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Conserved domains on  [gi|226874843|ref|NP_001152867|]
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NF-kappa-B inhibitor zeta isoform b [Mus musculus]

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];
339-603 1.90e-29

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 118.13  E-value: 1.90e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226874843 339 KLANIPQDQFLARDGDGDTFLHIAVAQGRRALSYVLARKMNALHMLDIKEHNGQSAFQVAVAANQHLIVQDLVNLGAQVN 418
Cdd:COG0666    2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226874843 419 TTDCWGRTPLHVCAEKGHSQVLQA-IQKGAvrsnqfvDLEATNYDGLTPLHCAVVAHNavvhelqrnrqshspevqdlll 497
Cdd:COG0666   82 AKDDGGNTLLHAAARNGDLEIVKLlLEAGA-------DVNARDKDGETPLHLAAYNGN---------------------- 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226874843 498 rnkslVDTIKCLIQMGAAVEAKDrKSGRTALHLAAEEANLELIRLFLELPsclSFVNAKAYNGNTALHVAASLQYrvtqL 577
Cdd:COG0666  133 -----LEIVKLLLEAGADVNAQD-NDGNTPLHLAAANGNLEIVKLLLEAG---ADVNARDNDGETPLHLAAENGH----L 199

                        250       260
                 ....*....|....*....|....*.
gi 226874843 578 DAVRLLMRKGADPSTRNLENEQPVHL 603
Cdd:COG0666  200 EIVKLLLEAGADVNAKDNDGKTALDL 225
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
339-603 1.90e-29

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 118.13  E-value: 1.90e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226874843 339 KLANIPQDQFLARDGDGDTFLHIAVAQGRRALSYVLARKMNALHMLDIKEHNGQSAFQVAVAANQHLIVQDLVNLGAQVN 418
Cdd:COG0666    2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226874843 419 TTDCWGRTPLHVCAEKGHSQVLQA-IQKGAvrsnqfvDLEATNYDGLTPLHCAVVAHNavvhelqrnrqshspevqdlll 497
Cdd:COG0666   82 AKDDGGNTLLHAAARNGDLEIVKLlLEAGA-------DVNARDKDGETPLHLAAYNGN---------------------- 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226874843 498 rnkslVDTIKCLIQMGAAVEAKDrKSGRTALHLAAEEANLELIRLFLELPsclSFVNAKAYNGNTALHVAASLQYrvtqL 577
Cdd:COG0666  133 -----LEIVKLLLEAGADVNAQD-NDGNTPLHLAAANGNLEIVKLLLEAG---ADVNARDNDGETPLHLAAENGH----L 199

                        250       260
                 ....*....|....*....|....*.
gi 226874843 578 DAVRLLMRKGADPSTRNLENEQPVHL 603
Cdd:COG0666  200 EIVKLLLEAGADVNAKDNDGKTALDL 225
PHA03095 PHA03095
ankyrin-like protein; Provisional
 406-602 2.72e-15

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 78.53  E-value: 2.72e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226874843 406 IVQDLVNLGAQVNTTDCWGRTPLHVCAEKGHSQVLQAIQ----KGAvrsnqfvDLEATNYDGLTPLHCavvahnavvhel 481
Cdd:PHA03095  29 EVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIVRllleAGA-------DVNAPERCGFTPLHL------------ 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226874843 482 qrnrqshspevqdlLLRNKSLVDTIKCLIQMGAAVEAKDrKSGRTALH--LAAEEANLELIRLFLELPSClsfVNAKAYN 559
Cdd:PHA03095  90 --------------YLYNATTLDVIKLLIKAGADVNAKD-KVGRTPLHvyLSGFNINPKVIRLLLRKGAD---VNALDLY 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 226874843 560 GNTALHVAasLQYRVTQLDAVRLLMRKGADPSTRNLENEQPVH 602
Cdd:PHA03095 152 GMTPLAVL--LKSRNANVELLRLLIDAGADVYAVDDRFRSLLH 192
Ank_2 pfam12796
Ankyrin repeats (3 copies);
503-594 7.86e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.45  E-value: 7.86e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226874843  503 VDTIKCLIQMGAAVEAKDrKSGRTALHLAAEEANLELIRLFLELPSclsfVNAKaYNGNTALHVAASLQYrvtqLDAVRL 582
Cdd:pfam12796  10 LELVKLLLENGADANLQD-KNGRTALHLAAKNGHLEIVKLLLEHAD----VNLK-DNGRTALHYAARSGH----LEIVKL 79

                          90
                  ....*....|..
gi 226874843  583 LMRKGADPSTRN 594
Cdd:pfam12796  80 LLEKGADINVKD 91
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 339-539 3.92e-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: 46.54  E-value: 3.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226874843 339 KLANIPQDQFLARDGDGDTFLHIAVAQGRRALSYVLARKMNALhmldIKE------HNGQSAFQVAVaANQHL-IVQDLV 411
Cdd:cd22192   35 KLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPEL----VNEpmtsdlYQGETALHIAV-VNQNLnLVRELI 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226874843 412 NLGAQVNT-----------TDC---WGRTPLHVCAEKGHSQVLQA-IQKGAvrsnqfvDLEATNYDGLTPLHCAVvahna 476
Cdd:cd22192  110 ARGADVVSpratgtffrpgPKNliyYGEHPLSFAACVGNEEIVRLlIEHGA-------DIRAQDSLGNTVLHILV----- 177

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 226874843 477 vvheLQRNRQShSPEVQDLLLRNKSLVDTIkcliqmgaAVEAKDRKSGRTALHLAAEEANLEL 539
Cdd:cd22192  178 ----LQPNKTF-ACQMYDLILSYDKEDDLQ--------PLDLVPNNQGLTPFKLAAKEGNIVM 227
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 384-598 8.14e-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: 39.29  E-value: 8.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226874843  384 LDIKEHNGQSAFQVAVAANQHLIV-QDLVNLGA-QVNTTDCWGRTPLHVCAEKGHSQVLQAIQKgavrsnqfvDLEATNY 461
Cdd:TIGR00870  10 EESPLSDEEKAFLPAAERGDLASVyRDLEEPKKlNINCPDRLGRSALFVAAIENENLELTELLL---------NLSCRGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226874843  462 DGLTPLHCAVVA-HNAV----VHELQRNRQSHSPEvqdlllrnkslvdtikcliqmgaavEAKDRKSGR-----TALHLA 531
Cdd:TIGR00870  81 VGDTLLHAISLEyVDAVeailLHLLAAFRKSGPLE-------------------------LANDQYTSEftpgiTALHLA 135

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 226874843  532 AEEANLELIRLFLE----LP---SCLSFVNAK----AYNGNTALHVAASLqyrvTQLDAVRLLMRKGADPSTR-NLENE 598
Cdd:TIGR00870 136 AHRQNYEIVKLLLErgasVParaCGDFFVKSQgvdsFYHGESPLNAAACL----GSPSIVALLSEDPADILTAdSLGNT 210
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 524-545 9.47e-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: 9.47e-03
                           10        20
                   ....*....|....*....|..
gi 226874843   524 GRTALHLAAEEANLELIRLFLE 545
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLD 23
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
339-603 1.90e-29

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 118.13  E-value: 1.90e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226874843 339 KLANIPQDQFLARDGDGDTFLHIAVAQGRRALSYVLARKMNALHMLDIKEHNGQSAFQVAVAANQHLIVQDLVNLGAQVN 418
Cdd:COG0666    2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226874843 419 TTDCWGRTPLHVCAEKGHSQVLQA-IQKGAvrsnqfvDLEATNYDGLTPLHCAVVAHNavvhelqrnrqshspevqdlll 497
Cdd:COG0666   82 AKDDGGNTLLHAAARNGDLEIVKLlLEAGA-------DVNARDKDGETPLHLAAYNGN---------------------- 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226874843 498 rnkslVDTIKCLIQMGAAVEAKDrKSGRTALHLAAEEANLELIRLFLELPsclSFVNAKAYNGNTALHVAASLQYrvtqL 577
Cdd:COG0666  133 -----LEIVKLLLEAGADVNAQD-NDGNTPLHLAAANGNLEIVKLLLEAG---ADVNARDNDGETPLHLAAENGH----L 199

                        250       260
                 ....*....|....*....|....*.
gi 226874843 578 DAVRLLMRKGADPSTRNLENEQPVHL 603
Cdd:COG0666  200 EIVKLLLEAGADVNAKDNDGKTALDL 225
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
339-598 7.16e-28

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 113.90  E-value: 7.16e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226874843 339 KLANIPQDQFLARDGDGDTFLHIAVAQGRR-ALSYVLARKMNalhmLDIKEHNGQSAFQVAVAANQHLIVQDLVNLGAQV 417
Cdd:COG0666   71 LLLLAAGADINAKDDGGNTLLHAAARNGDLeIVKLLLEAGAD----VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADV 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226874843 418 NTTDCWGRTPLHVCAEKGHSQVLQA-IQKGAvrsnqfvDLEATNYDGLTPLHCAVVAHNavvhelqrnrqshspevqdll 496
Cdd:COG0666  147 NAQDNDGNTPLHLAAANGNLEIVKLlLEAGA-------DVNARDNDGETPLHLAAENGH--------------------- 198

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226874843 497 lrnkslVDTIKCLIQMGAAVEAKDrKSGRTALHLAAEEANLELIRLFLELpscLSFVNAKAYNGNTALHVAASLQYrvtq 576
Cdd:COG0666  199 ------LEIVKLLLEAGADVNAKD-NDGKTALDLAAENGNLEIVKLLLEA---GADLNAKDKDGLTALLLAAAAGA---- 264

                        250       260
                 ....*....|....*....|..
gi 226874843 577 LDAVRLLMRKGADPSTRNLENE 598
Cdd:COG0666  265 ALIVKLLLLALLLLAAALLDLL 286
PHA03095 PHA03095
ankyrin-like protein; Provisional
 406-602 2.72e-15

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 78.53  E-value: 2.72e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226874843 406 IVQDLVNLGAQVNTTDCWGRTPLHVCAEKGHSQVLQAIQ----KGAvrsnqfvDLEATNYDGLTPLHCavvahnavvhel 481
Cdd:PHA03095  29 EVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIVRllleAGA-------DVNAPERCGFTPLHL------------ 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226874843 482 qrnrqshspevqdlLLRNKSLVDTIKCLIQMGAAVEAKDrKSGRTALH--LAAEEANLELIRLFLELPSClsfVNAKAYN 559
Cdd:PHA03095  90 --------------YLYNATTLDVIKLLIKAGADVNAKD-KVGRTPLHvyLSGFNINPKVIRLLLRKGAD---VNALDLY 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 226874843 560 GNTALHVAasLQYRVTQLDAVRLLMRKGADPSTRNLENEQPVH 602
Cdd:PHA03095 152 GMTPLAVL--LKSRNANVELLRLLIDAGADVYAVDDRFRSLLH 192
Ank_2 pfam12796
Ankyrin repeats (3 copies);
503-594 7.86e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.45  E-value: 7.86e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226874843  503 VDTIKCLIQMGAAVEAKDrKSGRTALHLAAEEANLELIRLFLELPSclsfVNAKaYNGNTALHVAASLQYrvtqLDAVRL 582
Cdd:pfam12796  10 LELVKLLLENGADANLQD-KNGRTALHLAAKNGHLEIVKLLLEHAD----VNLK-DNGRTALHYAARSGH----LEIVKL 79

                          90
                  ....*....|..
gi 226874843  583 LMRKGADPSTRN 594
Cdd:pfam12796  80 LLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 406-589 6.89e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 67.77  E-value: 6.89e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226874843 406 IVQDLVNLGAQVNTTDCWGRTPLHVCAEK--GHSQVLQA-IQKGAvrsnqfvDLEATNYDGLTPLHcAVVAHNAVvhELq 482
Cdd:PHA03100  88 IVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYlLDNGA-------NVNIKNSDGENLLH-LYLESNKI--DL- 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226874843 483 rnrqshspEVQDLLLRNKSLV---DTIKCLIQMGAAVEAKDRKsGRTALHLAAEEANLELIRLFLELPsclSFVNAKAYN 559
Cdd:PHA03100 157 --------KILKLLIDKGVDInakNRVNYLLSYGVPINIKDVY-GFTPLHYAVYNNNPEFVKYLLDLG---ANPNLVNKY 224

                        170       180       190
                 ....*....|....*....|....*....|
gi 226874843 560 GNTALHVAASLQYrvtqLDAVRLLMRKGAD 589
Cdd:PHA03100 225 GDTPLHIAILNNN----KEIFKLLLNNGPS 250
PHA03095 PHA03095
ankyrin-like protein; Provisional
 406-601 1.64e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 66.97  E-value: 1.64e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226874843 406 IVQDLVNLGAQVNTTDCWGRTPLHVCAeKG---HSQVLQA-IQKGAvrsnqfvDLEATNYDGLTPLHCAVVAHNAvvhel 481
Cdd:PHA03095  99 VIKLLIKAGADVNAKDKVGRTPLHVYL-SGfniNPKVIRLlLRKGA-------DVNALDLYGMTPLAVLLKSRNA----- 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226874843 482 qrnrqshSPEVQDLLL-----------RNKSLVDT-----------IKCLIQMGAAVEAKDRkSGRTALHLAAEEANLEL 539
Cdd:PHA03095 166 -------NVELLRLLIdagadvyavddRFRSLLHHhlqsfkprariVRELIRAGCDPAATDM-LGNTPLHSMATGSSCKR 237

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 226874843 540 IRLFLELPSCLSfVNAKAYNGNTALHVAASLQYRVtqldAVRLLMRKGADPSTRNLENEQPV 601
Cdd:PHA03095 238 SLVLPLLIAGIS-INARNRYGQTPLHYAAVFNNPR----ACRRLIALGADINAVSSDGNTPL 294
Ank_2 pfam12796
Ankyrin repeats (3 copies);
395-481 2.20e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 57.43  E-value: 2.20e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226874843  395 FQVAVAANQHLIVQDLVNLGAQVNTTDCWGRTPLHVCAEKGHSQVLQA-IQKGAVRSnqfvdleatNYDGLTPLHCAVVA 473
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLlLEHADVNL---------KDNGRTALHYAARS 71


                  ....*....
gi 226874843  474 -HNAVVHEL 481
Cdd:pfam12796  72 gHLEIVKLL 80
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 381-603 6.63e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 61.82  E-value: 6.63e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226874843 381 LHMLDIKEHNGQSA-------FQVAVAANQHLIVQDLVNLGAQVNTTDCWGRTPLHV-CAE---KGHSQVLQAIQKGAVr 449
Cdd:PHA02878  20 IEYIDHTENYSTSAslipfipLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIiCKEpnkLGMKEMIRSINKCSV- 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226874843 450 SNQFVDL-EATNYDGLTplhcavvahnaVVHELQRNRQSHSPEVQDLLLRNKSLVDTI-----KCLIQMGAAVEAKDRKS 523
Cdd:PHA02878  99 FYTLVAIkDAFNNRNVE-----------IFKIILTNRYKNIQTIDLVYIDKKSKDDIIeaeitKLLLSYGADINMKDRHK 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226874843 524 GRTALHLAAEEANLELIRLFLelpSCLSFVNAKAYNGNTALHVAASlQYRVtqlDAVRLLMRKGADPSTRNLENEQPVHL 603
Cdd:PHA02878 168 GNTALHYATENKDQRLTELLL---SYGANVNIPDKTNNSPLHHAVK-HYNK---PIVHILLENGASTDARDKCGNTPLHI 240
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 399-602 2.41e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 60.46  E-value: 2.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226874843 399 VAANQHLIVQDLVNLGAQVNTTDCWGRTPLHVCAEKGHSQVLQ-AIQKGAvrsnqfvDLEATNYDGLTPLHCAVVAHNA- 476
Cdd:PHA02876 153 IQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNlLLSYGA-------DVNIIALDDLSVLECAVDSKNId 225

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226874843 477 VVHELQRNRQSHSPEVQDLL--LRNKSLvDTIKCLIQMGAAVEAKDrKSGRTALHLAAEEANLEliRLFLELPSCLSFVN 554
Cdd:PHA02876 226 TIKAIIDNRSNINKNDLSLLkaIRNEDL-ETSLLLYDAGFSVNSID-DCKNTPLHHASQAPSLS--RLVPKLLERGADVN 301

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 226874843 555 AKAYNGNTALHVAASLQYrvtQLDAVRLLMRKGADPSTRNLENEQPVH 602
Cdd:PHA02876 302 AKNIKGETPLYLMAKNGY---DTENIRTLIMLGADVNAADRLYITPLH 346
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 351-531 4.41e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 55.74  E-value: 4.41e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226874843 351 RDGDGDTFLHIAVAQGrralsyvlarKMNALHML-------DIKEHNGQSAFQVAVAANQHLIVQDLVNLGAQVNTTDCW 423
Cdd:PHA02874 120 KDAELKTFLHYAIKKG----------DLESIKMLfeygadvNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNN 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226874843 424 GRTPLHVCAEKG-HSQVLQAIQKGAVRSNQFvdleatnYDGLTPLHCAVVAHNAVVHELQRNRqshSPEVQDL------- 495
Cdd:PHA02874 190 GESPLHNAAEYGdYACIKLLIDHGNHIMNKC-------KNGFTPLHNAIIHNRSAIELLINNA---SINDQDIdgstplh 259

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 226874843 496 -LLRNKSLVDTIKCLIQMGAAVEAKDRKsGRTALHLA 531
Cdd:PHA02874 260 hAINPPCDIDIIDILLYHKADISIKDNK-GENPIDTA 295
Ank_2 pfam12796
Ankyrin repeats (3 copies);
428-545 5.82e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 50.50  E-value: 5.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226874843  428 LHVCAEKGHSQVLQA-IQKGAvrsnqfvDLEATNYDGLTPLHCAVVAHNavvhelqrnrqshspevqdlllrnkslVDTI 506
Cdd:pfam12796   1 LHLAAKNGNLELVKLlLENGA-------DANLQDKNGRTALHLAAKNGH---------------------------LEIV 46

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 226874843  507 KCLIQmgaAVEAKDRKSGRTALHLAAEEANLELIRLFLE 545
Cdd:pfam12796  47 KLLLE---HADVNLKDNGRTALHYAARSGHLEIVKLLLE 82
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 406-602 1.00e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 55.07  E-value: 1.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226874843 406 IVQDLVNLGAQVNTTDCWGRTPLHVCAEKGH--SQVLQAIQKGAvrsnqfvDLEATNYDGLTPLHCAVVahnavvheLQR 483
Cdd:PHA02876 289 LVPKLLERGADVNAKNIKGETPLYLMAKNGYdtENIRTLIMLGA-------DVNAADRLYITPLHQAST--------LDR 353

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226874843 484 NRqshspevqdlllrnkslvDTIKCLIQMGAAVEAKDRKSgRTALHLAAEEANLELIRLFLELPSCLSFVNAKAyngNTA 563
Cdd:PHA02876 354 NK------------------DIVITLLELGANVNARDYCD-KTPIHYAAVRNNVVIINTLLDYGADIEALSQKI---GTA 411

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 226874843 564 LHVAAslqYRVTQLDAVRLLMRKGADPSTRNLENEQPVH 602
Cdd:PHA02876 412 LHFAL---CGTNPYMSVKTLIDRGANVNSKNKDLSTPLH 447
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 504-602 2.91e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 53.43  E-value: 2.91e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226874843 504 DTIKCLIQMGAAVEAKDRKSgRTALHLAAEEANLELIRLFLELPSClsfVNAKAYNGNTALHVAAslqyRVTQLDAVRLL 583
Cdd:PHA02874 105 DMIKTILDCGIDVNIKDAEL-KTFLHYAIKKGDLESIKMLFEYGAD---VNIEDDNGCYPIHIAI----KHNFFDIIKLL 176

                         90
                 ....*....|....*....
gi 226874843 584 MRKGADPSTRNLENEQPVH 602
Cdd:PHA02874 177 LEKGAYANVKDNNGESPLH 195
Ank_2 pfam12796
Ankyrin repeats (3 copies);
359-447 1.72e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 46.65  E-value: 1.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226874843  359 LHIAVAQGRRALSYVLARKMNALHMLDikeHNGQSAFQVAVAANQHLIVQDLVNLGAQVNTTDcwGRTPLHVCAEKGHSQ 438
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQD---KNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN--GRTALHYAARSGHLE 75

                          90
                  ....*....|
gi 226874843  439 VLQA-IQKGA 447
Cdd:pfam12796  76 IVKLlLEKGA 85
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 376-627 1.88e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 51.02  E-value: 1.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226874843 376 RKMNALHMLDIKEHNGQSAFQVAVAAN--------QHLIVQDLVNLGAQVNTTDCWGRTPLHVCAEKGHSQVLQAIQKGA 447
Cdd:PLN03192 502 KELHDLNVGDLLGDNGGEHDDPNMASNlltvastgNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHA 581

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226874843 448 VRsnqfVDLEATNydGLTPLHCAVVA-HNAVVHELQRNRQSHSPEVQ-DLLL----RNKslVDTIKCLIQMGAAVEAKDR 521
Cdd:PLN03192 582 CN----VHIRDAN--GNTALWNAISAkHHKIFRILYHFASISDPHAAgDLLCtaakRND--LTAMKELLKQGLNVDSEDH 653

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226874843 522 KsGRTALHLAAEEANLELIRLFLElpsclsfvnakayngNTALHVAASLQYRVTQLDAVRLLMRKGADPSTRNLENEQPV 601
Cdd:PLN03192 654 Q-GATALQVAMAEDHVDMVRLLIM---------------NGADVDKANTDDDFSPTELRELLQKRELGHSITIVDSVPAD 717

                        250       260
                 ....*....|....*....|....*.
gi 226874843 602 HLVPDGPVGEQIRRILKGKSIQQRAP 627
Cdd:PLN03192 718 EPDLGRDGGSRPGRLQGTSSDNQCRP 743
Ank_4 pfam13637
Ankyrin repeats (many copies);
393-441 4.97e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.80  E-value: 4.97e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 226874843  393 SAFQVAVAANQHLIVQDLVNLGAQVNTTDCWGRTPLHVCAEKGHSQVLQ 441
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLK 51
Ank_4 pfam13637
Ankyrin repeats (many copies);
524-569 1.01e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.03  E-value: 1.01e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 226874843  524 GRTALHLAAEEANLELIRLFLELPSClsfVNAKAYNGNTALHVAAS 569
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGAD---INAVDGNGETALHFAAS 43
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 489-603 1.10e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 48.06  E-value: 1.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226874843 489 SPEVQDLLLRNkslVDTIKCLIQMGAAVEAKdRKSGRTALHLAAEEANLELIRLFLELPSclsFVNAKAY-NGNTALHVA 567
Cdd:PHA02875  37 SPIKLAMKFRD---SEAIKLLMKHGAIPDVK-YPDIESELHDAVEEGDVKAVEELLDLGK---FADDVFYkDGMTPLHLA 109

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 226874843 568 ASLQyrvtQLDAVRLLMRKGADPSTRNLENEQPVHL 603
Cdd:PHA02875 110 TILK----KLDIMKLLIARGADPDIPNTDKFSPLHL 141
Ank_4 pfam13637
Ankyrin repeats (many copies);
424-471 2.09e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.26  E-value: 2.09e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 226874843  424 GRTPLHVCAEKGHSQVLQA-IQKGAvrsnqfvDLEATNYDGLTPLHCAV 471
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLlLEKGA-------DINAVDGNGETALHFAA 42
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 339-539 3.92e-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: 46.54  E-value: 3.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226874843 339 KLANIPQDQFLARDGDGDTFLHIAVAQGRRALSYVLARKMNALhmldIKE------HNGQSAFQVAVaANQHL-IVQDLV 411
Cdd:cd22192   35 KLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPEL----VNEpmtsdlYQGETALHIAV-VNQNLnLVRELI 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226874843 412 NLGAQVNT-----------TDC---WGRTPLHVCAEKGHSQVLQA-IQKGAvrsnqfvDLEATNYDGLTPLHCAVvahna 476
Cdd:cd22192  110 ARGADVVSpratgtffrpgPKNliyYGEHPLSFAACVGNEEIVRLlIEHGA-------DIRAQDSLGNTVLHILV----- 177

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 226874843 477 vvheLQRNRQShSPEVQDLLLRNKSLVDTIkcliqmgaAVEAKDRKSGRTALHLAAEEANLEL 539
Cdd:cd22192  178 ----LQPNKTF-ACQMYDLILSYDKEDDLQ--------PLDLVPNNQGLTPFKLAAKEGNIVM 227
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 355-488 4.20e-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: 46.54  E-value: 4.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226874843 355 GDTFLHIAVAQG---------RRALSYVLARKMNALHMLDIKE--HNGQSAFQVAVAANQHLIVQDLVNLGAQVNTTDCW 423
Cdd:cd22192   89 GETALHIAVVNQnlnlvreliARGADVVSPRATGTFFRPGPKNliYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSL 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226874843 424 GRTPLHVCaekghsqVLQAIQKgavRSNQFVDL--------------EATNYDGLTPLHCAVVAHNAVV--HELQRNRQS 487
Cdd:cd22192  169 GNTVLHIL-------VLQPNKT---FACQMYDLilsydkeddlqpldLVPNNQGLTPFKLAAKEGNIVMfqHLVQKRRHI 238


                 .
gi 226874843 488 H 488
Cdd:cd22192  239 Q 239
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 381-536 7.23e-05

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 45.77  E-value: 7.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226874843 381 LHMLDIKEHNGQSAFQVA----VAANQHLIVQDLVNL---GAQvnttdcwGRTPLHVCAEKGHSQVLQAIQKGAVRsnqF 453
Cdd:cd22192    8 LHLLQQKRISESPLLLAAkendVQAIKKLLKCPSCDLfqrGAL-------GETALHVAALYDNLEAAVVLMEAAPE---L 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226874843 454 VDLEATN--YDGLTPLHCAVVAHN-AVVHEL-QRNRQSHSPEVQDL--LLRNKSLV----------------DTIKCLIQ 511
Cdd:cd22192   78 VNEPMTSdlYQGETALHIAVVNQNlNLVRELiARGADVVSPRATGTffRPGPKNLIyygehplsfaacvgneEIVRLLIE 157

                        170       180
                 ....*....|....*....|....*
gi 226874843 512 MGAAVEAKDRKsGRTALHLAAEEAN 536
Cdd:cd22192  158 HGADIRAQDSL-GNTVLHILVLQPN 181
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 373-589 7.90e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 45.37  E-value: 7.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226874843 373 VLARKMNALHMLDIKEHNGQSAFQVAVAANQHLIVQDLVNLGAQVNTTDCWGRTPLHVCAEKGHSQVLQAIqkgaVRSNQ 452
Cdd:PHA02875  17 IARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEEL----LDLGK 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226874843 453 FVDlEATNYDGLTPLHCAVVAHNAVVHELQRNRQShSPEVQD--------LLLRNKSlVDTIKCLIQMGAAVEAKDrKSG 524
Cdd:PHA02875  93 FAD-DVFYKDGMTPLHLATILKKLDIMKLLIARGA-DPDIPNtdkfsplhLAVMMGD-IKGIELLIDHKACLDIED-CCG 168

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 226874843 525 RTALHLAAEEANLELIRLFLELPSCLSFVNAkayNGNTALHVAASLQYRVtqlDAVRLLMRKGAD 589
Cdd:PHA02875 169 CTPLIIAMAKGDIAICKMLLDSGANIDYFGK---NGCVAALCYAIENNKI---DIVRLFIKRGAD 227
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 500-593 1.25e-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: 1.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226874843 500 KSLVDTIKCLIQMGAAVEAKDRKSGRTALHLAA---EEANLELIRLFLEL----PSCLSFVNAKA----YNGNTALHVAA 568
Cdd:cd21882    2 EELLGLLECLRWYLTDSAYQRGATGKTCLHKAAlnlNDGVNEAIMLLLEAapdsGNPKELVNAPCtdefYQGQTALHIAI 81

                         90       100
                 ....*....|....*....|....*
gi 226874843 569 SLQyrvtQLDAVRLLMRKGADPSTR 593
Cdd:cd21882   82 ENR----NLNLVRLLVENGADVSAR 102
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 559-594 1.29e-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: 1.29e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 226874843  559 NGNTALHVAAslqYRVTQLDAVRLLMRKGADPSTRN 594
Cdd:pfam00023   1 DGNTPLHLAA---GRRGNLEIVKLLLSKGADVNARD 33
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 478-592 1.93e-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: 44.62  E-value: 1.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226874843 478 VHELQRNRQSHSPevqdLLLRNK-SLVDTIKCLI--------QMGAAveakdrksGRTALHLAAEEANLELIRLFLELPS 548
Cdd:cd22192    8 LHLLQQKRISESP----LLLAAKeNDVQAIKKLLkcpscdlfQRGAL--------GETALHVAALYDNLEAAVVLMEAAP 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 226874843 549 CLSF--VNAKAYNGNTALHVAASLQyrvtQLDAVRLLMRKGADPST 592
Cdd:cd22192   76 ELVNepMTSDLYQGETALHIAVVNQ----NLNLVRELIARGADVVS 117
Ank_2 pfam12796
Ankyrin repeats (3 copies);
351-421 3.89e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 39.71  E-value: 3.89e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 226874843  351 RDGDGDTFLHIAVAQGRRALSYVLARKMNalhmLDIKEhNGQSAFQVAVAANQHLIVQDLVNLGAQVNTTD 421
Cdd:pfam12796  26 QDKNGRTALHLAAKNGHLEIVKLLLEHAD----VNLKD-NGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 406-602 6.23e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 42.64  E-value: 6.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226874843 406 IVQDLVNLGAQVNttdcwgrtplHVCAEKGHSqVLQAIQkgaVRSNQFVDLEATNYDGLTPLHCAVVAHNAVVHELQ--- 482
Cdd:PHA02874  50 IVELFIKHGADIN----------HINTKIPHP-LLTAIK---IGAHDIIKLLIDNGVDTSILPIPCIEKDMIKTILDcgi 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226874843 483 ----RNRQSHSpeVQDLLLRNKSLvDTIKCLIQMGAAVEAKDrKSGRTALHLAAEEANLELIRLFLELPSclsFVNAKAY 558
Cdd:PHA02874 116 dvniKDAELKT--FLHYAIKKGDL-ESIKMLFEYGADVNIED-DNGCYPIHIAIKHNFFDIIKLLLEKGA---YANVKDN 188

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 226874843 559 NGNTALHVAAslqyRVTQLDAVRLLMRKGADPSTRNLENEQPVH 602
Cdd:PHA02874 189 NGESPLHNAA----EYGDYACIKLLIDHGNHIMNKCKNGFTPLH 228
PHA02743 PHA02743
Viral ankyrin protein; Provisional
 506-571 6.31e-04

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 40.95  E-value: 6.31e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 226874843 506 IKCLIQMGAAVEAKDRKSGRTALHLAAEEANLELIRLFLELPSclsfVNAKAYNG--NTALHVAASLQ 571
Cdd:PHA02743  76 IELLVNMGADINARELGTGNTLLHIAASTKNYELAEWLCRQLG----VNLGAINYqhETAYHIAYKMR 139
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 484-592 1.41e-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: 1.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226874843 484 NRQSHSPEVQDLLLRNKSLVDTIKCLIQmgAAVEAKDRKsGRTALHLAAEEANLELIRLFLE------LPSCLSFVNAKA 557
Cdd:cd22194  104 NINENTKEIVRILLAFAEENGILDRFIN--AEYTEEAYE-GQTALNIAIERRQGDIVKLLIAkgadvnAHAKGVFFNPKY 180

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 226874843 558 -----YNGNTALHVAASlqyrVTQLDAVRLLMRKGADPST 592
Cdd:cd22194  181 khegfYFGETPLALAAC----TNQPEIVQLLMEKESTDIT 216
Ank_5 pfam13857
Ankyrin repeats (many copies);
553-604 2.94e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.17  E-value: 2.94e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 226874843  553 VNAKAYNGNTALHVAASLQYrvtqLDAVRLLMRKGADPSTRNLENEQPVHLV 604
Cdd:pfam13857   9 LNRLDGEGYTPLHVAAKYGA----LEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 424-566 3.43e-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: 40.25  E-value: 3.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226874843 424 GRTPLHVCAEKGHSQVLQAIQ------KGAVRSNQFVDLEATN--YDGLTPLHCAVVAhnavvhelqrnrqshspevqdl 495
Cdd:cd21882   26 GKTCLHKAALNLNDGVNEAIMllleaaPDSGNPKELVNAPCTDefYQGQTALHIAIEN---------------------- 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226874843 496 llRNKSLVdtiKCLIQMGAAVEAKD-----RKSGRTA-------LHLAAEEANLELIRLFLELPSCLSFVNAKAYNGNTA 563
Cdd:cd21882   84 --RNLNLV---RLLVENGADVSARAtgrffRKSPGNLfyfgelpLSLAACTNQEEIVRLLLENGAQPAALEAQDSLGNTV 158


                 ...
gi 226874843 564 LHV 566
Cdd:cd21882  159 LHA 161
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 326-594 3.56e-03

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 40.67  E-value: 3.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226874843 326 KSFFQWQVEQEESKLANIPQDqfLARDGDGDTFLHIAVAQGRRALSYVLARKMNALHMLDIKEHNGQSAFQV--AVAANQ 403
Cdd:PHA02716 111 KQFYKQIIKDNKSKTANHVFD--IPNNGDMDILYTYFNSPNTRGIDLDLIKYMVDVGIVNLNYVCKKTGYGIlhAYLGNM 188

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226874843 404 HL---IVQDLVNLGAQVNTTDCWGRTPLHVCAEKGH---SQVLQAIQKGAVRsnqfvDLEATNydGLTPLHCAVV----- 472
Cdd:PHA02716 189 YVdidILEWLCNNGVNVNLQNNHLITPLHTYLITGNvcaSVIKKIIELGGDM-----DMKCVN--GMSPIMTYIInidni 261

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226874843 473 ---AHNAVVHELQRNRQSHSPEVQDL---LLRNKSlVDTIKCLIQMGAAVEAKDrKSGRTALH--LAAEEANLELIRLFL 544
Cdd:PHA02716 262 npeITNIYIESLDGNKVKNIPMILHSyitLARNID-ISVVYSFLQPGVKLHYKD-SAGRTCLHqyILRHNISTDIIKLLH 339

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 226874843 545 ELPSclsFVNAKAYNGNTALHVAASLQYRVT----------QLDAVRLLMRKGADPSTRN 594
Cdd:PHA02716 340 EYGN---DLNEPDNIGNTVLHTYLSMLSVVNildpetdndiRLDVIQCLISLGADITAVN 396
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 524-590 6.15e-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: 6.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226874843 524 GRTALHLAAEEANLELIRLFLELPSClsfVNAKA-------------YNGNTALHVAASlqyrVTQLDAVRLLMRKGADP 590
Cdd:cd21882   73 GQTALHIAIENRNLNLVRLLVENGAD---VSARAtgrffrkspgnlfYFGELPLSLAAC----TNQEEIVRLLLENGAQP 145
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 384-598 8.14e-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: 39.29  E-value: 8.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226874843  384 LDIKEHNGQSAFQVAVAANQHLIV-QDLVNLGA-QVNTTDCWGRTPLHVCAEKGHSQVLQAIQKgavrsnqfvDLEATNY 461
Cdd:TIGR00870  10 EESPLSDEEKAFLPAAERGDLASVyRDLEEPKKlNINCPDRLGRSALFVAAIENENLELTELLL---------NLSCRGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226874843  462 DGLTPLHCAVVA-HNAV----VHELQRNRQSHSPEvqdlllrnkslvdtikcliqmgaavEAKDRKSGR-----TALHLA 531
Cdd:TIGR00870  81 VGDTLLHAISLEyVDAVeailLHLLAAFRKSGPLE-------------------------LANDQYTSEftpgiTALHLA 135

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 226874843  532 AEEANLELIRLFLE----LP---SCLSFVNAK----AYNGNTALHVAASLqyrvTQLDAVRLLMRKGADPSTR-NLENE 598
Cdd:TIGR00870 136 AHRQNYEIVKLLLErgasVParaCGDFFVKSQgvdsFYHGESPLNAAACL----GSPSIVALLSEDPADILTAdSLGNT 210
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 524-545 9.47e-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: 9.47e-03
                           10        20
                   ....*....|....*....|..
gi 226874843   524 GRTALHLAAEEANLELIRLFLE 545
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLD 23
 
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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