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Conserved domains on  [gi|767903378|ref|XP_011539399|]
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terminal uridylyltransferase 4 isoform X1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TUTase pfam19088
TUTase nucleotidyltransferase domain; This nucleotidyltransferase domain is found in TUTase ...
 254-471 8.01e-140

TUTase nucleotidyltransferase domain; This nucleotidyltransferase domain is found in TUTase enzymes. Terminal uridyltransferases (TUTases) execute 3' RNA uridylation across protists, fungi, metazoan and plant species.


:

Pssm-ID: 465974  Cd Length: 218  Bit Score: 429.94  E-value: 8.01e-140
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903378   254 EMDYLENATVIDESALTPEQRLGLKQAEERLERDHIFRLEKRSPEYTNCRYLCKLCLIHIENIQGAHKHIKEKRHKKNIL 333
Cdd:pfam19088    1 DQDEDEDGPVIDESNLTAEQQLGLRQAEERLKRDYIHRLKKRSPEYPNFQYLCKLCSVHIENIQGAHKHIKEKRHKKNIM 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903378   334 EKQEESELRSLPPPSPAHLAALSVAVIELAKEHGITDDDLRVRQEIVEEMSKVITTFLPECSLRLYGSSLTRFALKSSDV 413
Cdd:pfam19088   81 EKQEENELRALPPPSPAQLKALGAAVLEVAQEHGISDEDFEVRQEIVTRMEKIIQQHLPDCSLRLYGSCLTRFAFKTSDI 160

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 767903378   414 NIDIKFPPKMNHPDLLIKVLGILKKNVLYVDVESDFHAKVPVVVCRDRKSGLLCRVSA 471
Cdd:pfam19088  161 NIDVQFPSTMTQPDVLIQVLEILKNSESYSDVESDFHAKVPVVFCRDKQSGLMCKVSA 218
NT_PAP_TUTase cd05402
Nucleotidyltransferase (NT) domain of poly(A) polymerases and terminal uridylyl transferases; ...
 971-1089 6.94e-38

Nucleotidyltransferase (NT) domain of poly(A) polymerases and terminal uridylyl transferases; Poly(A) polymerases (PAPs) catalyze mRNA poly(A) tail synthesis, and terminal uridylyl transferases (TUTases) uridylate RNA. PAPs in this subgroup include human PAP alpha, mouse testis-specific cytoplasmic PAP beta, human nuclear PAP gamma, Saccharomyces cerevisiae PAP1, TRF4 and-5, Schizosaccharomyces pombe caffeine-induced death proteins -1, and -14, Caenorhabditis elegans Germ Line Development-2, and Chlamydomonas reinhardtii MUT68. This family also includes human U6 snRNA-specific TUTase1, and Trypanosoma brucei 3'-TUTase-1,-2, and 4. This family belongs to the Pol beta-like NT superfamily. In the majority of enzymes in this superfamily, two carboxylates, Dx[D/E], together with a third more distal carboxylate, coordinate two divalent metal cations involved in a two-metal ion mechanism of nucleotide addition. For the majority of proteins in this family, these carboxylate residues are conserved.


:

Pssm-ID: 143392 [Multi-domain]  Cd Length: 114  Bit Score: 138.07  E-value: 6.94e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903378  971 NREQILIGLEKFIQKEYdEKARLCLFGSSKNGFGFRDSDLDICMTLEGHenaeKLNCKEIIENLAKILKRHPGLRNILPI 1050
Cdd:cd05402     1 KREEVLDRLQELIKEWF-PGAKLYPFGSYVTGLGLPGSDIDLCLLGPNH----RVDREDFLRKLAKLLKKSGEVVEVEPI 75

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 767903378 1051 TTAKVPIVKFEHRRSGLEGDISLYNTLAQHNTRMLATYA 1089
Cdd:cd05402    76 INARVPIIKFVDKPTGIEVDISFNNLNGIRNTKLLRAYV 114
TRF4 super family cl34961
DNA polymerase sigma [Replication, recombination and repair];
929-1261 9.53e-36

DNA polymerase sigma [Replication, recombination and repair];


The actual alignment was detected with superfamily member COG5260:

Pssm-ID: 227585 [Multi-domain]  Cd Length: 482  Bit Score: 143.37  E-value: 9.53e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903378  929 PEDFRKIDLKPLPP--MTNRFREILDLVCKRC---FDELSPPCSEQHNREQILIGLEKFIQKEYDEkARLCLFGSSKNGF 1003
Cdd:COG5260    30 PLDAKKVSIQELLElsIDSVFNEESDELTSELlefYDYIAPSDEELKRRKALLEKLRTLLKKEFPD-ADLKVFGSTETGL 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903378 1004 GFRDSDLDICMTLEGHENAEKLNCKEiienLAKILKRHPGLRNILPITTAKVPIVKFEHRRSGLEGDISLYNTLAQHNTR 1083
Cdd:COG5260   109 ALPKSDIDLCIISDPRGYKETRNAGS----LASHLFKKNLAKEVVVVSTARVPIIKLVDPQSGLHCDISFNNTNGIVNAK 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903378 1084 MLATYAAIDPRVQYLGYTMKVFAKRCDIGDASRGSLSSYAYILMVLYFLQQRKPPviPVLQEIFDGKQIPQRMVDGWNAF 1163
Cdd:COG5260   185 LIRSYLKEDPRLRPLVLIIKHWLKRRALNDVATGTLSSYTISCMVLSFLQMHPPF--LFFDNGLLSPLKYNKNIDNLGVL 262

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903378 1164 FFDKTEelkkrlpslgknteslgelwlgllrFYTEEFDFKEYVISIRQ-KKLLTTFEKQW--TSKC--IAIEDPF-DLNH 1237
Cdd:COG5260   263 FDDFFE-------------------------LYGKSFNYSLVVLSINSgDFYLPKYEKGWlkPSKPnsLSIQDPGtDRNN 317

                         330       340
                  ....*....|....*....|....
gi 767903378 1238 NLGAgVSRKMtNFIMKAFINGRKL 1261
Cdd:COG5260   318 DISA-VSFNI-KDIKAAFIRAFEL 339
PAP_assoc pfam03828
Cid1 family poly A polymerase; This domain is found in poly(A) polymerases and has been shown ...
 628-677 6.63e-13

Cid1 family poly A polymerase; This domain is found in poly(A) polymerases and has been shown to have polynucleotide adenylyltransferase activity. Proteins in this family have been located to both the nucleus and the cytoplasm.


:

Pssm-ID: 427532  Cd Length: 60  Bit Score: 64.90  E-value: 6.63e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 767903378   628 SLGQLWLELLKFYTLDFALEEYVICVRIQDILTRENKNWPKR------RIAIEDPF 677
Cdd:pfam03828    1 SLGELLIGFFEYYGREFDYENVVISIRTGGILSKKEKGWLRNegrrpfLLCIEDPF 56
Atrophin-1 super family cl38111
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 1404-1593 1.56e-09

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


The actual alignment was detected with superfamily member pfam03154:

Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 62.86  E-value: 1.56e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903378  1404 SAQQQGDQsirTRQSSECSESPSySPQPQPFPQNSSQSAAITQPSSQPGSQPKLGPPQqgAQPPHQVQMPL--------- 1474
Cdd:pfam03154  161 SAQQQILQ---TQPPVLQAQSGA-ASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPAT--SQPPNQTQSTAaphtliqqt 234

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903378  1475 -YNFPQSPPAQYSPMHNMGlLPMHPLQIPAPSWP---IHGPVihsAPGSAPSNIGlndPSIIFAQPAARPVAIPNTSHDG 1550
Cdd:pfam03154  235 pTLHPQRLPSPHPPLQPMT-QPPPPSQVSPQPLPqpsLHGQM---PPMPHSLQTG---PSHMQHPVPPQPFPLTPQSSQS 307

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 767903378  1551 HWPRTVAPNSLVNSGAVGNSEPGFRGLTPPIPWEHAPRPHFPL 1593
Cdd:pfam03154  308 QVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPAPL 350
PTZ00368 super family cl31762
universal minicircle sequence binding protein (UMSBP); Provisional
 1280-1375 3.05e-04

universal minicircle sequence binding protein (UMSBP); Provisional


The actual alignment was detected with superfamily member PTZ00368:

Pssm-ID: 173561 [Multi-domain]  Cd Length: 148  Bit Score: 42.87  E-value: 3.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903378 1280 SRVLTDGELAPNDRCCRVCGKIGHYMKDCPKRKssllfrlKKKDSEEEKEGNEEEKDSRDVLDPRDL------------- 1346
Cdd:PTZ00368   40 SRECPSAPGGRGERSCYNCGKTGHLSRECPEAP-------PGSGPRSCYNCGQTGHISRECPNRAKGgaarracyncgge 112

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 767903378 1347 -HDTRD----FRDPRDLR-CFICGDAGHVRRECPE 1375
Cdd:PTZ00368  113 gHISRDcpnaGKRPGGDKtCYNCGQTGHLSRDCPD 147
rplD super family cl29916
50S ribosomal protein L4; Provisional
 97-199 4.15e-04

50S ribosomal protein L4; Provisional


The actual alignment was detected with superfamily member PRK14907:

Pssm-ID: 184900 [Multi-domain]  Cd Length: 295  Bit Score: 44.17  E-value: 4.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903378   97 KAKKFPNSPVKAEKATISQAKSEKATSLQAKAEKSPKSPNSVKAEKASSYQMKSEKVPSSPAEAEKGPSLLLKDMRQKTE 176
Cdd:PRK14907   19 AAKKATTSKETAKTKKTAKTTSTKAAKKAAKVKKTKSVKTTTKKVTVKFEKTESVKKESVAKKTVKKEAVSAEVFEASNK 98

                          90       100
                  ....*....|....*....|...
gi 767903378  177 LQQIGKKIPSSFTSVDKVNIEAV 199
Cdd:PRK14907   99 LFKNTSKLPKKLFASEKIYSQAI 121
 
Name Accession Description Interval E-value
TUTase pfam19088
TUTase nucleotidyltransferase domain; This nucleotidyltransferase domain is found in TUTase ...
 254-471 8.01e-140

TUTase nucleotidyltransferase domain; This nucleotidyltransferase domain is found in TUTase enzymes. Terminal uridyltransferases (TUTases) execute 3' RNA uridylation across protists, fungi, metazoan and plant species.


Pssm-ID: 465974  Cd Length: 218  Bit Score: 429.94  E-value: 8.01e-140
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903378   254 EMDYLENATVIDESALTPEQRLGLKQAEERLERDHIFRLEKRSPEYTNCRYLCKLCLIHIENIQGAHKHIKEKRHKKNIL 333
Cdd:pfam19088    1 DQDEDEDGPVIDESNLTAEQQLGLRQAEERLKRDYIHRLKKRSPEYPNFQYLCKLCSVHIENIQGAHKHIKEKRHKKNIM 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903378   334 EKQEESELRSLPPPSPAHLAALSVAVIELAKEHGITDDDLRVRQEIVEEMSKVITTFLPECSLRLYGSSLTRFALKSSDV 413
Cdd:pfam19088   81 EKQEENELRALPPPSPAQLKALGAAVLEVAQEHGISDEDFEVRQEIVTRMEKIIQQHLPDCSLRLYGSCLTRFAFKTSDI 160

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 767903378   414 NIDIKFPPKMNHPDLLIKVLGILKKNVLYVDVESDFHAKVPVVVCRDRKSGLLCRVSA 471
Cdd:pfam19088  161 NIDVQFPSTMTQPDVLIQVLEILKNSESYSDVESDFHAKVPVVFCRDKQSGLMCKVSA 218
NT_PAP_TUTase cd05402
Nucleotidyltransferase (NT) domain of poly(A) polymerases and terminal uridylyl transferases; ...
 971-1089 6.94e-38

Nucleotidyltransferase (NT) domain of poly(A) polymerases and terminal uridylyl transferases; Poly(A) polymerases (PAPs) catalyze mRNA poly(A) tail synthesis, and terminal uridylyl transferases (TUTases) uridylate RNA. PAPs in this subgroup include human PAP alpha, mouse testis-specific cytoplasmic PAP beta, human nuclear PAP gamma, Saccharomyces cerevisiae PAP1, TRF4 and-5, Schizosaccharomyces pombe caffeine-induced death proteins -1, and -14, Caenorhabditis elegans Germ Line Development-2, and Chlamydomonas reinhardtii MUT68. This family also includes human U6 snRNA-specific TUTase1, and Trypanosoma brucei 3'-TUTase-1,-2, and 4. This family belongs to the Pol beta-like NT superfamily. In the majority of enzymes in this superfamily, two carboxylates, Dx[D/E], together with a third more distal carboxylate, coordinate two divalent metal cations involved in a two-metal ion mechanism of nucleotide addition. For the majority of proteins in this family, these carboxylate residues are conserved.


Pssm-ID: 143392 [Multi-domain]  Cd Length: 114  Bit Score: 138.07  E-value: 6.94e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903378  971 NREQILIGLEKFIQKEYdEKARLCLFGSSKNGFGFRDSDLDICMTLEGHenaeKLNCKEIIENLAKILKRHPGLRNILPI 1050
Cdd:cd05402     1 KREEVLDRLQELIKEWF-PGAKLYPFGSYVTGLGLPGSDIDLCLLGPNH----RVDREDFLRKLAKLLKKSGEVVEVEPI 75

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 767903378 1051 TTAKVPIVKFEHRRSGLEGDISLYNTLAQHNTRMLATYA 1089
Cdd:cd05402    76 INARVPIIKFVDKPTGIEVDISFNNLNGIRNTKLLRAYV 114
TRF4 COG5260
DNA polymerase sigma [Replication, recombination and repair];
929-1261 9.53e-36

DNA polymerase sigma [Replication, recombination and repair];


Pssm-ID: 227585 [Multi-domain]  Cd Length: 482  Bit Score: 143.37  E-value: 9.53e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903378  929 PEDFRKIDLKPLPP--MTNRFREILDLVCKRC---FDELSPPCSEQHNREQILIGLEKFIQKEYDEkARLCLFGSSKNGF 1003
Cdd:COG5260    30 PLDAKKVSIQELLElsIDSVFNEESDELTSELlefYDYIAPSDEELKRRKALLEKLRTLLKKEFPD-ADLKVFGSTETGL 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903378 1004 GFRDSDLDICMTLEGHENAEKLNCKEiienLAKILKRHPGLRNILPITTAKVPIVKFEHRRSGLEGDISLYNTLAQHNTR 1083
Cdd:COG5260   109 ALPKSDIDLCIISDPRGYKETRNAGS----LASHLFKKNLAKEVVVVSTARVPIIKLVDPQSGLHCDISFNNTNGIVNAK 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903378 1084 MLATYAAIDPRVQYLGYTMKVFAKRCDIGDASRGSLSSYAYILMVLYFLQQRKPPviPVLQEIFDGKQIPQRMVDGWNAF 1163
Cdd:COG5260   185 LIRSYLKEDPRLRPLVLIIKHWLKRRALNDVATGTLSSYTISCMVLSFLQMHPPF--LFFDNGLLSPLKYNKNIDNLGVL 262

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903378 1164 FFDKTEelkkrlpslgknteslgelwlgllrFYTEEFDFKEYVISIRQ-KKLLTTFEKQW--TSKC--IAIEDPF-DLNH 1237
Cdd:COG5260   263 FDDFFE-------------------------LYGKSFNYSLVVLSINSgDFYLPKYEKGWlkPSKPnsLSIQDPGtDRNN 317

                         330       340
                  ....*....|....*....|....
gi 767903378 1238 NLGAgVSRKMtNFIMKAFINGRKL 1261
Cdd:COG5260   318 DISA-VSFNI-KDIKAAFIRAFEL 339
NT_PAP_TUTase cd05402
Nucleotidyltransferase (NT) domain of poly(A) polymerases and terminal uridylyl transferases; ...
 375-487 4.11e-32

Nucleotidyltransferase (NT) domain of poly(A) polymerases and terminal uridylyl transferases; Poly(A) polymerases (PAPs) catalyze mRNA poly(A) tail synthesis, and terminal uridylyl transferases (TUTases) uridylate RNA. PAPs in this subgroup include human PAP alpha, mouse testis-specific cytoplasmic PAP beta, human nuclear PAP gamma, Saccharomyces cerevisiae PAP1, TRF4 and-5, Schizosaccharomyces pombe caffeine-induced death proteins -1, and -14, Caenorhabditis elegans Germ Line Development-2, and Chlamydomonas reinhardtii MUT68. This family also includes human U6 snRNA-specific TUTase1, and Trypanosoma brucei 3'-TUTase-1,-2, and 4. This family belongs to the Pol beta-like NT superfamily. In the majority of enzymes in this superfamily, two carboxylates, Dx[D/E], together with a third more distal carboxylate, coordinate two divalent metal cations involved in a two-metal ion mechanism of nucleotide addition. For the majority of proteins in this family, these carboxylate residues are conserved.


Pssm-ID: 143392 [Multi-domain]  Cd Length: 114  Bit Score: 121.51  E-value: 4.11e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903378  375 VRQEIVEEMSKVITTFLPECSLRLYGSSLTRFALKSSDVNIDIKFPP-KMNHPDLLIKVLGILKKNVLYVDVESDFHAKV 453
Cdd:cd05402     1 KREEVLDRLQELIKEWFPGAKLYPFGSYVTGLGLPGSDIDLCLLGPNhRVDREDFLRKLAKLLKKSGEVVEVEPIINARV 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 767903378  454 PVVVCRDRKSGLLCRVSAGNDMACLTTDLLTALG 487
Cdd:cd05402    81 PIIKFVDKPTGIEVDISFNNLNGIRNTKLLRAYV 114
TRF4 COG5260
DNA polymerase sigma [Replication, recombination and repair];
321-538 1.11e-23

DNA polymerase sigma [Replication, recombination and repair];


Pssm-ID: 227585 [Multi-domain]  Cd Length: 482  Bit Score: 106.78  E-value: 1.11e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903378  321 KHIKEKRHKKNILEKQEESELRSlppPSPAHLAALSVAVIELAKEHGITDDDLRVRQEIVEEMSKVITTFLPECSLRLYG 400
Cdd:COG5260    26 KERRPLDAKKVSIQELLELSIDS---VFNEESDELTSELLEFYDYIAPSDEELKRRKALLEKLRTLLKKEFPDADLKVFG 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903378  401 SSLTRFALKSSDVNIDIKFPPKMNHPDLLIKVLGI-LKKNVLYVDVESDFHAKVPVVVCRDRKSGLLCRVSAGNDMACLT 479
Cdd:COG5260   103 STETGLALPKSDIDLCIISDPRGYKETRNAGSLAShLFKKNLAKEVVVVSTARVPIIKLVDPQSGLHCDISFNNTNGIVN 182

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767903378  480 TDLLTALGKIEPVFIPLVLAFRYWAKLCYIDSQTDGGIPSYCFALMVMFFLQQRKPPLL 538
Cdd:COG5260   183 AKLIRSYLKEDPRLRPLVLIIKHWLKRRALNDVATGTLSSYTISCMVLSFLQMHPPFLF 241
PAP_assoc pfam03828
Cid1 family poly A polymerase; This domain is found in poly(A) polymerases and has been shown ...
 1184-1237 9.43e-18

Cid1 family poly A polymerase; This domain is found in poly(A) polymerases and has been shown to have polynucleotide adenylyltransferase activity. Proteins in this family have been located to both the nucleus and the cytoplasm.


Pssm-ID: 427532  Cd Length: 60  Bit Score: 78.77  E-value: 9.43e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903378  1184 SLGELWLGLLRFYTEEFDFKEYVISIRQKKLLTTFEKQWT------SKCIAIEDPFDLNH 1237
Cdd:pfam03828    1 SLGELLIGFFEYYGREFDYENVVISIRTGGILSKKEKGWLrnegrrPFLLCIEDPFDLDN 60
PAP_assoc pfam03828
Cid1 family poly A polymerase; This domain is found in poly(A) polymerases and has been shown ...
 628-677 6.63e-13

Cid1 family poly A polymerase; This domain is found in poly(A) polymerases and has been shown to have polynucleotide adenylyltransferase activity. Proteins in this family have been located to both the nucleus and the cytoplasm.


Pssm-ID: 427532  Cd Length: 60  Bit Score: 64.90  E-value: 6.63e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 767903378   628 SLGQLWLELLKFYTLDFALEEYVICVRIQDILTRENKNWPKR------RIAIEDPF 677
Cdd:pfam03828    1 SLGELLIGFFEYYGREFDYENVVISIRTGGILSKKEKGWLRNegrrpfLLCIEDPF 56
NTP_transf_2 pfam01909
Nucleotidyltransferase domain; Members of this family belong to a large family of ...
 979-1064 4.73e-10

Nucleotidyltransferase domain; Members of this family belong to a large family of nucleotidyltransferases. This family includes kanamycin nucleotidyltransferase (KNTase) which is a plasmid-coded enzyme responsible for some types of bacterial resistance to aminoglycosides. KNTase in-activates antibiotics by catalysing the addition of a nucleotidyl group onto the drug.


Pssm-ID: 396474  Cd Length: 91  Bit Score: 57.81  E-value: 4.73e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903378   979 LEKFIQ--KEYDEKARLCLFGSSKNGFGFRDSDLDICMTLEGHENAE-KLNCKEIIENLAKILKRHPGLRNILPITTAKV 1055
Cdd:pfam01909    1 LRKLREilKELFPVAEVVLFGSYARGTALPGSDIDLLVVFPEPVEEErLLKLAKIIKELEELLGLEVDLVTREKIEFPLV 80


                   ....*....
gi 767903378  1056 PIVKFEHRR 1064
Cdd:pfam01909   81 KIDILEERI 89
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 1404-1593 1.56e-09

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 62.86  E-value: 1.56e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903378  1404 SAQQQGDQsirTRQSSECSESPSySPQPQPFPQNSSQSAAITQPSSQPGSQPKLGPPQqgAQPPHQVQMPL--------- 1474
Cdd:pfam03154  161 SAQQQILQ---TQPPVLQAQSGA-ASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPAT--SQPPNQTQSTAaphtliqqt 234

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903378  1475 -YNFPQSPPAQYSPMHNMGlLPMHPLQIPAPSWP---IHGPVihsAPGSAPSNIGlndPSIIFAQPAARPVAIPNTSHDG 1550
Cdd:pfam03154  235 pTLHPQRLPSPHPPLQPMT-QPPPPSQVSPQPLPqpsLHGQM---PPMPHSLQTG---PSHMQHPVPPQPFPLTPQSSQS 307

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 767903378  1551 HWPRTVAPNSLVNSGAVGNSEPGFRGLTPPIPWEHAPRPHFPL 1593
Cdd:pfam03154  308 QVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPAPL 350
PHA03247 PHA03247
large tegument protein UL36; Provisional
 1406-1592 3.23e-08

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 58.80  E-value: 3.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903378 1406 QQQGDQSIRTRQSSECSESPSYSPQPQPFPQNSSQSAAITQPSSQPGSQPKLGPPQQGAQPPHQVQMPLYNFPQSPPAqy 1485
Cdd:PHA03247 2908 PPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPS-- 2985

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903378 1486 spmhnmgllpmhplqIPAPSWPIHGPVIHSAPG--SAPSNIGLNDpsiifaQPAARPVAIPNTSHDGHWPRTVAPNSLVN 1563
Cdd:PHA03247 2986 ---------------REAPASSTPPLTGHSLSRvsSWASSLALHE------ETDPPPVSLKQTLWPPDDTEDSDADSLFD 3044

                         170       180       190
                  ....*....|....*....|....*....|.
gi 767903378 1564 SGAVGNSEPGFRGLTPP--IPWEHAPRPHFP 1592
Cdd:PHA03247 3045 SDSERSDLEALDPLPPEphDPFAHEPDPATP 3075
KLF3_N cd21577
N-terminal domain of Kruppel-like factor 3; Kruppel-like factor 3 (KLF3; also called ...
 1410-1565 7.44e-05

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


Pssm-ID: 410554 [Multi-domain]  Cd Length: 214  Bit Score: 45.80  E-value: 7.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903378 1410 DQSIRTRQSSECSESPSYSPQPQPFPQNSSQSaaitqPSSQPGSQPKLGPPQQgaQPPhqvqmplynfpqSPPAQYSPMh 1489
Cdd:cd21577    23 DLSLSKRSSPPSSSSSSSSSSSSSSSPSSRAS-----PPSPYSKSSPPSPPQQ--RPL------------SPPLSLPPP- 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767903378 1490 nMGLLPMHPLQIPAPSWPIHGPVIHSAPGSAPSNIGLndpSIIfaqpaarpVAIPNTSHDGHWPRTVAPNSLVNSG 1565
Cdd:cd21577    83 -VAPPPLSPGSVPGGLPVISPVMVQPVPVLYPPHLHQ---PIM--------VSSSPPPDDDHHHHKASSMKPSELG 146
PTZ00368 PTZ00368
universal minicircle sequence binding protein (UMSBP); Provisional
 1280-1375 3.05e-04

universal minicircle sequence binding protein (UMSBP); Provisional


Pssm-ID: 173561 [Multi-domain]  Cd Length: 148  Bit Score: 42.87  E-value: 3.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903378 1280 SRVLTDGELAPNDRCCRVCGKIGHYMKDCPKRKssllfrlKKKDSEEEKEGNEEEKDSRDVLDPRDL------------- 1346
Cdd:PTZ00368   40 SRECPSAPGGRGERSCYNCGKTGHLSRECPEAP-------PGSGPRSCYNCGQTGHISRECPNRAKGgaarracyncgge 112

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 767903378 1347 -HDTRD----FRDPRDLR-CFICGDAGHVRRECPE 1375
Cdd:PTZ00368  113 gHISRDcpnaGKRPGGDKtCYNCGQTGHLSRDCPD 147
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
 1429-1507 3.09e-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: 43.24  E-value: 3.09e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903378   1429 PQPQPFPQNSSQSAAITQPSSQPgSQPKLGPPQQGAQP--PHQVQMPLYNFPQSPPAQysPMHNMGLLPMHPLQIPAPSW 1506
Cdd:smart00818   77 PGQHSMTPTQHHQPNLPQPAQQP-FQPQPLQPPQPQQPmqPQPPVHPIPPLPPQPPLP--PMFPMQPLPPLLPDLPLEAW 153


                    .
gi 767903378   1507 P 1507
Cdd:smart00818  154 P 154
rplD PRK14907
50S ribosomal protein L4; Provisional
 97-199 4.15e-04

50S ribosomal protein L4; Provisional


Pssm-ID: 184900 [Multi-domain]  Cd Length: 295  Bit Score: 44.17  E-value: 4.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903378   97 KAKKFPNSPVKAEKATISQAKSEKATSLQAKAEKSPKSPNSVKAEKASSYQMKSEKVPSSPAEAEKGPSLLLKDMRQKTE 176
Cdd:PRK14907   19 AAKKATTSKETAKTKKTAKTTSTKAAKKAAKVKKTKSVKTTTKKVTVKFEKTESVKKESVAKKTVKKEAVSAEVFEASNK 98

                          90       100
                  ....*....|....*....|...
gi 767903378  177 LQQIGKKIPSSFTSVDKVNIEAV 199
Cdd:PRK14907   99 LFKNTSKLPKKLFASEKIYSQAI 121
ZnF_C2HC smart00343
zinc finger;
1294-1310 8.99e-03

zinc finger;


Pssm-ID: 197667 [Multi-domain]  Cd Length: 17  Bit Score: 35.11  E-value: 8.99e-03
                            10
                    ....*....|....*..
gi 767903378   1294 CCRVCGKIGHYMKDCPK 1310
Cdd:smart00343    1 KCYNCGKEGHIARDCPS 17
 
Name Accession Description Interval E-value
TUTase pfam19088
TUTase nucleotidyltransferase domain; This nucleotidyltransferase domain is found in TUTase ...
 254-471 8.01e-140

TUTase nucleotidyltransferase domain; This nucleotidyltransferase domain is found in TUTase enzymes. Terminal uridyltransferases (TUTases) execute 3' RNA uridylation across protists, fungi, metazoan and plant species.


Pssm-ID: 465974  Cd Length: 218  Bit Score: 429.94  E-value: 8.01e-140
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903378   254 EMDYLENATVIDESALTPEQRLGLKQAEERLERDHIFRLEKRSPEYTNCRYLCKLCLIHIENIQGAHKHIKEKRHKKNIL 333
Cdd:pfam19088    1 DQDEDEDGPVIDESNLTAEQQLGLRQAEERLKRDYIHRLKKRSPEYPNFQYLCKLCSVHIENIQGAHKHIKEKRHKKNIM 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903378   334 EKQEESELRSLPPPSPAHLAALSVAVIELAKEHGITDDDLRVRQEIVEEMSKVITTFLPECSLRLYGSSLTRFALKSSDV 413
Cdd:pfam19088   81 EKQEENELRALPPPSPAQLKALGAAVLEVAQEHGISDEDFEVRQEIVTRMEKIIQQHLPDCSLRLYGSCLTRFAFKTSDI 160

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 767903378   414 NIDIKFPPKMNHPDLLIKVLGILKKNVLYVDVESDFHAKVPVVVCRDRKSGLLCRVSA 471
Cdd:pfam19088  161 NIDVQFPSTMTQPDVLIQVLEILKNSESYSDVESDFHAKVPVVFCRDKQSGLMCKVSA 218
NT_PAP_TUTase cd05402
Nucleotidyltransferase (NT) domain of poly(A) polymerases and terminal uridylyl transferases; ...
 971-1089 6.94e-38

Nucleotidyltransferase (NT) domain of poly(A) polymerases and terminal uridylyl transferases; Poly(A) polymerases (PAPs) catalyze mRNA poly(A) tail synthesis, and terminal uridylyl transferases (TUTases) uridylate RNA. PAPs in this subgroup include human PAP alpha, mouse testis-specific cytoplasmic PAP beta, human nuclear PAP gamma, Saccharomyces cerevisiae PAP1, TRF4 and-5, Schizosaccharomyces pombe caffeine-induced death proteins -1, and -14, Caenorhabditis elegans Germ Line Development-2, and Chlamydomonas reinhardtii MUT68. This family also includes human U6 snRNA-specific TUTase1, and Trypanosoma brucei 3'-TUTase-1,-2, and 4. This family belongs to the Pol beta-like NT superfamily. In the majority of enzymes in this superfamily, two carboxylates, Dx[D/E], together with a third more distal carboxylate, coordinate two divalent metal cations involved in a two-metal ion mechanism of nucleotide addition. For the majority of proteins in this family, these carboxylate residues are conserved.


Pssm-ID: 143392 [Multi-domain]  Cd Length: 114  Bit Score: 138.07  E-value: 6.94e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903378  971 NREQILIGLEKFIQKEYdEKARLCLFGSSKNGFGFRDSDLDICMTLEGHenaeKLNCKEIIENLAKILKRHPGLRNILPI 1050
Cdd:cd05402     1 KREEVLDRLQELIKEWF-PGAKLYPFGSYVTGLGLPGSDIDLCLLGPNH----RVDREDFLRKLAKLLKKSGEVVEVEPI 75

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 767903378 1051 TTAKVPIVKFEHRRSGLEGDISLYNTLAQHNTRMLATYA 1089
Cdd:cd05402    76 INARVPIIKFVDKPTGIEVDISFNNLNGIRNTKLLRAYV 114
TRF4 COG5260
DNA polymerase sigma [Replication, recombination and repair];
929-1261 9.53e-36

DNA polymerase sigma [Replication, recombination and repair];


Pssm-ID: 227585 [Multi-domain]  Cd Length: 482  Bit Score: 143.37  E-value: 9.53e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903378  929 PEDFRKIDLKPLPP--MTNRFREILDLVCKRC---FDELSPPCSEQHNREQILIGLEKFIQKEYDEkARLCLFGSSKNGF 1003
Cdd:COG5260    30 PLDAKKVSIQELLElsIDSVFNEESDELTSELlefYDYIAPSDEELKRRKALLEKLRTLLKKEFPD-ADLKVFGSTETGL 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903378 1004 GFRDSDLDICMTLEGHENAEKLNCKEiienLAKILKRHPGLRNILPITTAKVPIVKFEHRRSGLEGDISLYNTLAQHNTR 1083
Cdd:COG5260   109 ALPKSDIDLCIISDPRGYKETRNAGS----LASHLFKKNLAKEVVVVSTARVPIIKLVDPQSGLHCDISFNNTNGIVNAK 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903378 1084 MLATYAAIDPRVQYLGYTMKVFAKRCDIGDASRGSLSSYAYILMVLYFLQQRKPPviPVLQEIFDGKQIPQRMVDGWNAF 1163
Cdd:COG5260   185 LIRSYLKEDPRLRPLVLIIKHWLKRRALNDVATGTLSSYTISCMVLSFLQMHPPF--LFFDNGLLSPLKYNKNIDNLGVL 262

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903378 1164 FFDKTEelkkrlpslgknteslgelwlgllrFYTEEFDFKEYVISIRQ-KKLLTTFEKQW--TSKC--IAIEDPF-DLNH 1237
Cdd:COG5260   263 FDDFFE-------------------------LYGKSFNYSLVVLSINSgDFYLPKYEKGWlkPSKPnsLSIQDPGtDRNN 317

                         330       340
                  ....*....|....*....|....
gi 767903378 1238 NLGAgVSRKMtNFIMKAFINGRKL 1261
Cdd:COG5260   318 DISA-VSFNI-KDIKAAFIRAFEL 339
NT_PAP_TUTase cd05402
Nucleotidyltransferase (NT) domain of poly(A) polymerases and terminal uridylyl transferases; ...
 375-487 4.11e-32

Nucleotidyltransferase (NT) domain of poly(A) polymerases and terminal uridylyl transferases; Poly(A) polymerases (PAPs) catalyze mRNA poly(A) tail synthesis, and terminal uridylyl transferases (TUTases) uridylate RNA. PAPs in this subgroup include human PAP alpha, mouse testis-specific cytoplasmic PAP beta, human nuclear PAP gamma, Saccharomyces cerevisiae PAP1, TRF4 and-5, Schizosaccharomyces pombe caffeine-induced death proteins -1, and -14, Caenorhabditis elegans Germ Line Development-2, and Chlamydomonas reinhardtii MUT68. This family also includes human U6 snRNA-specific TUTase1, and Trypanosoma brucei 3'-TUTase-1,-2, and 4. This family belongs to the Pol beta-like NT superfamily. In the majority of enzymes in this superfamily, two carboxylates, Dx[D/E], together with a third more distal carboxylate, coordinate two divalent metal cations involved in a two-metal ion mechanism of nucleotide addition. For the majority of proteins in this family, these carboxylate residues are conserved.


Pssm-ID: 143392 [Multi-domain]  Cd Length: 114  Bit Score: 121.51  E-value: 4.11e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903378  375 VRQEIVEEMSKVITTFLPECSLRLYGSSLTRFALKSSDVNIDIKFPP-KMNHPDLLIKVLGILKKNVLYVDVESDFHAKV 453
Cdd:cd05402     1 KREEVLDRLQELIKEWFPGAKLYPFGSYVTGLGLPGSDIDLCLLGPNhRVDREDFLRKLAKLLKKSGEVVEVEPIINARV 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 767903378  454 PVVVCRDRKSGLLCRVSAGNDMACLTTDLLTALG 487
Cdd:cd05402    81 PIIKFVDKPTGIEVDISFNNLNGIRNTKLLRAYV 114
TRF4 COG5260
DNA polymerase sigma [Replication, recombination and repair];
321-538 1.11e-23

DNA polymerase sigma [Replication, recombination and repair];


Pssm-ID: 227585 [Multi-domain]  Cd Length: 482  Bit Score: 106.78  E-value: 1.11e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903378  321 KHIKEKRHKKNILEKQEESELRSlppPSPAHLAALSVAVIELAKEHGITDDDLRVRQEIVEEMSKVITTFLPECSLRLYG 400
Cdd:COG5260    26 KERRPLDAKKVSIQELLELSIDS---VFNEESDELTSELLEFYDYIAPSDEELKRRKALLEKLRTLLKKEFPDADLKVFG 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903378  401 SSLTRFALKSSDVNIDIKFPPKMNHPDLLIKVLGI-LKKNVLYVDVESDFHAKVPVVVCRDRKSGLLCRVSAGNDMACLT 479
Cdd:COG5260   103 STETGLALPKSDIDLCIISDPRGYKETRNAGSLAShLFKKNLAKEVVVVSTARVPIIKLVDPQSGLHCDISFNNTNGIVN 182

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767903378  480 TDLLTALGKIEPVFIPLVLAFRYWAKLCYIDSQTDGGIPSYCFALMVMFFLQQRKPPLL 538
Cdd:COG5260   183 AKLIRSYLKEDPRLRPLVLIIKHWLKRRALNDVATGTLSSYTISCMVLSFLQMHPPFLF 241
PAP_assoc pfam03828
Cid1 family poly A polymerase; This domain is found in poly(A) polymerases and has been shown ...
 1184-1237 9.43e-18

Cid1 family poly A polymerase; This domain is found in poly(A) polymerases and has been shown to have polynucleotide adenylyltransferase activity. Proteins in this family have been located to both the nucleus and the cytoplasm.


Pssm-ID: 427532  Cd Length: 60  Bit Score: 78.77  E-value: 9.43e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903378  1184 SLGELWLGLLRFYTEEFDFKEYVISIRQKKLLTTFEKQWT------SKCIAIEDPFDLNH 1237
Cdd:pfam03828    1 SLGELLIGFFEYYGREFDYENVVISIRTGGILSKKEKGWLrnegrrPFLLCIEDPFDLDN 60
PAP_assoc pfam03828
Cid1 family poly A polymerase; This domain is found in poly(A) polymerases and has been shown ...
 628-677 6.63e-13

Cid1 family poly A polymerase; This domain is found in poly(A) polymerases and has been shown to have polynucleotide adenylyltransferase activity. Proteins in this family have been located to both the nucleus and the cytoplasm.


Pssm-ID: 427532  Cd Length: 60  Bit Score: 64.90  E-value: 6.63e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 767903378   628 SLGQLWLELLKFYTLDFALEEYVICVRIQDILTRENKNWPKR------RIAIEDPF 677
Cdd:pfam03828    1 SLGELLIGFFEYYGREFDYENVVISIRTGGILSKKEKGWLRNegrrpfLLCIEDPF 56
NTP_transf_2 pfam01909
Nucleotidyltransferase domain; Members of this family belong to a large family of ...
 979-1064 4.73e-10

Nucleotidyltransferase domain; Members of this family belong to a large family of nucleotidyltransferases. This family includes kanamycin nucleotidyltransferase (KNTase) which is a plasmid-coded enzyme responsible for some types of bacterial resistance to aminoglycosides. KNTase in-activates antibiotics by catalysing the addition of a nucleotidyl group onto the drug.


Pssm-ID: 396474  Cd Length: 91  Bit Score: 57.81  E-value: 4.73e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903378   979 LEKFIQ--KEYDEKARLCLFGSSKNGFGFRDSDLDICMTLEGHENAE-KLNCKEIIENLAKILKRHPGLRNILPITTAKV 1055
Cdd:pfam01909    1 LRKLREilKELFPVAEVVLFGSYARGTALPGSDIDLLVVFPEPVEEErLLKLAKIIKELEELLGLEVDLVTREKIEFPLV 80


                   ....*....
gi 767903378  1056 PIVKFEHRR 1064
Cdd:pfam01909   81 KIDILEERI 89
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 1404-1593 1.56e-09

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 62.86  E-value: 1.56e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903378  1404 SAQQQGDQsirTRQSSECSESPSySPQPQPFPQNSSQSAAITQPSSQPGSQPKLGPPQqgAQPPHQVQMPL--------- 1474
Cdd:pfam03154  161 SAQQQILQ---TQPPVLQAQSGA-ASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPAT--SQPPNQTQSTAaphtliqqt 234

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903378  1475 -YNFPQSPPAQYSPMHNMGlLPMHPLQIPAPSWP---IHGPVihsAPGSAPSNIGlndPSIIFAQPAARPVAIPNTSHDG 1550
Cdd:pfam03154  235 pTLHPQRLPSPHPPLQPMT-QPPPPSQVSPQPLPqpsLHGQM---PPMPHSLQTG---PSHMQHPVPPQPFPLTPQSSQS 307

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 767903378  1551 HWPRTVAPNSLVNSGAVGNSEPGFRGLTPPIPWEHAPRPHFPL 1593
Cdd:pfam03154  308 QVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPAPL 350
PHA03247 PHA03247
large tegument protein UL36; Provisional
 1406-1592 3.23e-08

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 58.80  E-value: 3.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903378 1406 QQQGDQSIRTRQSSECSESPSYSPQPQPFPQNSSQSAAITQPSSQPGSQPKLGPPQQGAQPPHQVQMPLYNFPQSPPAqy 1485
Cdd:PHA03247 2908 PPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPS-- 2985

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903378 1486 spmhnmgllpmhplqIPAPSWPIHGPVIHSAPG--SAPSNIGLNDpsiifaQPAARPVAIPNTSHDGHWPRTVAPNSLVN 1563
Cdd:PHA03247 2986 ---------------REAPASSTPPLTGHSLSRvsSWASSLALHE------ETDPPPVSLKQTLWPPDDTEDSDADSLFD 3044

                         170       180       190
                  ....*....|....*....|....*....|.
gi 767903378 1564 SGAVGNSEPGFRGLTPP--IPWEHAPRPHFP 1592
Cdd:PHA03247 3045 SDSERSDLEALDPLPPEphDPFAHEPDPATP 3075
SOBP pfam15279
Sine oculis-binding protein; SOBP is associated with syndromic and nonsyndromic intellectual ...
 1423-1546 4.39e-06

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 characteriztic 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: 464609 [Multi-domain]  Cd Length: 325  Bit Score: 50.58  E-value: 4.39e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903378  1423 ESPSYSPQPQPFPQNSSQSAAITQPSSQPGSQPKLGPPQQGAQPPHQVQMPLYnFPQSPPAQYSPMHNM-GLLPMHPlqi 1501
Cdd:pfam15279  191 EPSSMPPPFLRPPPSIPQPNSPLSNPMLPGIGPPPKPPRNLGPPSNPMHRPPF-SPHHPPPPPTPPGPPpGLPPPPP--- 266

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 767903378  1502 papswPIHGPviHSAPGSAPSNIGLNDPSIIFAQPAARPVAIPNT 1546
Cdd:pfam15279  267 -----RGFTP--PFGPPFPPVNMMPNPPEMNFGLPSLAPLVPPVT 304
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 1398-1513 7.83e-06

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: 50.80  E-value: 7.83e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903378  1398 AQQVAGSAQQ--QGDQSIRTRQSSECSESPSYSPQPQPFPQNS-----------------SQSAAITQPSSQPGSQPKLG 1458
Cdd:pfam09770  211 AQQPAPAPAQppAAPPAQQAQQQQQFPPQIQQQQQPQQQPQQPqqhpgqghpvtilqrpqSPQPDPAQPSIQPQAQQFHQ 290

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 767903378  1459 -PPQQGAQPPHQVQMPLYNFPQSPPAQYSPMHNMGLLPMHPLQIPAPSWPIHGPVI 1513
Cdd:pfam09770  291 qPPPVPVQPTQILQNPNRLSAARVGYPQNPQPGVQPAPAHQAHRQQGSFGRQAPII 346
PHA03377 PHA03377
EBNA-3C; Provisional
 1393-1593 1.21e-05

EBNA-3C; Provisional


Pssm-ID: 177614 [Multi-domain]  Cd Length: 1000  Bit Score: 50.44  E-value: 1.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903378 1393 RNLVNAQQVAGSAQQQGDQSIRTRQS---SECSESPSYSPQPQPFPQNSSQSAAITQPSSQPgSQPKLGPPQ-------- 1461
Cdd:PHA03377  657 RDGSGIQQEPSSRRQPATQSTPPRPSwlpSVFVLPSVDAGRAQPSEESHLSSMSPTQPISHE-EQPRYEDPDdpldlslh 735

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903378 1462 --QGAQPPHQVQMPLYNFPQSPPAQYS------------------PMHNM------------GLLPMHPLQ----IPAPS 1505
Cdd:PHA03377  736 pdQAPPPSHQAPYSGHEEPQAQQAPYPgyweprppqapylgyqepQAQGVqvssypgyagpwGLRAQHPRYrhswAYWSQ 815

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903378 1506 WPIHGPVI--------HSAPGSAPSNIGLNDPSIIFaqPAARPVAIPNTSHDGHWPRTVAPNSLVNSGAVGNSEPGFRGL 1577
Cdd:PHA03377  816 YPGHGHPQgpwaprppHLPPQWDGSAGHGQDQVSQF--PHLQSETGPPRLQLSQVPQLPYSQTLVSSSAPSWSSPQPRAP 893

                         250
                  ....*....|....*.
gi 767903378 1578 TPPIPwEHAPRPHFPL 1593
Cdd:PHA03377  894 IRPIP-TRFPPPPMPL 908
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 1415-1633 2.20e-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: 49.38  E-value: 2.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903378  1415 TRQSSECSESPSyspqpqPFPQNSSQSAA-ITQPSSQPGSQPKlGPPQQGAQPPHQVQMPLYNFPQSPPaqyspmhnmgl 1493
Cdd:pfam03154  301 TPQSSQSQVPPG------PSPAAPGQSQQrIHTPPSQSQLQSQ-QPPREQPLPPAPLSMPHIKPPPTTP----------- 362

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903378  1494 LPmhplQIPAPSWPIHGP-VIHSAPGSAPSNigLNDPsiifaqPAARPVAIPNTSH--DGHWPrtvaPNSLVNSGAVGNS 1570
Cdd:pfam03154  363 IP----QLPNPQSHKHPPhLSGPSPFQMNSN--LPPP------PALKPLSSLSTHHppSAHPP----PLQLMPQSQQLPP 426

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767903378  1571 EPGF-RGLT-----PPIPWEHAPRPHFPLVPASWPYGLHqNFMHQGNARFQPNKPFYTQAGLPMHSNQP 1633
Cdd:pfam03154  427 PPAQpPVLTqsqslPPPAASHPPTSGLHQVPSQSPFPQH-PFVPGGPPPITPPSGPPTSTSSAMPGIQP 494
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
 1404-1523 3.30e-05

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


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 46.18  E-value: 3.30e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903378  1404 SAQQQGDQSIRTRQSSECSESPSYSPQPQPFPQNSSQSAaitQPSSQPGSQPKLGPPQQGA--QPPHQvqmPLYNFPQSP 1481
Cdd:pfam15240   15 SAQSSSEDVSQEDSPSLISEEEGQSQQGGQGPQGPPPGG---FPPQPPASDDPPGPPPPGGpqQPPPQ---GGKQKPQGP 88

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 767903378  1482 PAQYSPMHNMGLLPMHPLQI-------PAPSWPIHGPVIHSAPGSAPSN 1523
Cdd:pfam15240   89 PPQGGPRPPPGKPQGPPPQGgnqqqgpPPPGKPQGPPPQGGGPPPQGGN 137
PHA03247 PHA03247
large tegument protein UL36; Provisional
 1403-1566 4.84e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.40  E-value: 4.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903378 1403 GSAQQQGDQSIR--TRQSSECSESPSYSPQ---PQPFPQNSSQSAAITQPSSQPGSQPKlgPPQQGAQPPHQVQMPLYNF 1477
Cdd:PHA03247 2854 GSVAPGGDVRRRppSRSPAAKPAAPARPPVrrlARPAVSRSTESFALPPDQPERPPQPQ--APPPPQPQPQPPPPPQPQP 2931

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903378 1478 PQSPPAQYSPmhnmgllPMHPLQIPAPSWPIHGPVI-----HSAPGSAPSniglndPSIIFAQPA-ARPVAIPNTShdgh 1551
Cdd:PHA03247 2932 PPPPPPRPQP-------PLAPTTDPAGAGEPSGAVPqpwlgALVPGRVAV------PRFRVPQPApSREAPASSTP---- 2994

                         170
                  ....*....|....*
gi 767903378 1552 wPRTVAPNSLVNSGA 1566
Cdd:PHA03247 2995 -PLTGHSLSRVSSWA 3008
KLF3_N cd21577
N-terminal domain of Kruppel-like factor 3; Kruppel-like factor 3 (KLF3; also called ...
 1410-1565 7.44e-05

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


Pssm-ID: 410554 [Multi-domain]  Cd Length: 214  Bit Score: 45.80  E-value: 7.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903378 1410 DQSIRTRQSSECSESPSYSPQPQPFPQNSSQSaaitqPSSQPGSQPKLGPPQQgaQPPhqvqmplynfpqSPPAQYSPMh 1489
Cdd:cd21577    23 DLSLSKRSSPPSSSSSSSSSSSSSSSPSSRAS-----PPSPYSKSSPPSPPQQ--RPL------------SPPLSLPPP- 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767903378 1490 nMGLLPMHPLQIPAPSWPIHGPVIHSAPGSAPSNIGLndpSIIfaqpaarpVAIPNTSHDGHWPRTVAPNSLVNSG 1565
Cdd:cd21577    83 -VAPPPLSPGSVPGGLPVISPVMVQPVPVLYPPHLHQ---PIM--------VSSSPPPDDDHHHHKASSMKPSELG 146
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 1406-1511 1.32e-04

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 47.00  E-value: 1.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903378 1406 QQQGDQSIRTRQSSECSESPSYSPQPQPFPQNS-SQSAAITQPSSQPGSQPKLGPPQQGAQPPHQVQMPL--------YN 1476
Cdd:PRK10263  752 VQQPQQPVAPQQQYQQPQQPVAPQPQYQQPQQPvAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQqpvapqpqYQ 831

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 767903378 1477 FPQSPPAQySPMHNMgllpMHPLQI-PAPSWPIHGP 1511
Cdd:PRK10263  832 QPQQPVAP-QPQDTL----LHPLLMrNGDSRPLHKP 862
PHA03378 PHA03378
EBNA-3B; Provisional
 1430-1641 2.47e-04

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 45.83  E-value: 2.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903378 1430 QPQPFPQNSSQSAAITQPSSQPGSQPKLGPPQQGAQPPHQVQMPLYNFPQSPPAQYSPmhnmglLPMHPLQI-PAPSWPI 1508
Cdd:PHA03378  573 QIQPLTSPTTSQLASSAPSYAQTPWPVPHPSQTPEPPTTQSHIPETSAPRQWPMPLRP------IPMRPLRMqPITFNVL 646

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903378 1509 HGPVIHSAPGSAPSNIGLNdpsiiFAQPAARPVAIPNTSHDGHWPRTVAPnslvnsgavGNSEPGFRGLTPPIPWEHAP- 1587
Cdd:PHA03378  647 VFPTPHQPPQVEITPYKPT-----WTQIGHIPYQPSPTGANTMLPIQWAP---------GTMQPPPRAPTPMRPPAAPPg 712

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767903378 1588 ---RPHFPLVPASWPYGLHQNFMHQGNA--RFQPNKPFYTQAGLPMHSNQPILLSQGYP 1641
Cdd:PHA03378  713 raqRPAAATGRARPPAAAPGRARPPAAApgRARPPAAAPGRARPPAAAPGRARPPAAAP 771
PTZ00368 PTZ00368
universal minicircle sequence binding protein (UMSBP); Provisional
 1280-1375 3.05e-04

universal minicircle sequence binding protein (UMSBP); Provisional


Pssm-ID: 173561 [Multi-domain]  Cd Length: 148  Bit Score: 42.87  E-value: 3.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903378 1280 SRVLTDGELAPNDRCCRVCGKIGHYMKDCPKRKssllfrlKKKDSEEEKEGNEEEKDSRDVLDPRDL------------- 1346
Cdd:PTZ00368   40 SRECPSAPGGRGERSCYNCGKTGHLSRECPEAP-------PGSGPRSCYNCGQTGHISRECPNRAKGgaarracyncgge 112

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 767903378 1347 -HDTRD----FRDPRDLR-CFICGDAGHVRRECPE 1375
Cdd:PTZ00368  113 gHISRDcpnaGKRPGGDKtCYNCGQTGHLSRDCPD 147
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
 1429-1507 3.09e-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: 43.24  E-value: 3.09e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903378   1429 PQPQPFPQNSSQSAAITQPSSQPgSQPKLGPPQQGAQP--PHQVQMPLYNFPQSPPAQysPMHNMGLLPMHPLQIPAPSW 1506
Cdd:smart00818   77 PGQHSMTPTQHHQPNLPQPAQQP-FQPQPLQPPQPQQPmqPQPPVHPIPPLPPQPPLP--PMFPMQPLPPLLPDLPLEAW 153


                    .
gi 767903378   1507 P 1507
Cdd:smart00818  154 P 154
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 1422-1589 3.54e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 45.55  E-value: 3.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903378 1422 SESPSYSPQPQPFPQnSSQSAAiTQPSSQPGSQPKLGPPQQGAQPPHQVQMPLYN-FPQSPPAQYSPMHNMGLLPMHPLQ 1500
Cdd:PHA03307  105 SPTPPGPSSPDPPPP-TPPPAS-PPPSPAPDLSEMLRPVGSPGPPPAASPPAAGAsPAAVASDAASSRQAALPLSSPEET 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903378 1501 IPAPSWPIHGPVIHSAPGSAPSniGLNDPSIIFAQPAARPVAIPNTSHDGHWPRTVAPNSLVNSGAVGNSEPGFRGLTPP 1580
Cdd:PHA03307  183 ARAPSSPPAEPPPSTPPAAASP--RPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRP 260


                  ....*....
gi 767903378 1581 IPWEHAPRP 1589
Cdd:PHA03307  261 APITLPTRI 269
rplD PRK14907
50S ribosomal protein L4; Provisional
 97-199 4.15e-04

50S ribosomal protein L4; Provisional


Pssm-ID: 184900 [Multi-domain]  Cd Length: 295  Bit Score: 44.17  E-value: 4.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903378   97 KAKKFPNSPVKAEKATISQAKSEKATSLQAKAEKSPKSPNSVKAEKASSYQMKSEKVPSSPAEAEKGPSLLLKDMRQKTE 176
Cdd:PRK14907   19 AAKKATTSKETAKTKKTAKTTSTKAAKKAAKVKKTKSVKTTTKKVTVKFEKTESVKKESVAKKTVKKEAVSAEVFEASNK 98

                          90       100
                  ....*....|....*....|...
gi 767903378  177 LQQIGKKIPSSFTSVDKVNIEAV 199
Cdd:PRK14907   99 LFKNTSKLPKKLFASEKIYSQAI 121
PTZ00368 PTZ00368
universal minicircle sequence binding protein (UMSBP); Provisional
 1280-1376 2.52e-03

universal minicircle sequence binding protein (UMSBP); Provisional


Pssm-ID: 173561 [Multi-domain]  Cd Length: 148  Bit Score: 40.18  E-value: 2.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767903378 1280 SRVLTDGELAP--NDRCCRVCGKIGHYMKDCPKRKSSllfrlkkkdseeekegneeekdsrdvldprdlhdtrdfrdPRD 1357
Cdd:PTZ00368   13 SRECPNSAPAGaaKARPCYKCGEPGHLSRECPSAPGG----------------------------------------RGE 52

                          90
                  ....*....|....*....
gi 767903378 1358 LRCFICGDAGHVRRECPEV 1376
Cdd:PTZ00368   53 RSCYNCGKTGHLSRECPEA 71
ZnF_C2HC smart00343
zinc finger;
1294-1310 8.99e-03

zinc finger;


Pssm-ID: 197667 [Multi-domain]  Cd Length: 17  Bit Score: 35.11  E-value: 8.99e-03
                            10
                    ....*....|....*..
gi 767903378   1294 CCRVCGKIGHYMKDCPK 1310
Cdd:smart00343    1 KCYNCGKEGHIARDCPS 17
 
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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