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Conserved domains on  [gi|1678754866|ref|XP_029281479|]
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NF-kappa-B inhibitor epsilon [Cottoperca gobio]

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];
88-329 2.12e-34

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 127.76  E-value: 2.12e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678754866  88 SELSEQEENLLATITEDGDTILHLAIIHEDKCISQKLIQIFPKEVLDIQNNLYQTALHLATYLNLIGVVKGLVEKEVSLE 167
Cdd:COG0666     2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678754866 168 LQDQEGNTALHVACQHGQTECALELtrevsLSKMAPVlETQNWRGLACLHLATLNRQHQILKLLVKKGADLNIQeGTSGK 247
Cdd:COG0666    82 AKDDGGNTLLHAAARNGDLEIVKLL-----LEAGADV-NARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQ-DNDGN 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678754866 248 TALHLATELHDMTSVKLLLSRGANVDAAMFNGCTPLHLAVGRQDAAIANLLCQSGADTMLRNMEDETALDLA--NGNDDI 325
Cdd:COG0666   155 TPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAaeNGNLEI 234


                  ....
gi 1678754866 326 LALF 329
Cdd:COG0666   235 VKLL 238
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
88-329 2.12e-34

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 127.76  E-value: 2.12e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678754866  88 SELSEQEENLLATITEDGDTILHLAIIHEDKCISQKLIQIFPKEVLDIQNNLYQTALHLATYLNLIGVVKGLVEKEVSLE 167
Cdd:COG0666     2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678754866 168 LQDQEGNTALHVACQHGQTECALELtrevsLSKMAPVlETQNWRGLACLHLATLNRQHQILKLLVKKGADLNIQeGTSGK 247
Cdd:COG0666    82 AKDDGGNTLLHAAARNGDLEIVKLL-----LEAGADV-NARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQ-DNDGN 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678754866 248 TALHLATELHDMTSVKLLLSRGANVDAAMFNGCTPLHLAVGRQDAAIANLLCQSGADTMLRNMEDETALDLA--NGNDDI 325
Cdd:COG0666   155 TPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAaeNGNLEI 234


                  ....
gi 1678754866 326 LALF 329
Cdd:COG0666   235 VKLL 238
Ank_2 pfam12796
Ankyrin repeats (3 copies);
144-241 7.98e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 68.99  E-value: 7.98e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678754866 144 LHLATYLNLIGVVKGLVEKEVSLELQDQEGNTALHVACQHGQTECALELtrevsLSKMAPVLETQNWrglACLHLATLNR 223
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL-----LEHADVNLKDNGR---TALHYAARSG 72

                          90
                  ....*....|....*...
gi 1678754866 224 QHQILKLLVKKGADLNIQ 241
Cdd:pfam12796  73 HLEIVKLLLEKGADINVK 90
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 144-328 2.38e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 73.76  E-value: 2.38e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678754866 144 LHLATYLNLIGVVKGLVEKEVSLELQDQEGNTALHVACQHGQTECALELTREVSLSKMAPVL----ETQNWRGLACLHLA 219
Cdd:PHA02878   41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVFYTLvaikDAFNNRNVEIFKII 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678754866 220 TLNR---------------------QHQILKLLVKKGADLNIQEGTSGKTALHLATELHDMTSVKLLLSRGANVDAAMFN 278
Cdd:PHA02878  121 LTNRykniqtidlvyidkkskddiiEAEITKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKT 200

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1678754866 279 GCTPLHLAVGRQDAAIANLLCQSGADTMLRNMEDETALDLANG---NDDILAL 328
Cdd:PHA02878  201 NNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGyckDYDILKL 253
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 129-300 2.67e-07

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: 52.32  E-value: 2.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678754866 129 PKEVLDIQNNLYQ-----TALHLATYLNLIGVVKGLVEKEvSLELQDQ--EGNTALHVACQHGQTECALELTREvslskm 201
Cdd:cd22192     1 WAQMLDELHLLQQkriseSPLLLAAKENDVQAIKKLLKCP-SCDLFQRgaLGETALHVAALYDNLEAAVVLMEA------ 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678754866 202 APVL-----ETQNWRGLACLHLATLNRQHQILKLLVKKGADLNIQEGTS-------------GKTALHLATELHDMTSVK 263
Cdd:cd22192    74 APELvnepmTSDLYQGETALHIAVVNQNLNLVRELIARGADVVSPRATGtffrpgpknliyyGEHPLSFAACVGNEEIVR 153

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1678754866 264 LLLSRGANVDAAMFNGCTPLHLAVGRQDAAIAnllCQ 300
Cdd:cd22192   154 LLIEHGADIRAQDSLGNTVLHILVLQPNKTFA---CQ 187
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 212-320 1.41e-04

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 43.53  E-value: 1.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678754866 212 GLACLHLATLNRQ---HQILKLLVKKGAD-LNIQ--------EGTSGKTALHLATELHDMTSVKLLLSRGANVDAA---- 275
Cdd:TIGR00870  82 GDTLLHAISLEYVdavEAILLHLLAAFRKsGPLElandqytsEFTPGITALHLAAHRQNYEIVKLLLERGASVPARacgd 161

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1678754866 276 ----------MFNGCTPLHLAVGRQDAAIANLLCQSGADTmlrnmedETALDLAN 320
Cdd:TIGR00870 162 ffvksqgvdsFYHGESPLNAAACLGSPSIVALLSEDPADI-------LTADSLGN 209
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
88-329 2.12e-34

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 127.76  E-value: 2.12e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678754866  88 SELSEQEENLLATITEDGDTILHLAIIHEDKCISQKLIQIFPKEVLDIQNNLYQTALHLATYLNLIGVVKGLVEKEVSLE 167
Cdd:COG0666     2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678754866 168 LQDQEGNTALHVACQHGQTECALELtrevsLSKMAPVlETQNWRGLACLHLATLNRQHQILKLLVKKGADLNIQeGTSGK 247
Cdd:COG0666    82 AKDDGGNTLLHAAARNGDLEIVKLL-----LEAGADV-NARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQ-DNDGN 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678754866 248 TALHLATELHDMTSVKLLLSRGANVDAAMFNGCTPLHLAVGRQDAAIANLLCQSGADTMLRNMEDETALDLA--NGNDDI 325
Cdd:COG0666   155 TPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAaeNGNLEI 234


                  ....
gi 1678754866 326 LALF 329
Cdd:COG0666   235 VKLL 238
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
96-328 3.17e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 124.68  E-value: 3.17e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678754866  96 NLLATITEDGDTILHLAIIHEDKCISQKLIQIFPKEVLDIQNNLYQTALHLATYLNLIGVVKGLVEKEVSLELQDQEGNT 175
Cdd:COG0666    43 ALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGET 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678754866 176 ALHVACQHGQTECALELtrevsLSKMAPVlETQNWRGLACLHLATLNRQHQILKLLVKKGADLNIQEGtSGKTALHLATE 255
Cdd:COG0666   123 PLHLAAYNGNLEIVKLL-----LEAGADV-NAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDN-DGETPLHLAAE 195

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1678754866 256 LHDMTSVKLLLSRGANVDAAMFNGCTPLHLAVGRQDAAIANLLCQSGADTMLRNMEDETALDLANGNDDILAL 328
Cdd:COG0666   196 NGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIV 268
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
89-316 1.42e-27

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 109.66  E-value: 1.42e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678754866  89 ELSEQEENLLATITEDGDTILHLAIIHEDKCISQKLIQifPKEVLDIQNNLYQTALHLATYLNLIGVVKGLVEKEVSLEL 168
Cdd:COG0666    71 LLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLE--AGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNA 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678754866 169 QDQEGNTALHVACQHGQTECALELtrevsLSKMAPVlETQNWRGLACLHLATLNRQHQILKLLVKKGADLNIQEgTSGKT 248
Cdd:COG0666   149 QDNDGNTPLHLAAANGNLEIVKLL-----LEAGADV-NARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKD-NDGKT 221

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1678754866 249 ALHLATELHDMTSVKLLLSRGANVDAAMFNGCTPLHLAVGRQDAAIANLLCQSGADTMLRNMEDETAL 316
Cdd:COG0666   222 ALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
Ank_2 pfam12796
Ankyrin repeats (3 copies);
144-241 7.98e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 68.99  E-value: 7.98e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678754866 144 LHLATYLNLIGVVKGLVEKEVSLELQDQEGNTALHVACQHGQTECALELtrevsLSKMAPVLETQNWrglACLHLATLNR 223
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL-----LEHADVNLKDNGR---TALHYAARSG 72

                          90
                  ....*....|....*...
gi 1678754866 224 QHQILKLLVKKGADLNIQ 241
Cdd:pfam12796  73 HLEIVKLLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
216-309 1.57e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 68.22  E-value: 1.57e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678754866 216 LHLATLNRQHQILKLLVKKGADLNIQEgTSGKTALHLATELHDMTSVKLLLSRgANVDAAMfNGCTPLHLAVGRQDAAIA 295
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQD-KNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIV 77

                          90
                  ....*....|....
gi 1678754866 296 NLLCQSGADTMLRN 309
Cdd:pfam12796  78 KLLLEKGADINVKD 91
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 144-328 2.38e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 73.76  E-value: 2.38e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678754866 144 LHLATYLNLIGVVKGLVEKEVSLELQDQEGNTALHVACQHGQTECALELTREVSLSKMAPVL----ETQNWRGLACLHLA 219
Cdd:PHA02878   41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVFYTLvaikDAFNNRNVEIFKII 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678754866 220 TLNR---------------------QHQILKLLVKKGADLNIQEGTSGKTALHLATELHDMTSVKLLLSRGANVDAAMFN 278
Cdd:PHA02878  121 LTNRykniqtidlvyidkkskddiiEAEITKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKT 200

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1678754866 279 GCTPLHLAVGRQDAAIANLLCQSGADTMLRNMEDETALDLANG---NDDILAL 328
Cdd:PHA02878  201 NNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGyckDYDILKL 253
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 211-329 2.64e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 67.32  E-value: 2.64e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678754866 211 RGLACLHLATLNRQHQILKLLVKKGADLNIQEgTSGKTALHLATELHDMTSVKLLLSRGANVDAAMFNGCTPLHLAVGRQ 290
Cdd:PHA02875  101 DGMTPLHLATILKKLDIMKLLIARGADPDIPN-TDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKG 179

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1678754866 291 DAAIANLLCQSGA--DTMLRNmEDETALDLA--NGNDDILALF 329
Cdd:PHA02875  180 DIAICKMLLDSGAniDYFGKN-GCVAALCYAieNNKIDIVRLF 221
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 155-298 4.13e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 63.83  E-value: 4.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678754866 155 VVKGLVEKEVSLELQDQEGNTALHVACQHGQtecaLELTRevSLSKMAPVLETQNWRGLACLHLATLNRQHQILKLLVKK 234
Cdd:PHA02874  106 MIKTILDCGIDVNIKDAELKTFLHYAIKKGD----LESIK--MLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEK 179

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1678754866 235 GADLNIQEgTSGKTALHLATELHDMTSVKLLLSRGANVDAAMFNGCTPLHLAVGRQDAAIANLL 298
Cdd:PHA02874  180 GAYANVKD-NNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAIELLI 242
PHA03095 PHA03095
ankyrin-like protein; Provisional
 227-317 8.12e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 62.73  E-value: 8.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678754866 227 ILKLLVKKGADLNIqEGTSGKTALH--LATELHDMTSVKLLLSRGANVDAAMFNGCTPLHLAVGRQDAAIA--NLLCQSG 302
Cdd:PHA03095   99 VIKLLIKAGADVNA-KDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVEllRLLIDAG 177

                          90
                  ....*....|....*
gi 1678754866 303 ADTMLRNMEDETALD 317
Cdd:PHA03095  178 ADVYAVDDRFRSLLH 192
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 107-329 1.31e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 61.99  E-value: 1.31e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678754866 107 TILHLAIihEDKCISqKLIQIFPKEV-LDIQNNLYQTALHLATYLNLI-----GVVKGLVEKEVSLELQDQEGNTALHVA 180
Cdd:PHA03100   37 LPLYLAK--EARNID-VVKILLDNGAdINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYA 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678754866 181 CQhgQTECALELTREvsLSKMAPVLETQNWRGLACLHLAT--LNRQHQILKLLVKKGADLNIqegtsgktalhlatelhd 258
Cdd:PHA03100  114 IS--KKSNSYSIVEY--LLDNGANVNIKNSDGENLLHLYLesNKIDLKILKLLIDKGVDINA------------------ 171

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1678754866 259 MTSVKLLLSRGANVDAAMFNGCTPLHLAVGRQDAAIANLLCQSGADTMLRNMEDETALDLA--NGNDDILALF 329
Cdd:PHA03100  172 KNRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAilNNNKEIFKLL 244
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 208-329 1.42e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 58.91  E-value: 1.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678754866 208 QNWRGLACLHLATLNRQHQILKLLVKKGADLNIQEGTSgKTALHLAT-----ELHDMTSVKLLLSRGANVDAAMFNGCTP 282
Cdd:PHA03100   31 SYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNN-STPLHYLSnikynLTDVKEIVKLLLEYGANVNAPDNNGITP 109

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1678754866 283 LHLAVGR--QDAAIANLLCQSGADTMLRNMEDETALDLA---NGND-DILALF 329
Cdd:PHA03100  110 LLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYlesNKIDlKILKLL 162
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 170-303 1.73e-09

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 56.04  E-value: 1.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678754866 170 DQEGNTALHVACQHGQTECALELTREVSLSKMAPVLETqNWRGLACLHLATlnRQHQI-----LKLLVKKGADLNIQEGT 244
Cdd:PHA02736   14 DIEGENILHYLCRNGGVTDLLAFKNAISDENRYLVLEY-NRHGKQCVHIVS--NPDKAdpqekLKLLMEWGADINGKERV 90

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678754866 245 SGKTALHLATELHDMTSVKLLLSR-GANVDAAMFNGCTPLHLAVGRQDAAIANLLCQSGA 303
Cdd:PHA02736   91 FGNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYVACERHDAKMMNILRAKGA 150
Ank_2 pfam12796
Ankyrin repeats (3 copies);
109-192 7.94e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 52.43  E-value: 7.94e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678754866 109 LHLAIIHEDKCISQKLIQIFPKevLDIQNNLYQTALHLATYLNLIGVVKGLVEKeVSLELQDqEGNTALHVACQHGQTEC 188
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGAD--ANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEI 76


                  ....
gi 1678754866 189 ALEL 192
Cdd:pfam12796  77 VKLL 80
PHA03095 PHA03095
ankyrin-like protein; Provisional
 227-316 9.05e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 56.57  E-value: 9.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678754866 227 ILKLLVKKGADLNiQEGTSGKTALH--LATELHDMTS-VKLLLSRGANVDAAMFNGCTPLHLAVGRQD-AAIANLLCQSG 302
Cdd:PHA03095   29 EVRRLLAAGADVN-FRGEYGKTPLHlyLHYSSEKVKDiVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAG 107

                          90
                  ....*....|....
gi 1678754866 303 ADTMLRNMEDETAL 316
Cdd:PHA03095  108 ADVNAKDKVGRTPL 121
PHA02741 PHA02741
hypothetical protein; Provisional
 169-298 1.80e-08

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 53.12  E-value: 1.80e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678754866 169 QDQEGNTALHVACQHGQTECALELTREVSLSKMAPVLETQNWRGLACLHLATLNRQHQ----ILKLLVKKGADLNIQEGT 244
Cdd:PHA02741   17 KNSEGENFFHEAARCGCFDIIARFTPFIRGDCHAAALNATDDAGQMCIHIAAEKHEAQlaaeIIDHLIELGADINAQEML 96

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1678754866 245 SGKTALHLATELHDMTSVKlLLSRGANVDAAMFN--GCTPLHLAVGRQDAAIANLL 298
Cdd:PHA02741   97 EGDTALHLAAHRRDHDLAE-WLCCQPGIDLHFCNadNKSPFELAIDNEDVAMMQIL 151
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 154-313 2.14e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 55.64  E-value: 2.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678754866 154 GVVKGLVEKEVSLELQDQEGNTALHVACQHGQTECALELTrevslsKMAPVLETQNWRGLACLHLATLNRQHQILKLLVK 233
Cdd:PLN03192  539 ALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLL------KHACNVHIRDANGNTALWNAISAKHHKIFRILYH 612

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678754866 234 KGAdlnIQEGTSGKTALHLATELHDMTSVKLLLSRGANVDAAMFNGCTPLHLAVGRQDAAIANLLCQSGADTMLRNMEDE 313
Cdd:PLN03192  613 FAS---ISDPHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDDD 689
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 224-316 9.88e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 53.43  E-value: 9.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678754866 224 QHQILKLLVKKGADLNIQEGTSgKTALHLATELHDMTSVKLLLSRGANVDAAMFNGCTPLHLAVGRQDAAIANLLCQSGA 303
Cdd:PHA02874  103 EKDMIKTILDCGIDVNIKDAEL-KTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGA 181

                          90
                  ....*....|...
gi 1678754866 304 DTMLRNMEDETAL 316
Cdd:PHA02874  182 YANVKDNNGESPL 194
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 105-298 1.14e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 53.35  E-value: 1.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678754866 105 GDTILHLAIIHEDKCISQKLIQIFPK-EVLDIQNNlyqTALHLATYLNLIGVVKGLVEKEVSLELQDQEGNTALHVACQH 183
Cdd:PHA02878  168 GNTALHYATENKDQRLTELLLSYGANvNIPDKTNN---SPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGY 244

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678754866 184 gqtecaleltrevslskmapvletqnwrglaCLhlatlnrQHQILKLLVKKGADLNIQEGTSGKTALHLAteLHDMTSVK 263
Cdd:PHA02878  245 -------------------------------CK-------DYDILKLLLEHGVDVNAKSYILGLTALHSS--IKSERKLK 284

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1678754866 264 LLLSRGANVDAAMFNGCTPLHLAV-GRQDAAIANLL 298
Cdd:PHA02878  285 LLLEYGADINSLNSYKLTPLSSAVkQYLCINIGRIL 320
Ank_2 pfam12796
Ankyrin repeats (3 copies);
250-326 1.16e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 48.96  E-value: 1.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678754866 250 LHLATELHDMTSVKLLLSRGANVDAAMFNGCTPLHLAVGRQDAAIANLLCqsgaDTMLRNMEDE--TALDLA--NGNDDI 325
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL----EHADVNLKDNgrTALHYAarSGHLEI 76


                  .
gi 1678754866 326 L 326
Cdd:pfam12796  77 V 77
PHA03095 PHA03095
ankyrin-like protein; Provisional
 142-316 1.63e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 52.72  E-value: 1.63e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678754866 142 TALHL-ATYLNLIGVVKGLVEKEVSLELQDQEGNTALHVacqhgqtecaleltrevslskmapvletqnwrglaclHLAT 220
Cdd:PHA03095   85 TPLHLyLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHV-------------------------------------YLSG 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678754866 221 LNRQHQILKLLVKKGADLNIQEgTSGKTALHLATELHDMT--SVKLLLSRGANVDAAMFNGCTPLH--LAVGRQDAAIAN 296
Cdd:PHA03095  128 FNINPKVIRLLLRKGADVNALD-LYGMTPLAVLLKSRNANveLLRLLIDAGADVYAVDDRFRSLLHhhLQSFKPRARIVR 206

                         170       180
                  ....*....|....*....|
gi 1678754866 297 LLCQSGADTMLRNMEDETAL 316
Cdd:PHA03095  207 ELIRAGCDPAATDMLGNTPL 226
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 216-308 2.03e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 52.27  E-value: 2.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678754866 216 LHLATLNRQHQILKLLVKKGADLNIQEgTSGKTALHLATELHDMTSVKLLLSRGANVDAAMFNGCTPLHLAVGRQDAAIA 295
Cdd:PHA02874  128 LHYAIKKGDLESIKMLFEYGADVNIED-DNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACI 206

                          90
                  ....*....|...
gi 1678754866 296 NLLCQSGADTMLR 308
Cdd:PHA02874  207 KLLIDHGNHIMNK 219
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 129-300 2.67e-07

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: 52.32  E-value: 2.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678754866 129 PKEVLDIQNNLYQ-----TALHLATYLNLIGVVKGLVEKEvSLELQDQ--EGNTALHVACQHGQTECALELTREvslskm 201
Cdd:cd22192     1 WAQMLDELHLLQQkriseSPLLLAAKENDVQAIKKLLKCP-SCDLFQRgaLGETALHVAALYDNLEAAVVLMEA------ 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678754866 202 APVL-----ETQNWRGLACLHLATLNRQHQILKLLVKKGADLNIQEGTS-------------GKTALHLATELHDMTSVK 263
Cdd:cd22192    74 APELvnepmTSDLYQGETALHIAVVNQNLNLVRELIARGADVVSPRATGtffrpgpknliyyGEHPLSFAACVGNEEIVR 153

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1678754866 264 LLLSRGANVDAAMFNGCTPLHLAVGRQDAAIAnllCQ 300
Cdd:cd22192   154 LLIEHGADIRAQDSLGNTVLHILVLQPNKTFA---CQ 187
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 216-305 1.65e-06

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 49.63  E-value: 1.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678754866 216 LHLATLNRQHQILKLLVKKGADLNIQEGTS----GKTALHLATELHDMTSVKLLLSRGANV--------------DAAMF 277
Cdd:cd22192    55 LHVAALYDNLEAAVVLMEAAPELVNEPMTSdlyqGETALHIAVVNQNLNLVRELIARGADVvspratgtffrpgpKNLIY 134

                          90       100       110
                  ....*....|....*....|....*....|
gi 1678754866 278 NGCTPLHLA--VGRQDaaIANLLCQSGADT 305
Cdd:cd22192   135 YGEHPLSFAacVGNEE--IVRLLIEHGADI 162
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 94-319 2.69e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 48.81  E-value: 2.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678754866  94 EENLLATITEDG----------DTILHLAIIHEDKCISQKLIQIFPKEVLDIQNNLYqtALHLATYLNLIGVVKGLVEKE 163
Cdd:PHA02874  103 EKDMIKTILDCGidvnikdaelKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCY--PIHIAIKHNFFDIIKLLLEKG 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678754866 164 VSLELQDQEGNTALHVACQHGQTECaleltrevslskmapvletqnwrglaclhlatlnrqhqiLKLLVKKGADLNIQeG 243
Cdd:PHA02874  181 AYANVKDNNGESPLHNAAEYGDYAC---------------------------------------IKLLIDHGNHIMNK-C 220

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1678754866 244 TSGKTALHLATeLHDMTSVKLLLSrGANVDAAMFNGCTPLHLAVGRQ-DAAIANLLCQSGADTMLRNMEDETALDLA 319
Cdd:PHA02874  221 KNGFTPLHNAI-IHNRSAIELLIN-NASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTA 295
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 227-304 3.12e-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: 48.86  E-value: 3.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678754866 227 ILKLLVKKGADLnIQEGTSGKTALHLATeLHDMTSVKLLLSRGA------NVDAAMFNGCTPLHLAVGRQDAAIANLLCQ 300
Cdd:cd22192    33 IKKLLKCPSCDL-FQRGALGETALHVAA-LYDNLEAAVVLMEAApelvnePMTSDLYQGETALHIAVVNQNLNLVRELIA 110


                  ....
gi 1678754866 301 SGAD 304
Cdd:cd22192   111 RGAD 114
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 198-304 3.68e-06

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: 48.72  E-value: 3.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678754866 198 LSKMAPVLETQNWR-----------GLACLHLATLNRQHQILK-----LLVKKGADLNIQ--------EGTSGKTALHLA 253
Cdd:cd21882     1 LEELLGLLECLRWYltdsayqrgatGKTCLHKAALNLNDGVNEaimllLEAAPDSGNPKElvnapctdEFYQGQTALHIA 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1678754866 254 TELHDMTSVKLLLSRGANVDAA-------------MFNGCTPLHLAVGRQDAAIANLLCQSGAD 304
Cdd:cd21882    81 IENRNLNLVRLLVENGADVSARatgrffrkspgnlFYFGELPLSLAACTNQEEIVRLLLENGAQ 144
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 142-325 4.41e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 48.52  E-value: 4.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678754866 142 TALHLATYLNLIGVVKGLVEKEV-SLELQDQEGNTALHVAC-QHGQTECALELTREVSLS---KMAPVLETQNWRGLACL 216
Cdd:PHA02876   43 TAIHQALQLRQIDIVEEIIQQNPeLIYITDHKCHSTLHTICiIPNVMDIVISLTLDCDIIldiKYASIILNKHKLDEACI 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678754866 217 HlatlnrqhqILKLLVKkGADLN---IQEGTSGKTALHLATELHDMTSVKLLLSRGANVDAAMFNGCTPLHLAVGRQDAA 293
Cdd:PHA02876  123 H---------ILKEAIS-GNDIHydkINESIEYMKLIKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAK 192

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1678754866 294 IANLLCQSGADTMLRNMEDETALDLANGNDDI 325
Cdd:PHA02876  193 MVNLLLSYGADVNIIALDDLSVLECAVDSKNI 224
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 258-323 4.82e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.36  E-value: 4.82e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1678754866 258 DMTSVKLLLSRGANVDAAMFNGCTPLHLAVGRQDAAIANLLCQSGADTMLRNMEDETALDLANGND 323
Cdd:PTZ00322   94 DAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENG 159
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 101-319 9.32e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 47.37  E-value: 9.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678754866 101 ITEDGDTILHLAIIhedkciSQKLIQIfpKEVLDIQNNLYQTALHLATYLNLIGVVKGLV--EKEVSLELQDQEGNTALH 178
Cdd:PHA02876  207 IALDDLSVLECAVD------SKNIDTI--KAIIDNRSNINKNDLSLLKAIRNEDLETSLLlyDAGFSVNSIDDCKNTPLH 278

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678754866 179 VACQhgqtecaleltrEVSLSKMAPVL-------ETQNWRGLACLHLATLN-RQHQILKLLVKKGADLNIQEGTSgKTAL 250
Cdd:PHA02876  279 HASQ------------APSLSRLVPKLlergadvNAKNIKGETPLYLMAKNgYDTENIRTLIMLGADVNAADRLY-ITPL 345

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678754866 251 HLATEL-HDMTSVKLLLSRGANVDAAMFNGCTPLHLAVGRQDAAIANLLCQSGADTMLRNMEDETALDLA 319
Cdd:PHA02876  346 HQASTLdRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFA 415
PHA02743 PHA02743
Viral ankyrin protein; Provisional
 167-303 1.02e-05

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 45.19  E-value: 1.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678754866 167 ELQDQEGNTaLHVACQHGQTECALELTRevSLSKMAPVLETQNWRGLACLHLATL-NRQHQILK--LLVKKGADLNIQEG 243
Cdd:PHA02743   15 EIDEDEQNT-FLRICRTGNIYELMEVAP--FISGDGHLLHRYDHHGRQCTHMVAWyDRANAVMKieLLVNMGADINAREL 91

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1678754866 244 TSGKTALHLAT-----ELHDMTSVKLllsrGANVDAAMFNGCTPLHLAVGRQDAAIANLLCQSGA 303
Cdd:PHA02743   92 GTGNTLLHIAAstknyELAEWLCRQL----GVNLGAINYQHETAYHIAYKMRDRRMMEILRANGA 152
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 101-240 1.42e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 46.52  E-value: 1.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678754866 101 ITEDGDTILHLAIIHEDKCISQKLIQIfpKEVLDIQNNLYQTALHLATYLNLIGVVKGLVEKEVSLELQDQEGNTALHVA 180
Cdd:PHA02875   98 FYKDGMTPLHLATILKKLDIMKLLIAR--GADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIA 175

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1678754866 181 CQHGQTE-CALELTREVSLSKMAPvletqnwRG-LACLHLATLNRQHQILKLLVKKGADLNI 240
Cdd:PHA02875  176 MAKGDIAiCKMLLDSGANIDYFGK-------NGcVAALCYAIENNKIDIVRLFIKRGADCNI 230
PHA03095 PHA03095
ankyrin-like protein; Provisional
 153-296 2.85e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 45.79  E-value: 2.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678754866 153 IGVVKGLVEKEVSLELQDQEGNTALHVACQ--HGQTECALELTREVSLSKMAPVLetqnwrGLACLH-LATLNRQHQILK 229
Cdd:PHA03095  167 VELLRLLIDAGADVYAVDDRFRSLLHHHLQsfKPRARIVRELIRAGCDPAATDML------GNTPLHsMATGSSCKRSLV 240

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1678754866 230 L-LVKKGADLNIQEgTSGKTALHLATELHDMTSVKLLLSRGANVDAAMFNGCTPLHLAVGRQDAAIAN 296
Cdd:PHA03095  241 LpLLIAGISINARN-RYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVR 307
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 212-320 1.41e-04

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 43.53  E-value: 1.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678754866 212 GLACLHLATLNRQ---HQILKLLVKKGAD-LNIQ--------EGTSGKTALHLATELHDMTSVKLLLSRGANVDAA---- 275
Cdd:TIGR00870  82 GDTLLHAISLEYVdavEAILLHLLAAFRKsGPLElandqytsEFTPGITALHLAAHRQNYEIVKLLLERGASVPARacgd 161

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1678754866 276 ----------MFNGCTPLHLAVGRQDAAIANLLCQSGADTmlrnmedETALDLAN 320
Cdd:TIGR00870 162 ffvksqgvdsFYHGESPLNAAACLGSPSIVALLSEDPADI-------LTADSLGN 209
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 216-329 2.21e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 43.13  E-value: 2.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678754866 216 LHLATLNRQHQILKLLVKKGADLniqEGTSGK--TALHLAT-ELHDMTSVKLLLSRGANVDAAMFNGCTPLHLAVGRQ-D 291
Cdd:PHA02876  379 IHYAAVRNNVVIINTLLDYGADI---EALSQKigTALHFALcGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcK 455

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1678754866 292 AAIANLLCQSGADTMLRNMEDETALDLANGNDDILALF 329
Cdd:PHA02876  456 LDVIEMLLDNGADVNAINIQNQYPLLIALEYHGIVNIL 493
Ank_5 pfam13857
Ankyrin repeats (many copies);
265-319 2.57e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.48  E-value: 2.57e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1678754866 265 LLSRG-ANVDAAMFNGCTPLHLAVGRQDAAIANLLCQSGADTMLRNMEDETALDLA 319
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_2 pfam12796
Ankyrin repeats (3 copies);
102-170 2.74e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 39.33  E-value: 2.74e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1678754866 102 TEDGDTILHLAIIHEDKCISQKLIQifpKEVLDIQNNlYQTALHLATYLNLIGVVKGLVEKEVSLELQD 170
Cdd:pfam12796  27 DKNGRTALHLAAKNGHLEIVKLLLE---HADVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
Ank_4 pfam13637
Ankyrin repeats (many copies);
248-298 3.90e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.02  E-value: 3.90e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1678754866 248 TALHLATELHDMTSVKLLLSRGANVDAAMFNGCTPLHLAVGRQDAAIANLL 298
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
Ank_4 pfam13637
Ankyrin repeats (many copies);
142-192 4.66e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 37.64  E-value: 4.66e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1678754866 142 TALHLATYLNLIGVVKGLVEKEVSLELQDQEGNTALHVACQHGQTECALEL 192
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
Ank_5 pfam13857
Ankyrin repeats (many copies);
230-286 6.62e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.33  E-value: 6.62e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1678754866 230 LLVKKGADLNIQEGtSGKTALHLATELHDMTSVKLLLSRGANVDAAMFNGCTPLHLA 286
Cdd:pfam13857   1 LLEHGPIDLNRLDG-EGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 278-309 8.87e-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: 36.50  E-value: 8.87e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1678754866 278 NGCTPLHLAVGRQ-DAAIANLLCQSGADTMLRN 309
Cdd:pfam00023   1 DGNTPLHLAAGRRgNLEIVKLLLSKGADVNARD 33
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 206-313 1.51e-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: 40.51  E-value: 1.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678754866 206 ETQNWRGLACLHLATLNRQHQILKLLVKKGADLNIQ-EGT------------SGKTALHLATELHDMTSVKLLLSRGANv 272
Cdd:cd22194   135 TEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHaKGVffnpkykhegfyFGETPLALAACTNQPEIVQLLMEKEST- 213

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1678754866 273 DAAMFN--GCTPLH-LAVGRQDAAIANLLCQSGADTMLRNMEDE 313
Cdd:cd22194   214 DITSQDsrGNTVLHaLVTVAEDSKTQNDFVKRMYDMILLKSENK 257
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 85-328 1.62e-03

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 40.45  E-value: 1.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678754866  85 APSSELSEQEENLLATITEDGDTILHlAIIHEDKCISQKLIQIF---PKEVLDIQNNLYQTALHLATYLNLIGVVKGLVE 161
Cdd:TIGR00870   9 AEESPLSDEEKAFLPAAERGDLASVY-RDLEEPKKLNINCPDRLgrsALFVAAIENENLELTELLLNLSCRGAVGDTLLH 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678754866 162 KeVSLELQDQEGNTALHVACQHGQTEcALELTREVSLSKMAPvletqnwrGLACLHLATLNRQHQILKLLVKKGADLNI- 240
Cdd:TIGR00870  88 A-ISLEYVDAVEAILLHLLAAFRKSG-PLELANDQYTSEFTP--------GITALHLAAHRQNYEIVKLLLERGASVPAr 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678754866 241 ---------QEGTS---GKTALHLATELHDMTSVKLLLSRGANVDAAMFNGCTPLHLAVGRQDAAIAN----LLCQSGAD 304
Cdd:TIGR00870 158 acgdffvksQGVDSfyhGESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVMENEFKAEYeelsCQMYNFAL 237

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1678754866 305 TML------------RNMEDETALDLA--NGNDDILAL 328
Cdd:TIGR00870 238 SLLdklrdskeleviLNHQGLTPLKLAakEGRIVLFRL 275
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 229-298 1.67e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 40.27  E-value: 1.67e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678754866 229 KLLVKKGADLNIQEgTSGKTALHLATELHDMTSVKLLLSRGANVDAAMFNGCTPLHLAVGRQDAAIANLL 298
Cdd:PTZ00322   99 RILLTGGADPNCRD-YDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 102-274 1.79e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 40.03  E-value: 1.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678754866 102 TEDGDTILHLAIihEDKCISQKLIQIFpkevldIQNNlyqtalhlaTYLNLIGVVKGLVEKEVSLELQDQEGNTALHVAC 181
Cdd:PHA03100  138 NSDGENLLHLYL--ESNKIDLKILKLL------IDKG---------VDINAKNRVNYLLSYGVPINIKDVYGFTPLHYAV 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678754866 182 QHGQTEcaleltrevslskmapvletqnwrglaclhlatlnrqhqILKLLVKKGADLNIQEgTSGKTALHLATELHDMTS 261
Cdd:PHA03100  201 YNNNPE---------------------------------------FVKYLLDLGANPNLVN-KYGDTPLHIAILNNNKEI 240

                         170
                  ....*....|...
gi 1678754866 262 VKLLLSRGANVDA 274
Cdd:PHA03100  241 FKLLLNNGPSIKT 253
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 246-274 1.84e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 35.34  E-value: 1.84e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1678754866 246 GKTALHLATELHDMTS-VKLLLSRGANVDA 274
Cdd:pfam00023   2 GNTPLHLAAGRRGNLEiVKLLLSKGADVNA 31
Ank_5 pfam13857
Ankyrin repeats (many copies);
124-180 4.26e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.01  E-value: 4.26e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1678754866 124 LIQIFPKEVLDIQNNLYqTALHLATYLNLIGVVKGLVEKEVSLELQDQEGNTALHVA 180
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGY-TPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 105-234 4.94e-03

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 38.84  E-value: 4.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678754866 105 GDTILHLAIIHEDKCISQKLIQIFPKEV-LDIQNNLYQ--TALHLA--------------------------TYL----- 150
Cdd:cd22192    51 GETALHVAALYDNLEAAVVLMEAAPELVnEPMTSDLYQgeTALHIAvvnqnlnlvreliargadvvspratgTFFrpgpk 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678754866 151 NLI----------------GVVKGLVEKEVSLELQDQEGNTALHV---------ACQHGQTECALE-LTREVSLSKMapv 204
Cdd:cd22192   131 NLIyygehplsfaacvgneEIVRLLIEHGADIRAQDSLGNTVLHIlvlqpnktfACQMYDLILSYDkEDDLQPLDLV--- 207

                         170       180       190
                  ....*....|....*....|....*....|
gi 1678754866 205 letQNWRGLACLHLATLNRQHQILKLLVKK 234
Cdd:cd22192   208 ---PNNQGLTPFKLAAKEGNIVMFQHLVQK 234
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 212-301 5.06e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. 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: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 38.63  E-value: 5.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678754866 212 GLACLHLATLN----RQHQILKLL--VKKGADL----NIQEGTS---GKTALHLATELHDMTSVKLLLSRGANVDAA--- 275
Cdd:cd22196    47 GKTCLLKAMLNlhngQNDTISLLLdiAEKTGNLkefvNAAYTDSyykGQTALHIAIERRNMHLVELLVQNGADVHARasg 126

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1678754866 276 -----------MFNGCTPLHLAVGRQDAAIANLLCQS 301
Cdd:cd22196   127 effkkkkggpgFYFGELPLSLAACTNQLDIVKFLLEN 163
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 211-241 7.58e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 33.80  E-value: 7.58e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1678754866 211 RGLACLHLATLNRQH-QILKLLVKKGADLNIQ 241
Cdd:pfam00023   1 DGNTPLHLAAGRRGNlEIVKLLLSKGADVNAR 32
 
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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