGEECDCGPLKHCaKDPCC-LSNCTLTDGSTCAFGLCCKDCKFLPSGKVCRKEVNECDLPEWCNGTSHKCPDDFY 480
Cdd:smart00050   1 EEGEECDCGSPKEC-TDPCCdPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 32-150 1.26e-29

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: 113.95  E-value: 1.26e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759   32 DVVIPVRITG------TTRGMTPPGWLSYILPFGGQKHIIHIKVKKLLFSKHLPVFTYTDQGAILEDQPFVQNNCYYHGY 105
Cdd:pfam01562   1 EVVIPVRLDPsrrrrsLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 195232759  106 VEGDPESLVSLSTCfGGFQGILQINDFAYEIKPLAF----STTFEHLVY 150
Cdd:pfam01562  81 VEGHPDSSVALSTC-SGLRGFIRTENEEYLIEPLEKysreEGGHPHVVY 128
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 701-819 8.73e-12

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: 69.03  E-value: 8.73e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759  701 SKPIKKQQDVQTPSAKEEEKIQRRPHELP-PQSQPWVMPSQSQPPVTPSQSHPQ-VMPSQSQPPVTPSQSQPRVMP---- 774
Cdd:pfam03154 215 SQPPNQTQSTAAPHTLIQQTPTLHPQRLPsPHPPLQPMTQPPPPSQVSPQPLPQpSLHGQMPPMPHSLQTGPSHMQhpvp 294

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 195232759  775 ----------SQSQPPVMP-------SQSHPQLTPSQSQPPVTPSQRQ------PQLMPSQSQPPVTP 819
Cdd:pfam03154 295 pqpfpltpqsSQSQVPPGPspaapgqSQQRIHTPPSQSQLQSQQPPREqplppaPLSMPHIKPPPTTP 362
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
 725-816 1.40e-10

Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem to regulate formation of crystallites during the secretory stage of tooth enamel development and are thought to play a major role in the structural organisation and mineralisation of developing enamel. The extracellular matrix of the developing enamel comprises two major classes of protein: the hydrophobic amelogenins and the acidic enamelins. Circular dichroism studies of porcine amelogenin have shown that the protein consists of 3 discrete folding units: the N-terminal region appears to contain beta-strand structures, while the C-terminal region displays characteristics of a random coil conformation. Subsequent studies on the bovine protein have indicated the amelogenin structure to contain a repetitive beta-turn segment and a "beta-spiral" between Gln112 and Leu138, which sequester a (Pro, Leu, Gln) rich region. The beta-spiral offers a probable site for interactions with Ca2+ ions. Muatations in the human amelogenin gene (AMGX) cause X-linked hypoplastic amelogenesis imperfecta, a disease characterised by defective enamel. A 9bp deletion in exon 2 of AMGX results in the loss of codons for Ile5, Leu6, Phe7 and Ala8, and replacement by a new threonine codon, disrupting the 16-residue (Met1-Ala16) amelogenin signal peptide.


Pssm-ID: 197891 [Multi-domain]  Cd Length: 165  Bit Score: 60.57  E-value: 1.40e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759   725 PHELP--PQSQPWV-----MPSQSQPPVTPSQSHPQVMPSQSQPPV--TPSQSQPRVMPSQSQPPVMPsqsHPQLTPSQS 795
Cdd:smart00818  55 HHHIPvlPAQQPVVpqqplMPVPGQHSMTPTQHHQPNLPQPAQQPFqpQPLQPPQPQQPMQPQPPVHP---IPPLPPQPP 131

                           90       100
                   ....*....|....*....|.
gi 195232759   796 QPPVTPSQRQPQLMPSQSQPP 816
Cdd:smart00818 132 LPPMFPMQPLPPLLPDLPLEA 152
PHA03247 PHA03247
large tegument protein UL36; Provisional
 721-815 3.19e-08

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 57.64  E-value: 3.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759  721 IQRRPHELPPQSQPWVMP-----SQSQPPVTPS-QSHPQVMPSQSQPPVTPSQSQPRvmpSQSQPPVMPSQSHPQLTPSQ 794
Cdd:PHA03247 2862 VRRRPPSRSPAAKPAAPArppvrRLARPAVSRStESFALPPDQPERPPQPQAPPPPQ---PQPQPPPPPQPQPPPPPPPR 2938

                          90       100
                  ....*....|....*....|..
gi 195232759  795 SQPPVTP-SQRQPQLMPSQSQP 815
Cdd:PHA03247 2939 PQPPLAPtTDPAGAGEPSGAVP 2960
KLF10_11_N cd21974
N-terminal domain of Kruppel-like factor (KLF) 10, KLF11, and similar proteins; This subfamily ...
 729-820 3.52e-06

N-terminal domain of Kruppel-like factor (KLF) 10, KLF11, and similar proteins; This subfamily is composed of Kruppel-like factor or Krueppel-like factor (KLF) 10, KLF11, and similar proteins. KLF10 was first identified in human osteoblasts and plays a role in mediating estrogen (E2) signaling in bone and skeletal homeostasis and a regulatory role in tumor formation and metastasis. KLF11 is involved in cell growth, apoptosis, cellular inflammation and differentiation, endometriosis, and cholesterol, prostaglandin, neurotransmitter, fat, and sugar metabolism. KLF9, KLF10, KLF11, KLF13, KLF14, and KLF16 share a conserved a-helical motif AA/VXXL that mediates their binding to Sin3A and their activities as transcriptional repressors. KLF10/11 belong to a family of proteins, called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domain of KLF10, KLF11, and similar proteins.


Pssm-ID: 409243 [Multi-domain]  Cd Length: 229  Bit Score: 48.78  E-value: 3.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759 729 PPQSQPWVMPSQSQPPVTPSQSHPQVMPSQSQPPVTPSQSQPrvmPSQSQ-----------PPVMPSQSHPQLTP-SQSQ 796
Cdd:cd21974   60 PPYSPPFFEASHSPSVASLHPPSAASSQPPPEPESSEPPAAS---PQRAQatsvirhtadpVPVSPPPVLCQMLPvSSSS 136

                         90       100
                 ....*....|....*....|....
gi 195232759 797 PPVTPSQRQPQLMPSQSQPPVTPS 820
Cdd:cd21974  137 GVIVAFLKAPQQPSPQPQKPALPQ 160
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 700-820 1.01e-05

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 49.00  E-value: 1.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759 700 KSKPIKKQQDVQTPSAKEEEKIQRRPHELPPQSQPwvMPSQSQPPVTPS--QSHPQVMPsQSQPP---VTPSQSQPRV-- 772
Cdd:NF033839 366 KPQPEKPKPEVKPQPETPKPEVKPQPEKPKPEVKP--QPEKPKPEVKPQpeKPKPEVKP-QPEKPkpeVKPQPEKPKPev 442

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 195232759 773 --MPSQSQPPVMPSQSHP----QLTPSQSQPPVTPSQRQPQLMPSQSQP----PVTPS 820
Cdd:NF033839 443 kpQPEKPKPEVKPQPETPkpevKPQPEKPKPEVKPQPEKPKPDNSKPQAddkkPSTPN 500
myxo_disulf_rpt TIGR02232
Myxococcus cysteine-rich repeat; This model represents a sequence region shared between ...
 397-437 7.26e-03

Myxococcus cysteine-rich repeat; This model represents a sequence region shared between several proteins of Myxococcus xanthus DK 1622 and some eukaryotic proteins that include human pappalysin-1 (SP|Q13219). The region of about 40 amino acids contains several conserved Cys residues presumed to form disulfide bonds. The region appears in up to 13 repeats in Myxococcus.


Pssm-ID: 200169 [Multi-domain]  Cd Length: 38  Bit Score: 35.04  E-value: 7.26e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 195232759  397 VKRCGNGVVEEGEECDCGPLKhcAKDPCCLSnCTLTDGSTC 437
Cdd:TIGR02232   1 APTCGDGIIEPGEECDDGNTT--SGDGCSAT-CRLEEGFAC 38
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
330-360 7.50e-03

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 38.40  E-value: 7.50e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 195232759 330 VAHHLGHNLGMNHdedtcrCSQPRCIMHEGN 360
Cdd:COG1913  127 AVHELGHLFGLGH------CPNPRCVMHFSN 151
 
Name Accession Description Interval E-value
ZnMc_adamalysin_II_like cd04269
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ...
 198-386 9.84e-67

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: 220.18  E-value: 9.84e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759 198 RIVEIVVVIDNYLYIRYERNDSKLLEDLYVIVNIVDSILDVIGVKVLLFGLEIWTNKNLI-VVDDVRKSVHLYCKWKSEN 276
Cdd:cd04269    1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKIsVSGDAGETLNRFLDWKRSN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759 277 ITPRMQHDTSHLFTTLGLRG-LSGIGAFRGMCTPHRSCAIVTFMNKTLGTFSIAVAHHLGHNLGMNHDEDTCRCSQPRCI 355
Cdd:cd04269   81 LLPRKPHDNAQLLTGRDFDGnTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRSTCI 160

                        170       180       190
                 ....*....|....*....|....*....|...
gi 195232759 356 MHEGNPPITK-FSNCSYGDFWEYTVER-TKCLL 386
Cdd:cd04269  161 MAPSPSSLTDaFSNCSYEDYQKFLSRGgGQCLL 193
ACR smart00608
ADAM Cysteine-Rich Domain;
483-618 3.43e-55

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 186.41  E-value: 3.43e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759   483 DGIPCK-ERGYCYEKSCHDRNEQCRRIFGAGANTASETCYKELNTLGDRVGHCGIKNATYIKCNISDVQCGRIQCENVTE 561
Cdd:smart00608   2 DGTPCDnGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVSE 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 195232759   562 IPNMSDHTTVHWARFNDIMCWSTDYHLGMKgPDIGEVKDGTECGIDHICIHRHCVHI 618
Cdd:smart00608  82 LPLLGEHATVIYSNIGGLVCWSLDYHLGTD-PDIGMVKDGTKCGPGKVCINGQCVDV 137
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
 483-586 2.88e-44

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: 154.70  E-value: 2.88e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759  483 DGIPCKE-RGYCYEKSCHDRNEQCRRIFGAGANTASETCYKELNTLGDRVGHCGIKNATYIKCNISDVQCGRIQCENVTE 561
Cdd:pfam08516   1 DGTPCNNgQAYCYNGRCRDRDQQCQELFGKGAKSAPDACYEEVNSKGDRFGNCGRTNGGYVKCEKRDVLCGKLQCTNVKE 80

                          90       100
                  ....*....|....*....|....*
gi 195232759  562 IPNMSDHTTVHWARFNDIMCWSTDY 586
Cdd:pfam08516  81 LPLLGEHATVIYTNINGVTCWGTDY 105
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
 198-386 3.48e-40

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: 146.68  E-value: 3.48e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759  198 RIVEIVVVIDNYLYIRYERNDSKLLEDLYVIVNIVDSILDVIGVKVLLFGLEIWTNKNLI-VVDDVRKSVHLYCKWKSEN 276
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIdVSGDANDTLRNFLKWRQEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759  277 ITPRMQHDTSHLFTTLGLRGL-SGIGAFRGMCTPHRSCAIVTFMNKTLGTFSIAVAHHLGHNLGMNHDEDT--CRC-SQP 352
Cdd:pfam01421  81 LKKRKPHDVAQLLSGVEFGGTtVGAAYVGGMCSLEYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFNggCKCpPGG 160

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 195232759  353 RCIMHE--GNPPITKFSNCSYGDFWEYTVE-RTKCLL 386
Cdd:pfam01421 161 GCIMNPsaGSSFPRKFSNCSQEDFEQFLTKqKGACLF 197
Disintegrin pfam00200
Disintegrin;
406-478 1.32e-35

Disintegrin;


Pssm-ID: 459709  Cd Length: 74  Bit Score: 128.90  E-value: 1.32e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 195232759  406 EEGEECDCGPLKHCAKDPCCL-SNCTLTDGSTCAFGLCCKDCKFLPSGKVCRKEVNECDLPEWCNGTSHKCPDD 478
Cdd:pfam00200   1 EEGEECDCGSLEECTNDPCCDaKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
 406-480 2.92e-32

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: 119.72  E-value: 2.92e-32
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 195232759   406 EEGEECDCGPLKHCaKDPCC-LSNCTLTDGSTCAFGLCCKDCKFLPSGKVCRKEVNECDLPEWCNGTSHKCPDDFY 480
Cdd:smart00050   1 EEGEECDCGSPKEC-TDPCCdPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
 32-150 1.26e-29

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: 113.95  E-value: 1.26e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759   32 DVVIPVRITG------TTRGMTPPGWLSYILPFGGQKHIIHIKVKKLLFSKHLPVFTYTDQGAILEDQPFVQNNCYYHGY 105
Cdd:pfam01562   1 EVVIPVRLDPsrrrrsLASESTYLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGH 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 195232759  106 VEGDPESLVSLSTCfGGFQGILQINDFAYEIKPLAF----STTFEHLVY 150
Cdd:pfam01562  81 VEGHPDSSVALSTC-SGLRGFIRTENEEYLIEPLEKysreEGGHPHVVY 128
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
 198-372 3.00e-21

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: 92.10  E-value: 3.00e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759 198 RIVEIVVVIDNYLYIRYERNDSKLLEDLYVIVNIVDSILDVI----GVKVLLFGLEIWTNKNLIVVDDVRKSVHL--YCK 271
Cdd:cd04267    1 REIELVVVADHRMVSYFNSDENILQAYITELINIANSIYRSTnlrlGIRISLEGLQILKGEQFAPPIDSDASNTLnsFSF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759 272 WKSENitpRMQHDTSHLFT--TLGLRGLSGIGAFRGMCTPHRSCAIVTFMNKTLGTfSIAVAHHLGHNLGMNHDEDTC-- 347
Cdd:cd04267   81 WRAEG---PIRHDNAVLLTaqDFIEGDILGLAYVGSMCNPYSSVGVVEDTGFTLLT-ALTMAHELGHNLGAEHDGGDEla 156

                        170       180
                 ....*....|....*....|....*....
gi 195232759 348 --RCSQPRCIMHEGNPP--ITKFSNCSYG 372
Cdd:cd04267  157 feCDGGGNYIMAPVDSGlnSYRFSQCSIG 185
ZnMc_ADAMTS_like cd04273
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ...
 198-356 3.72e-17

Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions. This particular subfamily represents domain architectures that combine ADAM-like metalloproteinases with thrombospondin type-1 repeats. ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) proteinases are inhibited by TIMPs (tissue inhibitors of metalloproteinases), and they play roles in coagulation, angiogenesis, development and progression of arthritis. They hydrolyze the von Willebrand factor precursor and various components of the extracellular matrix.


Pssm-ID: 239801  Cd Length: 207  Bit Score: 80.75  E-value: 3.72e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759 198 RIVEIVVVIDNYLYIRYerNDSKLLEDLYVIVNIVDSIL--DVIG--VKVLLFGLEIWTN--KNLIVVDDVRKSVHLYCK 271
Cdd:cd04273    1 RYVETLVVADSKMVEFH--HGEDLEHYILTLMNIVASLYkdPSLGnsINIVVVRLIVLEDeeSGLLISGNAQKSLKSFCR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759 272 WKSENITPR----MQHDTSHLFT---------TLGLRGLSGIGafrGMCTPHRSCAIvtfmNKTLGtFSIA--VAHHLGH 336
Cdd:cd04273   79 WQKKLNPPNdsdpEHHDHAILLTrqdicrsngNCDTLGLAPVG---GMCSPSRSCSI----NEDTG-LSSAftIAHELGH 150

                        170       180
                 ....*....|....*....|...
gi 195232759 337 NLGMNHDEDTCRC---SQPRCIM 356
Cdd:cd04273  151 VLGMPHDGDGNSCgpeGKDGHIM 173
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 701-819 8.73e-12

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: 69.03  E-value: 8.73e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759  701 SKPIKKQQDVQTPSAKEEEKIQRRPHELP-PQSQPWVMPSQSQPPVTPSQSHPQ-VMPSQSQPPVTPSQSQPRVMP---- 774
Cdd:pfam03154 215 SQPPNQTQSTAAPHTLIQQTPTLHPQRLPsPHPPLQPMTQPPPPSQVSPQPLPQpSLHGQMPPMPHSLQTGPSHMQhpvp 294

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 195232759  775 ----------SQSQPPVMP-------SQSHPQLTPSQSQPPVTPSQRQ------PQLMPSQSQPPVTP 819
Cdd:pfam03154 295 pqpfpltpqsSQSQVPPGPspaapgqSQQRIHTPPSQSQLQSQQPPREqplppaPLSMPHIKPPPTTP 362
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
 725-816 1.40e-10

Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem to regulate formation of crystallites during the secretory stage of tooth enamel development and are thought to play a major role in the structural organisation and mineralisation of developing enamel. The extracellular matrix of the developing enamel comprises two major classes of protein: the hydrophobic amelogenins and the acidic enamelins. Circular dichroism studies of porcine amelogenin have shown that the protein consists of 3 discrete folding units: the N-terminal region appears to contain beta-strand structures, while the C-terminal region displays characteristics of a random coil conformation. Subsequent studies on the bovine protein have indicated the amelogenin structure to contain a repetitive beta-turn segment and a "beta-spiral" between Gln112 and Leu138, which sequester a (Pro, Leu, Gln) rich region. The beta-spiral offers a probable site for interactions with Ca2+ ions. Muatations in the human amelogenin gene (AMGX) cause X-linked hypoplastic amelogenesis imperfecta, a disease characterised by defective enamel. A 9bp deletion in exon 2 of AMGX results in the loss of codons for Ile5, Leu6, Phe7 and Ala8, and replacement by a new threonine codon, disrupting the 16-residue (Met1-Ala16) amelogenin signal peptide.


Pssm-ID: 197891 [Multi-domain]  Cd Length: 165  Bit Score: 60.57  E-value: 1.40e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759   725 PHELP--PQSQPWV-----MPSQSQPPVTPSQSHPQVMPSQSQPPV--TPSQSQPRVMPSQSQPPVMPsqsHPQLTPSQS 795
Cdd:smart00818  55 HHHIPvlPAQQPVVpqqplMPVPGQHSMTPTQHHQPNLPQPAQQPFqpQPLQPPQPQQPMQPQPPVHP---IPPLPPQPP 131

                           90       100
                   ....*....|....*....|.
gi 195232759   796 QPPVTPSQRQPQLMPSQSQPP 816
Cdd:smart00818 132 LPPMFPMQPLPPLLPDLPLEA 152
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
 726-819 1.79e-10

Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem to regulate formation of crystallites during the secretory stage of tooth enamel development and are thought to play a major role in the structural organisation and mineralisation of developing enamel. The extracellular matrix of the developing enamel comprises two major classes of protein: the hydrophobic amelogenins and the acidic enamelins. Circular dichroism studies of porcine amelogenin have shown that the protein consists of 3 discrete folding units: the N-terminal region appears to contain beta-strand structures, while the C-terminal region displays characteristics of a random coil conformation. Subsequent studies on the bovine protein have indicated the amelogenin structure to contain a repetitive beta-turn segment and a "beta-spiral" between Gln112 and Leu138, which sequester a (Pro, Leu, Gln) rich region. The beta-spiral offers a probable site for interactions with Ca2+ ions. Muatations in the human amelogenin gene (AMGX) cause X-linked hypoplastic amelogenesis imperfecta, a disease characterised by defective enamel. A 9bp deletion in exon 2 of AMGX results in the loss of codons for Ile5, Leu6, Phe7 and Ala8, and replacement by a new threonine codon, disrupting the 16-residue (Met1-Ala16) amelogenin signal peptide.


Pssm-ID: 197891 [Multi-domain]  Cd Length: 165  Bit Score: 60.19  E-value: 1.79e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759   726 HELPPQSQPWVMPSQS----QPPVTPSQSHPQVMPSQSQPPVTPSQSQPrvmPSQSQPPvMPSQSHPqltPSQSQPPVTP 801
Cdd:smart00818  50 HTLQPHHHIPVLPAQQpvvpQQPLMPVPGQHSMTPTQHHQPNLPQPAQQ---PFQPQPL-QPPQPQQ---PMQPQPPVHP 122

                           90       100
                   ....*....|....*....|....
gi 195232759   802 SQRQPQ------LMPSQSQPPVTP 819
Cdd:smart00818 123 IPPLPPqpplppMFPMQPLPPLLP 146
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 703-819 2.03e-10

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: 64.79  E-value: 2.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759  703 PIKKQQDVQTPSAKEEEKIQRRPHELPPQSQPWVMPSQSQPPVTP------SQSH----------PQVMPSQSQPPVT-- 764
Cdd:pfam03154 318 PGQSQQRIHTPPSQSQLQSQQPPREQPLPPAPLSMPHIKPPPTTPipqlpnPQSHkhpphlsgpsPFQMNSNLPPPPAlk 397

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759  765 ----------PS----------QSQPrVMPSQSQPPVMP-SQSHPqlTPSQSQPPVT-----PSQR---QPQLMPSQSqP 815
Cdd:pfam03154 398 plsslsthhpPSahppplqlmpQSQQ-LPPPPAQPPVLTqSQSLP--PPAASHPPTSglhqvPSQSpfpQHPFVPGGP-P 473


                  ....
gi 195232759  816 PVTP 819
Cdd:pfam03154 474 PITP 477
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 702-820 5.90e-10

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: 63.25  E-value: 5.90e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759  702 KPIKKQQDVQTPSAKEEekiqrrPHELPPQSQPwVMPSQSQPPV-TPSQSHPQvmPSQSQPPVTPSQSQPrvmpsqSQPP 780
Cdd:pfam03154 397 KPLSSLSTHHPPSAHPP------PLQLMPQSQQ-LPPPPAQPPVlTQSQSLPP--PAASHPPTSGLHQVP------SQSP 461

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 195232759  781 vMPSQSHPQLTPSQSQPPVTPSQRQPQLMPSqSQPPVTPS 820
Cdd:pfam03154 462 -FPQHPFVPGGPPPITPPSGPPTSTSSAMPG-IQPPSSAS 499
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 725-820 1.80e-09

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: 61.71  E-value: 1.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759  725 PHELPPQSQPwvmPSQSQPPVTP-------SQSHPQVMPSqSQPPVTPsqsqprvMPSQSQPPVMPSQSHPQLT------ 791
Cdd:pfam03154 208 PQGSPATSQP---PNQTQSTAAPhtliqqtPTLHPQRLPS-PHPPLQP-------MTQPPPPSQVSPQPLPQPSlhgqmp 276

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 195232759  792 ----PSQSQPPVTPSQRQPQLMP-----SQSQPPVTPS 820
Cdd:pfam03154 277 pmphSLQTGPSHMQHPVPPQPFPltpqsSQSQVPPGPS 314
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
 739-819 2.20e-09

Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem to regulate formation of crystallites during the secretory stage of tooth enamel development and are thought to play a major role in the structural organisation and mineralisation of developing enamel. The extracellular matrix of the developing enamel comprises two major classes of protein: the hydrophobic amelogenins and the acidic enamelins. Circular dichroism studies of porcine amelogenin have shown that the protein consists of 3 discrete folding units: the N-terminal region appears to contain beta-strand structures, while the C-terminal region displays characteristics of a random coil conformation. Subsequent studies on the bovine protein have indicated the amelogenin structure to contain a repetitive beta-turn segment and a "beta-spiral" between Gln112 and Leu138, which sequester a (Pro, Leu, Gln) rich region. The beta-spiral offers a probable site for interactions with Ca2+ ions. Muatations in the human amelogenin gene (AMGX) cause X-linked hypoplastic amelogenesis imperfecta, a disease characterised by defective enamel. A 9bp deletion in exon 2 of AMGX results in the loss of codons for Ile5, Leu6, Phe7 and Ala8, and replacement by a new threonine codon, disrupting the 16-residue (Met1-Ala16) amelogenin signal peptide.


Pssm-ID: 197891 [Multi-domain]  Cd Length: 165  Bit Score: 57.11  E-value: 2.20e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759   739 SQSQPPVTPSQSHPQVMPSQSQPPVTPSQSQprvMPSQSQPPVMPSQSHPQLTPSQSQPPVTPSQRQPQ--LMPSQSQPP 816
Cdd:smart00818  43 SQQHPPTHTLQPHHHIPVLPAQQPVVPQQPL---MPVPGQHSMTPTQHHQPNLPQPAQQPFQPQPLQPPqpQQPMQPQPP 119


                   ...
gi 195232759   817 VTP 819
Cdd:smart00818 120 VHP 122
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 696-820 2.83e-09

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: 60.94  E-value: 2.83e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759  696 RLCKKSKPIKKQQDVQTPSAKEEEKIQRRPHELPPQSQPwvmPSQSQPPVTPSQSHPQVMPSQSQPPV----TPSQSQPr 771
Cdd:pfam03154 142 RSTSPSIPSPQDNESDSDSSAQQQILQTQPPVLQAQSGA---ASPPSPPPPGTTQAATAGPTPSAPSVppqgSPATSQP- 217

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 195232759  772 vmPSQSQPPVMP-------SQSHPQLTPSqSQPPVTPSQRQPQlmPSQSQPPVTPS 820
Cdd:pfam03154 218 --PNQTQSTAAPhtliqqtPTLHPQRLPS-PHPPLQPMTQPPP--PSQVSPQPLPQ 268
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 731-819 6.43e-09

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 59.66  E-value: 6.43e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759  731 QSQPWVMPSQSQPPVTPSQS-HPQVMPSQSQPPVTPSQSQPRVMPSQSQPPvmPSQSHP--QLT-PSQSQPPVTPSQRQP 806
Cdd:pfam09770 206 QAKKPAQQPAPAPAQPPAAPpAQQAQQQQQFPPQIQQQQQPQQQPQQPQQH--PGQGHPvtILQrPQSPQPDPAQPSIQP 283

                          90
                  ....*....|...
gi 195232759  807 QLMPSQSQPPVTP 819
Cdd:pfam09770 284 QAQQFHQQPPPVP 296
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
 730-819 2.12e-08

Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem to regulate formation of crystallites during the secretory stage of tooth enamel development and are thought to play a major role in the structural organisation and mineralisation of developing enamel. The extracellular matrix of the developing enamel comprises two major classes of protein: the hydrophobic amelogenins and the acidic enamelins. Circular dichroism studies of porcine amelogenin have shown that the protein consists of 3 discrete folding units: the N-terminal region appears to contain beta-strand structures, while the C-terminal region displays characteristics of a random coil conformation. Subsequent studies on the bovine protein have indicated the amelogenin structure to contain a repetitive beta-turn segment and a "beta-spiral" between Gln112 and Leu138, which sequester a (Pro, Leu, Gln) rich region. The beta-spiral offers a probable site for interactions with Ca2+ ions. Muatations in the human amelogenin gene (AMGX) cause X-linked hypoplastic amelogenesis imperfecta, a disease characterised by defective enamel. A 9bp deletion in exon 2 of AMGX results in the loss of codons for Ile5, Leu6, Phe7 and Ala8, and replacement by a new threonine codon, disrupting the 16-residue (Met1-Ala16) amelogenin signal peptide.


Pssm-ID: 197891 [Multi-domain]  Cd Length: 165  Bit Score: 54.41  E-value: 2.12e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759   730 PQSQPwvMPSQSQPPVTPSQsHPQVmPSQS------QPPVTPSQSQPRVMPSQSQPPVMPsqshPQLTPSQSQPPVTPSQ 803
Cdd:smart00818  47 PPTHT--LQPHHHIPVLPAQ-QPVV-PQQPlmpvpgQHSMTPTQHHQPNLPQPAQQPFQP----QPLQPPQPQQPMQPQP 118

                           90
                   ....*....|....*.
gi 195232759   804 RQPQLMPSQSQPPVTP 819
Cdd:smart00818 119 PVHPIPPLPPQPPLPP 134
PHA03247 PHA03247
large tegument protein UL36; Provisional
 721-815 3.19e-08

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 57.64  E-value: 3.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759  721 IQRRPHELPPQSQPWVMP-----SQSQPPVTPS-QSHPQVMPSQSQPPVTPSQSQPRvmpSQSQPPVMPSQSHPQLTPSQ 794
Cdd:PHA03247 2862 VRRRPPSRSPAAKPAAPArppvrRLARPAVSRStESFALPPDQPERPPQPQAPPPPQ---PQPQPPPPPQPQPPPPPPPR 2938

                          90       100
                  ....*....|....*....|..
gi 195232759  795 SQPPVTP-SQRQPQLMPSQSQP 815
Cdd:PHA03247 2939 PQPPLAPtTDPAGAGEPSGAVP 2960
PHA03247 PHA03247
large tegument protein UL36; Provisional
 738-820 4.02e-08

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 57.26  E-value: 4.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759  738 PSQSQPPVTPSQSHPQVMpSQSQPPVTPS-QSQPRVMPSQSQPPVMPSQSHPQLTPsqsQPPVTPSQRQPQLMPSQSQPP 816
Cdd:PHA03247 2867 PSRSPAAKPAAPARPPVR-RLARPAVSRStESFALPPDQPERPPQPQAPPPPQPQP---QPPPPPQPQPPPPPPPRPQPP 2942


                  ....
gi 195232759  817 VTPS 820
Cdd:PHA03247 2943 LAPT 2946
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 713-817 5.49e-08

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: 56.70  E-value: 5.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759  713 PSAKEEEKIQRRPHELPPQSQPWV-MPSQSQP--PVTPSQSHPQVMPSQSQPPVTPSQSQ----------PRVMPSQSQP 779
Cdd:pfam03154 313 PSPAAPGQSQQRIHTPPSQSQLQSqQPPREQPlpPAPLSMPHIKPPPTTPIPQLPNPQSHkhpphlsgpsPFQMNSNLPP 392

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 195232759  780 P--VMPSQSHPQLTPSQSQPPvtPSQRQPQ---LMPSQSQPPV 817
Cdd:pfam03154 393 PpaLKPLSSLSTHHPPSAHPP--PLQLMPQsqqLPPPPAQPPV 433
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 737-819 7.33e-08

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 56.20  E-value: 7.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759  737 MPSQSQPPVTPSQSHPQVMPSQSQPPVTPSQSQPrvmPSQSQPPVMPSQSHPQLTPSQSQ-PPVTPSQRQPQLMPSQSQP 815
Cdd:pfam09770 203 MRAQAKKPAQQPAPAPAQPPAAPPAQQAQQQQQF---PPQIQQQQQPQQQPQQPQQHPGQgHPVTILQRPQSPQPDPAQP 279


                  ....
gi 195232759  816 PVTP 819
Cdd:pfam09770 280 SIQP 283
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
 282-372 1.14e-07

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: 52.14  E-value: 1.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759 282 QHDTSHLFTTLGLRGLSGIGAFRG-MCTPHRSCAIVTFMNKTLGTFSIAVAHHLGHNLGMNHDED-TCRCSQP------- 352
Cdd:cd00203   51 KADIAILVTRQDFDGGTGGWAYLGrVCDSLRGVGVLQDNQSGTKEGAQTIAHELGHALGFYHDHDrKDRDDYPtiddtln 130

                         90       100       110
                 ....*....|....*....|....*....|.
gi 195232759 353 ------RCIMHEGNPP-----ITKFSNCSYG 372
Cdd:cd00203  131 aedddyYSVMSYTKGSfsdgqRKDFSQCDID 161
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 713-819 1.94e-07

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 54.66  E-value: 1.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759  713 PSAKEEEKIQRRPHELPPQSQPwvmPSQSQPPVTPSQSHPQVMPSQSQPPvtPSQSQP-----RVMPSQSQPPVMPSQSH 787
Cdd:pfam09770 210 PAQQPAPAPAQPPAAPPAQQAQ---QQQQFPPQIQQQQQPQQQPQQPQQH--PGQGHPvtilqRPQSPQPDPAQPSIQPQ 284

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 195232759  788 PQLTPSQSQP-PVTPSQ------RQP---QLMPSQSQPPVTP 819
Cdd:pfam09770 285 AQQFHQQPPPvPVQPTQilqnpnRLSaarVGYPQNPQPGVQP 326
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 712-820 2.94e-07

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 54.32  E-value: 2.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759  712 TPSAKEEEKIQRRPHELPPQSQPwvmpsqsQPPVTPSQSHPQvmPSQSQPPvtPSQSQPRVMPSQSQPPVMPSQsHPQLT 791
Cdd:PRK10263  746 TPIVEPVQQPQQPVAPQQQYQQP-------QQPVAPQPQYQQ--PQQPVAP--QPQYQQPQQPVAPQPQYQQPQ-QPVAP 813

                          90       100
                  ....*....|....*....|....*....
gi 195232759  792 PSQSQPPVTPSQRQPQLmpSQSQPPVTPS 820
Cdd:PRK10263  814 QPQYQQPQQPVAPQPQY--QQPQQPVAPQ 840
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 706-819 3.28e-07

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 54.32  E-value: 3.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759  706 KQQDVQTPSAKEEEKIQRRPheLPPQSQPwvmpSQSQPPVTPSQSHPQVMPSQSQPPVTPSQSQPRVMPSQSQPPVMPSQ 785
Cdd:PRK10263  752 VQQPQQPVAPQQQYQQPQQP--VAPQPQY----QQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVA 825

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 195232759  786 SHPQLtpSQSQPPVTPSQRQ----PQLMPS-QSQP---PVTP 819
Cdd:PRK10263  826 PQPQY--QQPQQPVAPQPQDtllhPLLMRNgDSRPlhkPTTP 865
PRK12757 PRK12757
cell division protein FtsN; Provisional
 721-806 5.39e-07

cell division protein FtsN; Provisional


Pssm-ID: 237191 [Multi-domain]  Cd Length: 256  Bit Score: 51.58  E-value: 5.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759 721 IQRRPHELPPqsqpwvMPSQSQPPVTP-SQSHPQVMPSQSQPPVTPSQSQPRVMPSQSQPPVMPSQSHPqlTPSQSQPPV 799
Cdd:PRK12757  95 MRQQPTQLSE------VPYNEQTPQVPrSTVQIQQQAQQQQPPATTAQPQPVTPPRQTTAPVQPQTPAP--VRTQPAAPV 166


                 ....*..
gi 195232759 800 TPSQRQP 806
Cdd:PRK12757 167 TQAVEAP 173
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 713-805 8.19e-07

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 52.70  E-value: 8.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759  713 PSAKEEEKIQRRPHELPPQSQPWVmPSqsqpPVTPSQSHPQVMPSQSQP-PVTPSQSQPRVMPSQSQPPVMPSQS--HPQ 789
Cdd:pfam09606 378 PVPGQQVRQVTPNQFMRQSPQPSV-PS----PQGPGSQPPQSHPGGMIPsPALIPSPSPQMSQQPAQQRTIGQDSpgGSL 452

                          90
                  ....*....|....*...
gi 195232759  790 LTPSQSQ--PPVTPSQRQ 805
Cdd:pfam09606 453 NTPGQSAvnSPLNPQEEQ 470
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 725-816 9.68e-07

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: 52.46  E-value: 9.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759  725 PHELPPQSQPWV-MPSQSQPPVTPSQSHP-QVMPSQSQPPVTP---SQSQPRVMPSQSQPPVMPSQSHPQLTPSQSQP-- 797
Cdd:pfam03154 290 QHPVPPQPFPLTpQSSQSQVPPGPSPAAPgQSQQRIHTPPSQSqlqSQQPPREQPLPPAPLSMPHIKPPPTTPIPQLPnp 369

                          90       100
                  ....*....|....*....|....
gi 195232759  798 -----PVTPSQRQPQLMPSQSQPP 816
Cdd:pfam03154 370 qshkhPPHLSGPSPFQMNSNLPPP 393
PHA03247 PHA03247
large tegument protein UL36; Provisional
 707-820 1.14e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 52.63  E-value: 1.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759  707 QQDVQTPSAKEEEKIQR--RPhELPPQSQPWVMP--SQSQPPVTPSQSHPQvmpSQSQPPVTPSQSQPRVMPSQSQPPVM 782
Cdd:PHA03247 2869 RSPAAKPAAPARPPVRRlaRP-AVSRSTESFALPpdQPERPPQPQAPPPPQ---PQPQPPPPPQPQPPPPPPPRPQPPLA 2944

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 195232759  783 P-SQSHPQLTPSQSQPP-----------VTPSQRQPQLMPSQSQP-PVTPS 820
Cdd:PHA03247 2945 PtTDPAGAGEPSGAVPQpwlgalvpgrvAVPRFRVPQPAPSREAPaSSTPP 2995
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
 707-816 1.41e-06

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


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 49.27  E-value: 1.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759  707 QQDVQTPSAKEEEKIQRRPHELPPQSQPWVMPSQSQPPVTPSQSHPQVMPSqsQPPVTPSQSQPRVMPSQ---SQPPVMP 783
Cdd:pfam15240  24 SQEDSPSLISEEEGQSQQGGQGPQGPPPGGFPPQPPASDDPPGPPPPGGPQ--QPPPQGGKQKPQGPPPQggpRPPPGKP 101

                          90       100       110
                  ....*....|....*....|....*....|...
gi 195232759  784 SQSHPQLTPSQSQPPVTPSQRQPQLmPSQSQPP 816
Cdd:pfam15240 102 QGPPPQGGNQQQGPPPPGKPQGPPP-QGGGPPP 133
PHA03378 PHA03378
EBNA-3B; Provisional
 723-819 1.57e-06

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 51.99  E-value: 1.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759 723 RRPHELPPqsqPWVMPSQSQPP--VTPSQSHPQVMPSQSQPP------VTPSQSQP-RVMPSQSQPPVMPSQSHPQLTPS 793
Cdd:PHA03378 699 RAPTPMRP---PAAPPGRAQRPaaATGRARPPAAAPGRARPPaaapgrARPPAAAPgRARPPAAAPGRARPPAAAPGAPT 775

                         90       100
                 ....*....|....*....|....*...
gi 195232759 794 QSQPPVTP--SQRQPQLMPSQSQPPVTP 819
Cdd:PHA03378 776 PQPPPQAPpaPQQRPRGAPTPQPPPQAG 803
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
 722-819 1.89e-06

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


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 48.88  E-value: 1.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759  722 QRRPHELPPQSQ--PWVMPSQSQPPVTPSQSHPQVMPSQSQPPVTPSQSQPrvmPSQSQPPVmPSQSHPQLTPsqsQPPV 799
Cdd:pfam15240  74 QQPPPQGGKQKPqgPPPQGGPRPPPGKPQGPPPQGGNQQQGPPPPGKPQGP---PPQGGGPP-PQGGNQQGPP---PPPP 146

                          90       100
                  ....*....|....*....|
gi 195232759  800 TPSQRQPQLMPSQSQPPVTP 819
Cdd:pfam15240 147 GNPQGPPQRPPQPGNPQGPP 166
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
 724-820 2.56e-06

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


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 48.50  E-value: 2.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759  724 RPHELPPQSQPwvmpsqSQPPVTPSQSHPQVMPSQSQPPVTPSQSQ---PRVMPSQSQPPVMPSQSHPQLtPSQSQPPVT 800
Cdd:pfam15240  63 DPPGPPPPGGP------QQPPPQGGKQKPQGPPPQGGPRPPPGKPQgppPQGGNQQQGPPPPGKPQGPPP-QGGGPPPQG 135

                          90       100
                  ....*....|....*....|..
gi 195232759  801 PSQRQPQLMPSQSQ--PPVTPS 820
Cdd:pfam15240 136 GNQQGPPPPPPGNPqgPPQRPP 157
PRK12757 PRK12757
cell division protein FtsN; Provisional
 742-816 2.88e-06

cell division protein FtsN; Provisional


Pssm-ID: 237191 [Multi-domain]  Cd Length: 256  Bit Score: 49.66  E-value: 2.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759 742 QPPVTPSQshpqvMPSQSQPPVTP-SQSQPRVMPSQSQPPVMPSQSHPQLTPSQSQPPVTPSQRQP----QLMPSQSQPP 816
Cdd:PRK12757  97 QQPTQLSE-----VPYNEQTPQVPrSTVQIQQQAQQQQPPATTAQPQPVTPPRQTTAPVQPQTPAPvrtqPAAPVTQAVE 171
KLF10_11_N cd21974
N-terminal domain of Kruppel-like factor (KLF) 10, KLF11, and similar proteins; This subfamily ...
 729-820 3.52e-06

N-terminal domain of Kruppel-like factor (KLF) 10, KLF11, and similar proteins; This subfamily is composed of Kruppel-like factor or Krueppel-like factor (KLF) 10, KLF11, and similar proteins. KLF10 was first identified in human osteoblasts and plays a role in mediating estrogen (E2) signaling in bone and skeletal homeostasis and a regulatory role in tumor formation and metastasis. KLF11 is involved in cell growth, apoptosis, cellular inflammation and differentiation, endometriosis, and cholesterol, prostaglandin, neurotransmitter, fat, and sugar metabolism. KLF9, KLF10, KLF11, KLF13, KLF14, and KLF16 share a conserved a-helical motif AA/VXXL that mediates their binding to Sin3A and their activities as transcriptional repressors. KLF10/11 belong to a family of proteins, called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domain of KLF10, KLF11, and similar proteins.


Pssm-ID: 409243 [Multi-domain]  Cd Length: 229  Bit Score: 48.78  E-value: 3.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759 729 PPQSQPWVMPSQSQPPVTPSQSHPQVMPSQSQPPVTPSQSQPrvmPSQSQ-----------PPVMPSQSHPQLTP-SQSQ 796
Cdd:cd21974   60 PPYSPPFFEASHSPSVASLHPPSAASSQPPPEPESSEPPAAS---PQRAQatsvirhtadpVPVSPPPVLCQMLPvSSSS 136

                         90       100
                 ....*....|....*....|....
gi 195232759 797 PPVTPSQRQPQLMPSQSQPPVTPS 820
Cdd:cd21974  137 GVIVAFLKAPQQPSPQPQKPALPQ 160
PHA03247 PHA03247
large tegument protein UL36; Provisional
 729-816 3.53e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.09  E-value: 3.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759  729 PPQSQPWVMPSQSQPP---------VTPSQSHPQVMPSQSQPPVTPSQSQPRVMpSQSQPPVMPS-QSHPQLTPSQSQPP 798
Cdd:PHA03247 2831 PTSAQPTAPPPPPGPPppslplggsVAPGGDVRRRPPSRSPAAKPAAPARPPVR-RLARPAVSRStESFALPPDQPERPP 2909

                          90
                  ....*....|....*...
gi 195232759  799 VTPSQRQPQLMPSQSQPP 816
Cdd:PHA03247 2910 QPQAPPPPQPQPQPPPPP 2927
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 701-819 4.26e-06

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 50.47  E-value: 4.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759  701 SKPIKKQQDV---QTPS---AKEEEKIQRRPHELPPQ---SQPWVMPSQSQPPVTPSQSHPQVMPSQSQPPVTPSQSQPR 771
Cdd:PRK10263  354 AQPTVAWQPVpgpQTGEpviAPAPEGYPQQSQYAQPAvqyNEPLQQPVQPQQPYYAPAAEQPAQQPYYAPAPEQPAQQPY 433

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 195232759  772 VMPSQSQPPV-MPSQSHPQLTPSQSQPPVTPSQRQPQLM---PSQSQPPVTP 819
Cdd:PRK10263  434 YAPAPEQPVAgNAWQAEEQQSTFAPQSTYQTEQTYQQPAaqePLYQQPQPVE 485
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 701-819 4.44e-06

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 50.46  E-value: 4.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759 701 SKPIKKQQDVQTPSAKEEEKIQRRPHElPPQSQPWVMPSQSQPPVTPSQS-HPQ--VMPSQSQPPVTPSQSQPRVMPSQS 777
Cdd:PTZ00449 537 SKESDEPKEGGKPGETKEGEVGKKPGP-AKEHKPSKIPTLSKKPEFPKDPkHPKdpEEPKKPKRPRSAQRPTRPKSPKLP 615

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 195232759 778 QPPVMPSQSHPQLTPSQSQPPVTP----SQRQPQ--LMPSQSQPPVTP 819
Cdd:PTZ00449 616 ELLDIPKSPKRPESPKSPKRPPPPqrpsSPERPEgpKIIKSPKPPKSP 663
PHA03377 PHA03377
EBNA-3C; Provisional
 709-817 5.38e-06

EBNA-3C; Provisional


Pssm-ID: 177614 [Multi-domain]  Cd Length: 1000  Bit Score: 50.05  E-value: 5.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759  709 DVQTPSAKEEEKIQRRPHELPP-------QSQPWVMPsqsqPPVTPSQSHPqvmPSQSQPPVTPSQSQPRVM-PSQSQPP 780
Cdd:PHA03377  516 DVETTEEEESVTQPAKPHRKVQdgfqrsgRRQKRATP----PKVSPSDRGP---PKASPPVMAPPSTGPRVMaTPSTGPR 588

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 195232759  781 VM--PSQSHPQLTPSQSQPPV-TPSQRQPQ-LMPSQSQPPV 817
Cdd:PHA03377  589 DMapPSTGPRQQAKCKDGPPAsGPHEKQPPsSAPRDMAPSV 629
PHA03378 PHA03378
EBNA-3B; Provisional
 723-816 5.45e-06

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 50.07  E-value: 5.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759 723 RRPHElPPQSQP-WVMPSQSQPPVTPSQSHP---------QVMPSQSQPPV---TPSqSQPRVMPSQSQPPVMPS--QSH 787
Cdd:PHA03378 649 PTPHQ-PPQVEItPYKPTWTQIGHIPYQPSPtgantmlpiQWAPGTMQPPPrapTPM-RPPAAPPGRAQRPAAATgrARP 726

                         90       100       110
                 ....*....|....*....|....*....|.
gi 195232759 788 PQLTPSQSQPPVTP--SQRQPQLMPSQSQPP 816
Cdd:PHA03378 727 PAAAPGRARPPAAApgRARPPAAAPGRARPP 757
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
 707-819 5.48e-06

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


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 47.34  E-value: 5.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759  707 QQDVQTPSAKEEEKIQRRPH-ELPPQSQPWVMPSQSQPPVTPSQSHPQVMPSQSQPPvtPSQSQPRVMPSQSQ---PPVM 782
Cdd:pfam15240  32 ISEEEGQSQQGGQGPQGPPPgGFPPQPPASDDPPGPPPPGGPQQPPPQGGKQKPQGP--PPQGGPRPPPGKPQgppPQGG 109

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 195232759  783 PSQSHPQLTPSQSQPPvTPSQRQPQLMPSQSQPPVTP 819
Cdd:pfam15240 110 NQQQGPPPPGKPQGPP-PQGGGPPPQGGNQQGPPPPP 145
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 700-820 1.01e-05

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 49.00  E-value: 1.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759 700 KSKPIKKQQDVQTPSAKEEEKIQRRPHELPPQSQPwvMPSQSQPPVTPS--QSHPQVMPsQSQPP---VTPSQSQPRV-- 772
Cdd:NF033839 366 KPQPEKPKPEVKPQPETPKPEVKPQPEKPKPEVKP--QPEKPKPEVKPQpeKPKPEVKP-QPEKPkpeVKPQPEKPKPev 442

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 195232759 773 --MPSQSQPPVMPSQSHP----QLTPSQSQPPVTPSQRQPQLMPSQSQP----PVTPS 820
Cdd:NF033839 443 kpQPEKPKPEVKPQPETPkpevKPQPEKPKPEVKPQPEKPKPDNSKPQAddkkPSTPN 500
PHA03247 PHA03247
large tegument protein UL36; Provisional
 728-819 1.19e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.17  E-value: 1.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759  728 LPPQSQPwvmPSQSQPPVTPSQSHPQVMPSQSQPP------VTPSQSQPRVMPSQSQPPVMPSQSHPQLTpSQSQPPVTP 801
Cdd:PHA03247 2818 LPPAASP---AGPLPPPTSAQPTAPPPPPGPPPPSlplggsVAPGGDVRRRPPSRSPAAKPAAPARPPVR-RLARPAVSR 2893

                          90
                  ....*....|....*...
gi 195232759  802 SQRQPQLMPSQSQPPVTP 819
Cdd:PHA03247 2894 STESFALPPDQPERPPQP 2911
PRK12757 PRK12757
cell division protein FtsN; Provisional
 705-819 1.26e-05

cell division protein FtsN; Provisional


Pssm-ID: 237191 [Multi-domain]  Cd Length: 256  Bit Score: 47.73  E-value: 1.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759 705 KKQQDVQTPSAKeeekiQRRPHELPPQSQP-W----------VMPSQSQPPVT--PSQSHPQVMPSQSQ----------- 760
Cdd:PRK12757  23 KKEEAPLLPNHK-----PRTGNGLPPKPEErWryikelenrqIGVPTPTEPSAggEVNSPTQLTDEQRQlleqmqadmrq 97

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759 761 PPVTPSQsqprvMPSQSQPPVMP-SQSHPQLTPSQSQPPVTPSQRQPQLMPSQSQPPVTP 819
Cdd:PRK12757  98 QPTQLSE-----VPYNEQTPQVPrSTVQIQQQAQQQQPPATTAQPQPVTPPRQTTAPVQP 152
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
198-367 1.44e-05

Metallo-peptidase family M12;


Pssm-ID: 372673  Cd Length: 191  Bit Score: 46.64  E-value: 1.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759  198 RIVEIVVVIDNYLYIRYERNDSKLLedlyvIVNIVDSILDVI----GVKVLLFGLEIWTNKNLI-----VVDDVRKSVHL 268
Cdd:pfam13688   3 RTVALLVAADCSYVAAFGGDAAQAN-----IINMVNTASNVYerdfNISLGLVNLTISDSTCPYtppacSTGDSSDRLSE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759  269 YckWKSENITPRMQHDTSHLFT--TLGLRGLSGIGafrGMCTPHRSCAIVTFMNKTL-----GTFSIAVAHHLGHNLGMN 341
Cdd:pfam13688  78 F--QDFSAWRGTQNDDLAYLFLmtNCSGGGLAWLG---QLCNSGSAGSVSTRVSGNNvvvstATEWQVFAHEIGHNFGAV 152

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 195232759  342 HD------EDTCRCSQP------RCIMHEGNPP-ITKFS 367
Cdd:pfam13688 153 HDcdsstsSQCCPPSNStcpaggRYIMNPSSSPnSTDFS 191
KLF3_N cd21577
N-terminal domain of Kruppel-like factor 3; Kruppel-like factor 3 (KLF3; also called ...
 729-820 1.47e-05

N-terminal domain of Kruppel-like factor 3; Kruppel-like factor 3 (KLF3; also called Krueppel-like factor 3 and originally called Basic Kruppel-like Factor/BKLF), was the third member of the KLF family of zinc finger transcription factors to be discovered. KLF3 possesses a wide range of biological impacts on regulating apoptosis, differentiation, and proliferation in various tissues during the entire progression process. It has been proposed as a tumor suppressor in colorectal cancer. It appears to function predominantly as a repressor of transcription, turning genes off by recruiting the C-terminal Binding Protein co-repressors CtBP1 and CtBP2. CtBP docks onto a short motif (residues 61-65) in the N-terminus of KLF3, through the Proline-X-Aspartate-Leucine-Serine (PXDLS) motif. CtBP in turn recruits histone modifying enzymes to alter chromatin and repress gene expression. KLF3 belongs to a family of proteins, called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domain of KLF3.


Pssm-ID: 410554 [Multi-domain]  Cd Length: 214  Bit Score: 46.96  E-value: 1.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759 729 PPQSQPWVMPSQSQPPVTPSQSHPQvmPSQSQPPVTPSQSQPRVMPSQSQPPVMPSQSHPQLTPSQSQP-PVTPSqrqPQ 807
Cdd:cd21577   41 SSSSSSSSPSSRASPPSPYSKSSPP--SPPQQRPLSPPLSLPPPVAPPPLSPGSVPGGLPVISPVMVQPvPVLYP---PH 115

                         90
                 ....*....|...
gi 195232759 808 LMPSQSQPPVTPS 820
Cdd:cd21577  116 LHQPIMVSSSPPP 128
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
738-820 1.84e-05

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 48.23  E-value: 1.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759 738 PSQSQP---PVTPSQSHPQVMPSQSQPPVTPSQSQPRVMPSQSQPPVM-----PSQSHPQLTPSQSQPPVTPSQRQPqlM 809
Cdd:PRK14971 381 PVFTQPaaaPQPSAAAAASPSPSQSSAAAQPSAPQSATQPAGTPPTVSvdppaAVPVNPPSTAPQAVRPAQFKEEKK--I 458

                         90
                 ....*....|.
gi 195232759 810 PSQSQPPVTPS 820
Cdd:PRK14971 459 PVSKVSSLGPS 469
Mucin-like pfam16058
Mucin-like; This region is found repeated at the C-terminus (C-tail) of bile salt-activated ...
 738-820 2.03e-05

Mucin-like; This region is found repeated at the C-terminus (C-tail) of bile salt-activated lipase, where is O-glycosylated. This region is composed of biased amino acid composition that is likely to be disordered. The region contains many repeats of an approximately 11 residue degenerate repeat.


Pssm-ID: 464997 [Multi-domain]  Cd Length: 94  Bit Score: 43.95  E-value: 2.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759  738 PSQSQPPVTPSQSH--PQVMPSQS--QPPVTPSQSQprvmpsqSQPPVMPSQS--HPQLTPSQS--QPPVTPSQ--RQPQ 807
Cdd:pfam16058   3 SSITEPPRDPSGSYgePPRAPSSSytEPQRDPSSSI-------TEPPADPSSSytEPPRDPSGSytEPQRDPSSssTEPQ 75

                          90
                  ....*....|....*
gi 195232759  808 LMPSQS--QPPVTPS 820
Cdd:pfam16058  76 RDPSSSitEPPRDPS 90
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 703-815 2.53e-05

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 48.16  E-value: 2.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759  703 PIKKQQDVQTPSAKEEEkiQRRPHELPPQSQPWVMPSQSQPPvTPSQSHPQ--VMPS-QSQPPVTPSQSQPRVMPSQSQP 779
Cdd:PRK10263  761 PQQQYQQPQQPVAPQPQ--YQQPQQPVAPQPQYQQPQQPVAP-QPQYQQPQqpVAPQpQYQQPQQPVAPQPQYQQPQQPV 837

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 195232759  780 PVMPSQS--HPQLTPS-QSQPPVTPSQRQPQL-----MPSQSQP 815
Cdd:PRK10263  838 APQPQDTllHPLLMRNgDSRPLHKPTTPLPSLdlltpPPSEVEP 881
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 699-820 2.61e-05

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 48.15  E-value: 2.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759 699 KKSKPIKKQQDVQTPSAKEEEKIQRRPHElppqsqpwvmPSQSQPPVTPSQshPQVMPSQSQP-----PVTPSQSQPRVM 773
Cdd:PTZ00449 565 KEHKPSKIPTLSKKPEFPKDPKHPKDPEE----------PKKPKRPRSAQR--PTRPKSPKLPelldiPKSPKRPESPKS 632

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 195232759 774 PSQSQPPVMPSqshpqlTPSQSQPPVTPSQRQPqlmPSQSQPPVTPS 820
Cdd:PTZ00449 633 PKRPPPPQRPS------SPERPEGPKIIKSPKP---PKSPKPPFDPK 670
KLF4_N cd21582
N-terminal domain of Kruppel-like factor 4; Kruppel-like factor 4 (KLF4; also known as ...
 732-820 2.92e-05

N-terminal domain of Kruppel-like factor 4; Kruppel-like factor 4 (KLF4; also known as Krueppel-like factor 4 or gut-enriched Kruppel-like factor/GKLF) is a protein that, in humans, is encoded by the KLF4 gene. Evidence also suggests that KLF4 is a tumor suppressor in certain cancers, including colorectal cancer, gastric cancer, esophageal squamous cell carcinoma, intestinal cancer, prostate cancer, bladder cancer and lung cancer. It may act as a tumor promoter where increased KLF4 expression has been reported, such as in oral squamous cell carcinoma and in primary breast ductal carcinoma. KLF4 is one of four key factors that are essential for inducing pluripotent stem cells. KLF4 is highly expressed in non-dividing cells and its overexpression induces cell cycle arrest. KLF proteins KLF1, KLF2, KLF4, KLF5, KLF6, and KLF7 are transcriptional activators. KLF4 belongs to a family of proteins called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domain of KLF4, which is related to the N-terminal domains of KLF1 and KLF2.


Pssm-ID: 409228 [Multi-domain]  Cd Length: 335  Bit Score: 47.00  E-value: 2.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759 732 SQPwvMPSQSQPPVTPSQSHPQVMPSQSQPPVTP---SQSQPRVMPSQSQPPVMPSQSHPQLTPSQSQPPVT--PSQRQP 806
Cdd:cd21582  220 SRP--MDGHLGGNSQHGFSQRAPLPSRTTPSGGPgggNSSTAESLMSRDHHPSSQVLSHPPLPLPQGYHPSPgyPPFPPP 297

                         90
                 ....*....|....
gi 195232759 807 QLMPSQSQPPVTPS 820
Cdd:cd21582  298 PSQPQQYQELMSPG 311
PHA03247 PHA03247
large tegument protein UL36; Provisional
 725-811 3.00e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.01  E-value: 3.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759  725 PHELPPQSQPwVMPSQSQPP--VTPSQSHPQVMPSQSQPPVTPSQSQPRVmpsqsqpPVMPSQSHPQLTPSQSQPPVTPS 802
Cdd:PHA03247 2552 PPPLPPAAPP-AAPDRSVPPprPAPRPSEPAVTSRARRPDAPPQSARPRA-------PVDDRGDPRGPAPPSPLPPDTHA 2623


                  ....*....
gi 195232759  803 QRQPQLMPS 811
Cdd:PHA03247 2624 PDPPPPSPS 2632
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
 721-816 3.15e-05

Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem to regulate formation of crystallites during the secretory stage of tooth enamel development and are thought to play a major role in the structural organisation and mineralisation of developing enamel. The extracellular matrix of the developing enamel comprises two major classes of protein: the hydrophobic amelogenins and the acidic enamelins. Circular dichroism studies of porcine amelogenin have shown that the protein consists of 3 discrete folding units: the N-terminal region appears to contain beta-strand structures, while the C-terminal region displays characteristics of a random coil conformation. Subsequent studies on the bovine protein have indicated the amelogenin structure to contain a repetitive beta-turn segment and a "beta-spiral" between Gln112 and Leu138, which sequester a (Pro, Leu, Gln) rich region. The beta-spiral offers a probable site for interactions with Ca2+ ions. Muatations in the human amelogenin gene (AMGX) cause X-linked hypoplastic amelogenesis imperfecta, a disease characterised by defective enamel. A 9bp deletion in exon 2 of AMGX results in the loss of codons for Ile5, Leu6, Phe7 and Ala8, and replacement by a new threonine codon, disrupting the 16-residue (Met1-Ala16) amelogenin signal peptide.


Pssm-ID: 197891 [Multi-domain]  Cd Length: 165  Bit Score: 45.17  E-value: 3.15e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759   721 IQRRPHELPPQSQPwvmPSQSQPPvTPSQSHPqvmPSQSQPPVTPsqsqprvmpsqsQPPVMPSQSHPQLTPSQSQPPVT 800
Cdd:smart00818  85 TQHHQPNLPQPAQQ---PFQPQPL-QPPQPQQ---PMQPQPPVHP------------IPPLPPQPPLPPMFPMQPLPPLL 145

                           90
                   ....*....|....*.
gi 195232759   801 PSqrqpqlMPSQSQPP 816
Cdd:smart00818 146 PD------LPLEAWPA 155
PHA03378 PHA03378
EBNA-3B; Provisional
 721-816 3.25e-05

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 47.75  E-value: 3.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759 721 IQRRPHELPPQSQ-----------PWVMPSQSQPPVTPS-QSHP--QVMPSQSQPPVTPSQSQP-RVMPSQSQPPVMPSQ 785
Cdd:PHA03378 572 LQIQPLTSPTTSQlassapsyaqtPWPVPHPSQTPEPPTtQSHIpeTSAPRQWPMPLRPIPMRPlRMQPITFNVLVFPTP 651

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 195232759 786 SHP---QLTPSQS---QPPVTPSQ---------RQPQLMPSQSQPP 816
Cdd:PHA03378 652 HQPpqvEITPYKPtwtQIGHIPYQpsptgantmLPIQWAPGTMQPP 697
TYA pfam01021
Ty transposon capsid protein; Ty are yeast transposons. A 5.7kb transcript codes for p3 a ...
 699-820 4.28e-05

Ty transposon capsid protein; Ty are yeast transposons. A 5.7kb transcript codes for p3 a fusion protein of TYA and TYB. The TYA protein is analogous to the gag protein of retroviruses. TYA a is cleaved to form 46kd protein which can form mature virion like particles. This entry corresponds to the capsid protein from Ty1 and Ty2 transposons.


Pssm-ID: 425992  Cd Length: 384  Bit Score: 46.87  E-value: 4.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759  699 KKSKPIKKQQDVQTPSAKEEEKiqrrPHELPPQsqpwvmPSQSQPPvtpsqshpQVMPSQSQPPVTPSQSQPRVMPSQSQ 778
Cdd:pfam01021  29 KDSTKANSQQTTTPGSSAVPEN----HHHASPQ------PASVPPP--------QNGPYSQQCMMTPNQANPSGWPFYGH 90

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 195232759  779 PPVMPSqSHPQLTPSQSQPpvTPSQRQPQLMPSQSQPPVTPS 820
Cdd:pfam01021  91 PSMMPY-TPYQMSPMYFPP--GPQSQFPQYPSSVGTPLSTPS 129
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
 274-343 4.38e-05

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: 43.51  E-value: 4.38e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 195232759  274 SENITPRMQH---DTSHLFTTLGLRGLSGIGAFRGMCTPHRSCAIVTFMNKTLGTFSIAVAHHLGHNLGMNHD 343
Cdd:pfam13582  50 QEVNDTRIGQygyDLGHLFTGRDGGGGGGIAYVGGVCNSGSKFGVNSGSGPVGDTGADTFAHEIGHNFGLNHT 122
PRK12757 PRK12757
cell division protein FtsN; Provisional
 705-807 5.93e-05

cell division protein FtsN; Provisional


Pssm-ID: 237191 [Multi-domain]  Cd Length: 256  Bit Score: 45.42  E-value: 5.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759 705 KKQQDVQTPSA--KEEEKIQRRPHELPPQSQPwvmpsQSQPPVTPSQSHPQVMPSQSQPPVTPsqsqprvmpsQSQPPVM 782
Cdd:PRK12757  95 MRQQPTQLSEVpyNEQTPQVPRSTVQIQQQAQ-----QQQPPATTAQPQPVTPPRQTTAPVQP----------QTPAPVR 159

                         90       100
                 ....*....|....*....|....*
gi 195232759 783 PSQSHPQLTPSQsQPPVTPSQRQPQ 807
Cdd:PRK12757 160 TQPAAPVTQAVE-APKVEAEKEKEQ 183
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
 722-816 6.23e-05

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


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 44.26  E-value: 6.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759  722 QRRPHELPPQSQPWVMPSQSQPPVTPSQSHPQVMPSQSQPPVTPSQSQPRVMP--SQSQPPVMPSQSHPQLTPSQSQPPV 799
Cdd:pfam15240  17 QSSSEDVSQEDSPSLISEEEGQSQQGGQGPQGPPPGGFPPQPPASDDPPGPPPpgGPQQPPPQGGKQKPQGPPPQGGPRP 96

                          90       100
                  ....*....|....*....|
gi 195232759  800 TPSQRQ---PQLMPSQSQPP 816
Cdd:pfam15240  97 PPGKPQgppPQGGNQQQGPP 116
PHA03378 PHA03378
EBNA-3B; Provisional
 729-806 6.37e-05

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 46.60  E-value: 6.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759 729 PPQSQPWVM--PSQSQPPVTPSQSHPQVMPSQSQPPVTPS-QSQPRVMPSQSQPPvmpsQSHPqlTPSQSQPPVTPSQRQ 805
Cdd:PHA03378 746 PPAAAPGRArpPAAAPGRARPPAAAPGAPTPQPPPQAPPApQQRPRGAPTPQPPP----QAGP--TSMQLMPRAAPGQQG 819


                 .
gi 195232759 806 P 806
Cdd:PHA03378 820 P 820
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
708-818 6.87e-05

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 46.31  E-value: 6.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759 708 QDVQTPSAKEEEKIQRRPHELPPQSQPwVMPSQSQPPVTPSQSHPQVMPSQSQPPVTPSQSQPRVMPSQSQP-PVMPSQS 786
Cdd:PRK14971 364 QKGDDASGGRGPKQHIKPVFTQPAAAP-QPSAAAAASPSPSQSSAAAQPSAPQSATQPAGTPPTVSVDPPAAvPVNPPST 442

                         90       100       110
                 ....*....|....*....|....*....|..
gi 195232759 787 HPQLTPsqsqPPVTPSQRQPQLMPSQSQPPVT 818
Cdd:PRK14971 443 APQAVR----PAQFKEEKKIPVSKVSSLGPST 470
PHA03247 PHA03247
large tegument protein UL36; Provisional
 730-820 7.61e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.86  E-value: 7.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759  730 PQSQPwvMPSQSQPPVTPSQSHPQVMPSQSQP--PVTPSQSQPRVMPSQSQPPVMPSQSHPqlTPSQSQPPVTPSQRQPQ 807
Cdd:PHA03247 2569 PPPRP--APRPSEPAVTSRARRPDAPPQSARPraPVDDRGDPRGPAPPSPLPPDTHAPDPP--PPSPSPAANEPDPHPPP 2644

                          90
                  ....*....|...
gi 195232759  808 LMPSQSQPPVTPS 820
Cdd:PHA03247 2645 TVPPPERPRDDPA 2657
SAP130_C pfam16014
Histone deacetylase complex subunit SAP130 C-terminus;
743-819 7.92e-05

Histone deacetylase complex subunit SAP130 C-terminus;


Pssm-ID: 464973 [Multi-domain]  Cd Length: 371  Bit Score: 45.69  E-value: 7.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759  743 PPVTPSqshPQVMPSQS--QPPVT---PSQSQPRVMPSQSQPPVMPSQSHPQLTPSQSQPPVTPSqrQPQLMPSQSQPPV 817
Cdd:pfam16014  32 PPVTVA---VEALPGQNseQQTASaspPSQHPAQAIPTILAPAAPPSQPSVVLSTLPAAMAVTPP--IPASMANVVAPPT 106


                  ..
gi 195232759  818 TP 819
Cdd:pfam16014 107 QP 108
PHA03377 PHA03377
EBNA-3C; Provisional
 723-819 8.32e-05

EBNA-3C; Provisional


Pssm-ID: 177614 [Multi-domain]  Cd Length: 1000  Bit Score: 46.20  E-value: 8.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759  723 RRPHELPPQSqPWvmpsQSQPPVTPSQSHPQVMPSQSQ----PPVTPSQSQPRvmPSQSQPPVMPsqsHPQLTPSQSQPP 798
Cdd:PHA03377  815 QYPGHGHPQG-PW----APRPPHLPPQWDGSAGHGQDQvsqfPHLQSETGPPR--LQLSQVPQLP---YSQTLVSSSAPS 884

                          90       100
                  ....*....|....*....|...
gi 195232759  799 VTPSQRQPQL--MPSQSQPPVTP 819
Cdd:PHA03377  885 WSSPQPRAPIrpIPTRFPPPPMP 907
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
 736-820 8.68e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 46.01  E-value: 8.68e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759 736 VMPSQSQPPVTPSQSHPQVMPSQSQPPVTPSQSQPRVMPSQSQPPVMPSQSHPQLTPSQSQPPVTPSQRQPQLMPSQSQP 815
Cdd:PRK07994 364 PLPEPEVPPQSAAPAASAQATAAPTAAVAPPQAPAVPPPPASAPQQAPAVPLPETTSQLLAARQQLQRAQGATKAKKSEP 443


                 ....*
gi 195232759 816 PVTPS 820
Cdd:PRK07994 444 AAASR 448
YppG pfam14179
YppG-like protein; The YppG-like protein family includes the B. subtilis YppG protein, which ...
 747-798 1.12e-04

YppG-like protein; The YppG-like protein family includes the B. subtilis YppG protein, which is functionally uncharacterized. This family of proteins is found in bacteria. Proteins in this family are typically between 115 and 181 amino acids in length. There are two completely conserved residues (F and G) that may be functionally important.


Pssm-ID: 372950 [Multi-domain]  Cd Length: 101  Bit Score: 42.10  E-value: 1.12e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 195232759  747 PSQSHPQVMPSQSQPPVTPSQsQPRVMPSQSQPPVMP-SQSHPQLTPSQSQPP 798
Cdd:pfam14179   4 NSQPYPYFSQQVYQQPVQPQY-PPFAPQQYMPQPPMPyMNPYPKQQPQQQQPS 55
SP5_N cd22541
N-terminal domain of transcription factor Specificity Protein (SP) 5; Specificity Proteins ...
 724-815 1.51e-04

N-terminal domain of transcription factor Specificity Protein (SP) 5; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. There are many SPs in vertebrates (9 SPs in humans and mice, 7 SPs in the chicken, and 11 SPs in teleost fish), but arthropods only have 3 SPs. All of them contain clade SP5, which plays a potential role in human cancers and was found in several human tumors including hepatocellular carcinoma, gastric cancer, and colon cancer. Leukemia inhibitor factor/Stat3 and Wnt/beta-catenin signaling pathways converge on SP5 to promote mouse embryonic stem cell self-renewal. SP5 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. SP factors may be separated into three groups based on their domain architecture and the similarity of their N-terminal transactivation domains: SP1-4, SP5, and SP6-9. The transactivation domains between the three groups are not homologous to one another. This model represents the N-terminal domain of SP5.


Pssm-ID: 412096 [Multi-domain]  Cd Length: 143  Bit Score: 42.55  E-value: 1.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759 724 RPHELP------PQSQPWVMPSQSQPPVTPSQSHPQVMPSQSQPPVTPSQSQPRVMPSQSQPPVMPSQ--SHPQltpSQS 795
Cdd:cd22541    2 APHELPltppaePSFHQSLAYSFELSPVKMLPTPAPAPAASAPPHPSPVSSPTQQPQQLPPNPADDIPwwSIQQ---SNP 78

                         90       100
                 ....*....|....*....|
gi 195232759 796 QPPVTPSQRQPQLMPSQSQP 815
Cdd:cd22541   79 AHPPSTSTPLGHPTFAGYQP 98
KLF3_N cd21577
N-terminal domain of Kruppel-like factor 3; Kruppel-like factor 3 (KLF3; also called ...
 730-816 1.99e-04

N-terminal domain of Kruppel-like factor 3; Kruppel-like factor 3 (KLF3; also called Krueppel-like factor 3 and originally called Basic Kruppel-like Factor/BKLF), was the third member of the KLF family of zinc finger transcription factors to be discovered. KLF3 possesses a wide range of biological impacts on regulating apoptosis, differentiation, and proliferation in various tissues during the entire progression process. It has been proposed as a tumor suppressor in colorectal cancer. It appears to function predominantly as a repressor of transcription, turning genes off by recruiting the C-terminal Binding Protein co-repressors CtBP1 and CtBP2. CtBP docks onto a short motif (residues 61-65) in the N-terminus of KLF3, through the Proline-X-Aspartate-Leucine-Serine (PXDLS) motif. CtBP in turn recruits histone modifying enzymes to alter chromatin and repress gene expression. KLF3 belongs to a family of proteins, called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domain of KLF3.


Pssm-ID: 410554 [Multi-domain]  Cd Length: 214  Bit Score: 43.49  E-value: 1.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759 730 PQSQPWVMPSQSQPPVTPSQSHPQVMPSQSQPPVTPSQSQPRVMPSQSQP-PVMPSqSHPQLTPSQSQPPVTPSQrQPQL 808
Cdd:cd21577   58 PYSKSSPPSPPQQRPLSPPLSLPPPVAPPPLSPGSVPGGLPVISPVMVQPvPVLYP-PHLHQPIMVSSSPPPDDD-HHHH 135


                 ....*...
gi 195232759 809 MPSQSQPP 816
Cdd:cd21577  136 KASSMKPS 143
PRK11633 PRK11633
cell division protein DedD; Provisional
 728-816 2.93e-04

cell division protein DedD; Provisional


Pssm-ID: 236940 [Multi-domain]  Cd Length: 226  Bit Score: 43.07  E-value: 2.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759 728 LPPQSQPwvMPSQsqPP---VTPSQSHPQVMPSQSQPPVTPSQSQPRVMPSQSQPPVMPSQSHPQLTPSQSQPPVTPSQR 804
Cdd:PRK11633  56 MPAATQA--LPTQ--PPegaAEAVRAGDAAAPSLDPATVAPPNTPVEPEPAPVEPPKPKPVEKPKPKPKPQQKVEAPPAP 131

                         90
                 ....*....|..
gi 195232759 805 QPQLMPSQSQPP 816
Cdd:PRK11633 132 KPEPKPVVEEKA 143
KREPA2 cd23959
Kinetoplastid RNA Editing Protein A2 (KREPA2); The KREPA2 (TbMP63) protein is a component of ...
 734-816 3.17e-04

Kinetoplastid RNA Editing Protein A2 (KREPA2); The KREPA2 (TbMP63) protein is a component of the parasitic protozoan's KREPA RNA editing catalytic complex (RECC). Kinetoplastid RNA editing (KRE) proteins occur as pairs or sets of related proteins in multiple complexes. KREPA complex is composed of six components (KREPA1-6), which share a conserved C-terminal region containing an oligonucleotide-binding (OB)-fold-like domain. KREPAs are responsible for the site-specific insertion and deletion of U nucleotides in the kinetoplastid mitochondria pre-messenger RNA. Apart from the conserved C-terminal OB-fold domain, KREPA1, KREPA2, and KREPA3 contain two conserved C2H2 zinc-finger domains. KREPA2 and kinetoplastid RNA editing ligase 1 (KREL1) are specific for ligation post-U-deletion and are paralogous to KREL2 and KREPA1 that are specific for ligation post-U-insertion. KREPA2, is critical for RECC stability and KREL1 integration into the complex.


Pssm-ID: 467780 [Multi-domain]  Cd Length: 424  Bit Score: 44.09  E-value: 3.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759 734 PWVMPSQSQPPVTPSQSHPQVMPSQSQPPVTPSQSQPrvMPSQSQPPVMPSQSHPQLTPSQSQPPVTPSqrqPQLMPSQS 813
Cdd:cd23959  118 PFSASSSTQRETHKTAQVAPPKAEPQTAPVTPFGQLP--MFGQHPPPAKPLPAAAAAQQSSASPGEVAS---PFASGTVS 192


                 ...
gi 195232759 814 QPP 816
Cdd:cd23959  193 ASP 195
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 699-807 3.20e-04

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 44.26  E-value: 3.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759  699 KKSKPIKKQQDVQTPSAKEEEK---IQRRPHELPPQSQPWVMPSQSQPPvtPSQSHP----QVMPSQSQPPVTPSQSQPR 771
Cdd:pfam09770 208 KKPAQQPAPAPAQPPAAPPAQQaqqQQQFPPQIQQQQQPQQQPQQPQQH--PGQGHPvtilQRPQSPQPDPAQPSIQPQA 285

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 195232759  772 VMPSQSQPPVMPS--------------------------------QSHPQltpSQSQPPVTPSQRQPQ 807
Cdd:pfam09770 286 QQFHQQPPPVPVQptqilqnpnrlsaarvgypqnpqpgvqpapahQAHRQ---QGSFGRQAPIITHPQ 350
YppG pfam14179
YppG-like protein; The YppG-like protein family includes the B. subtilis YppG protein, which ...
 726-787 3.49e-04

YppG-like protein; The YppG-like protein family includes the B. subtilis YppG protein, which is functionally uncharacterized. This family of proteins is found in bacteria. Proteins in this family are typically between 115 and 181 amino acids in length. There are two completely conserved residues (F and G) that may be functionally important.


Pssm-ID: 372950 [Multi-domain]  Cd Length: 101  Bit Score: 40.56  E-value: 3.49e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 195232759  726 HELPPQSQPWVMPSQSQPPVTPsqSHPQVMPSQSQPPVTPSQSQPRVMPSQSQPPvmPSQSH 787
Cdd:pfam14179   1 YQHNSQPYPYFSQQVYQQPVQP--QYPPFAPQQYMPQPPMPYMNPYPKQQPQQQQ--PSQFQ 58
SAP130_C pfam16014
Histone deacetylase complex subunit SAP130 C-terminus;
729-820 3.64e-04

Histone deacetylase complex subunit SAP130 C-terminus;


Pssm-ID: 464973 [Multi-domain]  Cd Length: 371  Bit Score: 43.77  E-value: 3.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759  729 PPQSQPWVMPSQSQPPVTPSQSHPQVMPSQSQPPVTPsqSQPRVMPSQSQPPVMPSQSHPQLTPSQSQ-PPVTPSQRQPQ 807
Cdd:pfam16014  56 PSQHPAQAIPTILAPAAPPSQPSVVLSTLPAAMAVTP--PIPASMANVVAPPTQPAASSTAACAVSSVlPEIKIKQEAEP 133

                          90
                  ....*....|...
gi 195232759  808 LMPSQSQPPVTPS 820
Cdd:pfam16014 134 MDTSQSVPPLTPT 146
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
742-819 4.45e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 43.61  E-value: 4.45e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 195232759 742 QPPVTPSQSHPQVMPSQSQPPVTPSQSQPRVMPSQSQPPVMPSQSHPQLTPSQSQPPVT-PSQRQPQLMPSQSQPPVTP 819
Cdd:PRK14971 370 SGGRGPKQHIKPVFTQPAAAPQPSAAAAASPSPSQSSAAAQPSAPQSATQPAGTPPTVSvDPPAAVPVNPPSTAPQAVR 448
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 729-820 5.08e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.82  E-value: 5.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759 729 PPQSQPWVMPSQSQPPVTPSQSH-----PQVMPSQSQPPVTPSQSQPRVMPSQSQPPVMPSQSHPQLTPSQSQPPVTPSQ 803
Cdd:PRK07764 681 PPPAPAPAAPAAPAGAAPAQPAPapaatPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPP 760

                         90       100
                 ....*....|....*....|
gi 195232759 804 RQ---PQLMPSQSQPPVTPS 820
Cdd:PRK07764 761 PPapaPAAAPAAAPPPSPPS 780
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 729-820 5.08e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.82  E-value: 5.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759 729 PPQSQPWVMPSQSQPPVTPSQSHPQVMPSQSQPPVTPSQSQPRVMPSQSQPPVMPSQSHPQLTPSQSQPPVTPSQRQPQL 808
Cdd:PRK07764 416 APAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPA 495

                         90
                 ....*....|..
gi 195232759 809 MPSQSQPPVTPS 820
Cdd:PRK07764 496 APAAPAAPAGAD 507
KLF11_N cd21584
N-terminal domain of Kruppel-like factor 11; Kruppel-like factor 11 (KLF11; also known as ...
 739-820 5.37e-04

N-terminal domain of Kruppel-like factor 11; Kruppel-like factor 11 (KLF11; also known as Krueppel-like factor 11; Fetal Kruppel-like factor-1/FKLF-1; maturity-onset diabetes of the young 7/MODY7; TGFbeta Inducible Early Growth Response 2/TIEG2) is a protein that in humans is encoded by the KLF11 gene. KLF11 is involved in cell growth, apoptosis, cellular inflammation and differentiation, endometriosis, and cholesterol, prostaglandin, neurotransmitter, fat, and sugar metabolism. KLF9, KLF10, KLF11, KLF13, KLF14, and KLF16 share a conserved a-helical motif AA/VXXL that mediates their binding to Sin3A and their activities as transcriptional repressors. KLF11 belongs to a family of proteins, called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domain of KLF11.


Pssm-ID: 409242 [Multi-domain]  Cd Length: 217  Bit Score: 42.29  E-value: 5.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759 739 SQSQPPVTPSQSHPQVMPSQSQPPVTPSQSQPRVMPSQSQPPVMPSqshpqlTPSQSQP-PVTPSQRQPQLMPSQSQPPV 817
Cdd:cd21584   98 SSPPVPVPSPPVLCQMIPVSGQSGMISAFLQPPALSAGTVKPILPQ------TAPASQPlLVGSPVPQGTVMLVLPQASV 171


                 ...
gi 195232759 818 TPS 820
Cdd:cd21584  172 PQP 174
PRK11901 PRK11901
hypothetical protein; Reviewed
 738-805 6.22e-04

hypothetical protein; Reviewed


Pssm-ID: 237015 [Multi-domain]  Cd Length: 327  Bit Score: 42.75  E-value: 6.22e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 195232759 738 PSQSQPPVTPSQ----SHPQVMPSQSQP-PVTPSQSQPRVMPSQSQPPVMPSQSHPQL---TPSQSQPPVTPSQRQ 805
Cdd:PRK11901  66 SQQSSNNAGAEKnidlSGSSSLSSGNQSsPSAANNTSDGHDASGVKNTAPPQDISAPPispTPTQAAPPQTPNGQQ 141
KLF3_N cd21577
N-terminal domain of Kruppel-like factor 3; Kruppel-like factor 3 (KLF3; also called ...
 738-820 6.80e-04

N-terminal domain of Kruppel-like factor 3; Kruppel-like factor 3 (KLF3; also called Krueppel-like factor 3 and originally called Basic Kruppel-like Factor/BKLF), was the third member of the KLF family of zinc finger transcription factors to be discovered. KLF3 possesses a wide range of biological impacts on regulating apoptosis, differentiation, and proliferation in various tissues during the entire progression process. It has been proposed as a tumor suppressor in colorectal cancer. It appears to function predominantly as a repressor of transcription, turning genes off by recruiting the C-terminal Binding Protein co-repressors CtBP1 and CtBP2. CtBP docks onto a short motif (residues 61-65) in the N-terminus of KLF3, through the Proline-X-Aspartate-Leucine-Serine (PXDLS) motif. CtBP in turn recruits histone modifying enzymes to alter chromatin and repress gene expression. KLF3 belongs to a family of proteins, called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domain of KLF3.


Pssm-ID: 410554 [Multi-domain]  Cd Length: 214  Bit Score: 41.95  E-value: 6.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759 738 PSQSQPPVTPSQSHPQVMPSQSQPPVTPSQSQPRVMPSQSQPPvmPSQSHPQLTPSQSQPPVTPSQRQPQLMPSQSQP-P 816
Cdd:cd21577   32 PPSSSSSSSSSSSSSSSPSSRASPPSPYSKSSPPSPPQQRPLS--PPLSLPPPVAPPPLSPGSVPGGLPVISPVMVQPvP 109


                 ....
gi 195232759 817 VTPS 820
Cdd:cd21577  110 VLYP 113
PRK14950 PRK14950
DNA polymerase III subunits gamma and tau; Provisional
 727-804 6.83e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 43.26  E-value: 6.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759 727 ELPPQSQPWVMPSQSqPPVTPSQSHPQVMP---SQSQPPVTPSQSQPRVMPSQSQPPVMPSQSHP-QLTPSQSQPPVTPS 802
Cdd:PRK14950 374 AAPSPVRPTPAPSTR-PKAAAAANIPPKEPvreTATPPPVPPRPVAPPVPHTPESAPKLTRAAIPvDEKPKYTPPAPPKE 452


                 ..
gi 195232759 803 QR 804
Cdd:PRK14950 453 EE 454
KLF10_11_N cd21974
N-terminal domain of Kruppel-like factor (KLF) 10, KLF11, and similar proteins; This subfamily ...
 741-809 7.02e-04

N-terminal domain of Kruppel-like factor (KLF) 10, KLF11, and similar proteins; This subfamily is composed of Kruppel-like factor or Krueppel-like factor (KLF) 10, KLF11, and similar proteins. KLF10 was first identified in human osteoblasts and plays a role in mediating estrogen (E2) signaling in bone and skeletal homeostasis and a regulatory role in tumor formation and metastasis. KLF11 is involved in cell growth, apoptosis, cellular inflammation and differentiation, endometriosis, and cholesterol, prostaglandin, neurotransmitter, fat, and sugar metabolism. KLF9, KLF10, KLF11, KLF13, KLF14, and KLF16 share a conserved a-helical motif AA/VXXL that mediates their binding to Sin3A and their activities as transcriptional repressors. KLF10/11 belong to a family of proteins, called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domain of KLF10, KLF11, and similar proteins.


Pssm-ID: 409243 [Multi-domain]  Cd Length: 229  Bit Score: 41.84  E-value: 7.02e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759 741 SQPPVTPSQSHPQVMPSQSQPPVTPSQSQPRVMPSQ-SQPPVMpsqshpQLTPsqsQPPVTPSQRQPQLM 809
Cdd:cd21974  134 SSSGVIVAFLKAPQQPSPQPQKPALPQPQVVLVGGQvPQGPVM------LVVP---QPAVPQPYVQPTVV 194
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 729-820 7.33e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.05  E-value: 7.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759 729 PPQSQPWVMPSQSQPPVTPSQSHPQVMPSQSQPPVTPSQSQPrvmPSQSQPPVMPSQSHPqlTPSQSQPPVTPSQRQPQL 808
Cdd:PRK07764 412 PAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGA---PSPPPAAAPSAQPAP--APAAAPEPTAAPAPAPPA 486

                         90
                 ....*....|..
gi 195232759 809 MPSQSQPPVTPS 820
Cdd:PRK07764 487 APAPAAAPAAPA 498
Pneumo_att_G pfam05539
Pneumovirinae attachment membrane glycoprotein G;
698-819 7.92e-04

Pneumovirinae attachment membrane glycoprotein G;


Pssm-ID: 114270 [Multi-domain]  Cd Length: 408  Bit Score: 42.73  E-value: 7.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759  698 CKKSKpiKKQQDVQTPSAKEEEKIQRRPHELPPQSQPwvmPSQSQPPVTPSQSHPQVMPSQSQPPVTPSQSQPRVMPSQS 777
Cdd:pfam05539 165 CKEPK--TAVTTSKTTSWPTEVSHPTYPSQVTPQSQP---ATQGHQTATANQRLSSTEPVGTQGTTTSSNPEPQTEPPPS 239

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 195232759  778 QPPVMPSQSHPQLTPSQSQ---------------PPVTPSQRQPQlmpSQSQPPVTP 819
Cdd:pfam05539 240 QRGPSGSPQHPPSTTSQDQsttgdgqehtqrrktPPATSNRRSPH---STATPPPTT 293
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
702-817 9.61e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 42.84  E-value: 9.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759 702 KPIKKQQ--DVQTPSAKEEEKIQRRPHELPPQSQPwvmPSQSQPPVTPSQ-SHPQVMPSQSQPPVTPSQS-QPRVMPSQS 777
Cdd:PRK14971 380 KPVFTQPaaAPQPSAAAAASPSPSQSSAAAQPSAP---QSATQPAGTPPTvSVDPPAAVPVNPPSTAPQAvRPAQFKEEK 456

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 195232759 778 QPPVMPSQShpqLTPSQSQPpvtpsQRQPQLMPSQSQPPV 817
Cdd:PRK14971 457 KIPVSKVSS---LGPSTLRP-----IQEKAEQATGNIKEA 488
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 718-820 1.03e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 42.67  E-value: 1.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759 718 EEKIQRRPHELPPQSQPWVMPSQSQPPV-TPSQSHPQVMPSQSQPPVTPSQSQPRVMPSQSQPPVMPSQSHPQLTPSQSQ 796
Cdd:PRK07764 382 ERRLGVAGGAGAPAAAAPSAAAAAPAAApAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAA 461

                         90       100
                 ....*....|....*....|....
gi 195232759 797 PPVTPSQRQPQLMPSQSQPPVTPS 820
Cdd:PRK07764 462 PSAQPAPAPAAAPEPTAAPAPAPP 485
PLN02258 PLN02258
9-cis-epoxycarotenoid dioxygenase NCED
 731-813 1.12e-03

9-cis-epoxycarotenoid dioxygenase NCED


Pssm-ID: 215145 [Multi-domain]  Cd Length: 590  Bit Score: 42.38  E-value: 1.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759 731 QSQPWVMPSQSQPPVTPSQSHPQVMPSQSQPPvTPSQSQPRVMPSQSQPPVMPSQSHPQLTPSQSQPPVTPSQRQPQLMP 810
Cdd:PLN02258   1 SSSSNPTSRSQSHASSSSSSSSQSSPPSSTSP-RPRRRKPSASSLLHTPSILPLPKLSSPSPPSVTLPPAATTQTPQLNP 79


                 ...
gi 195232759 811 SQS 813
Cdd:PLN02258  80 LQR 82
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 729-820 1.14e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 42.67  E-value: 1.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759 729 PPQSQPWVMPSQSQPPVTPS-QSHPQVMPSQSQPPVTPSQSQPRVMPSQSQPPVMPSQSHPQLTPSQSQPPVTPSQRQPQ 807
Cdd:PRK07764 397 AAPSAAAAAPAAAPAPAAAApAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEP 476

                         90
                 ....*....|...
gi 195232759 808 LMPSQSQPPVTPS 820
Cdd:PRK07764 477 TAAPAPAPPAAPA 489
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 712-820 1.17e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 42.39  E-value: 1.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759 712 TPSAKEEEKIQRRPHELPPQSQPWVMPSQSQPPVTPSQSHPQvmPSQSQPPVTPSQSQPRVMPSQSQPPVMPSQSHPQLT 791
Cdd:PRK14951 383 RPEAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPPA--PVAAPAAAAPAAAPAAAPAAVALAPAPPAQAAPETV 460

                         90       100       110
                 ....*....|....*....|....*....|.
gi 195232759 792 --PSQSQPPVTPSQRQPQLMPSQSQPPVTPS 820
Cdd:PRK14951 461 aiPVRVAPEPAVASAAPAPAAAPAAARLTPT 491
PRK14950 PRK14950
DNA polymerase III subunits gamma and tau; Provisional
 734-819 1.53e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 42.10  E-value: 1.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759 734 PWVMPSQSQPPvTPSQSHPQVMPSQSqPPVTPSQSQPRVMP---SQSQPPVMPSQSHPQLTPSQSQPPVTPSQRQPQLMP 810
Cdd:PRK14950 364 PAPQPAKPTAA-APSPVRPTPAPSTR-PKAAAAANIPPKEPvreTATPPPVPPRPVAPPVPHTPESAPKLTRAAIPVDEK 441


                 ....*....
gi 195232759 811 SQSQPPVTP 819
Cdd:PRK14950 442 PKYTPPAPP 450
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 729-819 1.69e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.90  E-value: 1.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759 729 PPQSQPWVMPSQSQPPVTPSQSHPQVMPSQSQPPVTpsqsQPRVMPSQSQPPVMPSQSHPQLTPSQSQPPVTPSQRQPQL 808
Cdd:PRK07764 672 KAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAA----TPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDD 747

                         90
                 ....*....|.
gi 195232759 809 MPSQSQPPVTP 819
Cdd:PRK07764 748 PPDPAGAPAQP 758
PRK10856 PRK10856
cytoskeleton protein RodZ;
731-819 2.06e-03

cytoskeleton protein RodZ;


Pssm-ID: 236776 [Multi-domain]  Cd Length: 331  Bit Score: 41.17  E-value: 2.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759 731 QSQPWVMPSQSQPPVTPSQSHPQV-MPSQSQPPVTPSQSQPRVMPSQSQPpVMPSQSHPQLTPSQSQPPVTPSQRQPQLm 809
Cdd:PRK10856 160 QSVPLDTSTTTDPATTPAPAAPVDtTPTNSQTPAVATAPAPAVDPQQNAV-VAPSQANVDTAATPAPAAPATPDGAAPL- 237

                         90
                 ....*....|
gi 195232759 810 PSQSQPPVTP 819
Cdd:PRK10856 238 PTDQAGVSTP 247
DUF1720 pfam08226
Domain of unknown function (DUF1720); This domain is found in different combinations with ...
 728-791 2.08e-03

Domain of unknown function (DUF1720); This domain is found in different combinations with cortical patch components EF hand, SH3 and ENTH and is therefore likely to be involved in cytoskeletal processes. This family contains many hypothetical proteins.


Pssm-ID: 369766 [Multi-domain]  Cd Length: 75  Bit Score: 37.43  E-value: 2.08e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 195232759  728 LPPQSQPWVMPSQSQPPVTPSQSHPQ---VMPSQSQPpvTPSQSQP----RVMPSQSQP----PVMPSQSHPQLT 791
Cdd:pfam08226   1 MQPQQTGYMPPQQQQPQQTQQPLQPQptgFMPQQQTG--QGLQPQPtgmgQFQPLQPQQtgfqPQAQQGLQPQAT 73
PRK14950 PRK14950
DNA polymerase III subunits gamma and tau; Provisional
 718-812 2.23e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 41.33  E-value: 2.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759 718 EEKIQRRPHELPPQSQPwVMPSQSQPPVTPSQShPQVMPSQSQPPVTP---SQSQPRVMPSQSQPPVM-PSQSHPQLTPS 793
Cdd:PRK14950 357 EALLVPVPAPQPAKPTA-AAPSPVRPTPAPSTR-PKAAAAANIPPKEPvreTATPPPVPPRPVAPPVPhTPESAPKLTRA 434

                         90
                 ....*....|....*....
gi 195232759 794 QSQPPVTPSQRQPQLMPSQ 812
Cdd:PRK14950 435 AIPVDEKPKYTPPAPPKEE 453
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
 725-820 3.13e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 41.00  E-value: 3.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759 725 PHELPPQSQPWVMPSQSQPPVTPSQSHPQVMPSQSQPPVTPSQSQPRVMPSQSQPPVMPSQSHPQLTPSQSQPPVTPSQR 804
Cdd:PRK07994 371 PPQSAAPAASAQATAAPTAAVAPPQAPAVPPPPASAPQQAPAVPLPETTSQLLAARQQLQRAQGATKAKKSEPAAASRAR 450

                         90       100
                 ....*....|....*....|.
gi 195232759 805 -----QPQLMPSQSQPPVTPS 820
Cdd:PRK07994 451 pvnsaLERLASVRPAPSALEK 471
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 713-818 3.79e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 40.74  E-value: 3.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759 713 PSAKEEEKIQRRPHELPPQSQPWVMPSQSQPPVTPSQSHPQVMPSQSQPPVtpsqsQPRVMPSQSQPPVMPSQSHPQLTP 792
Cdd:PRK07764 414 AAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSA-----QPAPAPAAAPEPTAAPAPAPPAAP 488

                         90       100
                 ....*....|....*....|....*.
gi 195232759 793 SQSQPPVTPSQrqpqlmPSQSQPPVT 818
Cdd:PRK07764 489 APAAAPAAPAA------PAAPAGADD 508
KLF10_N cd21572
N-terminal domain of Kruppel-like factor 10; Kruppel-like factor 10 (KLF10; also known as ...
 729-820 4.49e-03

N-terminal domain of Kruppel-like factor 10; Kruppel-like factor 10 (KLF10; also known as Krueppel-like factor 10; early growth response(EGR)-alpha/EGRA; TGFbeta inducible early gene-1/TIEG1) is a protein that in humans is encoded by the KLF10 gene. KLF10 was first identified in human osteoblasts and plays a role in mediating estrogen (E2) signaling in bone and skeletal homeostasis and a regulatory role in tumor formation and metastasis. It may also play a role in adipocyte differentiation and adipose tissue function. KLF9, KLF10, KLF11, KLF13, KLF14, and KLF16 share a conserved a-helical motif AA/VXXL that mediates their binding to Sin3A and their activities as transcriptional repressors. KLF10 belongs to a family of proteins, called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domain of KLF10.


Pssm-ID: 409241 [Multi-domain]  Cd Length: 245  Bit Score: 39.58  E-value: 4.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759 729 PPQSQPWVMPSQSQPPVTPSQSHPQVMPSQSQPPVTPSqSQPRvmpSQ----------SQPPvmPSQSHPQLTPSQSQPP 798
Cdd:cd21572   60 PPYSPPHFEATHPPSAATLHPPAAQPPEEQHLSAETAA-SQQR---FQctsvirhtadAQPC--SCSSCPSSPSVVPSVP 133

                         90       100
                 ....*....|....*....|...
gi 195232759 799 VTPSQRQPqlMPSQSQ-PPVTPS 820
Cdd:cd21572  134 AGVAGVSP--VPVYCQiLPVSSS 154
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
 287-370 4.74e-03

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: 39.66  E-value: 4.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759 287 HLFT----TLGLRGLSGIGAFR-----GMCTPHR----------SCAIVTFMN--KTLGT--FSIAVAHHLGHNLGMNHD 343
Cdd:cd04270  105 HLFTyrdfDMGTLGLAYVGSPRdnsagGICEKAYyysngkkkylNTGLTTTVNygKRVPTkeSDLVTAHELGHNFGSPHD 184

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 195232759 344 EDTCRCSqP------RCIM--------HEGNppiTKFSNCS 370
Cdd:cd04270  185 PDIAECA-PgesqggNYIMyaratsgdKENN---KKFSPCS 221
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
 724-819 6.30e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 40.23  E-value: 6.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759 724 RPHELPPQSQpwvMPSQSQPPVTPSQSHPQVMPSQSQPPVTPSQSQPRVMPSQSQPPVMP------SQSHPQLTPSQSQP 797
Cdd:PRK07994 360 HPAAPLPEPE---VPPQSAAPAASAQATAAPTAAVAPPQAPAVPPPPASAPQQAPAVPLPettsqlLAARQQLQRAQGAT 436

                         90       100
                 ....*....|....*....|..
gi 195232759 798 PVTPSQRQPQLMPSQSQPPVTP 819
Cdd:PRK07994 437 KAKKSEPAAASRARPVNSALER 458
KLF4_N cd21582
N-terminal domain of Kruppel-like factor 4; Kruppel-like factor 4 (KLF4; also known as ...
 724-819 6.52e-03

N-terminal domain of Kruppel-like factor 4; Kruppel-like factor 4 (KLF4; also known as Krueppel-like factor 4 or gut-enriched Kruppel-like factor/GKLF) is a protein that, in humans, is encoded by the KLF4 gene. Evidence also suggests that KLF4 is a tumor suppressor in certain cancers, including colorectal cancer, gastric cancer, esophageal squamous cell carcinoma, intestinal cancer, prostate cancer, bladder cancer and lung cancer. It may act as a tumor promoter where increased KLF4 expression has been reported, such as in oral squamous cell carcinoma and in primary breast ductal carcinoma. KLF4 is one of four key factors that are essential for inducing pluripotent stem cells. KLF4 is highly expressed in non-dividing cells and its overexpression induces cell cycle arrest. KLF proteins KLF1, KLF2, KLF4, KLF5, KLF6, and KLF7 are transcriptional activators. KLF4 belongs to a family of proteins called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domain of KLF4, which is related to the N-terminal domains of KLF1 and KLF2.


Pssm-ID: 409228 [Multi-domain]  Cd Length: 335  Bit Score: 39.68  E-value: 6.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195232759 724 RPHELPPQSQPWVMPSQSQPPVTPSQSHPQvMPSQSQPPVTPSQSQPrvmpsqsqppvmPSQSHPQLTPSQSQPpvtpsQ 803
Cdd:cd21582  241 LPSRTTPSGGPGGGNSSTAESLMSRDHHPS-SQVLSHPPLPLPQGYH------------PSPGYPPFPPPPSQP-----Q 302

                         90
                 ....*....|....*.
gi 195232759 804 RQPQLMPSQSQPPVTP 819
Cdd:cd21582  303 QYQELMSPGSCLPEEP 318
YppG pfam14179
YppG-like protein; The YppG-like protein family includes the B. subtilis YppG protein, which ...
 765-816 6.85e-03

YppG-like protein; The YppG-like protein family includes the B. subtilis YppG protein, which is functionally uncharacterized. This family of proteins is found in bacteria. Proteins in this family are typically between 115 and 181 amino acids in length. There are two completely conserved residues (F and G) that may be functionally important.


Pssm-ID: 372950 [Multi-domain]  Cd Length: 101  Bit Score: 36.71  E-value: 6.85e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 195232759  765 PSQSQPRVMPSQSQPPVMPSqsHPQLTPSQ--SQPPVTPSQRQPQLMPSQSQPP 816
Cdd:pfam14179   4 NSQPYPYFSQQVYQQPVQPQ--YPPFAPQQymPQPPMPYMNPYPKQQPQQQQPS 55
myxo_disulf_rpt TIGR02232
Myxococcus cysteine-rich repeat; This model represents a sequence region shared between ...
 397-437 7.26e-03

Myxococcus cysteine-rich repeat; This model represents a sequence region shared between several proteins of Myxococcus xanthus DK 1622 and some eukaryotic proteins that include human pappalysin-1 (SP|Q13219). The region of about 40 amino acids contains several conserved Cys residues presumed to form disulfide bonds. The region appears in up to 13 repeats in Myxococcus.


Pssm-ID: 200169 [Multi-domain]  Cd Length: 38  Bit Score: 35.04  E-value: 7.26e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 195232759  397 VKRCGNGVVEEGEECDCGPLKhcAKDPCCLSnCTLTDGSTC 437
Cdd:TIGR02232   1 APTCGDGIIEPGEECDDGNTT--SGDGCSAT-CRLEEGFAC 38
COG1913 COG1913
Predicted Zn-dependent protease [General function prediction only];
330-360 7.50e-03

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


Pssm-ID: 441517  Cd Length: 175  Bit Score: 38.40  E-value: 7.50e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 195232759 330 VAHHLGHNLGMNHdedtcrCSQPRCIMHEGN 360
Cdd:COG1913  127 AVHELGHLFGLGH------CPNPRCVMHFSN 151
 
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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