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Conserved domains on  [gi|1475928774|ref|NP_001352634|]
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NF-kappa-B inhibitor delta isoform 4 [Homo sapiens]

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];
32-303 5.87e-22

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 93.48  E-value: 5.87e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475928774  32 AHMLALGPQQLLAQDEEGDTLLHLFAARGLRwaAYAAAEVLQVYRRLDIREHKGKTPLLVAAAANQPLIVEDLLNLGAEP 111
Cdd:COG0666    36 LLLLLLLALLALALADALGALLLLAAALAGD--LLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADV 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475928774 112 NAADHQGRSVLHVAATYGLPGVLLAVLNSGvqVDLEARDFEGLTPLHTAIlalnvamrpsdlcprvlstqARDRLDCVHM 191
Cdd:COG0666   114 NARDKDGETPLHLAAYNGNLEIVKLLLEAG--ADVNAQDNDGNTPLHLAA--------------------ANGNLEIVKL 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475928774 192 LLQMGANHTSQEiKSNKTVLHLAVQAANPTLVQLLLElpRGDLRTFVNmkAHGNTALHMAAALppgpAQEAIVRHLLAAG 271
Cdd:COG0666   172 LLEAGADVNARD-NDGETPLHLAAENGHLEIVKLLLE--AGADVNAKD--NDGKTALDLAAEN----GNLEIVKLLLEAG 242

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1475928774 272 ADPTLRNLENEQPVHLLRPGPGPEGLRQLLKR 303
Cdd:COG0666   243 ADLNAKDKDGLTALLLAAAAGAALIVKLLLLA 274
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
32-303 5.87e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 93.48  E-value: 5.87e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475928774  32 AHMLALGPQQLLAQDEEGDTLLHLFAARGLRwaAYAAAEVLQVYRRLDIREHKGKTPLLVAAAANQPLIVEDLLNLGAEP 111
Cdd:COG0666    36 LLLLLLLALLALALADALGALLLLAAALAGD--LLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADV 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475928774 112 NAADHQGRSVLHVAATYGLPGVLLAVLNSGvqVDLEARDFEGLTPLHTAIlalnvamrpsdlcprvlstqARDRLDCVHM 191
Cdd:COG0666   114 NARDKDGETPLHLAAYNGNLEIVKLLLEAG--ADVNAQDNDGNTPLHLAA--------------------ANGNLEIVKL 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475928774 192 LLQMGANHTSQEiKSNKTVLHLAVQAANPTLVQLLLElpRGDLRTFVNmkAHGNTALHMAAALppgpAQEAIVRHLLAAG 271
Cdd:COG0666   172 LLEAGADVNARD-NDGETPLHLAAENGHLEIVKLLLE--AGADVNAKD--NDGKTALDLAAEN----GNLEIVKLLLEAG 242

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1475928774 272 ADPTLRNLENEQPVHLLRPGPGPEGLRQLLKR 303
Cdd:COG0666   243 ADLNAKDKDGLTALLLAAAAGAALIVKLLLLA 274
Ank_2 pfam12796
Ankyrin repeats (3 copies);
186-278 1.12e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 57.43  E-value: 1.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475928774 186 LDCVHMLLQMGANHTSQEiKSNKTVLHLAVQAANPTLVQLLLELPRgdlrtfVNMKAHGNTALHMAAALppgpAQEAIVR 265
Cdd:pfam12796  10 LELVKLLLENGADANLQD-KNGRTALHLAAKNGHLEIVKLLLEHAD------VNLKDNGRTALHYAARS----GHLEIVK 78

                          90
                  ....*....|...
gi 1475928774 266 HLLAAGADPTLRN 278
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 46-287 8.64e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 59.27  E-value: 8.64e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475928774  46 DEEGDTLLHLFAArglrwaaYAAAEVLQVYR-------RLDIREHKGKTPL-LVAAAANQPLIVEDLLNLGAEPNAADHQ 117
Cdd:PHA03095   44 GEYGKTPLHLYLH-------YSSEKVKDIVRllleagaDVNAPERCGFTPLhLYLYNATTLDVIKLLIKAGADVNAKDKV 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475928774 118 GRSVLHVAATyGL---PGVLLAVLNSGVqvDLEARDFEGLTPLHtailalnVAMRPSDLCPRVlstqardrldcVHMLLQ 194
Cdd:PHA03095  117 GRTPLHVYLS-GFninPKVIRLLLRKGA--DVNALDLYGMTPLA-------VLLKSRNANVEL-----------LRLLID 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475928774 195 MGANHTSQEIKSNKTVLHLAVQA-ANPTLVQLLLElpRGDLRTFVNMkaHGNTALHMAAALppGPAQEAIVRHLLAAGAD 273
Cdd:PHA03095  176 AGADVYAVDDRFRSLLHHHLQSFkPRARIVRELIR--AGCDPAATDM--LGNTPLHSMATG--SSCKRSLVLPLLIAGIS 249

                         250
                  ....*....|....
gi 1475928774 274 PTLRNLENEQPVHL 287
Cdd:PHA03095  250 INARNRYGQTPLHY 263
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 87-253 1.35e-06

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: 49.63  E-value: 1.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475928774  87 TPLLVAAAANQPLIVEDLL-NLGAEPNAADHQGRSVLHVAATYGLPGVLLAVLNSG---VQVDLEARDFEGLTPLHTAIL 162
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAApelVNEPMTSDLYQGETALHIAVV 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475928774 163 ALNVAM------RPSD-LCPRVLSTQARDRLDC--------------------VHMLLQMGANHTSQEIKSNkTVLHLAV 215
Cdd:cd22192    99 NQNLNLvreliaRGADvVSPRATGTFFRPGPKNliyygehplsfaacvgneeiVRLLIEHGADIRAQDSLGN-TVLHILV 177

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1475928774 216 QAANPTLVQLLLEL-----PRGDLRTFVNMKAH-GNTALHMAAA 253
Cdd:cd22192   178 LQPNKTFACQMYDLilsydKEDDLQPLDLVPNNqGLTPFKLAAK 221
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 85-303 1.86e-04

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 43.15  E-value: 1.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475928774  85 GKTPLLVAAAANQPL-IVEDLLNLGAEPNAadhqGRSVLHVAATyGLPGVLLAVLNSGVQVDLEA------------RDF 151
Cdd:TIGR00870  52 GRSALFVAAIENENLeLTELLLNLSCRGAV----GDTLLHAISL-EYVDAVEAILLHLLAAFRKSgplelandqytsEFT 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475928774 152 EGLTPLHTAILalnvamrpsdlcprvlstqaRDRLDCVHMLLQMGAN----------HTSQEIKS---NKTVLHLAVQAA 218
Cdd:TIGR00870 127 PGITALHLAAH--------------------RQNYEIVKLLLERGASvparacgdffVKSQGVDSfyhGESPLNAAACLG 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475928774 219 NPTLVQLLLELPRGDLRTFvnmkAHGNTALHMAAALPPGPA---------QEAIVRHLlaAGADPTL-----RNLENEQP 284
Cdd:TIGR00870 187 SPSIVALLSEDPADILTAD----SLGNTLLHLLVMENEFKAeyeelscqmYNFALSLL--DKLRDSKeleviLNHQGLTP 260

                         250
                  ....*....|....*....
gi 1475928774 285 VHLLRPGPGPEGLRQLLKR 303
Cdd:TIGR00870 261 LKLAAKEGRIVLFRLKLAI 279
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
32-303 5.87e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 93.48  E-value: 5.87e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475928774  32 AHMLALGPQQLLAQDEEGDTLLHLFAARGLRwaAYAAAEVLQVYRRLDIREHKGKTPLLVAAAANQPLIVEDLLNLGAEP 111
Cdd:COG0666    36 LLLLLLLALLALALADALGALLLLAAALAGD--LLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADV 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475928774 112 NAADHQGRSVLHVAATYGLPGVLLAVLNSGvqVDLEARDFEGLTPLHTAIlalnvamrpsdlcprvlstqARDRLDCVHM 191
Cdd:COG0666   114 NARDKDGETPLHLAAYNGNLEIVKLLLEAG--ADVNAQDNDGNTPLHLAA--------------------ANGNLEIVKL 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475928774 192 LLQMGANHTSQEiKSNKTVLHLAVQAANPTLVQLLLElpRGDLRTFVNmkAHGNTALHMAAALppgpAQEAIVRHLLAAG 271
Cdd:COG0666   172 LLEAGADVNARD-NDGETPLHLAAENGHLEIVKLLLE--AGADVNAKD--NDGKTALDLAAEN----GNLEIVKLLLEAG 242

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1475928774 272 ADPTLRNLENEQPVHLLRPGPGPEGLRQLLKR 303
Cdd:COG0666   243 ADLNAKDKDGLTALLLAAAAGAALIVKLLLLA 274
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
27-282 6.24e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 79.23  E-value: 6.24e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475928774  27 LEVARAHMLALGPQQLLAQDEEGDTLLHLFAARG----LRWAAYAAAEVlqvyrrlDIREHKGKTPLLVAAAANQPLIVE 102
Cdd:COG0666    65 GDLLVALLLLAAGADINAKDDGGNTLLHAAARNGdleiVKLLLEAGADV-------NARDKDGETPLHLAAYNGNLEIVK 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475928774 103 DLLNLGAEPNAADHQGRSVLHVAATYGLPGVLLAVLNSGvqVDLEARDFEGLTPLHTAIlalnvamrpsdlcprvlstqA 182
Cdd:COG0666   138 LLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAG--ADVNARDNDGETPLHLAA--------------------E 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475928774 183 RDRLDCVHMLLQMGANHTSQEiKSNKTVLHLAVQAANPTLVQLLLELPRGDLrtfvNMKAHGNTALHMAAALppgpAQEA 262
Cdd:COG0666   196 NGHLEIVKLLLEAGADVNAKD-NDGKTALDLAAENGNLEIVKLLLEAGADLN----AKDKDGLTALLLAAAA----GAAL 266

                         250       260
                  ....*....|....*....|
gi 1475928774 263 IVRHLLAAGADPTLRNLENE 282
Cdd:COG0666   267 IVKLLLLALLLLAAALLDLL 286
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
87-303 1.84e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 63.43  E-value: 1.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475928774  87 TPLLVAAAANQPLIVEDLLNLGAEPNAADHQGRSVLHVAATYGLPGVLLAVLNSGVqvDLEARDFEGLTPLHTAILALNV 166
Cdd:COG0666    23 LLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGA--DINAKDDGGNTLLHAAARNGDL 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475928774 167 AM-------------RPSDLCPRVLSTQARDRLDCVHMLLQMGANHTSQEiKSNKTVLHLAVQAANPTLVQLLLELPrgd 233
Cdd:COG0666   101 EIvkllleagadvnaRDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQD-NDGNTPLHLAAANGNLEIVKLLLEAG--- 176

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1475928774 234 lrTFVNMK-AHGNTALHMAAALppgpAQEAIVRHLLAAGADPTLRNLENEQPVHLLRPGPGPEGLRQLLKR 303
Cdd:COG0666   177 --ADVNARdNDGETPLHLAAEN----GHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241
Ank_2 pfam12796
Ankyrin repeats (3 copies);
186-278 1.12e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 57.43  E-value: 1.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475928774 186 LDCVHMLLQMGANHTSQEiKSNKTVLHLAVQAANPTLVQLLLELPRgdlrtfVNMKAHGNTALHMAAALppgpAQEAIVR 265
Cdd:pfam12796  10 LELVKLLLENGADANLQD-KNGRTALHLAAKNGHLEIVKLLLEHAD------VNLKDNGRTALHYAARS----GHLEIVK 78

                          90
                  ....*....|...
gi 1475928774 266 HLLAAGADPTLRN 278
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 46-287 8.64e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 59.27  E-value: 8.64e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475928774  46 DEEGDTLLHLFAArglrwaaYAAAEVLQVYR-------RLDIREHKGKTPL-LVAAAANQPLIVEDLLNLGAEPNAADHQ 117
Cdd:PHA03095   44 GEYGKTPLHLYLH-------YSSEKVKDIVRllleagaDVNAPERCGFTPLhLYLYNATTLDVIKLLIKAGADVNAKDKV 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475928774 118 GRSVLHVAATyGL---PGVLLAVLNSGVqvDLEARDFEGLTPLHtailalnVAMRPSDLCPRVlstqardrldcVHMLLQ 194
Cdd:PHA03095  117 GRTPLHVYLS-GFninPKVIRLLLRKGA--DVNALDLYGMTPLA-------VLLKSRNANVEL-----------LRLLID 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475928774 195 MGANHTSQEIKSNKTVLHLAVQA-ANPTLVQLLLElpRGDLRTFVNMkaHGNTALHMAAALppGPAQEAIVRHLLAAGAD 273
Cdd:PHA03095  176 AGADVYAVDDRFRSLLHHHLQSFkPRARIVRELIR--AGCDPAATDM--LGNTPLHSMATG--SSCKRSLVLPLLIAGIS 249

                         250
                  ....*....|....
gi 1475928774 274 PTLRNLENEQPVHL 287
Cdd:PHA03095  250 INARNRYGQTPLHY 263
Ank_2 pfam12796
Ankyrin repeats (3 copies);
89-202 3.61e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 53.20  E-value: 3.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475928774  89 LLVAAAANQPLIVEDLLNLGAEPNAADHQGRSVLHVAATYGLPGVLLAVLNsgvQVDLEARDfEGLTPLHTAILAlnvam 168
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE---HADVNLKD-NGRTALHYAARS----- 71

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1475928774 169 rpsdlcprvlstqarDRLDCVHMLLQMGANHTSQ 202
Cdd:pfam12796  72 ---------------GHLEIVKLLLEKGADINVK 90
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 82-228 4.28e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 54.12  E-value: 4.28e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475928774  82 EHKGKTPLLVAAAANQPLIVEDLLNLGAEPNAADHQGRSVLHVAATYGLPGVLLAVLNSGVQVDleARDFEGLTPLHTAI 161
Cdd:PHA02878  165 RHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTD--ARDKCGNTPLHISV 242

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1475928774 162 lalnvamrpsdlcPRVLStqardrLDCVHMLLQMGANHTSQEIKSNKTVLHLAVQaaNPTLVQLLLE 228
Cdd:PHA02878  243 -------------GYCKD------YDILKLLLEHGVDVNAKSYILGLTALHSSIK--SERKLKLLLE 288
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 84-285 5.54e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 53.91  E-value: 5.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475928774  84 KGKTPL-LVAAAANQPLIVEDLLNLGAEPNAADHQGRSVLHVAATYG-LPGVLLAVLNSGVQVDleARDFEGLTPLHTAI 161
Cdd:PHA02876  306 KGETPLyLMAKNGYDTENIRTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGANVN--ARDYCDKTPIHYAA 383

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475928774 162 LALNVAMrpsdlcprvlstqardrldcVHMLLQMGAN--HTSQEIksnKTVLHLAVQAANP-TLVQLLLElpRGdlrTFV 238
Cdd:PHA02876  384 VRNNVVI--------------------INTLLDYGADieALSQKI---GTALHFALCGTNPyMSVKTLID--RG---ANV 435

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1475928774 239 NMK-AHGNTALHMAAALPPGPaqeAIVRHLLAAGADPTLRNLENEQPV 285
Cdd:PHA02876  436 NSKnKDLSTPLHYACKKNCKL---DVIEMLLDNGADVNAINIQNQYPL 480
PHA03095 PHA03095
ankyrin-like protein; Provisional
 100-288 1.11e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 52.72  E-value: 1.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475928774 100 IVEDLLNLGAEPNAADHQGRSVLHVAATYGLP---GVLLAVLNSGVQVDleARDFEGLTPLHTAILALNVamrpsdlcpr 176
Cdd:PHA03095   29 EVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEkvkDIVRLLLEAGADVN--APERCGFTPLHLYLYNATT---------- 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475928774 177 vlstqardrLDCVHMLLQMGANhTSQEIKSNKTVLH--LAVQAANPTLVQLLLEL---------------------PRGD 233
Cdd:PHA03095   97 ---------LDVIKLLIKAGAD-VNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKgadvnaldlygmtplavllksRNAN 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1475928774 234 LRTfVNM-----------KAHGNTALHMAAALPPgpAQEAIVRHLLAAGADPTLRNLENEQPVHLL 288
Cdd:PHA03095  167 VEL-LRLlidagadvyavDDRFRSLLHHHLQSFK--PRARIVRELIRAGCDPAATDMLGNTPLHSM 229
PHA03095 PHA03095
ankyrin-like protein; Provisional
 85-285 2.21e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 51.95  E-value: 2.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475928774  85 GKTPLLVAAA--ANQPLIVEDLLNLGAEPNAADHQGRSVLHV-----AATYGLPGVLLAVLNsgvqvDLEARDFEGLTPL 157
Cdd:PHA03095  117 GRTPLHVYLSgfNINPKVIRLLLRKGADVNALDLYGMTPLAVllksrNANVELLRLLIDAGA-----DVYAVDDRFRSLL 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475928774 158 HtaILALNVamrpsdlcprvlstqaRDRLDCVHMLLQMGANHTSQEIKSNkTVLHLAV---QAANPTLVQLLLELPRGDL 234
Cdd:PHA03095  192 H--HHLQSF----------------KPRARIVRELIRAGCDPAATDMLGN-TPLHSMAtgsSCKRSLVLPLLIAGISINA 252

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1475928774 235 RtfvnmKAHGNTALHMAAALPPGPAqeaiVRHLLAAGADPTLRNLENEQPV 285
Cdd:PHA03095  253 R-----NRYGQTPLHYAAVFNNPRA----CRRLIALGADINAVSSDGNTPL 294
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 87-253 1.35e-06

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: 49.63  E-value: 1.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475928774  87 TPLLVAAAANQPLIVEDLL-NLGAEPNAADHQGRSVLHVAATYGLPGVLLAVLNSG---VQVDLEARDFEGLTPLHTAIL 162
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAApelVNEPMTSDLYQGETALHIAVV 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475928774 163 ALNVAM------RPSD-LCPRVLSTQARDRLDC--------------------VHMLLQMGANHTSQEIKSNkTVLHLAV 215
Cdd:cd22192    99 NQNLNLvreliaRGADvVSPRATGTFFRPGPKNliyygehplsfaacvgneeiVRLLIEHGADIRAQDSLGN-TVLHILV 177

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1475928774 216 QAANPTLVQLLLEL-----PRGDLRTFVNMKAH-GNTALHMAAA 253
Cdd:cd22192   178 LQPNKTFACQMYDLilsydKEDDLQPLDLVPNNqGLTPFKLAAK 221
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 87-287 1.49e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 49.28  E-value: 1.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475928774  87 TPLLVAAAANQPLIVEDLLNLGAEPN--AADHQGRSVLHVAATYGLPGVLLAV---LNSGVQVDleARDFEGLTPLHTAI 161
Cdd:PHA03100   37 LPLYLAKEARNIDVVKILLDNGADINssTKNNSTPLHYLSNIKYNLTDVKEIVkllLEYGANVN--APDNNGITPLLYAI 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475928774 162 lalnvamrpsdlcprvlsTQARDRLDCVHMLLQMGANHTSQEiKSNKTVLHLAVQAANPTL--VQLLLElpRG---DLRT 236
Cdd:PHA03100  115 ------------------SKKSNSYSIVEYLLDNGANVNIKN-SDGENLLHLYLESNKIDLkiLKLLID--KGvdiNAKN 173

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1475928774 237 FVNM-----------KAHGNTALHMAAALPpgpaQEAIVRHLLAAGADPTLRNLENEQPVHL 287
Cdd:PHA03100  174 RVNYllsygvpinikDVYGFTPLHYAVYNN----NPEFVKYLLDLGANPNLVNKYGDTPLHI 231
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 89-227 1.52e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 49.48  E-value: 1.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475928774  89 LLVAAAANQPLIvEDLLNLGAEPNAADHQGRSVLHVAATYGLPGVLLAVLNSGVQVDLeaRDFEGLTPLHTAILA----- 163
Cdd:PLN03192  530 LTVASTGNAALL-EELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHI--RDANGNTALWNAISAkhhki 606

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1475928774 164 ---LNVAMRPSDlcPR----VLSTQA-RDRLDCVHMLLQMGANHTSQEiKSNKTVLHLAVQAANPTLVQLLL 227
Cdd:PLN03192  607 friLYHFASISD--PHaagdLLCTAAkRNDLTAMKELLKQGLNVDSED-HQGATALQVAMAEDHVDMVRLLI 675
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 99-303 2.75e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 48.91  E-value: 2.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475928774  99 LIVEDLLNLGAEPNAADHQGRSVLHVAATYGLPGVLLAVLNSGVQVDLEARDfeGLTPLHTAILALNVamrpsdlcprvl 178
Cdd:PHA02876  159 LIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALD--DLSVLECAVDSKNI------------ 224

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475928774 179 stqardrlDCVHMLLQMGANhtsqeikSNKTVLHLAVQAANPTLVQLLLELPRGdlRTFVNMKAHGNTALHMAAAlppGP 258
Cdd:PHA02876  225 --------DTIKAIIDNRSN-------INKNDLSLLKAIRNEDLETSLLLYDAG--FSVNSIDDCKNTPLHHASQ---AP 284

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1475928774 259 AQEAIVRHLLAAGADPTLRNLENEQPVHLL-RPGPGPEGLRQLLKR 303
Cdd:PHA02876  285 SLSRLVPKLLERGADVNAKNIKGETPLYLMaKNGYDTENIRTLIML 330
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 100-285 3.36e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 48.34  E-value: 3.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475928774 100 IVEDLLNLGAEPNAAD-HQGRSVLHVAATYGLPGVLLAVLNSGVQVDLEarDFEGLTPLHTAIlalnvamrpsdlcprvl 178
Cdd:PHA02878  149 ITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIP--DKTNNSPLHHAV----------------- 209

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475928774 179 stqARDRLDCVHMLLQMGANhTSQEIKSNKTVLHLAV-QAANPTLVQLLLElpRGdlrTFVNMKAH--GNTALHMAAAlp 255
Cdd:PHA02878  210 ---KHYNKPIVHILLENGAS-TDARDKCGNTPLHISVgYCKDYDILKLLLE--HG---VDVNAKSYilGLTALHSSIK-- 278

                         170       180       190
                  ....*....|....*....|....*....|
gi 1475928774 256 pgpaQEAIVRHLLAAGADPTLRNLENEQPV 285
Cdd:PHA02878  279 ----SERKLKLLLEYGADINSLNSYKLTPL 304
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 78-162 6.62e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 47.27  E-value: 6.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475928774  78 LDIREHKGKTPLLVAAAANQPLIVEDLLNLGAEPNAADHQGRSVLHVAATYGLPGVLLAVLNSGVQVDLEARDfeGLTPL 157
Cdd:PHA02874  150 VNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKN--GFTPL 227


                  ....*
gi 1475928774 158 HTAIL 162
Cdd:PHA02874  228 HNAII 232
Ank_2 pfam12796
Ankyrin repeats (3 copies);
45-115 2.51e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 42.03  E-value: 2.51e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1475928774  45 QDEEGDTLLHLFAARGlrwaAYAAAEVLQVYRRLDIREHkGKTPLLVAAAANQPLIVEDLLNLGAEPNAAD 115
Cdd:pfam12796  26 QDKNGRTALHLAAKNG----HLEIVKLLLEHADVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 125-287 5.38e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 44.60  E-value: 5.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475928774 125 AATYGLPGVLLAVLNSGVQVDLEARDfeGLTPLHTAILALNVAMrpsdlcprvlstqardrldcVHMLLQMGA--NHTSQ 202
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNFEIYD--GISPIKLAMKFRDSEA--------------------IKLLMKHGAipDVKYP 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475928774 203 EIKSNktvLHLAVQAANPTLVQLLLelprgDLRTFVN--MKAHGNTALHMAAALppgpAQEAIVRHLLAAGADPTLRNLE 280
Cdd:PHA02875   67 DIESE---LHDAVEEGDVKAVEELL-----DLGKFADdvFYKDGMTPLHLATIL----KKLDIMKLLIARGADPDIPNTD 134


                  ....*..
gi 1475928774 281 NEQPVHL 287
Cdd:PHA02875  135 KFSPLHL 141
PHA03095 PHA03095
ankyrin-like protein; Provisional
 44-162 7.26e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 44.25  E-value: 7.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475928774  44 AQDEEGDTLLHLFAARGLRWAAYaaaeVLQVYRR---LDIREHKGKTPLLVAAAANQPLIVEDLLNLGAEPNAADHQGRS 120
Cdd:PHA03095  217 ATDMLGNTPLHSMATGSSCKRSL----VLPLLIAgisINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNT 292

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1475928774 121 VLHVAATYGLPGVLLAVLNSGVQVDLEARDFEGLTPLHTAIL 162
Cdd:PHA03095  293 PLSLMVRNNNGRAVRAALAKNPSAETVAATLNTASVAGGDIP 334
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 85-303 1.86e-04

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 43.15  E-value: 1.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475928774  85 GKTPLLVAAAANQPL-IVEDLLNLGAEPNAadhqGRSVLHVAATyGLPGVLLAVLNSGVQVDLEA------------RDF 151
Cdd:TIGR00870  52 GRSALFVAAIENENLeLTELLLNLSCRGAV----GDTLLHAISL-EYVDAVEAILLHLLAAFRKSgplelandqytsEFT 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475928774 152 EGLTPLHTAILalnvamrpsdlcprvlstqaRDRLDCVHMLLQMGAN----------HTSQEIKS---NKTVLHLAVQAA 218
Cdd:TIGR00870 127 PGITALHLAAH--------------------RQNYEIVKLLLERGASvparacgdffVKSQGVDSfyhGESPLNAAACLG 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475928774 219 NPTLVQLLLELPRGDLRTFvnmkAHGNTALHMAAALPPGPA---------QEAIVRHLlaAGADPTL-----RNLENEQP 284
Cdd:TIGR00870 187 SPSIVALLSEDPADILTAD----SLGNTLLHLLVMENEFKAeyeelscqmYNFALSLL--DKLRDSKeleviLNHQGLTP 260

                         250
                  ....*....|....*....
gi 1475928774 285 VHLLRPGPGPEGLRQLLKR 303
Cdd:TIGR00870 261 LKLAAKEGRIVLFRLKLAI 279
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 78-141 2.96e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 41.96  E-value: 2.96e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1475928774  78 LDIREHKGKTPLLVAAAANQPLIVEDLLNLGAEPNAADHQGRSVLHVAATYGLPGVLLAVLNSG 141
Cdd:PHA03100  185 INIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNG 248
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 93-160 3.08e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 42.19  E-value: 3.08e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1475928774  93 AAANQPLIVEDLLNLGAEPNAADHQGRSVLHVAATYGLPGVLLAVLNSGvqVDLEARDFEGLTPLHTA 160
Cdd:PTZ00322   90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFG--ADPTLLDKDGKTPLELA 155
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 79-263 4.71e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 41.52  E-value: 4.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475928774  79 DIREHKGKTPLLVAAAANQPLIVEDLLNLGAEPNAADHQGRSVLHVAATYGLPGVLLAVLNSGVQVDLEarDFEGLTPLH 158
Cdd:PHA02875   96 DVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIE--DCCGCTPLI 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475928774 159 TAILALNVAmrpsdLCprvlstqardrldcvHMLLQMGANHTSQEIKSNKTVLHLAVQAANPTLVQLLLElpRG-DLRTF 237
Cdd:PHA02875  174 IAMAKGDIA-----IC---------------KMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLFIK--RGaDCNIM 231

                         170       180
                  ....*....|....*....|....*.
gi 1475928774 238 VNMKAHGNTALHMAAALPPGPAQEAI 263
Cdd:PHA02875  232 FMIEGEECTILDMICNMCTNLESEAI 257
Ank_5 pfam13857
Ankyrin repeats (many copies);
104-160 5.20e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.33  E-value: 5.20e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1475928774 104 LLNLG-AEPNAADHQGRSVLHVAATYGLPGVLLAVLNSGvqVDLEARDFEGLTPLHTA 160
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYG--VDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
87-129 8.04e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.87  E-value: 8.04e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1475928774  87 TPLLVAAAANQPLIVEDLLNLGAEPNAADHQGRSVLHVAATYG 129
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNG 45
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 243-278 1.29e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 35.73  E-value: 1.29e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1475928774 243 HGNTALHMAAALppgPAQEAIVRHLLAAGADPTLRN 278
Cdd:pfam00023   1 DGNTPLHLAAGR---RGNLEIVKLLLSKGADVNARD 33
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 71-211 1.37e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 40.43  E-value: 1.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475928774  71 VLQVYRRLDIREHKGKTPLLVAAAANQPLIVEDLLNLGAEPNAADHQGRSVLHVAATYGLPGVLLAVL-NSGVQVDLEAR 149
Cdd:PHA02876  361 LLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMSVKTLiDRGANVNSKNK 440

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1475928774 150 DFEglTPLHTAilalnvamrpsdlcprvlsTQARDRLDCVHMLLQMGANHTSQEIKSNKTVL 211
Cdd:PHA02876  441 DLS--TPLHYA-------------------CKKNCKLDVIEMLLDNGADVNAINIQNQYPLL 481
Ank_2 pfam12796
Ankyrin repeats (3 copies);
79-146 1.43e-03

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 37.40  E-value: 1.43e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1475928774  79 DIREHKGKTPLLVAAAANQPLIVEDLLNlGAEPNAADHqGRSVLHVAATYGLPGVLLAVLNSGVQVDL 146
Cdd:pfam12796  24 NLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINV 89
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 68-274 1.91e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 39.59  E-value: 1.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475928774  68 AAEVLQVYRRLDIREHKGKTPLLVAAAANQPLIVEDLLNLGAEPNAADHQGRSVLHVAATYGLPGVLLAVLNSGVQVDlE 147
Cdd:PHA02875   18 ARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFAD-D 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475928774 148 ARDFEGLTPLHTAILALNVAMrpsdlcprvlstqardrldcVHMLLQMGANhTSQEIKSNKTVLHLAVQAANPTLVQLLL 227
Cdd:PHA02875   97 VFYKDGMTPLHLATILKKLDI--------------------MKLLIARGAD-PDIPNTDKFSPLHLAVMMGDIKGIELLI 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1475928774 228 elprgDLRTFVNMK-AHGNTALHMAAALppgpAQEAIVRHLLAAGADP 274
Cdd:PHA02875  156 -----DHKACLDIEdCCGCTPLIIAMAK----GDIAICKMLLDSGANI 194
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 83-227 1.93e-03

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: 39.61  E-value: 1.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475928774  83 HKGKTPLLVAAAANQPLIVEDLLNLGAEPNAAD--------------HQGRSVLHVAATYGLPGVLLAVLNSGvqVDLEA 148
Cdd:cd22192    87 YQGETALHIAVVNQNLNLVRELIARGADVVSPRatgtffrpgpknliYYGEHPLSFAACVGNEEIVRLLIEHG--ADIRA 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475928774 149 RDFEGLTPLHtaILAL----NVAMRPSDLcprVLSTQARDRLDCVHMLL-QMGAnhtsqeiksnkTVLHLAVQAANPTLV 223
Cdd:cd22192   165 QDSLGNTVLH--ILVLqpnkTFACQMYDL---ILSYDKEDDLQPLDLVPnNQGL-----------TPFKLAAKEGNIVMF 228


                  ....
gi 1475928774 224 QLLL 227
Cdd:cd22192   229 QHLV 232
PHA02743 PHA02743
Viral ankyrin protein; Provisional
 189-251 4.46e-03

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 37.10  E-value: 4.46e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1475928774 189 VHMLLQMGANHTSQEIKSNKTVLHLAVQAANPTLVQLLLELPRGDLRTfVNMKAHgnTALHMA 251
Cdd:PHA02743   76 IELLVNMGADINARELGTGNTLLHIAASTKNYELAEWLCRQLGVNLGA-INYQHE--TAYHIA 135
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 85-160 5.12e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 38.59  E-value: 5.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475928774  85 GKTPLLVAAAANQPLIVEDLLNLGAEPNAA-DHQGRSVLHVAATyglpgvllAVLNSGVQVD-----------------L 146
Cdd:cd22194   188 GETPLALAACTNQPEIVQLLMEKESTDITSqDSRGNTVLHALVT--------VAEDSKTQNDfvkrmydmillksenknL 259

                          90
                  ....*....|....*
gi 1475928774 147 EA-RDFEGLTPLHTA 160
Cdd:cd22194   260 ETiRNNEGLTPLQLA 274
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 46-198 6.88e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 38.31  E-value: 6.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475928774  46 DEEGDTLLHLFAARGLRWAAYAaaeVLQVYRRLDIREHKGKTPLLVAAAANQPLIVEDLLNLGAEPNAadHQGRSVLHVA 125
Cdd:PLN03192  555 DSKGRTPLHIAASKGYEDCVLV---LLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDP--HAAGDLLCTA 629

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1475928774 126 ATYGLPGVLLAVLNSGVQVDLEARDfeGLTplhtailALNVAMrpsdlcprvlstqARDRLDCVHMLLQMGAN 198
Cdd:PLN03192  630 AKRNDLTAMKELLKQGLNVDSEDHQ--GAT-------ALQVAM-------------AEDHVDMVRLLIMNGAD 680
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 209-273 7.04e-03

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: 38.07  E-value: 7.04e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475928774 209 TVLHLAVQAANPTLVQLLLElprgDLRTFVNMKA-----HGNTALHMAAAlppgPAQEAIVRHLLAAGAD 273
Cdd:cd22192    53 TALHVAALYDNLEAAVVLME----AAPELVNEPMtsdlyQGETALHIAVV----NQNLNLVRELIARGAD 114
 
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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