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Conserved domains on  [gi|73765552|ref|NP_055084|]
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disintegrin and metalloproteinase domain-containing protein 29 preproprotein [Homo sapiens]

Protein Classification

ZnMc_adamalysin_II_like and ACR domain-containing protein (domain architecture ID 13660304)

protein containing domains Pep_M12B_propep, ZnMc_adamalysin_II_like, Disintegrin, and ACR

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 8.39e-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  Cd Length: 194  Bit Score: 220.18  E-value: 8.39e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552 198 RIVEIVVVIDNYLYIRYERNDSKLLEDLYVIVNIVDSILDVIGVKVLLFGLEIWTNKNLI-VVDDVRKSVHLYCKWKSEN 276
Cdd:cd04269   1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKIsVSGDAGETLNRFLDWKRSN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552 277 ITPRMQHDTSHLFTTLGLRG-LSGIGAFRGMCTPHRSCAIVTFMNKTLGTFSIAVAHHLGHNLGMNHDEDTCRCSQPRCI 355
Cdd:cd04269  81 LLPRKPHDNAQLLTGRDFDGnTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRSTCI 160
                       170       180       190
                ....*....|....*....|....*....|...
gi 73765552 356 MHEGNPPITK-FSNCSYGDFWEYTVER-TKCLL 386
Cdd:cd04269 161 MAPSPSSLTDaFSNCSYEDYQKFLSRGgGQCLL 193
ACR smart00608
ADAM Cysteine-Rich Domain;
483-618 2.92e-55

ADAM Cysteine-Rich Domain;


:

Pssm-ID: 214743  Cd Length: 137  Bit Score: 186.41  E-value: 2.92e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552    483 DGIPCK-ERGYCYEKSCHDRNEQCRRIFGAGANTASETCYKELNTLGDRVGHCGIKNATYIKCNISDVQCGRIQCENVTE 561
Cdd:smart00608   2 DGTPCDnGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVSE 81
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 73765552    562 IPNMSDHTTVHWARFNDIMCWSTDYHLGMKgPDIGEVKDGTECGIDHICIHRHCVHI 618
Cdd:smart00608  82 LPLLGEHATVIYSNIGGLVCWSLDYHLGTD-PDIGMVKDGTKCGPGKVCINGQCVDV 137
Disintegrin pfam00200
Disintegrin;
406-478 9.38e-36

Disintegrin;


:

Pssm-ID: 333919  Cd Length: 74  Bit Score: 129.24  E-value: 9.38e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 73765552   406 EEGEECDCGPLKHCAKDPCCLS-NCTLTDGSTCAFGLCCKDCKFLPSGKVCRKEVNECDLPEWCNGTSHKCPDD 478
Cdd:pfam00200   1 EEGEECDCGSTEECANDPCCDPkTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPAVNECDLPEYCNGTSAECPPD 74
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
32-150 5.51e-33

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: 334593  Cd Length: 125  Bit Score: 123.45  E-value: 5.51e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552    32 DVVIPVRITGTTR-----GMTPPGWLSYILPFGGQKHIIHIKVKKLLFSKHLPVFTYTDQGAILEDQPFVQNNCYYHGYV 106
Cdd:pfam01562   1 EIVIPVRVDASGRrrrslSSEYPDQLHYRLSAFGKEFHLHLEPNRGLLAPGFTVETYGEDGTEVTDQPPIQDHCHYQGHV 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 73765552   107 EGDPESLVSLSTCFGGfQGILQINDFAYEIKPL--AFSTTFEHLVY 150
Cdd:pfam01562  81 EGHPDSSVALSTCSGL-RGVIRTDNEEYFIEPLesSEEEGHPHVVY 125
Amelogenin super family cl33250
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
725-816 1.19e-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.


The actual alignment was detected with superfamily member smart00818:

Pssm-ID: 197891 [Multi-domain]  Cd Length: 165  Bit Score: 60.57  E-value: 1.19e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552    725 PHELP--PQSQPWV-----MPSQSQPPVTPSQSHPQVMPSQSQPPV--TPSQSQPRVMPSQSQPPVMPsqsHPQLTPSQS 795
Cdd:smart00818  55 HHHIPvlPAQQPVVpqqplMPVPGQHSMTPTQHHQPNLPQPAQQPFqpQPLQPPQPQQPMQPQPPVHP---IPPLPPQPP 131
                           90       100
                   ....*....|....*....|.
gi 73765552    796 QPPVTPSQRQPQLMPSQSQPP 816
Cdd:smart00818 132 LPPMFPMQPLPPLLPDLPLEA 152
 
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 8.39e-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  Cd Length: 194  Bit Score: 220.18  E-value: 8.39e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552 198 RIVEIVVVIDNYLYIRYERNDSKLLEDLYVIVNIVDSILDVIGVKVLLFGLEIWTNKNLI-VVDDVRKSVHLYCKWKSEN 276
Cdd:cd04269   1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKIsVSGDAGETLNRFLDWKRSN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552 277 ITPRMQHDTSHLFTTLGLRG-LSGIGAFRGMCTPHRSCAIVTFMNKTLGTFSIAVAHHLGHNLGMNHDEDTCRCSQPRCI 355
Cdd:cd04269  81 LLPRKPHDNAQLLTGRDFDGnTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRSTCI 160
                       170       180       190
                ....*....|....*....|....*....|...
gi 73765552 356 MHEGNPPITK-FSNCSYGDFWEYTVER-TKCLL 386
Cdd:cd04269 161 MAPSPSSLTDaFSNCSYEDYQKFLSRGgGQCLL 193
ACR smart00608
ADAM Cysteine-Rich Domain;
483-618 2.92e-55

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 186.41  E-value: 2.92e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552    483 DGIPCK-ERGYCYEKSCHDRNEQCRRIFGAGANTASETCYKELNTLGDRVGHCGIKNATYIKCNISDVQCGRIQCENVTE 561
Cdd:smart00608   2 DGTPCDnGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVSE 81
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 73765552    562 IPNMSDHTTVHWARFNDIMCWSTDYHLGMKgPDIGEVKDGTECGIDHICIHRHCVHI 618
Cdd:smart00608  82 LPLLGEHATVIYSNIGGLVCWSLDYHLGTD-PDIGMVKDGTKCGPGKVCINGQCVDV 137
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
483-596 3.15e-50

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: 337086  Cd Length: 115  Bit Score: 171.64  E-value: 3.15e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552   483 DGIPCK-ERGYCYEKSCHDRNEQCRRIFGAGANTASETCYKELNTLGDRVGHCGIKNATYIKCNISDVQCGRIQCENVTE 561
Cdd:pfam08516   1 DGTPCSnGTAYCYNGRCRDRDRQCQEIFGKGAKSAPDACYEEVNTKGDRFGNCGRTNGGYVKCNKRDVLCGKLQCTNVTE 80
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 73765552   562 IPNMSDHTTVHWARFNDIMCWSTDYHLGMKGPDIG 596
Cdd:pfam08516  81 LPRLGEHATVIYTYINGHTCWGTDYHLGMDVPDPG 115
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
198-386 3.17e-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 and fertilin. Fertilin and closely related proteins appear to not have some active site residues and may not be active enzymes.


Pssm-ID: 307535  Cd Length: 199  Bit Score: 146.65  E-value: 3.17e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552   198 RIVEIVVVIDNYLYIRYERNDSKLLEDLYVIVNIVDSILDVIGVKVLLFGLEIWTNKNLI-VVDDVRKSVHLYCKWKSEN 276
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDVNVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIdVSGDANDTLRNFLKWRQEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552   277 ITPRMQHDTSHLFTTLGLRGL-SGIGAFRGMCTPHRSCAIVTFMNKTLGTFSIAVAHHLGHNLGMNHDEDT-CRC-SQPR 353
Cdd:pfam01421  81 LKKRKPHDVAQLLSGRTFGGTtVGAAYPGGMCSPSYSGGVNLDHKINVEGFAVTMAHELGHNLGMTHDDITgCKCpPGGG 160
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 73765552   354 CIMHE--GNPPITKFSNCSYGDFWEYTVE-RTKCLL 386
Cdd:pfam01421 161 CIMNPsaGSSFGRKFSNCSQDDFEQFLLKqKGACLF 196
Disintegrin pfam00200
Disintegrin;
406-478 9.38e-36

Disintegrin;


Pssm-ID: 333919  Cd Length: 74  Bit Score: 129.24  E-value: 9.38e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 73765552   406 EEGEECDCGPLKHCAKDPCCLS-NCTLTDGSTCAFGLCCKDCKFLPSGKVCRKEVNECDLPEWCNGTSHKCPDD 478
Cdd:pfam00200   1 EEGEECDCGSTEECANDPCCDPkTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPAVNECDLPEYCNGTSAECPPD 74
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
32-150 5.51e-33

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: 334593  Cd Length: 125  Bit Score: 123.45  E-value: 5.51e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552    32 DVVIPVRITGTTR-----GMTPPGWLSYILPFGGQKHIIHIKVKKLLFSKHLPVFTYTDQGAILEDQPFVQNNCYYHGYV 106
Cdd:pfam01562   1 EIVIPVRVDASGRrrrslSSEYPDQLHYRLSAFGKEFHLHLEPNRGLLAPGFTVETYGEDGTEVTDQPPIQDHCHYQGHV 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 73765552   107 EGDPESLVSLSTCFGGfQGILQINDFAYEIKPL--AFSTTFEHLVY 150
Cdd:pfam01562  81 EGHPDSSVALSTCSGL-RGVIRTDNEEYFIEPLesSEEEGHPHVVY 125
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
406-480 2.49e-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: 2.49e-32
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 73765552    406 EEGEECDCGPLKHCaKDPCC-LSNCTLTDGSTCAFGLCCKDCKFLPSGKVCRKEVNECDLPEWCNGTSHKCPDDFY 480
Cdd:smart00050   1 EEGEECDCGSPKEC-TDPCCdPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
725-816 1.19e-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: 1.19e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552    725 PHELP--PQSQPWV-----MPSQSQPPVTPSQSHPQVMPSQSQPPV--TPSQSQPRVMPSQSQPPVMPsqsHPQLTPSQS 795
Cdd:smart00818  55 HHHIPvlPAQQPVVpqqplMPVPGQHSMTPTQHHQPNLPQPAQQPFqpQPLQPPQPQQPMQPQPPVHP---IPPLPPQPP 131
                           90       100
                   ....*....|....*....|.
gi 73765552    796 QPPVTPSQRQPQLMPSQSQPP 816
Cdd:smart00818 132 LPPMFPMQPLPPLLPDLPLEA 152
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
702-820 5.94e-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 characteristic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 335243 [Multi-domain]  Cd Length: 980  Bit Score: 62.73  E-value: 5.94e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552   702 KPIKKQQDVQTPSAkeeekiQRRPHELPPQSQPwVMPSQSQPPV-TPSQSHPqvMPSQSQPPVTPSQSQPRVMPSqSQPP 780
Cdd:pfam03154 386 KPLSSLPTHHPPSA------HPPPLQLMPQSQQ-LPSPPAQPPVlTQSQSHP--PKASPHPPTAASHSLPSQSPF-PQHS 455
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 73765552   781 VMPSQSHPQLTPSQSQPPVTPSQRQPQlMPSQSQPPVTPS 820
Cdd:pfam03154 456 FSPSGSPPVTPPSGPPPSPSPSMPGLQ-PPSSSATSVSSS 494
PHA03247 PHA03247
large tegument protein UL36; Provisional
721-815 2.73e-08

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 57.64  E-value: 2.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552   721 IQRRPHELPPQSQPWVMP-----SQSQPPVTPS-QSHPQVMPSQSQPPVTPSQSQPRvmpSQSQPPVMPSQSHPQLTPSQ 794
Cdd:PHA03247 2862 VRRRPPSRSPAAKPAAPArppvrRLARPAVSRStESFALPPDQPERPPQPQAPPPPQ---PQPQPPPPPQPQPPPPPPPR 2938
                          90       100
                  ....*....|....*....|..
gi 73765552   795 SQPPVTP-SQRQPQLMPSQSQP 815
Cdd:PHA03247 2939 PQPPLAPtTDPAGAGEPSGAVP 2960
DedD COG3147
Cell division protein DedD (periplasmic protein involved in septation) [Cell cycle control, ...
707-810 1.91e-05

Cell division protein DedD (periplasmic protein involved in septation) [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 225689 [Multi-domain]  Cd Length: 226  Bit Score: 46.42  E-value: 1.91e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552 707 QQDVQTPSAKEEEKIQR-RPHELPPQSQPWVMPSQSQPPVTPSQSH---PQVMPSQSQP----PVTPSQSQPRVMPSQSQ 778
Cdd:COG3147  35 QDEVAAIPLPPKPQGDRdEPRVLPAVVQVVALPTQPPEGVAQEIQDagdAAAASVDPQPvaqpPVESTPAGVPVAAQTPK 114
                        90       100       110
                ....*....|....*....|....*....|....
gi 73765552 779 PPVMPSQ--SHPQLTPSQSQPPVTPsQRQPQLMP 810
Cdd:COG3147 115 PVKPPKQppAGAVPAKPTPKPEPKP-VAEPAAAP 147
myxo_disulf_rpt TIGR02232
Myxococcus cysteine-rich repeat; This model represents a sequence region shared between ...
397-437 6.20e-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  Cd Length: 38  Bit Score: 35.04  E-value: 6.20e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 73765552   397 VKRCGNGVVEEGEECDCGPLKhcAKDPCCLSnCTLTDGSTC 437
Cdd:TIGR02232   1 APTCGDGIIEPGEECDDGNTT--SGDGCSAT-CRLEEGFAC 38
 
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 8.39e-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  Cd Length: 194  Bit Score: 220.18  E-value: 8.39e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552 198 RIVEIVVVIDNYLYIRYERNDSKLLEDLYVIVNIVDSILDVIGVKVLLFGLEIWTNKNLI-VVDDVRKSVHLYCKWKSEN 276
Cdd:cd04269   1 KYVELVVVVDNSLYKKYGSNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTDKDKIsVSGDAGETLNRFLDWKRSN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552 277 ITPRMQHDTSHLFTTLGLRG-LSGIGAFRGMCTPHRSCAIVTFMNKTLGTFSIAVAHHLGHNLGMNHDEDTCRCSQPRCI 355
Cdd:cd04269  81 LLPRKPHDNAQLLTGRDFDGnTVGLAYVGGMCSPKYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDDGGCTCGRSTCI 160
                       170       180       190
                ....*....|....*....|....*....|...
gi 73765552 356 MHEGNPPITK-FSNCSYGDFWEYTVER-TKCLL 386
Cdd:cd04269 161 MAPSPSSLTDaFSNCSYEDYQKFLSRGgGQCLL 193
ACR smart00608
ADAM Cysteine-Rich Domain;
483-618 2.92e-55

ADAM Cysteine-Rich Domain;


Pssm-ID: 214743  Cd Length: 137  Bit Score: 186.41  E-value: 2.92e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552    483 DGIPCK-ERGYCYEKSCHDRNEQCRRIFGAGANTASETCYKELNTLGDRVGHCGIKNATYIKCNISDVQCGRIQCENVTE 561
Cdd:smart00608   2 DGTPCDnGQGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGDRFGNCGRENGTYIPCAPEDVKCGKLQCTNVSE 81
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 73765552    562 IPNMSDHTTVHWARFNDIMCWSTDYHLGMKgPDIGEVKDGTECGIDHICIHRHCVHI 618
Cdd:smart00608  82 LPLLGEHATVIYSNIGGLVCWSLDYHLGTD-PDIGMVKDGTKCGPGKVCINGQCVDV 137
ADAM_CR pfam08516
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ...
483-596 3.15e-50

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: 337086  Cd Length: 115  Bit Score: 171.64  E-value: 3.15e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552   483 DGIPCK-ERGYCYEKSCHDRNEQCRRIFGAGANTASETCYKELNTLGDRVGHCGIKNATYIKCNISDVQCGRIQCENVTE 561
Cdd:pfam08516   1 DGTPCSnGTAYCYNGRCRDRDRQCQEIFGKGAKSAPDACYEEVNTKGDRFGNCGRTNGGYVKCNKRDVLCGKLQCTNVTE 80
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 73765552   562 IPNMSDHTTVHWARFNDIMCWSTDYHLGMKGPDIG 596
Cdd:pfam08516  81 LPRLGEHATVIYTYINGHTCWGTDYHLGMDVPDPG 115
Reprolysin pfam01421
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ...
198-386 3.17e-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 and fertilin. Fertilin and closely related proteins appear to not have some active site residues and may not be active enzymes.


Pssm-ID: 307535  Cd Length: 199  Bit Score: 146.65  E-value: 3.17e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552   198 RIVEIVVVIDNYLYIRYERNDSKLLEDLYVIVNIVDSILDVIGVKVLLFGLEIWTNKNLI-VVDDVRKSVHLYCKWKSEN 276
Cdd:pfam01421   1 KYIELFIVVDKQLFQKMGSDVNVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTDEDKIdVSGDANDTLRNFLKWRQEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552   277 ITPRMQHDTSHLFTTLGLRGL-SGIGAFRGMCTPHRSCAIVTFMNKTLGTFSIAVAHHLGHNLGMNHDEDT-CRC-SQPR 353
Cdd:pfam01421  81 LKKRKPHDVAQLLSGRTFGGTtVGAAYPGGMCSPSYSGGVNLDHKINVEGFAVTMAHELGHNLGMTHDDITgCKCpPGGG 160
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 73765552   354 CIMHE--GNPPITKFSNCSYGDFWEYTVE-RTKCLL 386
Cdd:pfam01421 161 CIMNPsaGSSFGRKFSNCSQDDFEQFLLKqKGACLF 196
Disintegrin pfam00200
Disintegrin;
406-478 9.38e-36

Disintegrin;


Pssm-ID: 333919  Cd Length: 74  Bit Score: 129.24  E-value: 9.38e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 73765552   406 EEGEECDCGPLKHCAKDPCCLS-NCTLTDGSTCAFGLCCKDCKFLPSGKVCRKEVNECDLPEWCNGTSHKCPDD 478
Cdd:pfam00200   1 EEGEECDCGSTEECANDPCCDPkTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPAVNECDLPEYCNGTSAECPPD 74
Pep_M12B_propep pfam01562
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ...
32-150 5.51e-33

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: 334593  Cd Length: 125  Bit Score: 123.45  E-value: 5.51e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552    32 DVVIPVRITGTTR-----GMTPPGWLSYILPFGGQKHIIHIKVKKLLFSKHLPVFTYTDQGAILEDQPFVQNNCYYHGYV 106
Cdd:pfam01562   1 EIVIPVRVDASGRrrrslSSEYPDQLHYRLSAFGKEFHLHLEPNRGLLAPGFTVETYGEDGTEVTDQPPIQDHCHYQGHV 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 73765552   107 EGDPESLVSLSTCFGGfQGILQINDFAYEIKPL--AFSTTFEHLVY 150
Cdd:pfam01562  81 EGHPDSSVALSTCSGL-RGVIRTDNEEYFIEPLesSEEEGHPHVVY 125
DISIN smart00050
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ...
406-480 2.49e-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: 2.49e-32
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 73765552    406 EEGEECDCGPLKHCaKDPCC-LSNCTLTDGSTCAFGLCCKDCKFLPSGKVCRKEVNECDLPEWCNGTSHKCPDDFY 480
Cdd:smart00050   1 EEGEECDCGSPKEC-TDPCCdPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
ZnMc_ADAM_like cd04267
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ...
198-372 2.56e-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: 2.56e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552 198 RIVEIVVVIDNYLYIRYERNDSKLLEDLYVIVNIVDSILDVI----GVKVLLFGLEIWTNKNLIVVDDVRKSVHL--YCK 271
Cdd:cd04267   1 REIELVVVADHRMVSYFNSDENILQAYITELINIANSIYRSTnlrlGIRISLEGLQILKGEQFAPPIDSDASNTLnsFSF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552 272 WKSENitpRMQHDTSHLFT--TLGLRGLSGIGAFRGMCTPHRSCAIVTFMNKTLGTfSIAVAHHLGHNLGMNHDEDTC-- 347
Cdd:cd04267  81 WRAEG---PIRHDNAVLLTaqDFIEGDILGLAYVGSMCNPYSSVGVVEDTGFTLLT-ALTMAHELGHNLGAEHDGGDEla 156
                       170       180
                ....*....|....*....|....*....
gi 73765552 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 3.18e-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: 3.18e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552 198 RIVEIVVVIDNYLYIRYerNDSKLLEDLYVIVNIVDSIL--DVIG--VKVLLFGLEIWTN--KNLIVVDDVRKSVHLYCK 271
Cdd:cd04273   1 RYVETLVVADSKMVEFH--HGEDLEHYILTLMNIVASLYkdPSLGnsINIVVVRLIVLEDeeSGLLISGNAQKSLKSFCR 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552 272 WKSENITPR----MQHDTSHLFT---------TLGLRGLSGIGafrGMCTPHRSCAIvtfmNKTLGtFSIA--VAHHLGH 336
Cdd:cd04273  79 WQKKLNPPNdsdpEHHDHAILLTrqdicrsngNCDTLGLAPVG---GMCSPSRSCSI----NEDTG-LSSAftIAHELGH 150
                       170       180
                ....*....|....*....|...
gi 73765552 337 NLGMNHDEDTCRC---SQPRCIM 356
Cdd:cd04273 151 VLGMPHDGDGNSCgpeGKDGHIM 173
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
725-816 1.19e-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: 1.19e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552    725 PHELP--PQSQPWV-----MPSQSQPPVTPSQSHPQVMPSQSQPPV--TPSQSQPRVMPSQSQPPVMPsqsHPQLTPSQS 795
Cdd:smart00818  55 HHHIPvlPAQQPVVpqqplMPVPGQHSMTPTQHHQPNLPQPAQQPFqpQPLQPPQPQQPMQPQPPVHP---IPPLPPQPP 131
                           90       100
                   ....*....|....*....|.
gi 73765552    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 1.53e-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: 1.53e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552    726 HELPPQSQPWVMPSQS----QPPVTPSQSHPQVMPSQSQPPVTPSQSQPrvmPSQSQPPvMPSQSHPqltPSQSQPPVTP 801
Cdd:smart00818  50 HTLQPHHHIPVLPAQQpvvpQQPLMPVPGQHSMTPTQHHQPNLPQPAQQ---PFQPQPL-QPPQPQQ---PMQPQPPVHP 122
                           90       100
                   ....*....|....*....|....
gi 73765552    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 ...
702-820 5.94e-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 characteristic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 335243 [Multi-domain]  Cd Length: 980  Bit Score: 62.73  E-value: 5.94e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552   702 KPIKKQQDVQTPSAkeeekiQRRPHELPPQSQPwVMPSQSQPPV-TPSQSHPqvMPSQSQPPVTPSQSQPRVMPSqSQPP 780
Cdd:pfam03154 386 KPLSSLPTHHPPSA------HPPPLQLMPQSQQ-LPSPPAQPPVlTQSQSHP--PKASPHPPTAASHSLPSQSPF-PQHS 455
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 73765552   781 VMPSQSHPQLTPSQSQPPVTPSQRQPQlMPSQSQPPVTPS 820
Cdd:pfam03154 456 FSPSGSPPVTPPSGPPPSPSPSMPGLQ-PPSSSATSVSSS 494
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
701-819 1.12e-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 characteristic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 335243 [Multi-domain]  Cd Length: 980  Bit Score: 61.96  E-value: 1.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552   701 SKPIKKQQDVQTPSAKEEEKIQRRPHELPPQSQPWVMPSQSQPP---VTPSQSHPQVMPSQSQPPVTPSQSQPRVMP--- 774
Cdd:pfam03154 209 SPPTTQPPLQPLPVASPHTLIQQTPTLHPQRLPSPHPPLQPMPDppsQVSPQSAPQPGLHGPMPPMPHSLQGPSHLPhpg 288
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 73765552   775 -----SQSQPPVMPS------QSHPQLTPSQSQPPVT-PSQRQ-----PQLMPSQSQPPVTP 819
Cdd:pfam03154 289 ppqpfGQGQVPPPPSlqaphpSQLQHTPPSQSQGPSPqPPREQplppaPLSMPHIKPPPTTP 350
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
707-820 1.75e-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 characteristic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 335243 [Multi-domain]  Cd Length: 980  Bit Score: 61.19  E-value: 1.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552   707 QQDVQTPSAKEEEKIQRRPHELPPQSQPWVMPSQSQPPVTP------SQSH------------PQvMPSQSQPP--VTPS 766
Cdd:pfam03154 310 SQLQHTPPSQSQGPSPQPPREQPLPPAPLSMPHIKPPPTTPipqlpnPQSHkhpphlsapspfPQ-MPSNLPPPpaLKPL 388
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 73765552   767 QSQPRVMPSQSQPP---VMPsQSHPqLTPSQSQPPVTpSQRQPQLMPSQSQPPVTPS 820
Cdd:pfam03154 389 SSLPTHHPPSAHPPplqLMP-QSQQ-LPSPPAQPPVL-TQSQSHPPKASPHPPTAAS 442
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
699-819 1.84e-09

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


Pssm-ID: 313063 [Multi-domain]  Cd Length: 837  Bit Score: 61.18  E-value: 1.84e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552   699 KKSKPIKKQQDVQTPSAKEEEKI--------QRRPHELPPQSQPWVMPSQsQPPVTPsqsHPQVMPSQSQPPVTPSQSQP 770
Cdd:pfam09770 166 KAAAPAPAPQPAAQPARSGSRKMmsleeveaAMRAQAKKPAQQPAPAPPQ-QPQAPP---AQQQQQQQQFPPQQQQQQQP 241
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 73765552   771 RVMPSQSQPPvmPSQSHP--QLT-PSQSQPPVTPSQRQPQLMPSQSQPPVTP 819
Cdd:pfam09770 242 QQQPQQPQQH--PGQGHPvtILQrPQSKQPDPPQPSPQPQAQPFHQQPPPVP 291
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
739-819 1.88e-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: 1.88e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552    739 SQSQPPVTPSQSHPQVMPSQSQPPVTPSQSQprvMPSQSQPPVMPSQSHPQLTPSQSQPPVTPSQRQPQ--LMPSQSQPP 816
Cdd:smart00818  43 SQQHPPTHTLQPHHHIPVLPAQQPVVPQQPL---MPVPGQHSMTPTQHHQPNLPQPAQQPFQPQPLQPPqpQQPMQPQPP 119

                   ...
gi 73765552    817 VTP 819
Cdd:smart00818 120 VHP 122
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
707-816 2.26e-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 characteristic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 335243 [Multi-domain]  Cd Length: 980  Bit Score: 60.80  E-value: 2.26e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552   707 QQDVQTPSAKEEEkiqrrPHELPPQSQPwvmPSQSQPPVTP-------SQSHPQVMPSqSQPPVTPSQSQPRVMPSQSQP 779
Cdd:pfam03154 193 ATPAPTPSAPSLP-----SQVSPPTTQP---PLQPLPVASPhtliqqtPTLHPQRLPS-PHPPLQPMPDPPSQVSPQSAP 263
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552   780 PV-----MPSQSHPQLTPS------------QSQPPVTPS------QRQPQLMPSQSQPP 816
Cdd:pfam03154 264 QPglhgpMPPMPHSLQGPShlphpgppqpfgQGQVPPPPSlqaphpSQLQHTPPSQSQGP 323
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
731-819 2.90e-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 characteristic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 335243 [Multi-domain]  Cd Length: 980  Bit Score: 60.80  E-value: 2.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552   731 QSQPWVMPSQS---QPPVTPSQSHPQVMPSQSQPPVTPSQSQPRVM-PSQSQPPVMPS---QSHPQLTPSQSQPPVTPSQ 803
Cdd:pfam03154 169 QTQPPVLQCQNgvpSPPPGPQTQVATPAPTPSAPSLPSQVSPPTTQpPLQPLPVASPHtliQQTPTLHPQRLPSPHPPLQ 248
                          90
                  ....*....|....*....
gi 73765552   804 RQ---PQLMPSQSQPPVTP 819
Cdd:pfam03154 249 PMpdpPSQVSPQSAPQPGL 267
Glutenin_hmw pfam03157
High molecular weight glutenin subunit; Members of this family include high molecular weight ...
700-816 6.66e-09

High molecular weight glutenin subunit; Members of this family include high molecular weight subunits of glutenin. This group of gluten proteins is thought to be largely responsible for the elastic properties of gluten, and hence, doughs. Indeed, glutenin high molecular weight subunits are classified as elastomeric proteins, because the glutenin network can withstand significant deformations without breaking, and return to the original conformation when the stress is removed. Elastomeric proteins differ considerably in amino acid sequence, but they are all polymers whose subunits consist of elastomeric domains, composed of repeated motifs, and non-elastic domains that mediate cross-linking between the subunits. The elastomeric domain motifs are all rich in glycine residues in addition to other hydrophobic residues. High molecular weight glutenin subunits have an extensive central elastomeric domain, flanked by two terminal non-elastic domains that form disulphide cross-links. The central elastomeric domain is characterized by the following three repeated motifs: PGQGQQ, GYYPTS[P/L]QQ, GQQ. It possesses overlapping beta-turns within and between the repeated motifs, and assumes a regular helical secondary structure with a diameter of approx. 1.9 nm and a pitch of approx. 1.5 nm.


Pssm-ID: 281191 [Multi-domain]  Cd Length: 772  Bit Score: 59.39  E-value: 6.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552   700 KSKPIKKQQDVQTPSAKEEEKIQRRPHELPPQsQP--WVMPSQSQP---PVTPSQSHPQVMPSQSQppvTPSQSQPRVMP 774
Cdd:pfam03157  61 QASPQRPGQGQQPGQGQQSGQGQQGYYPTSPQ-QPgqWQQPEQGQPgyyPTSPQQPGQLQQPAQGQ---QPGQGQQGRQP 136
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 73765552   775 SQSQPPVMPSQSHPQ----LTPSQSQPPVTPSQRQPQLMPSQSQPP 816
Cdd:pfam03157 137 GQGQPGYYPTSSQLQpgqlQQPAQGQQGQQPGQGQQGQQPGQGQQP 182
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
707-817 1.07e-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 characteristic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 335243 [Multi-domain]  Cd Length: 980  Bit Score: 58.88  E-value: 1.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552   707 QQDVQTPSAKEEEKIQRRPHELPPQSQ-PWVMPSQSQPPVTPSQSHPQVMPsqsqPPVTPSQSQPRV------------- 772
Cdd:pfam03154 295 QGQVPPPPSLQAPHPSQLQHTPPSQSQgPSPQPPREQPLPPAPLSMPHIKP----PPTTPIPQLPNPqshkhpphlsaps 370
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 73765552   773 ----MPSQSQPP--VMPSQSHPQLTPSQSQPPvtPSQRQPQ---LMPSQSQPPV 817
Cdd:pfam03154 371 pfpqMPSNLPPPpaLKPLSSLPTHHPPSAHPP--PLQLMPQsqqLPSPPAQPPV 422
Med25_SD1 pfam11235
Mediator complex subunit 25 synapsin 1; The overall function of the full-length Med25 is ...
703-820 1.27e-08

Mediator complex subunit 25 synapsin 1; The overall function of the full-length Med25 is efficiently to coordinate the transcriptional activation of RAR/RXR (retinoic acid receptor/retinoic X receptor) in higher eukaryotic cells. Human Med25 consists of several domains with different binding properties, the N-terminal, VWA, domain, this SD1 - synapsin 1 - domain from residues 229-381, a PTOV(B) or ACID domain from 395-545, an SD2 domain from residues 564-645 and a C-terminal NR box-containing domain (646-650) from 646-747. This The function of the SD domains is unclear.


Pssm-ID: 314226 [Multi-domain]  Cd Length: 166  Bit Score: 54.74  E-value: 1.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552   703 PIKKQQDV-QTPSAKEEEKIQRRP-HELPPQSQPWVMPSQSQppVTPSQSHPQ--VMPSQSQ--------PPVTPSQSQ- 769
Cdd:pfam11235  11 PLQPKQPVpQPPLPPVPAQLSAAPqQTLPPVPQPYQVAAPGT--LTAAQAAAQsaVEAAKNQkaglgprfSPINPLQQMa 88
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 73765552   770 PRVMP--SQSQPPVMPSQSHP---QLTPSQSQPP----VTPSQ---RQPQLMPSQSQP-PVTPS 820
Cdd:pfam11235  89 PGVGPpfNQAPPPALPQGSVPgmpKPLPPASQPSlvstVTTGSgllVQPPVQPTAQPGaPSMPG 152
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
730-819 1.81e-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: 1.81e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552    730 PQSQPwvMPSQSQPPVTPSQsHPQVmPSQS------QPPVTPSQSQPRVMPSQSQPPVMPsqshPQLTPSQSQPPVTPSQ 803
Cdd:smart00818  47 PPTHT--LQPHHHIPVLPAQ-QPVV-PQQPlmpvpgQHSMTPTQHHQPNLPQPAQQPFQP----QPLQPPQPQQPMQPQP 118
                           90
                   ....*....|....*.
gi 73765552    804 RQPQLMPSQSQPPVTP 819
Cdd:smart00818 119 PVHPIPPLPPQPPLPP 134
PHA03247 PHA03247
large tegument protein UL36; Provisional
721-815 2.73e-08

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 57.64  E-value: 2.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552   721 IQRRPHELPPQSQPWVMP-----SQSQPPVTPS-QSHPQVMPSQSQPPVTPSQSQPRvmpSQSQPPVMPSQSHPQLTPSQ 794
Cdd:PHA03247 2862 VRRRPPSRSPAAKPAAPArppvrRLARPAVSRStESFALPPDQPERPPQPQAPPPPQ---PQPQPPPPPQPQPPPPPPPR 2938
                          90       100
                  ....*....|....*....|..
gi 73765552   795 SQPPVTP-SQRQPQLMPSQSQP 815
Cdd:PHA03247 2939 PQPPLAPtTDPAGAGEPSGAVP 2960
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
706-820 3.21e-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 characteristic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 335243 [Multi-domain]  Cd Length: 980  Bit Score: 57.34  E-value: 3.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552   706 KQQDVQT-PSAKEEEKIQRRPHELPPQSQPWVMPSQSQPPVTPSQSHPQVM-PSQSQPPVTPS---QSQPRVMPSQSQPP 780
Cdd:pfam03154 164 QQQILQTqPPVLQCQNGVPSPPPGPQTQVATPAPTPSAPSLPSQVSPPTTQpPLQPLPVASPHtliQQTPTLHPQRLPSP 243
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 73765552   781 VMPSQSHP----QLTPSQSQPPVTPSQRQPQLMPSQSqPPVTPS 820
Cdd:pfam03154 244 HPPLQPMPdppsQVSPQSAPQPGLHGPMPPMPHSLQG-PSHLPH 286
PHA03247 PHA03247
large tegument protein UL36; Provisional
738-820 3.43e-08

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 57.26  E-value: 3.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552   738 PSQSQPPVTPSQSHPQVMpSQSQPPVTPS-QSQPRVMPSQSQPPVMPSQSHPQLTPsqsQPPVTPSQRQPQLMPSQSQPP 816
Cdd:PHA03247 2867 PSRSPAAKPAAPARPPVR-RLARPAVSRStESFALPPDQPERPPQPQAPPPPQPQP---QPPPPPQPQPPPPPPPRPQPP 2942

                  ....
gi 73765552   817 VTPS 820
Cdd:PHA03247 2943 LAPT 2946
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
729-820 3.55e-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 characteristic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 335243 [Multi-domain]  Cd Length: 980  Bit Score: 56.95  E-value: 3.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552   729 PPQSQPWVmPSQSQPPVT--PSQSHPQVMPS---QSQPPVTPSQSQPRVMPSQSQPPvMPSQSHPQLTPS---QSQPPVT 800
Cdd:pfam03154 197 PTPSAPSL-PSQVSPPTTqpPLQPLPVASPHtliQQTPTLHPQRLPSPHPPLQPMPD-PPSQVSPQSAPQpglHGPMPPM 274
                          90       100
                  ....*....|....*....|....*....
gi 73765552   801 PSQRQ-PQLMP--------SQSQPPVTPS 820
Cdd:pfam03154 275 PHSLQgPSHLPhpgppqpfGQGQVPPPPS 303
ZnMc cd00203
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ...
282-372 9.69e-08

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: 9.69e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552 282 QHDTSHLFTTLGLRGLSGIGAFRG-MCTPHRSCAIVTFMNKTLGTFSIAVAHHLGHNLGMNHDED-TCRCSQP------- 352
Cdd:cd00203  51 KADIAILVTRQDFDGGTGGWAYLGrVCDSLRGVGVLQDNQSGTKEGAQTIAHELGHALGFYHDHDrKDRDDYPtiddtln 130
                        90       100       110
                ....*....|....*....|....*....|.
gi 73765552 353 ------RCIMHEGNPP-----ITKFSNCSYG 372
Cdd:cd00203 131 aedddyYSVMSYTKGSfsdgqRKDFSQCDID 161
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
699-820 1.11e-07

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


Pssm-ID: 313063 [Multi-domain]  Cd Length: 837  Bit Score: 55.40  E-value: 1.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552   699 KKSKPIKKQQDVQTPS---AKEEEKIQRRPHELPPQSQPWVMPSQSQPPvtPSQSHP----QVMPSQSQPPVTPSQSQPR 771
Cdd:pfam09770 203 KKPAQQPAPAPPQQPQappAQQQQQQQQFPPQQQQQQQPQQQPQQPQQH--PGQGHPvtilQRPQSKQPDPPQPSPQPQA 280
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 73765552   772 VMPSQSQPPVMPSqshpqltPSQ--SQPPVTPSQRQPQLMPSQSQPPVTPS 820
Cdd:pfam09770 281 QPFHQQPPPVPVQ-------PTQilQNPNRLSAARVGYPQNPQPGVQPVPA 324
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
725-819 1.17e-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 characteristic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 335243 [Multi-domain]  Cd Length: 980  Bit Score: 55.41  E-value: 1.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552   725 PHELPPQsqPWVMPSQSQPPVTPSQSHP---QVMPsQSQPpVTPSQSQPRVMP-SQSQPPvmPSQSHPQLTPSQSQPPVT 800
Cdd:pfam03154 376 PSNLPPP--PALKPLSSLPTHHPPSAHPpplQLMP-QSQQ-LPSPPAQPPVLTqSQSHPP--KASPHPPTAASHSLPSQS 449
                          90
                  ....*....|....*....
gi 73765552   801 PSQRQPqLMPSQSqPPVTP 819
Cdd:pfam03154 450 PFPQHS-FSPSGS-PPVTP 466
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
725-816 1.51e-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 characteristic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 335243 [Multi-domain]  Cd Length: 980  Bit Score: 55.03  E-value: 1.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552   725 PHELPPQSqpwvmPSQSQPPVTPSQSHPQVMPSQSQPPVTPSQSQPrvMPSQSQPPVMPSQSHPQLTPsqsqPPVTPSqr 804
Cdd:pfam03154 285 PHPGPPQP-----FGQGQVPPPPSLQAPHPSQLQHTPPSQSQGPSP--QPPREQPLPPAPLSMPHIKP----PPTTPI-- 351
                          90
                  ....*....|....
gi 73765552   805 qPQLMPSQS--QPP 816
Cdd:pfam03154 352 -PQLPNPQShkHPP 364
PRK10263 PRK10263
DNA translocase FtsK; Provisional
712-820 2.50e-07

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 54.32  E-value: 2.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552   712 TPSAKEEEKIQRRPHELPPQSQPwvmpsqsQPPVTPSQSHPQvmPSQSQPPvtPSQSQPRVMPSQSQPPVMPSQsHPQLT 791
Cdd:PRK10263  746 TPIVEPVQQPQQPVAPQQQYQQP-------QQPVAPQPQYQQ--PQQPVAP--QPQYQQPQQPVAPQPQYQQPQ-QPVAP 813
                          90       100
                  ....*....|....*....|....*....
gi 73765552   792 PSQSQPPVTPSQRQPQLmpSQSQPPVTPS 820
Cdd:PRK10263  814 QPQYQQPQQPVAPQPQY--QQPQQPVAPQ 840
PRK10263 PRK10263
DNA translocase FtsK; Provisional
706-819 2.80e-07

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 54.32  E-value: 2.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552   706 KQQDVQTPSAKEEEKIQRRPheLPPQSQPwvmpSQSQPPVTPSQSHPQVMPSQSQPPVTPSQSQPRVMPSQSQPPVMPSQ 785
Cdd:PRK10263  752 VQQPQQPVAPQQQYQQPQQP--VAPQPQY----QQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVA 825
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 73765552   786 SHPQLtpSQSQPPVTPSQRQ----PQLMPS-QSQP---PVTP 819
Cdd:PRK10263  826 PQPQY--QQPQQPVAPQPQDtllhPLLMRNgDSRPlhkPTTP 865
Glutenin_hmw pfam03157
High molecular weight glutenin subunit; Members of this family include high molecular weight ...
702-814 2.91e-07

High molecular weight glutenin subunit; Members of this family include high molecular weight subunits of glutenin. This group of gluten proteins is thought to be largely responsible for the elastic properties of gluten, and hence, doughs. Indeed, glutenin high molecular weight subunits are classified as elastomeric proteins, because the glutenin network can withstand significant deformations without breaking, and return to the original conformation when the stress is removed. Elastomeric proteins differ considerably in amino acid sequence, but they are all polymers whose subunits consist of elastomeric domains, composed of repeated motifs, and non-elastic domains that mediate cross-linking between the subunits. The elastomeric domain motifs are all rich in glycine residues in addition to other hydrophobic residues. High molecular weight glutenin subunits have an extensive central elastomeric domain, flanked by two terminal non-elastic domains that form disulphide cross-links. The central elastomeric domain is characterized by the following three repeated motifs: PGQGQQ, GYYPTS[P/L]QQ, GQQ. It possesses overlapping beta-turns within and between the repeated motifs, and assumes a regular helical secondary structure with a diameter of approx. 1.9 nm and a pitch of approx. 1.5 nm.


Pssm-ID: 281191 [Multi-domain]  Cd Length: 772  Bit Score: 53.99  E-value: 2.91e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552   702 KPIKKQQDVQTPSAKE----EEKIQRRPHELPPQSQPWVMPSQSQP---PVTPSQSHPQVMPSQSQppvTPSQSQPRVMP 774
Cdd:pfam03157 388 QPGQLQQSAQGQKGQQpgqgQQPGQGQQGQQPGQGQQGQQPGQGQPgyyPTSPQQSGQGQQPGQWQ---QPGQGQPGYYP 464
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 73765552   775 SQsqpPVMPSQSHPQLTPSQSQPPVTPSQRQPQLMPSQSQ 814
Cdd:pfam03157 465 TS---PLQPGQGQPGYDPTSPQQPGQGQQPGQLQQPAQGQ 501
GGN pfam15685
Gametogenetin; GGN is a family of proteins largely found in mammals. It reacts with POG in the ...
729-819 3.76e-07

Gametogenetin; GGN is a family of proteins largely found in mammals. It reacts with POG in the maturation of sperm and is expressed virtually only in the testis. It is found to be associated with the intracellular membrane, binds with GGNBP1 and may be involved in vesicular trafficking.


Pssm-ID: 317988 [Multi-domain]  Cd Length: 648  Bit Score: 53.51  E-value: 3.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552   729 PPQSQPWVMPSQSQPPVTPSQSHPQVMPSQSQPPVTPSQSQPRVMPSQSQPPVMPsqshPQLTPSQSQPPVTPSQRQPQL 808
Cdd:pfam15685 432 PPGQQELPPMPPPVPPPTPQPPALQPTPLPVAPPPTPGPGHAESALAPPPAPALP----PALAADQTPAPAPAPSPAPAP 507
                          90
                  ....*....|.
gi 73765552   809 MPSQSQPPVTP 819
Cdd:pfam15685 508 TTAEPLPPAPA 518
PRK12757 PRK12757
cell division protein FtsN; Provisional
721-806 4.60e-07

cell division protein FtsN; Provisional


Pssm-ID: 237191 [Multi-domain]  Cd Length: 256  Bit Score: 51.58  E-value: 4.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552  721 IQRRPHELPPqsqpwvMPSQSQPPVTP-SQSHPQVMPSQSQPPVTPSQSQPRVMPSQSQPPVMPSQSHPqlTPSQSQPPV 799
Cdd:PRK12757  95 MRQQPTQLSE------VPYNEQTPQVPrSTVQIQQQAQQQQPPATTAQPQPVTPPRQTTAPVQPQTPAP--VRTQPAAPV 166

                 ....*..
gi 73765552  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 6.99e-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: 6.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552   713 PSAKEEEKIQRRPHELPPQSQPWVmPSqsqpPVTPSQSHPQVMPSQSQP-PVTPSQSQPRVMPSQSQPPVMPSQS--HPQ 789
Cdd:pfam09606 378 PVPGQQVRQVTPNQFMRQSPQPSV-PS----PQGPGSQPPQSHPGGMIPsPALIPSPSPQMSQQPAQQRTIGQDSpgGSL 452
                          90
                  ....*....|....*...
gi 73765552   790 LTPSQSQ--PPVTPSQRQ 805
Cdd:pfam09606 453 NTPGQSAvnSPLNPQEEQ 470
Pro-rich pfam15240
Proline-rich; This family includes several eukaryotic proline-rich proteins.
726-819 7.46e-07

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


Pssm-ID: 291893 [Multi-domain]  Cd Length: 160  Bit Score: 49.60  E-value: 7.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552   726 HELPPQSQPWVMPSQSQPPVTPSQSHPQVMPSQSQPPVTPSQSQPRVMPSQSQPPVMPSQSH-------PQLTPSQSQPP 798
Cdd:pfam15240  45 PQGPPPGGFPPQPPGPPPQGGPQQPPPQGGNPQGPPPQGGPQRPPGPGNQQGPPPQGGNQQQrppppgkPQGPPPQGGGP 124
                          90       100
                  ....*....|....*....|....*.
gi 73765552   799 VTPSQRQPQLMPS-----QSQPPVTP 819
Cdd:pfam15240 125 PPPQGGNQQGPPPpppgnPQGPPRPP 150
Retinal pfam15449
Retinal protein; This family of proteins is found in the photoreceptor cells of the retina. ...
700-820 8.12e-07

Retinal protein; This family of proteins is found in the photoreceptor cells of the retina. Mutations of the gene encoding this protein have been associated with retinal disorders such as retinitis pigmentosa and late-onset progressive retinal atrophy. The function of this family of proteins is unknown, but it is likely to be important in the development and function of the retina.


Pssm-ID: 317802 [Multi-domain]  Cd Length: 1292  Bit Score: 52.88  E-value: 8.12e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552    700 KSKP-IKKQQDVQTPSAKEEEKIQRRP--HELPPQSQPWVMPSQSQPPVTPSQShPQVMPSQSQPPVTPSQSQPRVMPSQ 776
Cdd:pfam15449 1010 RSPPlVRKASPTRAHWAPRADRRHPSLpsSHRPAQPSLPTVQRSPSPPLSPAPS-PPASPRVLSPPTSKKRTSPPPQHKL 1088
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 73765552    777 SQPPVmpsqSHPQLTPSQSQPPVTPSQRQPQLMPSQSQPPVTPS 820
Cdd:pfam15449 1089 PSPPP----ESPQAQHKLSSPPTQRTEASSPSSGPSPSPPTSPS 1128
PHA03247 PHA03247
large tegument protein UL36; Provisional
707-820 9.69e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 52.63  E-value: 9.69e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552   707 QQDVQTPSAKEEEKIQR--RPhELPPQSQPWVMP--SQSQPPVTPSQSHPQvmpSQSQPPVTPSQSQPRVMPSQSQPPVM 782
Cdd:PHA03247 2869 RSPAAKPAAPARPPVRRlaRP-AVSRSTESFALPpdQPERPPQPQAPPPPQ---PQPQPPPPPQPQPPPPPPPRPQPPLA 2944
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 73765552   783 P-SQSHPQLTPSQSQPP-----------VTPSQRQPQLMPSQSQP-PVTPS 820
Cdd:PHA03247 2945 PtTDPAGAGEPSGAVPQpwlgalvpgrvAVPRFRVPQPAPSREAPaSSTPP 2995
PRK03427 PRK03427
cell division protein ZipA; Provisional
718-820 1.01e-06

cell division protein ZipA; Provisional


Pssm-ID: 235124 [Multi-domain]  Cd Length: 333  Bit Score: 51.19  E-value: 1.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552  718 EEKIQR-RPHELPPQSQPWVMPS---QSQPPVTPSQSHPQVMPSQSQPPVTPSQSQP--RVMPSQSQPPVMPSQSHPQLT 791
Cdd:PRK03427  65 EVRVHRvNHAPANAQEHEAARPSpqhQYQPPYASAQPRQPVQQPPEAQVPPQHAPRPaqPAPQPVQQPAYQPQPEQPLQQ 144
                         90       100       110
                 ....*....|....*....|....*....|..
gi 73765552  792 P---SQsQPPVTPSQRQPQLmPSQSQPPVTPS 820
Cdd:PRK03427 145 PvspQV-APAPQPVHSAPQP-AQQAFQPAEPV 174
Pro-rich pfam15240
Proline-rich; This family includes several eukaryotic proline-rich proteins.
702-810 1.20e-06

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


Pssm-ID: 291893 [Multi-domain]  Cd Length: 160  Bit Score: 48.83  E-value: 1.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552   702 KPIKKQQDVQTPSAKEEEKIQRRPHELPPQSQPWVMPSQSQPPVTPSQSHP--QVMPSQSQPPVTPSQSQPrvmPSQSQP 779
Cdd:pfam15240  47 GPPPGGFPPQPPGPPPQGGPQQPPPQGGNPQGPPPQGGPQRPPGPGNQQGPppQGGNQQQRPPPPGKPQGP---PPQGGG 123
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 73765552   780 PVMPSQSHPQLTPS-----QSQPPVTPSQRQPQLMP 810
Cdd:pfam15240 124 PPPPQGGNQQGPPPpppgnPQGPPRPPQPGNPQGPP 159
PHA03378 PHA03378
EBNA-3B; Provisional
723-819 1.34e-06

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 51.99  E-value: 1.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552  723 RRPHELPPqsqPWVMPSQSQPP--VTPSQSHPQVMPSQSQPP------VTPSQSQP-RVMPSQSQPPVMPSQSHPQLTPS 793
Cdd:PHA03378 699 RAPTPMRP---PAAPPGRAQRPaaATGRARPPAAAPGRARPPaaapgrARPPAAAPgRARPPAAAPGRARPPAAAPGAPT 775
                         90       100
                 ....*....|....*....|....*...
gi 73765552  794 QSQPPVTP--SQRQPQLMPSQSQPPVTP 819
Cdd:PHA03378 776 PQPPPQAPpaPQQRPRGAPTPQPPPQAG 803
PRK03427 PRK03427
cell division protein ZipA; Provisional
713-819 1.48e-06

cell division protein ZipA; Provisional


Pssm-ID: 235124 [Multi-domain]  Cd Length: 333  Bit Score: 50.80  E-value: 1.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552  713 PSAKEEEKIQRRPHELPPQSQPWVMPSQSQPPVTPSQSHPQ--VMPSQSQPPVTPSQSQPRVMPSQ--SQPPVMPSQSHP 788
Cdd:PRK03427  82 EAARPSPQHQYQPPYASAQPRQPVQQPPEAQVPPQHAPRPAqpAPQPVQQPAYQPQPEQPLQQPVSpqVAPAPQPVHSAP 161
                         90       100       110
                 ....*....|....*....|....*....|.
gi 73765552  789 QLTPSQSQPPvtPSQRQPQLMPSQSQPPVTP 819
Cdd:PRK03427 162 QPAQQAFQPA--EPVAAPQPEPVAEPAPVMD 190
Caprin-1_C pfam12287
Cytoplasmic activation/proliferation-associated protein-1 C term; This family of proteins is ...
707-820 1.59e-06

Cytoplasmic activation/proliferation-associated protein-1 C term; This family of proteins is found in eukaryotes. Proteins in this family are typically between 343 and 708 amino acids in length. This family is the C terminal region of caprin-1. Caprin-1 is a protein involved in regulating cellular proliferation. In mutated phenotypes, the G1 phase of the cell cycle is greatly lengthened, impairing normal proliferation. The C terminal region of caprin-1 contains RGG motifs which are characteristic of RNA binding domains. It is possible that caprin-1 functions through an RNA binding mechanism.


Pssm-ID: 315051 [Multi-domain]  Cd Length: 327  Bit Score: 50.61  E-value: 1.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552   707 QQDVQTPSAKEEEKIQRrpheLPPQSQPWVMPSQSQ-PPVTPSQSHPQVM-----PSQSQPPVTpsqSQPRVMPSQSQP- 779
Cdd:pfam12287  34 QPPSQSPGSPVVSTEQR----LSQQSDFLQQPEQAQvSPVTCSSNACLVTdqassGSETEPFHT---SETRPQPEAIDPi 106
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 73765552   780 PVMPSQSHPQLTPSQSQPPVTpsqrQPQLMPSqsqPPVTPS 820
Cdd:pfam12287 107 PSSMSLPSELASPSPPLSPAS----QPQVFQS---PPASSS 140
Glutenin_hmw pfam03157
High molecular weight glutenin subunit; Members of this family include high molecular weight ...
713-820 2.20e-06

High molecular weight glutenin subunit; Members of this family include high molecular weight subunits of glutenin. This group of gluten proteins is thought to be largely responsible for the elastic properties of gluten, and hence, doughs. Indeed, glutenin high molecular weight subunits are classified as elastomeric proteins, because the glutenin network can withstand significant deformations without breaking, and return to the original conformation when the stress is removed. Elastomeric proteins differ considerably in amino acid sequence, but they are all polymers whose subunits consist of elastomeric domains, composed of repeated motifs, and non-elastic domains that mediate cross-linking between the subunits. The elastomeric domain motifs are all rich in glycine residues in addition to other hydrophobic residues. High molecular weight glutenin subunits have an extensive central elastomeric domain, flanked by two terminal non-elastic domains that form disulphide cross-links. The central elastomeric domain is characterized by the following three repeated motifs: PGQGQQ, GYYPTS[P/L]QQ, GQQ. It possesses overlapping beta-turns within and between the repeated motifs, and assumes a regular helical secondary structure with a diameter of approx. 1.9 nm and a pitch of approx. 1.5 nm.


Pssm-ID: 281191 [Multi-domain]  Cd Length: 772  Bit Score: 51.30  E-value: 2.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552   713 PSAKEEEKIQRRPHEL--------PPQSQPWVMPSQSQPPVTPSQSHpqvMPSQSQP---PVTPSQS---QPRVMPSQSQ 778
Cdd:pfam03157 245 PTSPQQPGQGQQPGQLqqpaqgqqPEQGQQGQQPGQGQQGQQPGQGQ---QPGQGQPgyyPTSPQQSgqgQPGYYPTSSQ 321
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 73765552   779 PPV---MPSQSHPQLTPSQSQPPVTPSQRQpqlMPSQSQPPVTPS 820
Cdd:pfam03157 322 QPTqsqQPGQGQQGQQVGQGQQAQQPGQGQ---QPGQGQPGYYPT 363
PRK12757 PRK12757
cell division protein FtsN; Provisional
742-816 2.46e-06

cell division protein FtsN; Provisional


Pssm-ID: 237191 [Multi-domain]  Cd Length: 256  Bit Score: 49.66  E-value: 2.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552  742 QPPVTPSQshpqvMPSQSQPPVTP-SQSQPRVMPSQSQPPVMPSQSHPQLTPSQSQPPVTPSQRQP----QLMPSQSQPP 816
Cdd:PRK12757  97 QQPTQLSE-----VPYNEQTPQVPrSTVQIQQQAQQQQPPATTAQPQPVTPPRQTTAPVQPQTPAPvrtqPAAPVTQAVE 171
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
731-819 2.91e-06

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: 50.78  E-value: 2.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552   731 QSQPWVMPSqsqPPVTPSQSHPQVMPSQSQPPvTPSQSQPRVMPSQSQPPVMPSqshPQLTPS-----QSQPPVTPSQRQ 805
Cdd:pfam09606 367 RGQPGMMSS---PSPVPGQQVRQVTPNQFMRQ-SPQPSVPSPQGPGSQPPQSHP---GGMIPSpalipSPSPQMSQQPAQ 439
                          90
                  ....*....|....*.
gi 73765552   806 PQLMPSQS--QPPVTP 819
Cdd:pfam09606 440 QRTIGQDSpgGSLNTP 455
PHA03247 PHA03247
large tegument protein UL36; Provisional
729-816 3.01e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.09  E-value: 3.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552   729 PPQSQPWVMPSQSQPP---------VTPSQSHPQVMPSQSQPPVTPSQSQPRVMpSQSQPPVMPS-QSHPQLTPSQSQPP 798
Cdd:PHA03247 2831 PTSAQPTAPPPPPGPPppslplggsVAPGGDVRRRPPSRSPAAKPAAPARPPVR-RLARPAVSRStESFALPPDQPERPP 2909
                          90
                  ....*....|....*...
gi 73765552   799 VTPSQRQPQLMPSQSQPP 816
Cdd:PHA03247 2910 QPQAPPPPQPQPQPPPPP 2927
PRK10263 PRK10263
DNA translocase FtsK; Provisional
701-819 3.63e-06

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 50.47  E-value: 3.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552   701 SKPIKKQQDV---QTPS---AKEEEKIQRRPHELPPQ---SQPWVMPSQSQPPVTPSQSHPQVMPSQSQPPVTPSQSQPR 771
Cdd:PRK10263  354 AQPTVAWQPVpgpQTGEpviAPAPEGYPQQSQYAQPAvqyNEPLQQPVQPQQPYYAPAAEQPAQQPYYAPAPEQPAQQPY 433
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 73765552   772 VMPSQSQPPV-MPSQSHPQLTPSQSQPPVTPSQRQPQLM---PSQSQPPVTP 819
Cdd:PRK10263  434 YAPAPEQPVAgNAWQAEEQQSTFAPQSTYQTEQTYQQPAaqePLYQQPQPVE 485
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
701-819 3.79e-06

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 50.46  E-value: 3.79e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552  701 SKPIKKQQDVQTPSAKEEEKIQRRPHElPPQSQPWVMPSQSQPPVTPSQS-HPQ--VMPSQSQPPVTPSQSQPRVMPSQS 777
Cdd:PTZ00449 537 SKESDEPKEGGKPGETKEGEVGKKPGP-AKEHKPSKIPTLSKKPEFPKDPkHPKdpEEPKKPKRPRSAQRPTRPKSPKLP 615
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 73765552  778 QPPVMPSQSHPQLTPSQSQPPVTP----SQRQPQ--LMPSQSQPPVTP 819
Cdd:PTZ00449 616 ELLDIPKSPKRPESPKSPKRPPPPqrpsSPERPEgpKIIKSPKPPKSP 663
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
707-820 4.08e-06

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


Pssm-ID: 313063 [Multi-domain]  Cd Length: 837  Bit Score: 50.39  E-value: 4.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552   707 QQDVQTPSAKEEEKIQRRPHELPPQSQPWVMPSQSQ----PPVTPSQSHPQVMPSQSQPPVTPSQSQPRVM---PSQSQP 779
Cdd:pfam09770 227 QQQQFPPQQQQQQQPQQQPQQPQQHPGQGHPVTILQrpqsKQPDPPQPSPQPQAQPFHQQPPPVPVQPTQIlqnPNRLSA 306
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 73765552   780 PVMPSQSHPQltPSQSQPPVTPSQRQPQLMPSQSQPPVTPS 820
Cdd:pfam09770 307 ARVGYPQNPQ--PGVQPVPAHQAHRQQGSFGRQAPIITHPQ 345
Glutenin_hmw pfam03157
High molecular weight glutenin subunit; Members of this family include high molecular weight ...
713-816 4.40e-06

High molecular weight glutenin subunit; Members of this family include high molecular weight subunits of glutenin. This group of gluten proteins is thought to be largely responsible for the elastic properties of gluten, and hence, doughs. Indeed, glutenin high molecular weight subunits are classified as elastomeric proteins, because the glutenin network can withstand significant deformations without breaking, and return to the original conformation when the stress is removed. Elastomeric proteins differ considerably in amino acid sequence, but they are all polymers whose subunits consist of elastomeric domains, composed of repeated motifs, and non-elastic domains that mediate cross-linking between the subunits. The elastomeric domain motifs are all rich in glycine residues in addition to other hydrophobic residues. High molecular weight glutenin subunits have an extensive central elastomeric domain, flanked by two terminal non-elastic domains that form disulphide cross-links. The central elastomeric domain is characterized by the following three repeated motifs: PGQGQQ, GYYPTS[P/L]QQ, GQQ. It possesses overlapping beta-turns within and between the repeated motifs, and assumes a regular helical secondary structure with a diameter of approx. 1.9 nm and a pitch of approx. 1.5 nm.


Pssm-ID: 281191 [Multi-domain]  Cd Length: 772  Bit Score: 50.14  E-value: 4.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552   713 PSAKEEEKIQRRPHELPPQSqpwvmPSQSQPPVTPSQS---HPQVMPSQSQPP---VTPSQSQPRVMPSQSQPPVMPSQS 786
Cdd:pfam03157  47 PSVTSPQQVSYYPGQASPQR-----PGQGQQPGQGQQSgqgQQGYYPTSPQQPgqwQQPEQGQPGYYPTSPQQPGQLQQP 121
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 73765552   787 HPQLTPSQSQPPVTPSQRQP-------QLMPSQSQPP 816
Cdd:pfam03157 122 AQGQQPGQGQQGRQPGQGQPgyyptssQLQPGQLQQP 158
PHA03377 PHA03377
EBNA-3C; Provisional
709-817 4.59e-06

EBNA-3C; Provisional


Pssm-ID: 177614 [Multi-domain]  Cd Length: 1000  Bit Score: 50.05  E-value: 4.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552   709 DVQTPSAKEEEKIQRRPHELPP-------QSQPWVMPsqsqPPVTPSQSHPqvmPSQSQPPVTPSQSQPRVM-PSQSQPP 780
Cdd:PHA03377  516 DVETTEEEESVTQPAKPHRKVQdgfqrsgRRQKRATP----PKVSPSDRGP---PKASPPVMAPPSTGPRVMaTPSTGPR 588
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 73765552   781 VM--PSQSHPQLTPSQSQPPV-TPSQRQPQ-LMPSQSQPPV 817
Cdd:PHA03377  589 DMapPSTGPRQQAKCKDGPPAsGPHEKQPPsSAPRDMAPSV 629
PHA03378 PHA03378
EBNA-3B; Provisional
723-816 4.65e-06

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 50.07  E-value: 4.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552  723 RRPHElPPQSQP-WVMPSQSQPPVTPSQSHP---------QVMPSQSQPPV---TPSqSQPRVMPSQSQPPVMPS--QSH 787
Cdd:PHA03378 649 PTPHQ-PPQVEItPYKPTWTQIGHIPYQPSPtgantmlpiQWAPGTMQPPPrapTPM-RPPAAPPGRAQRPAAATgrARP 726
                         90       100       110
                 ....*....|....*....|....*....|.
gi 73765552  788 PQLTPSQSQPPVTP--SQRQPQLMPSQSQPP 816
Cdd:PHA03378 727 PAAAPGRARPPAAApgRARPPAAAPGRARPP 757
Caprin-1_C pfam12287
Cytoplasmic activation/proliferation-associated protein-1 C term; This family of proteins is ...
731-820 4.81e-06

Cytoplasmic activation/proliferation-associated protein-1 C term; This family of proteins is found in eukaryotes. Proteins in this family are typically between 343 and 708 amino acids in length. This family is the C terminal region of caprin-1. Caprin-1 is a protein involved in regulating cellular proliferation. In mutated phenotypes, the G1 phase of the cell cycle is greatly lengthened, impairing normal proliferation. The C terminal region of caprin-1 contains RGG motifs which are characteristic of RNA binding domains. It is possible that caprin-1 functions through an RNA binding mechanism.


Pssm-ID: 315051 [Multi-domain]  Cd Length: 327  Bit Score: 49.07  E-value: 4.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552   731 QSQPWVMPSQ--SQPPVTPSQSHPQVMPSQSQPPVTPSQSQPRVMPSQSQPPVMPSQShpqLTPSQSQPPVTPSQR---- 804
Cdd:pfam12287  25 PSLSAIVSSQppSQSPGSPVVSTEQRLSQQSDFLQQPEQAQVSPVTCSSNACLVTDQA---SSGSETEPFHTSETRpqpe 101
                          90       100
                  ....*....|....*....|.
gi 73765552   805 -----QPQLMPSQSQPPVTPS 820
Cdd:pfam12287 102 aidpiPSSMSLPSELASPSPP 122
Rib_recp_KP_reg pfam05104
Ribosome receptor lysine/proline rich region; This highly conserved region is found towards ...
699-817 5.39e-06

Ribosome receptor lysine/proline rich region; This highly conserved region is found towards the C-terminus of the transmembrane domain. The function is unclear.


Pssm-ID: 309995 [Multi-domain]  Cd Length: 162  Bit Score: 46.92  E-value: 5.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552   699 KKSKP---IKKQQDVQTPSAKEEEKIQRRPhELPPQSQPWVMPSQSQPPVTP--SQSHPQVMPSQSQPPVTPSQSQPRVM 773
Cdd:pfam05104  43 KEDKPngkIPESESTQEPAEASEPYVEVVP-EAPPAPPPPAKPAPVPEPVPPpkKSKPPSVKPAAVAKAPAPVLAQAAPP 121
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 73765552   774 PSQSQPPvmPSQSHPQLTPSQSQPPVTPSQRQPqlMPSQSQPPV 817
Cdd:pfam05104 122 QAKPAPS--PKDKKKPEKKVAKVEPAPTKGKPP--ISSQKAAPL 161
Reprolysin_5 pfam13688
Metallo-peptidase family M12;
198-367 6.11e-06

Metallo-peptidase family M12;


Pssm-ID: 338898  Cd Length: 188  Bit Score: 47.37  E-value: 6.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552   198 RIVEIVVVIDNYLYIRYERNDSKllEDLYVIVNIVDSILDV-IGVKVLLFGLEIWTNKNLIV-----VDDVRKSVHLYCK 271
Cdd:pfam13688   3 RTVALLVAADCSYVAAFGGDAAQ--ANIINMVNTASNVYERnFNISLGLVNLTITDYTDPYTspptsSGNASDRLNRFQS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552   272 WKSENitPRMQHDTSHLFTTLGLRGlSGIGAFRGMCTPHRSCAIVTFMNKTLGTFS--IAVAHHLGHNLGMNHD-----E 344
Cdd:pfam13688  81 FSAWR--GTQNDDLAHLFLDTNCSG-GGLAWLGQLCNSGSAGSVSTSVNVVVGTATewQVFAHEIGHNFGAVHDcdsstT 157
                         170       180       190
                  ....*....|....*....|....*....|..
gi 73765552   345 DTCrCS--------QPRCIMHEGNPP-ITKFS 367
Cdd:pfam13688 158 SQC-CPpssstcpaGGRYIMNYASSPnSTYFS 188
Mucin-like pfam16058
Mucin-like; This domain is found repeated at the C-terminus (C-tail) of bile salt-activated ...
739-820 6.75e-06

Mucin-like; This domain is found repeated at the C-terminus (C-tail) of bile salt-activated lipase, where is is O-glycosylated.


Pssm-ID: 318310 [Multi-domain]  Cd Length: 100  Bit Score: 45.04  E-value: 6.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552   739 SQSQPPVTPSQShpqvmpsQSQPPVTPSqsqprvmPSQSQPPVMPSQS--HPQLTPSQS--QPPVTPSQR--QPQLMPSQ 812
Cdd:pfam16058   5 SITEPPRDPSSS-------YTEPQRAPS-------SSYTEPQRAPSSSytEPPRDPSSSytEPQSDPSGSytAPQRTPSS 70
                          90
                  ....*....|
gi 73765552   813 S--QPPVTPS 820
Cdd:pfam16058  71 SygEPPRDPS 80
PRK03427 PRK03427
cell division protein ZipA; Provisional
731-820 8.19e-06

cell division protein ZipA; Provisional


Pssm-ID: 235124 [Multi-domain]  Cd Length: 333  Bit Score: 48.49  E-value: 8.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552  731 QSQPWVMPSQSQPPVTPSQSHPQVMPSQSQP------PVTPSQSQPRVMPSQsQPPVMPS-QSHPQLTPSQSQPPVTPSQ 803
Cdd:PRK03427  91 QYQPPYASAQPRQPVQQPPEAQVPPQHAPRPaqpapqPVQQPAYQPQPEQPL-QQPVSPQvAPAPQPVHSAPQPAQQAFQ 169
                         90
                 ....*....|....*..
gi 73765552  804 RQPQLMPSQSQPPVTPS 820
Cdd:PRK03427 170 PAEPVAAPQPEPVAEPA 186
Glutenin_hmw pfam03157
High molecular weight glutenin subunit; Members of this family include high molecular weight ...
702-816 8.71e-06

High molecular weight glutenin subunit; Members of this family include high molecular weight subunits of glutenin. This group of gluten proteins is thought to be largely responsible for the elastic properties of gluten, and hence, doughs. Indeed, glutenin high molecular weight subunits are classified as elastomeric proteins, because the glutenin network can withstand significant deformations without breaking, and return to the original conformation when the stress is removed. Elastomeric proteins differ considerably in amino acid sequence, but they are all polymers whose subunits consist of elastomeric domains, composed of repeated motifs, and non-elastic domains that mediate cross-linking between the subunits. The elastomeric domain motifs are all rich in glycine residues in addition to other hydrophobic residues. High molecular weight glutenin subunits have an extensive central elastomeric domain, flanked by two terminal non-elastic domains that form disulphide cross-links. The central elastomeric domain is characterized by the following three repeated motifs: PGQGQQ, GYYPTS[P/L]QQ, GQQ. It possesses overlapping beta-turns within and between the repeated motifs, and assumes a regular helical secondary structure with a diameter of approx. 1.9 nm and a pitch of approx. 1.5 nm.


Pssm-ID: 281191 [Multi-domain]  Cd Length: 772  Bit Score: 49.37  E-value: 8.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552   702 KPIKKQQDvQTPSAKEEEKIQRRPHELPPQSQP--WVMPSQSQP------PVTPSQSHPQVMPSQSQPP---------VT 764
Cdd:pfam03157 418 QPGQGQQG-QQPGQGQPGYYPTSPQQSGQGQQPgqWQQPGQGQPgyyptsPLQPGQGQPGYDPTSPQQPgqgqqpgqlQQ 496
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 73765552   765 PSQSQPRVMPSQSQPPVMPSQSHPQLTPSQSQPPVTPSQRQPQLMPSQSQPP 816
Cdd:pfam03157 497 PAQGQQGQQLAQGQQGQQPAQVQQGQQPAQGQQGQQLGQGQQGQQPGQGQQP 548
PHA03247 PHA03247
large tegument protein UL36; Provisional
728-819 1.02e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.17  E-value: 1.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552   728 LPPQSQPwvmPSQSQPPVTPSQSHPQVMPSQSQPP------VTPSQSQPRVMPSQSQPPVMPSQSHPQLTpSQSQPPVTP 801
Cdd:PHA03247 2818 LPPAASP---AGPLPPPTSAQPTAPPPPPGPPPPSlplggsVAPGGDVRRRPPSRSPAAKPAAPARPPVR-RLARPAVSR 2893
                          90
                  ....*....|....*...
gi 73765552   802 SQRQPQLMPSQSQPPVTP 819
Cdd:PHA03247 2894 STESFALPPDQPERPPQP 2911
PRK12757 PRK12757
cell division protein FtsN; Provisional
705-819 1.08e-05

cell division protein FtsN; Provisional


Pssm-ID: 237191 [Multi-domain]  Cd Length: 256  Bit Score: 47.73  E-value: 1.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552  705 KKQQDVQTPSAKeeekiQRRPHELPPQSQP-W----------VMPSQSQPPVT--PSQSHPQVMPSQSQ----------- 760
Cdd:PRK12757  23 KKEEAPLLPNHK-----PRTGNGLPPKPEErWryikelenrqIGVPTPTEPSAggEVNSPTQLTDEQRQlleqmqadmrq 97
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552  761 PPVTPSQsqprvMPSQSQPPVMP-SQSHPQLTPSQSQPPVTPSQRQPQLMPSQSQPPVTP 819
Cdd:PRK12757  98 QPTQLSE-----VPYNEQTPQVPrSTVQIQQQAQQQQPPATTAQPQPVTPPRQTTAPVQP 152
GGN pfam15685
Gametogenetin; GGN is a family of proteins largely found in mammals. It reacts with POG in the ...
723-820 1.09e-05

Gametogenetin; GGN is a family of proteins largely found in mammals. It reacts with POG in the maturation of sperm and is expressed virtually only in the testis. It is found to be associated with the intracellular membrane, binds with GGNBP1 and may be involved in vesicular trafficking.


Pssm-ID: 317988 [Multi-domain]  Cd Length: 648  Bit Score: 48.89  E-value: 1.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552   723 RRPHE--LPPQSQPWVMPSQSQP--PVTPSQSHPQVMPSQSQPPvTPSQSQPRVMPSQSQPPVMPSQSHPQLTPSQSQPP 798
Cdd:pfam15685 405 RRPAPalLAPPMFIFPAPTNGEPvrPGPPGQQELPPMPPPVPPP-TPQPPALQPTPLPVAPPPTPGPGHAESALAPPPAP 483
                          90       100
                  ....*....|....*....|...
gi 73765552   799 VTPsqrqPQLMPSQSQPPV-TPS 820
Cdd:pfam15685 484 ALP----PALAADQTPAPApAPS 502
PRK03427 PRK03427
cell division protein ZipA; Provisional
703-805 1.31e-05

cell division protein ZipA; Provisional


Pssm-ID: 235124 [Multi-domain]  Cd Length: 333  Bit Score: 47.72  E-value: 1.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552  703 PIKKQQDVQTPSAKEEEKIQRRPHELPPQSQPW-VMPSQSQPPVTPSQSHPQvmPSQSQPPVTPSQSQPrVMPSQSQPPV 781
Cdd:PRK03427  95 PYASAQPRQPVQQPPEAQVPPQHAPRPAQPAPQpVQQPAYQPQPEQPLQQPV--SPQVAPAPQPVHSAP-QPAQQAFQPA 171
                         90       100
                 ....*....|....*....|....
gi 73765552  782 MPSQsHPQLTPSQSQPPVTPSQRQ 805
Cdd:PRK03427 172 EPVA-APQPEPVAEPAPVMDKPKR 194
Amelogenin pfam02948
Amelogenin; Amelogenins play a role in biomineralisation. They seem to regulate the formation ...
728-820 1.55e-05

Amelogenin; Amelogenins play a role in biomineralisation. They seem to regulate the formation of crystallites during the secretory stage of tooth enamel development. thought to play a major role in the structural organisation and mineralisation of developing enamel. They are found in the extracellular matrix. Mutations in X-chromosomal amelogenin can cause Amelogenesis imperfecta.


Pssm-ID: 308545 [Multi-domain]  Cd Length: 173  Bit Score: 45.81  E-value: 1.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552   728 LPPQsQPWVMPSQSQPPVTPSQS----HPQVMPSQSQPPVTPSQSQPRVMPSQSQPPVMPSQSHPqltPSQSQPPVTPSQ 803
Cdd:pfam02948  72 LPAH-HPFLIPQQPVVPVPGQHPvipqFQPAHGGPIHHPFQPQHTEHPLKPTQLSNPVHPMEPFK---PDHPNKPMFPLQ 147
                          90
                  ....*....|....*..
gi 73765552   804 RQPQLMPSQSQPPVTPS 820
Cdd:pfam02948 148 PLPPLFEDRPLEPWPAA 164
PRK14971 PRK14971
DNA polymerase III subunits gamma and tau; Provisional
738-820 1.57e-05

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 48.23  E-value: 1.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552  738 PSQSQP---PVTPSQSHPQVMPSQSQPPVTPSQSQPRVMPSQSQPPVM-----PSQSHPQLTPSQSQPPVTPSQRQPqlM 809
Cdd:PRK14971 381 PVFTQPaaaPQPSAAAAASPSPSQSSAAAQPSAPQSATQPAGTPPTVSvdppaAVPVNPPSTAPQAVRPAQFKEEKK--I 458
                         90
                 ....*....|.
gi 73765552  810 PSQSQPPVTPS 820
Cdd:PRK14971 459 PVSKVSSLGPS 469
Med26_M pfam15694
Mediator complex subunit 26 middle domain; Med26_M is the middle domain of subunit 26 of ...
729-820 1.77e-05

Mediator complex subunit 26 middle domain; Med26_M is the middle domain of subunit 26 of Mediator. Med19 and Med26 act synergistically to mediate the interaction between REST (a Kruppel-type zinc finger transcription factor that binds to a 21-bp RE1 silencing element present in over 900 human genes) and Mediator.


Pssm-ID: 317997 [Multi-domain]  Cd Length: 252  Bit Score: 46.76  E-value: 1.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552   729 PPQSQPWVMPSQSQPPvtPSQSHPQVMPSQSQPPVTPSQSQPRV-MPSQSQPPVMPSQSHPQLTPSQSQPPVTPSQRQPq 807
Cdd:pfam15694 118 SPSSRPQVDAAQVPSP--LPLSQPSTPPAQAKRAEKPPQSSHESsQHWLEQSDTESHQRHQDGTLTLESQSTSPGSKSP- 194
                          90
                  ....*....|...
gi 73765552   808 LMPSQSQPPVTPS 820
Cdd:pfam15694 195 LHPQENSPHRSGF 207
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
707-820 1.88e-05

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: 48.08  E-value: 1.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552   707 QQDVQTPSAKEEEKIQ-----RRPHELPPQS--QPWVMPSQSQPPVTPSQSHPQVMPSQSQP---PVTPSQSQPRVMPSQ 776
Cdd:pfam09606 317 QQGGNHPAAHQQQMNQsvgqgGQVVALGGLNhlETWNPGNFGGLGANPMQRGQPGMMSSPSPvpgQQVRQVTPNQFMRQS 396
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 73765552   777 SQP----PVMPSQSHPQLTPSQSQP-PVTPSQRQPQLMPSQSQPPVTPS 820
Cdd:pfam09606 397 PQPsvpsPQGPGSQPPQSHPGGMIPsPALIPSPSPQMSQQPAQQRTIGQ 445
DedD COG3147
Cell division protein DedD (periplasmic protein involved in septation) [Cell cycle control, ...
707-810 1.91e-05

Cell division protein DedD (periplasmic protein involved in septation) [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 225689 [Multi-domain]  Cd Length: 226  Bit Score: 46.42  E-value: 1.91e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552 707 QQDVQTPSAKEEEKIQR-RPHELPPQSQPWVMPSQSQPPVTPSQSH---PQVMPSQSQP----PVTPSQSQPRVMPSQSQ 778
Cdd:COG3147  35 QDEVAAIPLPPKPQGDRdEPRVLPAVVQVVALPTQPPEGVAQEIQDagdAAAASVDPQPvaqpPVESTPAGVPVAAQTPK 114
                        90       100       110
                ....*....|....*....|....*....|....
gi 73765552 779 PPVMPSQ--SHPQLTPSQSQPPVTPsQRQPQLMP 810
Cdd:COG3147 115 PVKPPKQppAGAVPAKPTPKPEPKP-VAEPAAAP 147
PRK10263 PRK10263
DNA translocase FtsK; Provisional
703-815 2.16e-05

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 48.16  E-value: 2.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552   703 PIKKQQDVQTPSAKEEEkiQRRPHELPPQSQPWVMPSQSQPPvTPSQSHPQ--VMPS-QSQPPVTPSQSQPRVMPSQSQP 779
Cdd:PRK10263  761 PQQQYQQPQQPVAPQPQ--YQQPQQPVAPQPQYQQPQQPVAP-QPQYQQPQqpVAPQpQYQQPQQPVAPQPQYQQPQQPV 837
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 73765552   780 PVMPSQS--HPQLTPS-QSQPPVTPSQRQPQL-----MPSQSQP 815
Cdd:PRK10263  838 APQPQDTllHPLLMRNgDSRPLHKPTTPLPSLdlltpPPSEVEP 881
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
699-820 2.22e-05

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 48.15  E-value: 2.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552  699 KKSKPIKKQQDVQTPSAKEEEKIQRRPHElppqsqpwvmPSQSQPPVTPSQshPQVMPSQSQP-----PVTPSQSQPRVM 773
Cdd:PTZ00449 565 KEHKPSKIPTLSKKPEFPKDPKHPKDPEE----------PKKPKRPRSAQR--PTRPKSPKLPelldiPKSPKRPESPKS 632
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 73765552  774 PSQSQPPVMPSqshpqlTPSQSQPPVTPSQRQPqlmPSQSQPPVTPS 820
Cdd:PTZ00449 633 PKRPPPPQRPS------SPERPEGPKIIKSPKP---PKSPKPPFDPK 670
PHA03247 PHA03247
large tegument protein UL36; Provisional
725-811 2.56e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.01  E-value: 2.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552   725 PHELPPQSQPwVMPSQSQPP--VTPSQSHPQVMPSQSQPPVTPSQSQPRVmpsqsqpPVMPSQSHPQLTPSQSQPPVTPS 802
Cdd:PHA03247 2552 PPPLPPAAPP-AAPDRSVPPprPAPRPSEPAVTSRARRPDAPPQSARPRA-------PVDDRGDPRGPAPPSPLPPDTHA 2623

                  ....*....
gi 73765552   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 2.69e-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: 2.69e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552    721 IQRRPHELPPQSQPwvmPSQSQPPvTPSQSHPqvmPSQSQPPVTPsqsqprvmpsqsQPPVMPSQSHPQLTPSQSQPPVT 800
Cdd:smart00818  85 TQHHQPNLPQPAQQ---PFQPQPL-QPPQPQQ---PMQPQPPVHP------------IPPLPPQPPLPPMFPMQPLPPLL 145
                           90
                   ....*....|....*.
gi 73765552    801 PSqrqpqlMPSQSQPP 816
Cdd:smart00818 146 PD------LPLEAWPA 155
PHA03378 PHA03378
EBNA-3B; Provisional
721-816 2.78e-05

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 47.75  E-value: 2.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552  721 IQRRPHELPPQSQ-----------PWVMPSQSQPPVTPS-QSHP--QVMPSQSQPPVTPSQSQP-RVMPSQSQPPVMPSQ 785
Cdd:PHA03378 572 LQIQPLTSPTTSQlassapsyaqtPWPVPHPSQTPEPPTtQSHIpeTSAPRQWPMPLRPIPMRPlRMQPITFNVLVFPTP 651
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 73765552  786 SHP---QLTPSQS---QPPVTPSQ---------RQPQLMPSQSQPP 816
Cdd:PHA03378 652 HQPpqvEITPYKPtwtQIGHIPYQpsptgantmLPIQWAPGTMQPP 697
Amelogenin pfam02948
Amelogenin; Amelogenins play a role in biomineralisation. They seem to regulate the formation ...
726-807 3.33e-05

Amelogenin; Amelogenins play a role in biomineralisation. They seem to regulate the formation of crystallites during the secretory stage of tooth enamel development. thought to play a major role in the structural organisation and mineralisation of developing enamel. They are found in the extracellular matrix. Mutations in X-chromosomal amelogenin can cause Amelogenesis imperfecta.


Pssm-ID: 308545 [Multi-domain]  Cd Length: 173  Bit Score: 45.04  E-value: 3.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552   726 HELPPQSQPwVMPSQSQPPVTPSQSHPQVMPSQSQPPVTPSQSQPrvmPSQSQPPVMPSQSHPQLTPSQSQPPVTPSQRQ 805
Cdd:pfam02948  92 HPVIPQFQP-AHGGPIHHPFQPQHTEHPLKPTQLSNPVHPMEPFK---PDHPNKPMFPLQPLPPLFEDRPLEPWPAADKT 167

                  ..
gi 73765552   806 PQ 807
Cdd:pfam02948 168 KQ 169
SPATA3 pfam15662
Spermatogenesis-associated protein 3 family; The SPATA3 family of proteins is expressed ...
716-806 3.58e-05

Spermatogenesis-associated protein 3 family; The SPATA3 family of proteins is expressed significantly in testis and faintly in epididymis in the ten tissues of testis, ovary, spleen, kidney, lung, heart, brain, epididymis, liver and skeletal muscle in mouse. Members are not expressed in the eight other tissues. This suggests that SPATA3 plays potential roles in spermatogenesis cell apoptosis or spermatogenesis.


Pssm-ID: 317965 [Multi-domain]  Cd Length: 191  Bit Score: 45.28  E-value: 3.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552   716 KEEEKIQRRPHELPPQSQPWVMPSQSQPPVTPSQSHPQVMPSQSQPPVTPSQSQPRVMPSQ--SQPPVMPSQSH--PQLT 791
Cdd:pfam15662   6 KKKSEARRHRGSTSQHASSESTPQQPSSESTPQQPSSESTPPHTSPETTPQQPSPESTPQQpaSQALPAPEIRHssRCLL 85
                          90
                  ....*....|....*
gi 73765552   792 PSQSQPPVTPSQRQP 806
Cdd:pfam15662  86 SQDTNTKAAPPSRKA 100
DUF5451 pfam17532
Family of unknown function (DUF5451); This is a family of unknown function found in ...
703-817 3.74e-05

Family of unknown function (DUF5451); This is a family of unknown function found in Epstein-Barr virus.


Pssm-ID: 340247  Cd Length: 148  Bit Score: 44.38  E-value: 3.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552   703 PIKKQQDVQTPSAKEEeKIQRRPHelpPQSQPWVMpsqsQPPvtpsqSHPQVMPSQSQPPVTPSQSQPRVmPSQSQPPVM 782
Cdd:pfam17532   3 PPVFQRLAHAPPAKRQ-ALETVPH---PQNRGQLM----SPK-----AHLPKMQRRPRPPAAKRRRFPLA-PQQVERPIL 68
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 73765552   783 PS-QSHPQ-LTPSQSQ-PPVTPSQRQPQLMPSQSQPPV 817
Cdd:pfam17532  69 PPvESTPQdLEAEEAQnCPQITGMIELCPDQHPMQPPI 106
FAM222A pfam15258
Protein family of FAM222A; This protein family, FAM222A are a domain of unknown function. This ...
722-820 4.14e-05

Protein family of FAM222A; This protein family, FAM222A are a domain of unknown function. This family of proteins is found in eukaryotes and are typically between 411 and 562 amino acids in length. In humans, the gene encoding this protein domain lies in the position, chromosome 12 open reading frame 34.


Pssm-ID: 317640  Cd Length: 529  Bit Score: 46.77  E-value: 4.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552   722 QRRPHELPPQSQPWVMPSQSQPPvtPSQSHPQVMPSQSQP--PVTPSQSQPRVMPSQSQPPVMpsQSHPQltpsqsQPPv 799
Cdd:pfam15258 133 QSLQHPMAPQPQTLAHPQGIPQP--QSLPHPQALQQPQLQglQHTQGLAQSQTLQHAAGPPTQ--TQALQ------QPP- 201
                          90       100
                  ....*....|....*....|..
gi 73765552   800 tPSQRQPQLMPSQSQPP-VTPS 820
Cdd:pfam15258 202 -PGLHGSRKLPDADAPPnVTVS 222
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
711-816 4.92e-05

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


Pssm-ID: 313063 [Multi-domain]  Cd Length: 837  Bit Score: 46.92  E-value: 4.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552   711 QTPSAKEEEKIQRRPHELPPQSQPWVMPSQSQPP-------------------------VTPSQSHPQvmPSQSQPPVTP 765
Cdd:pfam09770 103 QQPAARAASSAQPPASSLPSYQYASQQSQQPSEPartgyekykepepipdlqvdaslwgVAPKKAAAP--APAPQPAAQP 180
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 73765552   766 SQSQPRVMPS----------QSQPPVMPSQSHPQLTPSQSQPPVTPSQRQPQLMPSQSQPP 816
Cdd:pfam09770 181 ARSGSRKMMSleeveaamraQAKKPAQQPAPAPPQQPQAPPAQQQQQQQQFPPQQQQQQQP 241
PRK12757 PRK12757
cell division protein FtsN; Provisional
705-807 5.06e-05

cell division protein FtsN; Provisional


Pssm-ID: 237191 [Multi-domain]  Cd Length: 256  Bit Score: 45.42  E-value: 5.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552  705 KKQQDVQTPSA--KEEEKIQRRPHELPPQSQPwvmpsQSQPPVTPSQSHPQVMPSQSQPPVTPsqsqprvmpsQSQPPVM 782
Cdd:PRK12757  95 MRQQPTQLSEVpyNEQTPQVPRSTVQIQQQAQ-----QQQPPATTAQPQPVTPPRQTTAPVQP----------QTPAPVR 159
                         90       100
                 ....*....|....*....|....*
gi 73765552  783 PSQSHPQLTPSQsQPPVTPSQRQPQ 807
Cdd:PRK12757 160 TQPAAPVTQAVE-APKVEAEKEKEQ 183
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
707-809 5.18e-05

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


Pssm-ID: 313063 [Multi-domain]  Cd Length: 837  Bit Score: 46.54  E-value: 5.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552   707 QQDVQTPSAKEEEKIQRRPHelPPQSQPWVMPSQSQPPVTPSQSHPQVM-PSQ--SQPPVTPSQSQPRVMPSQSQPPVMP 783
Cdd:pfam09770 246 QQPQQHPGQGHPVTILQRPQ--SKQPDPPQPSPQPQAQPFHQQPPPVPVqPTQilQNPNRLSAARVGYPQNPQPGVQPVP 323
                          90       100
                  ....*....|....*....|....*..
gi 73765552   784 SQSHPQLTPSQSQPPvtPSQRQP-QLM 809
Cdd:pfam09770 324 AHQAHRQQGSFGRQA--PIITHPqQLA 348
PHA03378 PHA03378
EBNA-3B; Provisional
729-806 5.43e-05

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 46.60  E-value: 5.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552  729 PPQSQPWVM--PSQSQPPVTPSQSHPQVMPSQSQPPVTPS-QSQPRVMPSQSQPPvmpsQSHPqlTPSQSQPPVTPSQRQ 805
Cdd:PHA03378 746 PPAAAPGRArpPAAAPGRARPPAAAPGAPTPQPPPQAPPApQQRPRGAPTPQPPP----QAGP--TSMQLMPRAAPGQQG 819

                 .
gi 73765552  806 P 806
Cdd:PHA03378 820 P 820
PRK14971 PRK14971
DNA polymerase III subunits gamma and tau; Provisional
708-818 5.86e-05

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 46.31  E-value: 5.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552  708 QDVQTPSAKEEEKIQRRPHELPPQSQPwVMPSQSQPPVTPSQSHPQVMPSQSQPPVTPSQSQPRVMPSQSQP-PVMPSQS 786
Cdd:PRK14971 364 QKGDDASGGRGPKQHIKPVFTQPAAAP-QPSAAAAASPSPSQSSAAAQPSAPQSATQPAGTPPTVSVDPPAAvPVNPPST 442
                         90       100       110
                 ....*....|....*....|....*....|..
gi 73765552  787 HPQLTPsqsqPPVTPSQRQPQLMPSQSQPPVT 818
Cdd:PRK14971 443 APQAVR----PAQFKEEKKIPVSKVSSLGPST 470
PHA03247 PHA03247
large tegument protein UL36; Provisional
730-820 6.49e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.86  E-value: 6.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552   730 PQSQPwvMPSQSQPPVTPSQSHPQVMPSQSQP--PVTPSQSQPRVMPSQSQPPVMPSQSHPqlTPSQSQPPVTPSQRQPQ 807
Cdd:PHA03247 2569 PPPRP--APRPSEPAVTSRARRPDAPPQSARPraPVDDRGDPRGPAPPSPLPPDTHAPDPP--PPSPSPAANEPDPHPPP 2644
                          90
                  ....*....|...
gi 73765552   808 LMPSQSQPPVTPS 820
Cdd:PHA03247 2645 TVPPPERPRDDPA 2657
PHA03377 PHA03377
EBNA-3C; Provisional
723-819 7.10e-05

EBNA-3C; Provisional


Pssm-ID: 177614 [Multi-domain]  Cd Length: 1000  Bit Score: 46.20  E-value: 7.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552   723 RRPHELPPQSqPWvmpsQSQPPVTPSQSHPQVMPSQSQ----PPVTPSQSQPRvmPSQSQPPVMPsqsHPQLTPSQSQPP 798
Cdd:PHA03377  815 QYPGHGHPQG-PW----APRPPHLPPQWDGSAGHGQDQvsqfPHLQSETGPPR--LQLSQVPQLP---YSQTLVSSSAPS 884
                          90       100
                  ....*....|....*....|...
gi 73765552   799 VTPSQRQPQL--MPSQSQPPVTP 819
Cdd:PHA03377  885 WSSPQPRAPIrpIPTRFPPPPMP 907
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
736-820 7.41e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 46.01  E-value: 7.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552  736 VMPSQSQPPVTPSQSHPQVMPSQSQPPVTPSQSQPRVMPSQSQPPVMPSQSHPQLTPSQSQPPVTPSQRQPQLMPSQSQP 815
Cdd:PRK07994 364 PLPEPEVPPQSAAPAASAQATAAPTAAVAPPQAPAVPPPPASAPQQAPAVPLPETTSQLLAARQQLQRAQGATKAKKSEP 443

                 ....*
gi 73765552  816 PVTPS 820
Cdd:PRK07994 444 AAASR 448
G_path_suppress pfam15991
G-protein pathway suppressor; This family of proteins inhibits G-protein- and ...
699-820 1.07e-04

G-protein pathway suppressor; This family of proteins inhibits G-protein- and mitogen-activated protein kinase-mediated signal transduction.


Pssm-ID: 318248 [Multi-domain]  Cd Length: 267  Bit Score: 44.48  E-value: 1.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552   699 KKSKPIKKQQDVQTPSAKEEEKIQRR------PHELPPQSQPWVMPSQS-QPPVTPSQSHPQVMPSQSQPPVTPSQ-SQP 770
Cdd:pfam15991  90 TRKRQLKEQSELFALQQAAQTYLPQLsmqgspHHQQPPGPQMNDKRTRSpSPPVQQSHYYKQTAFFPGYPEHGQQKgSDG 169
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 73765552   771 RVMPSQSQPPVMPS------------QSHPQLTPSQSQP-PVTPSQ-----------RQPQLMPSQSQPPVTPS 820
Cdd:pfam15991 170 RRGYGVARTSWNKSpaqyppssqlfyPAVQYLPPPQPQGqADARLQtiyqpgyalplRQQYEHANQPSPFVSPS 243
Amelogenin pfam02948
Amelogenin; Amelogenins play a role in biomineralisation. They seem to regulate the formation ...
725-819 1.25e-04

Amelogenin; Amelogenins play a role in biomineralisation. They seem to regulate the formation of crystallites during the secretory stage of tooth enamel development. thought to play a major role in the structural organisation and mineralisation of developing enamel. They are found in the extracellular matrix. Mutations in X-chromosomal amelogenin can cause Amelogenesis imperfecta.


Pssm-ID: 308545 [Multi-domain]  Cd Length: 173  Bit Score: 43.12  E-value: 1.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552   725 PHELPPQSQPWVMPSQSQ-PPVTPSQsHPQVMPSQsqpPVTPSQSQPRVMPsQSQPPVMPSQSHPqltpsqSQPPVTPSQ 803
Cdd:pfam02948  50 PPMMPQQQHPSVHSTLHHvVPKLPAH-HPFLIPQQ---PVVPVPGQHPVIP-QFQPAHGGPIHHP------FQPQHTEHP 118
                          90       100
                  ....*....|....*....|....
gi 73765552   804 RQPQ--------LMPSQSQPPVTP 819
Cdd:pfam02948 119 LKPTqlsnpvhpMEPFKPDHPNKP 142
SOBP pfam15279
Sine oculis-binding protein; SOBP is associated with syndromic and nonsyndromic intellectual ...
699-820 1.42e-04

Sine oculis-binding protein; SOBP is associated with syndromic and nonsyndromic intellectual disability. It carries a zinc-finger of the zf-C2H2 type at the N-terminus, and a highly characteristic C-terminal PhPhPhPhPhPh motif. The deduced 873-amino acid protein contains an N-terminal nuclear localization signal (NLS), followed by 2 FCS-type zinc finger motifs, a proline-rich region (PR1), a putative RNA-binding motif region, and a C-terminal NLS embedded in a second proline-rich motif. SOBP is expressed in various human tissues, including developing mouse brain at embryonic day 14. In postnatal and adult mouse brain SOBP is expressed in all neurons, with intense staining in the limbic system. Highest expression is in layer V cortical neurons, hippocampus, pyriform cortex, dorsomedial nucleus of thalamus, amygdala, and hypothalamus. Postnatal expression of SOBP in the limbic system corresponds to a time of active synaptogenesis. the family is also referred to as Jackson circler, JXC1. In seven affected siblings from a consanguineous Israeli Arab family with mental retardation, anterior maxillary protrusion, and strabismus mutations were found in this protein.


Pssm-ID: 317654 [Multi-domain]  Cd Length: 303  Bit Score: 44.38  E-value: 1.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552   699 KKSKPIKKQQDVQTPSAKEEEKIQRRPHELPPQSQPWVM-PSQSQPPVTPSQSHPQVMPSQSQPP---VTPSQSQPrvmP 774
Cdd:pfam15279 128 RPPEPPSLVPPPLPPKLLRKRPGLRPPPGVPPGSPPMSMtPRGPLQKPQPPLPLPAFMEGSSMPPpflRPPPSIGN---L 204
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 73765552   775 SQSQPPVMPSQSHPQLTPSQSQPPVTPSQRQPQLMPSQSQPPVTPS 820
Cdd:pfam15279 205 QGPLPNQSLPPIGPPPKPPRTLGPPSNPMHRPPFSPHPPPPPTPSG 250
Herpes_TAF50 pfam03326
Herpesvirus transcription activation factor (transactivator); This family includes EBV BRLF1 ...
714-820 1.59e-04

Herpesvirus transcription activation factor (transactivator); This family includes EBV BRLF1 and similar ORF 50 proteins from other herpesviruses.


Pssm-ID: 308764 [Multi-domain]  Cd Length: 568  Bit Score: 45.08  E-value: 1.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552   714 SAKEEEKIQRRPHELPPQSQPWVMPSQsQPPVTPSQSHP---QVMPSQSQPPVTP-SQSQPRVMPSQ--SQPPVMPSQSH 787
Cdd:pfam03326 401 TAPEATSAISDVFQGTEVCQPKRIRAL-HPPGSPSANRPlpsSLAPTPTGPVHEPgSSLTPATVPQPldAAPVATPEASH 479
                          90       100       110
                  ....*....|....*....|....*....|...
gi 73765552   788 PQLTPSQSQPPvtPSQRQPQLMPSQSQPpvTPS 820
Cdd:pfam03326 480 ELQPPDEETPQ--PLDEDQALCGQQDAS--HPP 508
YppG pfam14179
YppG-like protein; The YppG-like protein family includes the B. subtilis YppG protein, which ...
747-805 2.34e-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: 316681 [Multi-domain]  Cd Length: 102  Bit Score: 40.92  E-value: 2.34e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 73765552   747 PSQSHPQVMPSQSQPPVTPSQSQprvMPSQSQPPVMPSQSHPQLTPSQSQPPVTPSQRQ 805
Cdd:pfam14179   4 NSQPYPYFSQQHYQQPPQPGYQP---QPPQQQAPQPPYQSPFNPYPKPGPLQQQPSQFQ 59
Retinal pfam15449
Retinal protein; This family of proteins is found in the photoreceptor cells of the retina. ...
721-820 2.38e-04

Retinal protein; This family of proteins is found in the photoreceptor cells of the retina. Mutations of the gene encoding this protein have been associated with retinal disorders such as retinitis pigmentosa and late-onset progressive retinal atrophy. The function of this family of proteins is unknown, but it is likely to be important in the development and function of the retina.


Pssm-ID: 317802 [Multi-domain]  Cd Length: 1292  Bit Score: 44.79  E-value: 2.38e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552    721 IQRRPHE-LPPQSQPWVMPSQSQPPVTPSQSHPQVMPSQSQPPVTPSQSQPRVMPSQSQ--------------PPVMPSQ 785
Cdd:pfam15449 1050 VQRSPSPpLSPAPSPPASPRVLSPPTSKKRTSPPPQHKLPSPPPESPQAQHKLSSPPTQrteasspssgpspsPPTSPSQ 1129
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 73765552    786 SHP-QLTPSQSQP--------------PVTPS--QRQPQLMPSQSQPPVTPS 820
Cdd:pfam15449 1130 GPKeTRDSEDSQAatakasgntcsifcPATSSlfEAKSPFSTAHPLPPPEAG 1181
PRK11633 PRK11633
cell division protein DedD; Provisional
728-816 2.50e-04

cell division protein DedD; Provisional


Pssm-ID: 236940 [Multi-domain]  Cd Length: 226  Bit Score: 43.07  E-value: 2.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552  728 LPPQSQPwvMPSQsqPP---VTPSQSHPQVMPSQSQPPVTPSQSQPRVMPSQSQPPVMPSQSHPQLTPSQSQPPVTPSQR 804
Cdd:PRK11633  56 MPAATQA--LPTQ--PPegaAEAVRAGDAAAPSLDPATVAPPNTPVEPEPAPVEPPKPKPVEKPKPKPKPQQKVEAPPAP 131
                         90
                 ....*....|..
gi 73765552  805 QPQLMPSQSQPP 816
Cdd:PRK11633 132 KPEPKPVVEEKA 143
ZipA COG3115
Cell division protein ZipA, interacts with FtsZ [Cell cycle control, cell division, chromosome ...
699-817 2.96e-04

Cell division protein ZipA, interacts with FtsZ [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 225657 [Multi-domain]  Cd Length: 324  Bit Score: 43.70  E-value: 2.96e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552 699 KKSKPikkQQDVQTPSAKEEEKIQRRPhelpPQSQPWVMPSQSQPPvtpsqsHPQVMPSQSQP----PVTPSQSQPRVMP 774
Cdd:COG3115  69 KNEAP---QFTQEHEAARQSPQHQYQP----EYASAQIKIPVPQPP------QISDPPAHPQPtqpaLDQEQPPEEARQP 135
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 73765552 775 SQSQPPVMPSQSHpQLTPSQSQPPVTPSQRQPQLMPSQSQPPV 817
Cdd:COG3115 136 VLPQEAPAPQPVH-SAAPQPAVQTVQPAVPEQQVQPEEVVEPA 177
SPATA3 pfam15662
Spermatogenesis-associated protein 3 family; The SPATA3 family of proteins is expressed ...
750-820 2.96e-04

Spermatogenesis-associated protein 3 family; The SPATA3 family of proteins is expressed significantly in testis and faintly in epididymis in the ten tissues of testis, ovary, spleen, kidney, lung, heart, brain, epididymis, liver and skeletal muscle in mouse. Members are not expressed in the eight other tissues. This suggests that SPATA3 plays potential roles in spermatogenesis cell apoptosis or spermatogenesis.


Pssm-ID: 317965 [Multi-domain]  Cd Length: 191  Bit Score: 42.58  E-value: 2.96e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 73765552   750 SHPQVMPSQSQPPVTPSQSQPrvmpSQSQPPVMPSQSHPQLTPSQSQPPVTPSQRQPQLMPSQSQPPVTPS 820
Cdd:pfam15662  17 STSQHASSESTPQQPSSESTP----QQPSSESTPPHTSPETTPQQPSPESTPQQPASQALPAPEIRHSSRC 83
Pex14_N pfam04695
Peroxisomal membrane anchor protein (Pex14p) conserved region; Family of peroxisomal membrane ...
750-816 3.68e-04

Peroxisomal membrane anchor protein (Pex14p) conserved region; Family of peroxisomal membrane anchor proteins which bind the PTS1 (peroxisomal targeting signal) receptor and are required for the import of PTS1-containing proteins into peroxisomes. Loss of functional Pex14p results in defects in both the PTS1 and PTS2-dependent import pathways. Deletion analysis of this conserved region implicates it in selective peroxisome degradation. In the majority of members this region is situated at the N-terminus of the protein.


Pssm-ID: 335869  Cd Length: 147  Bit Score: 41.52  E-value: 3.68e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 73765552   750 SHPQVMPSQSQPPVTPSQSQPRVMPSQSQPPvMPSQSHPQLTPSQSQPPVTPSQRQPQLMPSQSQPP 816
Cdd:pfam04695  48 RPPAASSSTQTQDGSSSSSATPQPQAPSQTS-QPPPSPPPPAAQSPQQYRPPIVTYPEFLTKPPRPP 113
PRK14971 PRK14971
DNA polymerase III subunits gamma and tau; Provisional
742-819 3.79e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 43.61  E-value: 3.79e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 73765552  742 QPPVTPSQSHPQVMPSQSQPPVTPSQSQPRVMPSQSQPPVMPSQSHPQLTPSQSQPPVT-PSQRQPQLMPSQSQPPVTP 819
Cdd:PRK14971 370 SGGRGPKQHIKPVFTQPAAAPQPSAAAAASPSPSQSSAAAQPSAPQSATQPAGTPPTVSvDPPAAVPVNPPSTAPQAVR 448
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
729-820 4.33e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.82  E-value: 4.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552  729 PPQSQPWVMPSQSQPPVTPSQSH-----PQVMPSQSQPPVTPSQSQPRVMPSQSQPPVMPSQSHPQLTPSQSQPPVTPSQ 803
Cdd:PRK07764 681 PPPAPAPAAPAAPAGAAPAQPAPapaatPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPP 760
                         90       100
                 ....*....|....*....|
gi 73765552  804 RQ---PQLMPSQSQPPVTPS 820
Cdd:PRK07764 761 PPapaPAAAPAAAPPPSPPS 780
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
729-820 4.33e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.82  E-value: 4.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552  729 PPQSQPWVMPSQSQPPVTPSQSHPQVMPSQSQPPVTPSQSQPRVMPSQSQPPVMPSQSHPQLTPSQSQPPVTPSQRQPQL 808
Cdd:PRK07764 416 APAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPA 495
                         90
                 ....*....|..
gi 73765552  809 MPSQSQPPVTPS 820
Cdd:PRK07764 496 APAAPAAPAGAD 507
PRK14971 PRK14971
DNA polymerase III subunits gamma and tau; Provisional
702-807 5.08e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 43.23  E-value: 5.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552  702 KPIKKQQ--DVQTPSAKEEEKIQRRPHELPPQSQPwvmPSQSQPPVTPSQ-SHPQVMPSQSQPPVTPSQS-QPRVMPSQS 777
Cdd:PRK14971 380 KPVFTQPaaAPQPSAAAAASPSPSQSSAAAQPSAP---QSATQPAGTPPTvSVDPPAAVPVNPPSTAPQAvRPAQFKEEK 456
                         90       100       110
                 ....*....|....*....|....*....|
gi 73765552  778 QPPVMPSQShpqLTPSQSQpPVTPSQRQPQ 807
Cdd:PRK14971 457 KIPVSKVSS---LGPSTLR-PIQEKAEQAT 482
PRK11901 PRK11901
hypothetical protein; Reviewed
738-805 5.31e-04

hypothetical protein; Reviewed


Pssm-ID: 237015 [Multi-domain]  Cd Length: 327  Bit Score: 42.75  E-value: 5.31e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 73765552  738 PSQSQPPVTPSQ----SHPQVMPSQSQP-PVTPSQSQPRVMPSQSQPPVMPSQSHPQL---TPSQSQPPVTPSQRQ 805
Cdd:PRK11901  66 SQQSSNNAGAEKnidlSGSSSLSSGNQSsPSAANNTSDGHDASGVKNTAPPQDISAPPispTPTQAAPPQTPNGQQ 141
SPATA3 pfam15662
Spermatogenesis-associated protein 3 family; The SPATA3 family of proteins is expressed ...
741-819 5.52e-04

Spermatogenesis-associated protein 3 family; The SPATA3 family of proteins is expressed significantly in testis and faintly in epididymis in the ten tissues of testis, ovary, spleen, kidney, lung, heart, brain, epididymis, liver and skeletal muscle in mouse. Members are not expressed in the eight other tissues. This suggests that SPATA3 plays potential roles in spermatogenesis cell apoptosis or spermatogenesis.


Pssm-ID: 317965 [Multi-domain]  Cd Length: 191  Bit Score: 41.81  E-value: 5.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552   741 SQPPVTPSQSHPQvmpsQSQPPVTPSQSQPRVMPSQSQPPVMPSQSHPQLTPSQ--SQPPVTPSQRQ--PQLMPSQSQPP 816
Cdd:pfam15662  17 STSQHASSESTPQ----QPSSESTPQQPSSESTPPHTSPETTPQQPSPESTPQQpaSQALPAPEIRHssRCLLSQDTNTK 92

                  ...
gi 73765552   817 VTP 819
Cdd:pfam15662  93 AAP 95
FAM75 pfam14650
FAM75 family;
738-820 6.02e-04

FAM75 family;


Pssm-ID: 317096  Cd Length: 381  Bit Score: 42.67  E-value: 6.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552   738 PSQSQPPVTPSQSHPQVMPSQSQPPVTPsqsqprvMPSQSQPPVMPsQSHPQL---TPSQSQP-PVTPSQRQPQLmpsQS 813
Cdd:pfam14650  42 SSSLESPSVLFNGISNASPVQIQAKESP-------QLSQAQPLPLP-EAQPQPltqTLPQSQPpPLAQVQTQAHL---QS 110

                  ....*..
gi 73765552   814 QPPVTPS 820
Cdd:pfam14650 111 SLPILPP 117
MITF_TFEB_C_3_N pfam15951
MITF/TFEB/TFEC/TFE3 N-terminus; This domain is found at the N-terminus of several ...
715-819 6.19e-04

MITF/TFEB/TFEC/TFE3 N-terminus; This domain is found at the N-terminus of several transcription factors including microphthalmia-associated transcription factor, transcription factor EB, transcription factor EC and transcription factor E3.


Pssm-ID: 318217  Cd Length: 149  Bit Score: 40.86  E-value: 6.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552   715 AKEEEKIQRRPHELPPQsqpwVMPSQSQPPvTPSQSHPQVMPSQSQPPV----------TPS-----QSQPRVMP---SQ 776
Cdd:pfam15951  13 LQQEEQREQQQQQAAMQ----YMQQRMPAS-TPAISVPQSRPSPAQVPVevlkvqthleNPTkyhiqQSQRQQVKqylST 87
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 73765552   777 SQPPVMPSQSHPQLTPSQSQPPVTPSQRQPQLMPSQSQP-PVTP 819
Cdd:pfam15951  88 TYGNKQAVQFMPASTAQAPPPEMSPGVREQQLVTSAGNSaPNSP 131
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
729-820 6.25e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.05  E-value: 6.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552  729 PPQSQPWVMPSQSQPPVTPSQSHPQVMPSQSQPPVTPSQSQPrvmPSQSQPPVMPSQSHPqlTPSQSQPPVTPSQRQPQL 808
Cdd:PRK07764 412 PAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGA---PSPPPAAAPSAQPAP--APAAAPEPTAAPAPAPPA 486
                         90
                 ....*....|..
gi 73765552  809 MPSQSQPPVTPS 820
Cdd:PRK07764 487 APAPAAAPAAPA 498
Pneumo_att_G pfam05539
Pneumovirinae attachment membrane glycoprotein G;
698-819 6.76e-04

Pneumovirinae attachment membrane glycoprotein G;


Pssm-ID: 114270 [Multi-domain]  Cd Length: 408  Bit Score: 42.73  E-value: 6.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552   698 CKKSKpiKKQQDVQTPSAKEEEKIQRRPHELPPQSQPwvmPSQSQPPVTPSQSHPQVMPSQSQPPVTPSQSQPRVMPSQS 777
Cdd:pfam05539 165 CKEPK--TAVTTSKTTSWPTEVSHPTYPSQVTPQSQP---ATQGHQTATANQRLSSTEPVGTQGTTTSSNPEPQTEPPPS 239
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 73765552   778 QPPVMPSQSHPQLTPSQSQ---------------PPVTPSQRQPQlmpSQSQPPVTP 819
Cdd:pfam05539 240 QRGPSGSPQHPPSTTSQDQsttgdgqehtqrrktPPATSNRRSPH---STATPPPTT 293
Reprolysin_3 pfam13582
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ...
284-343 6.94e-04

Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the characteristic binding motif HExxGHxxGxxH of Reprolysin-like peptidases of family M12B.


Pssm-ID: 316138  Cd Length: 122  Bit Score: 40.02  E-value: 6.94e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552   284 DTSHLFTTLGLRGLSGIGAFRGMCTPHRSCAIVTFMNKTLGTFSIAVAHHLGHNLGMNHD 343
Cdd:pfam13582  63 DLGHLFTGRDVGGGGGLAYVGSVCNSGSKAGVNGGSSPYGDCGVDTFAHEIGHNFGANHT 122
Spc7_N pfam15402
N-terminus of kinetochore NMS complex subunit Spc7;
725-820 7.05e-04

N-terminus of kinetochore NMS complex subunit Spc7;


Pssm-ID: 317767  Cd Length: 913  Bit Score: 43.19  E-value: 7.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552   725 PHELPPQS--QPWVMPSQSQPPVTPsqsHPQVMPSQSQPPVTPS-QSQPRVMPSQSQPPVMPSQSHPQLTPSQSqPPVTP 801
Cdd:pfam15402 606 DHAQPASSpfQENVRASPPKSPVTF---HVAPVASESGSPSLASvRSRPTRQSLGRRESTTPTSKSPQSSPVKN-TSTPS 681
                          90
                  ....*....|....*....
gi 73765552   802 SQRQPQlmPSQsqpPVTPS 820
Cdd:pfam15402 682 KQSTPR--VAR---PSTPA 695
SOBP pfam15279
Sine oculis-binding protein; SOBP is associated with syndromic and nonsyndromic intellectual ...
725-818 7.95e-04

Sine oculis-binding protein; SOBP is associated with syndromic and nonsyndromic intellectual disability. It carries a zinc-finger of the zf-C2H2 type at the N-terminus, and a highly characteristic C-terminal PhPhPhPhPhPh motif. The deduced 873-amino acid protein contains an N-terminal nuclear localization signal (NLS), followed by 2 FCS-type zinc finger motifs, a proline-rich region (PR1), a putative RNA-binding motif region, and a C-terminal NLS embedded in a second proline-rich motif. SOBP is expressed in various human tissues, including developing mouse brain at embryonic day 14. In postnatal and adult mouse brain SOBP is expressed in all neurons, with intense staining in the limbic system. Highest expression is in layer V cortical neurons, hippocampus, pyriform cortex, dorsomedial nucleus of thalamus, amygdala, and hypothalamus. Postnatal expression of SOBP in the limbic system corresponds to a time of active synaptogenesis. the family is also referred to as Jackson circler, JXC1. In seven affected siblings from a consanguineous Israeli Arab family with mental retardation, anterior maxillary protrusion, and strabismus mutations were found in this protein.


Pssm-ID: 317654 [Multi-domain]  Cd Length: 303  Bit Score: 42.07  E-value: 7.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552   725 PHELPPQSQPwvmPSQSQPP-VTPSQSHPQVMPSQS---QPPVTPSQSQPRVMPsqsQPPVMPSQSHPQLTPSQSQPPVT 800
Cdd:pfam15279 199 PSIGNLQGPL---PNQSLPPiGPPPKPPRTLGPPSNpmhRPPFSPHPPPPPTPS---GNPPGLPPPHPRGFPPPFGPPLP 272
                          90       100
                  ....*....|....*....|....
gi 73765552   801 PSQRQPQLM----PSQSQ--PPVT 818
Cdd:pfam15279 273 PVVMVPPEMnfglPSLAPlvPPVT 296
PRK14950 PRK14950
DNA polymerase III subunits gamma and tau; Provisional
718-820 8.21e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 42.49  E-value: 8.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552  718 EEKIQRRPHELPPQSQPwVMPSQSQPPVTPSQShPQVMPSQSQPPVTPsQSQPRVMPSQSQPPVMPSQSHPQltpsQSQP 797
Cdd:PRK14950 357 EALLVPVPAPQPAKPTA-AAPSPVRPTPAPSTR-PKAAAAANIPPKEP-VRETATPPPVPPRPVAPPVPHTP----ESAP 429
                         90       100
                 ....*....|....*....|...
gi 73765552  798 PVTPSQRQPQLMPSQSQPPVTPS 820
Cdd:PRK14950 430 KLTRAAIPVDEKPKYTPPAPPKE 452
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
718-820 8.79e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 42.67  E-value: 8.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552  718 EEKIQRRPHELPPQSQPWVMPSQSQPPV-TPSQSHPQVMPSQSQPPVTPSQSQPRVMPSQSQPPVMPSQSHPQLTPSQSQ 796
Cdd:PRK07764 382 ERRLGVAGGAGAPAAAAPSAAAAAPAAApAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAA 461
                         90       100
                 ....*....|....*....|....
gi 73765552  797 PPVTPSQRQPQLMPSQSQPPVTPS 820
Cdd:PRK07764 462 PSAQPAPAPAAAPEPTAAPAPAPP 485
PLN02258 PLN02258
9-cis-epoxycarotenoid dioxygenase NCED
731-813 9.52e-04

9-cis-epoxycarotenoid dioxygenase NCED


Pssm-ID: 215145  Cd Length: 590  Bit Score: 42.38  E-value: 9.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552  731 QSQPWVMPSQSQPPVTPSQSHPQVMPSQSQPPvTPSQSQPRVMPSQSQPPVMPSQSHPQLTPSQSQPPVTPSQRQPQLMP 810
Cdd:PLN02258   1 SSSSNPTSRSQSHASSSSSSSSQSSPPSSTSP-RPRRRKPSASSLLHTPSILPLPKLSSPSPPSVTLPPAATTQTPQLNP 79

                 ...
gi 73765552  811 SQS 813
Cdd:PLN02258  80 LQR 82
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
729-820 9.74e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 42.67  E-value: 9.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552  729 PPQSQPWVMPSQSQPPVTPS-QSHPQVMPSQSQPPVTPSQSQPRVMPSQSQPPVMPSQSHPQLTPSQSQPPVTPSQRQPQ 807
Cdd:PRK07764 397 AAPSAAAAAPAAAPAPAAAApAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEP 476
                         90
                 ....*....|...
gi 73765552  808 LMPSQSQPPVTPS 820
Cdd:PRK07764 477 TAAPAPAPPAAPA 489
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
712-820 1.00e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 42.39  E-value: 1.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552  712 TPSAKEEEKIQRRPHELPPQSQPWVMPSQSQPPVTPSQSHPQvmPSQSQPPVTPSQSQPRVMPSQSQPPVMPSQSHPQLT 791
Cdd:PRK14951 383 RPEAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPPA--PVAAPAAAAPAAAPAAAPAAVALAPAPPAQAAPETV 460
                         90       100       110
                 ....*....|....*....|....*....|.
gi 73765552  792 --PSQSQPPVTPSQRQPQLMPSQSQPPVTPS 820
Cdd:PRK14951 461 aiPVRVAPEPAVASAAPAPAAAPAAARLTPT 491
Ten_N pfam06484
Teneurin Intracellular Region; This family is found in the intracellular N-terminal region of ...
739-820 1.10e-03

Teneurin Intracellular Region; This family is found in the intracellular N-terminal region of the Teneurin family of proteins. These proteins are 'pair-rule' genes and are involved in tissue patterning, specifically probably neural patterning. The intracellular domain is cleaved in response to homophilic interaction of the extracellular domain, and translocates to the nucleus. Here it probably carries out to some transcriptional regulatory activity. The length of this region and the conservation suggests that there may be two structural domains here (personal obs:C Yeats).


Pssm-ID: 310827  Cd Length: 369  Bit Score: 41.86  E-value: 1.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552   739 SQSQPPVTPSQSHPQVMPSQSQPPVTPS---QSQPRVMPSQSQPPVMPSQSHPQLTP------SQSQPPVTPSQRQPQLM 809
Cdd:pfam06484 157 EENGPPLPCSSSSPSSPSEQHPPPPPPSpanECQRPLLGNNAAQPAQDSDSDEEFVPnsylvrAGSGNLSVPASEGPPNH 236
                          90
                  ....*....|...
gi 73765552   810 PSQS--QPPVTPS 820
Cdd:pfam06484 237 QNQStlRTPLPPP 249
DUF3295 pfam11702
Protein of unknown function (DUF3295); This family is conserved in fungi but the function is ...
711-810 1.26e-03

Protein of unknown function (DUF3295); This family is conserved in fungi but the function is not known.


Pssm-ID: 338068  Cd Length: 485  Bit Score: 41.92  E-value: 1.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552   711 QTPSAKEEEKIQRRPHELPPQSQPWVMPSQSQPPVtPSQS-----------HPQVMPSQSQPP-----VTPSQSQPRVM- 773
Cdd:pfam11702  80 PTPSAPPVVDITPRPSSPPPSSTSTPQPTASPSPE-PSSStstesscststAPSANSSDAPPVgsdtsVSSTGSSHSVVr 158
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 73765552   774 ---PSQSqPPVMPSQSHPQLTPSQSQPPVTPSQRQPQLMP 810
Cdd:pfam11702 159 gfsPSQI-SSSYRSQTQLSPAPSPSKPTSPSAPKPKPVQK 197
PRK14950 PRK14950
DNA polymerase III subunits gamma and tau; Provisional
727-804 1.34e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 42.10  E-value: 1.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552  727 ELPPQSQPWVMPSQSqPPVTPSQSHPQVMP---SQSQPPVTPSQ-SQPRVMPSQSQPPVMPSQSHPQLTPSQSQPPVTPS 802
Cdd:PRK14950 374 AAPSPVRPTPAPSTR-PKAAAAANIPPKEPvreTATPPPVPPRPvAPPVPHTPESAPKLTRAAIPVDEKPKYTPPAPPKE 452

                 ..
gi 73765552  803 QR 804
Cdd:PRK14950 453 EE 454
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
729-819 1.44e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.90  E-value: 1.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552  729 PPQSQPWVMPSQSQPPVTPSQSHPQVMPSQSQPPVTpsqsQPRVMPSQSQPPVMPSQSHPQLTPSQSQPPVTPSQRQPQL 808
Cdd:PRK07764 672 KAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAA----TPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDD 747
                         90
                 ....*....|.
gi 73765552  809 MPSQSQPPVTP 819
Cdd:PRK07764 748 PPDPAGAPAQP 758
PRK14954 PRK14954
DNA polymerase III subunits gamma and tau; Provisional
694-820 1.49e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184918 [Multi-domain]  Cd Length: 620  Bit Score: 41.85  E-value: 1.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552  694 LYRLCKKSKPIKKQQDVQTPSAKEEEKiqrrpheLPPQSQPwvMPSQSQPPVTPSQS--HPQVMPS-------QSQPPVT 764
Cdd:PRK14954 367 LLRLIELVRNDGGVAPSPAGSPDVKKK-------APEPDLP--QPDRHPGPAKPEAPgaRPAELPSpasaptpEQQPPVA 437
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 73765552  765 PSQSQPRvMPSQSQPPVMPSQShPQLTPSQSQPPVT-----PSQRQPqLMPSQSQPPVTPS 820
Cdd:PRK14954 438 RSAPLPP-SPQASAPRNVASGK-PGVDLGSWQGKFMnftrnGSRKQP-VQASSSDAAQTGV 495
FAM222A pfam15258
Protein family of FAM222A; This protein family, FAM222A are a domain of unknown function. This ...
730-819 1.64e-03

Protein family of FAM222A; This protein family, FAM222A are a domain of unknown function. This family of proteins is found in eukaryotes and are typically between 411 and 562 amino acids in length. In humans, the gene encoding this protein domain lies in the position, chromosome 12 open reading frame 34.


Pssm-ID: 317640  Cd Length: 529  Bit Score: 41.77  E-value: 1.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552   730 PQSQPWVMPS--QSQPPVTP-------SQSHPQVMPSQSQ-PPVTPSQSQPRVMP-SQSQPPvmPSQSHPQLTPSQSQPP 798
Cdd:pfam15258 105 PPSGPYAAPStlNHPPQGLPrpqalqhQQSLQHPMAPQPQtLAHPQGIPQPQSLPhPQALQQ--PQLQGLQHTQGLAQSQ 182
                          90       100
                  ....*....|....*....|.
gi 73765552   799 VTPsqrQPQLMPSQSQPPVTP 819
Cdd:pfam15258 183 TLQ---HAAGPPTQTQALQQP 200
PRK10856 PRK10856
cytoskeletal protein RodZ; Provisional
731-819 1.76e-03

cytoskeletal protein RodZ; Provisional


Pssm-ID: 236776 [Multi-domain]  Cd Length: 331  Bit Score: 41.17  E-value: 1.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552  731 QSQPWVMPSQSQPPVTPSQSHPQV-MPSQSQPPVTPSQSQPRVMPSQSQPpVMPSQSHPQLTPSQSQPPVTPSQRQPQLm 809
Cdd:PRK10856 160 QSVPLDTSTTTDPATTPAPAAPVDtTPTNSQTPAVATAPAPAVDPQQNAV-VAPSQANVDTAATPAPAAPATPDGAAPL- 237
                         90
                 ....*....|
gi 73765552  810 PSQSQPPVTP 819
Cdd:PRK10856 238 PTDQAGVSTP 247
YppG pfam14179
YppG-like protein; The YppG-like protein family includes the B. subtilis YppG protein, which ...
726-786 1.76e-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: 316681 [Multi-domain]  Cd Length: 102  Bit Score: 38.22  E-value: 1.76e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 73765552   726 HELPPQSQPWVMPSQSQPPVTPSQShPQVMPSQSQPPVTPSQSQPRVMPSQSQPPVMPSQS 786
Cdd:pfam14179   1 YQPNSQPYPYFSQQHYQQPPQPGYQ-PQPPQQQAPQPPYQSPFNPYPKPGPLQQQPSQFQS 60
PRK01741 PRK01741
cell division protein ZipA; Provisional
699-820 1.78e-03

cell division protein ZipA; Provisional


Pssm-ID: 234977 [Multi-domain]  Cd Length: 332  Bit Score: 41.26  E-value: 1.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552  699 KKSKPIKKQQDVQT-PSAKEEEKIQrrpheLPPQSQPWVMPSQSQPPVTPSQshpqvmPSQSQPPVTPSQSQPRVMPSQS 777
Cdd:PRK01741  80 EESESENEVQIQQEvEQSVDEIKIT-----LPNQEPAYYMQNHRSEPIQPTQ------PQYQSPTQTNVASMTIEETQSP 148
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 73765552  778 QPPVMPSQSH-PQLT-----PSQSQPPVTPSQRQ------PQLMPSQSQPPVTPS 820
Cdd:PRK01741 149 NVPIEGINSSsEQLRvelaeLAAEIYSDASHRVElaknfmEPQAETEAQPEATTN 203
FAM75 pfam14650
FAM75 family;
721-814 2.05e-03

FAM75 family;


Pssm-ID: 317096  Cd Length: 381  Bit Score: 41.13  E-value: 2.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552   721 IQRRPHELP--PQSQPWVMP-SQSQPpVTPSqshpqvmPSQSQPPvTPSQSQPRVMPsQSQPPVMPSQSHPQLTPSQSQP 797
Cdd:pfam14650  61 VQIQAKESPqlSQAQPLPLPeAQPQP-LTQT-------LPQSQPP-PLAQVQTQAHL-QSSLPILPPSSPPQIRTCGVSC 130
                          90
                  ....*....|....*...
gi 73765552   798 PvtPSQRQPQ-LMPSQSQ 814
Cdd:pfam14650 131 P--TSQNKAQsLIPTEIQ 146
Pex14_N pfam04695
Peroxisomal membrane anchor protein (Pex14p) conserved region; Family of peroxisomal membrane ...
718-798 2.10e-03

Peroxisomal membrane anchor protein (Pex14p) conserved region; Family of peroxisomal membrane anchor proteins which bind the PTS1 (peroxisomal targeting signal) receptor and are required for the import of PTS1-containing proteins into peroxisomes. Loss of functional Pex14p results in defects in both the PTS1 and PTS2-dependent import pathways. Deletion analysis of this conserved region implicates it in selective peroxisome degradation. In the majority of members this region is situated at the N-terminus of the protein.


Pssm-ID: 335869  Cd Length: 147  Bit Score: 39.21  E-value: 2.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552   718 EEKIQRRPHELPPQSQPWVMPSQSQPPVTPSqshpqvmPSQSQPPVTPSQSQPRVMPSQSQPPVMPSQSHPQLTPSQSQP 797
Cdd:pfam04695  40 DEALGRAGRPPAASSSTQTQDGSSSSSATPQ-------PQAPSQTSQPPPSPPPPAAQSPQQYRPPIVTYPEFLTKPPRP 112

                  .
gi 73765552   798 P 798
Cdd:pfam04695 113 P 113
SOBP pfam15279
Sine oculis-binding protein; SOBP is associated with syndromic and nonsyndromic intellectual ...
718-820 2.31e-03

Sine oculis-binding protein; SOBP is associated with syndromic and nonsyndromic intellectual disability. It carries a zinc-finger of the zf-C2H2 type at the N-terminus, and a highly characteristic C-terminal PhPhPhPhPhPh motif. The deduced 873-amino acid protein contains an N-terminal nuclear localization signal (NLS), followed by 2 FCS-type zinc finger motifs, a proline-rich region (PR1), a putative RNA-binding motif region, and a C-terminal NLS embedded in a second proline-rich motif. SOBP is expressed in various human tissues, including developing mouse brain at embryonic day 14. In postnatal and adult mouse brain SOBP is expressed in all neurons, with intense staining in the limbic system. Highest expression is in layer V cortical neurons, hippocampus, pyriform cortex, dorsomedial nucleus of thalamus, amygdala, and hypothalamus. Postnatal expression of SOBP in the limbic system corresponds to a time of active synaptogenesis. the family is also referred to as Jackson circler, JXC1. In seven affected siblings from a consanguineous Israeli Arab family with mental retardation, anterior maxillary protrusion, and strabismus mutations were found in this protein.


Pssm-ID: 317654 [Multi-domain]  Cd Length: 303  Bit Score: 40.53  E-value: 2.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552   718 EEKIQRRPHELPPQSQPWV--MPSQSQPPVTPSQSHPQVM-PSQSQPPVTPSQSQPRVMPSQS--QPPVMPSQSHPQLTP 792
Cdd:pfam15279 127 PRPPEPPSLVPPPLPPKLLrkRPGLRPPPGVPPGSPPMSMtPRGPLQKPQPPLPLPAFMEGSSmpPPFLRPPPSIGNLQG 206
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 73765552   793 SQSQPPVTPSQRQPQ----LMPSQS---QPPVTPS 820
Cdd:pfam15279 207 PLPNQSLPPIGPPPKpprtLGPPSNpmhRPPFSPH 241
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
725-820 2.67e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 41.00  E-value: 2.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552  725 PHELPPQSQPWVMPSQSQPPVTPSQSHPQVMPSQSQPPVTPSQSQPRVMPSQSQPPVMPSQSHPQLTPSQSQPPVTPSQR 804
Cdd:PRK07994 371 PPQSAAPAASAQATAAPTAAVAPPQAPAVPPPPASAPQQAPAVPLPETTSQLLAARQQLQRAQGATKAKKSEPAAASRAR 450
                         90       100
                 ....*....|....*....|.
gi 73765552  805 -----QPQLMPSQSQPPVTPS 820
Cdd:PRK07994 451 pvnsaLERLASVRPAPSALEK 471
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
713-818 3.24e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 40.74  E-value: 3.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552  713 PSAKEEEKIQRRPHELPPQSQPWVMPSQSQPPVTPSQSHPQVMPSQSQPPVtpsqsQPRVMPSQSQPPVMPSQSHPQLTP 792
Cdd:PRK07764 414 AAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSA-----QPAPAPAAAPEPTAAPAPAPPAAP 488
                         90       100
                 ....*....|....*....|....*.
gi 73765552  793 SQSQPPVTPSQrqpqlmPSQSQPPVT 818
Cdd:PRK07764 489 APAAAPAAPAA------PAAPAGADD 508
ZnMc_TACE_like cd04270
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ...
287-370 4.05e-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  Cd Length: 244  Bit Score: 39.66  E-value: 4.05e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552 287 HLFT----TLGLRGLSGIGAFR-----GMCTPHR----------SCAIVTFMN--KTLGT--FSIAVAHHLGHNLGMNHD 343
Cdd:cd04270 105 HLFTyrdfDMGTLGLAYVGSPRdnsagGICEKAYyysngkkkylNTGLTTTVNygKRVPTkeSDLVTAHELGHNFGSPHD 184
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 73765552 344 EDTCRCSqP------RCIM--------HEGNppiTKFSNCS 370
Cdd:cd04270 185 PDIAECA-PgesqggNYIMyaratsgdKENN---KKFSPCS 221
DUF1720 pfam08226
Domain of unknown function (DUF1720); This domain is found in different combinations with ...
728-807 5.29e-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: 336963 [Multi-domain]  Cd Length: 76  Bit Score: 36.27  E-value: 5.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552   728 LPPQSQPWVMPSQSQPPVTPSQSHPQVMPSQSQPPVTpsqsqprvMPSQSQPPVMPsQSHPQLTPSQSQPPVTPSQR-QP 806
Cdd:pfam08226   1 MQPQQTGFMPPQQQQPQQTQFGLQPQPTGFMPQQQTG--------QGLQPQPTGMG-QFQPGLQPQQTGFQPQAQQGlQP 71

                  .
gi 73765552   807 Q 807
Cdd:pfam08226  72 Q 72
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
724-819 5.38e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 40.23  E-value: 5.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552  724 RPHELPPQSQpwvMPSQSQPPVTPSQSHPQVMPSQSQPPVTPSQSQPRVMPSQSQPPVMP------SQSHPQLTPSQSQP 797
Cdd:PRK07994 360 HPAAPLPEPE---VPPQSAAPAASAQATAAPTAAVAPPQAPAVPPPPASAPQQAPAVPLPettsqlLAARQQLQRAQGAT 436
                         90       100
                 ....*....|....*....|..
gi 73765552  798 PVTPSQRQPQLMPSQSQPPVTP 819
Cdd:PRK07994 437 KAKKSEPAAASRARPVNSALER 458
myxo_disulf_rpt TIGR02232
Myxococcus cysteine-rich repeat; This model represents a sequence region shared between ...
397-437 6.20e-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  Cd Length: 38  Bit Score: 35.04  E-value: 6.20e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 73765552   397 VKRCGNGVVEEGEECDCGPLKhcAKDPCCLSnCTLTDGSTC 437
Cdd:TIGR02232   1 APTCGDGIIEPGEECDDGNTT--SGDGCSAT-CRLEEGFAC 38
PRK14948 PRK14948
DNA polymerase III subunits gamma and tau; Provisional
739-820 8.36e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237862 [Multi-domain]  Cd Length: 620  Bit Score: 39.56  E-value: 8.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73765552  739 SQSQPPVTPSQSHPQVMPSQSQPPVTPSQSQPRVMPSQSQPPVMPSQSHPQLTPSQSQPPVTPSqRQPQLMPSQSQPPVT 818
Cdd:PRK14948 512 SQSGSASNTAKTPPPPQKSPPPPAPTPPLPQPTATAPPPTPPPPPPTATQASSNAPAQIPADSS-PPPPIPEEPTPSPTK 590

                 ..
gi 73765552  819 PS 820
Cdd:PRK14948 591 DS 592
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.17
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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