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Conserved domains on  [gi|126517480|ref|NP_001075440|]
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ankyrin repeat domain-containing protein 63 [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];
12-173 2.45e-30

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 117.75  E-value: 2.45e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126517480  12 GTRTFLEAMQAGKVHLARFVLDAldRSIIDCRAEQGRTPLMVAVGLPDPAMrsrfVRLLLEQGAAVNLRDERGRTALSLA 91
Cdd:COG0666   87 GNTLLHAAARNGDLEIVKLLLEA--GADVNARDKDGETPLHLAAYNGNLEI----VKLLLEAGADVNAQDNDGNTPLHLA 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126517480  92 CERGHLDAVQLLVQFSGDPEATDSAGNSPVMWAAACGHGAVLEFLVrsfrRLGLRLDRTNRAGLTALQLAASRGHGTCVQ 171
Cdd:COG0666  161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLL----EAGADVNAKDNDGKTALDLAAENGNLEIVK 236


                 ..
gi 126517480 172 AL 173
Cdd:COG0666  237 LL 238
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
12-173 2.45e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 117.75  E-value: 2.45e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126517480  12 GTRTFLEAMQAGKVHLARFVLDAldRSIIDCRAEQGRTPLMVAVGLPDPAMrsrfVRLLLEQGAAVNLRDERGRTALSLA 91
Cdd:COG0666   87 GNTLLHAAARNGDLEIVKLLLEA--GADVNARDKDGETPLHLAAYNGNLEI----VKLLLEAGADVNAQDNDGNTPLHLA 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126517480  92 CERGHLDAVQLLVQFSGDPEATDSAGNSPVMWAAACGHGAVLEFLVrsfrRLGLRLDRTNRAGLTALQLAASRGHGTCVQ 171
Cdd:COG0666  161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLL----EAGADVNAKDNDGKTALDLAAENGNLEIVK 236


                 ..
gi 126517480 172 AL 173
Cdd:COG0666  237 LL 238
Ank_2 pfam12796
Ankyrin repeats (3 copies);
51-137 4.93e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.84  E-value: 4.93e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126517480   51 LMVAVGLPDPAMrsrfVRLLLEQGAAVNLRDERGRTALSLACERGHLDAVQLLVQFsGDPEATDSaGNSPVMWAAACGHG 130
Cdd:pfam12796   1 LHLAAKNGNLEL----VKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHL 74


                  ....*..
gi 126517480  131 AVLEFLV 137
Cdd:pfam12796  75 EIVKLLL 81
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 67-138 5.93e-12

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 67.23  E-value: 5.93e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 126517480  67 VRLLLEQGAAVNLRDERGRTALSLACERGHLDAVQLLVQFSGDPEATDSAGNSPVMWAAACGHGAVLEFLVR 138
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 19-165 6.00e-06

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 48.09  E-value: 6.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126517480  19 AMQAGKVHLARFVLDALDRSI---IDCRAEQGRTPLMVAVGLPDPAMrsrfVRLLLEQGAAVN--------LRDER---- 83
Cdd:cd22192   58 AALYDNLEAAVVLMEAAPELVnepMTSDLYQGETALHIAVVNQNLNL----VRELIARGADVVspratgtfFRPGPknli 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126517480  84 --GRTALSLACERGHLDAVQLLVQFSGDPEATDSAGNSP----VMWAA---ACghgAVLEFLVRSFRRLGL-RLDR-TNR 152
Cdd:cd22192  134 yyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVlhilVLQPNktfAC---QMYDLILSYDKEDDLqPLDLvPNN 210

                        170
                 ....*....|...
gi 126517480 153 AGLTALQLAASRG 165
Cdd:cd22192  211 QGLTPFKLAAKEG 223
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 47-165 3.48e-04

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 42.76  E-value: 3.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126517480   47 GRTPLMVAvglpdpAMRSRF--VRLLLEQGAAVNLR---DE-----------RGRTALSLACERGHLDAVQLLVQFSGDP 110
Cdd:TIGR00870 128 GITALHLA------AHRQNYeiVKLLLERGASVPARacgDFfvksqgvdsfyHGESPLNAAACLGSPSIVALLSEDPADI 201

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 126517480  111 EATDSAGNSPVmwaaacgHGAVLEF--------LVRSFRRLGLRLDR-----------TNRAGLTALQLAASRG 165
Cdd:TIGR00870 202 LTADSLGNTLL-------HLLVMENefkaeyeeLSCQMYNFALSLLDklrdskeleviLNHQGLTPLKLAAKEG 268
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 83-112 1.07e-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: 36.03  E-value: 1.07e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 126517480    83 RGRTALSLACERGHLDAVQLLVQFSGDPEA 112
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
12-173 2.45e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 117.75  E-value: 2.45e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126517480  12 GTRTFLEAMQAGKVHLARFVLDAldRSIIDCRAEQGRTPLMVAVGLPDPAMrsrfVRLLLEQGAAVNLRDERGRTALSLA 91
Cdd:COG0666   87 GNTLLHAAARNGDLEIVKLLLEA--GADVNARDKDGETPLHLAAYNGNLEI----VKLLLEAGADVNAQDNDGNTPLHLA 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126517480  92 CERGHLDAVQLLVQFSGDPEATDSAGNSPVMWAAACGHGAVLEFLVrsfrRLGLRLDRTNRAGLTALQLAASRGHGTCVQ 171
Cdd:COG0666  161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLL----EAGADVNAKDNDGKTALDLAAENGNLEIVK 236


                 ..
gi 126517480 172 AL 173
Cdd:COG0666  237 LL 238
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
12-173 1.06e-25

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 105.04  E-value: 1.06e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126517480  12 GTRTFLEAMQAGKVHLARFVLDA-LDrsiIDCRAEQGRTPLMVAVGLPDPAMrsrfVRLLLEQGAAVNLRDERGRTALSL 90
Cdd:COG0666  120 GETPLHLAAYNGNLEIVKLLLEAgAD---VNAQDNDGNTPLHLAAANGNLEI----VKLLLEAGADVNARDNDGETPLHL 192

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126517480  91 ACERGHLDAVQLLVQFSGDPEATDSAGNSPVMWAAACGHGAVLEFLvrsfRRLGLRLDRTNRAGLTALQLAASRGHGTCV 170
Cdd:COG0666  193 AAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLL----LEAGADLNAKDKDGLTALLLAAAAGAALIV 268


                 ...
gi 126517480 171 QAL 173
Cdd:COG0666  269 KLL 271
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
15-173 1.29e-19

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 88.09  E-value: 1.29e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126517480  15 TFLEAMQAGKVHLARFVLDALDRSIIDCRAEQGRTPLMVAVGLPDPAMrsrfVRLLLEQGAAVNLRDERGRTALSLACER 94
Cdd:COG0666   22 ALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLV----ALLLLAAGADINAKDDGGNTLLHAAARN 97

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 126517480  95 GHLDAVQLLVQFSGDPEATDSAGNSPVMWAAACGHGAVLEFLVRSfrrlGLRLDRTNRAGLTALQLAASRGHGTCVQAL 173
Cdd:COG0666   98 GDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA----GADVNAQDNDGNTPLHLAAANGNLEIVKLL 172
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
19-153 3.02e-16

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 78.46  E-value: 3.02e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126517480  19 AMQAGKVHLARFVLDAldRSIIDCRAEQGRTPLMVAVGLPDPAMrsrfVRLLLEQGAAVNLRDERGRTALSLACERGHLD 98
Cdd:COG0666  160 AAANGNLEIVKLLLEA--GADVNARDNDGETPLHLAAENGHLEI----VKLLLEAGADVNAKDNDGKTALDLAAENGNLE 233

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 126517480  99 AVQLLVQFSGDPEATDSAGNSPVMWAAACGHGAVLEFLVRSFRRLGLRLDRTNRA 153
Cdd:COG0666  234 IVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
Ank_2 pfam12796
Ankyrin repeats (3 copies);
51-137 4.93e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.84  E-value: 4.93e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126517480   51 LMVAVGLPDPAMrsrfVRLLLEQGAAVNLRDERGRTALSLACERGHLDAVQLLVQFsGDPEATDSaGNSPVMWAAACGHG 130
Cdd:pfam12796   1 LHLAAKNGNLEL----VKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHL 74


                  ....*..
gi 126517480  131 AVLEFLV 137
Cdd:pfam12796  75 EIVKLLL 81
Ank_2 pfam12796
Ankyrin repeats (3 copies);
88-173 1.95e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 68.22  E-value: 1.95e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126517480   88 LSLACERGHLDAVQLLVQFSGDPEATDSAGNSPVMWAAACGHGAVLEFLVRSFRrlglrLDRTNRaGLTALQLAASRGHG 167
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD-----VNLKDN-GRTALHYAARSGHL 74


                  ....*.
gi 126517480  168 TCVQAL 173
Cdd:pfam12796  75 EIVKLL 80
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 67-138 5.93e-12

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 67.23  E-value: 5.93e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 126517480  67 VRLLLEQGAAVNLRDERGRTALSLACERGHLDAVQLLVQFSGDPEATDSAGNSPVMWAAACGHGAVLEFLVR 138
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
Ank_2 pfam12796
Ankyrin repeats (3 copies);
40-114 7.30e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 55.51  E-value: 7.30e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 126517480   40 IDCRAEQGRTPLMVAV--GLPDpamrsrFVRLLLEQgAAVNLRDErGRTALSLACERGHLDAVQLLVQFSGDPEATD 114
Cdd:pfam12796  23 ANLQDKNGRTALHLAAknGHLE------IVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
Ank_4 pfam13637
Ankyrin repeats (many copies);
84-137 8.18e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.20  E-value: 8.18e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 126517480   84 GRTALSLACERGHLDAVQLLVQFSGDPEATDSAGNSPVMWAAACGHGAVLEFLV 137
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 10-173 7.16e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 54.49  E-value: 7.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126517480  10 RAGTRTFLEAMQAGK----VHLARFV---LDALDRSIIDCRAEQGR---TPLMVAVGLPDPAM-RSRFVRLLLEQGAAVN 78
Cdd:PLN03192 473 RLKTSTLIEAMQTRQednvVILKNFLqhhKELHDLNVGDLLGDNGGehdDPNMASNLLTVASTgNAALLEELLKAKLDPD 552

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126517480  79 LRDERGRTALSLACERGHLDAVQLLVQFSGDPEATDSAGNSpVMW-AAACGHGAVLEFL--------------------- 136
Cdd:PLN03192 553 IGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNT-ALWnAISAKHHKIFRILyhfasisdphaagdllctaak 631

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 126517480 137 ------VRSFRRLGLRLDRTNRAGLTALQLAASRGHGTCVQAL 173
Cdd:PLN03192 632 rndltaMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLL 674
Ank_4 pfam13637
Ankyrin repeats (many copies);
47-104 5.99e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.11  E-value: 5.99e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 126517480   47 GRTPLMVAvglpdpAMRSRF--VRLLLEQGAAVNLRDERGRTALSLACERGHLDAVQLLV 104
Cdd:pfam13637   1 ELTALHAA------AASGHLelLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 59-172 7.38e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 51.03  E-value: 7.38e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126517480  59 DPAMRSRFVRLLLEQGAAVNLRDE-RGRTALSLACERGHLDAVQLLVQFSGDPEATDSAGNSPVMWAAACGHGAVLEFLV 137
Cdd:PHA02878 142 DDIIEAEITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILL 221

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 126517480 138 RSfrrlGLRLDRTNRAGLTALQLAASR-----------GHGTCVQA 172
Cdd:PHA02878 222 EN----GASTDARDKCGNTPLHISVGYckdydilklllEHGVDVNA 263
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 57-173 9.49e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 50.73  E-value: 9.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126517480  57 LPDPAMRSRFVRLLLEQGAAVNLRDERGRTALSLACERGHLDAVQLLVQFSGDPEATDSAGNSPVMWAAACGHGAVLEFL 136
Cdd:PHA02874  97 LPIPCIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLL 176

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 126517480 137 VRSfrrlGLRLDRTNRAGLTALQLAASRGHGTCVQAL 173
Cdd:PHA02874 177 LEK----GAYANVKDNNGESPLHNAAEYGDYACIKLL 209
PHA03095 PHA03095
ankyrin-like protein; Provisional
 25-162 1.23e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 50.41  E-value: 1.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126517480  25 VHLARF-----VLDALDRSIIDCRA--EQGRTPLMVAVGLPDPAMRsrFVRLLLEQGAAVNLRDERGRTALSLACERGHL 97
Cdd:PHA03095 123 VYLSGFninpkVIRLLLRKGADVNAldLYGMTPLAVLLKSRNANVE--LLRLLIDAGADVYAVDDRFRSLLHHHLQSFKP 200

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126517480  98 DA--VQLLVQFSGDPEATDSAGNSPVMWAAA---CGHGAVLEFLVRsfrrlGLRLDRTNRAGLTALQLAA 162
Cdd:PHA03095 201 RAriVRELIRAGCDPAATDMLGNTPLHSMATgssCKRSLVLPLLIA-----GISINARNRYGQTPLHYAA 265
Ank_5 pfam13857
Ankyrin repeats (many copies);
70-121 1.78e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.64  E-value: 1.78e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 126517480   70 LLEQG-AAVNLRDERGRTALSLACERGHLDAVQLLVQFSGDPEATDSAGNSPV 121
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 40-109 4.19e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 48.51  E-value: 4.19e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126517480  40 IDCRAEQGRTPLMVAVGLPDPamrsRFVRLLLEQGAAVNLRDERGRTALSLACERGHLDAVQLLVQFSGD 109
Cdd:PHA03100 185 INIKDVYGFTPLHYAVYNNNP----EFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 67-139 5.27e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 48.12  E-value: 5.27e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 126517480  67 VRLLLEQGAAVNLRDERGRTALSLACERGHLDAVQLLVQFSGDPEATDSAGNSPVMWAAACGHGAVLEFLVRS 139
Cdd:PHA03100 175 VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNN 247
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 19-165 6.00e-06

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 48.09  E-value: 6.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126517480  19 AMQAGKVHLARFVLDALDRSI---IDCRAEQGRTPLMVAVGLPDPAMrsrfVRLLLEQGAAVN--------LRDER---- 83
Cdd:cd22192   58 AALYDNLEAAVVLMEAAPELVnepMTSDLYQGETALHIAVVNQNLNL----VRELIARGADVVspratgtfFRPGPknli 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126517480  84 --GRTALSLACERGHLDAVQLLVQFSGDPEATDSAGNSP----VMWAA---ACghgAVLEFLVRSFRRLGL-RLDR-TNR 152
Cdd:cd22192  134 yyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVlhilVLQPNktfAC---QMYDLILSYDKEDDLqPLDLvPNN 210

                        170
                 ....*....|...
gi 126517480 153 AGLTALQLAASRG 165
Cdd:cd22192  211 QGLTPFKLAAKEG 223
Ank_5 pfam13857
Ankyrin repeats (many copies);
35-91 7.16e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.10  E-value: 7.16e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 126517480   35 LDRSIIDCRAEQ--GRTPLMVAVGLPdpamRSRFVRLLLEQGAAVNLRDERGRTALSLA 91
Cdd:pfam13857   2 LEHGPIDLNRLDgeGYTPLHVAAKYG----ALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 41-107 9.55e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.59  E-value: 9.55e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 126517480  41 DCRAEQGRTPLMVAVGLPdpamRSRFVRLLLEQGAAVNLRDERGRTALSLACERGHLDAVQLLVQFS 107
Cdd:PTZ00322 109 NCRDYDGRTPLHIACANG----HVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHS 171
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 46-165 3.09e-05

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: 46.03  E-value: 3.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126517480  46 QGRTPLMVAVglpdpaMRS--RFVRLLLEQGAAVNLRDER-------------GRTALSLACERGHLDAVQLLVQFSGDP 110
Cdd:cd21882   72 QGQTALHIAI------ENRnlNLVRLLVENGADVSARATGrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQP 145

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 126517480 111 ---EATDSAGN------------SPVMWAAACG-HGAVLEFLVRSFRRLGLRLdRTNRAGLTALQLAASRG 165
Cdd:cd21882  146 aalEAQDSLGNtvlhalvlqadnTPENSAFVCQmYNLLLSYGAHLDPTQQLEE-IPNHQGLTPLKLAAVEG 215
Ank_4 pfam13637
Ankyrin repeats (many copies);
117-173 3.19e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.11  E-value: 3.19e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 126517480  117 GNSPVMWAAACGHgavlEFLVRSFRRLGLRLDRTNRAGLTALQLAASRGHGTCVQAL 173
Cdd:pfam13637   1 ELTALHAAAASGH----LELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 38-125 5.27e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.44  E-value: 5.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126517480  38 SIIDCRaeqgRTPLMVAVGLPDpamRSRFVRLLLEQGAAVNLRDERGRTALSLACERGH-LDAVQLLVQFSGDPEATDSA 116
Cdd:PHA02876 268 SIDDCK----NTPLHHASQAPS---LSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRL 340


                 ....*....
gi 126517480 117 GNSPVMWAA 125
Cdd:PHA02876 341 YITPLHQAS 349
PHA03095 PHA03095
ankyrin-like protein; Provisional
 40-158 6.62e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 44.63  E-value: 6.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126517480  40 IDCRAEQGRTPLMVAVGLPDPAmRSRFVRLLLEQGAAVNLRDERGRTAL-SLACERGHLDAVQLLVQFSGDPEATDSAGN 118
Cdd:PHA03095  40 VNFRGEYGKTPLHLYLHYSSEK-VKDIVRLLLEAGADVNAPERCGFTPLhLYLYNATTLDVIKLLIKAGADVNAKDKVGR 118

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 126517480 119 SP--VMWAAACGHGAVLEFLVrsfrRLGLRLDRTNRAGLTAL 158
Cdd:PHA03095 119 TPlhVYLSGFNINPKVIRLLL----RKGADVNALDLYGMTPL 156
PHA03095 PHA03095
ankyrin-like protein; Provisional
 14-100 9.07e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 44.25  E-value: 9.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126517480  14 RTFLEAMQAGKVHLARFVLDALDRSI-IDCRAEQGRTPLMVAVGLPDPamrsRFVRLLLEQGAAVNLRDERGRTALSLAC 92
Cdd:PHA03095 223 NTPLHSMATGSSCKRSLVLPLLIAGIsINARNRYGQTPLHYAAVFNNP----RACRRLIALGADINAVSSDGNTPLSLMV 298


                 ....*...
gi 126517480  93 ERGHLDAV 100
Cdd:PHA03095 299 RNNNGRAV 306
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 18-162 2.48e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 43.06  E-value: 2.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126517480  18 EAMQAGKVHLARFVLDaLDRSIIDCRAEQGRTPLMVAVGLPDPAMrsrfVRLLLEQGAAVNLRDERGRTALSLACERGHL 97
Cdd:PHA02875  74 DAVEEGDVKAVEELLD-LGKFADDVFYKDGMTPLHLATILKKLDI----MKLLIARGADPDIPNTDKFSPLHLAVMMGDI 148

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 126517480  98 DAVQLLVQFSGDPEATDSAGNSPVMWAAACGHGAVLEFLVRSfrrlGLRLDRTNRAGLTALQLAA 162
Cdd:PHA02875 149 KGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDS----GANIDYFGKNGCVAALCYA 209
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 47-165 3.48e-04

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 42.76  E-value: 3.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126517480   47 GRTPLMVAvglpdpAMRSRF--VRLLLEQGAAVNLR---DE-----------RGRTALSLACERGHLDAVQLLVQFSGDP 110
Cdd:TIGR00870 128 GITALHLA------AHRQNYeiVKLLLERGASVPARacgDFfvksqgvdsfyHGESPLNAAACLGSPSIVALLSEDPADI 201

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 126517480  111 EATDSAGNSPVmwaaacgHGAVLEF--------LVRSFRRLGLRLDR-----------TNRAGLTALQLAASRG 165
Cdd:TIGR00870 202 LTADSLGNTLL-------HLLVMENefkaeyeeLSCQMYNFALSLLDklrdskeleviLNHQGLTPLKLAAKEG 268
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 83-114 3.52e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 37.65  E-value: 3.52e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 126517480   83 RGRTALSLACER-GHLDAVQLLVQFSGDPEATD 114
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 46-82 4.41e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 37.27  E-value: 4.41e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 126517480   46 QGRTPLMVAVGLPDpamRSRFVRLLLEQGAAVNLRDE 82
Cdd:pfam00023   1 DGNTPLHLAAGRRG---NLEIVKLLLSKGADVNARDK 34
Ank_5 pfam13857
Ankyrin repeats (many copies);
102-161 4.96e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.71  E-value: 4.96e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 126517480  102 LLVQFSGDPEATDSAGNSPVMWAAACGHGAVLEFLVRsfRRLGLRLdrTNRAGLTALQLA 161
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLA--YGVDLNL--KDEEGLTALDLA 56
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 38-121 7.53e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 41.40  E-value: 7.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126517480  38 SIIDCRAEQGRTPLMVAVGLpdpAMRSRFVRLLLEQGAAVNLRDE-RGRTALSLACERGhlDAVQLLVQFSGDPEATDSA 116
Cdd:PHA02878 225 ASTDARDKCGNTPLHISVGY---CKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIKSE--RKLKLLLEYGADINSLNSY 299


                 ....*
gi 126517480 117 GNSPV 121
Cdd:PHA02878 300 KLTPL 304
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 83-112 1.07e-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: 36.03  E-value: 1.07e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 126517480    83 RGRTALSLACERGHLDAVQLLVQFSGDPEA 112
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA03095 PHA03095
ankyrin-like protein; Provisional
 63-172 2.60e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 39.62  E-value: 2.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126517480  63 RSRFVRLLLEQGAAVNLRDERGRTAL-SLA----CERGHLDavQLLVQFSGDpEATDSAGNSPVMWAAACG-HGAVLEFL 136
Cdd:PHA03095 201 RARIVRELIRAGCDPAATDMLGNTPLhSMAtgssCKRSLVL--PLLIAGISI-NARNRYGQTPLHYAAVFNnPRACRRLI 277

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 126517480 137 vrsfrRLGLRLDRTNRAGLTALQLAASRGHGTCVQA 172
Cdd:PHA03095 278 -----ALGADINAVSSDGNTPLSLMVRNNNGRAVRA 308
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 83-112 3.55e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 34.54  E-value: 3.55e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 126517480   83 RGRTALSLACERGHLDAVQLLVQFSGDPEA 112
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 44-165 3.59e-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: 39.36  E-value: 3.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126517480  44 AEQGRTPLMVAVglpdPAMRSRFVRLLLEQGAAVNLRDER--------------GRTALSLACERGHLDAVQLLVQFSGD 109
Cdd:cd22194  138 AYEGQTALNIAI----ERRQGDIVKLLIAKGADVNAHAKGvffnpkykhegfyfGETPLALAACTNQPEIVQLLMEKEST 213

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 126517480 110 PEAT-DSAGNSpVMWA---AACGHGAVLEFLVRSFRRLGLRLDR------TNRAGLTALQLAASRG 165
Cdd:cd22194  214 DITSqDSRGNT-VLHAlvtVAEDSKTQNDFVKRMYDMILLKSENknletiRNNEGLTPLQLAAKMG 278
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 67-161 4.44e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 38.79  E-value: 4.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126517480  67 VRLLLEQGAAVNLRDERGRTALSLACERGHLDAVQLLVQFSGDPEATDSAGNSPVMWAAACGHGAVLEFLVRSFRRLGLR 146
Cdd:PHA02874 140 IKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNK 219

                         90
                 ....*....|....*
gi 126517480 147 LDRtnraGLTALQLA 161
Cdd:PHA02874 220 CKN----GFTPLHNA 230
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 46-165 6.79e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely related to TRPV1, sharing high sequence identity (>50%), but TRPV2 shows a higher temperature threshold and sensitivity for activation than TRPV1. TRPV2 can be stimulated by ligands or lipids, and is involved in osmosensation and mechanosensation. TRPV2 is expressed in both neuronal and non-neuronal tissues, and it has been implicated in diverse physiological and pathophysiological processes, including cardiac-structure maintenance, innate immunity, and cancer. TRPV2 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 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.


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 38.68  E-value: 6.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126517480  46 QGRTPLMVAVglpdpAMRS-RFVRLLLEQGAAVNLRDER-------------GRTALSLACERGHLDAVQLLVQFSGDP- 110
Cdd:cd22197   93 RGHSALHIAI-----EKRSlQCVKLLVENGADVHARACGrffqkkqgtcfyfGELPLSLAACTKQWDVVNYLLENPHQPa 167

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 126517480 111 --EATDSAGNSPVmwaaacgHGAVL---------EFLVRSFRRL---GLRLDRT-------NRAGLTALQLAASRG 165
Cdd:cd22197  168 slQAQDSLGNTVL-------HALVMiadnspensALVIKMYDGLlqaGARLCPTvqleeisNHEGLTPLKLAAKEG 236
PHA03095 PHA03095
ankyrin-like protein; Provisional
 67-159 8.09e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 38.08  E-value: 8.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126517480  67 VRLLLEQGAAVNLRDERGRTALSLACERGH---LDAVQLLVQFSGDPEATDSAGNSPVMWAAAcgHGAVLEfLVRSFRRL 143
Cdd:PHA03095  30 VRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLY--NATTLD-VIKLLIKA 106

                         90
                 ....*....|....*.
gi 126517480 144 GLRLDRTNRAGLTALQ 159
Cdd:PHA03095 107 GADVNAKDKVGRTPLH 122
 
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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