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Conserved domains on  [gi|2565334754|ref|NP_640332|]
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NF-kappa-B inhibitor delta isoform 1 [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];
174-453 1.65e-28

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 113.90  E-value: 1.65e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2565334754 174 AHMLALGPQQLLAQDEEGDTLLHLFAARGLrwAAYAAAEVLQVYRRLDIREHKGKTPLLVAAAANQPLIVEDLLNLGAEP 253
Cdd:COG0666    36 LLLLLLLALLALALADALGALLLLAAALAG--DLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADV 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2565334754 254 NAADHQGRSVLHVAATYGLPGVLLAVLNSGvqVDLEARDFEGLTPLHTAIlalnvamrpsdlcprvlstqARDRLDCVHM 333
Cdd:COG0666   114 NARDKDGETPLHLAAYNGNLEIVKLLLEAG--ADVNAQDNDGNTPLHLAA--------------------ANGNLEIVKL 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2565334754 334 LLQMGANHTSQEiKSNKTVLHLAVQAANPTLVQLLLElpRGDLRTFVNmkAHGNTALHMAAALppgpAQEAIVRHLLAAG 413
Cdd:COG0666   172 LLEAGADVNARD-NDGETPLHLAAENGHLEIVKLLLE--AGADVNAKD--NDGKTALDLAAEN----GNLEIVKLLLEAG 242

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 2565334754 414 ADPTLRNLENEQPVHLLRPGPGPEGLRQLLKRSRVAPPGL 453
Cdd:COG0666   243 ADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 9-168 3.71e-04

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.39  E-value: 3.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2565334754    9 PGGPQSTPRNPRVSRGERSHCPTQTVKKLLEEQRRRQQQQPDAGGVQGQFL--PPPEQPLTPSVNEAVTGHPPFPAHSET 86
Cdd:PHA03247  2649 PERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLAdpPPPPPTPEPAPHALVSATPLPPGPAAA 2728

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2565334754   87 VGSGPSSLGFPDWDPNTHAAYTDSPYSCPASAAENFLPPDFYPPSDPGQP----CPFPQGMEAGPWRVSAP-PSGPPQFP 161
Cdd:PHA03247  2729 RQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGpprrLTRPAVASLSESRESLPsPWDPADPP 2808


                   ....*..
gi 2565334754  162 AVVPGPS 168
Cdd:PHA03247  2809 AAVLAPA 2815
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
174-453 1.65e-28

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 113.90  E-value: 1.65e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2565334754 174 AHMLALGPQQLLAQDEEGDTLLHLFAARGLrwAAYAAAEVLQVYRRLDIREHKGKTPLLVAAAANQPLIVEDLLNLGAEP 253
Cdd:COG0666    36 LLLLLLLALLALALADALGALLLLAAALAG--DLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADV 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2565334754 254 NAADHQGRSVLHVAATYGLPGVLLAVLNSGvqVDLEARDFEGLTPLHTAIlalnvamrpsdlcprvlstqARDRLDCVHM 333
Cdd:COG0666   114 NARDKDGETPLHLAAYNGNLEIVKLLLEAG--ADVNAQDNDGNTPLHLAA--------------------ANGNLEIVKL 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2565334754 334 LLQMGANHTSQEiKSNKTVLHLAVQAANPTLVQLLLElpRGDLRTFVNmkAHGNTALHMAAALppgpAQEAIVRHLLAAG 413
Cdd:COG0666   172 LLEAGADVNARD-NDGETPLHLAAENGHLEIVKLLLE--AGADVNAKD--NDGKTALDLAAEN----GNLEIVKLLLEAG 242

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 2565334754 414 ADPTLRNLENEQPVHLLRPGPGPEGLRQLLKRSRVAPPGL 453
Cdd:COG0666   243 ADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
Ank_2 pfam12796
Ankyrin repeats (3 copies);
328-420 3.10e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 62.44  E-value: 3.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2565334754 328 LDCVHMLLQMGANHTSQEiKSNKTVLHLAVQAANPTLVQLLLELPRgdlrtfVNMKAHGNTALHMAAALppgpAQEAIVR 407
Cdd:pfam12796  10 LELVKLLLENGADANLQD-KNGRTALHLAAKNGHLEIVKLLLEHAD------VNLKDNGRTALHYAARS----GHLEIVK 78

                          90
                  ....*....|...
gi 2565334754 408 HLLAAGADPTLRN 420
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 188-429 1.11e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 63.51  E-value: 1.11e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2565334754 188 DEEGDTLLHLFaargLRwaaYAAAEVLQVYR-------RLDIREHKGKTPL-LVAAAANQPLIVEDLLNLGAEPNAADHQ 259
Cdd:PHA03095   44 GEYGKTPLHLY----LH---YSSEKVKDIVRllleagaDVNAPERCGFTPLhLYLYNATTLDVIKLLIKAGADVNAKDKV 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2565334754 260 GRSVLHVAATyGL---PGVLLAVLNSGVqvDLEARDFEGLTPLHtailalnVAMRPSDLCPRVlstqardrldcVHMLLQ 336
Cdd:PHA03095  117 GRTPLHVYLS-GFninPKVIRLLLRKGA--DVNALDLYGMTPLA-------VLLKSRNANVEL-----------LRLLID 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2565334754 337 MGANHTSQEIKSNKTVLHLAVQA-ANPTLVQLLLElpRGDLRTFVNMkaHGNTALHMAAALppGPAQEAIVRHLLAAGAD 415
Cdd:PHA03095  176 AGADVYAVDDRFRSLLHHHLQSFkPRARIVRELIR--AGCDPAATDM--LGNTPLHSMATG--SSCKRSLVLPLLIAGIS 249

                         250
                  ....*....|....
gi 2565334754 416 PTLRNLENEQPVHL 429
Cdd:PHA03095  250 INARNRYGQTPLHY 263
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 229-395 1.62e-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: 50.40  E-value: 1.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2565334754 229 TPLLVAAAANQPLIVEDLL-NLGAEPNAADHQGRSVLHVAATYGLPGVLLAVLNSG---VQVDLEARDFEGLTPLHTAIL 304
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAApelVNEPMTSDLYQGETALHIAVV 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2565334754 305 ALNVAM------RPSD-LCPRVLSTQARDRLDC--------------------VHMLLQMGANHTSQEIKSNkTVLHLAV 357
Cdd:cd22192    99 NQNLNLvreliaRGADvVSPRATGTFFRPGPKNliyygehplsfaacvgneeiVRLLIEHGADIRAQDSLGN-TVLHILV 177

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2565334754 358 QAANPTLVQLLLEL-----PRGDLRTFVNMKAH-GNTALHMAAA 395
Cdd:cd22192   178 LQPNKTFACQMYDLilsydKEDDLQPLDLVPNNqGLTPFKLAAK 221
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 227-445 3.60e-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: 3.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2565334754 227 GKTPLLVAAAANQPL-IVEDLLNLGAEPNAadhqGRSVLHVAATyGLPGVLLAVLNSGVQVDLEA------------RDF 293
Cdd:TIGR00870  52 GRSALFVAAIENENLeLTELLLNLSCRGAV----GDTLLHAISL-EYVDAVEAILLHLLAAFRKSgplelandqytsEFT 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2565334754 294 EGLTPLHTAILalnvamrpsdlcprvlstqaRDRLDCVHMLLQMGAN----------HTSQEIKS---NKTVLHLAVQAA 360
Cdd:TIGR00870 127 PGITALHLAAH--------------------RQNYEIVKLLLERGASvparacgdffVKSQGVDSfyhGESPLNAAACLG 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2565334754 361 NPTLVQLLLELPRGDLRTFvnmkAHGNTALHMAAALPPGPA---------QEAIVRHLlaAGADPTL-----RNLENEQP 426
Cdd:TIGR00870 187 SPSIVALLSEDPADILTAD----SLGNTLLHLLVMENEFKAeyeelscqmYNFALSLL--DKLRDSKeleviLNHQGLTP 260

                         250
                  ....*....|....*....
gi 2565334754 427 VHLLRPGPGPEGLRQLLKR 445
Cdd:TIGR00870 261 LKLAAKEGRIVLFRLKLAI 279
PHA03247 PHA03247
large tegument protein UL36; Provisional
 9-168 3.71e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.39  E-value: 3.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2565334754    9 PGGPQSTPRNPRVSRGERSHCPTQTVKKLLEEQRRRQQQQPDAGGVQGQFL--PPPEQPLTPSVNEAVTGHPPFPAHSET 86
Cdd:PHA03247  2649 PERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLAdpPPPPPTPEPAPHALVSATPLPPGPAAA 2728

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2565334754   87 VGSGPSSLGFPDWDPNTHAAYTDSPYSCPASAAENFLPPDFYPPSDPGQP----CPFPQGMEAGPWRVSAP-PSGPPQFP 161
Cdd:PHA03247  2729 RQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGpprrLTRPAVASLSESRESLPsPWDPADPP 2808


                   ....*..
gi 2565334754  162 AVVPGPS 168
Cdd:PHA03247  2809 AAVLAPA 2815
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
174-453 1.65e-28

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 113.90  E-value: 1.65e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2565334754 174 AHMLALGPQQLLAQDEEGDTLLHLFAARGLrwAAYAAAEVLQVYRRLDIREHKGKTPLLVAAAANQPLIVEDLLNLGAEP 253
Cdd:COG0666    36 LLLLLLLALLALALADALGALLLLAAALAG--DLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADV 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2565334754 254 NAADHQGRSVLHVAATYGLPGVLLAVLNSGvqVDLEARDFEGLTPLHTAIlalnvamrpsdlcprvlstqARDRLDCVHM 333
Cdd:COG0666   114 NARDKDGETPLHLAAYNGNLEIVKLLLEAG--ADVNAQDNDGNTPLHLAA--------------------ANGNLEIVKL 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2565334754 334 LLQMGANHTSQEiKSNKTVLHLAVQAANPTLVQLLLElpRGDLRTFVNmkAHGNTALHMAAALppgpAQEAIVRHLLAAG 413
Cdd:COG0666   172 LLEAGADVNARD-NDGETPLHLAAENGHLEIVKLLLE--AGADVNAKD--NDGKTALDLAAEN----GNLEIVKLLLEAG 242

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 2565334754 414 ADPTLRNLENEQPVHLLRPGPGPEGLRQLLKRSRVAPPGL 453
Cdd:COG0666   243 ADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
169-424 5.89e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 98.49  E-value: 5.89e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2565334754 169 LEVARAHMLALGPQQLLAQDEEGDTLLHLFAARG----LRWAAYAAAEVlqvyrrlDIREHKGKTPLLVAAAANQPLIVE 244
Cdd:COG0666    65 GDLLVALLLLAAGADINAKDDGGNTLLHAAARNGdleiVKLLLEAGADV-------NARDKDGETPLHLAAYNGNLEIVK 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2565334754 245 DLLNLGAEPNAADHQGRSVLHVAATYGLPGVLLAVLNSGvqVDLEARDFEGLTPLHTAIlalnvamrpsdlcprvlstqA 324
Cdd:COG0666   138 LLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAG--ADVNARDNDGETPLHLAA--------------------E 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2565334754 325 RDRLDCVHMLLQMGANHTSQEiKSNKTVLHLAVQAANPTLVQLLLELPRGDLrtfvNMKAHGNTALHMAAALppgpAQEA 404
Cdd:COG0666   196 NGHLEIVKLLLEAGADVNAKD-NDGKTALDLAAENGNLEIVKLLLEAGADLN----AKDKDGLTALLLAAAA----GAAL 266

                         250       260
                  ....*....|....*....|
gi 2565334754 405 IVRHLLAAGADPTLRNLENE 424
Cdd:COG0666   267 IVKLLLLALLLLAAALLDLL 286
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
229-445 1.93e-16

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 79.61  E-value: 1.93e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2565334754 229 TPLLVAAAANQPLIVEDLLNLGAEPNAADHQGRSVLHVAATYGLPGVLLAVLNSGVqvDLEARDFEGLTPLHTAILALNV 308
Cdd:COG0666    23 LLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGA--DINAKDDGGNTLLHAAARNGDL 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2565334754 309 AM-------------RPSDLCPRVLSTQARDRLDCVHMLLQMGANHTSQEiKSNKTVLHLAVQAANPTLVQLLLElpRG- 374
Cdd:COG0666   101 EIvkllleagadvnaRDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQD-NDGNTPLHLAAANGNLEIVKLLLE--AGa 177

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2565334754 375 DlrtfVNMK-AHGNTALHMAAALppgpAQEAIVRHLLAAGADPTLRNLENEQPVHLLRPGPGPEGLRQLLKR 445
Cdd:COG0666   178 D----VNARdNDGETPLHLAAEN----GHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241
Ank_2 pfam12796
Ankyrin repeats (3 copies);
328-420 3.10e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 62.44  E-value: 3.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2565334754 328 LDCVHMLLQMGANHTSQEiKSNKTVLHLAVQAANPTLVQLLLELPRgdlrtfVNMKAHGNTALHMAAALppgpAQEAIVR 407
Cdd:pfam12796  10 LELVKLLLENGADANLQD-KNGRTALHLAAKNGHLEIVKLLLEHAD------VNLKDNGRTALHYAARS----GHLEIVK 78

                          90
                  ....*....|...
gi 2565334754 408 HLLAAGADPTLRN 420
Cdd:pfam12796  79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
231-344 9.22e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 58.20  E-value: 9.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2565334754 231 LLVAAAANQPLIVEDLLNLGAEPNAADHQGRSVLHVAATYGLPGVLLAVLNsgvQVDLEARDfEGLTPLHTAILAlnvam 310
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE---HADVNLKD-NGRTALHYAARS----- 71

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2565334754 311 rpsdlcprvlstqarDRLDCVHMLLQMGANHTSQ 344
Cdd:pfam12796  72 ---------------GHLEIVKLLLEKGADINVK 90
PHA03095 PHA03095
ankyrin-like protein; Provisional
 188-429 1.11e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 63.51  E-value: 1.11e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2565334754 188 DEEGDTLLHLFaargLRwaaYAAAEVLQVYR-------RLDIREHKGKTPL-LVAAAANQPLIVEDLLNLGAEPNAADHQ 259
Cdd:PHA03095   44 GEYGKTPLHLY----LH---YSSEKVKDIVRllleagaDVNAPERCGFTPLhLYLYNATTLDVIKLLIKAGADVNAKDKV 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2565334754 260 GRSVLHVAATyGL---PGVLLAVLNSGVqvDLEARDFEGLTPLHtailalnVAMRPSDLCPRVlstqardrldcVHMLLQ 336
Cdd:PHA03095  117 GRTPLHVYLS-GFninPKVIRLLLRKGA--DVNALDLYGMTPLA-------VLLKSRNANVEL-----------LRLLID 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2565334754 337 MGANHTSQEIKSNKTVLHLAVQA-ANPTLVQLLLElpRGDLRTFVNMkaHGNTALHMAAALppGPAQEAIVRHLLAAGAD 415
Cdd:PHA03095  176 AGADVYAVDDRFRSLLHHHLQSFkPRARIVRELIR--AGCDPAATDM--LGNTPLHSMATG--SSCKRSLVLPLLIAGIS 249

                         250
                  ....*....|....
gi 2565334754 416 PTLRNLENEQPVHL 429
Cdd:PHA03095  250 INARNRYGQTPLHY 263
PHA03095 PHA03095
ankyrin-like protein; Provisional
 242-430 1.89e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 56.19  E-value: 1.89e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2565334754 242 IVEDLLNLGAEPNAADHQGRSVLHVAATYGLP---GVLLAVLNSGVQVDleARDFEGLTPLHTAILALNVamrpsdlcpr 318
Cdd:PHA03095   29 EVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEkvkDIVRLLLEAGADVN--APERCGFTPLHLYLYNATT---------- 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2565334754 319 vlstqardrLDCVHMLLQMGANhTSQEIKSNKTVLH--LAVQAANPTLVQLLLEL---------------------PRGD 375
Cdd:PHA03095   97 ---------LDVIKLLIKAGAD-VNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKgadvnaldlygmtplavllksRNAN 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2565334754 376 LRTfVNM-----------KAHGNTALHMAAALPPgpAQEAIVRHLLAAGADPTLRNLENEQPVHLL 430
Cdd:PHA03095  167 VEL-LRLlidagadvyavDDRFRSLLHHHLQSFK--PRARIVRELIRAGCDPAATDMLGNTPLHSM 229
PHA03095 PHA03095
ankyrin-like protein; Provisional
 227-427 3.81e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 55.42  E-value: 3.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2565334754 227 GKTPL---LVAAAANqPLIVEDLLNLGAEPNAADHQGRSVLHV-----AATYGLPGVLLAVLNsgvqvDLEARDFEGLTP 298
Cdd:PHA03095  117 GRTPLhvyLSGFNIN-PKVIRLLLRKGADVNALDLYGMTPLAVllksrNANVELLRLLIDAGA-----DVYAVDDRFRSL 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2565334754 299 LHtaILALNVamrpsdlcprvlstqaRDRLDCVHMLLQMGANHTSQEIKSNkTVLHLAVQAAN--PTLVQLLLElpRGdl 376
Cdd:PHA03095  191 LH--HHLQSF----------------KPRARIVRELIRAGCDPAATDMLGN-TPLHSMATGSSckRSLVLPLLI--AG-- 247

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2565334754 377 rTFVN-MKAHGNTALHMAAALPPGPAqeaiVRHLLAAGADPTLRNLENEQPV 427
Cdd:PHA03095  248 -ISINaRNRYGQTPLHYAAVFNNPRA----CRRLIALGADINAVSSDGNTPL 294
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 224-370 9.66e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 54.12  E-value: 9.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2565334754 224 EHKGKTPLLVAAAANQPLIVEDLLNLGAEPNAADHQGRSVLHVAATYGLPGVLLAVLNSGVQVDleARDFEGLTPLHTAI 303
Cdd:PHA02878  165 RHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTD--ARDKCGNTPLHISV 242

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2565334754 304 lalnvamrpsdlcPRVLStqardrLDCVHMLLQMGANHTSQEIKSNKTVLHLAVQaaNPTLVQLLLE 370
Cdd:PHA02878  243 -------------GYCKD------YDILKLLLEHGVDVNAKSYILGLTALHSSIK--SERKLKLLLE 288
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 226-427 1.29e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 53.91  E-value: 1.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2565334754 226 KGKTPL-LVAAAANQPLIVEDLLNLGAEPNAADHQGRSVLHVAATYG-LPGVLLAVLNSGVQVDleARDFEGLTPLHTAI 303
Cdd:PHA02876  306 KGETPLyLMAKNGYDTENIRTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGANVN--ARDYCDKTPIHYAA 383

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2565334754 304 LALNVAMrpsdlcprvlstqardrldcVHMLLQMGAN--HTSQEIksnKTVLHLAVQAANP-TLVQLLLElpRGdlrTFV 380
Cdd:PHA02876  384 VRNNVVI--------------------INTLLDYGADieALSQKI---GTALHFALCGTNPyMSVKTLID--RG---ANV 435

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2565334754 381 NMK-AHGNTALHMAAALPPGPaqeAIVRHLLAAGADPTLRNLENEQPV 427
Cdd:PHA02876  436 NSKnKDLSTPLHYACKKNCKL---DVIEMLLDNGADVNAINIQNQYPL 480
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 229-395 1.62e-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: 50.40  E-value: 1.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2565334754 229 TPLLVAAAANQPLIVEDLL-NLGAEPNAADHQGRSVLHVAATYGLPGVLLAVLNSG---VQVDLEARDFEGLTPLHTAIL 304
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAApelVNEPMTSDLYQGETALHIAVV 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2565334754 305 ALNVAM------RPSD-LCPRVLSTQARDRLDC--------------------VHMLLQMGANHTSQEIKSNkTVLHLAV 357
Cdd:cd22192    99 NQNLNLvreliaRGADvVSPRATGTFFRPGPKNliyygehplsfaacvgneeiVRLLIEHGADIRAQDSLGN-TVLHILV 177

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2565334754 358 QAANPTLVQLLLEL-----PRGDLRTFVNMKAH-GNTALHMAAA 395
Cdd:cd22192   178 LQPNKTFACQMYDLilsydKEDDLQPLDLVPNNqGLTPFKLAAK 221
Ank_2 pfam12796
Ankyrin repeats (3 copies);
187-257 2.18e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 45.88  E-value: 2.18e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2565334754 187 QDEEGDTLLHLFAARGlrwaAYAAAEVLQVYRRLDIREHkGKTPLLVAAAANQPLIVEDLLNLGAEPNAAD 257
Cdd:pfam12796  26 QDKNGRTALHLAAKNG----HLEIVKLLLEHADVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 229-429 3.06e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 49.28  E-value: 3.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2565334754 229 TPLLVAAAANQPLIVEDLLNLGAEPN--AADHQGRSVLHVAATYGLPGVLLAV---LNSGVQVDleARDFEGLTPLHTAI 303
Cdd:PHA03100   37 LPLYLAKEARNIDVVKILLDNGADINssTKNNSTPLHYLSNIKYNLTDVKEIVkllLEYGANVN--APDNNGITPLLYAI 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2565334754 304 lalnvamrpsdlcprvlsTQARDRLDCVHMLLQMGANHTSQEiKSNKTVLHLAVQAANPTL--VQLLLElpRG---DLRT 378
Cdd:PHA03100  115 ------------------SKKSNSYSIVEYLLDNGANVNIKN-SDGENLLHLYLESNKIDLkiLKLLID--KGvdiNAKN 173

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2565334754 379 FVNM-----------KAHGNTALHMAAALPpgpaQEAIVRHLLAAGADPTLRNLENEQPVHL 429
Cdd:PHA03100  174 RVNYllsygvpinikDVYGFTPLHYAVYNN----NPEFVKYLLDLGANPNLVNKYGDTPLHI 231
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 231-369 3.30e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 49.48  E-value: 3.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2565334754 231 LLVAAAANQPLIvEDLLNLGAEPNAADHQGRSVLHVAATYGLPGVLLAVLNSGVQVDLeaRDFEGLTPLHTAILA----- 305
Cdd:PLN03192  530 LTVASTGNAALL-EELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHI--RDANGNTALWNAISAkhhki 606

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2565334754 306 ---LNVAMRPSDlcPR----VLSTQA-RDRLDCVHMLLQMGANHTSQEiKSNKTVLHLAVQAANPTLVQLLL 369
Cdd:PLN03192  607 friLYHFASISD--PHaagdLLCTAAkRNDLTAMKELLKQGLNVDSED-HQGATALQVAMAEDHVDMVRLLI 675
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 241-445 5.78e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 48.91  E-value: 5.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2565334754 241 LIVEDLLNLGAEPNAADHQGRSVLHVAATYGLPGVLLAVLNSGVQVDLEARDfeGLTPLHTAILALNVamrpsdlcprvl 320
Cdd:PHA02876  159 LIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALD--DLSVLECAVDSKNI------------ 224

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2565334754 321 stqardrlDCVHMLLQMGANhtsqeikSNKTVLHLAVQAANPTLVQLLLELPRGdlRTFVNMKAHGNTALHMAAAlppGP 400
Cdd:PHA02876  225 --------DTIKAIIDNRSN-------INKNDLSLLKAIRNEDLETSLLLYDAG--FSVNSIDDCKNTPLHHASQ---AP 284

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2565334754 401 AQEAIVRHLLAAGADPTLRNLENEQPVHLL-RPGPGPEGLRQLLKR 445
Cdd:PHA02876  285 SLSRLVPKLLERGADVNAKNIKGETPLYLMaKNGYDTENIRTLIML 330
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 242-427 6.87e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 48.34  E-value: 6.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2565334754 242 IVEDLLNLGAEPNAAD-HQGRSVLHVAATYGLPGVLLAVLNSGVQVDLEarDFEGLTPLHTAIlalnvamrpsdlcprvl 320
Cdd:PHA02878  149 ITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIP--DKTNNSPLHHAV----------------- 209

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2565334754 321 stqARDRLDCVHMLLQMGANhTSQEIKSNKTVLHLAV-QAANPTLVQLLLElpRGdlrTFVNMKAH--GNTALHMAAAlp 397
Cdd:PHA02878  210 ---KHYNKPIVHILLENGAS-TDARDKCGNTPLHISVgYCKDYDILKLLLE--HG---VDVNAKSYilGLTALHSSIK-- 278

                         170       180       190
                  ....*....|....*....|....*....|
gi 2565334754 398 pgpaQEAIVRHLLAAGADPTLRNLENEQPV 427
Cdd:PHA02878  279 ----SERKLKLLLEYGADINSLNSYKLTPL 304
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 220-304 1.32e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 47.27  E-value: 1.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2565334754 220 LDIREHKGKTPLLVAAAANQPLIVEDLLNLGAEPNAADHQGRSVLHVAATYGLPGVLLAVLNSGVQVDLEARDfeGLTPL 299
Cdd:PHA02874  150 VNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKN--GFTPL 227


                  ....*
gi 2565334754 300 HTAIL 304
Cdd:PHA02874  228 HNAII 232
PHA03095 PHA03095
ankyrin-like protein; Provisional
 186-304 4.42e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 45.79  E-value: 4.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2565334754 186 AQDEEGDTLLHLFAARGLRWAAYaaaeVLQVYRR---LDIREHKGKTPLLVAAAANQPLIVEDLLNLGAEPNAADHQGRS 262
Cdd:PHA03095  217 ATDMLGNTPLHSMATGSSCKRSL----VLPLLIAgisINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNT 292

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2565334754 263 VLHVAATYGLPGVLLAVLNSGVQVDLEARDFEGLTPLHTAIL 304
Cdd:PHA03095  293 PLSLMVRNNNGRAVRAALAKNPSAETVAATLNTASVAGGDIP 334
Ank_5 pfam13857
Ankyrin repeats (many copies);
246-302 4.97e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.79  E-value: 4.97e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2565334754 246 LLNLG-AEPNAADHQGRSVLHVAATYGLPGVLLAVLNSGvqVDLEARDFEGLTPLHTA 302
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYG--VDLNLKDEEGLTALDLA 56
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 267-429 1.03e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 44.60  E-value: 1.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2565334754 267 AATYGLPGVLLAVLNSGVQVDLEARDfeGLTPLHTAILALNVAMrpsdlcprvlstqardrldcVHMLLQMGA--NHTSQ 344
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNFEIYD--GISPIKLAMKFRDSEA--------------------IKLLMKHGAipDVKYP 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2565334754 345 EIKSNktvLHLAVQAANPTLVQLLLelprgDLRTFVN--MKAHGNTALHMAAALppgpAQEAIVRHLLAAGADPTLRNLE 422
Cdd:PHA02875   67 DIESE---LHDAVEEGDVKAVEELL-----DLGKFADdvFYKDGMTPLHLATIL----KKLDIMKLLIARGADPDIPNTD 134


                  ....*..
gi 2565334754 423 NEQPVHL 429
Cdd:PHA02875  135 KFSPLHL 141
Ank_4 pfam13637
Ankyrin repeats (many copies);
229-271 1.33e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.57  E-value: 1.33e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2565334754 229 TPLLVAAAANQPLIVEDLLNLGAEPNAADHQGRSVLHVAATYG 271
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNG 45
Ank_2 pfam12796
Ankyrin repeats (3 copies);
221-288 1.87e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 40.10  E-value: 1.87e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2565334754 221 DIREHKGKTPLLVAAAANQPLIVEDLLNlGAEPNAADHqGRSVLHVAATYGLPGVLLAVLNSGVQVDL 288
Cdd:pfam12796  24 NLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINV 89
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 385-420 2.34e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.42  E-value: 2.34e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2565334754 385 HGNTALHMAAALppgPAQEAIVRHLLAAGADPTLRN 420
Cdd:pfam00023   1 DGNTPLHLAAGR---RGNLEIVKLLLSKGADVNARD 33
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 227-445 3.60e-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: 3.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2565334754 227 GKTPLLVAAAANQPL-IVEDLLNLGAEPNAadhqGRSVLHVAATyGLPGVLLAVLNSGVQVDLEA------------RDF 293
Cdd:TIGR00870  52 GRSALFVAAIENENLeLTELLLNLSCRGAV----GDTLLHAISL-EYVDAVEAILLHLLAAFRKSgplelandqytsEFT 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2565334754 294 EGLTPLHTAILalnvamrpsdlcprvlstqaRDRLDCVHMLLQMGAN----------HTSQEIKS---NKTVLHLAVQAA 360
Cdd:TIGR00870 127 PGITALHLAAH--------------------RQNYEIVKLLLERGASvparacgdffVKSQGVDSfyhGESPLNAAACLG 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2565334754 361 NPTLVQLLLELPRGDLRTFvnmkAHGNTALHMAAALPPGPA---------QEAIVRHLlaAGADPTL-----RNLENEQP 426
Cdd:TIGR00870 187 SPSIVALLSEDPADILTAD----SLGNTLLHLLVMENEFKAeyeelscqmYNFALSLL--DKLRDSKeleviLNHQGLTP 260

                         250
                  ....*....|....*....
gi 2565334754 427 VHLLRPGPGPEGLRQLLKR 445
Cdd:TIGR00870 261 LKLAAKEGRIVLFRLKLAI 279
PHA03247 PHA03247
large tegument protein UL36; Provisional
 9-168 3.71e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.39  E-value: 3.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2565334754    9 PGGPQSTPRNPRVSRGERSHCPTQTVKKLLEEQRRRQQQQPDAGGVQGQFL--PPPEQPLTPSVNEAVTGHPPFPAHSET 86
Cdd:PHA03247  2649 PERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLAdpPPPPPTPEPAPHALVSATPLPPGPAAA 2728

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2565334754   87 VGSGPSSLGFPDWDPNTHAAYTDSPYSCPASAAENFLPPDFYPPSDPGQP----CPFPQGMEAGPWRVSAP-PSGPPQFP 161
Cdd:PHA03247  2729 RQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGpprrLTRPAVASLSESRESLPsPWDPADPP 2808


                   ....*..
gi 2565334754  162 AVVPGPS 168
Cdd:PHA03247  2809 AAVLAPA 2815
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 220-283 5.52e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 41.96  E-value: 5.52e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2565334754 220 LDIREHKGKTPLLVAAAANQPLIVEDLLNLGAEPNAADHQGRSVLHVAATYGLPGVLLAVLNSG 283
Cdd:PHA03100  185 INIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNG 248
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 235-302 5.55e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 42.58  E-value: 5.55e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2565334754 235 AAANQPLIVEDLLNLGAEPNAADHQGRSVLHVAATYGLPGVLLAVLNSGvqVDLEARDFEGLTPLHTA 302
Cdd:PTZ00322   90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFG--ADPTLLDKDGKTPLELA 155
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 221-405 8.68e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 41.52  E-value: 8.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2565334754 221 DIREHKGKTPLLVAAAANQPLIVEDLLNLGAEPNAADHQGRSVLHVAATYGLPGVLLAVLNSGVQVDLEarDFEGLTPLH 300
Cdd:PHA02875   96 DVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIE--DCCGCTPLI 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2565334754 301 TAILALNVAmrpsdLCprvlstqardrldcvHMLLQMGANHTSQEIKSNKTVLHLAVQAANPTLVQLLLElpRG-DLRTF 379
Cdd:PHA02875  174 IAMAKGDIA-----IC---------------KMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLFIK--RGaDCNIM 231

                         170       180
                  ....*....|....*....|....*.
gi 2565334754 380 VNMKAHGNTALHMAAALPPGPAQEAI 405
Cdd:PHA02875  232 FMIEGEECTILDMICNMCTNLESEAI 257
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 225-369 2.21e-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: 40.38  E-value: 2.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2565334754 225 HKGKTPLLVAAAANQPLIVEDLLNLGAEPNAAD--------------HQGRSVLHVAATYGLPGVLLAVLNSGvqVDLEA 290
Cdd:cd22192    87 YQGETALHIAVVNQNLNLVRELIARGADVVSPRatgtffrpgpknliYYGEHPLSFAACVGNEEIVRLLIEHG--ADIRA 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2565334754 291 RDFEGLTPLHtaILAL----NVAMRPSDLcprVLSTQARDRLDCVHMLL-QMGAnhtsqeiksnkTVLHLAVQAANPTLV 365
Cdd:cd22192   165 QDSLGNTVLH--ILVLqpnkTFACQMYDL---ILSYDKEDDLQPLDLVPnNQGL-----------TPFKLAAKEGNIVMF 228


                  ....
gi 2565334754 366 QLLL 369
Cdd:cd22192   229 QHLV 232
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 213-353 2.53e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 40.43  E-value: 2.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2565334754 213 VLQVYRRLDIREHKGKTPLLVAAAANQPLIVEDLLNLGAEPNAADHQGRSVLHVAATYGLPGVLLAVL-NSGVQVDLEAR 291
Cdd:PHA02876  361 LLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMSVKTLiDRGANVNSKNK 440

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2565334754 292 DFEglTPLHTAilalnvamrpsdlcprvlsTQARDRLDCVHMLLQMGANHTSQEIKSNKTVL 353
Cdd:PHA02876  441 DLS--TPLHYA-------------------CKKNCKLDVIEMLLDNGADVNAINIQNQYPLL 481
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 210-416 3.45e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 39.59  E-value: 3.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2565334754 210 AAEVLQVYRRLDIREHKGKTPLLVAAAANQPLIVEDLLNLGAEPNAADHQGRSVLHVAATYGLPGVLLAVLNSGVQVDlE 289
Cdd:PHA02875   18 ARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFAD-D 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2565334754 290 ARDFEGLTPLHTAILALNVAMrpsdlcprvlstqardrldcVHMLLQMGANhTSQEIKSNKTVLHLAVQAANPTLVQLLL 369
Cdd:PHA02875   97 VFYKDGMTPLHLATILKKLDI--------------------MKLLIARGAD-PDIPNTDKFSPLHLAVMMGDIKGIELLI 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2565334754 370 elprgDLRTFVNMK-AHGNTALHMAAALppgpAQEAIVRHLLAAGADP 416
Cdd:PHA02875  156 -----DHKACLDIEdCCGCTPLIIAMAK----GDIAICKMLLDSGANI 194
Ank_4 pfam13637
Ankyrin repeats (many copies);
260-310 3.78e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 35.33  E-value: 3.78e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2565334754 260 GRSVLHVAATYGLPGVLLAVLNSGVQVDleARDFEGLTPLHTAILALNVAM 310
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADIN--AVDGNGETALHFAASNGNVEV 49
PHA02743 PHA02743
Viral ankyrin protein; Provisional
 331-393 4.12e-03

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 37.87  E-value: 4.12e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2565334754 331 VHMLLQMGANHTSQEIKSNKTVLHLAVQAANPTLVQLLLELPRGDLRTfVNMKAHgnTALHMA 393
Cdd:PHA02743   76 IELLVNMGADINARELGTGNTLLHIAASTKNYELAEWLCRQLGVNLGA-INYQHE--TAYHIA 135
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 226-258 8.83e-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: 33.80  E-value: 8.83e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2565334754 226 KGKTPLLVAAA-ANQPLIVEDLLNLGAEPNAADH 258
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 351-415 9.21e-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: 38.46  E-value: 9.21e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2565334754 351 TVLHLAVQAANPTLVQLLLElprgDLRTFVNMKA-----HGNTALHMAAAlppgPAQEAIVRHLLAAGAD 415
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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