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Conserved domains on  [gi|393290873|ref|NP_001257307|]
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ankyrin repeat domain-containing protein 46 isoform 1 [Homo sapiens]

Protein Classification

ankyrin repeat domain-containing protein( domain architecture ID 11429852)

ankyrin repeat (ANK) domain-containing protein is involved in mediating protein-protein interactions

Gene Ontology:  GO:0005515
PubMed:  33435370|17176038

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
15-128 6.18e-30

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 112.74  E-value: 6.18e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393290873  15 PLLQACIDGDFNYSKRLLESGFDPNIRDSRGRTGLHLAAARGNVDICQLLHKFGADLLATDYQGNTALHL---CGHVDTI 91
Cdd:COG0666   90 LLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLaaaNGNLEIV 169

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 393290873  92 QFLVSNGLKIDICNHQGATPLVLAKRRGvNKDVIRLL 128
Cdd:COG0666  170 KLLLEAGADVNARDNDGETPLHLAAENG-HLEIVKLL 205
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
15-128 6.18e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 112.74  E-value: 6.18e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393290873  15 PLLQACIDGDFNYSKRLLESGFDPNIRDSRGRTGLHLAAARGNVDICQLLHKFGADLLATDYQGNTALHL---CGHVDTI 91
Cdd:COG0666   90 LLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLaaaNGNLEIV 169

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 393290873  92 QFLVSNGLKIDICNHQGATPLVLAKRRGvNKDVIRLL 128
Cdd:COG0666  170 KLLLEAGADVNARDNDGETPLHLAAENG-HLEIVKLL 205
Ank_2 pfam12796
Ankyrin repeats (3 copies);
16-103 2.41e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 71.30  E-value: 2.41e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393290873   16 LLQACIDGDFNYSKRLLESGFDPNIRDSRGRTGLHLAAARGNVDICQLLHKFgADLLATDYqGNTALHLC---GHVDTIQ 92
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAarsGHLEIVK 78

                          90
                  ....*....|.
gi 393290873   93 FLVSNGLKIDI 103
Cdd:pfam12796  79 LLLEKGADINV 89
PHA03095 PHA03095
ankyrin-like protein; Provisional
 31-128 1.36e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 66.20  E-value: 1.36e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393290873  31 LLESGFDPNIRDSRGRTGLHLAAARGNV-DICQLLHKFGADLLATDYQGNTALH--LCG---HVDTIQFLVSNGLKIDIC 104
Cdd:PHA03095  69 LLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKAGADVNAKDKVGRTPLHvyLSGfniNPKVIRLLLRKGADVNAL 148

                         90       100
                 ....*....|....*....|....*
gi 393290873 105 NHQGATPL-VLAKRRGVNKDVIRLL 128
Cdd:PHA03095 149 DLYGMTPLaVLLKSRNANVELLRLL 173
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 2-128 3.47e-08

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: 53.16  E-value: 3.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393290873    2 SYVFVNDSS-------QTnvPLLQACIDGDFNYSKRLLESGFDPNIR------------DS--RGRTGLHLAAARGNVDI 60
Cdd:TIGR00870 113 PLELANDQYtseftpgIT--ALHLAAHRQNYEIVKLLLERGASVPARacgdffvksqgvDSfyHGESPLNAAACLGSPSI 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393290873   61 CQLLHKFGADLLATDYQGNTALHLC-----GHVDTI-------QFLVSNGLKID-------ICNHQGATPLVLAKRRGvN 121
Cdd:TIGR00870 191 VALLSEDPADILTADSLGNTLLHLLvmeneFKAEYEelscqmyNFALSLLDKLRdskelevILNHQGLTPLKLAAKEG-R 269


                  ....*..
gi 393290873  122 KDVIRLL 128
Cdd:TIGR00870 270 IVLFRLK 276
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 15-119 4.43e-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: 43.85  E-value: 4.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393290873  15 PLLQACIDGDFNYSKRLLESGFDP-NIRD-----SRGRTGL-----H---LAAARGNVDICQLLHKFGADLLATDYQGNT 80
Cdd:cd22192   92 ALHIAVVNQNLNLVRELIARGADVvSPRAtgtffRPGPKNLiyygeHplsFAACVGNEEIVRLLIEHGADIRAQDSLGNT 171

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 393290873  81 ALHL----------CGHVDTIqfLVSNGLKIDIC-----NHQGATPLVLAKRRG 119
Cdd:cd22192  172 VLHIlvlqpnktfaCQMYDLI--LSYDKEDDLQPldlvpNNQGLTPFKLAAKEG 223
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 44-71 3.06e-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: 34.10  E-value: 3.06e-03
                           10        20
                   ....*....|....*....|....*...
gi 393290873    44 RGRTGLHLAAARGNVDICQLLHKFGADL 71
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
15-128 6.18e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 112.74  E-value: 6.18e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393290873  15 PLLQACIDGDFNYSKRLLESGFDPNIRDSRGRTGLHLAAARGNVDICQLLHKFGADLLATDYQGNTALHL---CGHVDTI 91
Cdd:COG0666   90 LLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLaaaNGNLEIV 169

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 393290873  92 QFLVSNGLKIDICNHQGATPLVLAKRRGvNKDVIRLL 128
Cdd:COG0666  170 KLLLEAGADVNARDNDGETPLHLAAENG-HLEIVKLL 205
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
15-143 3.24e-21

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 89.24  E-value: 3.24e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393290873  15 PLLQACIDGDFNYSKRLLESGFDPNIRDSRGRTGLHLAAARGNVDICQLLHKFGADLLATDYQGNTALHL---CGHVDTI 91
Cdd:COG0666  156 PLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLaaeNGNLEIV 235

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 393290873  92 QFLVSNGLKIDICNHQGATPLVLAKRRGVNKDVIRLLESLEEQEVKGFNRGT 143
Cdd:COG0666  236 KLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
7-128 6.71e-21

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 88.47  E-value: 6.71e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393290873   7 NDSSQTNVPLLQACIDGDFNYSKRLLESGFDPNIRDSRGRTGLHLAAARGNVDICQLLHKFGADLLATDYQGNTALHLC- 85
Cdd:COG0666   49 LADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAa 128

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 393290873  86 --GHVDTIQFLVSNGLKIDICNHQGATPLVLAKRRGvNKDVIRLL 128
Cdd:COG0666  129 ynGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANG-NLEIVKLL 172
Ank_2 pfam12796
Ankyrin repeats (3 copies);
16-103 2.41e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 71.30  E-value: 2.41e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393290873   16 LLQACIDGDFNYSKRLLESGFDPNIRDSRGRTGLHLAAARGNVDICQLLHKFgADLLATDYqGNTALHLC---GHVDTIQ 92
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAarsGHLEIVK 78

                          90
                  ....*....|.
gi 393290873   93 FLVSNGLKIDI 103
Cdd:pfam12796  79 LLLEKGADINV 89
PHA03095 PHA03095
ankyrin-like protein; Provisional
 31-128 1.36e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 66.20  E-value: 1.36e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393290873  31 LLESGFDPNIRDSRGRTGLHLAAARGNV-DICQLLHKFGADLLATDYQGNTALH--LCG---HVDTIQFLVSNGLKIDIC 104
Cdd:PHA03095  69 LLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKAGADVNAKDKVGRTPLHvyLSGfniNPKVIRLLLRKGADVNAL 148

                         90       100
                 ....*....|....*....|....*
gi 393290873 105 NHQGATPL-VLAKRRGVNKDVIRLL 128
Cdd:PHA03095 149 DLYGMTPLaVLLKSRNANVELLRLL 173
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 14-108 3.44e-12

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 65.30  E-value: 3.44e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393290873  14 VPLLQACIDGDFNYSKRLLESGFDPNIRDSRGRTGLHLAAARGNVDICQLLHKFGADLLATDYQGNTALHLCGHVDT--- 90
Cdd:PTZ00322  84 VELCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFrev 163

                         90
                 ....*....|....*...
gi 393290873  91 IQFLVSNGlkidICNHQG 108
Cdd:PTZ00322 164 VQLLSRHS----QCHFEL 177
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 7-128 3.50e-12

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 65.27  E-value: 3.50e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393290873   7 NDSSQTNVPLLQACIDGDFNYSKRLLESGFDPNIRDSRGRTGLHLAAARGNVDICQLLHKFGADLLATDYQGNTAL---- 82
Cdd:PLN03192 520 HDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALwnai 599

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 393290873  83 ---H----------------------LC-----GHVDTIQFLVSNGLKIDICNHQGATPLVLAKRRGvNKDVIRLL 128
Cdd:PLN03192 600 sakHhkifrilyhfasisdphaagdlLCtaakrNDLTAMKELLKQGLNVDSEDHQGATALQVAMAED-HVDMVRLL 674
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
11-128 1.71e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 62.28  E-value: 1.71e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393290873  11 QTNVPLLQACIDGDFNYSKRLLESGFDPNIRDSRGRTGLHLAAARGNVDICQLLHKFGADLLATDYQGNTALHLC---GH 87
Cdd:COG0666   20 LLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAarnGD 99

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 393290873  88 VDTIQFLVSNGLKIDICNHQGATPLVLAKRRGvNKDVIRLL 128
Cdd:COG0666  100 LEIVKLLLEAGADVNARDKDGETPLHLAAYNG-NLEIVKLL 139
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 8-142 7.89e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 60.75  E-value: 7.89e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393290873   8 DSSQTNVPllqaCIDGDFnySKRLLESGFDPNIRDSRGRTGLHLAAARGNVDICQLLHKFGADLLATDYQGNTALHLC-- 85
Cdd:PHA02874  93 DTSILPIP----CIEKDM--IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAik 166

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 393290873  86 -GHVDTIQFLVSNGLKIDICNHQGATPLVLAKRRGVNKDVIRLLESLEEQEVKgFNRG 142
Cdd:PHA02874 167 hNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNK-CKNG 223
Ank_4 pfam13637
Ankyrin repeats (many copies);
45-95 2.09e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.59  E-value: 2.09e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 393290873   45 GRTGLHLAAARGNVDICQLLHKFGADLLATDYQGNTALHLC---GHVDTIQFLV 95
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAasnGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
15-65 1.42e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.28  E-value: 1.42e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 393290873   15 PLLQACIDGDFNYSKRLLESGFDPNIRDSRGRTGLHLAAARGNVDICQLLH 65
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 13-128 2.81e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 56.61  E-value: 2.81e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393290873  13 NVPLLQAC-IDGDFNYSKRLLESGFDPNIRDSRGRTGLHLAAARGNVDICQLLHKFGADLLATDYQGNTALH--LCGH-- 87
Cdd:PHA02876 342 ITPLHQAStLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHfaLCGTnp 421

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 393290873  88 VDTIQFLVSNGLKIDICNHQGATPLVLAKRRGVNKDVIRLL 128
Cdd:PHA02876 422 YMSVKTLIDRGANVNSKNKDLSTPLHYACKKNCKLDVIEML 462
PHA03095 PHA03095
ankyrin-like protein; Provisional
 29-115 8.38e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 55.03  E-value: 8.38e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393290873  29 KRLLESGFDPNIRDSRGRTGLH--LAAARGNVDICQLLHKFGADLLATDYQGNTALHL------CGHVDtIQFLVSNGLK 100
Cdd:PHA03095 171 RLLIDAGADVYAVDDRFRSLLHhhLQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSmatgssCKRSL-VLPLLIAGIS 249

                         90
                 ....*....|....*
gi 393290873 101 IDICNHQGATPLVLA 115
Cdd:PHA03095 250 INARNRYGQTPLHYA 264
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 29-128 1.02e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 54.67  E-value: 1.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393290873  29 KRLLESGFDPNIRDSRGRTGLHLAA-----ARGNVDICQLLHKFGADLLATDYQGNTALHLC-----GHVDTIQFLVSNG 98
Cdd:PHA03100  52 KILLDNGADINSSTKNNSTPLHYLSnikynLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAiskksNSYSIVEYLLDNG 131

                         90       100       110
                 ....*....|....*....|....*....|.
gi 393290873  99 LKIDICNHQGATPLVLAKRRG-VNKDVIRLL 128
Cdd:PHA03100 132 ANVNIKNSDGENLLHLYLESNkIDLKILKLL 162
Ank_5 pfam13857
Ankyrin repeats (many copies);
31-85 1.61e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 49.65  E-value: 1.61e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 393290873   31 LLESG-FDPNIRDSRGRTGLHLAAARGNVDICQLLHKFGADLLATDYQGNTALHLC 85
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 6-112 1.74e-08

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 54.15  E-value: 1.74e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393290873   6 VNDSSQTNVPLL-----QACIDGDFNYSKRLLESGFDPNIRDSRGRTGLHLAAARGNV--DICQLLHKFGADLLATDYQG 78
Cdd:PHA02716 273 LDGNKVKNIPMIlhsyiTLARNIDISVVYSFLQPGVKLHYKDSAGRTCLHQYILRHNIstDIIKLLHEYGNDLNEPDNIG 352

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 393290873  79 NTALH-----LCG------------HVDTIQFLVSNGLKIDICNHQGATPL 112
Cdd:PHA02716 353 NTVLHtylsmLSVvnildpetdndiRLDVIQCLISLGADITAVNCLGYTPL 403
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 2-128 3.47e-08

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: 53.16  E-value: 3.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393290873    2 SYVFVNDSS-------QTnvPLLQACIDGDFNYSKRLLESGFDPNIR------------DS--RGRTGLHLAAARGNVDI 60
Cdd:TIGR00870 113 PLELANDQYtseftpgIT--ALHLAAHRQNYEIVKLLLERGASVPARacgdffvksqgvDSfyHGESPLNAAACLGSPSI 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393290873   61 CQLLHKFGADLLATDYQGNTALHLC-----GHVDTI-------QFLVSNGLKID-------ICNHQGATPLVLAKRRGvN 121
Cdd:TIGR00870 191 VALLSEDPADILTADSLGNTLLHLLvmeneFKAEYEelscqmyNFALSLLDKLRdskelevILNHQGLTPLKLAAKEG-R 269


                  ....*..
gi 393290873  122 KDVIRLL 128
Cdd:TIGR00870 270 IVLFRLK 276
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 29-123 2.61e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 49.43  E-value: 2.61e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393290873  29 KRLLESGFDPNIRDSRGRTGLH--LAAARGNVDICQLLHKFGADLLATDYQGNTALH--LCGHVD--TIQFLVSNGLKID 102
Cdd:PHA02859 107 KILIDSGSSITEEDEDGKNLLHmyMCNFNVRINVIKLLIDSGVSFLNKDFDNNNILYsyILFHSDkkIFDFLTSLGIDIN 186

                         90       100
                 ....*....|....*....|...
gi 393290873 103 ICNHQGATPLVLAKRRGV--NKD 123
Cdd:PHA02859 187 ETNKSGYNCYDLIKFRNLffNKQ 209
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 1-128 8.98e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 48.89  E-value: 8.98e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393290873   1 MSYVFVNDSSQTNVPllqacidgdfNYSKRLLESGFDPNIRDSRGRTGLHLAAAR--GNVDICQLLHKFGADLLATDYQG 78
Cdd:PHA03100  72 LHYLSNIKYNLTDVK----------EIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDG 141

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 393290873  79 NTALHL---CGHVDT--IQFLVSNG----------------LKIDICNHQGATPLVLAKRRgVNKDVIRLL 128
Cdd:PHA03100 142 ENLLHLyleSNKIDLkiLKLLIDKGvdinaknrvnyllsygVPINIKDVYGFTPLHYAVYN-NNPEFVKYL 211
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 29-103 9.23e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 48.89  E-value: 9.23e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 393290873  29 KRLLESGFDPNIRDSRGRTGLHLAAARGNVDICQLLHKFGADLLATDYQGNTALHLC---GHVDTIQFLVSNGLKIDI 103
Cdd:PHA03100 176 NYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAilnNNKEIFKLLLNNGPSIKT 253
Ank_2 pfam12796
Ankyrin repeats (3 copies);
15-75 9.72e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 45.49  E-value: 9.72e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 393290873   15 PLLQACIDGDFNYSKRLLESgFDPNIRDSrGRTGLHLAAARGNVDICQLLHKFGADLLATD 75
Cdd:pfam12796  33 ALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 31-82 4.22e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.94  E-value: 4.22e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 393290873  31 LLESGFDPNIRDSRGRTGLHLAAARGNVDICQLLHKFGADLLATDYQGNTAL 82
Cdd:PHA03095 243 LLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPL 294
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 28-137 1.66e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.05  E-value: 1.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393290873  28 SKRLLESGFDPNIRDSRGRTGLHLAAARGNVDICQLLHKFGADLLATDYQGNTALHLC---GHVDTIQFLVSNglkidic 104
Cdd:PHA02876 161 AEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAvdsKNIDTIKAIIDN------- 233

                         90       100       110
                 ....*....|....*....|....*....|...
gi 393290873 105 nhqgatplvlakRRGVNKDVIRLLESLEEQEVK 137
Cdd:PHA02876 234 ------------RSNINKNDLSLLKAIRNEDLE 254
Ank_4 pfam13637
Ankyrin repeats (many copies);
78-128 2.42e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 40.72  E-value: 2.42e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 393290873   78 GNTALHLC---GHVDTIQFLVSNGLKIDICNHQGATPLVLAKRRGvNKDVIRLL 128
Cdd:pfam13637   1 ELTALHAAaasGHLELLRLLLEKGADINAVDGNGETALHFAASNG-NVEVLKLL 53
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 6-128 2.63e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 44.27  E-value: 2.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393290873   6 VNDSSQTNVPLLQACIDGDFNYS---KRLLESGFDPNIRDSRGRTGLHLAAARGNVD--ICQLLHKFGAD---------- 70
Cdd:PHA03100  99 VNAPDNNGITPLLYAISKKSNSYsivEYLLDNGANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKGVDinaknrvnyl 178

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 393290873  71 ------LLATDYQGNTALHLC---GHVDTIQFLVSNGLKIDICNHQGATPLVLAKRRGvNKDVIRLL 128
Cdd:PHA03100 179 lsygvpINIKDVYGFTPLHYAvynNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNN-NKEIFKLL 244
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 8-128 3.22e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 44.10  E-value: 3.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393290873   8 DSSQTNVPLLQACIDGDFNYSKRLLESGFDPNIRDSRGRTGLHLAAARGNVDICQLLHKFGADLLATDYQGNTALHL--- 84
Cdd:PHA02878 164 DRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHIsvg 243

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 393290873  85 -CGHVDTIQFLVSNGLKIDICNH-QGATPLVLAKRrgvNKDVIRLL 128
Cdd:PHA02878 244 yCKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIK---SERKLKLL 286
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 13-70 3.60e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 43.89  E-value: 3.60e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 393290873  13 NVPLLQACIDGDFNYSKRLLESGFDPNIRDSRGRTGLHLAAARGNVDICQLLHKFGAD 70
Cdd:PHA03100 193 FTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 1-160 3.64e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 43.83  E-value: 3.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393290873   1 MSYVFVNDS--SQTNVPLLQACIDGDFNYSKRLLESGFDPNIRDSRGRTGLHLAAARGNVDICQLLHKFGADLLATDYQG 78
Cdd:PHA02875  89 DLGKFADDVfyKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCG 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393290873  79 NTALHLC---GHVDTIQFLVSNGLKIDICNHQGATPLVLAKRRGVNKDVIRLLesleeqevkgFNRGTHSKLETMQTAES 155
Cdd:PHA02875 169 CTPLIIAmakGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLF----------IKRGADCNIMFMIEGEE 238


                 ....*
gi 393290873 156 ESAME 160
Cdd:PHA02875 239 CTILD 243
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 15-119 4.43e-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: 43.85  E-value: 4.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393290873  15 PLLQACIDGDFNYSKRLLESGFDP-NIRD-----SRGRTGL-----H---LAAARGNVDICQLLHKFGADLLATDYQGNT 80
Cdd:cd22192   92 ALHIAVVNQNLNLVRELIARGADVvSPRAtgtffRPGPKNLiyygeHplsFAACVGNEEIVRLLIEHGADIRAQDSLGNT 171

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 393290873  81 ALHL----------CGHVDTIqfLVSNGLKIDIC-----NHQGATPLVLAKRRG 119
Cdd:cd22192  172 VLHIlvlqpnktfaCQMYDLI--LSYDKEDDLQPldlvpNNQGLTPFKLAAKEG 223
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 12-84 4.90e-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: 43.85  E-value: 4.90e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 393290873  12 TNVPLLQACIDGDFNYSKRLLES-GFDPNIRDSRGRTGLHLAAARGNVDICQLLHKFGADLL---ATD--YQGNTALHL 84
Cdd:cd22192   17 SESPLLLAAKENDVQAIKKLLKCpSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVnepMTSdlYQGETALHI 95
Ank_2 pfam12796
Ankyrin repeats (3 copies);
82-142 5.02e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 40.87  E-value: 5.02e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 393290873   82 LHLC---GHVDTIQFLVSNGLKIDICNHQGATPLVLAKRRGvNKDVIRLLesLEEQEVKGFNRG 142
Cdd:pfam12796   1 LHLAaknGNLELVKLLLENGADANLQDKNGRTALHLAAKNG-HLEIVKLL--LEHADVNLKDNG 61
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 10-129 9.96e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 42.74  E-value: 9.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393290873  10 SQTNVPLLQACIDGDFNYSKRLLESGFDPNIRDSRGRTGLHLAAARGNVD--ICQLLHKfGADLLATDYQGNTALHLCGH 87
Cdd:PHA02876 238 NKNDLSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSrlVPKLLER-GADVNAKNIKGETPLYLMAK 316

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 393290873  88 ----VDTIQFLVSNGLKIDICNHQGATPLVLAKRRGVNKD-VIRLLE 129
Cdd:PHA02876 317 ngydTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKDiVITLLE 363
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 27-225 1.15e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. 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.


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 42.49  E-value: 1.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393290873  27 YSKRLLESGFDPNIRDS-------RGRTG-------LHLAAARGNVDICQLL----HKfGADLLATDYQGNTALHLCGHV 88
Cdd:cd22196  109 LVELLVQNGADVHARASgeffkkkKGGPGfyfgelpLSLAACTNQLDIVKFLlenpHS-PADISARDSMGNTVLHALVEV 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393290873  89 -----DTIQFLVS--NGLKI------------DICNHQGATPLVLAKRRG---VNKDVIRllESLEEQEVKGFNRG---- 142
Cdd:cd22196  188 adntpENTKFVTKmyNEILIlgakirpllkleEITNKKGLTPLKLAAKTGkigIFAYILG--REIKEPECRHLSRKftew 265

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393290873 143 ----THSKL---ETMQTAESESAME--SHSLLNPNLQQG---EGVLSSFRTTWQEFVEDLGFWRVLLLIFVIALLSLgIA 210
Cdd:cd22196  266 aygpVHSSLydlSSIDTYEKNSVLEiiAYSSETPNRHEMllvEPLNKLLQDKWDKFVKRIFYFNFFVYFIYMIIFTL-AA 344

                        250
                 ....*....|....*...
gi 393290873 211 YY--VSGVLPF-VENQPE 225
Cdd:cd22196  345 YYrpVNKTPPFpIENTTG 362
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 44-75 1.96e-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: 37.65  E-value: 1.96e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 393290873   44 RGRTGLHLAAAR-GNVDICQLLHKFGADLLATD 75
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
PHA02946 PHA02946
ankyin-like protein; Provisional
 24-113 2.86e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 41.19  E-value: 2.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393290873  24 DFNYSKRLLESGFDPNIRDSRGRTGLHLAAARGNVDICQLLHKFGADLLATDYQGNTALHLCGHVDT-----IQFLVSNG 98
Cdd:PHA02946  51 DERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevierINLLVQYG 130

                         90
                 ....*....|....*.
gi 393290873  99 LKI-DICNHQGATPLV 113
Cdd:PHA02946 131 AKInNSVDEEGCGPLL 146
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 14-128 3.15e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 41.13  E-value: 3.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393290873  14 VPLLQACIDGDFNYSKRLLESGFDPNIRDSRGRTGLHLAAARGNVDICQLLHKFGAdllATDYQG---NTALHLC---GH 87
Cdd:PHA02875   4 VALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGA---IPDVKYpdiESELHDAveeGD 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 393290873  88 VDTIQFLVSNGLKI-DICNHQGATPLVLAKRRGvNKDVIRLL 128
Cdd:PHA02875  81 VKAVEELLDLGKFAdDVFYKDGMTPLHLATILK-KLDIMKLL 121
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 13-128 4.30e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 40.72  E-value: 4.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393290873  13 NVPLLQACIDGDFNYSKRLLESGFDPNIRDSRGRTGLHLAAARGNVDICQLLHKFGADLLATDYQGNTALH--LCGHVDT 90
Cdd:PHA02874 158 CYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHnaIIHNRSA 237

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 393290873  91 IQFLVSNGlKIDICNHQGATPLVLAKRRGVNKDVIRLL 128
Cdd:PHA02874 238 IELLINNA-SINDQDIDGSTPLHHAINPPCDIDIIDIL 274
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 30-118 6.83e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 40.43  E-value: 6.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393290873  30 RLLESGFDPNIRDSRGRTGLHLAAARG-NVDICQLLHKFGADLLATDYQGNTALH----LCGHVDTIQFLVSNGLKIDIC 104
Cdd:PHA02876 292 KLLERGADVNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHqastLDRNKDIVITLLELGANVNAR 371

                         90
                 ....*....|....
gi 393290873 105 NHQGATPLVLAKRR 118
Cdd:PHA02876 372 DYCDKTPIHYAAVR 385
PHA03095 PHA03095
ankyrin-like protein; Provisional
 51-128 1.07e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 39.62  E-value: 1.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393290873  51 LAAARGNVDICQLLHKFGADLLATDYQGNTALHLCGH------VDTIQFLVSNGL---KIDICnhqGATPLVLAKRRGVN 121
Cdd:PHA03095  20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHLYLHyssekvKDIVRLLLEAGAdvnAPERC---GFTPLHLYLYNATT 96


                 ....*..
gi 393290873 122 KDVIRLL 128
Cdd:PHA03095  97 LDVIKLL 103
PHA03095 PHA03095
ankyrin-like protein; Provisional
 27-119 1.44e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 39.24  E-value: 1.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393290873  27 YSKRLLESGFDPNIRDSRGRTGLHLAAARG---NVDICQLLHKfGADLLATDYQGNTALHLC-GHVDTIQF--LVSNGLK 100
Cdd:PHA03095 204 IVRELIRAGCDPAATDMLGNTPLHSMATGSsckRSLVLPLLIA-GISINARNRYGQTPLHYAaVFNNPRACrrLIALGAD 282

                         90
                 ....*....|....*....
gi 393290873 101 IDICNHQGATPLVLAKRRG 119
Cdd:PHA03095 283 INAVSSDGNTPLSLMVRNN 301
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 77-106 2.33e-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: 34.57  E-value: 2.33e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 393290873   77 QGNTALHLC----GHVDTIQFLVSNGLKIDICNH 106
Cdd:pfam00023   1 DGNTPLHLAagrrGNLEIVKLLLSKGADVNARDK 34
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 44-73 2.56e-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: 34.54  E-value: 2.56e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 393290873   44 RGRTGLHLAAARGNVDICQLLHKFGADLLA 73
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
63-115 2.92e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.01  E-value: 2.92e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 393290873   63 LLHKFGADLLATDYQGNTALHL---CGHVDTIQFLVSNGLKIDICNHQGATPLVLA 115
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVaakYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 44-71 3.06e-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: 34.10  E-value: 3.06e-03
                           10        20
                   ....*....|....*....|....*...
gi 393290873    44 RGRTGLHLAAARGNVDICQLLHKFGADL 71
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 45-119 4.52e-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: 37.55  E-value: 4.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393290873  45 GRTGLHLAAARGNVDICQLLHKFGAD---LLATDYQGNTALHLC-----GHVDTIQF-------LVSNGLKID------- 102
Cdd:cd21882  119 GELPLSLAACTNQEEIVRLLLENGAQpaaLEAQDSLGNTVLHALvlqadNTPENSAFvcqmynlLLSYGAHLDptqqlee 198

                         90
                 ....*....|....*..
gi 393290873 103 ICNHQGATPLVLAKRRG 119
Cdd:cd21882  199 IPNHQGLTPLKLAAVEG 215
PHA02741 PHA02741
hypothetical protein; Provisional
 39-124 6.86e-03

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 36.17  E-value: 6.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393290873  39 NIRDSRGRTGLHLAAARGN----VDICQLLHKFGADLLATD-YQGNTALHLCGH---VDTIQFLVSN-GLKIDICNHQGA 109
Cdd:PHA02741  54 NATDDAGQMCIHIAAEKHEaqlaAEIIDHLIELGADINAQEmLEGDTALHLAAHrrdHDLAEWLCCQpGIDLHFCNADNK 133

                         90
                 ....*....|....*
gi 393290873 110 TPLVLAKrrgVNKDV 124
Cdd:PHA02741 134 SPFELAI---DNEDV 145
PHA02946 PHA02946
ankyin-like protein; Provisional
 15-114 8.74e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 36.96  E-value: 8.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 393290873  15 PLLqACIDGDFNYSKRLLESGFDPNIRDSRGRTGL--HLAAARGNVDICQLLHKFGADLLATDYQGNTALHL-CG----H 87
Cdd:PHA02946 144 PLL-ACTDPSERVFKKIMSIGFEARIVDKFGKNHIhrHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHIvCSktvkN 222

                         90       100
                 ....*....|....*....|....*..
gi 393290873  88 VDTIQFLVSNgLKIDICNHQGATPLVL 114
Cdd:PHA02946 223 VDIINLLLPS-TDVNKQNKFGDSPLTL 248
PHA02743 PHA02743
Viral ankyrin protein; Provisional
 31-84 9.28e-03

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 35.56  E-value: 9.28e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 393290873  31 LLESGFDPNIRDSR-GRTGLHLAAARGNVDICQ-LLHKFGADLLATDYQGNTALHL 84
Cdd:PHA02743  79 LVNMGADINARELGtGNTLLHIAASTKNYELAEwLCRQLGVNLGAINYQHETAYHI 134
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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