|
Name |
Accession |
Description |
Interval |
E-value |
| R3H_encore_like |
cd02642 |
R3H domain of encore-like and DIP1-like proteins. Drosophila encore is involved in the ... |
163-224 |
6.19e-26 |
|
R3H domain of encore-like and DIP1-like proteins. Drosophila encore is involved in the germline exit after four mitotic divisions, by facilitating SCF-ubiquitin-proteasome-dependent proteolysis. Maize DBF1-interactor protein 1 (DIP1) containing an R3H domain is a potential regulator of DBF1 activity in stress responses. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner. :
Pssm-ID: 100071 Cd Length: 63 Bit Score: 101.14 E-value: 6.19e-26
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034630830 163 DRMILLKMEQEIIDFIADNNNHYKKFPQMSSYQRMLVHRVAAYFGLDHNVDQTG-KSVIINKT 224
Cdd:cd02642 1 DRLFVLKLEKDLLAFIKDSTRQSLELPPMNSYYRLLAHRVAQYYGLDHNVDNSGgKCVIVNKT 63
|
|
| SUZ |
pfam12752 |
SUZ domain; The SUZ domain is a conserved RNA-binding domain found in eukaryotes and enriched ... |
245-300 |
2.56e-13 |
|
SUZ domain; The SUZ domain is a conserved RNA-binding domain found in eukaryotes and enriched in positively charged amino acids. It was first characterized in the C.elegans protein Szy-20 where it has been shown to bind RNA and allow their localization to the centrosome. Warning- the domain has a compositionally biased character. :
Pssm-ID: 463689 [Multi-domain] Cd Length: 56 Bit Score: 65.04 E-value: 2.56e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034630830 245 ESQKRFILKRDNSSIDKEDNQQNRMHPFRDDRRSKSIEEREEEYQRVRERIFAHDS 300
Cdd:pfam12752 1 PPPKMKILRRPSSGSSSSSSAGSSGASSSSGSDSKTLEEREAEYAEARARIFGSSE 56
|
|
| PAT1 super family |
cl37801 |
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ... |
588-775 |
7.85e-04 |
|
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division. The actual alignment was detected with superfamily member pfam09770:
Pssm-ID: 401645 [Multi-domain] Cd Length: 846 Bit Score: 43.10 E-value: 7.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034630830 588 PPSGPVYPSSLmPQPAQQPSYVIASTG-----QQLPTGGFSGSGPPISQQVLQPPPSPqgfvQQPPPAQMPVYYYPSGQY 662
Cdd:pfam09770 166 APKKAAAPAPA-PQPAAQPASLPAPSRkmmslEEVEAAMRAQAKKPAQQPAPAPAQPP----AAPPAQQAQQQQQFPPQI 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034630830 663 PTSTTQQYRPMAPVQYNAQrsqqmpqaaqqaGYQPVLSGQQGFQGLIGVQQPPQSQNVINNQQGTPVQS---------VM 733
Cdd:pfam09770 241 QQQQQPQQQPQQPQQHPGQ------------GHPVTILQRPQSPQPDPAQPSIQPQAQQFHQQPPPVPVqptqilqnpNR 308
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1034630830 734 VSYPTMSSYQVPMTQGSQGLPQQSYQQPIMLPNQAGQGSLPA 775
Cdd:pfam09770 309 LSAARVGYPQNPQPGVQPAPAHQAHRQQGSFGRQAPIITHPQ 350
|
|
| PHA03247 super family |
cl33720 |
large tegument protein UL36; Provisional |
408-675 |
2.23e-03 |
|
large tegument protein UL36; Provisional The actual alignment was detected with superfamily member PHA03247:
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 41.85 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034630830 408 PPLQSTPLVSGVAAGSPGCVPYPENGIGGQVAPSSTSYILLPLEAATGIPPGSillnphtgqpfVNPDGTPAIYNPPTSQ 487
Cdd:PHA03247 2701 PPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGG-----------PARPARPPTTAGPPAP 2769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034630830 488 QPLRSAMVGQSQQQPPQQQPSPQPQQQVQPPQPQMAGPlvTQSVQGLQASSQSVQYPAVSFPPqhllPVSPTQhfpmrdd 567
Cdd:PHA03247 2770 APPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADP--PAAVLAPAAALPPAASPAGPLPP----PTSAQP------- 2836
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034630830 568 vatqfgqmtlsrqssgETPEPPSGPVyPSSLMPQPAQQPSYVIASTG--QQLPTGGFSGSGPPISQqVLQPPPSPQGFVQ 645
Cdd:PHA03247 2837 ----------------TAPPPPPGPP-PPSLPLGGSVAPGGDVRRRPpsRSPAAKPAAPARPPVRR-LARPAVSRSTESF 2898
|
250 260 270
....*....|....*....|....*....|.
gi 1034630830 646 -QPPPAQMPVYYYPSGQYPTSTTQQYRPMAP 675
Cdd:PHA03247 2899 aLPPDQPERPPQPQAPPPPQPQPQPPPPPQP 2929
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| R3H_encore_like |
cd02642 |
R3H domain of encore-like and DIP1-like proteins. Drosophila encore is involved in the ... |
163-224 |
6.19e-26 |
|
R3H domain of encore-like and DIP1-like proteins. Drosophila encore is involved in the germline exit after four mitotic divisions, by facilitating SCF-ubiquitin-proteasome-dependent proteolysis. Maize DBF1-interactor protein 1 (DIP1) containing an R3H domain is a potential regulator of DBF1 activity in stress responses. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner.
Pssm-ID: 100071 Cd Length: 63 Bit Score: 101.14 E-value: 6.19e-26
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034630830 163 DRMILLKMEQEIIDFIADNNNHYKKFPQMSSYQRMLVHRVAAYFGLDHNVDQTG-KSVIINKT 224
Cdd:cd02642 1 DRLFVLKLEKDLLAFIKDSTRQSLELPPMNSYYRLLAHRVAQYYGLDHNVDNSGgKCVIVNKT 63
|
|
| R3H |
smart00393 |
Putative single-stranded nucleic acids-binding domain; |
147-224 |
3.46e-14 |
|
Putative single-stranded nucleic acids-binding domain;
Pssm-ID: 214647 Cd Length: 79 Bit Score: 68.10 E-value: 3.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034630830 147 IDLHEFLINTLKNNSRDRMILLKMEQEIIDFIAdNNNHYKKFPQMSSYQRMLVHRVAAYFGLDHNVDQTG--KSVIINKT 224
Cdd:smart00393 1 ADFLPVTLDALSYRPRRREELIELELEIARFVK-STKESVELPPMNSYERKIVHELAEKYGLESESFGEGpkRRVVISKK 79
|
|
| SUZ |
pfam12752 |
SUZ domain; The SUZ domain is a conserved RNA-binding domain found in eukaryotes and enriched ... |
245-300 |
2.56e-13 |
|
SUZ domain; The SUZ domain is a conserved RNA-binding domain found in eukaryotes and enriched in positively charged amino acids. It was first characterized in the C.elegans protein Szy-20 where it has been shown to bind RNA and allow their localization to the centrosome. Warning- the domain has a compositionally biased character.
Pssm-ID: 463689 [Multi-domain] Cd Length: 56 Bit Score: 65.04 E-value: 2.56e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034630830 245 ESQKRFILKRDNSSIDKEDNQQNRMHPFRDDRRSKSIEEREEEYQRVRERIFAHDS 300
Cdd:pfam12752 1 PPPKMKILRRPSSGSSSSSSAGSSGASSSSGSDSKTLEEREAEYAEARARIFGSSE 56
|
|
| R3H |
pfam01424 |
R3H domain; The name of the R3H domain comes from the characteriztic spacing of the most ... |
165-223 |
3.50e-12 |
|
R3H domain; The name of the R3H domain comes from the characteriztic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to be binding ssDNA.
Pssm-ID: 460206 Cd Length: 60 Bit Score: 61.74 E-value: 3.50e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034630830 165 MILLKMEQEIIDFIADNNNHYKkFPQMSSYQRMLVHRVAAYFGLDHNV--DQTGKSVIINK 223
Cdd:pfam01424 1 EFLEQLAEKLAEFVKDTGKSLE-LPPMSSYERRIIHELAQKYGLESESegEEPNRRVVVYK 60
|
|
| PAT1 |
pfam09770 |
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ... |
588-775 |
7.85e-04 |
|
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.
Pssm-ID: 401645 [Multi-domain] Cd Length: 846 Bit Score: 43.10 E-value: 7.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034630830 588 PPSGPVYPSSLmPQPAQQPSYVIASTG-----QQLPTGGFSGSGPPISQQVLQPPPSPqgfvQQPPPAQMPVYYYPSGQY 662
Cdd:pfam09770 166 APKKAAAPAPA-PQPAAQPASLPAPSRkmmslEEVEAAMRAQAKKPAQQPAPAPAQPP----AAPPAQQAQQQQQFPPQI 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034630830 663 PTSTTQQYRPMAPVQYNAQrsqqmpqaaqqaGYQPVLSGQQGFQGLIGVQQPPQSQNVINNQQGTPVQS---------VM 733
Cdd:pfam09770 241 QQQQQPQQQPQQPQQHPGQ------------GHPVTILQRPQSPQPDPAQPSIQPQAQQFHQQPPPVPVqptqilqnpNR 308
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1034630830 734 VSYPTMSSYQVPMTQGSQGLPQQSYQQPIMLPNQAGQGSLPA 775
Cdd:pfam09770 309 LSAARVGYPQNPQPGVQPAPAHQAHRQQGSFGRQAPIITHPQ 350
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
408-675 |
2.23e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 41.85 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034630830 408 PPLQSTPLVSGVAAGSPGCVPYPENGIGGQVAPSSTSYILLPLEAATGIPPGSillnphtgqpfVNPDGTPAIYNPPTSQ 487
Cdd:PHA03247 2701 PPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGG-----------PARPARPPTTAGPPAP 2769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034630830 488 QPLRSAMVGQSQQQPPQQQPSPQPQQQVQPPQPQMAGPlvTQSVQGLQASSQSVQYPAVSFPPqhllPVSPTQhfpmrdd 567
Cdd:PHA03247 2770 APPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADP--PAAVLAPAAALPPAASPAGPLPP----PTSAQP------- 2836
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034630830 568 vatqfgqmtlsrqssgETPEPPSGPVyPSSLMPQPAQQPSYVIASTG--QQLPTGGFSGSGPPISQqVLQPPPSPQGFVQ 645
Cdd:PHA03247 2837 ----------------TAPPPPPGPP-PPSLPLGGSVAPGGDVRRRPpsRSPAAKPAAPARPPVRR-LARPAVSRSTESF 2898
|
250 260 270
....*....|....*....|....*....|.
gi 1034630830 646 -QPPPAQMPVYYYPSGQYPTSTTQQYRPMAP 675
Cdd:PHA03247 2899 aLPPDQPERPPQPQAPPPPQPQPQPPPPPQP 2929
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
589-781 |
4.76e-03 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 40.84 E-value: 4.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034630830 589 PSGPVYPSSLMPQPAQQPSYVIASTgQQLPtggfsgsGPPISQQVLQPppSPQGFVQQPPPAQmpvyyyPSGQYPTSTTQ 668
Cdd:PRK10263 336 PVEPVTQTPPVASVDVPPAQPTVAW-QPVP-------GPQTGEPVIAP--APEGYPQQSQYAQ------PAVQYNEPLQQ 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034630830 669 QYRPMAPVQYNAQRSQQMPQAAQQAGYQPVLSGQQGFQgligVQQPPQSQNVINNQQGTPVQSvMVSYPTMSSYQVPMTQ 748
Cdd:PRK10263 400 PVQPQQPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPA----PEQPVAGNAWQAEEQQSTFAP-QSTYQTEQTYQQPAAQ 474
|
170 180 190
....*....|....*....|....*....|...
gi 1034630830 749 GSQGLPQQSYQQPIMLPNQAGQGSLPATGMPVY 781
Cdd:PRK10263 475 EPLYQQPQPVEQQPVVEPEPVVEETKPARPPLY 507
|
|
| SP1-4_arthropods_N |
cd22553 |
N-terminal domain of transcription factor Specificity Protein (SP) 1-4 from arthropods; ... |
558-801 |
8.13e-03 |
|
N-terminal domain of transcription factor Specificity Protein (SP) 1-4 from arthropods; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. There are many SPs in vertebrates (9 SPs in humans and mice, 7 SPs in the chicken, and 11 SPs in teleost fish), but arthropods only have 3 SPs. One SP is clade SP1-4, which is expressed ubiquitously throughout development. SP1-4 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. This model represents the N-terminal domain of SP1-4 from arthropods.
Pssm-ID: 411778 [Multi-domain] Cd Length: 384 Bit Score: 39.62 E-value: 8.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034630830 558 PTQHFPMRDDVATQFGQMTLSRQSSGETPEPPSGPVYPSSLMPQ--PAQQPsyVIASTGQ------QLPTGGFSGSGPPI 629
Cdd:cd22553 113 ANQQTLIRPNTVQGQANASNVLQNIAQIASGGNAVQLPLNNMTQtiPVQVP--VSTANGQtvyqtiQVPIQAIQSGNAGG 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034630830 630 SQQVLQPPPSPQgfVQQPPPAQMPVYYYPSGQ-----YPTSTTQQYRPMAPVQYNaQRSQQMPQAAQQAGYQPVLSGQQG 704
Cdd:cd22553 191 GNQALQAQVIPQ--LAQAAQLQPQQLAQVSSQgyiqqIPANASQQQPQMVQQGPN-QSGQIIGQVASASSIQAAAIPLTV 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034630830 705 FQGLIGvqqppqSQNVINNQQGTPVQSV--------MVSYPTMSSYQVPMTQGSQGLPQQSYQQPIMLPNQAGQGSLPAT 776
Cdd:cd22553 268 YTGALA------GQNGSNQQQVGQIVTSpiqgmtqgLTAPASSSIPTVVQQQAIQGNPLPPGTQIIAAGQQLQQDPNDPT 341
|
250 260
....*....|....*....|....*
gi 1034630830 777 GMPVYCNVTPPTPQnNLRLIGPHCP 801
Cdd:cd22553 342 KWQVVADGTPGSKK-RLRRVACTCP 365
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| R3H_encore_like |
cd02642 |
R3H domain of encore-like and DIP1-like proteins. Drosophila encore is involved in the ... |
163-224 |
6.19e-26 |
|
R3H domain of encore-like and DIP1-like proteins. Drosophila encore is involved in the germline exit after four mitotic divisions, by facilitating SCF-ubiquitin-proteasome-dependent proteolysis. Maize DBF1-interactor protein 1 (DIP1) containing an R3H domain is a potential regulator of DBF1 activity in stress responses. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner.
Pssm-ID: 100071 Cd Length: 63 Bit Score: 101.14 E-value: 6.19e-26
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034630830 163 DRMILLKMEQEIIDFIADNNNHYKKFPQMSSYQRMLVHRVAAYFGLDHNVDQTG-KSVIINKT 224
Cdd:cd02642 1 DRLFVLKLEKDLLAFIKDSTRQSLELPPMNSYYRLLAHRVAQYYGLDHNVDNSGgKCVIVNKT 63
|
|
| R3H |
smart00393 |
Putative single-stranded nucleic acids-binding domain; |
147-224 |
3.46e-14 |
|
Putative single-stranded nucleic acids-binding domain;
Pssm-ID: 214647 Cd Length: 79 Bit Score: 68.10 E-value: 3.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034630830 147 IDLHEFLINTLKNNSRDRMILLKMEQEIIDFIAdNNNHYKKFPQMSSYQRMLVHRVAAYFGLDHNVDQTG--KSVIINKT 224
Cdd:smart00393 1 ADFLPVTLDALSYRPRRREELIELELEIARFVK-STKESVELPPMNSYERKIVHELAEKYGLESESFGEGpkRRVVISKK 79
|
|
| SUZ |
pfam12752 |
SUZ domain; The SUZ domain is a conserved RNA-binding domain found in eukaryotes and enriched ... |
245-300 |
2.56e-13 |
|
SUZ domain; The SUZ domain is a conserved RNA-binding domain found in eukaryotes and enriched in positively charged amino acids. It was first characterized in the C.elegans protein Szy-20 where it has been shown to bind RNA and allow their localization to the centrosome. Warning- the domain has a compositionally biased character.
Pssm-ID: 463689 [Multi-domain] Cd Length: 56 Bit Score: 65.04 E-value: 2.56e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034630830 245 ESQKRFILKRDNSSIDKEDNQQNRMHPFRDDRRSKSIEEREEEYQRVRERIFAHDS 300
Cdd:pfam12752 1 PPPKMKILRRPSSGSSSSSSAGSSGASSSSGSDSKTLEEREAEYAEARARIFGSSE 56
|
|
| R3H |
cd02325 |
R3H domain. The name of the R3H domain comes from the characteristic spacing of the most ... |
167-223 |
1.85e-12 |
|
R3H domain. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. R3H domains are found in proteins together with ATPase domains, SF1 helicase domains, SF2 DEAH helicase domains, Cys-rich repeats, ring-type zinc fingers, and KH domains. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner.
Pssm-ID: 100064 Cd Length: 59 Bit Score: 62.63 E-value: 1.85e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034630830 167 LLKMEQEIIDFIADNNNHYKKFPQMSSYQRMLVHRVAAYFGLDHNVDQTG--KSVIINK 223
Cdd:cd02325 1 REEREEELEAFAKDAAGKSLELPPMNSYERKLIHDLAEYYGLKSESEGEGpnRRVVITK 59
|
|
| R3H |
pfam01424 |
R3H domain; The name of the R3H domain comes from the characteriztic spacing of the most ... |
165-223 |
3.50e-12 |
|
R3H domain; The name of the R3H domain comes from the characteriztic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to be binding ssDNA.
Pssm-ID: 460206 Cd Length: 60 Bit Score: 61.74 E-value: 3.50e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034630830 165 MILLKMEQEIIDFIADNNNHYKkFPQMSSYQRMLVHRVAAYFGLDHNV--DQTGKSVIINK 223
Cdd:pfam01424 1 EFLEQLAEKLAEFVKDTGKSLE-LPPMSSYERRIIHELAQKYGLESESegEEPNRRVVVYK 60
|
|
| PAT1 |
pfam09770 |
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ... |
588-775 |
7.85e-04 |
|
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.
Pssm-ID: 401645 [Multi-domain] Cd Length: 846 Bit Score: 43.10 E-value: 7.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034630830 588 PPSGPVYPSSLmPQPAQQPSYVIASTG-----QQLPTGGFSGSGPPISQQVLQPPPSPqgfvQQPPPAQMPVYYYPSGQY 662
Cdd:pfam09770 166 APKKAAAPAPA-PQPAAQPASLPAPSRkmmslEEVEAAMRAQAKKPAQQPAPAPAQPP----AAPPAQQAQQQQQFPPQI 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034630830 663 PTSTTQQYRPMAPVQYNAQrsqqmpqaaqqaGYQPVLSGQQGFQGLIGVQQPPQSQNVINNQQGTPVQS---------VM 733
Cdd:pfam09770 241 QQQQQPQQQPQQPQQHPGQ------------GHPVTILQRPQSPQPDPAQPSIQPQAQQFHQQPPPVPVqptqilqnpNR 308
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1034630830 734 VSYPTMSSYQVPMTQGSQGLPQQSYQQPIMLPNQAGQGSLPA 775
Cdd:pfam09770 309 LSAARVGYPQNPQPGVQPAPAHQAHRQQGSFGRQAPIITHPQ 350
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
408-675 |
2.23e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 41.85 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034630830 408 PPLQSTPLVSGVAAGSPGCVPYPENGIGGQVAPSSTSYILLPLEAATGIPPGSillnphtgqpfVNPDGTPAIYNPPTSQ 487
Cdd:PHA03247 2701 PPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGG-----------PARPARPPTTAGPPAP 2769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034630830 488 QPLRSAMVGQSQQQPPQQQPSPQPQQQVQPPQPQMAGPlvTQSVQGLQASSQSVQYPAVSFPPqhllPVSPTQhfpmrdd 567
Cdd:PHA03247 2770 APPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADP--PAAVLAPAAALPPAASPAGPLPP----PTSAQP------- 2836
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034630830 568 vatqfgqmtlsrqssgETPEPPSGPVyPSSLMPQPAQQPSYVIASTG--QQLPTGGFSGSGPPISQqVLQPPPSPQGFVQ 645
Cdd:PHA03247 2837 ----------------TAPPPPPGPP-PPSLPLGGSVAPGGDVRRRPpsRSPAAKPAAPARPPVRR-LARPAVSRSTESF 2898
|
250 260 270
....*....|....*....|....*....|.
gi 1034630830 646 -QPPPAQMPVYYYPSGQYPTSTTQQYRPMAP 675
Cdd:PHA03247 2899 aLPPDQPERPPQPQAPPPPQPQPQPPPPPQP 2929
|
|
| R3H_unknown_2 |
cd06006 |
R3H domain of a group of fungal proteins with unknown function. The name of the R3H domain ... |
169-209 |
2.78e-03 |
|
R3H domain of a group of fungal proteins with unknown function. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner.
Pssm-ID: 100076 Cd Length: 59 Bit Score: 36.58 E-value: 2.78e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1034630830 169 KMEQEIIDFIADNNNHYKKFPQMSSYQRMLVHRVAAYFGLD 209
Cdd:cd06006 3 QIESTLRKFINDKSKRSLRFPPMRSPQRAFIHELAKDYGLY 43
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
405-824 |
2.82e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 41.46 E-value: 2.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034630830 405 RTHPPLQSTPLVSGVAAGS----PGCVPYPENGIG---------GQVAPSStsyilLPLEAATGIPPgsillnPHTGQPF 471
Cdd:PHA03247 2566 RSVPPPRPAPRPSEPAVTSrarrPDAPPQSARPRApvddrgdprGPAPPSP-----LPPDTHAPDPP------PPSPSPA 2634
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034630830 472 VNPDGTPAIYNPPTSQQPLRSAMVGQSQQQPPQQQPSPQPQQQVQPPQ-PQMAGPLVTQSVQGL------QASSQSVQYP 544
Cdd:PHA03247 2635 ANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRpRRRAARPTVGSLTSLadppppPPTPEPAPHA 2714
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034630830 545 AVSFPPQHLLPVSPTQHFPMR----------DDVATQFGQMTLSRQSSGETPEPPSGPVYPSS----------------- 597
Cdd:PHA03247 2715 LVSATPLPPGPAAARQASPALpaapappavpAGPATPGGPARPARPPTTAGPPAPAPPAAPAAgpprrltrpavaslses 2794
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034630830 598 -----LMPQPAQQPSYVIASTGQQLPTGGFSGSGPPISQQVLQPPPSPQGFVqqPPPAQMPVYYYPSGQY---PTSTTQQ 669
Cdd:PHA03247 2795 reslpSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPP--PPSLPLGGSVAPGGDVrrrPPSRSPA 2872
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034630830 670 YRPMAPVQYNAQRSQqmpqaaqqagyQPVLSGQQGFQGLIGVQQPPQSQNVINNQQGTPVQSVMVSYPTMSsyqvPMTQG 749
Cdd:PHA03247 2873 AKPAAPARPPVRRLA-----------RPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPP----PPPPP 2937
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034630830 750 SQGLPQQSYQQPIMLPNQAGQGSLPATGMPVYCNVTPPTpqnnlRLIGPHCPSSTVPVMSASCRTNCASMSNAGW 824
Cdd:PHA03247 2938 RPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPR-----FRVPQPAPSREAPASSTPPLTGHSLSRVSSW 3007
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
487-825 |
4.12e-03 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 40.91 E-value: 4.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034630830 487 QQPLRSAMVGQSQQQPPQQQPSPQPQQQVQPPQPQMAGPLVTQSVQGLQASSQSVQYPAVSFPPQHLLPVSPTQHFPMRD 566
Cdd:pfam03154 164 QQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQTPTLHPQRLP 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034630830 567 DVATQFGQMTLSRQSSGETPEPPSGPVY--PSSLMPQPAQ------------QPSYVIASTGQ-QLPTGGFSGSGPPISQ 631
Cdd:pfam03154 244 SPHPPLQPMTQPPPPSQVSPQPLPQPSLhgQMPPMPHSLQtgpshmqhpvppQPFPLTPQSSQsQVPPGPSPAAPGQSQQ 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034630830 632 QVLQPPPSPQGFVQQP------PPAQMPVyyyPSGQYPTSTtqqyrPMAPVQyNAQRSQqmpqaaqqagYQPVLSGQQGF 705
Cdd:pfam03154 324 RIHTPPSQSQLQSQQPpreqplPPAPLSM---PHIKPPPTT-----PIPQLP-NPQSHK----------HPPHLSGPSPF 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034630830 706 QGLIGVQQPPQSQnvinnqqgtPVQSVMVSYPTmSSYQVP---MTQgSQGLPQQSYQQPIMLPNQ---AGQGSLPATGMP 779
Cdd:pfam03154 385 QMNSNLPPPPALK---------PLSSLSTHHPP-SAHPPPlqlMPQ-SQQLPPPPAQPPVLTQSQslpPPAASHPPTSGL 453
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1034630830 780 VYCNVTPPTPQNnlrligPHCPSSTVPVMSASCRTNCASMSNAGWQ 825
Cdd:pfam03154 454 HQVPSQSPFPQH------PFVPGGPPPITPPSGPPTSTSSAMPGIQ 493
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
465-789 |
4.20e-03 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 40.91 E-value: 4.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034630830 465 PHTGQPFVNPDGTPAIYNPPTSQQPLRSAMvgQSQQQPPQQQPSPQPQQQVQPPQPQMAGPLVTQSVQGLQASSQSVQYP 544
Cdd:pfam03154 199 PTPSAPSVPPQGSPATSQPPNQTQSTAAPH--TLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSPQPLPQPSLHGQMP 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034630830 545 AVSFP----PQHLLPVSPTQHFPMRDDVATQFGQMTLSRQSSGETPEPPSGPvyPSSLMPQPAQQPSYviastgQQLPTG 620
Cdd:pfam03154 277 PMPHSlqtgPSHMQHPVPPQPFPLTPQSSQSQVPPGPSPAAPGQSQQRIHTP--PSQSQLQSQQPPRE------QPLPPA 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034630830 621 gfsgsgpPISQQVLQPPPS--------PQG-----FVQQPPPAQMPVYY-YPSGQYPTSTTQQYRPMAPVQYNAQRSQQM 686
Cdd:pfam03154 349 -------PLSMPHIKPPPTtpipqlpnPQShkhppHLSGPSPFQMNSNLpPPPALKPLSSLSTHHPPSAHPPPLQLMPQS 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034630830 687 PQAAQQAGYQPVLSGQQGFQGLIGVQQPPQSQNVINNQQGTPVQSVMVSYPT-MSSYQVPMTQGSQGLPqqSYQQPIMLP 765
Cdd:pfam03154 422 QQLPPPPAQPPVLTQSQSLPPPAASHPPTSGLHQVPSQSPFPQHPFVPGGPPpITPPSGPPTSTSSAMP--GIQPPSSAS 499
|
330 340
....*....|....*....|....
gi 1034630830 766 nqagqgslPATGMPVYCNVTPPTP 789
Cdd:pfam03154 500 --------VSSSGPVPAAVSCPLP 515
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
589-781 |
4.76e-03 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 40.84 E-value: 4.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034630830 589 PSGPVYPSSLMPQPAQQPSYVIASTgQQLPtggfsgsGPPISQQVLQPppSPQGFVQQPPPAQmpvyyyPSGQYPTSTTQ 668
Cdd:PRK10263 336 PVEPVTQTPPVASVDVPPAQPTVAW-QPVP-------GPQTGEPVIAP--APEGYPQQSQYAQ------PAVQYNEPLQQ 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034630830 669 QYRPMAPVQYNAQRSQQMPQAAQQAGYQPVLSGQQGFQgligVQQPPQSQNVINNQQGTPVQSvMVSYPTMSSYQVPMTQ 748
Cdd:PRK10263 400 PVQPQQPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPA----PEQPVAGNAWQAEEQQSTFAP-QSTYQTEQTYQQPAAQ 474
|
170 180 190
....*....|....*....|....*....|...
gi 1034630830 749 GSQGLPQQSYQQPIMLPNQAGQGSLPATGMPVY 781
Cdd:PRK10263 475 EPLYQQPQPVEQQPVVEPEPVVEETKPARPPLY 507
|
|
| PRK14971 |
PRK14971 |
DNA polymerase III subunit gamma/tau; |
581-677 |
5.57e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237874 [Multi-domain] Cd Length: 614 Bit Score: 40.14 E-value: 5.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034630830 581 SSGETPEPPSGP---VYPSSLMPQPAQQPSYVIASTGQQLPTGgfSGSGPPISQQVLQPPPS-PQGFVQQPPPAQMPVYY 656
Cdd:PRK14971 364 QKGDDASGGRGPkqhIKPVFTQPAAAPQPSAAAAASPSPSQSS--AAAQPSAPQSATQPAGTpPTVSVDPPAAVPVNPPS 441
|
90 100
....*....|....*....|.
gi 1034630830 657 YPSGQYPTSTTQQYRPMAPVQ 677
Cdd:PRK14971 442 TAPQAVRPAQFKEEKKIPVSK 462
|
|
| R3H_Smubp-2_like |
cd02641 |
R3H domain of Smubp-2_like proteins. Smubp-2_like proteins also contain a helicase_like and ... |
174-221 |
6.11e-03 |
|
R3H domain of Smubp-2_like proteins. Smubp-2_like proteins also contain a helicase_like and an AN1-like Zinc finger domain and have been shown to bind single-stranded DNA. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA.
Pssm-ID: 100070 Cd Length: 60 Bit Score: 35.79 E-value: 6.11e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1034630830 174 IIDFIADNNNHYKKFP-QMSSYQRMLVHRVAAYFGLDHNVDQTGKSVII 221
Cdd:cd02641 8 VKAFMKDPKATELEFPpTLSSHDRLLVHELAEELGLRHESTGEGSDRVI 56
|
|
| SP1-4_arthropods_N |
cd22553 |
N-terminal domain of transcription factor Specificity Protein (SP) 1-4 from arthropods; ... |
558-801 |
8.13e-03 |
|
N-terminal domain of transcription factor Specificity Protein (SP) 1-4 from arthropods; Specificity Proteins (SPs) are transcription factors that are involved in many cellular processes, including cell differentiation, cell growth, apoptosis, immune responses, response to DNA damage, and chromatin remodeling. There are many SPs in vertebrates (9 SPs in humans and mice, 7 SPs in the chicken, and 11 SPs in teleost fish), but arthropods only have 3 SPs. One SP is clade SP1-4, which is expressed ubiquitously throughout development. SP1-4 belongs to a family of proteins, called the SP/Kruppel or Krueppel-like Factor (KLF) family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. SP factors preferentially bind GC boxes, while KLFs bind CACCC boxes. Another characteristic hallmark of SP factors is the presence of the Buttonhead (BTD) box CXCPXC, just N-terminal to the zinc fingers. The function of the BTD box is unknown, but it is thought to play an important physiological role. Another feature of most SP factors is the presence of a conserved amino acid stretch, the so-called SP box, located close to the N-terminus. This model represents the N-terminal domain of SP1-4 from arthropods.
Pssm-ID: 411778 [Multi-domain] Cd Length: 384 Bit Score: 39.62 E-value: 8.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034630830 558 PTQHFPMRDDVATQFGQMTLSRQSSGETPEPPSGPVYPSSLMPQ--PAQQPsyVIASTGQ------QLPTGGFSGSGPPI 629
Cdd:cd22553 113 ANQQTLIRPNTVQGQANASNVLQNIAQIASGGNAVQLPLNNMTQtiPVQVP--VSTANGQtvyqtiQVPIQAIQSGNAGG 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034630830 630 SQQVLQPPPSPQgfVQQPPPAQMPVYYYPSGQ-----YPTSTTQQYRPMAPVQYNaQRSQQMPQAAQQAGYQPVLSGQQG 704
Cdd:cd22553 191 GNQALQAQVIPQ--LAQAAQLQPQQLAQVSSQgyiqqIPANASQQQPQMVQQGPN-QSGQIIGQVASASSIQAAAIPLTV 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034630830 705 FQGLIGvqqppqSQNVINNQQGTPVQSV--------MVSYPTMSSYQVPMTQGSQGLPQQSYQQPIMLPNQAGQGSLPAT 776
Cdd:cd22553 268 YTGALA------GQNGSNQQQVGQIVTSpiqgmtqgLTAPASSSIPTVVQQQAIQGNPLPPGTQIIAAGQQLQQDPNDPT 341
|
250 260
....*....|....*....|....*
gi 1034630830 777 GMPVYCNVTPPTPQnNLRLIGPHCP 801
Cdd:cd22553 342 KWQVVADGTPGSKK-RLRRVACTCP 365
|
|
|