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Conserved domains on  [gi|564359768|ref|XP_006241592|]
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ankyrin repeat domain-containing protein 46 isoform X1 [Rattus norvegicus]

Protein Classification

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

ankyrin repeat domain-containing protein; ANK proteins mediate specific protein-protein interactions without necessarily recognizing specific primary sequences which allows for one ankyrin repeat domain to recognize and bind to a variety of intracellular substrates and may be involved in a wide array of functions

Gene Ontology:  GO:0005515
PubMed:  17176038
SCOP:  4000366

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 5.39e-32

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 118.13  E-value: 5.39e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359768  15 PLLQACIDGDFTYSKRLLESGFDPNIRDSRGRTGLHLAAARGNVDICQLLHKFGADPLATDYQGNTALHL---CGHVDTI 91
Cdd:COG0666   90 LLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLaaaNGNLEIV 169

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 564359768  92 QFLVSNGLKIDICNHQGATPLVLAKRRGvNKDVIRLL 128
Cdd:COG0666  170 KLLLEAGADVNARDNDGETPLHLAAENG-HLEIVKLL 205
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
15-128 5.39e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 118.13  E-value: 5.39e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359768  15 PLLQACIDGDFTYSKRLLESGFDPNIRDSRGRTGLHLAAARGNVDICQLLHKFGADPLATDYQGNTALHL---CGHVDTI 91
Cdd:COG0666   90 LLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLaaaNGNLEIV 169

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 564359768  92 QFLVSNGLKIDICNHQGATPLVLAKRRGvNKDVIRLL 128
Cdd:COG0666  170 KLLLEAGADVNARDNDGETPLHLAAENG-HLEIVKLL 205
Ank_2 pfam12796
Ankyrin repeats (3 copies);
16-103 7.19e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.84  E-value: 7.19e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359768   16 LLQACIDGDFTYSKRLLESGFDPNIRDSRGRTGLHLAAARGNVDICQLLHKFgADPLATDYqGNTALHLC---GHVDTIQ 92
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAarsGHLEIVK 78

                          90
                  ....*....|.
gi 564359768   93 FLVSNGLKIDI 103
Cdd:pfam12796  79 LLLEKGADINV 89
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 14-108 1.47e-13

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 69.16  E-value: 1.47e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359768  14 VPLLQACIDGDFTYSKRLLESGFDPNIRDSRGRTGLHLAAARGNVDICQLLHKFGADPLATDYQGNTALHLCGHVDT--- 90
Cdd:PTZ00322  84 VELCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFrev 163

                         90
                 ....*....|....*...
gi 564359768  91 IQFLVSNGlkidICNHQG 108
Cdd:PTZ00322 164 VQLLSRHS----QCHFEL 177
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 2-128 1.64e-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: 54.32  E-value: 1.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359768    2 SYVFVNDSS-------QTnvPLLQACIDGDFTYSKRLLESGFDPNIR------------DS--RGRTGLHLAAARGNVDI 60
Cdd:TIGR00870 113 PLELANDQYtseftpgIT--ALHLAAHRQNYEIVKLLLERGASVPARacgdffvksqgvDSfyHGESPLNAAACLGSPSI 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359768   61 CQLLHKFGADPLATDYQGNTALHLC-----GHVDTI-------QFLVSNGLKID-------ICNHQGATPLVLAKRRGvN 121
Cdd:TIGR00870 191 VALLSEDPADILTADSLGNTLLHLLvmeneFKAEYEelscqmyNFALSLLDKLRdskelevILNHQGLTPLKLAAKEG-R 269


                  ....*..
gi 564359768  122 KDVIRLL 128
Cdd:TIGR00870 270 IVLFRLK 276
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 12-128 2.00e-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: 45.00  E-value: 2.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359768  12 TNVPLLQACIDGDFTYSKRLLES-GFDPNIRDSRGRTGLHLAAARGNVDICQLLHKFGAD----PLATD-YQGNTALHLC 85
Cdd:cd22192   17 SESPLLLAAKENDVQAIKKLLKCpSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElvnePMTSDlYQGETALHIA 96

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564359768  86 ---GHVDTIQFLVSNGlkIDICN----------------HQGATPLVLAKRRGvNKDVIRLL 128
Cdd:cd22192   97 vvnQNLNLVRELIARG--ADVVSpratgtffrpgpknliYYGEHPLSFAACVG-NEEIVRLL 155
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 44-71 1.04e-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: 1.04e-03
                           10        20
                   ....*....|....*....|....*...
gi 564359768    44 RGRTGLHLAAARGNVDICQLLHKFGADP 71
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
15-128 5.39e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 118.13  E-value: 5.39e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359768  15 PLLQACIDGDFTYSKRLLESGFDPNIRDSRGRTGLHLAAARGNVDICQLLHKFGADPLATDYQGNTALHL---CGHVDTI 91
Cdd:COG0666   90 LLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLaaaNGNLEIV 169

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 564359768  92 QFLVSNGLKIDICNHQGATPLVLAKRRGvNKDVIRLL 128
Cdd:COG0666  170 KLLLEAGADVNARDNDGETPLHLAAENG-HLEIVKLL 205
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
15-143 9.25e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 93.48  E-value: 9.25e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359768  15 PLLQACIDGDFTYSKRLLESGFDPNIRDSRGRTGLHLAAARGNVDICQLLHKFGADPLATDYQGNTALHL---CGHVDTI 91
Cdd:COG0666  156 PLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLaaeNGNLEIV 235

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 564359768  92 QFLVSNGLKIDICNHQGATPLVLAKRRGVNKDVIRLLESLEEQEVKGFNRGT 143
Cdd:COG0666  236 KLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
7-128 2.64e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 92.32  E-value: 2.64e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359768   7 NDSSQTNVPLLQACIDGDFTYSKRLLESGFDPNIRDSRGRTGLHLAAARGNVDICQLLHKFGADPLATDYQGNTALHLC- 85
Cdd:COG0666   49 LADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAa 128

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 564359768  86 --GHVDTIQFLVSNGLKIDICNHQGATPLVLAKRRGvNKDVIRLL 128
Cdd:COG0666  129 ynGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANG-NLEIVKLL 172
Ank_2 pfam12796
Ankyrin repeats (3 copies);
16-103 7.19e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.84  E-value: 7.19e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359768   16 LLQACIDGDFTYSKRLLESGFDPNIRDSRGRTGLHLAAARGNVDICQLLHKFgADPLATDYqGNTALHLC---GHVDTIQ 92
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAarsGHLEIVK 78

                          90
                  ....*....|.
gi 564359768   93 FLVSNGLKIDI 103
Cdd:pfam12796  79 LLLEKGADINV 89
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 14-108 1.47e-13

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 69.16  E-value: 1.47e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359768  14 VPLLQACIDGDFTYSKRLLESGFDPNIRDSRGRTGLHLAAARGNVDICQLLHKFGADPLATDYQGNTALHLCGHVDT--- 90
Cdd:PTZ00322  84 VELCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFrev 163

                         90
                 ....*....|....*...
gi 564359768  91 IQFLVSNGlkidICNHQG 108
Cdd:PTZ00322 164 VQLLSRHS----QCHFEL 177
PHA03095 PHA03095
ankyrin-like protein; Provisional
 31-128 3.73e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 64.66  E-value: 3.73e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359768  31 LLESGFDPNIRDSRGRTGLHLAAARGNV-DICQLLHKFGADPLATDYQGNTALH--LCG---HVDTIQFLVSNGLKIDIC 104
Cdd:PHA03095  69 LLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKAGADVNAKDKVGRTPLHvyLSGfniNPKVIRLLLRKGADVNAL 148

                         90       100
                 ....*....|....*....|....*
gi 564359768 105 NHQGATPL-VLAKRRGVNKDVIRLL 128
Cdd:PHA03095 149 DLYGMTPLaVLLKSRNANVELLRLL 173
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
11-128 4.08e-12

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 64.20  E-value: 4.08e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359768  11 QTNVPLLQACIDGDFTYSKRLLESGFDPNIRDSRGRTGLHLAAARGNVDICQLLHKFGADPLATDYQGNTALHLC---GH 87
Cdd:COG0666   20 LLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAarnGD 99

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 564359768  88 VDTIQFLVSNGLKIDICNHQGATPLVLAKRRGvNKDVIRLL 128
Cdd:COG0666  100 LEIVKLLLEAGADVNARDKDGETPLHLAAYNG-NLEIVKLL 139
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 7-128 6.82e-12

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 64.50  E-value: 6.82e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359768   7 NDSSQTNVPLLQACIDGDFTYSKRLLESGFDPNIRDSRGRTGLHLAAARGNVDICQLLHKFGADPLATDYQGNTAL---- 82
Cdd:PLN03192 520 HDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALwnai 599

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564359768  83 ---H----------------------LC-----GHVDTIQFLVSNGLKIDICNHQGATPLVLAKRRGvNKDVIRLL 128
Cdd:PLN03192 600 sakHhkifrilyhfasisdphaagdlLCtaakrNDLTAMKELLKQGLNVDSEDHQGATALQVAMAED-HVDMVRLL 674
Ank_4 pfam13637
Ankyrin repeats (many copies);
45-95 3.24e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 56.90  E-value: 3.24e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 564359768   45 GRTGLHLAAARGNVDICQLLHKFGADPLATDYQGNTALHLC---GHVDTIQFLV 95
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAasnGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 8-142 1.31e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 60.36  E-value: 1.31e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359768   8 DSSQTNVPllqaCIDGDFTysKRLLESGFDPNIRDSRGRTGLHLAAARGNVDICQLLHKFGADPLATDYQGNTALHLC-- 85
Cdd:PHA02874  93 DTSILPIP----CIEKDMI--KTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAik 166

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 564359768  86 -GHVDTIQFLVSNGLKIDICNHQGATPLVLAKRRGVNKDVIRLLESLEEQEVKgFNRG 142
Cdd:PHA02874 167 hNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNK-CKNG 223
PHA03095 PHA03095
ankyrin-like protein; Provisional
 29-115 3.96e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 58.88  E-value: 3.96e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359768  29 KRLLESGFDPNIRDSRGRTGLH--LAAARGNVDICQLLHKFGADPLATDYQGNTALHL------CGHVDtIQFLVSNGLK 100
Cdd:PHA03095 171 RLLIDAGADVYAVDDRFRSLLHhhLQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSmatgssCKRSL-VLPLLIAGIS 249

                         90
                 ....*....|....*
gi 564359768 101 IDICNHQGATPLVLA 115
Cdd:PHA03095 250 INARNRYGQTPLHYA 264
Ank_4 pfam13637
Ankyrin repeats (many copies);
15-65 4.81e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.43  E-value: 4.81e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 564359768   15 PLLQACIDGDFTYSKRLLESGFDPNIRDSRGRTGLHLAAARGNVDICQLLH 65
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 1-128 2.90e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 56.15  E-value: 2.90e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359768   1 MSYVFVNDSSQTNV--PLLQACIDGDFTYSKRLLESG-FDPNIRDSRGRTGLHLAAARGNVDICQLLHKFGADPLATDYQ 77
Cdd:PHA02875  55 MKHGAIPDVKYPDIesELHDAVEEGDVKAVEELLDLGkFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTD 134

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 564359768  78 GNTALHLC---GHVDTIQFLVSNGLKIDICNHQGATPLVLAKRRGvNKDVIRLL 128
Cdd:PHA02875 135 KFSPLHLAvmmGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKG-DIAICKML 187
Ank_5 pfam13857
Ankyrin repeats (many copies);
31-85 4.60e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 50.81  E-value: 4.60e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 564359768   31 LLESG-FDPNIRDSRGRTGLHLAAARGNVDICQLLHKFGADPLATDYQGNTALHLC 85
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 29-128 6.14e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 55.44  E-value: 6.14e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359768  29 KRLLESGFDPNIRDSRGRTGLHLAA-----ARGNVDICQLLHKFGADPLATDYQGNTALHLC-----GHVDTIQFLVSNG 98
Cdd:PHA03100  52 KILLDNGADINSSTKNNSTPLHYLSnikynLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAiskksNSYSIVEYLLDNG 131

                         90       100       110
                 ....*....|....*....|....*....|.
gi 564359768  99 LKIDICNHQGATPLVLAKRRG-VNKDVIRLL 128
Cdd:PHA03100 132 ANVNIKNSDGENLLHLYLESNkIDLKILKLL 162
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 13-128 1.55e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 54.30  E-value: 1.55e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359768  13 NVPLLQA-CIDGDFTYSKRLLESGFDPNIRDSRGRTGLHLAAARGNVDICQLLHKFGADPLATDYQGNTALH--LCGH-- 87
Cdd:PHA02876 342 ITPLHQAsTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHfaLCGTnp 421

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 564359768  88 VDTIQFLVSNGLKIDICNHQGATPLVLAKRRGVNKDVIRLL 128
Cdd:PHA02876 422 YMSVKTLIDRGANVNSKNKDLSTPLHYACKKNCKLDVIEML 462
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 2-128 1.64e-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: 54.32  E-value: 1.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359768    2 SYVFVNDSS-------QTnvPLLQACIDGDFTYSKRLLESGFDPNIR------------DS--RGRTGLHLAAARGNVDI 60
Cdd:TIGR00870 113 PLELANDQYtseftpgIT--ALHLAAHRQNYEIVKLLLERGASVPARacgdffvksqgvDSfyHGESPLNAAACLGSPSI 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359768   61 CQLLHKFGADPLATDYQGNTALHLC-----GHVDTI-------QFLVSNGLKID-------ICNHQGATPLVLAKRRGvN 121
Cdd:TIGR00870 191 VALLSEDPADILTADSLGNTLLHLLvmeneFKAEYEelscqmyNFALSLLDKLRdskelevILNHQGLTPLKLAAKEG-R 269


                  ....*..
gi 564359768  122 KDVIRLL 128
Cdd:TIGR00870 270 IVLFRLK 276
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 29-123 2.13e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 52.51  E-value: 2.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359768  29 KRLLESGFDPNIRDSRGRTGLH--LAAARGNVDICQLLHKFGADPLATDYQGNTALH--LCGHVD--TIQFLVSNGLKID 102
Cdd:PHA02859 107 KILIDSGSSITEEDEDGKNLLHmyMCNFNVRINVIKLLIDSGVSFLNKDFDNNNILYsyILFHSDkkIFDFLTSLGIDIN 186

                         90       100
                 ....*....|....*....|...
gi 564359768 103 ICNHQGATPLVLAKRRGV--NKD 123
Cdd:PHA02859 187 ETNKSGYNCYDLIKFRNLffNKQ 209
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 6-112 4.96e-08

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 52.99  E-value: 4.96e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359768   6 VNDSSQTNVPL-------LQACIDGDFTYSkrLLESGFDPNIRDSRGRTGLHLAAARGNV--DICQLLHKFGADPLATDY 76
Cdd:PHA02716 273 LDGNKVKNIPMilhsyitLARNIDISVVYS--FLQPGVKLHYKDSAGRTCLHQYILRHNIstDIIKLLHEYGNDLNEPDN 350

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 564359768  77 QGNTALH-----LCG------------HVDTIQFLVSNGLKIDICNHQGATPL 112
Cdd:PHA02716 351 IGNTVLHtylsmLSVvnildpetdndiRLDVIQCLISLGADITAVNCLGYTPL 403
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 29-103 1.18e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 51.59  E-value: 1.18e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564359768  29 KRLLESGFDPNIRDSRGRTGLHLAAARGNVDICQLLHKFGADPLATDYQGNTALHLC---GHVDTIQFLVSNGLKIDI 103
Cdd:PHA03100 176 NYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAilnNNKEIFKLLLNNGPSIKT 253
Ank_2 pfam12796
Ankyrin repeats (3 copies);
15-75 6.64e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 45.88  E-value: 6.64e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564359768   15 PLLQACIDGDFTYSKRLLESgFDPNIRDSrGRTGLHLAAARGNVDICQLLHKFGADPLATD 75
Cdd:pfam12796  33 ALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 31-82 1.20e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 48.48  E-value: 1.20e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 564359768  31 LLESGFDPNIRDSRGRTGLHLAAARGNVDICQLLHKFGADPLATDYQGNTAL 82
Cdd:PHA03095 243 LLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPL 294
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 1-128 4.90e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 46.58  E-value: 4.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359768   1 MSYVFVNDSSQTNVPLLqacidgdftySKRLLESGFDPNIRDSRGRTGLHLAAAR--GNVDICQLLHKFGADPLATDYQG 78
Cdd:PHA03100  72 LHYLSNIKYNLTDVKEI----------VKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDG 141

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564359768  79 NTALHL---CGHVDT--IQFLVSNG----------------LKIDICNHQGATPLVLAKRRgVNKDVIRLL 128
Cdd:PHA03100 142 ENLLHLyleSNKIDLkiLKLLIDKGvdinaknrvnyllsygVPINIKDVYGFTPLHYAVYN-NNPEFVKYL 211
Ank_4 pfam13637
Ankyrin repeats (many copies);
78-128 7.97e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.88  E-value: 7.97e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 564359768   78 GNTALHLC---GHVDTIQFLVSNGLKIDICNHQGATPLVLAKRRGvNKDVIRLL 128
Cdd:pfam13637   1 ELTALHAAaasGHLELLRLLLEKGADINAVDGNGETALHFAASNG-NVEVLKLL 53
Ank_2 pfam12796
Ankyrin repeats (3 copies);
82-142 1.34e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 42.41  E-value: 1.34e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564359768   82 LHLC---GHVDTIQFLVSNGLKIDICNHQGATPLVLAKRRGvNKDVIRLLesLEEQEVKGFNRG 142
Cdd:pfam12796   1 LHLAaknGNLELVKLLLENGADANLQDKNGRTALHLAAKNG-HLEIVKLL--LEHADVNLKDNG 61
PHA02946 PHA02946
ankyin-like protein; Provisional
 24-113 1.45e-05

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 45.04  E-value: 1.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359768  24 DFTYSKRLLESGFDPNIRDSRGRTGLHLAAARGNVDICQLLHKFGADPLATDYQGNTALHLCGHVDT-----IQFLVSNG 98
Cdd:PHA02946  51 DERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevierINLLVQYG 130

                         90
                 ....*....|....*.
gi 564359768  99 LKI-DICNHQGATPLV 113
Cdd:PHA02946 131 AKInNSVDEEGCGPLL 146
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 12-128 2.00e-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: 45.00  E-value: 2.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359768  12 TNVPLLQACIDGDFTYSKRLLES-GFDPNIRDSRGRTGLHLAAARGNVDICQLLHKFGAD----PLATD-YQGNTALHLC 85
Cdd:cd22192   17 SESPLLLAAKENDVQAIKKLLKCpSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElvnePMTSDlYQGETALHIA 96

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564359768  86 ---GHVDTIQFLVSNGlkIDICN----------------HQGATPLVLAKRRGvNKDVIRLL 128
Cdd:cd22192   97 vvnQNLNLVRELIARG--ADVVSpratgtffrpgpknliYYGEHPLSFAACVG-NEEIVRLL 155
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 49-119 2.42e-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: 44.62  E-value: 2.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359768  49 LHLAAARGNVDICQLLHKFGADPLATDYQGNTALHL----------CGHVDTIqfLVSNGLKIDIC-----NHQGATPLV 113
Cdd:cd22192  140 LSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHIlvlqpnktfaCQMYDLI--LSYDKEDDLQPldlvpNNQGLTPFK 217


                 ....*.
gi 564359768 114 LAKRRG 119
Cdd:cd22192  218 LAAKEG 223
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 1-137 2.88e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 44.67  E-value: 2.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359768   1 MSYVFVNDSSQTNVPLLQACIDGDFTYSKRLLESGFDPNIRDSRGRTGLHLAAARGNVDICQLLHKFGADPLATDYQGNT 80
Cdd:PHA02876 134 IHYDKINESIEYMKLIKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLS 213

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359768  81 ALHLC---GHVDTIQFLVSNglkidicnhqgatplvlakRRGVNKDVIRLLESLEEQEVK 137
Cdd:PHA02876 214 VLECAvdsKNIDTIKAIIDN-------------------RSNINKNDLSLLKAIRNEDLE 254
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 44-75 5.35e-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: 39.19  E-value: 5.35e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 564359768   44 RGRTGLHLAAAR-GNVDICQLLHKFGADPLATD 75
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 8-128 5.99e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 43.33  E-value: 5.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359768   8 DSSQTNVPLLQACIDGDFTYSKRLLESGFDPNIRDSRGRTGLHLAAARGNVDICQLLHKFGADPLATDYQGNTALHL--- 84
Cdd:PHA02878 164 DRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHIsvg 243

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 564359768  85 -CGHVDTIQFLVSNGLKIDICNH-QGATPLVLAKRrgvNKDVIRLL 128
Cdd:PHA02878 244 yCKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIK---SERKLKLL 286
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 14-128 1.06e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 42.67  E-value: 1.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359768  14 VPLLQACIDGDFTYSKRLLESGFDPNIRDSRGRTGLHLAAARGNVDICQLLHKFGADPLATDYQGNTALHLC---GHVDT 90
Cdd:PHA02875   4 VALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAveeGDVKA 83

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 564359768  91 IQFLVSNGLKI-DICNHQGATPLVLAKRRGvNKDVIRLL 128
Cdd:PHA02875  84 VEELLDLGKFAdDVFYKDGMTPLHLATILK-KLDIMKLL 121
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 10-129 2.16e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 41.97  E-value: 2.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359768  10 SQTNVPLLQACIDGDFTYSKRLLESGFDPNIRDSRGRTGLHLAAARGNVD--ICQLLHKfGADPLATDYQGNTALHLCGH 87
Cdd:PHA02876 238 NKNDLSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSrlVPKLLER-GADVNAKNIKGETPLYLMAK 316

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 564359768  88 ----VDTIQFLVSNGLKIDICNHQGATPLVLAKRRGVNKD-VIRLLE 129
Cdd:PHA02876 317 ngydTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKDiVITLLE 363
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 6-128 2.71e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 41.19  E-value: 2.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359768   6 VNDSSQTNVPLLQACIDGDFTYS---KRLLESGFDPNIRDSRGRTGLHLAAARGNVD--ICQLLHKFGAD---------- 70
Cdd:PHA03100  99 VNAPDNNGITPLLYAISKKSNSYsivEYLLDNGANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKGVDinaknrvnyl 178

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564359768  71 -----PL-ATDYQGNTALHLC---GHVDTIQFLVSNGLKIDICNHQGATPLVLAKRRGvNKDVIRLL 128
Cdd:PHA03100 179 lsygvPInIKDVYGFTPLHYAvynNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNN-NKEIFKLL 244
PHA02946 PHA02946
ankyin-like protein; Provisional
 15-114 4.43e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 40.81  E-value: 4.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359768  15 PLLqACIDGDFTYSKRLLESGFDPNIRDSRGRTGLH--LAAARGNVDICQLLHKFGADPLATDYQGNTALHL-CG----H 87
Cdd:PHA02946 144 PLL-ACTDPSERVFKKIMSIGFEARIVDKFGKNHIHrhLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHIvCSktvkN 222

                         90       100
                 ....*....|....*....|....*..
gi 564359768  88 VDTIQFLVSNgLKIDICNHQGATPLVL 114
Cdd:PHA02946 223 VDIINLLLPS-TDVNKQNKFGDSPLTL 248
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 45-119 6.12e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 40.25  E-value: 6.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359768  45 GRTGLHLAAARGNVDICQLLHKFGADP---LATDYQGNTALHLC-----GHVDTIQF-------LVSNGLKID------- 102
Cdd:cd21882  119 GELPLSLAACTNQEEIVRLLLENGAQPaalEAQDSLGNTVLHALvlqadNTPENSAFvcqmynlLLSYGAHLDptqqlee 198

                         90
                 ....*....|....*..
gi 564359768 103 ICNHQGATPLVLAKRRG 119
Cdd:cd21882  199 IPNHQGLTPLKLAAVEG 215
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 15-103 6.12e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 40.36  E-value: 6.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359768  15 PLLQACIDGDFTYSKRLLESGFDPNIRDSRGRTGLHLAAARGNVDICQLLHKFGADPLATDYQGNTALhLCGHV-----D 89
Cdd:PHA02875 138 PLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAA-LCYAIennkiD 216

                         90
                 ....*....|....
gi 564359768  90 TIQFLVSNGLKIDI 103
Cdd:PHA02875 217 IVRLFIKRGADCNI 230
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 44-71 1.04e-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: 1.04e-03
                           10        20
                   ....*....|....*....|....*...
gi 564359768    44 RGRTGLHLAAARGNVDICQLLHKFGADP 71
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 44-73 1.11e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 35.31  E-value: 1.11e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 564359768   44 RGRTGLHLAAARGNVDICQLLHKFGADPLA 73
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
63-115 1.23e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.17  E-value: 1.23e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 564359768   63 LLHKFGADPLATDYQGNTALHL---CGHVDTIQFLVSNGLKIDICNHQGATPLVLA 115
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVaakYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 30-118 1.36e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 39.28  E-value: 1.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359768  30 RLLESGFDPNIRDSRGRTGLHLAAARG-NVDICQLLHKFGADPLATDYQGNTALH----LCGHVDTIQFLVSNGLKIDIC 104
Cdd:PHA02876 292 KLLERGADVNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHqastLDRNKDIVITLLELGANVNAR 371

                         90
                 ....*....|....
gi 564359768 105 NHQGATPLVLAKRR 118
Cdd:PHA02876 372 DYCDKTPIHYAAVR 385
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 77-106 1.41e-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: 35.34  E-value: 1.41e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 564359768   77 QGNTALHLC----GHVDTIQFLVSNGLKIDICNH 106
Cdd:pfam00023   1 DGNTPLHLAagrrGNLEIVKLLLSKGADVNARDK 34
PHA03095 PHA03095
ankyrin-like protein; Provisional
 51-128 1.97e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 38.85  E-value: 1.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359768  51 LAAARGNVDICQLLHKFGADPLATDYQGNTALHLCGH------VDTIQFLVSNGL---KIDICnhqGATPLVLAKRRGVN 121
Cdd:PHA03095  20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHLYLHyssekvKDIVRLLLEAGAdvnAPERC---GFTPLHLYLYNATT 96


                 ....*..
gi 564359768 122 KDVIRLL 128
Cdd:PHA03095  97 LDVIKLL 103
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 13-128 2.79e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 38.41  E-value: 2.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359768  13 NVPLLQACIDGDFTYSKRLLESGFDPNIRDSRGRTGLHLAAARGNVDICQLLHKFGADPLATDYQGNTALH--LCGHVDT 90
Cdd:PHA02874 158 CYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHnaIIHNRSA 237

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 564359768  91 IQFLVSNGlKIDICNHQGATPLVLAKRRGVNKDVIRLL 128
Cdd:PHA02874 238 IELLINNA-SINDQDIDGSTPLHHAINPPCDIDIIDIL 274
PHA03095 PHA03095
ankyrin-like protein; Provisional
 26-119 4.80e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 37.70  E-value: 4.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564359768  26 TYSKRLLESGFDPNIRDSRGRTGLHLAAARG---NVDICQLLHKfGADPLATDYQGNTALHLC-GHVDTIQF--LVSNGL 99
Cdd:PHA03095 203 RIVRELIRAGCDPAATDMLGNTPLHSMATGSsckRSLVLPLLIA-GISINARNRYGQTPLHYAaVFNNPRACrrLIALGA 281

                         90       100
                 ....*....|....*....|
gi 564359768 100 KIDICNHQGATPLVLAKRRG 119
Cdd:PHA03095 282 DINAVSSDGNTPLSLMVRNN 301
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 16-70 5.15e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 37.54  E-value: 5.15e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 564359768  16 LLQACIDGDFTYSKRLLESGFDPNIRDSRGRTGLHLAAARGNVDICQLLHKFGAD 70
Cdd:PLN03192 626 LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGAD 680
 
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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