inversin isoform X1 [Macaca mulatta]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| ANKYR | COG0666 | Ankyrin repeat [Signal transduction mechanisms]; |
270-560 | 1.43e-51 | |||||
Ankyrin repeat [Signal transduction mechanisms]; : Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 183.23 E-value: 1.43e-51
|
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| ANKYR | COG0666 | Ankyrin repeat [Signal transduction mechanisms]; |
19-240 | 7.45e-37 | |||||
Ankyrin repeat [Signal transduction mechanisms]; : Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 140.86 E-value: 7.45e-37
|
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| PHA03307 super family | cl33723 | transcriptional regulator ICP4; Provisional |
615-832 | 5.99e-07 | |||||
transcriptional regulator ICP4; Provisional The actual alignment was detected with superfamily member PHA03307: Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 54.02 E-value: 5.99e-07
|
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| Ank_4 | pfam13637 | Ankyrin repeats (many copies); |
221-275 | 8.53e-06 | |||||
Ankyrin repeats (many copies); : Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 44.19 E-value: 8.53e-06
|
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| IQCD | cd23767 | IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ... |
908-939 | 2.39e-04 | |||||
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory complex protein 10 (DRC10), belongs to the IQ motif-containing protein family which contains a C-terminal conserved IQ motif domain and two coiled-coil domains. The IQ motif ([ILV]QxxxRxxxx[RK]), where x stands for any amino-acid residue, interacts with calmodulin (CaM) in a calcium-independent manner and is present in proteins with a wide diversity of biological functions. The IQCD protein was found to primarily accumulate in the acrosome area of round and elongating spermatids of the testis during late stage of spermiogenesis and was then localized to the acrosome and tail regions of mature spermatozoa. The expression of IQCD follows the trajectory of acrosome development during spermatogenesis. IQCD is associated with neuroblastoma and neurodegenerative diseases, and is reported to interact with the nuclear retinoid X receptor in the presence of 9-cis-retinoic acid, thereby activating the transcriptional activity of the receptor. : Pssm-ID: 467745 [Multi-domain] Cd Length: 37 Bit Score: 39.45 E-value: 2.39e-04
|
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| IQCD | cd23767 | IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ... |
553-579 | 1.39e-03 | |||||
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory complex protein 10 (DRC10), belongs to the IQ motif-containing protein family which contains a C-terminal conserved IQ motif domain and two coiled-coil domains. The IQ motif ([ILV]QxxxRxxxx[RK]), where x stands for any amino-acid residue, interacts with calmodulin (CaM) in a calcium-independent manner and is present in proteins with a wide diversity of biological functions. The IQCD protein was found to primarily accumulate in the acrosome area of round and elongating spermatids of the testis during late stage of spermiogenesis and was then localized to the acrosome and tail regions of mature spermatozoa. The expression of IQCD follows the trajectory of acrosome development during spermatogenesis. IQCD is associated with neuroblastoma and neurodegenerative diseases, and is reported to interact with the nuclear retinoid X receptor in the presence of 9-cis-retinoic acid, thereby activating the transcriptional activity of the receptor. : Pssm-ID: 467745 [Multi-domain] Cd Length: 37 Bit Score: 37.14 E-value: 1.39e-03
|
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| Name | Accession | Description | Interval | E-value | |||||
| ANKYR | COG0666 | Ankyrin repeat [Signal transduction mechanisms]; |
270-560 | 1.43e-51 | |||||
Ankyrin repeat [Signal transduction mechanisms]; Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 183.23 E-value: 1.43e-51
|
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| ANKYR | COG0666 | Ankyrin repeat [Signal transduction mechanisms]; |
19-240 | 7.45e-37 | |||||
Ankyrin repeat [Signal transduction mechanisms]; Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 140.86 E-value: 7.45e-37
|
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| PHA03100 | PHA03100 | ankyrin repeat protein; Provisional |
336-554 | 1.05e-23 | |||||
ankyrin repeat protein; Provisional Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 105.13 E-value: 1.05e-23
|
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| Ank_2 | pfam12796 | Ankyrin repeats (3 copies); |
394-486 | 5.43e-22 | |||||
Ankyrin repeats (3 copies); Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 91.33 E-value: 5.43e-22
|
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| PHA02874 | PHA02874 | ankyrin repeat protein; Provisional |
62-262 | 3.89e-20 | |||||
ankyrin repeat protein; Provisional Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 94.65 E-value: 3.89e-20
|
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| Ank_2 | pfam12796 | Ankyrin repeats (3 copies); |
85-179 | 2.03e-19 | |||||
Ankyrin repeats (3 copies); Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 84.01 E-value: 2.03e-19
|
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| TRPV5-6 | cd22192 | Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
291-497 | 4.32e-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: 60.41 E-value: 4.32e-09
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| TRPV5-6 | cd22192 | Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
166-294 | 9.13e-08 | |||||
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: 56.17 E-value: 9.13e-08
|
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| PHA03307 | PHA03307 | transcriptional regulator ICP4; Provisional |
615-832 | 5.99e-07 | |||||
transcriptional regulator ICP4; Provisional Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 54.02 E-value: 5.99e-07
|
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| Ank_4 | pfam13637 | Ankyrin repeats (many copies); |
221-275 | 8.53e-06 | |||||
Ankyrin repeats (many copies); Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 44.19 E-value: 8.53e-06
|
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| PTZ00322 | PTZ00322 | 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
215-275 | 1.15e-04 | |||||
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 46.04 E-value: 1.15e-04
|
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| trp | TIGR00870 | transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
150-345 | 1.22e-04 | |||||
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: 46.23 E-value: 1.22e-04
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| ANK | smart00248 | ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
48-76 | 1.60e-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: 1.60e-04
|
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| IQCD | cd23767 | IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ... |
908-939 | 2.39e-04 | |||||
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory complex protein 10 (DRC10), belongs to the IQ motif-containing protein family which contains a C-terminal conserved IQ motif domain and two coiled-coil domains. The IQ motif ([ILV]QxxxRxxxx[RK]), where x stands for any amino-acid residue, interacts with calmodulin (CaM) in a calcium-independent manner and is present in proteins with a wide diversity of biological functions. The IQCD protein was found to primarily accumulate in the acrosome area of round and elongating spermatids of the testis during late stage of spermiogenesis and was then localized to the acrosome and tail regions of mature spermatozoa. The expression of IQCD follows the trajectory of acrosome development during spermatogenesis. IQCD is associated with neuroblastoma and neurodegenerative diseases, and is reported to interact with the nuclear retinoid X receptor in the presence of 9-cis-retinoic acid, thereby activating the transcriptional activity of the receptor. Pssm-ID: 467745 [Multi-domain] Cd Length: 37 Bit Score: 39.45 E-value: 2.39e-04
|
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| ANK | smart00248 | ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
422-451 | 3.64e-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: 38.72 E-value: 3.64e-04
|
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| IQCD | cd23767 | IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ... |
553-579 | 1.39e-03 | |||||
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory complex protein 10 (DRC10), belongs to the IQ motif-containing protein family which contains a C-terminal conserved IQ motif domain and two coiled-coil domains. The IQ motif ([ILV]QxxxRxxxx[RK]), where x stands for any amino-acid residue, interacts with calmodulin (CaM) in a calcium-independent manner and is present in proteins with a wide diversity of biological functions. The IQCD protein was found to primarily accumulate in the acrosome area of round and elongating spermatids of the testis during late stage of spermiogenesis and was then localized to the acrosome and tail regions of mature spermatozoa. The expression of IQCD follows the trajectory of acrosome development during spermatogenesis. IQCD is associated with neuroblastoma and neurodegenerative diseases, and is reported to interact with the nuclear retinoid X receptor in the presence of 9-cis-retinoic acid, thereby activating the transcriptional activity of the receptor. Pssm-ID: 467745 [Multi-domain] Cd Length: 37 Bit Score: 37.14 E-value: 1.39e-03
|
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| ANK | smart00248 | ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
256-280 | 3.26e-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: 36.03 E-value: 3.26e-03
|
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| Name | Accession | Description | Interval | E-value | |||||||
| ANKYR | COG0666 | Ankyrin repeat [Signal transduction mechanisms]; |
270-560 | 1.43e-51 | |||||||
Ankyrin repeat [Signal transduction mechanisms]; Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 183.23 E-value: 1.43e-51
|
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| ANKYR | COG0666 | Ankyrin repeat [Signal transduction mechanisms]; |
306-594 | 1.79e-48 | |||||||
Ankyrin repeat [Signal transduction mechanisms]; Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 174.37 E-value: 1.79e-48
|
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| ANKYR | COG0666 | Ankyrin repeat [Signal transduction mechanisms]; |
247-493 | 1.31e-45 | |||||||
Ankyrin repeat [Signal transduction mechanisms]; Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 166.28 E-value: 1.31e-45
|
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| ANKYR | COG0666 | Ankyrin repeat [Signal transduction mechanisms]; |
19-240 | 7.45e-37 | |||||||
Ankyrin repeat [Signal transduction mechanisms]; Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 140.86 E-value: 7.45e-37
|
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| ANKYR | COG0666 | Ankyrin repeat [Signal transduction mechanisms]; |
1-324 | 5.98e-36 | |||||||
Ankyrin repeat [Signal transduction mechanisms]; Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 138.16 E-value: 5.98e-36
|
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| ANKYR | COG0666 | Ankyrin repeat [Signal transduction mechanisms]; |
96-460 | 2.63e-34 | |||||||
Ankyrin repeat [Signal transduction mechanisms]; Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 133.54 E-value: 2.63e-34
|
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| ANKYR | COG0666 | Ankyrin repeat [Signal transduction mechanisms]; |
64-355 | 1.77e-33 | |||||||
Ankyrin repeat [Signal transduction mechanisms]; Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 131.23 E-value: 1.77e-33
|
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| ANKYR | COG0666 | Ankyrin repeat [Signal transduction mechanisms]; |
19-186 | 6.75e-25 | |||||||
Ankyrin repeat [Signal transduction mechanisms]; Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 106.19 E-value: 6.75e-25
|
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| PHA03100 | PHA03100 | ankyrin repeat protein; Provisional |
336-554 | 1.05e-23 | |||||||
ankyrin repeat protein; Provisional Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 105.13 E-value: 1.05e-23
|
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| Ank_2 | pfam12796 | Ankyrin repeats (3 copies); |
394-486 | 5.43e-22 | |||||||
Ankyrin repeats (3 copies); Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 91.33 E-value: 5.43e-22
|
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| Ank_2 | pfam12796 | Ankyrin repeats (3 copies); |
427-518 | 6.28e-22 | |||||||
Ankyrin repeats (3 copies); Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 90.95 E-value: 6.28e-22
|
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| Ank_2 | pfam12796 | Ankyrin repeats (3 copies); |
361-453 | 1.02e-21 | |||||||
Ankyrin repeats (3 copies); Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 90.56 E-value: 1.02e-21
|
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| PHA02876 | PHA02876 | ankyrin repeat protein; Provisional |
141-548 | 1.68e-20 | |||||||
ankyrin repeat protein; Provisional Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 97.44 E-value: 1.68e-20
|
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| PHA02874 | PHA02874 | ankyrin repeat protein; Provisional |
62-262 | 3.89e-20 | |||||||
ankyrin repeat protein; Provisional Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 94.65 E-value: 3.89e-20
|
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| PHA03100 | PHA03100 | ankyrin repeat protein; Provisional |
120-421 | 4.04e-20 | |||||||
ankyrin repeat protein; Provisional Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 94.35 E-value: 4.04e-20
|
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| Ank_2 | pfam12796 | Ankyrin repeats (3 copies); |
293-387 | 4.50e-20 | |||||||
Ankyrin repeats (3 copies); Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 85.94 E-value: 4.50e-20
|
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| PHA02876 | PHA02876 | ankyrin repeat protein; Provisional |
59-416 | 9.77e-20 | |||||||
ankyrin repeat protein; Provisional Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 95.13 E-value: 9.77e-20
|
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| Ank_2 | pfam12796 | Ankyrin repeats (3 copies); |
85-179 | 2.03e-19 | |||||||
Ankyrin repeats (3 copies); Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 84.01 E-value: 2.03e-19
|
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| Ank_2 | pfam12796 | Ankyrin repeats (3 copies); |
460-548 | 2.62e-19 | |||||||
Ankyrin repeats (3 copies); Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 83.63 E-value: 2.62e-19
|
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| PHA03095 | PHA03095 | ankyrin-like protein; Provisional |
252-495 | 5.79e-19 | |||||||
ankyrin-like protein; Provisional Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 91.24 E-value: 5.79e-19
|
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| PHA03095 | PHA03095 | ankyrin-like protein; Provisional |
32-315 | 1.35e-17 | |||||||
ankyrin-like protein; Provisional Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 87.00 E-value: 1.35e-17
|
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| PHA02874 | PHA02874 | ankyrin repeat protein; Provisional |
214-493 | 2.13e-17 | |||||||
ankyrin repeat protein; Provisional Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 86.17 E-value: 2.13e-17
|
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| Ank_2 | pfam12796 | Ankyrin repeats (3 copies); |
19-111 | 1.71e-16 | |||||||
Ankyrin repeats (3 copies); Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 75.54 E-value: 1.71e-16
|
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| Ank_2 | pfam12796 | Ankyrin repeats (3 copies); |
225-319 | 5.29e-16 | |||||||
Ankyrin repeats (3 copies); Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 74.38 E-value: 5.29e-16
|
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| PHA03095 | PHA03095 | ankyrin-like protein; Provisional |
344-548 | 1.13e-15 | |||||||
ankyrin-like protein; Provisional Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 81.22 E-value: 1.13e-15
|
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| PHA03095 | PHA03095 | ankyrin-like protein; Provisional |
163-460 | 1.82e-15 | |||||||
ankyrin-like protein; Provisional Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 80.45 E-value: 1.82e-15
|
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| PHA02875 | PHA02875 | ankyrin repeat protein; Provisional |
215-451 | 3.70e-15 | |||||||
ankyrin repeat protein; Provisional Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 78.88 E-value: 3.70e-15
|
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| PHA02874 | PHA02874 | ankyrin repeat protein; Provisional |
291-532 | 4.76e-15 | |||||||
ankyrin repeat protein; Provisional Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 78.85 E-value: 4.76e-15
|
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| Ank_2 | pfam12796 | Ankyrin repeats (3 copies); |
153-252 | 9.27e-15 | |||||||
Ankyrin repeats (3 copies); Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 70.53 E-value: 9.27e-15
|
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| PHA02874 | PHA02874 | ankyrin repeat protein; Provisional |
350-557 | 2.46e-14 | |||||||
ankyrin repeat protein; Provisional Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 76.54 E-value: 2.46e-14
|
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| Ank_2 | pfam12796 | Ankyrin repeats (3 copies); |
186-278 | 5.00e-14 | |||||||
Ankyrin repeats (3 copies); Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 68.60 E-value: 5.00e-14
|
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| PHA03100 | PHA03100 | ankyrin repeat protein; Provisional |
370-548 | 5.02e-14 | |||||||
ankyrin repeat protein; Provisional Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 75.47 E-value: 5.02e-14
|
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| PHA02878 | PHA02878 | ankyrin repeat protein; Provisional |
224-493 | 1.44e-13 | |||||||
ankyrin repeat protein; Provisional Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 74.53 E-value: 1.44e-13
|
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| PHA03095 | PHA03095 | ankyrin-like protein; Provisional |
17-201 | 2.02e-13 | |||||||
ankyrin-like protein; Provisional Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 73.91 E-value: 2.02e-13
|
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| PHA03100 | PHA03100 | ankyrin repeat protein; Provisional |
49-205 | 7.16e-13 | |||||||
ankyrin repeat protein; Provisional Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 72.01 E-value: 7.16e-13
|
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| PHA02875 | PHA02875 | ankyrin repeat protein; Provisional |
333-548 | 8.19e-13 | |||||||
ankyrin repeat protein; Provisional Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 71.56 E-value: 8.19e-13
|
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| PHA02878 | PHA02878 | ankyrin repeat protein; Provisional |
61-394 | 1.27e-12 | |||||||
ankyrin repeat protein; Provisional Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 71.45 E-value: 1.27e-12
|
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| PHA02874 | PHA02874 | ankyrin repeat protein; Provisional |
92-477 | 2.10e-12 | |||||||
ankyrin repeat protein; Provisional Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 70.38 E-value: 2.10e-12
|
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| PLN03192 | PLN03192 | Voltage-dependent potassium channel; Provisional |
262-477 | 3.94e-11 | |||||||
Voltage-dependent potassium channel; Provisional Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 67.20 E-value: 3.94e-11
|
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| Ank_4 | pfam13637 | Ankyrin repeats (many copies); |
48-101 | 4.27e-11 | |||||||
Ankyrin repeats (many copies); Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 58.83 E-value: 4.27e-11
|
|||||||||||
| PHA02878 | PHA02878 | ankyrin repeat protein; Provisional |
51-276 | 4.98e-11 | |||||||
ankyrin repeat protein; Provisional Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 66.44 E-value: 4.98e-11
|
|||||||||||
| Ank_4 | pfam13637 | Ankyrin repeats (many copies); |
357-410 | 1.54e-10 | |||||||
Ankyrin repeats (many copies); Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 57.28 E-value: 1.54e-10
|
|||||||||||
| PHA02798 | PHA02798 | ankyrin-like protein; Provisional |
404-529 | 2.17e-10 | |||||||
ankyrin-like protein; Provisional Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 64.47 E-value: 2.17e-10
|
|||||||||||
| PHA03100 | PHA03100 | ankyrin repeat protein; Provisional |
50-243 | 2.98e-10 | |||||||
ankyrin repeat protein; Provisional Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 63.53 E-value: 2.98e-10
|
|||||||||||
| PHA02875 | PHA02875 | ankyrin repeat protein; Provisional |
16-175 | 3.75e-10 | |||||||
ankyrin repeat protein; Provisional Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 63.47 E-value: 3.75e-10
|
|||||||||||
| Ank_4 | pfam13637 | Ankyrin repeats (many copies); |
423-475 | 3.78e-10 | |||||||
Ankyrin repeats (many copies); Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 56.13 E-value: 3.78e-10
|
|||||||||||
| PHA02875 | PHA02875 | ankyrin repeat protein; Provisional |
222-400 | 4.16e-10 | |||||||
ankyrin repeat protein; Provisional Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 63.09 E-value: 4.16e-10
|
|||||||||||
| PLN03192 | PLN03192 | Voltage-dependent potassium channel; Provisional |
298-481 | 9.45e-10 | |||||||
Voltage-dependent potassium channel; Provisional Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 62.96 E-value: 9.45e-10
|
|||||||||||
| PHA02874 | PHA02874 | ankyrin repeat protein; Provisional |
18-195 | 1.13e-09 | |||||||
ankyrin repeat protein; Provisional Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 61.90 E-value: 1.13e-09
|
|||||||||||
| Ank_4 | pfam13637 | Ankyrin repeats (many copies); |
456-509 | 1.16e-09 | |||||||
Ankyrin repeats (many copies); Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 54.97 E-value: 1.16e-09
|
|||||||||||
| PHA02875 | PHA02875 | ankyrin repeat protein; Provisional |
48-248 | 2.44e-09 | |||||||
ankyrin repeat protein; Provisional Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 60.78 E-value: 2.44e-09
|
|||||||||||
| PHA02876 | PHA02876 | ankyrin repeat protein; Provisional |
335-558 | 4.28e-09 | |||||||
ankyrin repeat protein; Provisional Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 60.46 E-value: 4.28e-09
|
|||||||||||
| TRPV5-6 | cd22192 | Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
291-497 | 4.32e-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: 60.41 E-value: 4.32e-09
|
|||||||||||
| Ank_4 | pfam13637 | Ankyrin repeats (many copies); |
322-377 | 4.91e-09 | |||||||
Ankyrin repeats (many copies); Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 53.05 E-value: 4.91e-09
|
|||||||||||
| PTZ00322 | PTZ00322 | 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
426-509 | 5.10e-09 | |||||||
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 60.30 E-value: 5.10e-09
|
|||||||||||
| PTZ00322 | PTZ00322 | 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
474-546 | 6.11e-09 | |||||||
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 59.91 E-value: 6.11e-09
|
|||||||||||
| Ank_4 | pfam13637 | Ankyrin repeats (many copies); |
392-443 | 1.64e-08 | |||||||
Ankyrin repeats (many copies); Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 51.51 E-value: 1.64e-08
|
|||||||||||
| PTZ00322 | PTZ00322 | 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
226-323 | 3.05e-08 | |||||||
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 57.99 E-value: 3.05e-08
|
|||||||||||
| PLN03192 | PLN03192 | Voltage-dependent potassium channel; Provisional |
430-516 | 8.99e-08 | |||||||
Voltage-dependent potassium channel; Provisional Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 56.41 E-value: 8.99e-08
|
|||||||||||
| TRPV5-6 | cd22192 | Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
166-294 | 9.13e-08 | |||||||
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: 56.17 E-value: 9.13e-08
|
|||||||||||
| TRPV5-6 | cd22192 | Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
21-236 | 9.36e-08 | |||||||
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: 56.17 E-value: 9.36e-08
|
|||||||||||
| PHA02875 | PHA02875 | ankyrin repeat protein; Provisional |
430-548 | 5.00e-07 | |||||||
ankyrin repeat protein; Provisional Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 53.46 E-value: 5.00e-07
|
|||||||||||
| PHA03307 | PHA03307 | transcriptional regulator ICP4; Provisional |
615-832 | 5.99e-07 | |||||||
transcriptional regulator ICP4; Provisional Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 54.02 E-value: 5.99e-07
|
|||||||||||
| PTZ00322 | PTZ00322 | 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
365-442 | 6.27e-07 | |||||||
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 53.75 E-value: 6.27e-07
|
|||||||||||
| Ank_5 | pfam13857 | Ankyrin repeats (many copies); |
442-494 | 6.60e-07 | |||||||
Ankyrin repeats (many copies); Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 47.34 E-value: 6.60e-07
|
|||||||||||
| PTZ00322 | PTZ00322 | 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
334-411 | 7.25e-07 | |||||||
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 53.36 E-value: 7.25e-07
|
|||||||||||
| Ank_5 | pfam13857 | Ankyrin repeats (many copies); |
67-120 | 1.98e-06 | |||||||
Ankyrin repeats (many copies); Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 45.80 E-value: 1.98e-06
|
|||||||||||
| Ank_5 | pfam13857 | Ankyrin repeats (many copies); |
479-531 | 2.41e-06 | |||||||
Ankyrin repeats (many copies); Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 45.80 E-value: 2.41e-06
|
|||||||||||
| Ank_4 | pfam13637 | Ankyrin repeats (many copies); |
256-309 | 2.87e-06 | |||||||
Ankyrin repeats (many copies); Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 45.34 E-value: 2.87e-06
|
|||||||||||
| Ank_5 | pfam13857 | Ankyrin repeats (many copies); |
412-463 | 3.26e-06 | |||||||
Ankyrin repeats (many copies); Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 45.42 E-value: 3.26e-06
|
|||||||||||
| PHA02878 | PHA02878 | ankyrin repeat protein; Provisional |
33-186 | 3.31e-06 | |||||||
ankyrin repeat protein; Provisional Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 51.03 E-value: 3.31e-06
|
|||||||||||
| PHA02791 | PHA02791 | ankyrin-like protein; Provisional |
218-411 | 3.84e-06 | |||||||
ankyrin-like protein; Provisional Pssm-ID: 165154 [Multi-domain] Cd Length: 284 Bit Score: 50.04 E-value: 3.84e-06
|
|||||||||||
| Ank_4 | pfam13637 | Ankyrin repeats (many copies); |
489-544 | 4.25e-06 | |||||||
Ankyrin repeats (many copies); Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 44.96 E-value: 4.25e-06
|
|||||||||||
| Ank_5 | pfam13857 | Ankyrin repeats (many copies); |
139-189 | 6.06e-06 | |||||||
Ankyrin repeats (many copies); Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 44.64 E-value: 6.06e-06
|
|||||||||||
| Ank_4 | pfam13637 | Ankyrin repeats (many copies); |
221-275 | 8.53e-06 | |||||||
Ankyrin repeats (many copies); Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 44.19 E-value: 8.53e-06
|
|||||||||||
| PHA03307 | PHA03307 | transcriptional regulator ICP4; Provisional |
614-834 | 1.57e-05 | |||||||
transcriptional regulator ICP4; Provisional Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 49.40 E-value: 1.57e-05
|
|||||||||||
| PTZ00322 | PTZ00322 | 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
406-476 | 4.79e-05 | |||||||
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 47.59 E-value: 4.79e-05
|
|||||||||||
| Ank_4 | pfam13637 | Ankyrin repeats (many copies); |
81-134 | 5.97e-05 | |||||||
Ankyrin repeats (many copies); Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 41.49 E-value: 5.97e-05
|
|||||||||||
| PHA02798 | PHA02798 | ankyrin-like protein; Provisional |
373-591 | 6.10e-05 | |||||||
ankyrin-like protein; Provisional Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 46.75 E-value: 6.10e-05
|
|||||||||||
| PHA03307 | PHA03307 | transcriptional regulator ICP4; Provisional |
611-817 | 6.13e-05 | |||||||
transcriptional regulator ICP4; Provisional Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 47.47 E-value: 6.13e-05
|
|||||||||||
| Ank | pfam00023 | Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
356-387 | 7.17e-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: 40.74 E-value: 7.17e-05
|
|||||||||||
| PHA02875 | PHA02875 | ankyrin repeat protein; Provisional |
389-548 | 8.49e-05 | |||||||
ankyrin repeat protein; Provisional Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 46.14 E-value: 8.49e-05
|
|||||||||||
| PTZ00322 | PTZ00322 | 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
215-275 | 1.15e-04 | |||||||
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 46.04 E-value: 1.15e-04
|
|||||||||||
| trp | TIGR00870 | transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
150-345 | 1.22e-04 | |||||||
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: 46.23 E-value: 1.22e-04
|
|||||||||||
| Ank_5 | pfam13857 | Ankyrin repeats (many copies); |
33-88 | 1.45e-04 | |||||||
Ankyrin repeats (many copies); Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 40.79 E-value: 1.45e-04
|
|||||||||||
| ANK | smart00248 | ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
48-76 | 1.60e-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: 1.60e-04
|
|||||||||||
| IQCD | cd23767 | IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ... |
908-939 | 2.39e-04 | |||||||
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory complex protein 10 (DRC10), belongs to the IQ motif-containing protein family which contains a C-terminal conserved IQ motif domain and two coiled-coil domains. The IQ motif ([ILV]QxxxRxxxx[RK]), where x stands for any amino-acid residue, interacts with calmodulin (CaM) in a calcium-independent manner and is present in proteins with a wide diversity of biological functions. The IQCD protein was found to primarily accumulate in the acrosome area of round and elongating spermatids of the testis during late stage of spermiogenesis and was then localized to the acrosome and tail regions of mature spermatozoa. The expression of IQCD follows the trajectory of acrosome development during spermatogenesis. IQCD is associated with neuroblastoma and neurodegenerative diseases, and is reported to interact with the nuclear retinoid X receptor in the presence of 9-cis-retinoic acid, thereby activating the transcriptional activity of the receptor. Pssm-ID: 467745 [Multi-domain] Cd Length: 37 Bit Score: 39.45 E-value: 2.39e-04
|
|||||||||||
| Ank | pfam00023 | Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
48-79 | 2.40e-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: 39.19 E-value: 2.40e-04
|
|||||||||||
| Ank_5 | pfam13857 | Ankyrin repeats (many copies); |
243-296 | 3.61e-04 | |||||||
Ankyrin repeats (many copies); Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 39.64 E-value: 3.61e-04
|
|||||||||||
| ANK | smart00248 | ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
422-451 | 3.64e-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: 38.72 E-value: 3.64e-04
|
|||||||||||
| Ank_5 | pfam13857 | Ankyrin repeats (many copies); |
347-394 | 3.91e-04 | |||||||
Ankyrin repeats (many copies); Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 39.25 E-value: 3.91e-04
|
|||||||||||
| PHA03100 | PHA03100 | ankyrin repeat protein; Provisional |
45-106 | 6.09e-04 | |||||||
ankyrin repeat protein; Provisional Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 43.50 E-value: 6.09e-04
|
|||||||||||
| ANK | smart00248 | ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
148-175 | 6.51e-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: 37.95 E-value: 6.51e-04
|
|||||||||||
| ANK | smart00248 | ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
488-516 | 6.83e-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: 37.95 E-value: 6.83e-04
|
|||||||||||
| trp | TIGR00870 | transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
326-545 | 6.94e-04 | |||||||
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: 43.53 E-value: 6.94e-04
|
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| Ank_4 | pfam13637 | Ankyrin repeats (many copies); |
151-199 | 7.85e-04 | |||||||
Ankyrin repeats (many copies); Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 38.41 E-value: 7.85e-04
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| PHA02878 | PHA02878 | ankyrin repeat protein; Provisional |
292-548 | 8.23e-04 | |||||||
ankyrin repeat protein; Provisional Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 43.33 E-value: 8.23e-04
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| trp | TIGR00870 | transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
228-477 | 1.00e-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: 43.15 E-value: 1.00e-03
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| Ank | pfam00023 | Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
422-453 | 1.05e-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: 37.65 E-value: 1.05e-03
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| Ank_3 | pfam13606 | Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
422-451 | 1.16e-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: 37.24 E-value: 1.16e-03
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| PHA02946 | PHA02946 | ankyin-like protein; Provisional |
95-410 | 1.19e-03 | |||||||
ankyin-like protein; Provisional Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 42.73 E-value: 1.19e-03
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| TRPV | cd21882 | Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
336-497 | 1.22e-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). Pssm-ID: 411975 [Multi-domain] Cd Length: 600 Bit Score: 42.94 E-value: 1.22e-03
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| Ank | pfam00023 | Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
456-487 | 1.26e-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: 37.27 E-value: 1.26e-03
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| ANK | smart00248 | ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
456-484 | 1.29e-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: 1.29e-03
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| IQCD | cd23767 | IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ... |
553-579 | 1.39e-03 | |||||||
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory complex protein 10 (DRC10), belongs to the IQ motif-containing protein family which contains a C-terminal conserved IQ motif domain and two coiled-coil domains. The IQ motif ([ILV]QxxxRxxxx[RK]), where x stands for any amino-acid residue, interacts with calmodulin (CaM) in a calcium-independent manner and is present in proteins with a wide diversity of biological functions. The IQCD protein was found to primarily accumulate in the acrosome area of round and elongating spermatids of the testis during late stage of spermiogenesis and was then localized to the acrosome and tail regions of mature spermatozoa. The expression of IQCD follows the trajectory of acrosome development during spermatogenesis. IQCD is associated with neuroblastoma and neurodegenerative diseases, and is reported to interact with the nuclear retinoid X receptor in the presence of 9-cis-retinoic acid, thereby activating the transcriptional activity of the receptor. Pssm-ID: 467745 [Multi-domain] Cd Length: 37 Bit Score: 37.14 E-value: 1.39e-03
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| PTZ00322 | PTZ00322 | 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
55-135 | 1.39e-03 | |||||||
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 42.58 E-value: 1.39e-03
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| PLN03192 | PLN03192 | Voltage-dependent potassium channel; Provisional |
65-318 | 1.46e-03 | |||||||
Voltage-dependent potassium channel; Provisional Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 42.55 E-value: 1.46e-03
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| ANK | smart00248 | ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
82-106 | 1.46e-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: 1.46e-03
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| Ank_3 | pfam13606 | Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
356-385 | 1.69e-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: 36.85 E-value: 1.69e-03
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| Ank_4 | pfam13637 | Ankyrin repeats (many copies); |
114-169 | 2.23e-03 | |||||||
Ankyrin repeats (many copies); Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 37.25 E-value: 2.23e-03
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| Ank_3 | pfam13606 | Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
47-76 | 2.27e-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: 2.27e-03
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| Ank_4 | pfam13637 | Ankyrin repeats (many copies); |
185-240 | 2.34e-03 | |||||||
Ankyrin repeats (many copies); Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 37.25 E-value: 2.34e-03
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| ANK | smart00248 | ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
359-385 | 2.40e-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: 36.41 E-value: 2.40e-03
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| Ank | pfam00023 | Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
82-111 | 2.72e-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: 2.72e-03
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| Ank_5 | pfam13857 | Ankyrin repeats (many copies); |
316-364 | 3.15e-03 | |||||||
Ankyrin repeats (many copies); Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 36.94 E-value: 3.15e-03
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| ANK | smart00248 | ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
256-280 | 3.26e-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: 36.03 E-value: 3.26e-03
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| PHA02876 | PHA02876 | ankyrin repeat protein; Provisional |
405-581 | 3.41e-03 | |||||||
ankyrin repeat protein; Provisional Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 41.59 E-value: 3.41e-03
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| Ank_3 | pfam13606 | Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
148-177 | 5.78e-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: 35.31 E-value: 5.78e-03
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| Ank_3 | pfam13606 | Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
256-278 | 5.89e-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: 35.31 E-value: 5.89e-03
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| PTZ00322 | PTZ00322 | 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
22-101 | 8.39e-03 | |||||||
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 40.27 E-value: 8.39e-03
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