transcription elongation regulator 1 isoform X4 [Mus musculus]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||||||
| PRP40 super family | cl34905 | Splicing factor [RNA processing and modification]; |
408-1022 | 1.42e-23 | |||||||||
Splicing factor [RNA processing and modification]; The actual alignment was detected with superfamily member COG5104: Pssm-ID: 227435 [Multi-domain] Cd Length: 590 Bit Score: 106.70 E-value: 1.42e-23
|
|||||||||||||
| WW | pfam00397 | WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
137-162 | 5.74e-08 | |||||||||
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro. : Pssm-ID: 459800 [Multi-domain] Cd Length: 30 Bit Score: 49.43 E-value: 5.74e-08
|
|||||||||||||
| FF | smart00441 | Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ... |
1017-1081 | 2.09e-04 | |||||||||
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often contains two conserved Phe (F) residues. : Pssm-ID: 128718 [Multi-domain] Cd Length: 55 Bit Score: 40.25 E-value: 2.09e-04
|
|||||||||||||
| half-pint super family | cl31128 | poly-U binding splicing factor, half-pint family; The proteins represented by this model ... |
304-469 | 5.31e-04 | |||||||||
poly-U binding splicing factor, half-pint family; The proteins represented by this model contain three RNA recognition motifs (rrm: pfam00076) and have been characterized as poly-pyrimidine tract binding proteins associated with RNA splicing factors. In the case of PUF60 (GP|6176532), in complex with p54, and in the presence of U2AF, facilitates association of U2 snRNP with pre-mRNA. The actual alignment was detected with superfamily member TIGR01645: Pssm-ID: 130706 [Multi-domain] Cd Length: 612 Bit Score: 43.91 E-value: 5.31e-04
|
|||||||||||||
| Name | Accession | Description | Interval | E-value | |||||||||
| PRP40 | COG5104 | Splicing factor [RNA processing and modification]; |
408-1022 | 1.42e-23 | |||||||||
Splicing factor [RNA processing and modification]; Pssm-ID: 227435 [Multi-domain] Cd Length: 590 Bit Score: 106.70 E-value: 1.42e-23
|
|||||||||||||
| FF | pfam01846 | FF domain; This domain has been predicted to be involved in protein-protein interaction. This ... |
798-847 | 1.45e-13 | |||||||||
FF domain; This domain has been predicted to be involved in protein-protein interaction. This domain was recently shown to bind the hyperphosphorylated C-terminal repeat domain of RNA polymerase II, confirming its role in protein-protein interactions. Pssm-ID: 426471 [Multi-domain] Cd Length: 50 Bit Score: 65.94 E-value: 1.45e-13
|
|||||||||||||
| FF | smart00441 | Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ... |
959-1014 | 9.16e-10 | |||||||||
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often contains two conserved Phe (F) residues. Pssm-ID: 128718 [Multi-domain] Cd Length: 55 Bit Score: 55.27 E-value: 9.16e-10
|
|||||||||||||
| WW | cd00201 | Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
420-449 | 9.21e-09 | |||||||||
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs. Pssm-ID: 238122 [Multi-domain] Cd Length: 31 Bit Score: 51.76 E-value: 9.21e-09
|
|||||||||||||
| WW | pfam00397 | WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
137-162 | 5.74e-08 | |||||||||
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro. Pssm-ID: 459800 [Multi-domain] Cd Length: 30 Bit Score: 49.43 E-value: 5.74e-08
|
|||||||||||||
| WW | smart00456 | Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
132-164 | 5.76e-08 | |||||||||
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides. Pssm-ID: 197736 [Multi-domain] Cd Length: 33 Bit Score: 49.52 E-value: 5.76e-08
|
|||||||||||||
| WW | cd00201 | Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
137-164 | 1.54e-07 | |||||||||
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs. Pssm-ID: 238122 [Multi-domain] Cd Length: 31 Bit Score: 48.29 E-value: 1.54e-07
|
|||||||||||||
| PRP40 | COG5104 | Splicing factor [RNA processing and modification]; |
124-173 | 1.19e-05 | |||||||||
Splicing factor [RNA processing and modification]; Pssm-ID: 227435 [Multi-domain] Cd Length: 590 Bit Score: 49.31 E-value: 1.19e-05
|
|||||||||||||
| PTZ00121 | PTZ00121 | MAEBL; Provisional |
714-1054 | 1.33e-05 | |||||||||
MAEBL; Provisional Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.75 E-value: 1.33e-05
|
|||||||||||||
| FF | smart00441 | Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ... |
1017-1081 | 2.09e-04 | |||||||||
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often contains two conserved Phe (F) residues. Pssm-ID: 128718 [Multi-domain] Cd Length: 55 Bit Score: 40.25 E-value: 2.09e-04
|
|||||||||||||
| FF | pfam01846 | FF domain; This domain has been predicted to be involved in protein-protein interaction. This ... |
1019-1078 | 2.12e-04 | |||||||||
FF domain; This domain has been predicted to be involved in protein-protein interaction. This domain was recently shown to bind the hyperphosphorylated C-terminal repeat domain of RNA polymerase II, confirming its role in protein-protein interactions. Pssm-ID: 426471 [Multi-domain] Cd Length: 50 Bit Score: 39.75 E-value: 2.12e-04
|
|||||||||||||
| half-pint | TIGR01645 | poly-U binding splicing factor, half-pint family; The proteins represented by this model ... |
304-469 | 5.31e-04 | |||||||||
poly-U binding splicing factor, half-pint family; The proteins represented by this model contain three RNA recognition motifs (rrm: pfam00076) and have been characterized as poly-pyrimidine tract binding proteins associated with RNA splicing factors. In the case of PUF60 (GP|6176532), in complex with p54, and in the presence of U2AF, facilitates association of U2 snRNP with pre-mRNA. Pssm-ID: 130706 [Multi-domain] Cd Length: 612 Bit Score: 43.91 E-value: 5.31e-04
|
|||||||||||||
| PHA02682 | PHA02682 | ORF080 virion core protein; Provisional |
307-429 | 6.89e-04 | |||||||||
ORF080 virion core protein; Provisional Pssm-ID: 177464 [Multi-domain] Cd Length: 280 Bit Score: 42.93 E-value: 6.89e-04
|
|||||||||||||
| Herpes_BLLF1 | pfam05109 | Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
258-352 | 2.21e-03 | |||||||||
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo. Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 42.21 E-value: 2.21e-03
|
|||||||||||||
| KLF3_N | cd21577 | N-terminal domain of Kruppel-like factor 3; Kruppel-like factor 3 (KLF3; also called ... |
300-397 | 4.41e-03 | |||||||||
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: 40.02 E-value: 4.41e-03
|
|||||||||||||
| SMC_prok_A | TIGR02169 | chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
848-1057 | 7.25e-03 | |||||||||
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins] Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.44 E-value: 7.25e-03
|
|||||||||||||
| Name | Accession | Description | Interval | E-value | |||||||||
| PRP40 | COG5104 | Splicing factor [RNA processing and modification]; |
408-1022 | 1.42e-23 | |||||||||
Splicing factor [RNA processing and modification]; Pssm-ID: 227435 [Multi-domain] Cd Length: 590 Bit Score: 106.70 E-value: 1.42e-23
|
|||||||||||||
| FF | pfam01846 | FF domain; This domain has been predicted to be involved in protein-protein interaction. This ... |
798-847 | 1.45e-13 | |||||||||
FF domain; This domain has been predicted to be involved in protein-protein interaction. This domain was recently shown to bind the hyperphosphorylated C-terminal repeat domain of RNA polymerase II, confirming its role in protein-protein interactions. Pssm-ID: 426471 [Multi-domain] Cd Length: 50 Bit Score: 65.94 E-value: 1.45e-13
|
|||||||||||||
| FF | pfam01846 | FF domain; This domain has been predicted to be involved in protein-protein interaction. This ... |
731-780 | 1.46e-11 | |||||||||
FF domain; This domain has been predicted to be involved in protein-protein interaction. This domain was recently shown to bind the hyperphosphorylated C-terminal repeat domain of RNA polymerase II, confirming its role in protein-protein interactions. Pssm-ID: 426471 [Multi-domain] Cd Length: 50 Bit Score: 60.16 E-value: 1.46e-11
|
|||||||||||||
| FF | smart00441 | Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ... |
959-1014 | 9.16e-10 | |||||||||
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often contains two conserved Phe (F) residues. Pssm-ID: 128718 [Multi-domain] Cd Length: 55 Bit Score: 55.27 E-value: 9.16e-10
|
|||||||||||||
| FF | pfam01846 | FF domain; This domain has been predicted to be involved in protein-protein interaction. This ... |
666-713 | 9.85e-10 | |||||||||
FF domain; This domain has been predicted to be involved in protein-protein interaction. This domain was recently shown to bind the hyperphosphorylated C-terminal repeat domain of RNA polymerase II, confirming its role in protein-protein interactions. Pssm-ID: 426471 [Multi-domain] Cd Length: 50 Bit Score: 55.16 E-value: 9.85e-10
|
|||||||||||||
| FF | smart00441 | Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ... |
797-850 | 1.97e-09 | |||||||||
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often contains two conserved Phe (F) residues. Pssm-ID: 128718 [Multi-domain] Cd Length: 55 Bit Score: 54.50 E-value: 1.97e-09
|
|||||||||||||
| FF | pfam01846 | FF domain; This domain has been predicted to be involved in protein-protein interaction. This ... |
902-953 | 3.41e-09 | |||||||||
FF domain; This domain has been predicted to be involved in protein-protein interaction. This domain was recently shown to bind the hyperphosphorylated C-terminal repeat domain of RNA polymerase II, confirming its role in protein-protein interactions. Pssm-ID: 426471 [Multi-domain] Cd Length: 50 Bit Score: 53.61 E-value: 3.41e-09
|
|||||||||||||
| WW | cd00201 | Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
420-449 | 9.21e-09 | |||||||||
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs. Pssm-ID: 238122 [Multi-domain] Cd Length: 31 Bit Score: 51.76 E-value: 9.21e-09
|
|||||||||||||
| WW | pfam00397 | WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
420-447 | 3.35e-08 | |||||||||
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro. Pssm-ID: 459800 [Multi-domain] Cd Length: 30 Bit Score: 50.20 E-value: 3.35e-08
|
|||||||||||||
| WW | pfam00397 | WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
137-162 | 5.74e-08 | |||||||||
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro. Pssm-ID: 459800 [Multi-domain] Cd Length: 30 Bit Score: 49.43 E-value: 5.74e-08
|
|||||||||||||
| WW | smart00456 | Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
132-164 | 5.76e-08 | |||||||||
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides. Pssm-ID: 197736 [Multi-domain] Cd Length: 33 Bit Score: 49.52 E-value: 5.76e-08
|
|||||||||||||
| WW | smart00456 | Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
422-449 | 6.23e-08 | |||||||||
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides. Pssm-ID: 197736 [Multi-domain] Cd Length: 33 Bit Score: 49.52 E-value: 6.23e-08
|
|||||||||||||
| FF | smart00441 | Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ... |
730-783 | 1.54e-07 | |||||||||
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often contains two conserved Phe (F) residues. Pssm-ID: 128718 [Multi-domain] Cd Length: 55 Bit Score: 49.11 E-value: 1.54e-07
|
|||||||||||||
| WW | cd00201 | Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
137-164 | 1.54e-07 | |||||||||
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs. Pssm-ID: 238122 [Multi-domain] Cd Length: 31 Bit Score: 48.29 E-value: 1.54e-07
|
|||||||||||||
| FF | pfam01846 | FF domain; This domain has been predicted to be involved in protein-protein interaction. This ... |
960-1011 | 3.31e-07 | |||||||||
FF domain; This domain has been predicted to be involved in protein-protein interaction. This domain was recently shown to bind the hyperphosphorylated C-terminal repeat domain of RNA polymerase II, confirming its role in protein-protein interactions. Pssm-ID: 426471 [Multi-domain] Cd Length: 50 Bit Score: 47.84 E-value: 3.31e-07
|
|||||||||||||
| FF | smart00441 | Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ... |
901-956 | 2.97e-06 | |||||||||
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often contains two conserved Phe (F) residues. Pssm-ID: 128718 [Multi-domain] Cd Length: 55 Bit Score: 45.26 E-value: 2.97e-06
|
|||||||||||||
| FF | smart00441 | Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ... |
664-715 | 7.62e-06 | |||||||||
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often contains two conserved Phe (F) residues. Pssm-ID: 128718 [Multi-domain] Cd Length: 55 Bit Score: 44.10 E-value: 7.62e-06
|
|||||||||||||
| WW | smart00456 | Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ... |
520-548 | 1.02e-05 | |||||||||
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides. Pssm-ID: 197736 [Multi-domain] Cd Length: 33 Bit Score: 43.36 E-value: 1.02e-05
|
|||||||||||||
| DUF5401 | pfam17380 | Family of unknown function (DUF5401); This is a family of unknown function found in ... |
705-955 | 1.12e-05 | |||||||||
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea. Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 49.74 E-value: 1.12e-05
|
|||||||||||||
| PRP40 | COG5104 | Splicing factor [RNA processing and modification]; |
124-173 | 1.19e-05 | |||||||||
Splicing factor [RNA processing and modification]; Pssm-ID: 227435 [Multi-domain] Cd Length: 590 Bit Score: 49.31 E-value: 1.19e-05
|
|||||||||||||
| PTZ00121 | PTZ00121 | MAEBL; Provisional |
714-1054 | 1.33e-05 | |||||||||
MAEBL; Provisional Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.75 E-value: 1.33e-05
|
|||||||||||||
| WW | cd00201 | Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ... |
519-548 | 1.80e-05 | |||||||||
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs. Pssm-ID: 238122 [Multi-domain] Cd Length: 31 Bit Score: 42.52 E-value: 1.80e-05
|
|||||||||||||
| PRP40 | COG5104 | Splicing factor [RNA processing and modification]; |
137-172 | 7.86e-05 | |||||||||
Splicing factor [RNA processing and modification]; Pssm-ID: 227435 [Multi-domain] Cd Length: 590 Bit Score: 46.61 E-value: 7.86e-05
|
|||||||||||||
| PTZ00121 | PTZ00121 | MAEBL; Provisional |
717-986 | 7.94e-05 | |||||||||
MAEBL; Provisional Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.06 E-value: 7.94e-05
|
|||||||||||||
| PTZ00121 | PTZ00121 | MAEBL; Provisional |
593-1007 | 1.01e-04 | |||||||||
MAEBL; Provisional Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.67 E-value: 1.01e-04
|
|||||||||||||
| WW | pfam00397 | WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ... |
519-546 | 1.99e-04 | |||||||||
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro. Pssm-ID: 459800 [Multi-domain] Cd Length: 30 Bit Score: 39.41 E-value: 1.99e-04
|
|||||||||||||
| FF | smart00441 | Contains two conserved F residues; A novel motif that often accompanies WW domains. Often ... |
1017-1081 | 2.09e-04 | |||||||||
Contains two conserved F residues; A novel motif that often accompanies WW domains. Often contains two conserved Phe (F) residues. Pssm-ID: 128718 [Multi-domain] Cd Length: 55 Bit Score: 40.25 E-value: 2.09e-04
|
|||||||||||||
| FF | pfam01846 | FF domain; This domain has been predicted to be involved in protein-protein interaction. This ... |
1019-1078 | 2.12e-04 | |||||||||
FF domain; This domain has been predicted to be involved in protein-protein interaction. This domain was recently shown to bind the hyperphosphorylated C-terminal repeat domain of RNA polymerase II, confirming its role in protein-protein interactions. Pssm-ID: 426471 [Multi-domain] Cd Length: 50 Bit Score: 39.75 E-value: 2.12e-04
|
|||||||||||||
| PTZ00121 | PTZ00121 | MAEBL; Provisional |
701-1073 | 3.30e-04 | |||||||||
MAEBL; Provisional Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.13 E-value: 3.30e-04
|
|||||||||||||
| half-pint | TIGR01645 | poly-U binding splicing factor, half-pint family; The proteins represented by this model ... |
304-469 | 5.31e-04 | |||||||||
poly-U binding splicing factor, half-pint family; The proteins represented by this model contain three RNA recognition motifs (rrm: pfam00076) and have been characterized as poly-pyrimidine tract binding proteins associated with RNA splicing factors. In the case of PUF60 (GP|6176532), in complex with p54, and in the presence of U2AF, facilitates association of U2 snRNP with pre-mRNA. Pssm-ID: 130706 [Multi-domain] Cd Length: 612 Bit Score: 43.91 E-value: 5.31e-04
|
|||||||||||||
| PRK03918 | PRK03918 | DNA double-strand break repair ATPase Rad50; |
720-1074 | 5.47e-04 | |||||||||
DNA double-strand break repair ATPase Rad50; Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 5.47e-04
|
|||||||||||||
| PHA02682 | PHA02682 | ORF080 virion core protein; Provisional |
307-429 | 6.89e-04 | |||||||||
ORF080 virion core protein; Provisional Pssm-ID: 177464 [Multi-domain] Cd Length: 280 Bit Score: 42.93 E-value: 6.89e-04
|
|||||||||||||
| SMC_N | pfam02463 | RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
702-1094 | 1.09e-03 | |||||||||
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination. Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 43.42 E-value: 1.09e-03
|
|||||||||||||
| HEC1 | COG5185 | Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
717-999 | 1.77e-03 | |||||||||
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning]; Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 42.25 E-value: 1.77e-03
|
|||||||||||||
| Herpes_BLLF1 | pfam05109 | Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
258-352 | 2.21e-03 | |||||||||
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo. Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 42.21 E-value: 2.21e-03
|
|||||||||||||
| KLF3_N | cd21577 | N-terminal domain of Kruppel-like factor 3; Kruppel-like factor 3 (KLF3; also called ... |
300-397 | 4.41e-03 | |||||||||
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: 40.02 E-value: 4.41e-03
|
|||||||||||||
| COG4913 | COG4913 | Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
840-971 | 5.64e-03 | |||||||||
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 5.64e-03
|
|||||||||||||
| SMC_prok_A | TIGR02169 | chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
848-1057 | 7.25e-03 | |||||||||
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins] Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.44 E-value: 7.25e-03
|
|||||||||||||
| PHA03369 | PHA03369 | capsid maturational protease; Provisional |
316-473 | 7.52e-03 | |||||||||
capsid maturational protease; Provisional Pssm-ID: 223061 [Multi-domain] Cd Length: 663 Bit Score: 40.37 E-value: 7.52e-03
|
|||||||||||||
| PLN02316 | PLN02316 | synthase/transferase |
837-922 | 9.07e-03 | |||||||||
synthase/transferase Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 40.24 E-value: 9.07e-03
|
|||||||||||||
| Blast search parameters | ||||
|
