ankyrin repeat domain-containing protein 42 isoform 1 [Homo sapiens]
List of domain hits
Name | Accession | Description | Interval | E-value | ||||||
ANKYR | COG0666 | Ankyrin repeat [Signal transduction mechanisms]; |
30-264 | 1.33e-35 | ||||||
Ankyrin repeat [Signal transduction mechanisms]; : Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 134.70 E-value: 1.33e-35
|
||||||||||
PHA03100 super family | cl39094 | ankyrin repeat protein; Provisional |
112-444 | 1.19e-11 | ||||||
ankyrin repeat protein; Provisional The actual alignment was detected with superfamily member PHA03100: Pssm-ID: 476869 [Multi-domain] Cd Length: 422 Bit Score: 66.61 E-value: 1.19e-11
|
||||||||||
COG4372 | COG4372 | Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
426-482 | 1.94e-04 | ||||||
Uncharacterized protein, contains DUF3084 domain [Function unknown]; : Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.74 E-value: 1.94e-04
|
||||||||||
Name | Accession | Description | Interval | E-value | ||||||
ANKYR | COG0666 | Ankyrin repeat [Signal transduction mechanisms]; |
30-264 | 1.33e-35 | ||||||
Ankyrin repeat [Signal transduction mechanisms]; Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 134.70 E-value: 1.33e-35
|
||||||||||
Ank_2 | pfam12796 | Ankyrin repeats (3 copies); |
64-156 | 1.83e-19 | ||||||
Ankyrin repeats (3 copies); Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 83.24 E-value: 1.83e-19
|
||||||||||
PHA03095 | PHA03095 | ankyrin-like protein; Provisional |
48-226 | 1.34e-15 | ||||||
ankyrin-like protein; Provisional Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 79.30 E-value: 1.34e-15
|
||||||||||
PHA03100 | PHA03100 | ankyrin repeat protein; Provisional |
112-444 | 1.19e-11 | ||||||
ankyrin repeat protein; Provisional Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 66.61 E-value: 1.19e-11
|
||||||||||
Ank_2 | pfam12796 | Ankyrin repeats (3 copies); |
197-328 | 1.03e-10 | ||||||
Ankyrin repeats (3 copies); Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 58.20 E-value: 1.03e-10
|
||||||||||
TRPV5-6 | cd22192 | Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
62-202 | 1.70e-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: 47.31 E-value: 1.70e-05
|
||||||||||
ANK | smart00248 | ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
59-87 | 3.37e-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: 40.65 E-value: 3.37e-05
|
||||||||||
DR0291 | COG1579 | Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
348-482 | 6.32e-05 | ||||||
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only]; Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.53 E-value: 6.32e-05
|
||||||||||
COG4372 | COG4372 | Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
426-482 | 1.94e-04 | ||||||
Uncharacterized protein, contains DUF3084 domain [Function unknown]; Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.74 E-value: 1.94e-04
|
||||||||||
ANK | smart00248 | ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
297-326 | 2.22e-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: 38.34 E-value: 2.22e-04
|
||||||||||
trp | TIGR00870 | transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
62-134 | 8.68e-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: 41.99 E-value: 8.68e-04
|
||||||||||
ERM_helical | pfam20492 | Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
427-482 | 1.44e-03 | ||||||
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins. Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 38.75 E-value: 1.44e-03
|
||||||||||
Mplasa_alph_rch | TIGR04523 | helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
430-486 | 5.23e-03 | ||||||
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown. Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 39.62 E-value: 5.23e-03
|
||||||||||
eNOPS_SF | cd12931 | NOPS domain, including C-terminal helical extension region, in the p54nrb/PSF/PSP1 family; All ... |
427-470 | 5.51e-03 | ||||||
NOPS domain, including C-terminal helical extension region, in the p54nrb/PSF/PSP1 family; All members in this family contain a DBHS domain (for Drosophila behavior, human splicing), which comprises two conserved RNA recognition motifs (RRM1 and RRM2), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a charged protein-protein interaction NOPS (NONA and PSP1) domain with a long helical C-terminal extension. The NOPS domain specifically binds to RRM2 domain of the partner DBHS protein via a substantial interaction surface. Its highly conserved C-terminal residues are critical for functional DBHS dimerization while the highly conserved C-terminal helical extension, forming a right-handed antiparallel heterodimeric coiled-coil, is essential for localization of these proteins to subnuclear bodies. PSF has an additional large N-terminal domain that differentiates it from other family members. The p54nrb/PSF/PSP1 family includes 54 kDa nuclear RNA- and DNA-binding protein (p54nrb), polypyrimidine tract-binding protein (PTB)-associated-splicing factor (PSF) and paraspeckle protein 1 (PSP1), which are ubiquitously expressed and are well conserved in vertebrates. p54nrb, also termed NONO or NMT55, is a multi-functional protein involved in numerous nuclear processes including transcriptional regulation, splicing, DNA unwinding, nuclear retention of hyperedited double-stranded RNA, viral RNA processing, control of cell proliferation, and circadian rhythm maintenance. PSF, also termed POMp100, is also a multi-functional protein that binds RNA, single-stranded DNA (ssDNA), double-stranded DNA (dsDNA) and many factors, and mediates diverse activities in the cell. PSP1, also termed PSPC1, is a novel nucleolar factor that accumulates within a new nucleoplasmic compartment, termed paraspeckles, and diffusely distributes in the nucleoplasm. The cellular function of PSP1 remains unknown currently. The family also includes some p54nrb/PSF/PSP1 homologs from invertebrate species. For instance, the Drosophila melanogaster gene no-ontransient A (nonA) encoding puff-specific protein Bj6 (also termed NONA) and Chironomus tentans hrp65 gene encoding protein Hrp65. D. melanogaster NONA is involved in eye development and behavior and may play a role in circadian rhythm maintenance, similar to vertebrate p54nrb. C. tentans Hrp65 is a component of nuclear fibers associated with ribonucleoprotein particles in transit from the gene to the nuclear pore. Pssm-ID: 240579 [Multi-domain] Cd Length: 90 Bit Score: 36.07 E-value: 5.51e-03
|
||||||||||
PRK03992 | PRK03992 | proteasome-activating nucleotidase; Provisional |
428-490 | 5.97e-03 | ||||||
proteasome-activating nucleotidase; Provisional Pssm-ID: 179699 [Multi-domain] Cd Length: 389 Bit Score: 39.05 E-value: 5.97e-03
|
||||||||||
Name | Accession | Description | Interval | E-value | |||||||
ANKYR | COG0666 | Ankyrin repeat [Signal transduction mechanisms]; |
30-264 | 1.33e-35 | |||||||
Ankyrin repeat [Signal transduction mechanisms]; Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 134.70 E-value: 1.33e-35
|
|||||||||||
ANKYR | COG0666 | Ankyrin repeat [Signal transduction mechanisms]; |
49-297 | 1.43e-29 | |||||||
Ankyrin repeat [Signal transduction mechanisms]; Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 117.75 E-value: 1.43e-29
|
|||||||||||
ANKYR | COG0666 | Ankyrin repeat [Signal transduction mechanisms]; |
42-368 | 2.55e-28 | |||||||
Ankyrin repeat [Signal transduction mechanisms]; Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 114.28 E-value: 2.55e-28
|
|||||||||||
ANKYR | COG0666 | Ankyrin repeat [Signal transduction mechanisms]; |
17-194 | 4.04e-24 | |||||||
Ankyrin repeat [Signal transduction mechanisms]; Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 102.34 E-value: 4.04e-24
|
|||||||||||
ANKYR | COG0666 | Ankyrin repeat [Signal transduction mechanisms]; |
111-434 | 2.51e-21 | |||||||
Ankyrin repeat [Signal transduction mechanisms]; Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 94.25 E-value: 2.51e-21
|
|||||||||||
Ank_2 | pfam12796 | Ankyrin repeats (3 copies); |
64-156 | 1.83e-19 | |||||||
Ankyrin repeats (3 copies); Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 83.24 E-value: 1.83e-19
|
|||||||||||
Ank_2 | pfam12796 | Ankyrin repeats (3 copies); |
98-189 | 7.80e-16 | |||||||
Ankyrin repeats (3 copies); Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 72.84 E-value: 7.80e-16
|
|||||||||||
PHA03095 | PHA03095 | ankyrin-like protein; Provisional |
48-226 | 1.34e-15 | |||||||
ankyrin-like protein; Provisional Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 79.30 E-value: 1.34e-15
|
|||||||||||
PHA02874 | PHA02874 | ankyrin repeat protein; Provisional |
45-239 | 2.21e-15 | |||||||
ankyrin repeat protein; Provisional Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 78.47 E-value: 2.21e-15
|
|||||||||||
PHA02874 | PHA02874 | ankyrin repeat protein; Provisional |
34-403 | 2.27e-15 | |||||||
ankyrin repeat protein; Provisional Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 78.08 E-value: 2.27e-15
|
|||||||||||
PHA03095 | PHA03095 | ankyrin-like protein; Provisional |
34-334 | 3.36e-15 | |||||||
ankyrin-like protein; Provisional Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 77.76 E-value: 3.36e-15
|
|||||||||||
Ank_2 | pfam12796 | Ankyrin repeats (3 copies); |
30-123 | 2.95e-14 | |||||||
Ankyrin repeats (3 copies); Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 68.22 E-value: 2.95e-14
|
|||||||||||
Ank_2 | pfam12796 | Ankyrin repeats (3 copies); |
130-214 | 3.01e-14 | |||||||
Ankyrin repeats (3 copies); Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 68.22 E-value: 3.01e-14
|
|||||||||||
PHA02875 | PHA02875 | ankyrin repeat protein; Provisional |
30-185 | 1.13e-13 | |||||||
ankyrin repeat protein; Provisional Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 72.72 E-value: 1.13e-13
|
|||||||||||
PHA03100 | PHA03100 | ankyrin repeat protein; Provisional |
26-214 | 2.36e-12 | |||||||
ankyrin repeat protein; Provisional Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 68.92 E-value: 2.36e-12
|
|||||||||||
PHA03100 | PHA03100 | ankyrin repeat protein; Provisional |
112-444 | 1.19e-11 | |||||||
ankyrin repeat protein; Provisional Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 66.61 E-value: 1.19e-11
|
|||||||||||
Ank_2 | pfam12796 | Ankyrin repeats (3 copies); |
197-328 | 1.03e-10 | |||||||
Ankyrin repeats (3 copies); Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 58.20 E-value: 1.03e-10
|
|||||||||||
Ank_2 | pfam12796 | Ankyrin repeats (3 copies); |
269-350 | 1.16e-10 | |||||||
Ankyrin repeats (3 copies); Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 58.20 E-value: 1.16e-10
|
|||||||||||
PLN03192 | PLN03192 | Voltage-dependent potassium channel; Provisional |
133-358 | 1.23e-10 | |||||||
Voltage-dependent potassium channel; Provisional Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 64.12 E-value: 1.23e-10
|
|||||||||||
Ank_4 | pfam13637 | Ankyrin repeats (many copies); |
62-113 | 1.83e-10 | |||||||
Ankyrin repeats (many copies); Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 56.13 E-value: 1.83e-10
|
|||||||||||
Ank_4 | pfam13637 | Ankyrin repeats (many copies); |
159-212 | 4.86e-10 | |||||||
Ankyrin repeats (many copies); Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 54.97 E-value: 4.86e-10
|
|||||||||||
Ank_4 | pfam13637 | Ankyrin repeats (many copies); |
269-318 | 2.42e-09 | |||||||
Ankyrin repeats (many copies); Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 53.05 E-value: 2.42e-09
|
|||||||||||
Ank_4 | pfam13637 | Ankyrin repeats (many copies); |
128-179 | 9.06e-09 | |||||||
Ankyrin repeats (many copies); Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 51.51 E-value: 9.06e-09
|
|||||||||||
PHA02876 | PHA02876 | ankyrin repeat protein; Provisional |
29-350 | 1.04e-08 | |||||||
ankyrin repeat protein; Provisional Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 57.77 E-value: 1.04e-08
|
|||||||||||
Ank_5 | pfam13857 | Ankyrin repeats (many copies); |
283-338 | 7.97e-08 | |||||||
Ankyrin repeats (many copies); Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 48.88 E-value: 7.97e-08
|
|||||||||||
PLN03192 | PLN03192 | Voltage-dependent potassium channel; Provisional |
67-228 | 1.01e-07 | |||||||
Voltage-dependent potassium channel; Provisional Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 54.87 E-value: 1.01e-07
|
|||||||||||
PTZ00322 | PTZ00322 | 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
98-195 | 1.02e-07 | |||||||
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 54.52 E-value: 1.02e-07
|
|||||||||||
Ank_4 | pfam13637 | Ankyrin repeats (many copies); |
93-138 | 1.09e-07 | |||||||
Ankyrin repeats (many copies); Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 48.42 E-value: 1.09e-07
|
|||||||||||
PHA02878 | PHA02878 | ankyrin repeat protein; Provisional |
49-215 | 1.14e-07 | |||||||
ankyrin repeat protein; Provisional Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 54.12 E-value: 1.14e-07
|
|||||||||||
Ank_4 | pfam13637 | Ankyrin repeats (many copies); |
298-350 | 2.85e-07 | |||||||
Ankyrin repeats (many copies); Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 47.27 E-value: 2.85e-07
|
|||||||||||
PHA02875 | PHA02875 | ankyrin repeat protein; Provisional |
32-253 | 2.09e-06 | |||||||
ankyrin repeat protein; Provisional Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 49.99 E-value: 2.09e-06
|
|||||||||||
PHA02878 | PHA02878 | ankyrin repeat protein; Provisional |
109-199 | 3.88e-06 | |||||||
ankyrin repeat protein; Provisional Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 49.49 E-value: 3.88e-06
|
|||||||||||
Ank_5 | pfam13857 | Ankyrin repeats (many copies); |
84-133 | 5.25e-06 | |||||||
Ankyrin repeats (many copies); Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 43.87 E-value: 5.25e-06
|
|||||||||||
TRPV5-6 | cd22192 | Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
62-202 | 1.70e-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: 47.31 E-value: 1.70e-05
|
|||||||||||
Ank_4 | pfam13637 | Ankyrin repeats (many copies); |
30-80 | 2.04e-05 | |||||||
Ankyrin repeats (many copies); Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 41.88 E-value: 2.04e-05
|
|||||||||||
PTZ00322 | PTZ00322 | 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
118-203 | 2.12e-05 | |||||||
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 47.20 E-value: 2.12e-05
|
|||||||||||
Ank | pfam00023 | Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
297-329 | 2.59e-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: 41.12 E-value: 2.59e-05
|
|||||||||||
ANK | smart00248 | ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
59-87 | 3.37e-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: 40.65 E-value: 3.37e-05
|
|||||||||||
TRPV5-6 | cd22192 | Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
62-214 | 4.89e-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: 46.16 E-value: 4.89e-05
|
|||||||||||
PHA02878 | PHA02878 | ankyrin repeat protein; Provisional |
79-199 | 5.56e-05 | |||||||
ankyrin repeat protein; Provisional Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 45.64 E-value: 5.56e-05
|
|||||||||||
Ank_5 | pfam13857 | Ankyrin repeats (many copies); |
58-100 | 5.95e-05 | |||||||
Ankyrin repeats (many copies); Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 40.79 E-value: 5.95e-05
|
|||||||||||
Ank_3 | pfam13606 | Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
59-88 | 6.27e-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: 39.93 E-value: 6.27e-05
|
|||||||||||
DR0291 | COG1579 | Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
348-482 | 6.32e-05 | |||||||
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only]; Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.53 E-value: 6.32e-05
|
|||||||||||
Ank_5 | pfam13857 | Ankyrin repeats (many copies); |
117-166 | 6.96e-05 | |||||||
Ankyrin repeats (many copies); Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 40.79 E-value: 6.96e-05
|
|||||||||||
PHA02878 | PHA02878 | ankyrin repeat protein; Provisional |
29-166 | 8.96e-05 | |||||||
ankyrin repeat protein; Provisional Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 44.87 E-value: 8.96e-05
|
|||||||||||
PHA02875 | PHA02875 | ankyrin repeat protein; Provisional |
118-331 | 8.99e-05 | |||||||
ankyrin repeat protein; Provisional Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 44.98 E-value: 8.99e-05
|
|||||||||||
PHA02946 | PHA02946 | ankyin-like protein; Provisional |
33-198 | 9.43e-05 | |||||||
ankyin-like protein; Provisional Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 45.04 E-value: 9.43e-05
|
|||||||||||
PHA03095 | PHA03095 | ankyrin-like protein; Provisional |
42-138 | 1.48e-04 | |||||||
ankyrin-like protein; Provisional Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 44.25 E-value: 1.48e-04
|
|||||||||||
PTZ00322 | PTZ00322 | 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
269-350 | 1.56e-04 | |||||||
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 44.50 E-value: 1.56e-04
|
|||||||||||
PHA02798 | PHA02798 | ankyrin-like protein; Provisional |
109-332 | 1.58e-04 | |||||||
ankyrin-like protein; Provisional Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 44.44 E-value: 1.58e-04
|
|||||||||||
COG4372 | COG4372 | Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
426-482 | 1.94e-04 | |||||||
Uncharacterized protein, contains DUF3084 domain [Function unknown]; Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.74 E-value: 1.94e-04
|
|||||||||||
ANK | smart00248 | ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
297-326 | 2.22e-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: 38.34 E-value: 2.22e-04
|
|||||||||||
Ank_2 | pfam12796 | Ankyrin repeats (3 copies); |
302-363 | 2.31e-04 | |||||||
Ankyrin repeats (3 copies); Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 40.10 E-value: 2.31e-04
|
|||||||||||
Ank_3 | pfam13606 | Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
297-326 | 3.17e-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: 38.01 E-value: 3.17e-04
|
|||||||||||
PHA02946 | PHA02946 | ankyin-like protein; Provisional |
101-213 | 3.27e-04 | |||||||
ankyin-like protein; Provisional Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 43.12 E-value: 3.27e-04
|
|||||||||||
Ank | pfam00023 | Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
59-90 | 3.49e-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: 38.04 E-value: 3.49e-04
|
|||||||||||
PHA03100 | PHA03100 | ankyrin repeat protein; Provisional |
49-118 | 6.47e-04 | |||||||
ankyrin repeat protein; Provisional Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 42.34 E-value: 6.47e-04
|
|||||||||||
TRPV3 | cd22194 | Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
84-214 | 6.95e-04 | |||||||
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: 42.44 E-value: 6.95e-04
|
|||||||||||
trp | TIGR00870 | transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
62-134 | 8.68e-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: 41.99 E-value: 8.68e-04
|
|||||||||||
Ank | pfam00023 | Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
125-157 | 1.03e-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: 1.03e-03
|
|||||||||||
ERM_helical | pfam20492 | Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
427-482 | 1.44e-03 | |||||||
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins. Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 38.75 E-value: 1.44e-03
|
|||||||||||
PTZ00322 | PTZ00322 | 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
57-147 | 2.13e-03 | |||||||
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 40.65 E-value: 2.13e-03
|
|||||||||||
ANK | smart00248 | ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
125-154 | 2.21e-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: 35.64 E-value: 2.21e-03
|
|||||||||||
Ank | pfam00023 | Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
92-124 | 2.60e-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: 35.73 E-value: 2.60e-03
|
|||||||||||
HalX | pfam08663 | HalX domain; HalX is a domain of unknown function, previously (mis)annotated as HoxA-like ... |
430-479 | 2.92e-03 | |||||||
HalX domain; HalX is a domain of unknown function, previously (mis)annotated as HoxA-like transcriptional regulator. Pssm-ID: 400823 Cd Length: 68 Bit Score: 36.45 E-value: 2.92e-03
|
|||||||||||
Mplasa_alph_rch | TIGR04523 | helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
430-486 | 5.23e-03 | |||||||
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown. Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 39.62 E-value: 5.23e-03
|
|||||||||||
eNOPS_SF | cd12931 | NOPS domain, including C-terminal helical extension region, in the p54nrb/PSF/PSP1 family; All ... |
427-470 | 5.51e-03 | |||||||
NOPS domain, including C-terminal helical extension region, in the p54nrb/PSF/PSP1 family; All members in this family contain a DBHS domain (for Drosophila behavior, human splicing), which comprises two conserved RNA recognition motifs (RRM1 and RRM2), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), and a charged protein-protein interaction NOPS (NONA and PSP1) domain with a long helical C-terminal extension. The NOPS domain specifically binds to RRM2 domain of the partner DBHS protein via a substantial interaction surface. Its highly conserved C-terminal residues are critical for functional DBHS dimerization while the highly conserved C-terminal helical extension, forming a right-handed antiparallel heterodimeric coiled-coil, is essential for localization of these proteins to subnuclear bodies. PSF has an additional large N-terminal domain that differentiates it from other family members. The p54nrb/PSF/PSP1 family includes 54 kDa nuclear RNA- and DNA-binding protein (p54nrb), polypyrimidine tract-binding protein (PTB)-associated-splicing factor (PSF) and paraspeckle protein 1 (PSP1), which are ubiquitously expressed and are well conserved in vertebrates. p54nrb, also termed NONO or NMT55, is a multi-functional protein involved in numerous nuclear processes including transcriptional regulation, splicing, DNA unwinding, nuclear retention of hyperedited double-stranded RNA, viral RNA processing, control of cell proliferation, and circadian rhythm maintenance. PSF, also termed POMp100, is also a multi-functional protein that binds RNA, single-stranded DNA (ssDNA), double-stranded DNA (dsDNA) and many factors, and mediates diverse activities in the cell. PSP1, also termed PSPC1, is a novel nucleolar factor that accumulates within a new nucleoplasmic compartment, termed paraspeckles, and diffusely distributes in the nucleoplasm. The cellular function of PSP1 remains unknown currently. The family also includes some p54nrb/PSF/PSP1 homologs from invertebrate species. For instance, the Drosophila melanogaster gene no-ontransient A (nonA) encoding puff-specific protein Bj6 (also termed NONA) and Chironomus tentans hrp65 gene encoding protein Hrp65. D. melanogaster NONA is involved in eye development and behavior and may play a role in circadian rhythm maintenance, similar to vertebrate p54nrb. C. tentans Hrp65 is a component of nuclear fibers associated with ribonucleoprotein particles in transit from the gene to the nuclear pore. Pssm-ID: 240579 [Multi-domain] Cd Length: 90 Bit Score: 36.07 E-value: 5.51e-03
|
|||||||||||
TRPV1-4 | cd22193 | Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ... |
84-214 | 5.89e-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: 39.39 E-value: 5.89e-03
|
|||||||||||
PRK03992 | PRK03992 | proteasome-activating nucleotidase; Provisional |
428-490 | 5.97e-03 | |||||||
proteasome-activating nucleotidase; Provisional Pssm-ID: 179699 [Multi-domain] Cd Length: 389 Bit Score: 39.05 E-value: 5.97e-03
|
|||||||||||
PHA02878 | PHA02878 | ankyrin repeat protein; Provisional |
162-350 | 6.07e-03 | |||||||
ankyrin repeat protein; Provisional Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 39.09 E-value: 6.07e-03
|
|||||||||||
Ank_5 | pfam13857 | Ankyrin repeats (many copies); |
150-199 | 9.29e-03 | |||||||
Ankyrin repeats (many copies); Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 34.63 E-value: 9.29e-03
|
|||||||||||
Blast search parameters | ||||
|