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Conserved domains on  [gi|2462507008|ref|XP_054191532|]
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terminal uridylyltransferase 4 isoform X46 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NT_PAP_TUTase cd05402
Nucleotidyltransferase (NT) domain of poly(A) polymerases and terminal uridylyl transferases; ...
 231-349 9.69e-39

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: 139.61  E-value: 9.69e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507008 231 NREQILIGLEKFIQKEYdEKARLCLFGSSKNGFGFRDSDLDICMTLEGHenaeKLNCKEIIENLAKILKRHPGLRNILPI 310
Cdd:cd05402     1 KREEVLDRLQELIKEWF-PGAKLYPFGSYVTGLGLPGSDIDLCLLGPNH----RVDREDFLRKLAKLLKKSGEVVEVEPI 75

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2462507008 311 TTAKVPIVKFEHRRSGLEGDISLYNTLAQHNTRMLATYA 349
Cdd:cd05402    76 INARVPIIKFVDKPTGIEVDISFNNLNGIRNTKLLRAYV 114
TRF4 super family cl34961
DNA polymerase sigma [Replication, recombination and repair];
167-521 1.30e-37

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: 147.61  E-value: 1.30e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507008 167 SGKPPTIVCSI-CKKDGHSKND--CPEDFRKIDLKPLPP--MTNRFREILDLVCKRC---FDELSPPCSEQHNREQILIG 238
Cdd:COG5260     5 SKLFISLNSSSeEEFETIMEQKerRPLDAKKVSIQELLElsIDSVFNEESDELTSELlefYDYIAPSDEELKRRKALLEK 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507008 239 LEKFIQKEYDEkARLCLFGSSKNGFGFRDSDLDICMTLEGHENAEKLNCKEiienLAKILKRHPGLRNILPITTAKVPIV 318
Cdd:COG5260    85 LRTLLKKEFPD-ADLKVFGSTETGLALPKSDIDLCIISDPRGYKETRNAGS----LASHLFKKNLAKEVVVVSTARVPII 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507008 319 KFEHRRSGLEGDISLYNTLAQHNTRMLATYAAIDPRVQYLGYTMKVFAKRCDIGDASRGSLSSYAYILMVLYFLQQRKPP 398
Cdd:COG5260   160 KLVDPQSGLHCDISFNNTNGIVNAKLIRSYLKEDPRLRPLVLIIKHWLKRRALNDVATGTLSSYTISCMVLSFLQMHPPF 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507008 399 viPVLQEIFDGKQIPQRMVDGWNAFFFDKTEelkkrlpslgknteslgelwlgllrFYTEEFDFKEYVISIRQ-KKLLTT 477
Cdd:COG5260   240 --LFFDNGLLSPLKYNKNIDNLGVLFDDFFE-------------------------LYGKSFNYSLVVLSINSgDFYLPK 292

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 2462507008 478 FEKQW--TSKC--IAIEDPF-DLNHNLGAgVSRKMtNFIMKAFINGRKL 521
Cdd:COG5260   293 YEKGWlkPSKPnsLSIQDPGtDRNNDISA-VSFNI-KDIKAAFIRAFEL 339
Atrophin-1 super family cl38111
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 664-853 9.12e-09

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are 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: 59.40  E-value: 9.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507008 664 SAQQQGDQsirTRQSSECSESPSySPQPQPFPQNSSQSAAITQPSSQPGSQPKLGPPQqgAQPPHQVQMPL--------- 734
Cdd:pfam03154 161 SAQQQILQ---TQPPVLQAQSGA-ASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPAT--SQPPNQTQSTAaphtliqqt 234

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507008 735 -YNFPQSPPAQYSPMHNMGlLPMHPLQIPAPSWP---IHGPVihsAPGSAPSNIGlndPSIIFAQPAARPVAIPNTSHDG 810
Cdd:pfam03154 235 pTLHPQRLPSPHPPLQPMT-QPPPPSQVSPQPLPqpsLHGQM---PPMPHSLQTG---PSHMQHPVPPQPFPLTPQSSQS 307

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2462507008 811 HWPRTVAPNSLVNSGAVGNSEPGFRGLTPPIPWEHAPRPHFPL 853
Cdd:pfam03154 308 QVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPAPL 350
PTZ00368 super family cl31762
universal minicircle sequence binding protein (UMSBP); Provisional
 540-635 8.62e-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: 40.56  E-value: 8.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507008 540 SRVLTDGELAPNDRCCRVCGKIGHYMKDCPKRKssllfrlKKKDSEEEKEGNEEEKDSRDVLDPRDL------------- 606
Cdd:PTZ00368   40 SRECPSAPGGRGERSCYNCGKTGHLSRECPEAP-------PGSGPRSCYNCGQTGHISRECPNRAKGgaarracyncgge 112

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2462507008 607 -HDTRD----FRDPRDLR-CFICGDAGHVRRECPE 635
Cdd:PTZ00368  113 gHISRDcpnaGKRPGGDKtCYNCGQTGHLSRDCPD 147
 
Name Accession Description Interval E-value
NT_PAP_TUTase cd05402
Nucleotidyltransferase (NT) domain of poly(A) polymerases and terminal uridylyl transferases; ...
 231-349 9.69e-39

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: 139.61  E-value: 9.69e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507008 231 NREQILIGLEKFIQKEYdEKARLCLFGSSKNGFGFRDSDLDICMTLEGHenaeKLNCKEIIENLAKILKRHPGLRNILPI 310
Cdd:cd05402     1 KREEVLDRLQELIKEWF-PGAKLYPFGSYVTGLGLPGSDIDLCLLGPNH----RVDREDFLRKLAKLLKKSGEVVEVEPI 75

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2462507008 311 TTAKVPIVKFEHRRSGLEGDISLYNTLAQHNTRMLATYA 349
Cdd:cd05402    76 INARVPIIKFVDKPTGIEVDISFNNLNGIRNTKLLRAYV 114
TRF4 COG5260
DNA polymerase sigma [Replication, recombination and repair];
167-521 1.30e-37

DNA polymerase sigma [Replication, recombination and repair];


Pssm-ID: 227585 [Multi-domain]  Cd Length: 482  Bit Score: 147.61  E-value: 1.30e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507008 167 SGKPPTIVCSI-CKKDGHSKND--CPEDFRKIDLKPLPP--MTNRFREILDLVCKRC---FDELSPPCSEQHNREQILIG 238
Cdd:COG5260     5 SKLFISLNSSSeEEFETIMEQKerRPLDAKKVSIQELLElsIDSVFNEESDELTSELlefYDYIAPSDEELKRRKALLEK 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507008 239 LEKFIQKEYDEkARLCLFGSSKNGFGFRDSDLDICMTLEGHENAEKLNCKEiienLAKILKRHPGLRNILPITTAKVPIV 318
Cdd:COG5260    85 LRTLLKKEFPD-ADLKVFGSTETGLALPKSDIDLCIISDPRGYKETRNAGS----LASHLFKKNLAKEVVVVSTARVPII 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507008 319 KFEHRRSGLEGDISLYNTLAQHNTRMLATYAAIDPRVQYLGYTMKVFAKRCDIGDASRGSLSSYAYILMVLYFLQQRKPP 398
Cdd:COG5260   160 KLVDPQSGLHCDISFNNTNGIVNAKLIRSYLKEDPRLRPLVLIIKHWLKRRALNDVATGTLSSYTISCMVLSFLQMHPPF 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507008 399 viPVLQEIFDGKQIPQRMVDGWNAFFFDKTEelkkrlpslgknteslgelwlgllrFYTEEFDFKEYVISIRQ-KKLLTT 477
Cdd:COG5260   240 --LFFDNGLLSPLKYNKNIDNLGVLFDDFFE-------------------------LYGKSFNYSLVVLSINSgDFYLPK 292

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 2462507008 478 FEKQW--TSKC--IAIEDPF-DLNHNLGAgVSRKMtNFIMKAFINGRKL 521
Cdd:COG5260   293 YEKGWlkPSKPnsLSIQDPGtDRNNDISA-VSFNI-KDIKAAFIRAFEL 339
PAP_assoc pfam03828
Cid1 family poly A polymerase; This domain is found in poly(A) polymerases and has been shown ...
 444-497 1.26e-17

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: 77.61  E-value: 1.26e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507008 444 SLGELWLGLLRFYTEEFDFKEYVISIRQKKLLTTFEKQWT------SKCIAIEDPFDLNH 497
Cdd:pfam03828   1 SLGELLIGFFEYYGREFDYENVVISIRTGGILSKKEKGWLrnegrrPFLLCIEDPFDLDN 60
NTP_transf_2 pfam01909
Nucleotidyltransferase domain; Members of this family belong to a large family of ...
 239-324 2.56e-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: 2.56e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507008 239 LEKFIQ--KEYDEKARLCLFGSSKNGFGFRDSDLDICMTLEGHENAE-KLNCKEIIENLAKILKRHPGLRNILPITTAKV 315
Cdd:pfam01909   1 LRKLREilKELFPVAEVVLFGSYARGTALPGSDIDLLVVFPEPVEEErLLKLAKIIKELEELLGLEVDLVTREKIEFPLV 80


                  ....*....
gi 2462507008 316 PIVKFEHRR 324
Cdd:pfam01909  81 KIDILEERI 89
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 664-853 9.12e-09

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are 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: 59.40  E-value: 9.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507008 664 SAQQQGDQsirTRQSSECSESPSySPQPQPFPQNSSQSAAITQPSSQPGSQPKLGPPQqgAQPPHQVQMPL--------- 734
Cdd:pfam03154 161 SAQQQILQ---TQPPVLQAQSGA-ASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPAT--SQPPNQTQSTAaphtliqqt 234

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507008 735 -YNFPQSPPAQYSPMHNMGlLPMHPLQIPAPSWP---IHGPVihsAPGSAPSNIGlndPSIIFAQPAARPVAIPNTSHDG 810
Cdd:pfam03154 235 pTLHPQRLPSPHPPLQPMT-QPPPPSQVSPQPLPqpsLHGQM---PPMPHSLQTG---PSHMQHPVPPQPFPLTPQSSQS 307

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2462507008 811 HWPRTVAPNSLVNSGAVGNSEPGFRGLTPPIPWEHAPRPHFPL 853
Cdd:pfam03154 308 QVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPAPL 350
PHA03247 PHA03247
large tegument protein UL36; Provisional
 666-852 6.74e-08

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 56.87  E-value: 6.74e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507008  666 QQQGDQSIRTRQSSECSESPSYSPQPQPFPQNSSQSAAITQPSSQPGSQPKLGPPQQGAQPPHQVQMPLYNFPQSPPAqy 745
Cdd:PHA03247  2908 PPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPS-- 2985

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507008  746 spmhnmgllpmhplqIPAPSWPIHGPVIHSAPG--SAPSNIGLNDpsiifaQPAARPVAIPNTSHDGHWPRTVAPNSLVN 823
Cdd:PHA03247  2986 ---------------REAPASSTPPLTGHSLSRvsSWASSLALHE------ETDPPPVSLKQTLWPPDDTEDSDADSLFD 3044

                          170       180       190
                   ....*....|....*....|....*....|.
gi 2462507008  824 SGAVGNSEPGFRGLTPP--IPWEHAPRPHFP 852
Cdd:PHA03247  3045 SDSERSDLEALDPLPPEphDPFAHEPDPATP 3075
KLF3_N cd21577
N-terminal domain of Kruppel-like factor 3; Kruppel-like factor 3 (KLF3; also called ...
 670-825 2.21e-04

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


Pssm-ID: 410554 [Multi-domain]  Cd Length: 214  Bit Score: 43.49  E-value: 2.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507008 670 DQSIRTRQSSECSESPSYSPQPQPFPQNSSQSaaitqPSSQPGSQPKLGPPQQgaQPPhqvqmplynfpqSPPAQYSPMh 749
Cdd:cd21577    23 DLSLSKRSSPPSSSSSSSSSSSSSSSPSSRAS-----PPSPYSKSSPPSPPQQ--RPL------------SPPLSLPPP- 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462507008 750 nMGLLPMHPLQIPAPSWPIHGPVIHSAPGSAPSNIGLndpSIIfaqpaarpVAIPNTSHDGHWPRTVAPNSLVNSG 825
Cdd:cd21577    83 -VAPPPLSPGSVPGGLPVISPVMVQPVPVLYPPHLHQ---PIM--------VSSSPPPDDDHHHHKASSMKPSELG 146
PTZ00368 PTZ00368
universal minicircle sequence binding protein (UMSBP); Provisional
 540-635 8.62e-04

universal minicircle sequence binding protein (UMSBP); Provisional


Pssm-ID: 173561 [Multi-domain]  Cd Length: 148  Bit Score: 40.56  E-value: 8.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507008 540 SRVLTDGELAPNDRCCRVCGKIGHYMKDCPKRKssllfrlKKKDSEEEKEGNEEEKDSRDVLDPRDL------------- 606
Cdd:PTZ00368   40 SRECPSAPGGRGERSCYNCGKTGHLSRECPEAP-------PGSGPRSCYNCGQTGHISRECPNRAKGgaarracyncgge 112

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2462507008 607 -HDTRD----FRDPRDLR-CFICGDAGHVRRECPE 635
Cdd:PTZ00368  113 gHISRDcpnaGKRPGGDKtCYNCGQTGHLSRDCPD 147
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
 689-767 3.31e-03

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: 39.39  E-value: 3.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507008  689 PQPQPFPQNSSQSAAITQPSSQPgSQPKLGPPQQGAQP--PHQVQMPLYNFPQSPPAQysPMHNMGLLPMHPLQIPAPSW 766
Cdd:smart00818  77 PGQHSMTPTQHHQPNLPQPAQQP-FQPQPLQPPQPQQPmqPQPPVHPIPPLPPQPPLP--PMFPMQPLPPLLPDLPLEAW 153


                   .
gi 2462507008  767 P 767
Cdd:smart00818 154 P 154
ZnF_C2HC smart00343
zinc finger;
554-570 7.71e-03

zinc finger;


Pssm-ID: 197667 [Multi-domain]  Cd Length: 17  Bit Score: 34.73  E-value: 7.71e-03
                           10
                   ....*....|....*..
gi 2462507008  554 CCRVCGKIGHYMKDCPK 570
Cdd:smart00343   1 KCYNCGKEGHIARDCPS 17
 
Name Accession Description Interval E-value
NT_PAP_TUTase cd05402
Nucleotidyltransferase (NT) domain of poly(A) polymerases and terminal uridylyl transferases; ...
 231-349 9.69e-39

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: 139.61  E-value: 9.69e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507008 231 NREQILIGLEKFIQKEYdEKARLCLFGSSKNGFGFRDSDLDICMTLEGHenaeKLNCKEIIENLAKILKRHPGLRNILPI 310
Cdd:cd05402     1 KREEVLDRLQELIKEWF-PGAKLYPFGSYVTGLGLPGSDIDLCLLGPNH----RVDREDFLRKLAKLLKKSGEVVEVEPI 75

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2462507008 311 TTAKVPIVKFEHRRSGLEGDISLYNTLAQHNTRMLATYA 349
Cdd:cd05402    76 INARVPIIKFVDKPTGIEVDISFNNLNGIRNTKLLRAYV 114
TRF4 COG5260
DNA polymerase sigma [Replication, recombination and repair];
167-521 1.30e-37

DNA polymerase sigma [Replication, recombination and repair];


Pssm-ID: 227585 [Multi-domain]  Cd Length: 482  Bit Score: 147.61  E-value: 1.30e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507008 167 SGKPPTIVCSI-CKKDGHSKND--CPEDFRKIDLKPLPP--MTNRFREILDLVCKRC---FDELSPPCSEQHNREQILIG 238
Cdd:COG5260     5 SKLFISLNSSSeEEFETIMEQKerRPLDAKKVSIQELLElsIDSVFNEESDELTSELlefYDYIAPSDEELKRRKALLEK 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507008 239 LEKFIQKEYDEkARLCLFGSSKNGFGFRDSDLDICMTLEGHENAEKLNCKEiienLAKILKRHPGLRNILPITTAKVPIV 318
Cdd:COG5260    85 LRTLLKKEFPD-ADLKVFGSTETGLALPKSDIDLCIISDPRGYKETRNAGS----LASHLFKKNLAKEVVVVSTARVPII 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507008 319 KFEHRRSGLEGDISLYNTLAQHNTRMLATYAAIDPRVQYLGYTMKVFAKRCDIGDASRGSLSSYAYILMVLYFLQQRKPP 398
Cdd:COG5260   160 KLVDPQSGLHCDISFNNTNGIVNAKLIRSYLKEDPRLRPLVLIIKHWLKRRALNDVATGTLSSYTISCMVLSFLQMHPPF 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507008 399 viPVLQEIFDGKQIPQRMVDGWNAFFFDKTEelkkrlpslgknteslgelwlgllrFYTEEFDFKEYVISIRQ-KKLLTT 477
Cdd:COG5260   240 --LFFDNGLLSPLKYNKNIDNLGVLFDDFFE-------------------------LYGKSFNYSLVVLSINSgDFYLPK 292

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 2462507008 478 FEKQW--TSKC--IAIEDPF-DLNHNLGAgVSRKMtNFIMKAFINGRKL 521
Cdd:COG5260   293 YEKGWlkPSKPnsLSIQDPGtDRNNDISA-VSFNI-KDIKAAFIRAFEL 339
PAP_assoc pfam03828
Cid1 family poly A polymerase; This domain is found in poly(A) polymerases and has been shown ...
 444-497 1.26e-17

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: 77.61  E-value: 1.26e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507008 444 SLGELWLGLLRFYTEEFDFKEYVISIRQKKLLTTFEKQWT------SKCIAIEDPFDLNH 497
Cdd:pfam03828   1 SLGELLIGFFEYYGREFDYENVVISIRTGGILSKKEKGWLrnegrrPFLLCIEDPFDLDN 60
NTP_transf_2 pfam01909
Nucleotidyltransferase domain; Members of this family belong to a large family of ...
 239-324 2.56e-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: 2.56e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507008 239 LEKFIQ--KEYDEKARLCLFGSSKNGFGFRDSDLDICMTLEGHENAE-KLNCKEIIENLAKILKRHPGLRNILPITTAKV 315
Cdd:pfam01909   1 LRKLREilKELFPVAEVVLFGSYARGTALPGSDIDLLVVFPEPVEEErLLKLAKIIKELEELLGLEVDLVTREKIEFPLV 80


                  ....*....
gi 2462507008 316 PIVKFEHRR 324
Cdd:pfam01909  81 KIDILEERI 89
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 664-853 9.12e-09

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are 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: 59.40  E-value: 9.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507008 664 SAQQQGDQsirTRQSSECSESPSySPQPQPFPQNSSQSAAITQPSSQPGSQPKLGPPQqgAQPPHQVQMPL--------- 734
Cdd:pfam03154 161 SAQQQILQ---TQPPVLQAQSGA-ASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPAT--SQPPNQTQSTAaphtliqqt 234

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507008 735 -YNFPQSPPAQYSPMHNMGlLPMHPLQIPAPSWP---IHGPVihsAPGSAPSNIGlndPSIIFAQPAARPVAIPNTSHDG 810
Cdd:pfam03154 235 pTLHPQRLPSPHPPLQPMT-QPPPPSQVSPQPLPqpsLHGQM---PPMPHSLQTG---PSHMQHPVPPQPFPLTPQSSQS 307

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2462507008 811 HWPRTVAPNSLVNSGAVGNSEPGFRGLTPPIPWEHAPRPHFPL 853
Cdd:pfam03154 308 QVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPAPL 350
PHA03247 PHA03247
large tegument protein UL36; Provisional
 666-852 6.74e-08

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 56.87  E-value: 6.74e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507008  666 QQQGDQSIRTRQSSECSESPSYSPQPQPFPQNSSQSAAITQPSSQPGSQPKLGPPQQGAQPPHQVQMPLYNFPQSPPAqy 745
Cdd:PHA03247  2908 PPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPS-- 2985

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507008  746 spmhnmgllpmhplqIPAPSWPIHGPVIHSAPG--SAPSNIGLNDpsiifaQPAARPVAIPNTSHDGHWPRTVAPNSLVN 823
Cdd:PHA03247  2986 ---------------REAPASSTPPLTGHSLSRvsSWASSLALHE------ETDPPPVSLKQTLWPPDDTEDSDADSLFD 3044

                          170       180       190
                   ....*....|....*....|....*....|.
gi 2462507008  824 SGAVGNSEPGFRGLTPP--IPWEHAPRPHFP 852
Cdd:PHA03247  3045 SDSERSDLEALDPLPPEphDPFAHEPDPATP 3075
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 658-773 8.27e-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: 49.65  E-value: 8.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507008 658 AQQVAGSAQQ--QGDQSIRTRQSSECSESPSYSPQPQPFPQNS-----------------SQSAAITQPSSQPGSQPKLG 718
Cdd:pfam09770 211 AQQPAPAPAQppAAPPAQQAQQQQQFPPQIQQQQQPQQQPQQPqqhpgqghpvtilqrpqSPQPDPAQPSIQPQAQQFHQ 290

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462507008 719 -PPQQGAQPPHQVQMPLYNFPQSPPAQYSPMHNMGLLPMHPLQIPAPSWPIHGPVI 773
Cdd:pfam09770 291 qPPPVPVQPTQILQNPNRLSAARVGYPQNPQPGVQPAPAHQAHRQQGSFGRQAPII 346
SOBP pfam15279
Sine oculis-binding protein; SOBP is associated with syndromic and nonsyndromic intellectual ...
 683-806 3.12e-05

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: 47.12  E-value: 3.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507008 683 ESPSYSPQPQPFPQNSSQSAAITQPSSQPGSQPKLGPPQQGAQPPHQVQMPLYnFPQSPPAQYSPMHNM-GLLPMHPlqi 761
Cdd:pfam15279 191 EPSSMPPPFLRPPPSIPQPNSPLSNPMLPGIGPPPKPPRNLGPPSNPMHRPPF-SPHHPPPPPTPPGPPpGLPPPPP--- 266

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2462507008 762 papswPIHGPviHSAPGSAPSNIGLNDPSIIFAQPAARPVAIPNT 806
Cdd:pfam15279 267 -----RGFTP--PFGPPFPPVNMMPNPPEMNFGLPSLAPLVPPVT 304
PHA03377 PHA03377
EBNA-3C; Provisional
 653-853 6.49e-05

EBNA-3C; Provisional


Pssm-ID: 177614 [Multi-domain]  Cd Length: 1000  Bit Score: 46.97  E-value: 6.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507008  653 RNLVNAQQVAGSAQQQGDQSIRTRQS---SECSESPSYSPQPQPFPQNSSQSAAITQPSSQPgSQPKLGPPQ-------- 721
Cdd:PHA03377   657 RDGSGIQQEPSSRRQPATQSTPPRPSwlpSVFVLPSVDAGRAQPSEESHLSSMSPTQPISHE-EQPRYEDPDdpldlslh 735

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507008  722 --QGAQPPHQVQMPLYNFPQSPPAQYS------------------PMHNM------------GLLPMHPLQ----IPAPS 765
Cdd:PHA03377   736 pdQAPPPSHQAPYSGHEEPQAQQAPYPgyweprppqapylgyqepQAQGVqvssypgyagpwGLRAQHPRYrhswAYWSQ 815

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507008  766 WPIHGPVI--------HSAPGSAPSNIGLNDPSIIFaqPAARPVAIPNTSHDGHWPRTVAPNSLVNSGAVGNSEPGFRGL 837
Cdd:PHA03377   816 YPGHGHPQgpwaprppHLPPQWDGSAGHGQDQVSQF--PHLQSETGPPRLQLSQVPQLPYSQTLVSSSAPSWSSPQPRAP 893

                          250
                   ....*....|....*.
gi 2462507008  838 TPPIPwEHAPRPHFPL 853
Cdd:PHA03377   894 IRPIP-TRFPPPPMPL 908
PHA03247 PHA03247
large tegument protein UL36; Provisional
 663-826 1.16e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.08  E-value: 1.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507008  663 GSAQQQGDQSIR--TRQSSECSESPSYSPQ---PQPFPQNSSQSAAITQPSSQPGSQPKlgPPQQGAQPPHQVQMPLYNF 737
Cdd:PHA03247  2854 GSVAPGGDVRRRppSRSPAAKPAAPARPPVrrlARPAVSRSTESFALPPDQPERPPQPQ--APPPPQPQPQPPPPPQPQP 2931

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507008  738 PQSPPAQYSPmhnmgllPMHPLQIPAPSWPIHGPVI-----HSAPGSAPSniglndPSIIFAQPA-ARPVAIPNTShdgh 811
Cdd:PHA03247  2932 PPPPPPRPQP-------PLAPTTDPAGAGEPSGAVPqpwlgALVPGRVAV------PRFRVPQPApSREAPASSTP---- 2994

                          170
                   ....*....|....*
gi 2462507008  812 wPRTVAPNSLVNSGA 826
Cdd:PHA03247  2995 -PLTGHSLSRVSSWA 3008
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 675-859 1.20e-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: 45.91  E-value: 1.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507008 675 TRQSSECSESPSyspqpqPFPQNSSQSAA-ITQPSSQPGSQPKlGPPQQGAQPPHQVQMPLYNFPQSPP--------AQY 745
Cdd:pfam03154 301 TPQSSQSQVPPG------PSPAAPGQSQQrIHTPPSQSQLQSQ-QPPREQPLPPAPLSMPHIKPPPTTPipqlpnpqSHK 373

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507008 746 SPMHNMGLLPMH-PLQIPAPSW--PIHGPVIHSAPGSAPSNIGLNDPSIIFAQPAARPvaiPNTSHDGHWPRTVAPNSLV 822
Cdd:pfam03154 374 HPPHLSGPSPFQmNSNLPPPPAlkPLSSLSTHHPPSAHPPPLQLMPQSQQLPPPPAQP---PVLTQSQSLPPPAASHPPT 450

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2462507008 823 NSGAVGNSEPGFrgltPPIPWEHAPRPhfPLVPASWP 859
Cdd:pfam03154 451 SGLHQVPSQSPF----PQHPFVPGGPP--PITPPSGP 481
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 666-771 1.28e-04

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 45.85  E-value: 1.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507008  666 QQQGDQSIRTRQSSECSESPSYSPQPQPFPQNS-SQSAAITQPSSQPGSQPKLGPPQQGAQPPHQVQMPL--------YN 736
Cdd:PRK10263   752 VQQPQQPVAPQQQYQQPQQPVAPQPQYQQPQQPvAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQqpvapqpqYQ 831

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2462507008  737 FPQSPPAQySPMHNMgllpMHPLQI-PAPSWPIHGP 771
Cdd:PRK10263   832 QPQQPVAP-QPQDTL----LHPLLMrNGDSRPLHKP 862
KLF3_N cd21577
N-terminal domain of Kruppel-like factor 3; Kruppel-like factor 3 (KLF3; also called ...
 670-825 2.21e-04

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


Pssm-ID: 410554 [Multi-domain]  Cd Length: 214  Bit Score: 43.49  E-value: 2.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507008 670 DQSIRTRQSSECSESPSYSPQPQPFPQNSSQSaaitqPSSQPGSQPKLGPPQQgaQPPhqvqmplynfpqSPPAQYSPMh 749
Cdd:cd21577    23 DLSLSKRSSPPSSSSSSSSSSSSSSSPSSRAS-----PPSPYSKSSPPSPPQQ--RPL------------SPPLSLPPP- 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462507008 750 nMGLLPMHPLQIPAPSWPIHGPVIHSAPGSAPSNIGLndpSIIfaqpaarpVAIPNTSHDGHWPRTVAPNSLVNSG 825
Cdd:cd21577    83 -VAPPPLSPGSVPGGLPVISPVMVQPVPVLYPPHLHQ---PIM--------VSSSPPPDDDHHHHKASSMKPSELG 146
Glutenin_hmw pfam03157
High molecular weight glutenin subunit; Members of this family include high molecular weight ...
 660-900 2.21e-04

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


Pssm-ID: 367362 [Multi-domain]  Cd Length: 786  Bit Score: 44.94  E-value: 2.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507008 660 QVAGSAQQ--QGDQSIRTRQSSECSE-SPSYSPQPQPFPQNSSQSAAITQP--------SSQPGSQPKLGPPQQGAQP-- 726
Cdd:pfam03157 171 QQSGQRQQpgQGQQLRQGQQGQQSGQgQPGYYPTSSQQPGQLQQTGQGQQGqqpergqqGQQPGQGQQPGQGQQGQQPgq 250

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507008 727 ---PHQVQMPLYNFPQSPPAQY--SPMHNMGLLPMHPLQiPAPSWPIHGPVIHSAPGSAPSNIGLNDPSIIFAQPAARPV 801
Cdd:pfam03157 251 pqqLGQGQQGYYPISPQQPRQWqqSGQGQQGYYPTSLQQ-PGQGQSGYYPTSQQQAGQLQQEQQLGQEQQDQQPGQGRQG 329

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507008 802 AIPNTSHDGHWPRTvapnslvnSGAVGNSEPGFRGLTPPIPWEHAPRpHFPLVPASWPYGLHQNFMHQGNARFQPNkpfy 881
Cdd:pfam03157 330 QQPGQGQQGQQPAQ--------GQQPGQGQPGYYPTSPQQPGQGQPG-YYPTSQQQPQQGQQPEQGQQGQQQGQGQ---- 396

                         250
                  ....*....|....*....
gi 2462507008 882 tQAGLPMHSNQPILLSQGY 900
Cdd:pfam03157 397 -QGQQPGQGQQPGQGQPGY 414
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 682-849 6.86e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 43.62  E-value: 6.86e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507008  682 SESPSYSPQPQPFPQnSSQSAAiTQPSSQPGSQPKLGPPQQGAQPPHQVQMPLYN-FPQSPPAQYSPMHNMGLLPMHPLQ 760
Cdd:PHA03307   105 SPTPPGPSSPDPPPP-TPPPAS-PPPSPAPDLSEMLRPVGSPGPPPAASPPAAGAsPAAVASDAASSRQAALPLSSPEET 182

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507008  761 IPAPSWPIHGPVIHSAPGSAPSniGLNDPSIIFAQPAARPVAIPNTSHDGHWPRTVAPNSLVNSGAVGNSEPGFRGLTPP 840
Cdd:PHA03307   183 ARAPSSPPAEPPPSTPPAAASP--RPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRP 260


                   ....*....
gi 2462507008  841 IPWEHAPRP 849
Cdd:PHA03307   261 APITLPTRI 269
PHA03378 PHA03378
EBNA-3B; Provisional
 690-901 7.09e-04

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 43.52  E-value: 7.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507008 690 QPQPFPQNSSQSAAITQPSSQPGSQPKLGPPQQGAQPPHQVQMPLYNFPQSPPAQYSPmhnmglLPMHPLQI-PAPSWPI 768
Cdd:PHA03378  573 QIQPLTSPTTSQLASSAPSYAQTPWPVPHPSQTPEPPTTQSHIPETSAPRQWPMPLRP------IPMRPLRMqPITFNVL 646

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507008 769 HGPVIHSAPGSAPSNIGLNdpsiiFAQPAARPVAIPNTSHDGHWPRTVAPnslvnsgavGNSEPGFRGLTPPIPWEHAP- 847
Cdd:PHA03378  647 VFPTPHQPPQVEITPYKPT-----WTQIGHIPYQPSPTGANTMLPIQWAP---------GTMQPPPRAPTPMRPPAAPPg 712

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462507008 848 ---RPHFPLVPASWPYGLHQNFMHQGNA--RFQPNKPFYTQAGLPMHSNQPILLSQGYP 901
Cdd:PHA03378  713 raqRPAAATGRARPPAAAPGRARPPAAApgRARPPAAAPGRARPPAAAPGRARPPAAAP 771
PHA03378 PHA03378
EBNA-3B; Provisional
 659-849 8.41e-04

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 43.13  E-value: 8.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507008 659 QQVAGSAQQQGDQSIRTRQSSECSESPSYSPQPQPFPqnssqsAAITQPSSQPGSQPklgPPQqgaQPPHQVQMplynFP 738
Cdd:PHA03378  748 AAAPGRARPPAAAPGRARPPAAAPGAPTPQPPPQAPP------APQQRPRGAPTPQP---PPQ---AGPTSMQL----MP 811

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507008 739 QSPPAQYSPMHNM-------GLLPMHP-LQIPAPSWPIHGPVIHSAPGSAPSNIGLNDPsiIFAQPAARPVAIPNtshDG 810
Cdd:PHA03378  812 RAAPGQQGPTKQIlrqlltgGVKRGRPsLKKPAALERQAAAGPTPSPGSGTSDKIVQAP--VFYPPVLQPIQVMR---QL 886

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2462507008 811 HWPRTVAPNSLVNSgavGNSEPGFRGLTPPIPWEHAPRP 849
Cdd:PHA03378  887 GSVRAAAASTVTQA---PTEYTGERRGVGPMHPTDIPPS 922
PTZ00368 PTZ00368
universal minicircle sequence binding protein (UMSBP); Provisional
 540-635 8.62e-04

universal minicircle sequence binding protein (UMSBP); Provisional


Pssm-ID: 173561 [Multi-domain]  Cd Length: 148  Bit Score: 40.56  E-value: 8.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507008 540 SRVLTDGELAPNDRCCRVCGKIGHYMKDCPKRKssllfrlKKKDSEEEKEGNEEEKDSRDVLDPRDL------------- 606
Cdd:PTZ00368   40 SRECPSAPGGRGERSCYNCGKTGHLSRECPEAP-------PGSGPRSCYNCGQTGHISRECPNRAKGgaarracyncgge 112

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2462507008 607 -HDTRD----FRDPRDLR-CFICGDAGHVRRECPE 635
Cdd:PTZ00368  113 gHISRDcpnaGKRPGGDKtCYNCGQTGHLSRDCPD 147
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
 664-783 1.97e-03

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


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 40.02  E-value: 1.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507008 664 SAQQQGDQSIRTRQSSECSESPSYSPQPQPFPQNSSQSAaitQPSSQPGSQPKLGPPQQGA--QPPHQvqmPLYNFPQSP 741
Cdd:pfam15240  15 SAQSSSEDVSQEDSPSLISEEEGQSQQGGQGPQGPPPGG---FPPQPPASDDPPGPPPPGGpqQPPPQ---GGKQKPQGP 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2462507008 742 PAQYSPMHNMGLLPMHPLQI-------PAPSWPIHGPVIHSAPGSAPSN 783
Cdd:pfam15240  89 PPQGGPRPPPGKPQGPPPQGgnqqqgpPPPGKPQGPPPQGGGPPPQGGN 137
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
 689-767 3.31e-03

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: 39.39  E-value: 3.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507008  689 PQPQPFPQNSSQSAAITQPSSQPgSQPKLGPPQQGAQP--PHQVQMPLYNFPQSPPAQysPMHNMGLLPMHPLQIPAPSW 766
Cdd:smart00818  77 PGQHSMTPTQHHQPNLPQPAQQP-FQPQPLQPPQPQQPmqPQPPVHPIPPLPPQPPLP--PMFPMQPLPPLLPDLPLEAW 153


                   .
gi 2462507008  767 P 767
Cdd:smart00818 154 P 154
PRK14971 PRK14971
DNA polymerase III subunit gamma/tau;
654-772 4.15e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237874 [Multi-domain]  Cd Length: 614  Bit Score: 40.91  E-value: 4.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507008 654 NLVNAQQVAGSAQ-QQGDQSIRTRQSSECSESPSYSPQPQPFPQNSSQSAAITQPSSQPGSQPKLGPPQQGAQPPHQVQM 732
Cdd:PRK14971  358 QLAQLTQKGDDASgGRGPKQHIKPVFTQPAAAPQPSAAAAASPSPSQSSAAAQPSAPQSATQPAGTPPTVSVDPPAAVPV 437

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2462507008 733 PLynfPQSPPAQYSPMHNMGLLPMHPLQIPAPSWPIHGPV 772
Cdd:PRK14971  438 NP---PSTAPQAVRPAQFKEEKKIPVSKVSSLGPSTLRPI 474
PTZ00368 PTZ00368
universal minicircle sequence binding protein (UMSBP); Provisional
 540-636 6.21e-03

universal minicircle sequence binding protein (UMSBP); Provisional


Pssm-ID: 173561 [Multi-domain]  Cd Length: 148  Bit Score: 38.25  E-value: 6.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507008 540 SRVLTDGELAP--NDRCCRVCGKIGHYMKDCPKRKSSllfrlkkkdseeekegneeekdsrdvldprdlhdtrdfrdPRD 617
Cdd:PTZ00368   13 SRECPNSAPAGaaKARPCYKCGEPGHLSRECPSAPGG----------------------------------------RGE 52

                          90
                  ....*....|....*....
gi 2462507008 618 LRCFICGDAGHVRRECPEV 636
Cdd:PTZ00368   53 RSCYNCGKTGHLSRECPEA 71
ZnF_C2HC smart00343
zinc finger;
554-570 7.71e-03

zinc finger;


Pssm-ID: 197667 [Multi-domain]  Cd Length: 17  Bit Score: 34.73  E-value: 7.71e-03
                           10
                   ....*....|....*..
gi 2462507008  554 CCRVCGKIGHYMKDCPK 570
Cdd:smart00343   1 KCYNCGKEGHIARDCPS 17
TUTase pfam19088
TUTase nucleotidyltransferase domain; This nucleotidyltransferase domain is found in TUTase ...
 232-327 9.37e-03

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: 38.57  E-value: 9.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507008 232 REQILIGLEKFIQKEYDEKArLCLFGSSKNGFGFRDSDLDICMTLeghenAEKLNCKEIIENLAKILKRHPGLRNILPIT 311
Cdd:pfam19088 123 RQEIVTRMEKIIQQHLPDCS-LRLYGSCLTRFAFKTSDINIDVQF-----PSTMTQPDVLIQVLEILKNSESYSDVESDF 196

                          90
                  ....*....|....*.
gi 2462507008 312 TAKVPIVKFEHRRSGL 327
Cdd:pfam19088 197 HAKVPVVFCRDKQSGL 212
 
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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