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Conserved domains on  [gi|528485865|ref|XP_005166560|]
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ankyrin repeat domain-containing protein 46 isoform X1 [Danio rerio]

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 1.22e-29

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 111.97  E-value: 1.22e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485865  15 PLLQACIDGDLSFARRLLETGCDPNIRDHRGRTGLHLAAARGNVDICRFLHKFGADLLATDYQGNTALHL---CGHVDTI 91
Cdd:COG0666   90 LLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLaaaNGNLEIV 169

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 528485865  92 QFLVSNGLKIDICNHNGSTPLVLAKRRGvNKDAIRLL 128
Cdd:COG0666  170 KLLLEAGADVNARDNDGETPLHLAAENG-HLEIVKLL 205
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
15-128 1.22e-29

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 111.97  E-value: 1.22e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485865  15 PLLQACIDGDLSFARRLLETGCDPNIRDHRGRTGLHLAAARGNVDICRFLHKFGADLLATDYQGNTALHL---CGHVDTI 91
Cdd:COG0666   90 LLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLaaaNGNLEIV 169

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 528485865  92 QFLVSNGLKIDICNHNGSTPLVLAKRRGvNKDAIRLL 128
Cdd:COG0666  170 KLLLEAGADVNARDNDGETPLHLAAENG-HLEIVKLL 205
Ank_2 pfam12796
Ankyrin repeats (3 copies);
16-103 4.55e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 78.62  E-value: 4.55e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485865   16 LLQACIDGDLSFARRLLETGCDPNIRDHRGRTGLHLAAARGNVDICRFLHKFgADLLATDYqGNTALHLC---GHVDTIQ 92
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAarsGHLEIVK 78

                          90
                  ....*....|.
gi 528485865   93 FLVSNGLKIDI 103
Cdd:pfam12796  79 LLLEKGADINV 89
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 13-108 7.56e-15

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 73.01  E-value: 7.56e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485865  13 SVPLLQACIDGDLSFARRLLETGCDPNIRDHRGRTGLHLAAARGNVDICRFLHKFGADLLATDYQGNTALHLCGHVDT-- 90
Cdd:PTZ00322  83 TVELCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFre 162

                         90
                 ....*....|....*....
gi 528485865  91 -IQFLVSNGlkidICNHNG 108
Cdd:PTZ00322 163 vVQLLSRHS----QCHFEL 177
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 15-128 2.99e-07

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: 50.46  E-value: 2.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485865   15 PLLQACIDGDLSFARRLLETGCDPNIR---------DHR-----GRTGLHLAAARGNVDICRFLHKFGADLLATDYQGNT 80
Cdd:TIGR00870 131 ALHLAAHRQNYEIVKLLLERGASVPARacgdffvksQGVdsfyhGESPLNAAACLGSPSIVALLSEDPADILTADSLGNT 210

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528485865   81 ALHLC-----GHVDTI-------QFLVSNGLKID-------ICNHNGSTPLVLAKRRGvNKDAIRLL 128
Cdd:TIGR00870 211 LLHLLvmeneFKAEYEelscqmyNFALSLLDKLRdskelevILNHQGLTPLKLAAKEG-RIVLFRLK 276
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 12-84 5.88e-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: 43.46  E-value: 5.88e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528485865  12 TSVPLLQACIDGDLSFARRLLET-GCDPNIRDHRGRTGLHLAAARGNVDICRFLHKFGADLL---ATD--YQGNTALHL 84
Cdd:cd22192   17 SESPLLLAAKENDVQAIKKLLKCpSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVnepMTSdlYQGETALHI 95
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 44-71 3.24e-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: 3.24e-03
                           10        20
                   ....*....|....*....|....*...
gi 528485865    44 RGRTGLHLAAARGNVDICRFLHKFGADL 71
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
15-128 1.22e-29

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 111.97  E-value: 1.22e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485865  15 PLLQACIDGDLSFARRLLETGCDPNIRDHRGRTGLHLAAARGNVDICRFLHKFGADLLATDYQGNTALHL---CGHVDTI 91
Cdd:COG0666   90 LLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLaaaNGNLEIV 169

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 528485865  92 QFLVSNGLKIDICNHNGSTPLVLAKRRGvNKDAIRLL 128
Cdd:COG0666  170 KLLLEAGADVNARDNDGETPLHLAAENG-HLEIVKLL 205
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
15-174 1.20e-27

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 106.58  E-value: 1.20e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485865  15 PLLQACIDGDLSFARRLLETGCDPNIRDHRGRTGLHLAAARGNVDICRFLHKFGADLLATDYQGNTALHLC---GHVDTI 91
Cdd:COG0666  123 PLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAaenGHLEIV 202

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485865  92 QFLVSNGLKIDICNHNGSTPLVLAKRRGVNKDAIRLLEGLEEQEVKGFNRGAHSKLEAMQMAESESAMESHSLLNPNLQN 171
Cdd:COG0666  203 KLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282


                 ...
gi 528485865 172 SEG 174
Cdd:COG0666  283 LDL 285
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
6-128 9.03e-21

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 88.09  E-value: 9.03e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485865   6 INDSSQTSVPLLQACIDGDLSFARRLLETGCDPNIRDHRGRTGLHLAAARGNVDICRFLHKFGADLLATDYQGNTALHLC 85
Cdd:COG0666   48 ALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLA 127

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 528485865  86 ---GHVDTIQFLVSNGLKIDICNHNGSTPLVLAKRRGvNKDAIRLL 128
Cdd:COG0666  128 aynGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANG-NLEIVKLL 172
Ank_2 pfam12796
Ankyrin repeats (3 copies);
16-103 4.55e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 78.62  E-value: 4.55e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485865   16 LLQACIDGDLSFARRLLETGCDPNIRDHRGRTGLHLAAARGNVDICRFLHKFgADLLATDYqGNTALHLC---GHVDTIQ 92
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAarsGHLEIVK 78

                          90
                  ....*....|.
gi 528485865   93 FLVSNGLKIDI 103
Cdd:pfam12796  79 LLLEKGADINV 89
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 13-108 7.56e-15

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 73.01  E-value: 7.56e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485865  13 SVPLLQACIDGDLSFARRLLETGCDPNIRDHRGRTGLHLAAARGNVDICRFLHKFGADLLATDYQGNTALHLCGHVDT-- 90
Cdd:PTZ00322  83 TVELCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFre 162

                         90
                 ....*....|....*....
gi 528485865  91 -IQFLVSNGlkidICNHNG 108
Cdd:PTZ00322 163 vVQLLSRHS----QCHFEL 177
PHA03095 PHA03095
ankyrin-like protein; Provisional
 29-128 7.85e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 63.89  E-value: 7.85e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485865  29 RRLLETGCDPNIRDHRGRTGLHLAAARGNV-DICRFLHKFGADLLATDYQGNTALH--LCG---HVDTIQFLVSNGLKID 102
Cdd:PHA03095  67 RLLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKAGADVNAKDKVGRTPLHvyLSGfniNPKVIRLLLRKGADVN 146

                         90       100
                 ....*....|....*....|....*..
gi 528485865 103 ICNHNGSTPL-VLAKRRGVNKDAIRLL 128
Cdd:PHA03095 147 ALDLYGMTPLaVLLKSRNANVELLRLL 173
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 8-119 5.03e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 61.52  E-value: 5.03e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485865   8 DSSQTSVPllqaCIDGDLsfARRLLETGCDPNIRDHRGRTGLHLAAARGNVDICRFLHKFGADLLATDYQGNTALHLC-- 85
Cdd:PHA02874  93 DTSILPIP----CIEKDM--IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAik 166

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 528485865  86 -GHVDTIQFLVSNGLKIDICNHNGSTPLVLAKRRG 119
Cdd:PHA02874 167 hNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYG 201
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
15-128 5.50e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 60.74  E-value: 5.50e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485865  15 PLLQACIDGDLSFARRLLETGCDPNIRDHRGRTGLHLAAARGNVDICRFLHKFGADLLATDYQGNTALHLC---GHVDTI 91
Cdd:COG0666   24 LLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAarnGDLEIV 103

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 528485865  92 QFLVSNGLKIDICNHNGSTPLVLAKRRGvNKDAIRLL 128
Cdd:COG0666  104 KLLLEAGADVNARDKDGETPLHLAAYNG-NLEIVKLL 139
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 7-128 1.63e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 60.27  E-value: 1.63e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485865   7 NDSSQTSVPLLQACIDGDLSFARRLLETGCDPNIRDHRGRTGLHLAAARGNVDICRFLHKFGADLLATDYQGNTAL---- 82
Cdd:PLN03192 520 HDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALwnai 599

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528485865  83 ---H----------------------LC-----GHVDTIQFLVSNGLKIDICNHNGSTPLVLAKRRGvNKDAIRLL 128
Cdd:PLN03192 600 sakHhkifrilyhfasisdphaagdlLCtaakrNDLTAMKELLKQGLNVDSEDHQGATALQVAMAED-HVDMVRLL 674
Ank_4 pfam13637
Ankyrin repeats (many copies);
45-95 1.74e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.59  E-value: 1.74e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 528485865   45 GRTGLHLAAARGNVDICRFLHKFGADLLATDYQGNTALHLC---GHVDTIQFLV 95
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAasnGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
15-65 2.03e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.59  E-value: 2.03e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 528485865   15 PLLQACIDGDLSFARRLLETGCDPNIRDHRGRTGLHLAAARGNVDICRFLH 65
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 29-115 6.56e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 58.11  E-value: 6.56e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485865  29 RRLLETGCDPNIRDHRGRTGLH--LAAARGNVDICRFLHKFGADLLATDYQGNTALHL------CGHVDtIQFLVSNGLK 100
Cdd:PHA03095 171 RLLIDAGADVYAVDDRFRSLLHhhLQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSmatgssCKRSL-VLPLLIAGIS 249

                         90
                 ....*....|....*
gi 528485865 101 IDICNHNGSTPLVLA 115
Cdd:PHA03095 250 INARNRYGQTPLHYA 264
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 16-139 9.35e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 57.67  E-value: 9.35e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485865  16 LLQACIDGDLSFARRLLETGCDPNIRDHRGRTGLHLAAARGNVDICRFLHKFGADLLATDYQGNTALHLC---GHVDTIQ 92
Cdd:PHA02874 128 LHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAaeyGDYACIK 207

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 528485865  93 FLVSNGLKIDICNHNGSTPLVLAKRRgvNKDAIRLL---EGLEEQEVKGF 139
Cdd:PHA02874 208 LLIDHGNHIMNKCKNGFTPLHNAIIH--NRSAIELLinnASINDQDIDGS 255
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 15-128 1.18e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 57.77  E-value: 1.18e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485865  15 PLLQAC-IDGDLSFARRLLETGCDPNIRDHRGRTGLHLAAARGNVDICRFLHKFGADLLATDYQGNTALH--LCGH--VD 89
Cdd:PHA02876 344 PLHQAStLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHfaLCGTnpYM 423

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 528485865  90 TIQFLVSNGLKIDICNHNGSTPLVLAKRRGVNKDAIRLL 128
Cdd:PHA02876 424 SVKTLIDRGANVNSKNKDLSTPLHYACKKNCKLDVIEML 462
PHA03095 PHA03095
ankyrin-like protein; Provisional
 29-128 1.90e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 56.96  E-value: 1.90e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485865  29 RRLLETGCDPNIRDHRGRTGLHLAAARGN---VDICRFLHKFGADLLATDYQGNTALHLCGH----VDTIQFLVSNGLKI 101
Cdd:PHA03095  31 RRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYnattLDVIKLLIKAGADV 110

                         90       100
                 ....*....|....*....|....*...
gi 528485865 102 DICNHNGSTPL-VLAKRRGVNKDAIRLL 128
Cdd:PHA03095 111 NAKDKVGRTPLhVYLSGFNINPKVIRLL 138
Ank_5 pfam13857
Ankyrin repeats (many copies);
31-85 4.46e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 51.19  E-value: 4.46e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 528485865   31 LLETG-CDPNIRDHRGRTGLHLAAARGNVDICRFLHKFGADLLATDYQGNTALHLC 85
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_2 pfam12796
Ankyrin repeats (3 copies);
15-75 5.75e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 48.96  E-value: 5.75e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528485865   15 PLLQACIDGDLSFARRLLETgCDPNIRDHrGRTGLHLAAARGNVDICRFLHKFGADLLATD 75
Cdd:pfam12796  33 ALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 30-128 7.93e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 51.97  E-value: 7.93e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485865  30 RLLETGCDPNIRDHRGRTGLHLAA-----ARGNVDICRFLHKFGADLLATDYQGNTALHLC-----GHVDTIQFLVSNGL 99
Cdd:PHA03100  53 ILLDNGADINSSTKNNSTPLHYLSnikynLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAiskksNSYSIVEYLLDNGA 132

                         90       100       110
                 ....*....|....*....|....*....|
gi 528485865 100 KIDICNHNGSTPLVLAKRRG-VNKDAIRLL 128
Cdd:PHA03100 133 NVNIKNSDGENLLHLYLESNkIDLKILKLL 162
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 31-128 1.22e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 51.59  E-value: 1.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485865  31 LLETGCDPNIRDHRGRTGLHLAAAR--GNVDICRFLHKFGADLLATDYQGNTALHL---CGHVDT--IQFLVSNGLKIDI 103
Cdd:PHA03100  92 LLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLyleSNKIDLkiLKLLIDKGVDINA 171

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 528485865 104 CNH----------------NGSTPLVLAKRRgVNKDAIRLL 128
Cdd:PHA03100 172 KNRvnyllsygvpinikdvYGFTPLHYAVYN-NNPEFVKYL 211
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 31-114 1.65e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 51.41  E-value: 1.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485865  31 LLETGCDPNIRDHRGRTGL-------H------------------------LAAARGNVDICRFLHKFGADLLATDYQGN 79
Cdd:PLN03192 577 LLKHACNVHIRDANGNTALwnaisakHhkifrilyhfasisdphaagdllcTAAKRNDLTAMKELLKQGLNVDSEDHQGA 656

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 528485865  80 TALHLC---GHVDTIQFLVSNGLKIDICN-HNGSTPLVL 114
Cdd:PLN03192 657 TALQVAmaeDHVDMVRLLIMNGADVDKANtDDDFSPTEL 695
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 24-112 2.55e-07

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 50.68  E-value: 2.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485865  24 DLSFARRLLETGCDPNIRDHRGRTGLHLAAARGNV--DICRFLHKFGADLLATDYQGNTALH-----LCG---------- 86
Cdd:PHA02716 296 DISVVYSFLQPGVKLHYKDSAGRTCLHQYILRHNIstDIIKLLHEYGNDLNEPDNIGNTVLHtylsmLSVvnildpetdn 375

                         90       100
                 ....*....|....*....|....*...
gi 528485865  87 --HVDTIQFLVSNGLKIDICNHNGSTPL 112
Cdd:PHA02716 376 diRLDVIQCLISLGADITAVNCLGYTPL 403
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 15-128 2.99e-07

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: 50.46  E-value: 2.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485865   15 PLLQACIDGDLSFARRLLETGCDPNIR---------DHR-----GRTGLHLAAARGNVDICRFLHKFGADLLATDYQGNT 80
Cdd:TIGR00870 131 ALHLAAHRQNYEIVKLLLERGASVPARacgdffvksQGVdsfyhGESPLNAAACLGSPSIVALLSEDPADILTADSLGNT 210

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528485865   81 ALHLC-----GHVDTI-------QFLVSNGLKID-------ICNHNGSTPLVLAKRRGvNKDAIRLL 128
Cdd:TIGR00870 211 LLHLLvmeneFKAEYEelscqmyNFALSLLDKLRdskelevILNHQGLTPLKLAAKEG-RIVLFRLK 276
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 31-123 4.06e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 49.05  E-value: 4.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485865  31 LLETGCDPNIRDHRGRTGLH--LAAARGNVDICRFLHKFGADLLATDYQGNTALH--LCGHVD--TIQFLVSNGLKIDIC 104
Cdd:PHA02859 109 LIDSGSSITEEDEDGKNLLHmyMCNFNVRINVIKLLIDSGVSFLNKDFDNNNILYsyILFHSDkkIFDFLTSLGIDINET 188

                         90       100
                 ....*....|....*....|.
gi 528485865 105 NHNGSTPLVLAKRRGV--NKD 123
Cdd:PHA02859 189 NKSGYNCYDLIKFRNLffNKQ 209
PHA03095 PHA03095
ankyrin-like protein; Provisional
 31-82 8.17e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 48.87  E-value: 8.17e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 528485865  31 LLETGCDPNIRDHRGRTGLHLAAARGNVDICRFLHKFGADLLATDYQGNTAL 82
Cdd:PHA03095 243 LLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPL 294
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 30-103 1.97e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 47.74  E-value: 1.97e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528485865  30 RLLETGCDPNIRDHRGRTGLHLAAARGNVDICRFLHKFGADLLATDYQGNTALHLC---GHVDTIQFLVSNGLKIDI 103
Cdd:PHA03100 177 YLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAilnNNKEIFKLLLNNGPSIKT 253
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 1-137 3.38e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 47.37  E-value: 3.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485865   1 MSYVFINDSSQTSVPLLQACIDGDLSFARRLLETGCDPNIRDHRGRTGLHLAAARGNVDICRFLHKFGADLLATDYQGNT 80
Cdd:PHA02876 134 IHYDKINESIEYMKLIKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLS 213

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485865  81 ALHLC---GHVDTIQFLVSNglkidicnhngstplvlakRRGVNKDAIRLLEGLEEQEVK 137
Cdd:PHA02876 214 VLECAvdsKNIDTIKAIIDN-------------------RSNINKNDLSLLKAIRNEDLE 254
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 1-160 1.06e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 45.75  E-value: 1.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485865   1 MSYVFINDS--SQTSVPLLQACIDGDLSFARRLLETGCDPNIRDHRGRTGLHLAAARGNVDICRFLHKFGADLLATDYQG 78
Cdd:PHA02875  89 DLGKFADDVfyKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCG 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485865  79 NTALHLC---GHVDTIQFLVSNGLKIDICNHNGSTPLVLAKRRGVNKDAIRLLegleeqevkgFNRGAHSKLEAMQMAES 155
Cdd:PHA02875 169 CTPLIIAmakGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLF----------IKRGADCNIMFMIEGEE 238


                 ....*
gi 528485865 156 ESAME 160
Cdd:PHA02875 239 CTILD 243
Ank_2 pfam12796
Ankyrin repeats (3 copies);
82-142 1.41e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 42.41  E-value: 1.41e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528485865   82 LHLC---GHVDTIQFLVSNGLKIDICNHNGSTPLVLAKRRGvNKDAIRLLegLEEQEVKGFNRG 142
Cdd:pfam12796   1 LHLAaknGNLELVKLLLENGADANLQDKNGRTALHLAAKNG-HLEIVKLL--LEHADVNLKDNG 61
PHA03095 PHA03095
ankyrin-like protein; Provisional
 29-126 1.43e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 45.40  E-value: 1.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485865  29 RRLLETGCDPNIRDHRGRTGLHLAAARGNvdiCRFLHKF-----GADLLATDYQGNTALHLC-GHVDTIQF--LVSNGLK 100
Cdd:PHA03095 206 RELIRAGCDPAATDMLGNTPLHSMATGSS---CKRSLVLplliaGISINARNRYGQTPLHYAaVFNNPRACrrLIALGAD 282

                         90       100
                 ....*....|....*....|....*.
gi 528485865 101 IDICNHNGSTPLVLAKRRGvNKDAIR 126
Cdd:PHA03095 283 INAVSSDGNTPLSLMVRNN-NGRAVR 307
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 15-70 1.82e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 45.04  E-value: 1.82e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 528485865  15 PLLQACIDGDLSFARRLLETGCDPNIRDHRGRTGLHLAAARGNVDICRFLHKFGAD 70
Cdd:PHA03100 195 PLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 16-75 3.85e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 44.09  E-value: 3.85e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485865  16 LLQACIDGDLSFARRLLETGCDPNIRDHRGRTGLHLAAARGNVDICRFLHKFGADLLATD 75
Cdd:PLN03192 626 LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAN 685
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 6-128 5.22e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 43.72  E-value: 5.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485865   6 INDSSQTSVPLLQACIDGDLSFARRLLETGCDPNIRDHRGRTGLHLAAARGNVDICRFLHKFGADLLATDYQGNTALHL- 84
Cdd:PHA02878 162 MKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHIs 241

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 528485865  85 ---CGHVDTIQFLVSNGLKIDICNH-NGSTPLVLAKRrgvNKDAIRLL 128
Cdd:PHA02878 242 vgyCKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIK---SERKLKLL 286
Ank_4 pfam13637
Ankyrin repeats (many copies);
78-128 5.53e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.57  E-value: 5.53e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 528485865   78 GNTALHLC---GHVDTIQFLVSNGLKIDICNHNGSTPLVLAKRRGvNKDAIRLL 128
Cdd:pfam13637   1 ELTALHAAaasGHLELLRLLLEKGADINAVDGNGETALHFAASNG-NVEVLKLL 53
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 12-84 5.88e-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: 43.46  E-value: 5.88e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528485865  12 TSVPLLQACIDGDLSFARRLLET-GCDPNIRDHRGRTGLHLAAARGNVDICRFLHKFGADLL---ATD--YQGNTALHL 84
Cdd:cd22192   17 SESPLLLAAKENDVQAIKKLLKCpSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVnepMTSdlYQGETALHI 95
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 15-119 9.72e-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: 42.69  E-value: 9.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485865  15 PLLQACIDGDLSFARRLLETGCD------------PNIRD--HRGRTGLHLAAARGNVDICRFLHKFGADLLATDYQGNT 80
Cdd:cd22192   92 ALHIAVVNQNLNLVRELIARGADvvspratgtffrPGPKNliYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNT 171

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 528485865  81 ALHL----------CGHVDTIqfLVSNGLKIDIC-----NHNGSTPLVLAKRRG 119
Cdd:cd22192  172 VLHIlvlqpnktfaCQMYDLI--LSYDKEDDLQPldlvpNNQGLTPFKLAAKEG 223
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 31-115 1.37e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 42.34  E-value: 1.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485865  31 LLETGCDPNIRDHRGRTGLHLAAARGNVD--ICRFLHKFGAD----------------LLATDYQGNTALHLC---GHVD 89
Cdd:PHA03100 127 LLDNGANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKGVDinaknrvnyllsygvpINIKDVYGFTPLHYAvynNNPE 206

                         90       100
                 ....*....|....*....|....*.
gi 528485865  90 TIQFLVSNGLKIDICNHNGSTPLVLA 115
Cdd:PHA03100 207 FVKYLLDLGANPNLVNKYGDTPLHIA 232
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 6-118 1.93e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 41.97  E-value: 1.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485865   6 INDSSQTsvPLLQACIDGDLS-FARRLLETGCDPNIRDHRGRTGLHLAAARG-NVDICRFLHKFGADLLATDYQGNTALH 83
Cdd:PHA02876 269 IDDCKNT--PLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLH 346

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 528485865  84 ----LCGHVDTIQFLVSNGLKIDICNHNGSTPLVLAKRR 118
Cdd:PHA02876 347 qastLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVR 385
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 44-75 2.47e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 37.27  E-value: 2.47e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 528485865   44 RGRTGLHLAAAR-GNVDICRFLHKFGADLLATD 75
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
PHA03095 PHA03095
ankyrin-like protein; Provisional
 7-66 2.67e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 41.55  E-value: 2.67e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528485865   7 NDSSQTsvPLLQACIDGDLSFARRLLETGCDPNIRDHRGRTGLHLAAARGNVDICR-FLHK 66
Cdd:PHA03095 254 NRYGQT--PLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRaALAK 312
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 14-128 1.06e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 39.59  E-value: 1.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485865  14 VPLLQACIDGDLSFARRLLETGCDPNIRDHRGRTGLHLAAARGNVDICRFLHKFGAdllATDYQG---NTALHLC---GH 87
Cdd:PHA02875   4 VALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGA---IPDVKYpdiESELHDAveeGD 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 528485865  88 VDTIQFLVSNGLKI-DICNHNGSTPLVLAKRRGvNKDAIRLL 128
Cdd:PHA02875  81 VKAVEELLDLGKFAdDVFYKDGMTPLHLATILK-KLDIMKLL 121
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 44-73 1.30e-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: 1.30e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 528485865   44 RGRTGLHLAAARGNVDICRFLHKFGADLLA 73
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA03095 PHA03095
ankyrin-like protein; Provisional
 51-128 2.54e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 38.47  E-value: 2.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485865  51 LAAARGNVDICRFLHKFGADLLATDYQGNTALHLCGH------VDTIQFLVSNGLKIDICNHNGSTPLVLAKRRGVNKDA 124
Cdd:PHA03095  20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHLYLHyssekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDV 99


                 ....
gi 528485865 125 IRLL 128
Cdd:PHA03095 100 IKLL 103
PHA02946 PHA02946
ankyin-like protein; Provisional
 24-113 2.95e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 38.11  E-value: 2.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485865  24 DLSFARRLLETGCDPNIRDHRGRTGLHLAAARGNVDICRFLHKFGADLLATDYQGNTALHLCGHVDT-----IQFLVSNG 98
Cdd:PHA02946  51 DERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevierINLLVQYG 130

                         90
                 ....*....|....*.
gi 528485865  99 LKI-DICNHNGSTPLV 113
Cdd:PHA02946 131 AKInNSVDEEGCGPLL 146
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 77-106 3.08e-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: 34.19  E-value: 3.08e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 528485865   77 QGNTALHLC----GHVDTIQFLVSNGLKIDICNH 106
Cdd:pfam00023   1 DGNTPLHLAagrrGNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 44-71 3.24e-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: 3.24e-03
                           10        20
                   ....*....|....*....|....*...
gi 528485865    44 RGRTGLHLAAARGNVDICRFLHKFGADL 71
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
Ank_5 pfam13857
Ankyrin repeats (many copies);
15-52 3.70e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 34.63  E-value: 3.70e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 528485865   15 PLLQACIDGDLSFARRLLETGCDPNIRDHRGRTGLHLA 52
Cdd:pfam13857  19 PLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 24-119 3.74e-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: 37.94  E-value: 3.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528485865  24 DLSFARRLLETGCDPNIR------DHRGRTG-------LHLAAARGNVDICRFLHKFGAD---LLATDYQGNTALHLC-- 85
Cdd:cd21882   85 NLNLVRLLVENGADVSARatgrffRKSPGNLfyfgelpLSLAACTNQEEIVRLLLENGAQpaaLEAQDSLGNTVLHALvl 164

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 528485865  86 ---GHVDTIQF-------LVSNGLKID-------ICNHNGSTPLVLAKRRG 119
Cdd:cd21882  165 qadNTPENSAFvcqmynlLLSYGAHLDptqqleeIPNHQGLTPLKLAAVEG 215
 
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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