ankyrin repeat and KH domain-containing protein 1 isoform X8 [Cyprinodon tularosa]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| ANKYR | COG0666 | Ankyrin repeat [Signal transduction mechanisms]; |
344-626 | 2.20e-59 | |||||
Ankyrin repeat [Signal transduction mechanisms]; : Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 207.11 E-value: 2.20e-59
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| ANKYR | COG0666 | Ankyrin repeat [Signal transduction mechanisms]; |
181-464 | 9.19e-57 | |||||
Ankyrin repeat [Signal transduction mechanisms]; : Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 199.80 E-value: 9.19e-57
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| ANKYR | COG0666 | Ankyrin repeat [Signal transduction mechanisms]; |
1124-1417 | 4.66e-55 | |||||
Ankyrin repeat [Signal transduction mechanisms]; : Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 194.79 E-value: 4.66e-55
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| KH-I_ANKHD1 | cd22503 | type I K homology (KH) RNA-binding domain found in ankyrin repeat and KH domain-containing ... |
1789-1871 | 8.52e-49 | |||||
type I K homology (KH) RNA-binding domain found in ankyrin repeat and KH domain-containing protein 1 (ANKHD1) and similar proteins; ANKHD1, also called HIV-1 Vpr-binding ankyrin repeat protein, or multiple ankyrin repeats single KH domain, or Hmask, is highly expressed in various cancer tissues and is involved in cancer progression, including proliferation and invasion. It acts as a scaffolding protein that may be associated with the abnormal phenotype of leukemia cells. It may play might have a role in MM cell proliferation and cell cycle progression by regulating expression of p21. It also regulates cell cycle progression and proliferation in multiple myeloma cells. ANKHD1 is a component of Hippo signaling pathway. It functions as a positive regulator of YAP1 and promotes cell growth and cell cycle progression through Cyclin A upregulation in prostate cancer cells. : Pssm-ID: 411931 Cd Length: 83 Bit Score: 168.77 E-value: 8.52e-49
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| Ank_2 | pfam12796 | Ankyrin repeats (3 copies); |
594-683 | 1.01e-14 | |||||
Ankyrin repeats (3 copies); : Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 71.69 E-value: 1.01e-14
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| PHA03247 super family | cl33720 | large tegument protein UL36; Provisional |
1969-2252 | 3.05e-10 | |||||
large tegument protein UL36; Provisional The actual alignment was detected with superfamily member PHA03247: Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 66.50 E-value: 3.05e-10
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| PRK03918 super family | cl35229 | DNA double-strand break repair ATPase Rad50; |
771-866 | 3.27e-05 | |||||
DNA double-strand break repair ATPase Rad50; The actual alignment was detected with superfamily member PRK03918: Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.68 E-value: 3.27e-05
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| TRPV super family | cl40437 | Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
1349-1501 | 1.43e-03 | |||||
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic). The actual alignment was detected with superfamily member cd22194: Pssm-ID: 454755 [Multi-domain] Cd Length: 680 Bit Score: 43.98 E-value: 1.43e-03
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| ANK | smart00248 | ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
1109-1137 | 3.99e-03 | |||||
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure. : Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 36.80 E-value: 3.99e-03
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| Name | Accession | Description | Interval | E-value | |||||||
| ANKYR | COG0666 | Ankyrin repeat [Signal transduction mechanisms]; |
344-626 | 2.20e-59 | |||||||
Ankyrin repeat [Signal transduction mechanisms]; Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 207.11 E-value: 2.20e-59
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| ANKYR | COG0666 | Ankyrin repeat [Signal transduction mechanisms]; |
181-464 | 9.19e-57 | |||||||
Ankyrin repeat [Signal transduction mechanisms]; Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 199.80 E-value: 9.19e-57
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| ANKYR | COG0666 | Ankyrin repeat [Signal transduction mechanisms]; |
1124-1417 | 4.66e-55 | |||||||
Ankyrin repeat [Signal transduction mechanisms]; Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 194.79 E-value: 4.66e-55
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| KH-I_ANKHD1 | cd22503 | type I K homology (KH) RNA-binding domain found in ankyrin repeat and KH domain-containing ... |
1789-1871 | 8.52e-49 | |||||||
type I K homology (KH) RNA-binding domain found in ankyrin repeat and KH domain-containing protein 1 (ANKHD1) and similar proteins; ANKHD1, also called HIV-1 Vpr-binding ankyrin repeat protein, or multiple ankyrin repeats single KH domain, or Hmask, is highly expressed in various cancer tissues and is involved in cancer progression, including proliferation and invasion. It acts as a scaffolding protein that may be associated with the abnormal phenotype of leukemia cells. It may play might have a role in MM cell proliferation and cell cycle progression by regulating expression of p21. It also regulates cell cycle progression and proliferation in multiple myeloma cells. ANKHD1 is a component of Hippo signaling pathway. It functions as a positive regulator of YAP1 and promotes cell growth and cell cycle progression through Cyclin A upregulation in prostate cancer cells. Pssm-ID: 411931 Cd Length: 83 Bit Score: 168.77 E-value: 8.52e-49
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| PHA03095 | PHA03095 | ankyrin-like protein; Provisional |
198-520 | 2.19e-27 | |||||||
ankyrin-like protein; Provisional Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 118.59 E-value: 2.19e-27
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| PHA03095 | PHA03095 | ankyrin-like protein; Provisional |
1124-1411 | 1.02e-26 | |||||||
ankyrin-like protein; Provisional Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 116.66 E-value: 1.02e-26
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| Ank_2 | pfam12796 | Ankyrin repeats (3 copies); |
263-353 | 1.57e-25 | |||||||
Ankyrin repeats (3 copies); Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 102.50 E-value: 1.57e-25
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| Ank_2 | pfam12796 | Ankyrin repeats (3 copies); |
528-618 | 6.84e-24 | |||||||
Ankyrin repeats (3 copies); Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 97.88 E-value: 6.84e-24
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| Ank_2 | pfam12796 | Ankyrin repeats (3 copies); |
1249-1340 | 6.73e-22 | |||||||
Ankyrin repeats (3 copies); Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 92.10 E-value: 6.73e-22
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| PHA03100 | PHA03100 | ankyrin repeat protein; Provisional |
208-423 | 1.21e-19 | |||||||
ankyrin repeat protein; Provisional Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 94.35 E-value: 1.21e-19
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| KH_1 | pfam00013 | KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ... |
1790-1854 | 2.01e-15 | |||||||
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause paraneoplastic opsoclonus ataxia. Pssm-ID: 459630 [Multi-domain] Cd Length: 65 Bit Score: 72.70 E-value: 2.01e-15
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| Ank_2 | pfam12796 | Ankyrin repeats (3 copies); |
594-683 | 1.01e-14 | |||||||
Ankyrin repeats (3 copies); Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 71.69 E-value: 1.01e-14
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| TRPV5-6 | cd22192 | Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
327-544 | 2.50e-11 | |||||||
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues. Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 69.27 E-value: 2.50e-11
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| PHA03247 | PHA03247 | large tegument protein UL36; Provisional |
1969-2252 | 3.05e-10 | |||||||
large tegument protein UL36; Provisional Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 66.50 E-value: 3.05e-10
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| KH | smart00322 | K homology RNA-binding domain; |
1792-1856 | 3.70e-10 | |||||||
K homology RNA-binding domain; Pssm-ID: 197652 [Multi-domain] Cd Length: 68 Bit Score: 58.08 E-value: 3.70e-10
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| Herpes_BLLF1 | pfam05109 | Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
1981-2397 | 6.09e-10 | |||||||
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: 64.94 E-value: 6.09e-10
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| TRPV5-6 | cd22192 | Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
1172-1400 | 2.64e-09 | |||||||
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues. Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 62.72 E-value: 2.64e-09
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| PTZ00322 | PTZ00322 | 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
594-706 | 5.90e-07 | |||||||
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 55.29 E-value: 5.90e-07
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| trp | TIGR00870 | transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
1135-1332 | 5.72e-06 | |||||||
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds] Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 52.01 E-value: 5.72e-06
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| TRPV5-6 | cd22192 | Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
196-351 | 6.12e-06 | |||||||
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues. Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 51.55 E-value: 6.12e-06
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| trp | TIGR00870 | transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
299-454 | 9.51e-06 | |||||||
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds] Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 51.24 E-value: 9.51e-06
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| ANK | smart00248 | ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
459-488 | 1.38e-05 | |||||||
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure. Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 43.73 E-value: 1.38e-05
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| trp | TIGR00870 | transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
190-449 | 3.14e-05 | |||||||
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds] Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 49.69 E-value: 3.14e-05
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| PRK03918 | PRK03918 | DNA double-strand break repair ATPase Rad50; |
771-866 | 3.27e-05 | |||||||
DNA double-strand break repair ATPase Rad50; Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.68 E-value: 3.27e-05
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| ANK | smart00248 | ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
324-352 | 4.76e-05 | |||||||
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure. Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 42.19 E-value: 4.76e-05
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| ANK | smart00248 | ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
1245-1273 | 7.12e-05 | |||||||
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure. Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 41.80 E-value: 7.12e-05
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| Caldesmon | pfam02029 | Caldesmon; |
779-866 | 3.88e-04 | |||||||
Caldesmon; Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 45.63 E-value: 3.88e-04
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| YhaN | COG4717 | Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
778-867 | 5.95e-04 | |||||||
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 5.95e-04
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| TRPV3 | cd22194 | Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
1349-1501 | 1.43e-03 | |||||||
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. Pssm-ID: 411978 [Multi-domain] Cd Length: 680 Bit Score: 43.98 E-value: 1.43e-03
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| SMC_prok_B | TIGR02168 | chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
773-867 | 3.46e-03 | |||||||
chromosome segregation protein SMC, common bacterial 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. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins] Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.12 E-value: 3.46e-03
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| ANK | smart00248 | ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
1109-1137 | 3.99e-03 | |||||||
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure. Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 36.80 E-value: 3.99e-03
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| F-BAR_CIP4-like | cd07653 | The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Cdc42-Interacting Protein 4 ... |
812-866 | 9.16e-03 | |||||||
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Cdc42-Interacting Protein 4 and similar proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. This subfamily is composed of Cdc42-Interacting Protein 4 (CIP4), Formin Binding Protein 17 (FBP17), FormiN Binding Protein 1-Like (FNBP1L), and similar proteins. CIP4 and FNBP1L are Cdc42 effectors that bind Wiskott-Aldrich syndrome protein (WASP) and function in endocytosis. CIP4 and FBP17 bind to the Fas ligand and may be implicated in the inflammatory response. CIP4 may also play a role in phagocytosis. Members of this subfamily typically contain an N-terminal F-BAR domain and a C-terminal SH3 domain. In addition, some members such as FNBP1L contain a central Cdc42-binding HR1 domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules. Pssm-ID: 153337 [Multi-domain] Cd Length: 251 Bit Score: 40.31 E-value: 9.16e-03
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| Name | Accession | Description | Interval | E-value | ||||||||
| ANKYR | COG0666 | Ankyrin repeat [Signal transduction mechanisms]; |
344-626 | 2.20e-59 | ||||||||
Ankyrin repeat [Signal transduction mechanisms]; Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 207.11 E-value: 2.20e-59
|
||||||||||||
| ANKYR | COG0666 | Ankyrin repeat [Signal transduction mechanisms]; |
407-683 | 2.11e-58 | ||||||||
Ankyrin repeat [Signal transduction mechanisms]; Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 204.42 E-value: 2.11e-58
|
||||||||||||
| ANKYR | COG0666 | Ankyrin repeat [Signal transduction mechanisms]; |
244-523 | 5.80e-58 | ||||||||
Ankyrin repeat [Signal transduction mechanisms]; Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 203.26 E-value: 5.80e-58
|
||||||||||||
| ANKYR | COG0666 | Ankyrin repeat [Signal transduction mechanisms]; |
403-659 | 6.83e-58 | ||||||||
Ankyrin repeat [Signal transduction mechanisms]; Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 202.88 E-value: 6.83e-58
|
||||||||||||
| ANKYR | COG0666 | Ankyrin repeat [Signal transduction mechanisms]; |
181-464 | 9.19e-57 | ||||||||
Ankyrin repeat [Signal transduction mechanisms]; Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 199.80 E-value: 9.19e-57
|
||||||||||||
| ANKYR | COG0666 | Ankyrin repeat [Signal transduction mechanisms]; |
306-594 | 1.19e-55 | ||||||||
Ankyrin repeat [Signal transduction mechanisms]; Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 196.33 E-value: 1.19e-55
|
||||||||||||
| ANKYR | COG0666 | Ankyrin repeat [Signal transduction mechanisms]; |
1124-1417 | 4.66e-55 | ||||||||
Ankyrin repeat [Signal transduction mechanisms]; Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 194.79 E-value: 4.66e-55
|
||||||||||||
| ANKYR | COG0666 | Ankyrin repeat [Signal transduction mechanisms]; |
272-561 | 7.18e-55 | ||||||||
Ankyrin repeat [Signal transduction mechanisms]; Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 194.40 E-value: 7.18e-55
|
||||||||||||
| ANKYR | COG0666 | Ankyrin repeat [Signal transduction mechanisms]; |
139-425 | 1.38e-54 | ||||||||
Ankyrin repeat [Signal transduction mechanisms]; Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 193.25 E-value: 1.38e-54
|
||||||||||||
| ANKYR | COG0666 | Ankyrin repeat [Signal transduction mechanisms]; |
1162-1435 | 1.56e-53 | ||||||||
Ankyrin repeat [Signal transduction mechanisms]; Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 190.55 E-value: 1.56e-53
|
||||||||||||
| ANKYR | COG0666 | Ankyrin repeat [Signal transduction mechanisms]; |
1093-1384 | 1.83e-52 | ||||||||
Ankyrin repeat [Signal transduction mechanisms]; Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 187.47 E-value: 1.83e-52
|
||||||||||||
| ANKYR | COG0666 | Ankyrin repeat [Signal transduction mechanisms]; |
1191-1434 | 4.61e-49 | ||||||||
Ankyrin repeat [Signal transduction mechanisms]; Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 177.45 E-value: 4.61e-49
|
||||||||||||
| ANKYR | COG0666 | Ankyrin repeat [Signal transduction mechanisms]; |
134-396 | 4.93e-49 | ||||||||
Ankyrin repeat [Signal transduction mechanisms]; Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 177.45 E-value: 4.93e-49
|
||||||||||||
| KH-I_ANKHD1 | cd22503 | type I K homology (KH) RNA-binding domain found in ankyrin repeat and KH domain-containing ... |
1789-1871 | 8.52e-49 | ||||||||
type I K homology (KH) RNA-binding domain found in ankyrin repeat and KH domain-containing protein 1 (ANKHD1) and similar proteins; ANKHD1, also called HIV-1 Vpr-binding ankyrin repeat protein, or multiple ankyrin repeats single KH domain, or Hmask, is highly expressed in various cancer tissues and is involved in cancer progression, including proliferation and invasion. It acts as a scaffolding protein that may be associated with the abnormal phenotype of leukemia cells. It may play might have a role in MM cell proliferation and cell cycle progression by regulating expression of p21. It also regulates cell cycle progression and proliferation in multiple myeloma cells. ANKHD1 is a component of Hippo signaling pathway. It functions as a positive regulator of YAP1 and promotes cell growth and cell cycle progression through Cyclin A upregulation in prostate cancer cells. Pssm-ID: 411931 Cd Length: 83 Bit Score: 168.77 E-value: 8.52e-49
|
||||||||||||
| ANKYR | COG0666 | Ankyrin repeat [Signal transduction mechanisms]; |
1225-1434 | 3.90e-42 | ||||||||
Ankyrin repeat [Signal transduction mechanisms]; Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 157.42 E-value: 3.90e-42
|
||||||||||||
| KH-I_MASK | cd22404 | type I K homology (KH) RNA-binding domain found in Mask family proteins; The Mask family ... |
1789-1859 | 2.32e-33 | ||||||||
type I K homology (KH) RNA-binding domain found in Mask family proteins; The Mask family includes Drosophila melanogaster ankyrin repeat and KH domain-containing protein Mask, and its mammalian homologues Mask1/ANKHD1 and Mask2/ANKRD17. Mask, also called multiple ankyrin repeat single KH domain-containing protein, is a large ankyrin repeat and KH domain-containing protein involved in Drosophila receptor tyrosine kinase signaling. It acts as a mediator of receptor tyrosine kinase (RTK) signaling and may act either downstream of MAPK or transduce signaling through a parallel branch of the RTK pathway. Mask is required for the development and organization of indirect flight muscle sarcomeres by regulating the formation of M line and H zone and the correct assembly of thick and thin filaments in the sarcomere. Mask1/ANKHD1, also called HIV-1 Vpr-binding ankyrin repeat protein, or multiple ankyrin repeats single KH domain, or Hmask, is highly expressed in various cancer tissues and is involved in cancer progression, including proliferation and invasion. Mask2/ANKRD17, also called ankyrin repeat protein 17, or gene trap ankyrin repeat protein (GTAR), or serologically defined breast cancer antigen NY-BR-16, is a ubiquitously expressed ankyrin factor essential for the vascular integrity during embryogenesis. It may be directly involved in the DNA replication process and play pivotal roles in cell cycle and DNA regulation. It is also involved in innate immune defense against bacteria and viruses. Pssm-ID: 411832 [Multi-domain] Cd Length: 71 Bit Score: 124.24 E-value: 2.32e-33
|
||||||||||||
| KH-I_ANKRD17 | cd22502 | type I K homology (KH) RNA-binding domain found in ankyrin repeat domain-containing protein 17 ... |
1789-1859 | 3.13e-33 | ||||||||
type I K homology (KH) RNA-binding domain found in ankyrin repeat domain-containing protein 17 (ANKRD17) and similar proteins; ANKRD17, also called ankyrin repeat protein 17, or gene trap ankyrin repeat protein (GTAR), or serologically defined breast cancer antigen NY-BR-16, is a ubiquitously expressed ankyrin factor essential for the vascular integrity during embryogenesis. It may be directly involved in the DNA replication process and play pivotal roles in cell cycle and DNA regulation. It is also involved in innate immune defense against bacteria and viruses. Pssm-ID: 411930 [Multi-domain] Cd Length: 71 Bit Score: 123.71 E-value: 3.13e-33
|
||||||||||||
| PHA03095 | PHA03095 | ankyrin-like protein; Provisional |
198-520 | 2.19e-27 | ||||||||
ankyrin-like protein; Provisional Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 118.59 E-value: 2.19e-27
|
||||||||||||
| PHA03095 | PHA03095 | ankyrin-like protein; Provisional |
1124-1411 | 1.02e-26 | ||||||||
ankyrin-like protein; Provisional Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 116.66 E-value: 1.02e-26
|
||||||||||||
| PHA03095 | PHA03095 | ankyrin-like protein; Provisional |
1191-1420 | 9.35e-26 | ||||||||
ankyrin-like protein; Provisional Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 113.58 E-value: 9.35e-26
|
||||||||||||
| PHA03100 | PHA03100 | ankyrin repeat protein; Provisional |
1179-1467 | 1.39e-25 | ||||||||
ankyrin repeat protein; Provisional Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 112.45 E-value: 1.39e-25
|
||||||||||||
| Ank_2 | pfam12796 | Ankyrin repeats (3 copies); |
263-353 | 1.57e-25 | ||||||||
Ankyrin repeats (3 copies); Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 102.50 E-value: 1.57e-25
|
||||||||||||
| PHA03100 | PHA03100 | ankyrin repeat protein; Provisional |
407-585 | 5.04e-25 | ||||||||
ankyrin repeat protein; Provisional Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 110.91 E-value: 5.04e-25
|
||||||||||||
| Ank_2 | pfam12796 | Ankyrin repeats (3 copies); |
528-618 | 6.84e-24 | ||||||||
Ankyrin repeats (3 copies); Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 97.88 E-value: 6.84e-24
|
||||||||||||
| PHA03095 | PHA03095 | ankyrin-like protein; Provisional |
354-664 | 1.07e-22 | ||||||||
ankyrin-like protein; Provisional Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 104.34 E-value: 1.07e-22
|
||||||||||||
| PHA02876 | PHA02876 | ankyrin repeat protein; Provisional |
184-583 | 1.65e-22 | ||||||||
ankyrin repeat protein; Provisional Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 105.53 E-value: 1.65e-22
|
||||||||||||
| Ank_2 | pfam12796 | Ankyrin repeats (3 copies); |
296-388 | 4.48e-22 | ||||||||
Ankyrin repeats (3 copies); Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 92.49 E-value: 4.48e-22
|
||||||||||||
| Ank_2 | pfam12796 | Ankyrin repeats (3 copies); |
1249-1340 | 6.73e-22 | ||||||||
Ankyrin repeats (3 copies); Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 92.10 E-value: 6.73e-22
|
||||||||||||
| PHA03100 | PHA03100 | ankyrin repeat protein; Provisional |
247-488 | 7.09e-22 | ||||||||
ankyrin repeat protein; Provisional Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 101.28 E-value: 7.09e-22
|
||||||||||||
| PHA03095 | PHA03095 | ankyrin-like protein; Provisional |
244-612 | 1.71e-20 | ||||||||
ankyrin-like protein; Provisional Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 97.79 E-value: 1.71e-20
|
||||||||||||
| PHA03095 | PHA03095 | ankyrin-like protein; Provisional |
264-652 | 2.70e-20 | ||||||||
ankyrin-like protein; Provisional Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 97.02 E-value: 2.70e-20
|
||||||||||||
| Ank_2 | pfam12796 | Ankyrin repeats (3 copies); |
1214-1308 | 3.43e-20 | ||||||||
Ankyrin repeats (3 copies); Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 87.09 E-value: 3.43e-20
|
||||||||||||
| Ank_2 | pfam12796 | Ankyrin repeats (3 copies); |
396-489 | 3.50e-20 | ||||||||
Ankyrin repeats (3 copies); Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 87.09 E-value: 3.50e-20
|
||||||||||||
| Ank_2 | pfam12796 | Ankyrin repeats (3 copies); |
464-553 | 5.31e-20 | ||||||||
Ankyrin repeats (3 copies); Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 86.71 E-value: 5.31e-20
|
||||||||||||
| PHA03100 | PHA03100 | ankyrin repeat protein; Provisional |
208-423 | 1.21e-19 | ||||||||
ankyrin repeat protein; Provisional Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 94.35 E-value: 1.21e-19
|
||||||||||||
| Ank_2 | pfam12796 | Ankyrin repeats (3 copies); |
1181-1274 | 1.23e-19 | ||||||||
Ankyrin repeats (3 copies); Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 85.55 E-value: 1.23e-19
|
||||||||||||
| Ank_2 | pfam12796 | Ankyrin repeats (3 copies); |
431-522 | 1.35e-19 | ||||||||
Ankyrin repeats (3 copies); Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 85.55 E-value: 1.35e-19
|
||||||||||||
| PHA02876 | PHA02876 | ankyrin repeat protein; Provisional |
309-679 | 1.45e-19 | ||||||||
ankyrin repeat protein; Provisional Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 95.90 E-value: 1.45e-19
|
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| Ank_2 | pfam12796 | Ankyrin repeats (3 copies); |
1351-1434 | 1.08e-18 | ||||||||
Ankyrin repeats (3 copies); Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 82.86 E-value: 1.08e-18
|
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| Ank_2 | pfam12796 | Ankyrin repeats (3 copies); |
196-288 | 2.66e-18 | ||||||||
Ankyrin repeats (3 copies); Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 82.09 E-value: 2.66e-18
|
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| PHA03095 | PHA03095 | ankyrin-like protein; Provisional |
474-696 | 4.12e-18 | ||||||||
ankyrin-like protein; Provisional Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 90.08 E-value: 4.12e-18
|
||||||||||||
| PHA02876 | PHA02876 | ankyrin repeat protein; Provisional |
1112-1421 | 4.63e-18 | ||||||||
ankyrin repeat protein; Provisional Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 91.28 E-value: 4.63e-18
|
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| PHA03100 | PHA03100 | ankyrin repeat protein; Provisional |
1124-1277 | 5.14e-18 | ||||||||
ankyrin repeat protein; Provisional Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 89.34 E-value: 5.14e-18
|
||||||||||||
| PHA02874 | PHA02874 | ankyrin repeat protein; Provisional |
1153-1472 | 5.41e-18 | ||||||||
ankyrin repeat protein; Provisional Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 89.64 E-value: 5.41e-18
|
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| Ank_2 | pfam12796 | Ankyrin repeats (3 copies); |
1114-1207 | 1.36e-17 | ||||||||
Ankyrin repeats (3 copies); Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 79.77 E-value: 1.36e-17
|
||||||||||||
| Ank_2 | pfam12796 | Ankyrin repeats (3 copies); |
1316-1410 | 1.40e-17 | ||||||||
Ankyrin repeats (3 copies); Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 79.77 E-value: 1.40e-17
|
||||||||||||
| Ank_2 | pfam12796 | Ankyrin repeats (3 copies); |
1283-1377 | 2.83e-17 | ||||||||
Ankyrin repeats (3 copies); Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 79.00 E-value: 2.83e-17
|
||||||||||||
| PLN03192 | PLN03192 | Voltage-dependent potassium channel; Provisional |
263-433 | 2.68e-16 | ||||||||
Voltage-dependent potassium channel; Provisional Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 85.69 E-value: 2.68e-16
|
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| PHA02875 | PHA02875 | ankyrin repeat protein; Provisional |
204-400 | 3.66e-16 | ||||||||
ankyrin repeat protein; Provisional Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 83.50 E-value: 3.66e-16
|
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| PHA02874 | PHA02874 | ankyrin repeat protein; Provisional |
264-594 | 6.98e-16 | ||||||||
ankyrin repeat protein; Provisional Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 83.09 E-value: 6.98e-16
|
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| PHA03095 | PHA03095 | ankyrin-like protein; Provisional |
1101-1343 | 9.35e-16 | ||||||||
ankyrin-like protein; Provisional Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 82.77 E-value: 9.35e-16
|
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| PHA02875 | PHA02875 | ankyrin repeat protein; Provisional |
266-500 | 1.53e-15 | ||||||||
ankyrin repeat protein; Provisional Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 81.58 E-value: 1.53e-15
|
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| KH_1 | pfam00013 | KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ... |
1790-1854 | 2.01e-15 | ||||||||
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause paraneoplastic opsoclonus ataxia. Pssm-ID: 459630 [Multi-domain] Cd Length: 65 Bit Score: 72.70 E-value: 2.01e-15
|
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| PHA02875 | PHA02875 | ankyrin repeat protein; Provisional |
1112-1304 | 2.15e-15 | ||||||||
ankyrin repeat protein; Provisional Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 81.19 E-value: 2.15e-15
|
||||||||||||
| PHA03095 | PHA03095 | ankyrin-like protein; Provisional |
1291-1434 | 9.70e-15 | ||||||||
ankyrin-like protein; Provisional Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 79.68 E-value: 9.70e-15
|
||||||||||||
| Ank_2 | pfam12796 | Ankyrin repeats (3 copies); |
594-683 | 1.01e-14 | ||||||||
Ankyrin repeats (3 copies); Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 71.69 E-value: 1.01e-14
|
||||||||||||
| PHA02875 | PHA02875 | ankyrin repeat protein; Provisional |
295-519 | 1.82e-14 | ||||||||
ankyrin repeat protein; Provisional Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 78.49 E-value: 1.82e-14
|
||||||||||||
| KH-I | cd00105 | K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found ... |
1791-1853 | 2.29e-14 | ||||||||
K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found in a wide variety of proteins including ribosomal proteins, transcription factors and post-transcriptional modifiers of mRNA. There are two different KH domains that belong to different protein folds, but they share a single KH motif. The KH motif is folded into a beta alpha alpha beta unit. In addition to the core, type II KH domains (e.g. ribosomal protein S3) include an N-terminal extension and type I KH domains (e.g. hnRNP K) contain a C-terminal extension. Some KH-I superfamily members contain a divergent KH domain that lacks the RNA-binding GXXG motif. Some others have a mutated GXXG motif which may or may not have nucleic acid binding ability. Pssm-ID: 411802 [Multi-domain] Cd Length: 63 Bit Score: 69.63 E-value: 2.29e-14
|
||||||||||||
| PHA02875 | PHA02875 | ankyrin repeat protein; Provisional |
1179-1371 | 2.35e-14 | ||||||||
ankyrin repeat protein; Provisional Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 78.11 E-value: 2.35e-14
|
||||||||||||
| PHA02878 | PHA02878 | ankyrin repeat protein; Provisional |
1093-1449 | 2.60e-14 | ||||||||
ankyrin repeat protein; Provisional Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 78.38 E-value: 2.60e-14
|
||||||||||||
| PHA02876 | PHA02876 | ankyrin repeat protein; Provisional |
1102-1373 | 4.13e-14 | ||||||||
ankyrin repeat protein; Provisional Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 78.57 E-value: 4.13e-14
|
||||||||||||
| PHA02875 | PHA02875 | ankyrin repeat protein; Provisional |
405-649 | 1.90e-13 | ||||||||
ankyrin repeat protein; Provisional Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 75.03 E-value: 1.90e-13
|
||||||||||||
| PHA02874 | PHA02874 | ankyrin repeat protein; Provisional |
438-664 | 2.71e-13 | ||||||||
ankyrin repeat protein; Provisional Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 75.00 E-value: 2.71e-13
|
||||||||||||
| PHA02875 | PHA02875 | ankyrin repeat protein; Provisional |
1184-1405 | 3.15e-13 | ||||||||
ankyrin repeat protein; Provisional Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 74.64 E-value: 3.15e-13
|
||||||||||||
| PHA02875 | PHA02875 | ankyrin repeat protein; Provisional |
229-452 | 1.04e-12 | ||||||||
ankyrin repeat protein; Provisional Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 72.72 E-value: 1.04e-12
|
||||||||||||
| PHA02878 | PHA02878 | ankyrin repeat protein; Provisional |
262-520 | 1.06e-12 | ||||||||
ankyrin repeat protein; Provisional Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 73.38 E-value: 1.06e-12
|
||||||||||||
| PHA02874 | PHA02874 | ankyrin repeat protein; Provisional |
401-616 | 1.17e-12 | ||||||||
ankyrin repeat protein; Provisional Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 72.69 E-value: 1.17e-12
|
||||||||||||
| PHA02878 | PHA02878 | ankyrin repeat protein; Provisional |
196-434 | 1.20e-12 | ||||||||
ankyrin repeat protein; Provisional Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 72.99 E-value: 1.20e-12
|
||||||||||||
| KH-I_HEN4_like_rpt5 | cd22462 | fifth type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana KH ... |
1792-1856 | 1.38e-12 | ||||||||
fifth type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana KH domain-containing protein HEN4 and similar protein; HEN4, also called protein HUA ENHANCER 4, plays a role in floral reproductive organ identity in the third whorl and floral determinacy specification by specifically promoting the processing of AGAMOUS (AG) pre-mRNA. It functions in association with HUA1 and HUA2. HEN4 contains five K-homology (KH) RNA-binding domains. The model corresponds to the KH5 domain of HEN4. Pssm-ID: 411890 [Multi-domain] Cd Length: 66 Bit Score: 64.58 E-value: 1.38e-12
|
||||||||||||
| Ank_2 | pfam12796 | Ankyrin repeats (3 copies); |
1096-1172 | 2.97e-12 | ||||||||
Ankyrin repeats (3 copies); Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 64.75 E-value: 2.97e-12
|
||||||||||||
| PHA02876 | PHA02876 | ankyrin repeat protein; Provisional |
1192-1446 | 4.10e-12 | ||||||||
ankyrin repeat protein; Provisional Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 72.02 E-value: 4.10e-12
|
||||||||||||
| PLN03192 | PLN03192 | Voltage-dependent potassium channel; Provisional |
261-387 | 5.25e-12 | ||||||||
Voltage-dependent potassium channel; Provisional Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 71.82 E-value: 5.25e-12
|
||||||||||||
| PHA03100 | PHA03100 | ankyrin repeat protein; Provisional |
446-683 | 6.82e-12 | ||||||||
ankyrin repeat protein; Provisional Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 70.46 E-value: 6.82e-12
|
||||||||||||
| PHA02875 | PHA02875 | ankyrin repeat protein; Provisional |
1217-1434 | 7.92e-12 | ||||||||
ankyrin repeat protein; Provisional Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 70.02 E-value: 7.92e-12
|
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| PHA02878 | PHA02878 | ankyrin repeat protein; Provisional |
194-384 | 1.10e-11 | ||||||||
ankyrin repeat protein; Provisional Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 69.91 E-value: 1.10e-11
|
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| Ank_4 | pfam13637 | Ankyrin repeats (many copies); |
524-577 | 1.21e-11 | ||||||||
Ankyrin repeats (many copies); Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 61.52 E-value: 1.21e-11
|
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| PLN03192 | PLN03192 | Voltage-dependent potassium channel; Provisional |
498-707 | 1.39e-11 | ||||||||
Voltage-dependent potassium channel; Provisional Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 70.28 E-value: 1.39e-11
|
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| PLN03192 | PLN03192 | Voltage-dependent potassium channel; Provisional |
407-587 | 1.81e-11 | ||||||||
Voltage-dependent potassium channel; Provisional Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 69.90 E-value: 1.81e-11
|
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| TRPV5-6 | cd22192 | Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
327-544 | 2.50e-11 | ||||||||
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues. Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 69.27 E-value: 2.50e-11
|
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| TRPV5-6 | cd22192 | Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
525-661 | 2.59e-11 | ||||||||
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues. Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 69.27 E-value: 2.59e-11
|
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| Ank_4 | pfam13637 | Ankyrin repeats (many copies); |
261-312 | 4.14e-11 | ||||||||
Ankyrin repeats (many copies); Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 59.98 E-value: 4.14e-11
|
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| KH-I_PCBP_rpt3 | cd22439 | third type I K homology (KH) RNA-binding domain found in the family of poly(C)-binding ... |
1790-1855 | 4.17e-11 | ||||||||
third type I K homology (KH) RNA-binding domain found in the family of poly(C)-binding proteins (PCBPs); The PCBP family, also known as hnRNP E family, comprises four members, PCBP1-4, which are RNA-binding proteins that interact in a sequence-specific manner with single-stranded poly(C) sequences. They are mainly involved in various posttranscriptional regulations, including mRNA stabilization or translational activation/silencing. Besides, PCBPs may share iron chaperone activity. PCBPs contain three K-homology (KH) RNA-binding domains. The model corresponds to the third one. Pssm-ID: 411867 [Multi-domain] Cd Length: 68 Bit Score: 60.71 E-value: 4.17e-11
|
||||||||||||
| PHA02798 | PHA02798 | ankyrin-like protein; Provisional |
272-491 | 6.30e-11 | ||||||||
ankyrin-like protein; Provisional Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 67.55 E-value: 6.30e-11
|
||||||||||||
| PHA03100 | PHA03100 | ankyrin repeat protein; Provisional |
203-324 | 6.69e-11 | ||||||||
ankyrin repeat protein; Provisional Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 67.00 E-value: 6.69e-11
|
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| KH-I_TDRKH_rpt2 | cd22429 | second type I K homology (KH) RNA-binding domain found in tudor and KH domain-containing ... |
1790-1866 | 6.96e-11 | ||||||||
second type I K homology (KH) RNA-binding domain found in tudor and KH domain-containing protein (TDRKH) and similar proteins; TDRKH, also called tudor domain-containing protein 2 (TDRD2), is a mitochondria-anchored RNA-binding protein that is required for spermatogenesis and involved in piRNA biogenesis. It specifically recruits MIWI, but not MILI, to engage the piRNA pathway. TDRKH contains two K-homology (KH) RNA-binding domains and one tudor domain, which are involved in binding to RNA or single-strand DNA. The model corresponds to the second one. Pssm-ID: 411857 [Multi-domain] Cd Length: 82 Bit Score: 60.43 E-value: 6.96e-11
|
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| PHA02878 | PHA02878 | ankyrin repeat protein; Provisional |
305-564 | 7.26e-11 | ||||||||
ankyrin repeat protein; Provisional Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 67.21 E-value: 7.26e-11
|
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| PHA02876 | PHA02876 | ankyrin repeat protein; Provisional |
1091-1338 | 8.80e-11 | ||||||||
ankyrin repeat protein; Provisional Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 67.78 E-value: 8.80e-11
|
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| PHA02875 | PHA02875 | ankyrin repeat protein; Provisional |
1278-1434 | 1.21e-10 | ||||||||
ankyrin repeat protein; Provisional Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 66.17 E-value: 1.21e-10
|
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| PHA03247 | PHA03247 | large tegument protein UL36; Provisional |
1969-2252 | 3.05e-10 | ||||||||
large tegument protein UL36; Provisional Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 66.50 E-value: 3.05e-10
|
||||||||||||
| PLN03192 | PLN03192 | Voltage-dependent potassium channel; Provisional |
507-677 | 3.61e-10 | ||||||||
Voltage-dependent potassium channel; Provisional Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 65.66 E-value: 3.61e-10
|
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| KH | smart00322 | K homology RNA-binding domain; |
1792-1856 | 3.70e-10 | ||||||||
K homology RNA-binding domain; Pssm-ID: 197652 [Multi-domain] Cd Length: 68 Bit Score: 58.08 E-value: 3.70e-10
|
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| Herpes_BLLF1 | pfam05109 | Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
1981-2397 | 6.09e-10 | ||||||||
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: 64.94 E-value: 6.09e-10
|
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| Ank_4 | pfam13637 | Ankyrin repeats (many copies); |
1347-1400 | 6.59e-10 | ||||||||
Ankyrin repeats (many copies); Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 56.90 E-value: 6.59e-10
|
||||||||||||
| PHA03100 | PHA03100 | ankyrin repeat protein; Provisional |
1121-1237 | 7.96e-10 | ||||||||
ankyrin repeat protein; Provisional Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 63.92 E-value: 7.96e-10
|
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| Ank_4 | pfam13637 | Ankyrin repeats (many copies); |
325-379 | 8.93e-10 | ||||||||
Ankyrin repeats (many copies); Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 56.51 E-value: 8.93e-10
|
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| Ank_2 | pfam12796 | Ankyrin repeats (3 copies); |
1384-1438 | 1.03e-09 | ||||||||
Ankyrin repeats (3 copies); Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 57.43 E-value: 1.03e-09
|
||||||||||||
| PHA03247 | PHA03247 | large tegument protein UL36; Provisional |
1967-2307 | 1.50e-09 | ||||||||
large tegument protein UL36; Provisional Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 64.19 E-value: 1.50e-09
|
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| Ank_4 | pfam13637 | Ankyrin repeats (many copies); |
1110-1163 | 1.62e-09 | ||||||||
Ankyrin repeats (many copies); Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 55.74 E-value: 1.62e-09
|
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| PHA02989 | PHA02989 | ankyrin repeat protein; Provisional |
271-578 | 1.81e-09 | ||||||||
ankyrin repeat protein; Provisional Pssm-ID: 222954 [Multi-domain] Cd Length: 494 Bit Score: 62.84 E-value: 1.81e-09
|
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| Atrophin-1 | pfam03154 | Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
1997-2497 | 1.88e-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: 63.63 E-value: 1.88e-09
|
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| PHA02874 | PHA02874 | ankyrin repeat protein; Provisional |
208-332 | 1.96e-09 | ||||||||
ankyrin repeat protein; Provisional Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 62.67 E-value: 1.96e-09
|
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| PLN03192 | PLN03192 | Voltage-dependent potassium channel; Provisional |
187-365 | 2.54e-09 | ||||||||
Voltage-dependent potassium channel; Provisional Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 62.96 E-value: 2.54e-09
|
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| TRPV5-6 | cd22192 | Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
1172-1400 | 2.64e-09 | ||||||||
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues. Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 62.72 E-value: 2.64e-09
|
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| Ank_4 | pfam13637 | Ankyrin repeats (many copies); |
1380-1433 | 2.70e-09 | ||||||||
Ankyrin repeats (many copies); Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 54.97 E-value: 2.70e-09
|
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| Ank_4 | pfam13637 | Ankyrin repeats (many copies); |
429-480 | 4.44e-09 | ||||||||
Ankyrin repeats (many copies); Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 54.59 E-value: 4.44e-09
|
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| Ank_4 | pfam13637 | Ankyrin repeats (many copies); |
557-610 | 6.20e-09 | ||||||||
Ankyrin repeats (many copies); Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 53.82 E-value: 6.20e-09
|
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| PTZ00322 | PTZ00322 | 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
1088-1197 | 7.45e-09 | ||||||||
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 61.45 E-value: 7.45e-09
|
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| PHA02874 | PHA02874 | ankyrin repeat protein; Provisional |
196-356 | 8.74e-09 | ||||||||
ankyrin repeat protein; Provisional Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 60.36 E-value: 8.74e-09
|
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| Ank_4 | pfam13637 | Ankyrin repeats (many copies); |
626-677 | 8.91e-09 | ||||||||
Ankyrin repeats (many copies); Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 53.43 E-value: 8.91e-09
|
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| TRPV5-6 | cd22192 | Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
1247-1434 | 9.81e-09 | ||||||||
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues. Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 60.80 E-value: 9.81e-09
|
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| KH-I_NOVA_rpt3 | cd09031 | third type I K homology (KH) RNA-binding domain found in the family of neuro-oncological ... |
1791-1852 | 1.25e-08 | ||||||||
third type I K homology (KH) RNA-binding domain found in the family of neuro-oncological ventral antigen (Nova); The family includes two related neuronal RNA-binding proteins, Nova-1 and Nova-2. Nova-1, also called onconeural ventral antigen 1, or paraneoplastic Ri antigen, or ventral neuron-specific protein 1, may regulate RNA splicing or metabolism in a specific subset of developing neurons. It interacts with RNA containing repeats of the YCAY sequence. It is a brain-enriched splicing factor regulating neuronal alternative splicing. Nova-1 is involved in neurological disorders and carcinogenesis. Nova-2, also called astrocytic NOVA1-like RNA-binding protein, is a neuronal RNA-binding protein expressed in a broader central nervous system (CNS) distribution than Nova-1. It functions in neuronal RNA metabolism. NOVA family proteins contain three K-homology (KH) RNA-binding domains. The model corresponds to the third one. Pssm-ID: 411807 [Multi-domain] Cd Length: 71 Bit Score: 53.74 E-value: 1.25e-08
|
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| PHA02878 | PHA02878 | ankyrin repeat protein; Provisional |
304-650 | 1.27e-08 | ||||||||
ankyrin repeat protein; Provisional Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 60.28 E-value: 1.27e-08
|
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| KH-I_FUBP_rpt4 | cd22399 | fourth type I K homology (KH) RNA-binding domain found in the FUBP family RNA/DNA-binding ... |
1794-1853 | 1.48e-08 | ||||||||
fourth type I K homology (KH) RNA-binding domain found in the FUBP family RNA/DNA-binding proteins; The far upstream element-binding protein (FUBP) family includes FUBP1-3. FUBP1, also called FBP, or FUSE-binding protein 1, or DNA helicase V, or DH V, binds RNA and single-stranded DNA (ssDNA) and may act both as activator and repressor of transcription. It regulates MYC expression by binding to a single-stranded far-upstream element (FUSE) upstream of the MYC promoter. FUBP2, also called FUSE-binding protein 2, or KH type-splicing regulatory protein (KSRP), or p75, is a single-strand nucleic acid binding protein implicated in a variety of cellular processes, including splicing in the nucleus, mRNA decay, maturation of miRNA, and transcriptional control of proto-oncogenes such as c-myc. It regulates the stability and/or translatability of many mRNA species, encoding immune-relevant proteins, either by binding to AU-rich elements (AREs) of mRNA 3'UTR or by facilitating miRNA biogenesis to target mRNA. FUBP3, also called FUSE-binding protein 3, or MARTA2, was previously shown to mediate dendritic targeting of MAP2 mRNA in neurons. It may interact with single-stranded DNA from the far-upstream element (FUSE) and activate gene expression. It is required for beta-actin mRNA localization. It also interacts with fibroblast growth factor 9 (FGF9) 3'-UTR UG repeats and positively controls FGF9 expression through increasing translation of FGF9 mRNA. FUBP proteins contain four K-homology (KH) RNA-binding domains. The model corresponds to the fourth one. Pssm-ID: 411827 [Multi-domain] Cd Length: 67 Bit Score: 53.38 E-value: 1.48e-08
|
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| PLN03192 | PLN03192 | Voltage-dependent potassium channel; Provisional |
1247-1410 | 1.72e-08 | ||||||||
Voltage-dependent potassium channel; Provisional Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 60.27 E-value: 1.72e-08
|
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| PTZ00322 | PTZ00322 | 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
1216-1318 | 1.79e-08 | ||||||||
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 59.91 E-value: 1.79e-08
|
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| Ank_4 | pfam13637 | Ankyrin repeats (many copies); |
292-345 | 1.93e-08 | ||||||||
Ankyrin repeats (many copies); Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 52.66 E-value: 1.93e-08
|
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| KH-I_ScSCP160_rpt1 | cd22446 | first type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ... |
1788-1858 | 2.51e-08 | ||||||||
first type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein SCP160 and similar proteins; SCP160, also called protein HX, is a new yeast protein associated with the nuclear membrane and the endoplasmic reticulum. It is involved in the control of mitotic chromosome transmission. It is required during cell division for faithful partitioning of the ER-nuclear envelope membranes which enclose the duplicated chromosomes in yeast. SCP160 contains seven K-homology (KH) RNA-binding domains. The model corresponds to the first one. Pssm-ID: 411874 [Multi-domain] Cd Length: 86 Bit Score: 53.18 E-value: 2.51e-08
|
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| Ank_4 | pfam13637 | Ankyrin repeats (many copies); |
460-514 | 2.72e-08 | ||||||||
Ankyrin repeats (many copies); Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 52.28 E-value: 2.72e-08
|
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| PHA02989 | PHA02989 | ankyrin repeat protein; Provisional |
1191-1429 | 3.51e-08 | ||||||||
ankyrin repeat protein; Provisional Pssm-ID: 222954 [Multi-domain] Cd Length: 494 Bit Score: 58.98 E-value: 3.51e-08
|
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| KH-I_NOVA_rpt2 | cd22436 | second type I K homology (KH) RNA-binding domain found in the family of neuro-oncological ... |
1792-1852 | 4.50e-08 | ||||||||
second type I K homology (KH) RNA-binding domain found in the family of neuro-oncological ventral antigen (Nova); The family includes two related neuronal RNA-binding proteins, Nova-1 and Nova-2. Nova-1, also called onconeural ventral antigen 1, or paraneoplastic Ri antigen, or ventral neuron-specific protein 1, may regulate RNA splicing or metabolism in a specific subset of developing neurons. It interacts with RNA containing repeats of the YCAY sequence. It is a brain-enriched splicing factor regulating neuronal alternative splicing. Nova-1 is involved in neurological disorders and carcinogenesis. Nova-2, also called astrocytic NOVA1-like RNA-binding protein, is a neuronal RNA-binding protein expressed in a broader central nervous system (CNS) distribution than Nova-1. It functions in neuronal RNA metabolism. NOVA family proteins contain three K-homology (KH) RNA-binding domains. The model corresponds to the second one. Pssm-ID: 411864 [Multi-domain] Cd Length: 70 Bit Score: 52.24 E-value: 4.50e-08
|
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| KH-I_TDRKH_rpt1 | cd22428 | first type I K homology (KH) RNA-binding domain found in tudor and KH domain-containing ... |
1791-1856 | 4.69e-08 | ||||||||
first type I K homology (KH) RNA-binding domain found in tudor and KH domain-containing protein (TDRKH) and similar proteins; TDRKH, also called tudor domain-containing protein 2 (TDRD2), is a mitochondria-anchored RNA-binding protein that is required for spermatogenesis and involved in piRNA biogenesis. It specifically recruits MIWI, but not MILI, to engage the piRNA pathway. TDRKH contains two K-homology (KH) RNA-binding domains and one tudor domain, which are involved in binding to RNA or single-strand DNA. The model corresponds to the first one. Pssm-ID: 411856 [Multi-domain] Cd Length: 74 Bit Score: 52.34 E-value: 4.69e-08
|
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| KH-I_Rnc1_rpt3 | cd22457 | third type I K homology (KH) RNA-binding domain found in Schizosaccharomyces pombe RNA-binding ... |
1791-1852 | 1.11e-07 | ||||||||
third type I K homology (KH) RNA-binding domain found in Schizosaccharomyces pombe RNA-binding protein Rnc1 and similar proteins; Rnc1, also called RNA-binding protein that suppresses calcineurin deletion 1, is an RNA-binding protein that acts as an important regulator of the posttranscriptional expression of the MAPK phosphatase Pmp1 in fission yeast. It binds and stabilizes pmp1 mRNA and hence acts as a negative regulator of pmk1 signaling. Overexpression of Rnc1 suppresses the Cl(-) sensitivity of calcineurin deletion. The nuclear export of Rnc1 requires mRNA-binding ability and the mRNA export factor Rae1. Rnc1 contains three K-homology (KH) RNA-binding domains. The model corresponds to the third one. Pssm-ID: 411885 [Multi-domain] Cd Length: 64 Bit Score: 50.92 E-value: 1.11e-07
|
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| KH-I_FUBP_rpt1 | cd22396 | first type I K homology (KH) RNA-binding domain found in the FUBP family RNA/DNA-binding ... |
1795-1856 | 1.12e-07 | ||||||||
first type I K homology (KH) RNA-binding domain found in the FUBP family RNA/DNA-binding proteins; The far upstream element-binding protein (FUBP) family includes FUBP1-3. FUBP1, also called FBP, or FUSE-binding protein 1, or DNA helicase V, or DH V, binds RNA and single-stranded DNA (ssDNA) and may act both as activator and repressor of transcription. It regulates MYC expression by binding to a single-stranded far-upstream element (FUSE) upstream of the MYC promoter. FUBP2, also called FUSE-binding protein 2, or KH type-splicing regulatory protein (KSRP), or p75, is a single-strand nucleic acid binding protein implicated in a variety of cellular processes, including splicing in the nucleus, mRNA decay, maturation of miRNA, and transcriptional control of proto-oncogenes such as c-myc. It regulates the stability and/or translatability of many mRNA species, encoding immune-relevant proteins, either by binding to AU-rich elements (AREs) of mRNA 3'UTR or by facilitating miRNA biogenesis to target mRNA. FUBP3, also called FUSE-binding protein 3, or MARTA2, was previously shown to mediate dendritic targeting of MAP2 mRNA in neurons. It may interact with single-stranded DNA from the far-upstream element (FUSE) and activate gene expression. It is required for beta-actin mRNA localization. It also interacts with fibroblast growth factor 9 (FGF9) 3'-UTR UG repeats and positively controls FGF9 expression through increasing translation of FGF9 mRNA. FUBP proteins contain four K-homology (KH) RNA-binding domains. The model corresponds to the first one. Pssm-ID: 411824 [Multi-domain] Cd Length: 68 Bit Score: 50.72 E-value: 1.12e-07
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| Ank_4 | pfam13637 | Ankyrin repeats (many copies); |
1247-1299 | 1.34e-07 | ||||||||
Ankyrin repeats (many copies); Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 50.35 E-value: 1.34e-07
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| KH-I_IGF2BP_rpt1 | cd22400 | first type I K homology (KH) RNA-binding domain found in the insulin-like growth factor 2 ... |
1792-1852 | 1.60e-07 | ||||||||
first type I K homology (KH) RNA-binding domain found in the insulin-like growth factor 2 mRNA-binding protein (IGF2BP) family; The IGF2BP family includes three members: IGF2BP1/IMP-1/ CRD-BP/ VICKZ1, IGF2BP2/IMP-2/ VICKZ2, and IGF2BP3/IMP-3/VICKZ3, which are RNA-binding factors that recruit target transcripts to cytoplasmic protein-RNA complexes (mRNPs). They function by binding to the 5' UTR of the insulin-like growth factor 2 (IGF2) mRNA and regulating IGF2 translation. IGF2BP proteins contain four K-homology (KH) RNA-binding domains which are important in RNA binding and are known to be involved in RNA synthesis and metabolism. The model corresponds to the first one. Pssm-ID: 411828 [Multi-domain] Cd Length: 68 Bit Score: 50.35 E-value: 1.60e-07
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| KH-I_IGF2BP_rpt4 | cd22403 | fourth type I K homology (KH) RNA-binding domain found in the insulin-like growth factor 2 ... |
1793-1851 | 3.31e-07 | ||||||||
fourth type I K homology (KH) RNA-binding domain found in the insulin-like growth factor 2 mRNA-binding protein (IGF2BP) family; The IGF2BP family includes three members: IGF2BP1/IMP-1/CRD-BP/VICKZ1, IGF2BP2/IMP-2/VICKZ2, and IGF2BP3/IMP-3/VICKZ3, which are RNA-binding factors that recruit target transcripts to cytoplasmic protein-RNA complexes (mRNPs). They function by binding to the 5' UTR of the insulin-like growth factor 2 (IGF2) mRNA and regulating IGF2 translation. IGF2BP proteins contain four K-homology (KH) RNA-binding domains which are important in RNA binding and are known to be involved in RNA synthesis and metabolism. The model corresponds to the fourth one. Pssm-ID: 411831 [Multi-domain] Cd Length: 66 Bit Score: 49.55 E-value: 3.31e-07
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| Ank_4 | pfam13637 | Ankyrin repeats (many copies); |
590-644 | 3.87e-07 | ||||||||
Ankyrin repeats (many copies); Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 48.81 E-value: 3.87e-07
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| Ank_5 | pfam13857 | Ankyrin repeats (many copies); |
261-299 | 4.28e-07 | ||||||||
Ankyrin repeats (many copies); Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 48.88 E-value: 4.28e-07
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| KH-I_Mextli_like | cd22454 | type I K homology (KH) RNA-binding domain found in Drosophila melanogaster eukaryotic ... |
1795-1856 | 5.42e-07 | ||||||||
type I K homology (KH) RNA-binding domain found in Drosophila melanogaster eukaryotic translation initiation factor 4E-binding protein Mextli and similar proteins; Mextli is a novel eukaryotic translation initiation factor 4E-binding protein that promotes translation in Drosophila melanogaster. Pssm-ID: 411882 [Multi-domain] Cd Length: 71 Bit Score: 49.24 E-value: 5.42e-07
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| PTZ00322 | PTZ00322 | 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
594-706 | 5.90e-07 | ||||||||
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 55.29 E-value: 5.90e-07
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| Ank_4 | pfam13637 | Ankyrin repeats (many copies); |
392-447 | 5.96e-07 | ||||||||
Ankyrin repeats (many copies); Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 48.42 E-value: 5.96e-07
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| KH-I_PNPase | cd02393 | type I K homology (KH) RNA-binding domain found in polyribonucleotide nucleotidyltransferase ... |
1789-1859 | 6.40e-07 | ||||||||
type I K homology (KH) RNA-binding domain found in polyribonucleotide nucleotidyltransferase (PNPase) and similar proteins; PNPase, also called polynucleotide phosphorylase, is a polyribonucleotide nucleotidyl transferase that degrades mRNA in prokaryotes and plant chloroplasts. It catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction. It is also involved, along with RNase II, in tRNA processing. The C-terminal region of PNPase contains domains homologous to those in other RNA binding proteins: a KH domain and an S1 domain. The model corresponds to the KH domain. Pssm-ID: 411803 [Multi-domain] Cd Length: 70 Bit Score: 48.63 E-value: 6.40e-07
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| Ank_4 | pfam13637 | Ankyrin repeats (many copies); |
1211-1265 | 6.57e-07 | ||||||||
Ankyrin repeats (many copies); Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 48.42 E-value: 6.57e-07
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| Ank_4 | pfam13637 | Ankyrin repeats (many copies); |
361-414 | 6.57e-07 | ||||||||
Ankyrin repeats (many copies); Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 48.42 E-value: 6.57e-07
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| PLN03192 | PLN03192 | Voltage-dependent potassium channel; Provisional |
1268-1433 | 7.91e-07 | ||||||||
Voltage-dependent potassium channel; Provisional Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 54.87 E-value: 7.91e-07
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| KH-I_PCBP4_rpt3 | cd22523 | third type I K homology (KH) RNA-binding domain found in poly(rC)-binding protein 4 (PCBP4) ... |
1790-1854 | 8.97e-07 | ||||||||
third type I K homology (KH) RNA-binding domain found in poly(rC)-binding protein 4 (PCBP4) and similar proteins; PCBP4, also called alpha-CP4, or heterogeneous nuclear ribonucleoprotein E4, or hnRNP E4, is a single-stranded nucleic acid binding protein that binds preferentially to oligo dC. It regulates both basal and stress-induced p21 expression through binding p21 3'-UTR and modulating p21 mRNA stability. It also plays a role in the cell cycle and is implicated in lung tumor suppression. PCBP4 contains three K-homology (KH) RNA-binding domains. The model corresponds to the third one. Pssm-ID: 411951 Cd Length: 68 Bit Score: 48.35 E-value: 8.97e-07
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| KH-I_PCBP_rpt2 | cd02396 | second type I K homology (KH) RNA-binding domain found in the family of poly(C)-binding ... |
1792-1856 | 9.10e-07 | ||||||||
second type I K homology (KH) RNA-binding domain found in the family of poly(C)-binding proteins (PCBPs); The PCBP family, also known as hnRNP E family, comprises four members, PCBP1-4, which are RNA-binding proteins that interact in a sequence-specific manner with single-stranded poly(C) sequences. They are mainly involved in various posttranscriptional regulations, including mRNA stabilization or translational activation/silencing. Besides, PCBPs may share iron chaperone activity. PCBPs contain three K-homology (KH) RNA-binding domains. The model corresponds to the second one. Pssm-ID: 411806 [Multi-domain] Cd Length: 72 Bit Score: 48.42 E-value: 9.10e-07
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| PTZ00322 | PTZ00322 | 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
266-347 | 9.75e-07 | ||||||||
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 54.52 E-value: 9.75e-07
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| KH-I_HNRNPK_rpt3 | cd22434 | third type I K homology (KH) RNA-binding domain found in heterogeneous nuclear ... |
1790-1865 | 1.28e-06 | ||||||||
third type I K homology (KH) RNA-binding domain found in heterogeneous nuclear ribonucleoprotein K (hnRNP K) and similar proteins; hnRNP K, also called transformation up-regulated nuclear protein (TUNP), is a pre-mRNA binding protein that binds tenaciously to poly(C) sequences. It may be involved in the nuclear metabolism of hnRNAs, particularly for pre-mRNAs that contain cytidine-rich sequences. It can also bind poly(C) single-stranded DNA. hnRNP K plays an important role in p53/TP53 response to DNA damage, acting at the level of both transcription activation and repression. hnRNP K contains three K-homology (KH) RNA-binding domains. The model corresponds to the third one. Pssm-ID: 411862 [Multi-domain] Cd Length: 74 Bit Score: 48.08 E-value: 1.28e-06
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| PLN03192 | PLN03192 | Voltage-dependent potassium channel; Provisional |
1105-1285 | 1.71e-06 | ||||||||
Voltage-dependent potassium channel; Provisional Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 53.72 E-value: 1.71e-06
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| Ank_5 | pfam13857 | Ankyrin repeats (many copies); |
1129-1184 | 1.92e-06 | ||||||||
Ankyrin repeats (many copies); Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 46.96 E-value: 1.92e-06
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| TRPV5-6 | cd22192 | Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
428-612 | 2.26e-06 | ||||||||
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues. Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 53.09 E-value: 2.26e-06
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| KH-I_IGF2BP_rpt2 | cd22401 | second type I K homology (KH) RNA-binding domain found in the insulin-like growth factor 2 ... |
1792-1854 | 2.50e-06 | ||||||||
second type I K homology (KH) RNA-binding domain found in the insulin-like growth factor 2 mRNA-binding protein (IGF2BP) family; The IGF2BP family includes three members: IGF2BP1/IMP-1/ CRD-BP/ VICKZ1, IGF2BP2/IMP-2/ VICKZ2, and IGF2BP3/IMP-3/VICKZ3, which are RNA-binding factors that recruit target transcripts to cytoplasmic protein-RNA complexes (mRNPs). They function by binding to the 5' UTR of the insulin-like growth factor 2 (IGF2) mRNA and regulating IGF2 translation. IGF2BP proteins contain four K-homology (KH) RNA-binding domains which are important in RNA binding and are known to be involved in RNA synthesis and metabolism. The model corresponds to the second one. Pssm-ID: 411829 [Multi-domain] Cd Length: 72 Bit Score: 47.22 E-value: 2.50e-06
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| PTZ00322 | PTZ00322 | 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
381-480 | 2.55e-06 | ||||||||
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 52.98 E-value: 2.55e-06
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| PHA02878 | PHA02878 | ankyrin repeat protein; Provisional |
430-679 | 2.63e-06 | ||||||||
ankyrin repeat protein; Provisional Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 52.57 E-value: 2.63e-06
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| KH-I_ScSCP160_rpt4 | cd22449 | fourth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ... |
1792-1856 | 2.80e-06 | ||||||||
fourth type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein SCP160 and similar proteins; SCP160, also called protein HX, is a new yeast protein associated with the nuclear membrane and the endoplasmic reticulum. It is involved in the control of mitotic chromosome transmission. It is required during cell division for faithful partitioning of the ER-nuclear envelope membranes which enclose the duplicated chromosomes in yeast. SCP160 contains seven K-homology (KH) RNA-binding domains. The model corresponds to the fourth one. Pssm-ID: 411877 [Multi-domain] Cd Length: 70 Bit Score: 46.88 E-value: 2.80e-06
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| KH-I_ScSCP160_rpt2 | cd22447 | second type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ... |
1793-1856 | 2.99e-06 | ||||||||
second type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein SCP160 and similar proteins; SCP160, also called protein HX, is a new yeast protein associated with the nuclear membrane and the endoplasmic reticulum. It is involved in the control of mitotic chromosome transmission. It is required during cell division for faithful partitioning of the ER-nuclear envelope membranes which enclose the duplicated chromosomes in yeast. SCP160 contains seven K-homology (KH) RNA-binding domains. The model corresponds to the second one. Pssm-ID: 411875 [Multi-domain] Cd Length: 80 Bit Score: 47.41 E-value: 2.99e-06
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| Ank | pfam00023 | Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
459-491 | 3.01e-06 | ||||||||
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity. Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 45.74 E-value: 3.01e-06
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| PHA03095 | PHA03095 | ankyrin-like protein; Provisional |
563-696 | 3.18e-06 | ||||||||
ankyrin-like protein; Provisional Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 52.33 E-value: 3.18e-06
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| PTZ00322 | PTZ00322 | 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
1316-1413 | 3.83e-06 | ||||||||
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 52.59 E-value: 3.83e-06
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| KH-I_Vigilin_rpt14 | cd22417 | fourteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ... |
1792-1858 | 4.83e-06 | ||||||||
fourteenth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, also called high density lipoprotein-binding protein, or HDL-binding protein, is a ubiquitous and highly conserved RNA-binding protein that shuttles between nucleus and cytoplasm presumably in contact with RNA molecules. It may be involved in chromosome partitioning at mitosis, facilitating translation and tRNA transport, and control of mRNA metabolism, including estrogen-mediated stabilization of vitellogenin mRNA. Vigilin is up-regulated by cholesterol loading of cells and functions to protect cells from over-accumulation of cholesterol. It may play a role in cell sterol metabolism. Disruption of human vigilin impairs chromosome condensation and segregation. Vigilin has a unique structure of 14-15 consecutively arranged, but non-identical K-homology (KH) domains which apparently mediate RNA-protein binding. The model corresponds to the fourteenth one. Pssm-ID: 411845 [Multi-domain] Cd Length: 72 Bit Score: 46.43 E-value: 4.83e-06
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| KH-I_ScSCP160_rpt7 | cd22452 | seventh type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein ... |
1793-1854 | 4.97e-06 | ||||||||
seventh type I K homology (KH) RNA-binding domain found in Saccharomyces cerevisiae Protein SCP160 and similar proteins; SCP160, also called protein HX, is a new yeast protein associated with the nuclear membrane and the endoplasmic reticulum. It is involved in the control of mitotic chromosome transmission. It is required during cell division for faithful partitioning of the ER-nuclear envelope membranes which enclose the duplicated chromosomes in yeast. SCP160 contains seven K-homology (KH) RNA-binding domains. The model corresponds to the seventh one. Pssm-ID: 411880 [Multi-domain] Cd Length: 65 Bit Score: 46.16 E-value: 4.97e-06
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| trp | TIGR00870 | transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
1135-1332 | 5.72e-06 | ||||||||
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds] Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 52.01 E-value: 5.72e-06
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| TRPV5-6 | cd22192 | Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
196-351 | 6.12e-06 | ||||||||
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues. Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 51.55 E-value: 6.12e-06
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| Ank | pfam00023 | Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
1379-1411 | 8.58e-06 | ||||||||
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity. Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 44.59 E-value: 8.58e-06
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| KH-I_NOVA_rpt1 | cd22435 | first type I K homology (KH) RNA-binding domain found in the family of neuro-oncological ... |
1792-1852 | 9.28e-06 | ||||||||
first type I K homology (KH) RNA-binding domain found in the family of neuro-oncological ventral antigen (Nova); The family includes two related neuronal RNA-binding proteins, Nova-1 and Nova-2. Nova-1, also called onconeural ventral antigen 1, or paraneoplastic Ri antigen, or ventral neuron-specific protein 1, may regulate RNA splicing or metabolism in a specific subset of developing neurons. It interacts with RNA containing repeats of the YCAY sequence. It is a brain-enriched splicing factor regulating neuronal alternative splicing. Nova-1 is involved in neurological disorders and carcinogenesis. Nova-2, also called astrocytic NOVA1-like RNA-binding protein, is a neuronal RNA-binding protein expressed in a broader central nervous system (CNS) distribution than Nova-1. It functions in neuronal RNA metabolism. NOVA family proteins contain three K-homology (KH) RNA-binding domains. The model corresponds to the first one. Pssm-ID: 411863 [Multi-domain] Cd Length: 73 Bit Score: 45.61 E-value: 9.28e-06
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| KH-I_FUBP2_rpt4 | cd22488 | fourth type I K homology (KH) RNA-binding domain found in far upstream element-binding protein ... |
1793-1852 | 9.36e-06 | ||||||||
fourth type I K homology (KH) RNA-binding domain found in far upstream element-binding protein 2 (FUBP2) and similar proteins; FUBP2, also called FUSE-binding protein 2, or KH type-splicing regulatory protein (KSRP), or p75, is a single-strand nucleic acid binding protein implicated in a variety of cellular processes, including splicing in the nucleus, mRNA decay, maturation of miRNA, and transcriptional control of proto-oncogenes such as c-myc. It regulates the stability and/or translatability of many mRNA species, encoding immune-relevant proteins, either by binding to AU-rich elements (AREs) of mRNA 3'UTR or by facilitating miRNA biogenesis to target mRNA. FUBP2 contains four K-homology (KH) RNA-binding domains. The model corresponds to the fourth one. Pssm-ID: 411916 Cd Length: 69 Bit Score: 45.48 E-value: 9.36e-06
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| trp | TIGR00870 | transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
299-454 | 9.51e-06 | ||||||||
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds] Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 51.24 E-value: 9.51e-06
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| PHA02875 | PHA02875 | ankyrin repeat protein; Provisional |
528-679 | 1.00e-05 | ||||||||
ankyrin repeat protein; Provisional Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 50.76 E-value: 1.00e-05
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| Ank_4 | pfam13637 | Ankyrin repeats (many copies); |
1312-1367 | 1.02e-05 | ||||||||
Ankyrin repeats (many copies); Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 44.96 E-value: 1.02e-05
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| TRPV5-6 | cd22192 | Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
139-340 | 1.07e-05 | ||||||||
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues. Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 50.78 E-value: 1.07e-05
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| TRPV5-6 | cd22192 | Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
1112-1231 | 1.10e-05 | ||||||||
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues. Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 50.78 E-value: 1.10e-05
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| ANK | smart00248 | ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
459-488 | 1.38e-05 | ||||||||
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure. Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 43.73 E-value: 1.38e-05
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| Ank_5 | pfam13857 | Ankyrin repeats (many copies); |
344-396 | 1.51e-05 | ||||||||
Ankyrin repeats (many copies); Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 44.64 E-value: 1.51e-05
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| Ank | pfam00023 | Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
261-288 | 1.92e-05 | ||||||||
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity. Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 43.43 E-value: 1.92e-05
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| Ank_4 | pfam13637 | Ankyrin repeats (many copies); |
1179-1230 | 1.96e-05 | ||||||||
Ankyrin repeats (many copies); Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 44.19 E-value: 1.96e-05
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| Ank_3 | pfam13606 | Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
1245-1273 | 2.28e-05 | ||||||||
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 43.40 E-value: 2.28e-05
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| PLN03192 | PLN03192 | Voltage-dependent potassium channel; Provisional |
1158-1340 | 2.77e-05 | ||||||||
Voltage-dependent potassium channel; Provisional Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 49.87 E-value: 2.77e-05
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| KH-I_PCBP3_rpt3 | cd22522 | third type I K homology (KH) RNA-binding domain found in poly(rC)-binding protein 3 (PCBP3) ... |
1790-1854 | 3.13e-05 | ||||||||
third type I K homology (KH) RNA-binding domain found in poly(rC)-binding protein 3 (PCBP3) and similar proteins; PCBP3, also called alpha-CP3, or PCBP3-overlapping transcript, or PCBP3-overlapping transcript 1, or heterogeneous nuclear ribonucleoprotein E3, or hnRNP E3, is a single-stranded nucleic acid binding protein that binds preferentially to oligo dC. It can function as a repressor dependent on binding to single-strand and double-stranded poly(C) sequences. PCBP3 contains three K-homology (KH) RNA-binding domains. The model corresponds to the third one. Pssm-ID: 411950 [Multi-domain] Cd Length: 75 Bit Score: 44.33 E-value: 3.13e-05
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| trp | TIGR00870 | transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
190-449 | 3.14e-05 | ||||||||
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds] Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 49.69 E-value: 3.14e-05
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| PRK03918 | PRK03918 | DNA double-strand break repair ATPase Rad50; |
771-866 | 3.27e-05 | ||||||||
DNA double-strand break repair ATPase Rad50; Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.68 E-value: 3.27e-05
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| KH-I_AKAP1 | cd22395 | type I K homology (KH) RNA-binding domain found in mitochondrial A-kinase anchor protein 1 ... |
1795-1852 | 3.34e-05 | ||||||||
type I K homology (KH) RNA-binding domain found in mitochondrial A-kinase anchor protein 1 (AKAP1) and similar proteins; AKAP1, also called A-kinase anchor protein 149 kDa, or AKAP 149, or dual specificity A-kinase-anchoring protein 1, or D-AKAP-1, or protein kinase A-anchoring protein 1 (PRKA1), or spermatid A-kinase anchor protein 84, or S-AKAP84, is a novel developmentally regulated A kinase anchor protein of male germ cells. It binds to type I and II regulatory subunits of protein kinase A and anchors them to the cytoplasmic face of the mitochondrial outer membrane. Pssm-ID: 411823 [Multi-domain] Cd Length: 68 Bit Score: 44.05 E-value: 3.34e-05
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| Ank_5 | pfam13857 | Ankyrin repeats (many copies); |
519-564 | 3.37e-05 | ||||||||
Ankyrin repeats (many copies); Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 43.49 E-value: 3.37e-05
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| KH-I_BTR1_rpt2 | cd22437 | second type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana protein BTR1 ... |
1792-1852 | 4.31e-05 | ||||||||
second type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana protein BTR1 and similar proteins; BTR1, also called Binding to ToMV RNA 1, is a negative regulator of tomato mosaic virus (ToMV) multiplication but has no effect on the multiplication of cucumber mosaic virus (CMV). BTR1 contains three K-homology (KH) RNA-binding domains. The model corresponds to the second one. Pssm-ID: 411865 [Multi-domain] Cd Length: 69 Bit Score: 43.75 E-value: 4.31e-05
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| Ank_5 | pfam13857 | Ankyrin repeats (many copies); |
446-501 | 4.31e-05 | ||||||||
Ankyrin repeats (many copies); Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 43.10 E-value: 4.31e-05
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| KH-I_PEPPER_rpt1_like | cd22459 | first type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana RNA-binding KH ... |
1792-1838 | 4.55e-05 | ||||||||
first type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana RNA-binding KH domain-containing protein PEPPER and similar proteins; The family includes a group of plant RNA-binding KH domain-containing proteins, such as PEPPER, flowering locus K homology domain protein (FLK), RNA-binding KH domain-containing protein RCF3 and KH domain-containing protein HEN4. PEPPER regulates vegetative and gynoecium development. It acts as a positive regulator of the central floral repressor FLOWERING LOCUS C. In concert with HUA2, PEPPER antagonizes FLK by positively regulating FLC probably at transcriptional and post-transcriptional levels, and thus acts as a negative regulator of flowering. FLK, also called flowering locus KH domain protein, regulates positively flowering by repressing FLC expression and post-transcriptional modification. PEPPER and FLK contain three K-homology (KH) RNA-binding domains. RCF3, also called protein ENHANCED STRESS RESPONSE 1 (ESR1), or protein HIGH OSMOTIC STRESS GENE EXPRESSION 5 (HOS5), or protein REGULATOR OF CBF GENE EXPRESSION 3, or protein SHINY 1 (SHI1), acts as negative regulator of osmotic stress-induced gene expression. It is involved in the regulation of thermotolerance responses under heat stress. It functions as an upstream regulator of heat stress transcription factor (HSF) genes. HEN4, also called protein HUA ENHANCER 4, plays a role in floral reproductive organ identity in the third whorl and floral determinacy specification by specifically promoting the processing of AGAMOUS (AG) pre-mRNA. It functions in association with HUA1 and HUA2. RCF3 and HEN4 contain five KH RNA-binding domains. The model corresponds to the KH1 domain of PEPPER and FLK, as well as KH1 and KH3 domains of RCF3 and HEN4. Pssm-ID: 411887 [Multi-domain] Cd Length: 69 Bit Score: 43.37 E-value: 4.55e-05
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| TRPV3 | cd22194 | Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
475-685 | 4.68e-05 | ||||||||
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. Pssm-ID: 411978 [Multi-domain] Cd Length: 680 Bit Score: 48.99 E-value: 4.68e-05
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| ANK | smart00248 | ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
324-352 | 4.76e-05 | ||||||||
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure. Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 42.19 E-value: 4.76e-05
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| PHA02884 | PHA02884 | ankyrin repeat protein; Provisional |
304-401 | 5.14e-05 | ||||||||
ankyrin repeat protein; Provisional Pssm-ID: 165212 [Multi-domain] Cd Length: 300 Bit Score: 48.06 E-value: 5.14e-05
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| PTZ00322 | PTZ00322 | 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
329-435 | 5.15e-05 | ||||||||
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 48.74 E-value: 5.15e-05
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| KH-I_PCBP1_2_rpt3 | cd22521 | third type I K homology (KH) RNA-binding domain found in poly(rC)-binding protein 1 (PCBP1) ... |
1790-1860 | 5.41e-05 | ||||||||
third type I K homology (KH) RNA-binding domain found in poly(rC)-binding protein 1 (PCBP1) and similar proteins; The family includes PCBP1 (also called alpha-CP1, or heterogeneous nuclear ribonucleoprotein E1, or hnRNP E1, or nucleic acid-binding protein SUB2.3) and PCBP2 (also called alpha-CP2, or heterogeneous nuclear ribonucleoprotein E2, or hnRNP E2). They are single-stranded nucleic acid binding proteins that bind preferentially to oligo dC. They act as iron chaperones for ferritin. In case of infection by poliovirus, PCBP1 plays a role in initiation of viral RNA replication in concert with the viral protein 3CD. PCBP2 is a major cellular poly(rC)-binding protein. It also binds poly(rU). PCBP2 negatively regulates cellular antiviral responses mediated by MAVS signaling. It acts as an adapter between MAVS and the E3 ubiquitin ligase ITCH, therefore triggering MAVS ubiquitination and degradation. PCBP2 forms a metabolon with the heme oxygenase 1/cytochrome P450 reductase complex for heme catabolism and iron transfer. Both PCBP1 and PCBP2 contain three K-homology (KH) RNA-binding domains. The model corresponds to the third one. Pssm-ID: 411949 Cd Length: 76 Bit Score: 43.50 E-value: 5.41e-05
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| TRPV3 | cd22194 | Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
1102-1231 | 5.88e-05 | ||||||||
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. Pssm-ID: 411978 [Multi-domain] Cd Length: 680 Bit Score: 48.60 E-value: 5.88e-05
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| KH-I_DDX43_DDX53 | cd22430 | type I K homology (KH) RNA-binding domain found in DEAD box protein 43 (DDX43), DEAD box ... |
1793-1858 | 6.02e-05 | ||||||||
type I K homology (KH) RNA-binding domain found in DEAD box protein 43 (DDX43), DEAD box protein 53 (DDX53) and similar proteins; DDX43 (also called cancer/testis antigen 13, or DEAD box protein HAGE, or helical antigen) displays tumor-specific expression. Diseases associated with DDX43 include rheumatoid lung disease. DDX53 (also called cancer-associated gene protein, or cancer/testis antigen 26, or DEAD box protein CAGE) shows high expression level in various tumors and is involved in anti-cancer drug resistance. Both DDX46 and DDX53 are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. Pssm-ID: 411858 [Multi-domain] Cd Length: 66 Bit Score: 43.04 E-value: 6.02e-05
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| PRK03918 | PRK03918 | DNA double-strand break repair ATPase Rad50; |
778-867 | 6.22e-05 | ||||||||
DNA double-strand break repair ATPase Rad50; Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.52 E-value: 6.22e-05
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| PRK12323 | PRK12323 | DNA polymerase III subunit gamma/tau; |
2018-2202 | 6.39e-05 | ||||||||
DNA polymerase III subunit gamma/tau; Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 48.33 E-value: 6.39e-05
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| Ank | pfam00023 | Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
526-554 | 6.42e-05 | ||||||||
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity. Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 41.89 E-value: 6.42e-05
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| PHA02859 | PHA02859 | ankyrin repeat protein; Provisional |
261-386 | 6.59e-05 | ||||||||
ankyrin repeat protein; Provisional Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 46.74 E-value: 6.59e-05
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| KH-I_FUBP_rpt3 | cd22398 | third type I K homology (KH) RNA-binding domain found in the FUBP family RNA/DNA-binding ... |
1795-1856 | 6.68e-05 | ||||||||
third type I K homology (KH) RNA-binding domain found in the FUBP family RNA/DNA-binding proteins; The far upstream element-binding protein (FUBP) family includes FUBP1-3. FUBP1, also called FBP, or FUSE-binding protein 1, or DNA helicase V, or DH V, binds RNA and single-stranded DNA (ssDNA) and may act both as activator and repressor of transcription. It regulates MYC expression by binding to a single-stranded far-upstream element (FUSE) upstream of the MYC promoter. FUBP2, also called FUSE-binding protein 2, or KH type-splicing regulatory protein (KSRP), or p75, is a single-strand nucleic acid binding protein implicated in a variety of cellular processes, including splicing in the nucleus, mRNA decay, maturation of miRNA, and transcriptional control of proto-oncogenes such as c-myc. It regulates the stability and/or translatability of many mRNA species, encoding immune-relevant proteins, either by binding to AU-rich elements (AREs) of mRNA 3'UTR or by facilitating miRNA biogenesis to target mRNA. FUBP3, also called FUSE-binding protein 3, or MARTA2, was previously shown to mediate dendritic targeting of MAP2 mRNA in neurons. It may interact with single-stranded DNA from the far-upstream element (FUSE) and activate gene expression. It is required for beta-actin mRNA localization. It also interacts with fibroblast growth factor 9 (FGF9) 3'-UTR UG repeats and positively controls FGF9 expression through increasing translation of FGF9 mRNA. FUBP proteins contain four K-homology (KH) RNA-binding domains. The model corresponds to the third one. Pssm-ID: 411826 [Multi-domain] Cd Length: 67 Bit Score: 43.02 E-value: 6.68e-05
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| ANK | smart00248 | ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
1245-1273 | 7.12e-05 | ||||||||
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure. Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 41.80 E-value: 7.12e-05
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| Ank_5 | pfam13857 | Ankyrin repeats (many copies); |
311-366 | 7.54e-05 | ||||||||
Ankyrin repeats (many copies); Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 42.33 E-value: 7.54e-05
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| DUF5585 | pfam17823 | Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
1996-2309 | 8.24e-05 | ||||||||
Family of unknown function (DUF5585); This is a family of unknown function found in chordata. Pssm-ID: 465521 [Multi-domain] Cd Length: 506 Bit Score: 48.03 E-value: 8.24e-05
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| TRPV1-4 | cd22193 | Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ... |
394-612 | 8.29e-05 | ||||||||
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. Pssm-ID: 411977 [Multi-domain] Cd Length: 607 Bit Score: 47.87 E-value: 8.29e-05
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| Ank_3 | pfam13606 | Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
459-488 | 8.76e-05 | ||||||||
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 41.47 E-value: 8.76e-05
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| Ank_5 | pfam13857 | Ankyrin repeats (many copies); |
278-329 | 9.83e-05 | ||||||||
Ankyrin repeats (many copies); Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 42.33 E-value: 9.83e-05
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| Ank_4 | pfam13637 | Ankyrin repeats (many copies); |
1145-1197 | 1.03e-04 | ||||||||
Ankyrin repeats (many copies); Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 41.88 E-value: 1.03e-04
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| PTZ00322 | PTZ00322 | 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
1365-1432 | 1.14e-04 | ||||||||
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 47.59 E-value: 1.14e-04
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| PTZ00322 | PTZ00322 | 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
301-423 | 1.22e-04 | ||||||||
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 47.59 E-value: 1.22e-04
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| KH-I_FUBP3_rpt4 | cd22489 | fourth type I K homology (KH) RNA-binding domain found in far upstream element-binding protein ... |
1794-1853 | 1.22e-04 | ||||||||
fourth type I K homology (KH) RNA-binding domain found in far upstream element-binding protein 3 (FUBP3) and similar proteins; FUBP3, also called FUSE-binding protein 3, or MARTA2, was previously shown to mediate dendritic targeting of MAP2 mRNA in neurons. It may interact with single-stranded DNA from the far-upstream element (FUSE) and activate gene expression. It is required for beta-actin mRNA localization. It also interacts with fibroblast growth factor 9 (FGF9) 3'-UTR UG repeats and positively controls FGF9 expression through increasing translation of FGF9 mRNA. FUBP3 contains four K-homology (KH) RNA-binding domains. The model corresponds to the fourth one. Pssm-ID: 411917 [Multi-domain] Cd Length: 69 Bit Score: 42.22 E-value: 1.22e-04
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| Ank | pfam00023 | Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
590-620 | 1.28e-04 | ||||||||
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity. Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 41.12 E-value: 1.28e-04
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| PTZ00322 | PTZ00322 | 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
1253-1342 | 1.33e-04 | ||||||||
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 47.59 E-value: 1.33e-04
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| KH-I_RCF3_like_rpt5 | cd22463 | fifth type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana RNA-binding KH ... |
1793-1856 | 1.37e-04 | ||||||||
fifth type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana RNA-binding KH domain-containing protein RCF3 and similar protein; RCF3, also called protein ENHANCED STRESS RESPONSE 1 (ESR1), or protein HIGH OSMOTIC STRESS GENE EXPRESSION 5 (HOS5), or protein REGULATOR OF CBF GENE EXPRESSION 3, or protein SHINY 1 (SHI1), acts as negative regulator of osmotic stress-induced gene expression. It is involved in the regulation of thermotolerance responses under heat stress. It functions as an upstream regulator of heat stress transcription factor (HSF) genes. HEN4, also called protein HUA ENHANCER 4, plays a role in floral reproductive organ identity in the third whorl and floral determinacy specification by specifically promoting the processing of AGAMOUS (AG) pre-mRNA. It functions in association with HUA1 and HUA2. RCF3 contains five K-homology (KH) RNA-binding domains. The model corresponds to the KH5 domain of RCF3. Pssm-ID: 411891 [Multi-domain] Cd Length: 71 Bit Score: 42.42 E-value: 1.37e-04
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| PHA02875 | PHA02875 | ankyrin repeat protein; Provisional |
199-286 | 1.41e-04 | ||||||||
ankyrin repeat protein; Provisional Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 46.91 E-value: 1.41e-04
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| ANK | smart00248 | ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
590-617 | 1.47e-04 | ||||||||
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure. Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 41.03 E-value: 1.47e-04
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| ANK | smart00248 | ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
526-552 | 1.55e-04 | ||||||||
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure. Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 41.03 E-value: 1.55e-04
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| Ank | pfam00023 | Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
324-352 | 1.57e-04 | ||||||||
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity. Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 41.12 E-value: 1.57e-04
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| Ank_5 | pfam13857 | Ankyrin repeats (many copies); |
1229-1286 | 1.64e-04 | ||||||||
Ankyrin repeats (many copies); Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 41.56 E-value: 1.64e-04
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| Ank | pfam00023 | Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
1245-1274 | 1.95e-04 | ||||||||
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity. Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 40.74 E-value: 1.95e-04
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| Ank_3 | pfam13606 | Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
324-353 | 2.06e-04 | ||||||||
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 40.70 E-value: 2.06e-04
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| TRPV | cd21882 | Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
1245-1400 | 2.25e-04 | ||||||||
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic). Pssm-ID: 411975 [Multi-domain] Cd Length: 600 Bit Score: 46.80 E-value: 2.25e-04
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| ANK | smart00248 | ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
557-584 | 2.29e-04 | ||||||||
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure. Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 40.26 E-value: 2.29e-04
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| PTZ00322 | PTZ00322 | 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
525-622 | 2.44e-04 | ||||||||
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 46.43 E-value: 2.44e-04
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| KH-I_PEPPER_rpt2_like | cd22460 | second type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana RNA-binding KH ... |
1792-1857 | 2.58e-04 | ||||||||
second type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana RNA-binding KH domain-containing protein PEPPER and similar proteins; The family includes a group of plant RNA-binding KH domain-containing proteins, such as PEPPER, flowering locus K homology domain protein (FLK), RNA-binding KH domain-containing protein RCF3 and KH domain-containing protein HEN4. PEPPER regulates vegetative and gynoecium development. It acts as a positive regulator of the central floral repressor FLOWERING LOCUS C. In concert with HUA2, PEPPER antagonizes FLK by positively regulating FLC probably at transcriptional and post-transcriptional levels, and thus acts as a negative regulator of flowering. FLK, also called flowering locus KH domain protein, regulates positively flowering by repressing FLC expression and post-transcriptional modification. PEPPER and FLK contain three K-homology (KH) RNA-binding domains. RCF3, also called protein ENHANCED STRESS RESPONSE 1 (ESR1), or protein HIGH OSMOTIC STRESS GENE EXPRESSION 5 (HOS5), or protein REGULATOR OF CBF GENE EXPRESSION 3, or protein SHINY 1 (SHI1), acts as negative regulator of osmotic stress-induced gene expression. It is involved in the regulation of thermotolerance responses under heat stress. It functions as an upstream regulator of heat stress transcription factor (HSF) genes. HEN4, also called protein HUA ENHANCER 4, plays a role in floral reproductive organ identity in the third whorl and floral determinacy specification by specifically promoting the processing of AGAMOUS (AG) pre-mRNA. It functions in association with HUA1 and HUA2. RCF3 and HEN4 contain five KH RNA-binding domains. The model corresponds to the KH2 domain of PEPPER and FLK, as well as KH2 and KH4 domains of RCF3 and HEN4. Pssm-ID: 411888 [Multi-domain] Cd Length: 73 Bit Score: 41.45 E-value: 2.58e-04
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| PTZ00322 | PTZ00322 | 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
1149-1253 | 2.65e-04 | ||||||||
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 46.43 E-value: 2.65e-04
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| TRPV | cd21882 | Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
370-626 | 2.83e-04 | ||||||||
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic). Pssm-ID: 411975 [Multi-domain] Cd Length: 600 Bit Score: 46.41 E-value: 2.83e-04
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| PHA02859 | PHA02859 | ankyrin repeat protein; Provisional |
356-487 | 3.50e-04 | ||||||||
ankyrin repeat protein; Provisional Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 44.42 E-value: 3.50e-04
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| ANK | smart00248 | ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
261-287 | 3.59e-04 | ||||||||
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure. Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 39.88 E-value: 3.59e-04
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| PHA02989 | PHA02989 | ankyrin repeat protein; Provisional |
373-645 | 3.82e-04 | ||||||||
ankyrin repeat protein; Provisional Pssm-ID: 222954 [Multi-domain] Cd Length: 494 Bit Score: 45.89 E-value: 3.82e-04
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| Caldesmon | pfam02029 | Caldesmon; |
779-866 | 3.88e-04 | ||||||||
Caldesmon; Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 45.63 E-value: 3.88e-04
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| KH-I_PCBP_rpt1 | cd22438 | first type I K homology (KH) RNA-binding domain found in the family of poly(C)-binding ... |
1800-1865 | 4.86e-04 | ||||||||
first type I K homology (KH) RNA-binding domain found in the family of poly(C)-binding proteins (PCBPs); The PCBP family, also known as hnRNP E family, comprises four members, PCBP1-4, which are RNA-binding proteins that interact in a sequence-specific manner with single-stranded poly(C) sequences. They are mainly involved in various posttranscriptional regulations, including mRNA stabilization or translational activation/silencing. Besides, PCBPs may share iron chaperone activity. PCBPs contain three K-homology (KH) RNA-binding domains. The model corresponds to the first one. Pssm-ID: 411866 [Multi-domain] Cd Length: 67 Bit Score: 40.70 E-value: 4.86e-04
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| Ank_4 | pfam13637 | Ankyrin repeats (many copies); |
1279-1332 | 4.92e-04 | ||||||||
Ankyrin repeats (many copies); Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 40.34 E-value: 4.92e-04
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| Ank_3 | pfam13606 | Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
590-617 | 5.18e-04 | ||||||||
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 39.55 E-value: 5.18e-04
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| Ank_4 | pfam13637 | Ankyrin repeats (many copies); |
496-544 | 5.76e-04 | ||||||||
Ankyrin repeats (many copies); Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 39.95 E-value: 5.76e-04
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| YhaN | COG4717 | Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
778-867 | 5.95e-04 | ||||||||
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 5.95e-04
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| MAP7 | pfam05672 | MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
778-866 | 6.10e-04 | ||||||||
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent. Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 42.72 E-value: 6.10e-04
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| KH-I_BTR1_rpt3 | cd22514 | third type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana protein BTR1 and ... |
1790-1856 | 6.22e-04 | ||||||||
third type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana protein BTR1 and similar proteins; BTR1, also called Binding to ToMV RNA 1, is a negative regulator of tomato mosaic virus (ToMV) multiplication but has no effect on the multiplication of cucumber mosaic virus (CMV). BTR1 contains three K-homology (KH) RNA-binding domains. The model corresponds to the third one. Pssm-ID: 411942 [Multi-domain] Cd Length: 71 Bit Score: 40.48 E-value: 6.22e-04
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| ANK | smart00248 | ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
1379-1408 | 6.48e-04 | ||||||||
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure. Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 39.11 E-value: 6.48e-04
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| KH-I_Vigilin_rpt8 | cd22411 | eighth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ... |
1790-1853 | 6.49e-04 | ||||||||
eighth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, also called high density lipoprotein-binding protein, or HDL-binding protein, is a ubiquitous and highly conserved RNA-binding protein that shuttles between nucleus and cytoplasm presumably in contact with RNA molecules. It may be involved in chromosome partitioning at mitosis, facilitating translation and tRNA transport, and control of mRNA metabolism, including estrogen-mediated stabilization of vitellogenin mRNA. Vigilin is up-regulated by cholesterol loading of cells and functions to protect cells from over-accumulation of cholesterol. It may play a role in cell sterol metabolism. Disruption of human vigilin impairs chromosome condensation and segregation. Vigilin has a unique structure of 14-15 consecutively arranged, but non-identical K-homology (KH) domains which apparently mediate RNA-protein binding. The model corresponds to the eighth one. Pssm-ID: 411839 [Multi-domain] Cd Length: 62 Bit Score: 39.88 E-value: 6.49e-04
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| ANK | smart00248 | ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
1142-1171 | 7.22e-04 | ||||||||
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure. Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 39.11 E-value: 7.22e-04
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| PTZ00322 | PTZ00322 | 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
196-292 | 8.78e-04 | ||||||||
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 44.89 E-value: 8.78e-04
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| PHA02798 | PHA02798 | ankyrin-like protein; Provisional |
372-498 | 9.44e-04 | ||||||||
ankyrin-like protein; Provisional Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 44.44 E-value: 9.44e-04
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| Ank | pfam00023 | Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
1142-1172 | 9.47e-04 | ||||||||
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity. Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 38.81 E-value: 9.47e-04
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| Ank_5 | pfam13857 | Ankyrin repeats (many copies); |
1297-1354 | 9.63e-04 | ||||||||
Ankyrin repeats (many copies); Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 39.25 E-value: 9.63e-04
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| KH-I_IGF2BP2_rpt4 | cd22500 | fourth type I K homology (KH) RNA-binding domain found in insulin-like growth factor 2 ... |
1793-1857 | 9.65e-04 | ||||||||
fourth type I K homology (KH) RNA-binding domain found in insulin-like growth factor 2 mRNA-binding protein 2 (IGF2BP2) and similar proteins; IGF2BP2, also called IGF2 mRNA-binding protein 2 (IMP-2), or hepatocellular carcinoma autoantigen p62, or IGF-II mRNA-binding protein 2, or VICKZ family member 2 (VICKZ2), is an RNA-binding factor that recruits target transcripts to cytoplasmic protein-RNA complexes (mRNPs). It functions by binding to the 5' UTR of the insulin-like growth factor 2 (IGF2) mRNA and regulating IGF2 translation. It also binds to beta-actin/ACTB and MYC transcripts. IGF2BP2 can form homooligomers and heterooligomers with IGF2BP1 and IGF2BP3 in an RNA-dependent manner. It contains four K-homology (KH) RNA-binding domains which are important in RNA binding and are known to be involved in RNA synthesis and metabolism. The model corresponds to the fourth one. Pssm-ID: 411928 Cd Length: 78 Bit Score: 40.12 E-value: 9.65e-04
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| PTZ00322 | PTZ00322 | 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
229-322 | 9.81e-04 | ||||||||
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 44.50 E-value: 9.81e-04
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| Com_YlbF | pfam06133 | Control of competence regulator ComK, YlbF/YmcA; YlbF Is a family of short Gram-positive and ... |
783-859 | 1.03e-03 | ||||||||
Control of competence regulator ComK, YlbF/YmcA; YlbF Is a family of short Gram-positive and archaeal proteins that includes both YlbF and YmcA which may interact synergistically. The family is necessary for correct biofilm formation, as null mutants of ymcA and ylbF fail to form pellicles at air-liquid interfaces and grow on solid media as smooth, undifferentiated colonies. During development, YmcA, YlbF and YaaT, family PSPI, pfam04468, interact directly with one another forming a stable ternary complex, in vitro. All three proteins are required for competence, sporulation and the formation of biofilms. The YmcA-YlbF-YaaT complex affects the phosphotransfer between Spo0F and Spo0B, thus accelerating the production of Spo0A~P. The three processes of biofilm formation, mature spore formation and competence all require the active, phosphorylated form of Spo0A, as Spo0A-P. Pssm-ID: 428784 [Multi-domain] Cd Length: 103 Bit Score: 40.60 E-value: 1.03e-03
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| PHA02716 | PHA02716 | CPXV016; CPX019; EVM010; Provisional |
272-464 | 1.04e-03 | ||||||||
CPXV016; CPX019; EVM010; Provisional Pssm-ID: 165089 [Multi-domain] Cd Length: 764 Bit Score: 44.52 E-value: 1.04e-03
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| ANK | smart00248 | ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
292-320 | 1.10e-03 | ||||||||
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure. Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 38.34 E-value: 1.10e-03
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| TRPV1-4 | cd22193 | Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ... |
1309-1419 | 1.29e-03 | ||||||||
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. Pssm-ID: 411977 [Multi-domain] Cd Length: 607 Bit Score: 44.02 E-value: 1.29e-03
|
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| PHA02884 | PHA02884 | ankyrin repeat protein; Provisional |
1191-1275 | 1.42e-03 | ||||||||
ankyrin repeat protein; Provisional Pssm-ID: 165212 [Multi-domain] Cd Length: 300 Bit Score: 43.43 E-value: 1.42e-03
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| TRPV3 | cd22194 | Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
1349-1501 | 1.43e-03 | ||||||||
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. Pssm-ID: 411978 [Multi-domain] Cd Length: 680 Bit Score: 43.98 E-value: 1.43e-03
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| ANK | smart00248 | ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
1210-1237 | 1.51e-03 | ||||||||
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure. Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 37.95 E-value: 1.51e-03
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| PHA03307 | PHA03307 | transcriptional regulator ICP4; Provisional |
1890-2218 | 1.54e-03 | ||||||||
transcriptional regulator ICP4; Provisional Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 44.01 E-value: 1.54e-03
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| TRPV3 | cd22194 | Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
323-544 | 1.88e-03 | ||||||||
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. Pssm-ID: 411978 [Multi-domain] Cd Length: 680 Bit Score: 43.59 E-value: 1.88e-03
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| KH-I_PEPPER_like_rpt3 | cd22461 | third type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana RNA-binding KH ... |
1790-1856 | 2.37e-03 | ||||||||
third type I K homology (KH) RNA-binding domain found in Arabidopsis thaliana RNA-binding KH domain-containing protein PEPPER and similar proteins; The family includes a group of plant RNA-binding KH domain-containing proteins, such as PEPPER and flowering locus K homology domain protein (FLK). PEPPER regulates vegetative and gynoecium development. It acts as a positive regulator of the central floral repressor FLOWERING LOCUS C. In concert with HUA2, PEPPER antagonizes FLK by positively regulating FLC probably at transcriptional and post-transcriptional levels, and thus acts as a negative regulator of flowering. FLK, also called flowering locus KH domain protein, regulates positively flowering by repressing FLC expression and post-transcriptional modification. PEPPER and FLK contain three K-homology (KH) RNA-binding domains. The model corresponds to the KH3 domain of PEPPER and FLK. Pssm-ID: 411889 Cd Length: 69 Bit Score: 38.69 E-value: 2.37e-03
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| KH-I_IGF2BP1_rpt4 | cd22499 | fourth type I K homology (KH) RNA-binding domain found in insulin-like growth factor 2 ... |
1793-1858 | 2.50e-03 | ||||||||
fourth type I K homology (KH) RNA-binding domain found in insulin-like growth factor 2 mRNA-binding protein 1 (IGF2BP1) and similar proteins; IGF2BP1, also called IGF2 mRNA-binding protein 1 (IMP-1), or coding region determinant-binding protein (CRD-BP), or IGF-II mRNA-binding protein 1, or VICKZ family member 1 (VICKZ1), or zipcode-binding protein 1 (ZBP-1), is an RNA-binding factor that recruits target transcripts to cytoplasmic protein-RNA complexes (mRNPs). It functions by binding to the 5' UTR of the insulin-like growth factor 2 (IGF2) mRNA and regulating IGF2 translation. It regulates localized beta-actin/ACTB mRNA translation, a crucial process for cell polarity, cell migration and neurite outgrowth. IGF2BP1 can form homodimers and heterodimers with IGF2BP1 and IGF2BP3. It contains four K-homology (KH) RNA-binding domains which are important in RNA binding and are known to be involved in RNA synthesis and metabolism. The model corresponds to the fourth one. Pssm-ID: 411927 Cd Length: 76 Bit Score: 38.86 E-value: 2.50e-03
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| Ank_5 | pfam13857 | Ankyrin repeats (many copies); |
1331-1387 | 2.60e-03 | ||||||||
Ankyrin repeats (many copies); Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 38.10 E-value: 2.60e-03
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| KH-I_PNPT1 | cd09033 | type I K homology (KH) RNA-binding domain found in mitochondrial polyribonucleotide ... |
1790-1825 | 2.67e-03 | ||||||||
type I K homology (KH) RNA-binding domain found in mitochondrial polyribonucleotide nucleotidyltransferase 1 (PNPT1) and similar proteins; PNPT1, also called 3'-5' RNA exonuclease OLD35, or PNPase old-35, or polynucleotide phosphorylase 1, or PNPase 1, or polynucleotide phosphorylase-like protein, is an RNA-binding protein implicated in numerous RNA metabolic processes. It catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'-to-5' direction. It acts as a mitochondrial intermembrane factor with RNA-processing exoribonulease activity. PNPT1 is a component of the mitochondrial degradosome (mtEXO) complex, that degrades 3' overhang double-stranded RNA with a 3'-to-5' directionality in an ATP-dependent manner. It is involved in the degradation of non-coding mitochondrial transcripts (MT-ncRNA) and tRNA-like molecules and required for correct processing and polyadenylation of mitochondrial mRNAs. PNPT1 also plays a role as a cytoplasmic RNA import factor that mediates the translocation of small RNA components, like the 5S RNA, the RNA subunit of ribonuclease P and the mitochondrial RNA-processing (MRP) RNA, into the mitochondrial matrix. Pssm-ID: 411809 [Multi-domain] Cd Length: 67 Bit Score: 38.33 E-value: 2.67e-03
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| Ank_5 | pfam13857 | Ankyrin repeats (many copies); |
1365-1417 | 2.71e-03 | ||||||||
Ankyrin repeats (many copies); Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 38.10 E-value: 2.71e-03
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| KH-I_PCBP1_2_rpt2 | cd22518 | second type I K homology (KH) RNA-binding domain found in poly(rC)-binding protein 1 (PCBP1) ... |
1792-1852 | 2.75e-03 | ||||||||
second type I K homology (KH) RNA-binding domain found in poly(rC)-binding protein 1 (PCBP1) and similar proteins; The family includes PCBP1 (also called alpha-CP1, or heterogeneous nuclear ribonucleoprotein E1, or hnRNP E1, or nucleic acid-binding protein SUB2.3) and PCBP2 (also called alpha-CP2, or heterogeneous nuclear ribonucleoprotein E2, or hnRNP E2). They are single-stranded nucleic acid binding proteins that bind preferentially to oligo dC. They act as iron chaperones for ferritin. In case of infection by poliovirus, PCBP1 plays a role in initiation of viral RNA replication in concert with the viral protein 3CD. PCBP2 is a major cellular poly(rC)-binding protein. It also binds poly(rU). PCBP2 negatively regulates cellular antiviral responses mediated by MAVS signaling. It acts as an adapter between MAVS and the E3 ubiquitin ligase ITCH, therefore triggering MAVS ubiquitination and degradation. PCBP2 forms a metabolon with the heme oxygenase 1/cytochrome P450 reductase complex for heme catabolism and iron transfer. Both PCBP1 and PCBP2 contain three K-homology (KH) RNA-binding domains. The model corresponds to the second one. Pssm-ID: 411946 [Multi-domain] Cd Length: 78 Bit Score: 38.95 E-value: 2.75e-03
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| Ank_5 | pfam13857 | Ankyrin repeats (many copies); |
1195-1252 | 2.87e-03 | ||||||||
Ankyrin repeats (many copies); Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 38.10 E-value: 2.87e-03
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| Ank_5 | pfam13857 | Ankyrin repeats (many copies); |
1173-1217 | 2.93e-03 | ||||||||
Ankyrin repeats (many copies); Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 38.10 E-value: 2.93e-03
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| TRPV3 | cd22194 | Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
293-480 | 2.96e-03 | ||||||||
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. Pssm-ID: 411978 [Multi-domain] Cd Length: 680 Bit Score: 43.21 E-value: 2.96e-03
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| KH-I_FUBP1_rpt4 | cd22487 | fourth type I K homology (KH) RNA-binding domain found in far upstream element-binding protein ... |
1793-1856 | 2.98e-03 | ||||||||
fourth type I K homology (KH) RNA-binding domain found in far upstream element-binding protein 1 (FUBP1) and similar proteins; FUBP1, also called FBP, or FUSE-binding protein 1, or DNA helicase V, or DH V, binds RNA and single-stranded DNA (ssDNA) and may act both as activator and repressor of transcription. It regulates MYC expression by binding to a single-stranded far-upstream element (FUSE) upstream of the MYC promoter. FUBP1 contains four K-homology (KH) RNA-binding domains. The model corresponds to the fourth one. Pssm-ID: 411915 Cd Length: 72 Bit Score: 38.40 E-value: 2.98e-03
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| PLN03192 | PLN03192 | Voltage-dependent potassium channel; Provisional |
1326-1432 | 3.05e-03 | ||||||||
Voltage-dependent potassium channel; Provisional Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 42.93 E-value: 3.05e-03
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| KH-I_PCBP4_rpt2 | cd22520 | second type I K homology (KH) RNA-binding domain found in poly(rC)-binding protein 4 (PCBP4) ... |
1792-1856 | 3.17e-03 | ||||||||
second type I K homology (KH) RNA-binding domain found in poly(rC)-binding protein 4 (PCBP4) and similar proteins; PCBP4, also called alpha-CP4, or heterogeneous nuclear ribonucleoprotein E4, or hnRNP E4, is a single-stranded nucleic acid binding protein that binds preferentially to oligo dC. It regulates both basal and stress-induced p21 expression through binding p21 3'-UTR and modulating p21 mRNA stability. It also plays a role in the cell cycle and is implicated in lung tumor suppression. PCBP4 contains three K-homology (KH) RNA-binding domains. The model corresponds to the second one. Pssm-ID: 411948 [Multi-domain] Cd Length: 72 Bit Score: 38.46 E-value: 3.17e-03
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| PHA02798 | PHA02798 | ankyrin-like protein; Provisional |
1124-1339 | 3.21e-03 | ||||||||
ankyrin-like protein; Provisional Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 42.90 E-value: 3.21e-03
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| PHA02876 | PHA02876 | ankyrin repeat protein; Provisional |
530-618 | 3.26e-03 | ||||||||
ankyrin repeat protein; Provisional Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 42.74 E-value: 3.26e-03
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| KH-I_Vigilin_rpt6 | cd02394 | sixth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ... |
1791-1857 | 3.39e-03 | ||||||||
sixth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, also called high density lipoprotein-binding protein, or HDL-binding protein, is a ubiquitous and highly conserved RNA-binding protein that shuttles between nucleus and cytoplasm presumably in contact with RNA molecules. It may be involved in chromosome partitioning at mitosis, facilitating translation and tRNA transport, and control of mRNA metabolism, including estrogen-mediated stabilization of vitellogenin mRNA. Vigilin is up-regulated by cholesterol loading of cells and functions to protect cells from over-accumulation of cholesterol. It may play a role in cell sterol metabolism. Disruption of human vigilin impairs chromosome condensation and segregation. Vigilin has a unique structure of 14-15 consecutively arranged, but non-identical K-homology (KH) domains which apparently mediate RNA-protein binding. The model corresponds to the sixth one. Pssm-ID: 411804 [Multi-domain] Cd Length: 68 Bit Score: 38.32 E-value: 3.39e-03
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| SMC_prok_B | TIGR02168 | chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
773-867 | 3.46e-03 | ||||||||
chromosome segregation protein SMC, common bacterial 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. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins] Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.12 E-value: 3.46e-03
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| PHA03100 | PHA03100 | ankyrin repeat protein; Provisional |
1100-1171 | 3.47e-03 | ||||||||
ankyrin repeat protein; Provisional Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 42.34 E-value: 3.47e-03
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| ANK | smart00248 | ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
361-384 | 3.48e-03 | ||||||||
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure. Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 37.18 E-value: 3.48e-03
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| COG4026 | COG4026 | Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ... |
792-866 | 3.67e-03 | ||||||||
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only]; Pssm-ID: 443204 [Multi-domain] Cd Length: 287 Bit Score: 42.02 E-value: 3.67e-03
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| Ank_5 | pfam13857 | Ankyrin repeats (many copies); |
576-631 | 3.90e-03 | ||||||||
Ankyrin repeats (many copies); Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 37.71 E-value: 3.90e-03
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| ANK | smart00248 | ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
1109-1137 | 3.99e-03 | ||||||||
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure. Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 36.80 E-value: 3.99e-03
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| Ank | pfam00023 | Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
1109-1141 | 4.02e-03 | ||||||||
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity. Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 36.88 E-value: 4.02e-03
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| PRK03918 | PRK03918 | DNA double-strand break repair ATPase Rad50; |
773-866 | 4.26e-03 | ||||||||
DNA double-strand break repair ATPase Rad50; Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 4.26e-03
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| trp | TIGR00870 | transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
1114-1302 | 4.39e-03 | ||||||||
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds] Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 42.38 E-value: 4.39e-03
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| Ank | pfam00023 | Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
1312-1340 | 4.52e-03 | ||||||||
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity. Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 36.88 E-value: 4.52e-03
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| TRPV1-4 | cd22193 | Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ... |
261-346 | 5.12e-03 | ||||||||
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. Pssm-ID: 411977 [Multi-domain] Cd Length: 607 Bit Score: 42.09 E-value: 5.12e-03
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| KH-I_IGF2BP_rpt3 | cd22402 | third type I K homology (KH) RNA-binding domain found in the insulin-like growth factor 2 ... |
1793-1844 | 5.61e-03 | ||||||||
third type I K homology (KH) RNA-binding domain found in the insulin-like growth factor 2 mRNA-binding protein (IGF2BP) family; The IGF2BP family includes three members: IGF2BP1/IMP-1/ CRD-BP/ VICKZ1, IGF2BP2/IMP-2/ VICKZ2, and IGF2BP3/IMP-3/VICKZ3, which are RNA-binding factors that recruit target transcripts to cytoplasmic protein-RNA complexes (mRNPs). They function by binding to the 5' UTR of the insulin-like growth factor 2 (IGF2) mRNA and regulating IGF2 translation. IGF2BP proteins contain four K-homology (KH) RNA-binding domains which are important in RNA binding and are known to be involved in RNA synthesis and metabolism. The model corresponds to the third one. Pssm-ID: 411830 [Multi-domain] Cd Length: 66 Bit Score: 37.62 E-value: 5.61e-03
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| Ank_3 | pfam13606 | Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
526-552 | 5.98e-03 | ||||||||
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 36.47 E-value: 5.98e-03
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| Ank_3 | pfam13606 | Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
557-585 | 6.04e-03 | ||||||||
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 36.47 E-value: 6.04e-03
|
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| Ank | pfam00023 | Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
393-421 | 6.26e-03 | ||||||||
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity. Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 36.50 E-value: 6.26e-03
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| PRK07003 | PRK07003 | DNA polymerase III subunit gamma/tau; |
1996-2254 | 7.09e-03 | ||||||||
DNA polymerase III subunit gamma/tau; Pssm-ID: 235906 [Multi-domain] Cd Length: 830 Bit Score: 41.76 E-value: 7.09e-03
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| KH-I_Rnc1_rpt1 | cd22455 | first type I K homology (KH) RNA-binding domain found in Schizosaccharomyces pombe RNA-binding ... |
1793-1852 | 7.94e-03 | ||||||||
first type I K homology (KH) RNA-binding domain found in Schizosaccharomyces pombe RNA-binding protein Rnc1 and similar proteins; Rnc1, also called RNA-binding protein that suppresses calcineurin deletion 1, is an RNA-binding protein that acts as an important regulator of the posttranscriptional expression of the MAPK phosphatase Pmp1 in fission yeast. It binds and stabilizes pmp1 mRNA and hence acts as a negative regulator of pmk1 signaling. Overexpression of Rnc1 suppresses the Cl(-) sensitivity of calcineurin deletion. The nuclear export of Rnc1 requires mRNA-binding ability and the mRNA export factor Rae1. Rnc1 contains three K-homology (KH) RNA-binding domains. The model corresponds to the first one. Pssm-ID: 411883 Cd Length: 70 Bit Score: 37.27 E-value: 7.94e-03
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| Ank_3 | pfam13606 | Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
261-287 | 8.28e-03 | ||||||||
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 36.08 E-value: 8.28e-03
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| KH-I_Vigilin_rpt5 | cd22409 | fifth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, ... |
1790-1864 | 8.94e-03 | ||||||||
fifth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, also called high density lipoprotein-binding protein, or HDL-binding protein, is a ubiquitous and highly conserved RNA-binding protein that shuttles between nucleus and cytoplasm presumably in contact with RNA molecules. It may be involved in chromosome partitioning at mitosis, facilitating translation and tRNA transport, and control of mRNA metabolism, including estrogen-mediated stabilization of vitellogenin mRNA. Vigilin is up-regulated by cholesterol loading of cells and functions to protect cells from over-accumulation of cholesterol. It may play a role in cell sterol metabolism. Disruption of human vigilin impairs chromosome condensation and segregation. Vigilin has a unique structure of 14-15 consecutively arranged, but non-identical K-homology (KH) domains which apparently mediate RNA-protein binding. The model corresponds to the fifth one. Pssm-ID: 411837 [Multi-domain] Cd Length: 70 Bit Score: 37.18 E-value: 8.94e-03
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| F-BAR_CIP4-like | cd07653 | The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Cdc42-Interacting Protein 4 ... |
812-866 | 9.16e-03 | ||||||||
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Cdc42-Interacting Protein 4 and similar proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. This subfamily is composed of Cdc42-Interacting Protein 4 (CIP4), Formin Binding Protein 17 (FBP17), FormiN Binding Protein 1-Like (FNBP1L), and similar proteins. CIP4 and FNBP1L are Cdc42 effectors that bind Wiskott-Aldrich syndrome protein (WASP) and function in endocytosis. CIP4 and FBP17 bind to the Fas ligand and may be implicated in the inflammatory response. CIP4 may also play a role in phagocytosis. Members of this subfamily typically contain an N-terminal F-BAR domain and a C-terminal SH3 domain. In addition, some members such as FNBP1L contain a central Cdc42-binding HR1 domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules. Pssm-ID: 153337 [Multi-domain] Cd Length: 251 Bit Score: 40.31 E-value: 9.16e-03
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| TRPV3 | cd22194 | Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
1169-1397 | 9.64e-03 | ||||||||
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. Pssm-ID: 411978 [Multi-domain] Cd Length: 680 Bit Score: 41.28 E-value: 9.64e-03
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