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Conserved domains on  [gi|2462624973|ref|XP_054219069|]
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transmembrane protein 8B isoform X8 [Homo sapiens]

Protein Classification

TMEM8 family protein( domain architecture ID 10572301)

TMEM8 family protein is a DUF3522 domain-containing protein; similar to Homo sapiens transmembrane protein 8B, post-GPI attachment to proteins factor 6 and protein myomaker

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DUF3522 pfam12036
Protein of unknown function (DUF3522); This family of proteins is functionally uncharacterized. ...
 454-566 2.90e-34

Protein of unknown function (DUF3522); This family of proteins is functionally uncharacterized. This protein is found in eukaryotes. Proteins in this family are typically between 220 to 787 amino acids in length. This family belongs to the CREST superfamily, which are distant members of the GPCR superfamily.


:

Pssm-ID: 463441  Cd Length: 183  Bit Score: 128.94  E-value: 2.90e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624973 454 MFLPPVVLAIRSRYVLEAAVYTFTMFFSTFYHACDqpgIVVFCIMDYDVLQFC-------DFLGSLMSVWVTVIAMARLQ 526
Cdd:pfam12036  15 AFLPAIYVALKRRYHFEAFVYTFTMFFSFMYHACD---SGVFCFMKYDVLQLCegdwhrlDNIGSILSFWVTFVYLADFD 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2462624973 527 PVVKQVLYLLGAMLLSMALQLDRHGLWNLLGPSLFALGIL 566
Cdd:pfam12036  92 EVLKRFLHYFGLLLTAIAQEKDPWNLWNTLIPILIGLLIL 131
Atrophin-1 super family cl38111
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 21-149 7.28e-06

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


The actual alignment was detected with superfamily member pfam03154:

Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 49.38  E-value: 7.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624973  21 PPSPRFPHRPQPLPGSPSRTPFQSLPLAWPPSRPRPSFHPLS------QIPAQALSQPHSQclLKALAQPRPLLQSPSQP 94
Cdd:pfam03154 188 PPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTliqqtpTLHPQRLPSPHPP--LQPMTQPPPPSQVSPQP 265

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462624973  95 FLPS----------HSL----PLFKPQCPAQPNPLSQPLPSSLCLPKSLPLVPPISH---TLPLSQPRLKSG 149
Cdd:pfam03154 266 LPQPslhgqmppmpHSLqtgpSHMQHPVPPQPFPLTPQSSQSQVPPGPSPAAPGQSQqriHTPPSQSQLQSQ 337
 
Name Accession Description Interval E-value
DUF3522 pfam12036
Protein of unknown function (DUF3522); This family of proteins is functionally uncharacterized. ...
 454-566 2.90e-34

Protein of unknown function (DUF3522); This family of proteins is functionally uncharacterized. This protein is found in eukaryotes. Proteins in this family are typically between 220 to 787 amino acids in length. This family belongs to the CREST superfamily, which are distant members of the GPCR superfamily.


Pssm-ID: 463441  Cd Length: 183  Bit Score: 128.94  E-value: 2.90e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624973 454 MFLPPVVLAIRSRYVLEAAVYTFTMFFSTFYHACDqpgIVVFCIMDYDVLQFC-------DFLGSLMSVWVTVIAMARLQ 526
Cdd:pfam12036  15 AFLPAIYVALKRRYHFEAFVYTFTMFFSFMYHACD---SGVFCFMKYDVLQLCegdwhrlDNIGSILSFWVTFVYLADFD 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2462624973 527 PVVKQVLYLLGAMLLSMALQLDRHGLWNLLGPSLFALGIL 566
Cdd:pfam12036  92 EVLKRFLHYFGLLLTAIAQEKDPWNLWNTLIPILIGLLIL 131
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 21-149 7.28e-06

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 49.38  E-value: 7.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624973  21 PPSPRFPHRPQPLPGSPSRTPFQSLPLAWPPSRPRPSFHPLS------QIPAQALSQPHSQclLKALAQPRPLLQSPSQP 94
Cdd:pfam03154 188 PPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTliqqtpTLHPQRLPSPHPP--LQPMTQPPPPSQVSPQP 265

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462624973  95 FLPS----------HSL----PLFKPQCPAQPNPLSQPLPSSLCLPKSLPLVPPISH---TLPLSQPRLKSG 149
Cdd:pfam03154 266 LPQPslhgqmppmpHSLqtgpSHMQHPVPPQPFPLTPQSSQSQVPPGPSPAAPGQSQqriHTPPSQSQLQSQ 337
PHA03247 PHA03247
large tegument protein UL36; Provisional
 34-144 1.50e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.78  E-value: 1.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624973   34 PGSP-SRTPFQSLPLAWPPSRPRPsfhplsqiPAQALSQPHSQCLLKALAQPRPLLQSPSQPFLPSHSLPLFKPQCPAQP 112
Cdd:PHA03247  2858 PGGDvRRRPPSRSPAAKPAAPARP--------PVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQP 2929

                           90       100       110
                   ....*....|....*....|....*....|..
gi 2462624973  113 NPLSQPlpsslcLPKSLPLVPPISHTLPLSQP 144
Cdd:PHA03247  2930 QPPPPP------PPRPQPPLAPTTDPAGAGEP 2955
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
 31-133 3.80e-04

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: 41.70  E-value: 3.80e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624973   31 QPLPGSPSRTPFQSLPL-----AWPPSRPRPSFHPLSQIPA----------QALSQPHSQCLLKALAQPRPLLQSPSQPF 95
Cdd:smart00818  38 QIIPVSQQHPPTHTLQPhhhipVLPAQQPVVPQQPLMPVPGqhsmtptqhhQPNLPQPAQQPFQPQPLQPPQPQQPMQPQ 117

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2462624973   96 LPSHSLPLFKPQCPAQPNPLSQPLPSslcLPKSLPLVP 133
Cdd:smart00818 118 PPVHPIPPLPPQPPLPPMFPMQPLPP---LLPDLPLEA 152
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 29-134 1.80e-03

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


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 41.29  E-value: 1.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624973  29 RPQPLPGSPSRTPFQSLPLAWP---PSRPRPSFHPLSQIPAQALS-QPHSQcllKALAQPRPLLQSPSQPFLPSHSLPLF 104
Cdd:NF033839  311 KPEPETPKPEVKPQLEKPKPEVkpqPEKPKPEVKPQLETPKPEVKpQPEKP---KPEVKPQPEKPKPEVKPQPETPKPEV 387

                          90       100       110
                  ....*....|....*....|....*....|
gi 2462624973 105 KPQcPAQPNPLSQPLPSSlclPKslPLVPP 134
Cdd:NF033839  388 KPQ-PEKPKPEVKPQPEK---PK--PEVKP 411
 
Name Accession Description Interval E-value
DUF3522 pfam12036
Protein of unknown function (DUF3522); This family of proteins is functionally uncharacterized. ...
 454-566 2.90e-34

Protein of unknown function (DUF3522); This family of proteins is functionally uncharacterized. This protein is found in eukaryotes. Proteins in this family are typically between 220 to 787 amino acids in length. This family belongs to the CREST superfamily, which are distant members of the GPCR superfamily.


Pssm-ID: 463441  Cd Length: 183  Bit Score: 128.94  E-value: 2.90e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624973 454 MFLPPVVLAIRSRYVLEAAVYTFTMFFSTFYHACDqpgIVVFCIMDYDVLQFC-------DFLGSLMSVWVTVIAMARLQ 526
Cdd:pfam12036  15 AFLPAIYVALKRRYHFEAFVYTFTMFFSFMYHACD---SGVFCFMKYDVLQLCegdwhrlDNIGSILSFWVTFVYLADFD 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2462624973 527 PVVKQVLYLLGAMLLSMALQLDRHGLWNLLGPSLFALGIL 566
Cdd:pfam12036  92 EVLKRFLHYFGLLLTAIAQEKDPWNLWNTLIPILIGLLIL 131
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 21-149 7.28e-06

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 49.38  E-value: 7.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624973  21 PPSPRFPHRPQPLPGSPSRTPFQSLPLAWPPSRPRPSFHPLS------QIPAQALSQPHSQclLKALAQPRPLLQSPSQP 94
Cdd:pfam03154 188 PPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTliqqtpTLHPQRLPSPHPP--LQPMTQPPPPSQVSPQP 265

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462624973  95 FLPS----------HSL----PLFKPQCPAQPNPLSQPLPSSLCLPKSLPLVPPISH---TLPLSQPRLKSG 149
Cdd:pfam03154 266 LPQPslhgqmppmpHSLqtgpSHMQHPVPPQPFPLTPQSSQSQVPPGPSPAAPGQSQqriHTPPSQSQLQSQ 337
PHA03247 PHA03247
large tegument protein UL36; Provisional
 34-144 1.50e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.78  E-value: 1.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624973   34 PGSP-SRTPFQSLPLAWPPSRPRPsfhplsqiPAQALSQPHSQCLLKALAQPRPLLQSPSQPFLPSHSLPLFKPQCPAQP 112
Cdd:PHA03247  2858 PGGDvRRRPPSRSPAAKPAAPARP--------PVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQP 2929

                           90       100       110
                   ....*....|....*....|....*....|..
gi 2462624973  113 NPLSQPlpsslcLPKSLPLVPPISHTLPLSQP 144
Cdd:PHA03247  2930 QPPPPP------PPRPQPPLAPTTDPAGAGEP 2955
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 30-143 7.48e-05

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 46.30  E-value: 7.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624973  30 PQPLPGSPSRTPFQSLPLAWPPSRPRPSFHPLSQ------IPAQALSQPHSQCLLKALAQ---PRPLLQSPSQ------P 94
Cdd:pfam03154 387 NSNLPPPPALKPLSSLSTHHPPSAHPPPLQLMPQsqqlppPPAQPPVLTQSQSLPPPAAShppTSGLHQVPSQspfpqhP 466

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462624973  95 FLPSHSLPLFKPQCPAQPNPLSQPL---PSSLCLPKSLPLVPPISHTLPLSQ 143
Cdd:pfam03154 467 FVPGGPPPITPPSGPPTSTSSAMPGiqpPSSASVSSSGPVPAAVSCPLPPVQ 518
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 30-147 1.08e-04

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 45.53  E-value: 1.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624973  30 PQPLPGSPSRTPFQSLPLAWPPSRPRPSFHPLSQI--------------------------PAQALSQPHSQCLLKALAQ 83
Cdd:pfam03154 197 AGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTLIqqtptlhpqrlpsphpplqpmtqpppPSQVSPQPLPQPSLHGQMP 276

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624973  84 PRP-LLQS---------PSQPF-LPSHSL-----PLFKPQCPAQPN-----PLSQPLPSSLCLPKSLPLVPPishtlPLS 142
Cdd:pfam03154 277 PMPhSLQTgpshmqhpvPPQPFpLTPQSSqsqvpPGPSPAAPGQSQqrihtPPSQSQLQSQQPPREQPLPPA-----PLS 351


                  ....*
gi 2462624973 143 QPRLK 147
Cdd:pfam03154 352 MPHIK 356
PHA03247 PHA03247
large tegument protein UL36; Provisional
 30-145 2.96e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.54  E-value: 2.96e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624973   30 PQPLPGSPSRTPFQSLPLawPPSRPRPSFHPLSQIPAQALSQPHSQcllkALAQPRPLLQSPSQPFLPSHSLPLFKPQCP 109
Cdd:PHA03247  2871 PAAKPAAPARPPVRRLAR--PAVSRSTESFALPPDQPERPPQPQAP----PPPQPQPQPPPPPQPQPPPPPPPRPQPPLA 2944

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2462624973  110 AQPNPLSQPLPSSLCLPKSLPLVPPISHTLP---LSQPR 145
Cdd:PHA03247  2945 PTTDPAGAGEPSGAVPQPWLGALVPGRVAVPrfrVPQPA 2983
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
 31-133 3.80e-04

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: 41.70  E-value: 3.80e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624973   31 QPLPGSPSRTPFQSLPL-----AWPPSRPRPSFHPLSQIPA----------QALSQPHSQCLLKALAQPRPLLQSPSQPF 95
Cdd:smart00818  38 QIIPVSQQHPPTHTLQPhhhipVLPAQQPVVPQQPLMPVPGqhsmtptqhhQPNLPQPAQQPFQPQPLQPPQPQQPMQPQ 117

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2462624973   96 LPSHSLPLFKPQCPAQPNPLSQPLPSslcLPKSLPLVP 133
Cdd:smart00818 118 PPVHPIPPLPPQPPLPPMFPMQPLPP---LLPDLPLEA 152
PHA01929 PHA01929
putative scaffolding protein
 34-134 5.46e-04

putative scaffolding protein


Pssm-ID: 177328  Cd Length: 306  Bit Score: 42.73  E-value: 5.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624973  34 PGSPSRTPfQSLPLAWPPSRPRPSFHPlsQIPAQALSQPHSQCLLKALAQPRPLlqsPSQPFLPSHSlplfkPQCPAQPN 113
Cdd:PHA01929   10 PGLAGLVA-NVPPAAAPTPQPNPVIQP--QAPVQPGQPGAPQQLAIPTQQPQPV---PTSAMTPHVV-----QQAPAQPA 78

                          90       100
                  ....*....|....*....|.
gi 2462624973 114 PLSQPLPSSLcLPKSLPLVPP 134
Cdd:PHA01929   79 PAAPPAAGAA-LPEALEVPPP 98
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 28-143 6.85e-04

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


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 43.10  E-value: 6.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624973  28 HRPQPLPGSPSRTPFQSLPLAwPPSRPRPSFHPLSQIPAQALSQPHSQCLLKALAQPRPLLQSPSQPFLPSHSLPLfKPQ 107
Cdd:pfam09770 244 QQPQQQPQQPQQHPGQGHPVT-ILQRPQSPQPDPAQPSIQPQAQQFHQQPPPVPVQPTQILQNPNRLSAARVGYPQ-NPQ 321

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2462624973 108 CPAQPNPLSQPLPSSLCLPKSLPLVPPISHTLPLSQ 143
Cdd:pfam09770 322 PGVQPAPAHQAHRQQGSFGRQAPIITHPQQLAQLSE 357
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 28-141 1.27e-03

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 42.06  E-value: 1.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624973  28 HRPQPLPGSPSRTPFQSLPLAWPPSRPRPSFHPLSQIPAQALSQPHSQCLLKALAQPRPLLQSPSQPFLPSHSLP---LF 104
Cdd:pfam03154 288 HMQHPVPPQPFPLTPQSSQSQVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPAPLSMPHIKPPPTTPipqLP 367

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2462624973 105 KPQCPAQPNPLSQP----LPSSLCLPKSL-PLV------PPISHTLPL 141
Cdd:pfam03154 368 NPQSHKHPPHLSGPspfqMNSNLPPPPALkPLSslsthhPPSAHPPPL 415
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 29-134 1.80e-03

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


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 41.29  E-value: 1.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624973  29 RPQPLPGSPSRTPFQSLPLAWP---PSRPRPSFHPLSQIPAQALS-QPHSQcllKALAQPRPLLQSPSQPFLPSHSLPLF 104
Cdd:NF033839  311 KPEPETPKPEVKPQLEKPKPEVkpqPEKPKPEVKPQLETPKPEVKpQPEKP---KPEVKPQPEKPKPEVKPQPETPKPEV 387

                          90       100       110
                  ....*....|....*....|....*....|
gi 2462624973 105 KPQcPAQPNPLSQPLPSSlclPKslPLVPP 134
Cdd:NF033839  388 KPQ-PEKPKPEVKPQPEK---PK--PEVKP 411
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 29-140 2.59e-03

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 41.29  E-value: 2.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624973  29 RPQPLPGSPSR-TPFQSLPLAWPPSRPRPSfHPLSQIPA-QALSQPHSQCLLKALAQPRPLLQSPS-QPF--LPSHSLPL 103
Cdd:pfam03154 331 QSQLQSQQPPReQPLPPAPLSMPHIKPPPT-TPIPQLPNpQSHKHPPHLSGPSPFQMNSNLPPPPAlKPLssLSTHHPPS 409

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2462624973 104 FKPQcPAQPNPLSQPLPSSLCLPKSL---PLVPPISHTLP 140
Cdd:pfam03154 410 AHPP-PLQLMPQSQQLPPPPAQPPVLtqsQSLPPPAASHP 448
PHA03379 PHA03379
EBNA-3A; Provisional
 28-145 8.44e-03

EBNA-3A; Provisional


Pssm-ID: 223066 [Multi-domain]  Cd Length: 935  Bit Score: 39.66  E-value: 8.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462624973  28 HRPQPLPGSPSRTPFQSLPLAWPPSRP----------------RPSFHPLSQI--PAQALSQPHSQC---LLKALAQPR- 85
Cdd:PHA03379  524 VMPQPMPVEPVPVPTVALERPVCPAPPliamqgpgetsgivrvRERWRPAPWTpnPPRSPSQMSVRDrlaRLRAEAQPYq 603

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462624973  86 -PLLQSPSQPFLPSHSLPLFKPQCPAQPNPLSQPLPSSLCLPKS--LPLVPPISHTLPLSQPR 145
Cdd:PHA03379  604 aSVEVQPPQLTQVSPQQPMEYPLEPEQQMFPGSPFSQVADVMRAggVPAMQPQYFDLPLQQPI 666
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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