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Conserved domains on  [gi|1958665568|ref|XP_038944298|]
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NF-kappa-B inhibitor zeta isoform X1 [Rattus norvegicus]

Protein Classification

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

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
354-618 1.03e-31

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 124.68  E-value: 1.03e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665568 354 KLANISQEQFLSRDGDGDTFLHIAVAQGRRALSYVLARKMNALHMLDvkeHNGQSAFQVAVAANQHLIVQDLVNLGAQVN 433
Cdd:COG0666    38 LLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD---DGGNTLLHAAARNGDLEIVKLLLEAGADVN 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665568 434 TTDCWGRTPLHVCAEKGHSQVLQA-IQKGAvrsnqfvDLEATNYDGLTPLHCAVLAHNsvvhdlqrsqqphspevqdlll 512
Cdd:COG0666   115 ARDKDGETPLHLAAYNGNLEIVKLlLEAGA-------DVNAQDNDGNTPLHLAAANGN---------------------- 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665568 513 knkslVDTIKCLIQMGAAVEAKDrKSGRTALHLAAEEANLELIRLFLELPsclSFVNAKAYNGNTALHVAASLQYRvtql 592
Cdd:COG0666   166 -----LEIVKLLLEAGADVNARD-NDGETPLHLAAENGHLEIVKLLLEAG---ADVNAKDNDGKTALDLAAENGNL---- 232

                         250       260
                  ....*....|....*....|....*.
gi 1958665568 593 DAVRLLMRKGADPSTRNLENEQPVHL 618
Cdd:COG0666   233 EIVKLLLEAGADLNAKDKDGLTALLL 258
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
354-618 1.03e-31

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 124.68  E-value: 1.03e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665568 354 KLANISQEQFLSRDGDGDTFLHIAVAQGRRALSYVLARKMNALHMLDvkeHNGQSAFQVAVAANQHLIVQDLVNLGAQVN 433
Cdd:COG0666    38 LLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD---DGGNTLLHAAARNGDLEIVKLLLEAGADVN 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665568 434 TTDCWGRTPLHVCAEKGHSQVLQA-IQKGAvrsnqfvDLEATNYDGLTPLHCAVLAHNsvvhdlqrsqqphspevqdlll 512
Cdd:COG0666   115 ARDKDGETPLHLAAYNGNLEIVKLlLEAGA-------DVNAQDNDGNTPLHLAAANGN---------------------- 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665568 513 knkslVDTIKCLIQMGAAVEAKDrKSGRTALHLAAEEANLELIRLFLELPsclSFVNAKAYNGNTALHVAASLQYRvtql 592
Cdd:COG0666   166 -----LEIVKLLLEAGADVNARD-NDGETPLHLAAENGHLEIVKLLLEAG---ADVNAKDNDGKTALDLAAENGNL---- 232

                         250       260
                  ....*....|....*....|....*.
gi 1958665568 593 DAVRLLMRKGADPSTRNLENEQPVHL 618
Cdd:COG0666   233 EIVKLLLEAGADLNAKDKDGLTALLL 258
PHA03095 PHA03095
ankyrin-like protein; Provisional
 421-617 8.88e-15

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 76.99  E-value: 8.88e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665568 421 IVQDLVNLGAQVNTTDCWGRTPLHVCAEKGHSQVLQAIQ----KGAvrsnqfvDLEATNYDGLTPLHCavlahnsvvhdl 496
Cdd:PHA03095   29 EVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIVRllleAGA-------DVNAPERCGFTPLHL------------ 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665568 497 qrsqqphspevqdlLLKNKSLVDTIKCLIQMGAAVEAKDrKSGRTALH--LAAEEANLELIRLFLELPSClsfVNAKAYN 574
Cdd:PHA03095   90 --------------YLYNATTLDVIKLLIKAGADVNAKD-KVGRTPLHvyLSGFNINPKVIRLLLRKGAD---VNALDLY 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1958665568 575 GNTALHVAasLQYRVTQLDAVRLLMRKGADPSTRNLENEQPVH 617
Cdd:PHA03095  152 GMTPLAVL--LKSRNANVELLRLLIDAGADVYAVDDRFRSLLH 192
Ank_2 pfam12796
Ankyrin repeats (3 copies);
518-609 8.06e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.45  E-value: 8.06e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665568 518 VDTIKCLIQMGAAVEAKDrKSGRTALHLAAEEANLELIRLFLELPSclsfVNAKaYNGNTALHVAASLQYrvtqLDAVRL 597
Cdd:pfam12796  10 LELVKLLLENGADANLQD-KNGRTALHLAAKNGHLEIVKLLLEHAD----VNLK-DNGRTALHYAARSGH----LEIVKL 79

                          90
                  ....*....|..
gi 1958665568 598 LMRKGADPSTRN 609
Cdd:pfam12796  80 LLEKGADINVKD 91
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 363-554 6.62e-05

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 46.16  E-value: 6.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665568 363 FLSRDGDGDTFLHIAVAQGRRALSYVLARKMNALhmldVKE------HNGQSAFQVAVaANQHL-IVQDLVNLGAQVNT- 434
Cdd:cd22192    44 LFQRGALGETALHVAALYDNLEAAVVLMEAAPEL----VNEpmtsdlYQGETALHIAV-VNQNLnLVRELIARGADVVSp 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665568 435 ----------TDC---WGRTPLHVCAEKGHSQVLQA-IQKGAvrsnqfvDLEATNYDGLTPLHCAVLAHNSVVhdlqrsq 500
Cdd:cd22192   119 ratgtffrpgPKNliyYGEHPLSFAACVGNEEIVRLlIEHGA-------DIRAQDSLGNTVLHILVLQPNKTF------- 184

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958665568 501 qphSPEVQDLLL-----KNKSLVDTIKcliqmgaaveakdRKSGRTALHLAAEEANLEL 554
Cdd:cd22192   185 ---ACQMYDLILsydkeDDLQPLDLVP-------------NNQGLTPFKLAAKEGNIVM 227
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 405-613 3.95e-03

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: 40.45  E-value: 3.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665568 405 NGQSAFQVAVAANQHLIV-QDLVNLGA-QVNTTDCWGRTPLHVCAEKGHSQVLQAIQKgavrsnqfvDLEATNYDGLTPL 482
Cdd:TIGR00870  16 DEEKAFLPAAERGDLASVyRDLEEPKKlNINCPDRLGRSALFVAAIENENLELTELLL---------NLSCRGAVGDTLL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665568 483 HCAVLAHNSVVHDLQRSQQPHSPEVQDLLLKNKSLVDTIKcliqmgaaveakdrkSGRTALHLAAEEANLELIRLFLE-- 560
Cdd:TIGR00870  87 HAISLEYVDAVEAILLHLLAAFRKSGPLELANDQYTSEFT---------------PGITALHLAAHRQNYEIVKLLLErg 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958665568 561 --LP---SCLSFVNAK----AYNGNTALHVAASLqyrvTQLDAVRLLMRKGADPSTR-NLENE 613
Cdd:TIGR00870 152 asVParaCGDFFVKSQgvdsFYHGESPLNAAACL----GSPSIVALLSEDPADILTAdSLGNT 210
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 539-560 9.69e-03

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.10  E-value: 9.69e-03
                           10        20
                   ....*....|....*....|..
gi 1958665568  539 GRTALHLAAEEANLELIRLFLE 560
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLD 23
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
354-618 1.03e-31

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 124.68  E-value: 1.03e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665568 354 KLANISQEQFLSRDGDGDTFLHIAVAQGRRALSYVLARKMNALHMLDvkeHNGQSAFQVAVAANQHLIVQDLVNLGAQVN 433
Cdd:COG0666    38 LLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD---DGGNTLLHAAARNGDLEIVKLLLEAGADVN 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665568 434 TTDCWGRTPLHVCAEKGHSQVLQA-IQKGAvrsnqfvDLEATNYDGLTPLHCAVLAHNsvvhdlqrsqqphspevqdlll 512
Cdd:COG0666   115 ARDKDGETPLHLAAYNGNLEIVKLlLEAGA-------DVNAQDNDGNTPLHLAAANGN---------------------- 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665568 513 knkslVDTIKCLIQMGAAVEAKDrKSGRTALHLAAEEANLELIRLFLELPsclSFVNAKAYNGNTALHVAASLQYRvtql 592
Cdd:COG0666   166 -----LEIVKLLLEAGADVNARD-NDGETPLHLAAENGHLEIVKLLLEAG---ADVNAKDNDGKTALDLAAENGNL---- 232

                         250       260
                  ....*....|....*....|....*.
gi 1958665568 593 DAVRLLMRKGADPSTRNLENEQPVHL 618
Cdd:COG0666   233 EIVKLLLEAGADLNAKDKDGLTALLL 258
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
354-618 8.59e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 119.29  E-value: 8.59e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665568 354 KLANISQEQFLSRDGDGDTFLHIAVAQGRRALSYVLARKMNALHMLDVKEHNGQSAFQVAVAANQHLIVQDLVNLGAQVN 433
Cdd:COG0666     2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665568 434 TTDCWGRTPLHVCAEKGHSQVLQA-IQKGAvrsnqfvDLEATNYDGLTPLHCAVLAHNsvvhdlqrsqqphspevqdlll 512
Cdd:COG0666    82 AKDDGGNTLLHAAARNGDLEIVKLlLEAGA-------DVNARDKDGETPLHLAAYNGN---------------------- 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665568 513 knkslVDTIKCLIQMGAAVEAKDrKSGRTALHLAAEEANLELIRLFLELPsclSFVNAKAYNGNTALHVAASLQYrvtqL 592
Cdd:COG0666   133 -----LEIVKLLLEAGADVNAQD-NDGNTPLHLAAANGNLEIVKLLLEAG---ADVNARDNDGETPLHLAAENGH----L 199

                         250       260
                  ....*....|....*....|....*.
gi 1958665568 593 DAVRLLMRKGADPSTRNLENEQPVHL 618
Cdd:COG0666   200 EIVKLLLEAGADVNAKDNDGKTALDL 225
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
366-613 9.07e-28

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 113.51  E-value: 9.07e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665568 366 RDGDGDTFLHIAVAQGRR-ALSYVLARKMNalhmLDVKEHNGQSAFQVAVAANQHLIVQDLVNLGAQVNTTDCWGRTPLH 444
Cdd:COG0666    83 KDDGGNTLLHAAARNGDLeIVKLLLEAGAD----VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLH 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665568 445 VCAEKGHSQVLQA-IQKGAvrsnqfvDLEATNYDGLTPLHCAVLAHNsvvhdlqrsqqphspevqdlllknkslVDTIKC 523
Cdd:COG0666   159 LAAANGNLEIVKLlLEAGA-------DVNARDNDGETPLHLAAENGH---------------------------LEIVKL 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665568 524 LIQMGAAVEAKDrKSGRTALHLAAEEANLELIRLFLELpscLSFVNAKAYNGNTALHVAASLQYrvtqLDAVRLLMRKGA 603
Cdd:COG0666   205 LLEAGADVNAKD-NDGKTALDLAAENGNLEIVKLLLEA---GADLNAKDKDGLTALLLAAAAGA----ALIVKLLLLALL 276

                         250
                  ....*....|
gi 1958665568 604 DPSTRNLENE 613
Cdd:COG0666   277 LLAAALLDLL 286
PHA03095 PHA03095
ankyrin-like protein; Provisional
 421-617 8.88e-15

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 76.99  E-value: 8.88e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665568 421 IVQDLVNLGAQVNTTDCWGRTPLHVCAEKGHSQVLQAIQ----KGAvrsnqfvDLEATNYDGLTPLHCavlahnsvvhdl 496
Cdd:PHA03095   29 EVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIVRllleAGA-------DVNAPERCGFTPLHL------------ 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665568 497 qrsqqphspevqdlLLKNKSLVDTIKCLIQMGAAVEAKDrKSGRTALH--LAAEEANLELIRLFLELPSClsfVNAKAYN 574
Cdd:PHA03095   90 --------------YLYNATTLDVIKLLIKAGADVNAKD-KVGRTPLHvyLSGFNINPKVIRLLLRKGAD---VNALDLY 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1958665568 575 GNTALHVAasLQYRVTQLDAVRLLMRKGADPSTRNLENEQPVH 617
Cdd:PHA03095  152 GMTPLAVL--LKSRNANVELLRLLIDAGADVYAVDDRFRSLLH 192
Ank_2 pfam12796
Ankyrin repeats (3 copies);
518-609 8.06e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.45  E-value: 8.06e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665568 518 VDTIKCLIQMGAAVEAKDrKSGRTALHLAAEEANLELIRLFLELPSclsfVNAKaYNGNTALHVAASLQYrvtqLDAVRL 597
Cdd:pfam12796  10 LELVKLLLENGADANLQD-KNGRTALHLAAKNGHLEIVKLLLEHAD----VNLK-DNGRTALHYAARSGH----LEIVKL 79

                          90
                  ....*....|..
gi 1958665568 598 LMRKGADPSTRN 609
Cdd:pfam12796  80 LLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 421-604 2.51e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 72.39  E-value: 2.51e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665568 421 IVQDLVNLGAQVNTTDCWGRTPLHVCAEK--GHSQVLQA-IQKGAvrsnqfvDLEATNYDGLTPLHcAVLAHNSVvhDLq 497
Cdd:PHA03100   88 IVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYlLDNGA-------NVNIKNSDGENLLH-LYLESNKI--DL- 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665568 498 rsqqphspEVQDLLLKNKSLV---DTIKCLIQMGAAVEAKDRKsGRTALHLAAEEANLELIRLFLELPsclSFVNAKAYN 574
Cdd:PHA03100  157 --------KILKLLIDKGVDInakNRVNYLLSYGVPINIKDVY-GFTPLHYAVYNNNPEFVKYLLDLG---ANPNLVNKY 224

                         170       180       190
                  ....*....|....*....|....*....|
gi 1958665568 575 GNTALHVAASLQYrvtqLDAVRLLMRKGAD 604
Cdd:PHA03100  225 GDTPLHIAILNNN----KEIFKLLLNNGPS 250
PHA03095 PHA03095
ankyrin-like protein; Provisional
 355-618 1.15e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 64.28  E-value: 1.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665568 355 LANISQEQFlsRDGDGDTFLHIAVAQGRRALSYVLARKMNALHMLDVKEHNGQSAFQVAVAANQHL-IVQDLVNLGAQVN 433
Cdd:PHA03095   34 LAAGADVNF--RGEYGKTPLHLYLHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAGADVN 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665568 434 TTDCWGRTPLHVCAeKG---HSQVLQA-IQKGAvrsnqfvDLEATNYDGLTPLHCavlahnsvvhdlqrsqqphspevqd 509
Cdd:PHA03095  112 AKDKVGRTPLHVYL-SGfniNPKVIRLlLRKGA-------DVNALDLYGMTPLAV------------------------- 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665568 510 lLLKNKSL-VDTIKCLIQMGAAVEAKDrKSGRTALHLAAE--EANLELIRlflELPSCLSFVNAKAYNGNTALHVAAslq 586
Cdd:PHA03095  159 -LLKSRNAnVELLRLLIDAGADVYAVD-DRFRSLLHHHLQsfKPRARIVR---ELIRAGCDPAATDMLGNTPLHSMA--- 230

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1958665568 587 yrvTQLDAVRLLMR----KGADPSTRNLENEQPVHL 618
Cdd:PHA03095  231 ---TGSSCKRSLVLplliAGISINARNRYGQTPLHY 263
Ank_2 pfam12796
Ankyrin repeats (3 copies);
410-490 2.25e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 57.43  E-value: 2.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665568 410 FQVAVAANQHLIVQDLVNLGAQVNTTDCWGRTPLHVCAEKGHSQVLQA-IQKGAVRSnqfvdleatNYDGLTPLHCAVLA 488
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLlLEHADVNL---------KDNGRTALHYAARS 71


                  ..
gi 1958665568 489 HN 490
Cdd:pfam12796  72 GH 73
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 396-618 6.58e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 58.74  E-value: 6.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665568 396 LHMLDVKEHNGQSA-------FQVAVAANQHLIVQDLVNLGAQVNTTDCWGRTPLHV-CAE---KGHSQVLQAIQKGAVr 464
Cdd:PHA02878   20 IEYIDHTENYSTSAslipfipLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIiCKEpnkLGMKEMIRSINKCSV- 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665568 465 SNQFVDL-EATNYDGltplhcaVLAHNSVVHDLQRSQQphspEVQDLLLKNKSLVDTI-----KCLIQMGAAVEAKDRKS 538
Cdd:PHA02878   99 FYTLVAIkDAFNNRN-------VEIFKIILTNRYKNIQ----TIDLVYIDKKSKDDIIeaeitKLLLSYGADINMKDRHK 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665568 539 GRTALHLAAEEANLELIRLFLelpSCLSFVNAKAYNGNTALHVAASlQYRVtqlDAVRLLMRKGADPSTRNLENEQPVHL 618
Cdd:PHA02878  168 GNTALHYATENKDQRLTELLL---SYGANVNIPDKTNNSPLHHAVK-HYNK---PIVHILLENGASTDARDKCGNTPLHI 240
Ank_2 pfam12796
Ankyrin repeats (3 copies);
443-560 3.46e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 51.27  E-value: 3.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665568 443 LHVCAEKGHSQVLQA-IQKGAvrsnqfvDLEATNYDGLTPLHCAVLAHNsvvhdlqrsqqphspevqdlllknkslVDTI 521
Cdd:pfam12796   1 LHLAAKNGNLELVKLlLENGA-------DANLQDKNGRTALHLAAKNGH---------------------------LEIV 46

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1958665568 522 KCLIQmgaAVEAKDRKSGRTALHLAAEEANLELIRLFLE 560
Cdd:pfam12796  47 KLLLE---HADVNLKDNGRTALHYAARSGHLEIVKLLLE 82
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 421-632 8.28e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 55.27  E-value: 8.28e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665568 421 IVQDLVNLGAQVNTTD-CWGRTPLHVCAEKGHSQVLQ-AIQKGAvrsnqfvDLEATNYDGLTPLHCAVLAHNSvvhdlqr 498
Cdd:PHA02878  149 ITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTElLLSYGA-------NVNIPDKTNNSPLHHAVKHYNK------- 214

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665568 499 sqqphspevqdlllknkslvDTIKCLIQMGAAVEAKDrKSGRTALHLAAEEA-NLELIRLFLELPSClsfVNAKAY-NGN 576
Cdd:PHA02878  215 --------------------PIVHILLENGASTDARD-KCGNTPLHISVGYCkDYDILKLLLEHGVD---VNAKSYiLGL 270

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958665568 577 TALHVAaslqyrVTQLDAVRLLMRKGADPSTRNLENEQPVHLVPDGPVGEQIRRIL 632
Cdd:PHA02878  271 TALHSS------IKSERKLKLLLEYGADINSLNSYKLTPLSSAVKQYLCINIGRIL 320
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 414-617 1.23e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 55.07  E-value: 1.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665568 414 VAANQHLIVQDLVNLGAQVNTTDCWGRTPLHVCAEKGHSQVLQ-AIQKGAvrsnqfvDLEATNYDGLTPLHCAVLAHN-- 490
Cdd:PHA02876  153 IQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNlLLSYGA-------DVNIIALDDLSVLECAVDSKNid 225

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665568 491 ---SVV--------HDLQRSQQPHSPEVQDLLL--------------KNK---------SLVDTIKCLIQMGAAVEAKDR 536
Cdd:PHA02876  226 tikAIIdnrsninkNDLSLLKAIRNEDLETSLLlydagfsvnsiddcKNTplhhasqapSLSRLVPKLLERGADVNAKNI 305

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665568 537 KsGRTALHLAAEEA-NLELIRLFLELPSClsfVNAKAYNGNTALHVAASL-QYRvtqlDAVRLLMRKGADPSTRNLENEQ 614
Cdd:PHA02876  306 K-GETPLYLMAKNGyDTENIRTLIMLGAD---VNAADRLYITPLHQASTLdRNK----DIVITLLELGANVNARDYCDKT 377


                  ...
gi 1958665568 615 PVH 617
Cdd:PHA02876  378 PIH 380
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 391-642 1.97e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 54.49  E-value: 1.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665568 391 RKMNALHMLDVKEHNGQSAFQVAVAAN--------QHLIVQDLVNLGAQVNTTDCWGRTPLHVCAEKGHSQVLQAIQKGA 462
Cdd:PLN03192  502 KELHDLNVGDLLGDNGGEHDDPNMASNlltvastgNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHA 581

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665568 463 VRsnqfVDLEATNydGLTPLHCAVLA-HNS---VVHDLQRSQQPHSPevQDLLL--KNKSLVDTIKCLIQMGAAVEAKDR 536
Cdd:PLN03192  582 CN----VHIRDAN--GNTALWNAISAkHHKifrILYHFASISDPHAA--GDLLCtaAKRNDLTAMKELLKQGLNVDSEDH 653

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665568 537 KsGRTALHLAAEEANLELIRLFLElpsclsfvnakayngNTALHVAASLQYRVTQLDAVRLLMRKGADPSTRNLENEQPV 616
Cdd:PLN03192  654 Q-GATALQVAMAEDHVDMVRLLIM---------------NGADVDKANTDDDFSPTELRELLQKRELGHSITIVDSVPAD 717

                         250       260
                  ....*....|....*....|....*.
gi 1958665568 617 HLVPDGPVGEQIRRILKGKSIQQRVP 642
Cdd:PLN03192  718 EPDLGRDGGSRPGRLQGTSSDNQCRP 743
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 519-617 3.01e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 53.43  E-value: 3.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665568 519 DTIKCLIQMGAAVEAKDRKSgRTALHLAAEEANLELIRLFLELPSClsfVNAKAYNGNTALHVAAslqyRVTQLDAVRLL 598
Cdd:PHA02874  105 DMIKTILDCGIDVNIKDAEL-KTFLHYAIKKGDLESIKMLFEYGAD---VNIEDDNGCYPIHIAI----KHNFFDIIKLL 176

                          90
                  ....*....|....*....
gi 1958665568 599 MRKGADPSTRNLENEQPVH 617
Cdd:PHA02874  177 LEKGAYANVKDNNGESPLH 195
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 422-616 3.27e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 53.53  E-value: 3.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665568 422 VQDLVNLGAQVNTTDCWGRTPLHVCA--EKGHSQVLQAIQKGAvrsnqfvDLEATNYDGLTPLHCAVLAHNSVVhdlqrs 499
Cdd:PHA02876  324 IRTLIMLGADVNAADRLYITPLHQAStlDRNKDIVITLLELGA-------NVNARDYCDKTPIHYAAVRNNVVI------ 390

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665568 500 qqphspevqdlllknkslvdtIKCLIQMGAAVEAKDRKSGrTALHLAAEEANLEL-IRLFLELPSClsfVNAKAYNGNTA 578
Cdd:PHA02876  391 ---------------------INTLLDYGADIEALSQKIG-TALHFALCGTNPYMsVKTLIDRGAN---VNSKNKDLSTP 445

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1958665568 579 LHVAASlqyRVTQLDAVRLLMRKGADPSTRNLENEQPV 616
Cdd:PHA02876  446 LHYACK---KNCKLDVIEMLLDNGADVNAINIQNQYPL 480
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 421-617 3.38e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 53.53  E-value: 3.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665568 421 IVQDLVNLGAQVNTTDCWGRTPLHVCAEKGH--SQVLQAIQKGAvrsnqfvDLEATNYDGLTPLHCAvlahnsvvhdlqr 498
Cdd:PHA02876  289 LVPKLLERGADVNAKNIKGETPLYLMAKNGYdtENIRTLIMLGA-------DVNAADRLYITPLHQA------------- 348

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665568 499 sqqphspevqDLLLKNKslvDTIKCLIQMGAAVEAKDRKSgRTALHLAAEEANLELIRLFLELPSCLSFVNAKAyngNTA 578
Cdd:PHA02876  349 ----------STLDRNK---DIVITLLELGANVNARDYCD-KTPIHYAAVRNNVVIINTLLDYGADIEALSQKI---GTA 411

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1958665568 579 LHVAAslqYRVTQLDAVRLLMRKGADPSTRNLENEQPVH 617
Cdd:PHA02876  412 LHFAL---CGTNPYMSVKTLIDRGANVNSKNKDLSTPLH 447
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 366-520 3.91e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 53.04  E-value: 3.91e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665568 366 RDGDGDTFLHIAVAQGrralsyvlarKMNALHML-------DVKEHNGQSAFQVAVAANQHLIVQDLVNLGAQVNTTDCW 438
Cdd:PHA02874  120 KDAELKTFLHYAIKKG----------DLESIKMLfeygadvNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNN 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665568 439 GRTPLHVCAEKG-HSQVLQAIQKGAVRSNQFvdleatnYDGLTPLHCAVLAHNSVVhdlqrsqqphspevqDLLLKNKSL 517
Cdd:PHA02874  190 GESPLHNAAEYGdYACIKLLIDHGNHIMNKC-------KNGFTPLHNAIIHNRSAI---------------ELLINNASI 247


                  ...
gi 1958665568 518 VDT 520
Cdd:PHA02874  248 NDQ 250
Ank_2 pfam12796
Ankyrin repeats (3 copies);
374-462 1.77e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 46.65  E-value: 1.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665568 374 LHIAVAQGRRALSYVLARKMNALHMLDvkeHNGQSAFQVAVAANQHLIVQDLVNLGAQVNTTDcwGRTPLHVCAEKGHSQ 453
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQD---KNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN--GRTALHYAARSGHLE 75

                          90
                  ....*....|
gi 1958665568 454 VLQA-IQKGA 462
Cdd:pfam12796  76 IVKLlLEKGA 85
Ank_4 pfam13637
Ankyrin repeats (many copies);
439-496 3.65e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.57  E-value: 3.65e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665568 439 GRTPLHVCAEKGHSQVLQA-IQKGAvrsnqfvDLEATNYDGLTPLHCAVLAHN-SVVHDL 496
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLlLEKGA-------DINAVDGNGETALHFAASNGNvEVLKLL 53
Ank_4 pfam13637
Ankyrin repeats (many copies);
408-456 5.09e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.80  E-value: 5.09e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1958665568 408 SAFQVAVAANQHLIVQDLVNLGAQVNTTDCWGRTPLHVCAEKGHSQVLQ 456
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLK 51
Ank_4 pfam13637
Ankyrin repeats (many copies);
539-584 1.03e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.03  E-value: 1.03e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1958665568 539 GRTALHLAAEEANLELIRLFLELPSClsfVNAKAYNGNTALHVAAS 584
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGAD---INAVDGNGETALHFAAS 43
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 476-618 2.52e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 46.91  E-value: 2.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665568 476 YDGLTPLHCAVLAHNSVVhdlqrsqqphspevqdlllknkslvdtIKCLIQMGAAVEAKdRKSGRTALHLAAEEANLELI 555
Cdd:PHA02875   33 YDGISPIKLAMKFRDSEA---------------------------IKLLMKHGAIPDVK-YPDIESELHDAVEEGDVKAV 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958665568 556 RLFLELPSclsFVNAKAY-NGNTALHVAASLQyrvtQLDAVRLLMRKGADPSTRNLENEQPVHL 618
Cdd:PHA02875   85 EELLDLGK---FADDVFYkDGMTPLHLATILK----KLDIMKLLIARGADPDIPNTDKFSPLHL 141
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 363-554 6.62e-05

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 46.16  E-value: 6.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665568 363 FLSRDGDGDTFLHIAVAQGRRALSYVLARKMNALhmldVKE------HNGQSAFQVAVaANQHL-IVQDLVNLGAQVNT- 434
Cdd:cd22192    44 LFQRGALGETALHVAALYDNLEAAVVLMEAAPEL----VNEpmtsdlYQGETALHIAV-VNQNLnLVRELIARGADVVSp 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665568 435 ----------TDC---WGRTPLHVCAEKGHSQVLQA-IQKGAvrsnqfvDLEATNYDGLTPLHCAVLAHNSVVhdlqrsq 500
Cdd:cd22192   119 ratgtffrpgPKNliyYGEHPLSFAACVGNEEIVRLlIEHGA-------DIRAQDSLGNTVLHILVLQPNKTF------- 184

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958665568 501 qphSPEVQDLLL-----KNKSLVDTIKcliqmgaaveakdRKSGRTALHLAAEEANLEL 554
Cdd:cd22192   185 ---ACQMYDLILsydkeDDLQPLDLVP-------------NNQGLTPFKLAAKEGNIVM 227
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 515-608 1.29e-04

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 45.26  E-value: 1.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665568 515 KSLVDTIKCLIQMGAAVEAKDRKSGRTALHLAA---EEANLELIRLFLEL----PSCLSFVNAKA----YNGNTALHVAA 583
Cdd:cd21882     2 EELLGLLECLRWYLTDSAYQRGATGKTCLHKAAlnlNDGVNEAIMLLLEAapdsGNPKELVNAPCtdefYQGQTALHIAI 81

                          90       100
                  ....*....|....*....|....*
gi 1958665568 584 SLQyrvtQLDAVRLLMRKGADPSTR 608
Cdd:cd21882    82 ENR----NLNLVRLLVENGADVSAR 102
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 574-609 1.31e-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: 39.58  E-value: 1.31e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1958665568 574 NGNTALHVAAslqYRVTQLDAVRLLMRKGADPSTRN 609
Cdd:pfam00023   1 DGNTPLHLAA---GRRGNLEIVKLLLSKGADVNARD 33
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 388-604 2.08e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 44.21  E-value: 2.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665568 388 VLARKMNALHMLDVKEHNGQSAFQVAVAANQHLIVQDLVNLGAQVNTTDCWGRTPLHVCAEKGHSQVLQAIqkgaVRSNQ 467
Cdd:PHA02875   17 IARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEEL----LDLGK 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665568 468 FVDlEATNYDGLTPLHCAVLAHNSVVHD--LQRSQQPHSPEVQ-----DLLLKNKSlVDTIKCLIQMGAAVEAKDrKSGR 540
Cdd:PHA02875   93 FAD-DVFYKDGMTPLHLATILKKLDIMKllIARGADPDIPNTDkfsplHLAVMMGD-IKGIELLIDHKACLDIED-CCGC 169

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958665568 541 TALHLAAEEANLELIRLFLELPSCLSFVNAkayNGNTALHVAASLQYRVtqlDAVRLLMRKGAD 604
Cdd:PHA02875  170 TPLIIAMAKGDIAICKMLLDSGANIDYFGK---NGCVAALCYAIENNKI---DIVRLFIKRGAD 227
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 425-583 3.12e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 43.90  E-value: 3.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665568 425 LVNLGAQVNTTDCWGRTPLHVCAEKGHSQVL--QAIQKGAvrsnqfvDLEATNYDGLTPLHcavlahnsvvhdlqrsqqp 502
Cdd:PHA02876  259 LYDAGFSVNSIDDCKNTPLHHASQAPSLSRLvpKLLERGA-------DVNAKNIKGETPLY------------------- 312

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665568 503 hspevqdLLLKNKSLVDTIKCLIQMGAAVEAKDRKSgRTALHLAAE-EANLELIRLFLELPSClsfVNAKAYNGNTALHV 581
Cdd:PHA02876  313 -------LMAKNGYDTENIRTLIMLGADVNAADRLY-ITPLHQASTlDRNKDIVITLLELGAN---VNARDYCDKTPIHY 381


                  ..
gi 1958665568 582 AA 583
Cdd:PHA02876  382 AA 383
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 539-607 3.45e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 43.85  E-value: 3.45e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958665568 539 GRTALHLAAEEANLELIRLFLELPSCLSF--VNAKAYNGNTALHVAASLQyrvtQLDAVRLLMRKGADPST 607
Cdd:cd22192    51 GETALHVAALYDNLEAAVVLMEAAPELVNepMTSDLYQGETALHIAVVNQ----NLNLVRELIARGADVVS 117
Ank_2 pfam12796
Ankyrin repeats (3 copies);
365-436 3.55e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 40.10  E-value: 3.55e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958665568 365 SRDGDGDTFLHIAVAQGRRALSYVLARKMNalhmLDVKEhNGQSAFQVAVAANQHLIVQDLVNLGAQVNTTD 436
Cdd:pfam12796  25 LQDKNGRTALHLAAKNGHLEIVKLLLEHAD----VNLKD-NGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 402-560 3.89e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 43.47  E-value: 3.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665568 402 KEHNGQSAFqvavaaNQHL--------IVQDLVNLGAQVNTTDCWGRTPLHVCAEKG---HSQVLQAIQKGavrsnqfVD 470
Cdd:PHA03095  183 VDDRFRSLL------HHHLqsfkprarIVRELIRAGCDPAATDMLGNTPLHSMATGSsckRSLVLPLLIAG-------IS 249

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665568 471 LEATNYDGLTPLHCAVlAHNsvvhdlqrsqqphspevqdlllkNKSLVDtikCLIQMGAAVEAKDRkSGRTALHLAAEEA 550
Cdd:PHA03095  250 INARNRYGQTPLHYAA-VFN-----------------------NPRACR---RLIALGADINAVSS-DGNTPLSLMVRNN 301

                         170
                  ....*....|
gi 1958665568 551 NLELIRLFLE 560
Cdd:PHA03095  302 NGRAVRAALA 311
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 421-617 4.43e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 43.03  E-value: 4.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665568 421 IVQDLVNLGAQVNttdcwgrtplHVCAEKGHSqVLQAIQkgaVRSNQFVDLEATNY--DGLTPLHCAVLAHNSVVHDLQR 498
Cdd:PHA02874   50 IVELFIKHGADIN----------HINTKIPHP-LLTAIK---IGAHDIIKLLIDNGvdTSILPIPCIEKDMIKTILDCGI 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665568 499 SQQPHSPEVQDLL---LKNKSLvDTIKCLIQMGAAVEAKDrKSGRTALHLAAEEANLELIRLFLELPSclsFVNAKAYNG 575
Cdd:PHA02874  116 DVNIKDAELKTFLhyaIKKGDL-ESIKMLFEYGADVNIED-DNGCYPIHIAIKHNFFDIIKLLLEKGA---YANVKDNNG 190

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1958665568 576 NTALHVAAslqyRVTQLDAVRLLMRKGADPSTRNLENEQPVH 617
Cdd:PHA02874  191 ESPLHNAA----EYGDYACIKLLIDHGNHIMNKCKNGFTPLH 228
PHA02743 PHA02743
Viral ankyrin protein; Provisional
 521-586 7.98e-04

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 40.57  E-value: 7.98e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958665568 521 IKCLIQMGAAVEAKDRKSGRTALHLAAEEANLELIRLFLELPSclsfVNAKAYNG--NTALHVAASLQ 586
Cdd:PHA02743   76 IELLVNMGADINARELGTGNTLLHIAASTKNYELAEWLCRQLG----VNLGAINYqhETAYHIAYKMR 139
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 502-607 1.65e-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: 41.67  E-value: 1.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665568 502 PHSPEVQDLLLKNKSLVDTIKCLIQmgAAVEAKDRKsGRTALHLAAEEANLELIRLFLE------LPSCLSFVNAKA--- 572
Cdd:cd22194   107 ENTKEIVRILLAFAEENGILDRFIN--AEYTEEAYE-GQTALNIAIERRQGDIVKLLIAkgadvnAHAKGVFFNPKYkhe 183

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1958665568 573 --YNGNTALHVAASlqyrVTQLDAVRLLMRKGADPST 607
Cdd:cd22194   184 gfYFGETPLALAAC----TNQPEIVQLLMEKESTDIT 216
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 370-498 1.92e-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: 41.15  E-value: 1.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665568 370 GDTFLHIAVAQG---------RRALSYVLARKMNALHMLDVKE--HNGQSAFQVAVAANQHLIVQDLVNLGAQVNTTDCW 438
Cdd:cd22192    89 GETALHIAVVNQnlnlvreliARGADVVSPRATGTFFRPGPKNliYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSL 168

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958665568 439 GRTPLHVCaekghsqVLQAIQKgavRSNQFVDL--------------EATNYDGLTPLHCAVLAHNSVV--HDLQR 498
Cdd:cd22192   169 GNTVLHIL-------VLQPNKT---FACQMYDLilsydkeddlqpldLVPNNQGLTPFKLAAKEGNIVMfqHLVQK 234
Ank_5 pfam13857
Ankyrin repeats (many copies);
568-619 3.01e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.17  E-value: 3.01e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958665568 568 VNAKAYNGNTALHVAASLQYrvtqLDAVRLLMRKGADPSTRNLENEQPVHLV 619
Cdd:pfam13857   9 LNRLDGEGYTPLHVAAKYGA----LEIVRVLLAYGVDLNLKDEEGLTALDLA 56
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 405-613 3.95e-03

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: 40.45  E-value: 3.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665568 405 NGQSAFQVAVAANQHLIV-QDLVNLGA-QVNTTDCWGRTPLHVCAEKGHSQVLQAIQKgavrsnqfvDLEATNYDGLTPL 482
Cdd:TIGR00870  16 DEEKAFLPAAERGDLASVyRDLEEPKKlNINCPDRLGRSALFVAAIENENLELTELLL---------NLSCRGAVGDTLL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665568 483 HCAVLAHNSVVHDLQRSQQPHSPEVQDLLLKNKSLVDTIKcliqmgaaveakdrkSGRTALHLAAEEANLELIRLFLE-- 560
Cdd:TIGR00870  87 HAISLEYVDAVEAILLHLLAAFRKSGPLELANDQYTSEFT---------------PGITALHLAAHRQNYEIVKLLLErg 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958665568 561 --LP---SCLSFVNAK----AYNGNTALHVAASLqyrvTQLDAVRLLMRKGADPSTR-NLENE 613
Cdd:TIGR00870 152 asVParaCGDFFVKSQgvdsFYHGESPLNAAACL----GSPSIVALLSEDPADILTAdSLGNT 210
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 539-605 6.34e-03

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 39.48  E-value: 6.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665568 539 GRTALHLAAEEANLELIRLFLELPSClsfVNAKA-------------YNGNTALHVAASlqyrVTQLDAVRLLMRKGADP 605
Cdd:cd21882    73 GQTALHIAIENRNLNLVRLLVENGAD---VSARAtgrffrkspgnlfYFGELPLSLAAC----TNQEEIVRLLLENGAQP 145
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 539-560 9.69e-03

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.10  E-value: 9.69e-03
                           10        20
                   ....*....|....*....|..
gi 1958665568  539 GRTALHLAAEEANLELIRLFLE 560
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLD 23
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 439-581 1.00e-02

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 39.09  E-value: 1.00e-02
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665568 439 GRTPLHVCAEKGHSQVLQAIQ------KGAVRSNQFVDLEATN--YDGLTPLHCAVLAHNsvvhdlqrsqqphspevqdl 510
Cdd:cd21882    26 GKTCLHKAALNLNDGVNEAIMllleaaPDSGNPKELVNAPCTDefYQGQTALHIAIENRN-------------------- 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665568 511 llknkslVDTIKCLIQMGAAVEAKD-----RKSGRTA-------LHLAAEEANLELIRLFLELPSCLSFVNAKAYNGNTA 578
Cdd:cd21882    86 -------LNLVRLLVENGADVSARAtgrffRKSPGNLfyfgelpLSLAACTNQEEIVRLLLENGAQPAALEAQDSLGNTV 158


                  ...
gi 1958665568 579 LHV 581
Cdd:cd21882   159 LHA 161
 
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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