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Conserved domains on  [gi|1205974750|ref|XP_021301268|]
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26S proteasome non-ATPase regulatory subunit 10 [Sorghum bicolor]

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];
89-270 2.16e-30

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 118.13  E-value: 2.16e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205974750  89 PLHLAAANGNAEMCRFLIKVGDVDVDAADSDGATPLIFAIQGlGSTTVVRLLLNNGANLNKADNSGVAPLHIAAERGLYE 168
Cdd:COG0666    56 LLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARN-GDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLE 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205974750 169 VAELLLSREAEVDLMCENGGAPIHIAAENGHAKFLKLLLQHEADYNAGDP--VTALVIAAGKGLTDCIKCLLKAGADANI 246
Cdd:COG0666   135 IVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNdgETPLHLAAENGHLEIVKLLLEAGADVNA 214

                         170       180
                  ....*....|....*....|....
gi 1205974750 247 PDEDGKLPVQIAACQGWKECVEIL 270
Cdd:COG0666   215 KDNDGKTALDLAAENGNLEIVKLL 238
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
89-270 2.16e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 118.13  E-value: 2.16e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205974750  89 PLHLAAANGNAEMCRFLIKVGDVDVDAADSDGATPLIFAIQGlGSTTVVRLLLNNGANLNKADNSGVAPLHIAAERGLYE 168
Cdd:COG0666    56 LLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARN-GDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLE 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205974750 169 VAELLLSREAEVDLMCENGGAPIHIAAENGHAKFLKLLLQHEADYNAGDP--VTALVIAAGKGLTDCIKCLLKAGADANI 246
Cdd:COG0666   135 IVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNdgETPLHLAAENGHLEIVKLLLEAGADVNA 214

                         170       180
                  ....*....|....*....|....
gi 1205974750 247 PDEDGKLPVQIAACQGWKECVEIL 270
Cdd:COG0666   215 KDNDGKTALDLAAENGNLEIVKLL 238
Ank_2 pfam12796
Ankyrin repeats (3 copies);
158-248 7.05e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 83.63  E-value: 7.05e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205974750 158 LHIAAERGLYEVAELLLSREAEVDLMCENGGAPIHIAAENGHAKFLKLLLQHEADYNAGDPVTALVIAAGKGLTDCIKCL 237
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGRTALHYAARSGHLEIVKLL 80

                          90
                  ....*....|.
gi 1205974750 238 LKAGADANIPD 248
Cdd:pfam12796  81 LEKGADINVKD 91
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 154-260 3.13e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 58.08  E-value: 3.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205974750 154 GVAPLHIAAERGLYEVAELLLSREAEVDLMCENGGAPIHIAAENGHAKFLKLLLQHEADYNAGD--PVTALVIAAGKGLT 231
Cdd:PHA02875  102 GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDccGCTPLIIAMAKGDI 181

                          90       100
                  ....*....|....*....|....*....
gi 1205974750 232 DCIKCLLKAGADaniPDEDGKLPVQIAAC 260
Cdd:PHA02875  182 AICKMLLDSGAN---IDYFGKNGCVAALC 207
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 190-215 4.68e-04

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: 37.18  E-value: 4.68e-04
                           10        20
                   ....*....|....*....|....*.
gi 1205974750  190 PIHIAAENGHAKFLKLLLQHEADYNA 215
Cdd:smart00248   5 PLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 154-217 2.12e-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: 40.06  E-value: 2.12e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1205974750 154 GVAPLHIAAERGLYEVAELLLSREAEVDLMCE--------------NGGAPIHIAAENGHAKFLKLLLQHEADYNAGD 217
Cdd:TIGR00870 128 GITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAAACLGSPSIVALLSEDPADILTAD 205
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 44-262 5.26e-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: 5.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205974750  44 LLNAALEGDLSRVKELVEElneegKGVDeVVTAAAVGVTGtkrrgpLHLAAANGNAEMCRFLIKvgdvdvdaadsdGATP 123
Cdd:cd22192    21 LLLAAKENDVQAIKKLLKC-----PSCD-LFQRGALGETA------LHVAALYDNLEAAVVLME------------AAPE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205974750 124 LIFaiQGLGSTTVVrlllnnganlnkadnsGVAPLHIAAERGLYEVAELLLSREAEV--------------DLMCENGGA 189
Cdd:cd22192    77 LVN--EPMTSDLYQ----------------GETALHIAVVNQNLNLVRELIARGADVvspratgtffrpgpKNLIYYGEH 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205974750 190 PIHIAAENGHAKFLKLLLQHEADYNAGD-----PVTALVIAAGKGL-TDCIKCLLKAGADAN------IPDEDGKLPVQI 257
Cdd:cd22192   139 PLSFAACVGNEEIVRLLIEHGADIRAQDslgntVLHILVLQPNKTFaCQMYDLILSYDKEDDlqpldlVPNNQGLTPFKL 218


                  ....*
gi 1205974750 258 AACQG 262
Cdd:cd22192   219 AAKEG 223
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
89-270 2.16e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 118.13  E-value: 2.16e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205974750  89 PLHLAAANGNAEMCRFLIKVGDVDVDAADSDGATPLIFAIQGlGSTTVVRLLLNNGANLNKADNSGVAPLHIAAERGLYE 168
Cdd:COG0666    56 LLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARN-GDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLE 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205974750 169 VAELLLSREAEVDLMCENGGAPIHIAAENGHAKFLKLLLQHEADYNAGDP--VTALVIAAGKGLTDCIKCLLKAGADANI 246
Cdd:COG0666   135 IVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNdgETPLHLAAENGHLEIVKLLLEAGADVNA 214

                         170       180
                  ....*....|....*....|....
gi 1205974750 247 PDEDGKLPVQIAACQGWKECVEIL 270
Cdd:COG0666   215 KDNDGKTALDLAAENGNLEIVKLL 238
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
89-270 3.21e-28

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 111.97  E-value: 3.21e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205974750  89 PLHLAAANGNAEMCRFLIKVGDVDVDAADSDGATPLIFAIQGLGSTTVVRLLLNNGANLNKADNSGVAPLHIAAERGLYE 168
Cdd:COG0666    22 ALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLE 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205974750 169 VAELLLSREAEVDLMCENGGAPIHIAAENGHAKFLKLLLQHEADYNAGDP--VTALVIAAGKGLTDCIKCLLKAGADANI 246
Cdd:COG0666   102 IVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNdgNTPLHLAAANGNLEIVKLLLEAGADVNA 181

                         170       180
                  ....*....|....*....|....
gi 1205974750 247 PDEDGKLPVQIAACQGWKECVEIL 270
Cdd:COG0666   182 RDNDGETPLHLAAENGHLEIVKLL 205
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
89-270 1.27e-25

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 105.04  E-value: 1.27e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205974750  89 PLHLAAANGNAEMCRFLIKVGDVDVDAADSdGATPLIFAIQGlGSTTVVRLLLNNGANLNKADNSGVAPLHIAAERGLYE 168
Cdd:COG0666    90 LLHAAARNGDLEIVKLLLEAGADVNARDKD-GETPLHLAAYN-GNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLE 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205974750 169 VAELLLSREAEVDLMCENGGAPIHIAAENGHAKFLKLLLQHEADYNAGDP--VTALVIAAGKGLTDCIKCLLKAGADANI 246
Cdd:COG0666   168 IVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNdgKTALDLAAENGNLEIVKLLLEAGADLNA 247

                         170       180
                  ....*....|....*....|....
gi 1205974750 247 PDEDGKLPVQIAACQGWKECVEIL 270
Cdd:COG0666   248 KDKDGLTALLLAAAAGAALIVKLL 271
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
44-253 1.75e-20

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 90.78  E-value: 1.75e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205974750  44 LLNAALEGDLSRVKELVEelneegKGVDevvtaaaVGVTGTKRRGPLHLAAANGNAEMCRFLIKVGDVDVDAADSdGATP 123
Cdd:COG0666    91 LHAAARNGDLEIVKLLLE------AGAD-------VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDND-GNTP 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205974750 124 LIFAIQGlGSTTVVRLLLNNGANLNKADNSGVAPLHIAAERGLYEVAELLLSREAEVDLMCENGGAPIHIAAENGHAKFL 203
Cdd:COG0666   157 LHLAAAN-GNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIV 235

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1205974750 204 KLLLQHEADYNAGDP--VTALVIAAGKGLTDCIKCLLKAGADANIPDEDGKL 253
Cdd:COG0666   236 KLLLEAGADLNAKDKdgLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
Ank_2 pfam12796
Ankyrin repeats (3 copies);
158-248 7.05e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 83.63  E-value: 7.05e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205974750 158 LHIAAERGLYEVAELLLSREAEVDLMCENGGAPIHIAAENGHAKFLKLLLQHEADYNAGDPVTALVIAAGKGLTDCIKCL 237
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGRTALHYAARSGHLEIVKLL 80

                          90
                  ....*....|.
gi 1205974750 238 LKAGADANIPD 248
Cdd:pfam12796  81 LEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
121-270 4.26e-19

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 86.55  E-value: 4.26e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205974750 121 ATPLIFAIQGLGSTTVVRLLLNNGANLNKADNSGVAPLHIAAERGLYEVAELLLSREAEVDLMCENGGAPIHIAAENGHA 200
Cdd:COG0666    21 LALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDL 100

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1205974750 201 KFLKLLLQHEADYNAGDP--VTALVIAAGKGLTDCIKCLLKAGADANIPDEDGKLPVQIAACQGWKECVEIL 270
Cdd:COG0666   101 EIVKLLLEAGADVNARDKdgETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLL 172
Ank_2 pfam12796
Ankyrin repeats (3 copies);
90-217 7.64e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 69.37  E-value: 7.64e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205974750  90 LHLAAANGNAEMCRFLIKVGDVDVDAadsdgatplifaiqglgsttvvrlllnnganlnkaDNSGVAPLHIAAERGLYEV 169
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQ-----------------------------------DKNGRTALHLAAKNGHLEI 45

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1205974750 170 AELLLSrEAEVDlMCENGGAPIHIAAENGHAKFLKLLLQHEADYNAGD 217
Cdd:pfam12796  46 VKLLLE-HADVN-LKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
191-270 8.30e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 66.68  E-value: 8.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205974750 191 IHIAAENGHAKFLKLLLQHEADYNAGDP--VTALVIAAGKGLTDCIKCLLKaGADANIPDeDGKLPVQIAACQGWKECVE 268
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKngRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78


                  ..
gi 1205974750 269 IL 270
Cdd:pfam12796  79 LL 80
Ank_2 pfam12796
Ankyrin repeats (3 copies);
44-183 3.31e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 56.28  E-value: 3.31e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205974750  44 LLNAALEGDLSRVKELVEELNEegkgvdevvtaaaVGVTGTKRRGPLHLAAANGNAEMCRFLIKvgdvdvdaadsdgatp 123
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGAD-------------ANLQDKNGRTALHLAAKNGHLEIVKLLLE---------------- 51

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205974750 124 lifaiqglgsttvvrlllnngANLNKADNSGVAPLHIAAERGLYEVAELLLSREAEVDLM 183
Cdd:pfam12796  52 ---------------------HADVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINVK 90
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 154-260 3.13e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 58.08  E-value: 3.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205974750 154 GVAPLHIAAERGLYEVAELLLSREAEVDLMCENGGAPIHIAAENGHAKFLKLLLQHEADYNAGD--PVTALVIAAGKGLT 231
Cdd:PHA02875  102 GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDccGCTPLIIAMAKGDI 181

                          90       100
                  ....*....|....*....|....*....
gi 1205974750 232 DCIKCLLKAGADaniPDEDGKLPVQIAAC 260
Cdd:PHA02875  182 AICKMLLDSGAN---IDYFGKNGCVAALC 207
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 145-259 3.60e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 58.14  E-value: 3.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205974750 145 ANLNKADNSGVAPLHIAA--ERGLYEVAELLLSREAEVDLMCENGGAPIHIAAENGHAKF--LKLLLQHEADYNAGDPV- 219
Cdd:PHA03100   97 ANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLkiLKLLIDKGVDINAKNRVn 176

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1205974750 220 -----------------TALVIAAGKGLTDCIKCLLKAGADANIPDEDGKLPVQIAA 259
Cdd:PHA03100  177 yllsygvpinikdvygfTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAI 233
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 151-270 1.32e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 56.80  E-value: 1.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205974750 151 DNSGVAPLHIAAERGLYEVAELLLSREAEVDLMCENGGAPIHIAAENGHAKFLKLLLQHEAdynAGDPVTA---LVIAAG 227
Cdd:PLN03192  555 DSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFAS---ISDPHAAgdlLCTAAK 631

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1205974750 228 KGLTDCIKCLLKAGADANIPDEDGKLPVQIAACQGWKECVEIL 270
Cdd:PLN03192  632 RNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLL 674
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 42-246 4.17e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 54.61  E-value: 4.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205974750  42 AELLNAALEGDLSRVkelvEELNEEGKGVDEVVTAAavGVTgtkrrgPLHLAAANGNAEMCRFLIKvgdvdvdaadsDGA 121
Cdd:PHA02875   70 SELHDAVEEGDVKAV----EELLDLGKFADDVFYKD--GMT------PLHLATILKKLDIMKLLIA-----------RGA 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205974750 122 TPLIfaiqglgsttvvrlllnnganlnkADNSGVAPLHIAAERGLYEVAELLLSREAEVDLMCENGGAPIHIAAENGHAK 201
Cdd:PHA02875  127 DPDI------------------------PNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIA 182

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1205974750 202 FLKLLLQHEA--DYNAGDP-VTALVIAAGKGLTDCIKCLLKAGADANI 246
Cdd:PHA02875  183 ICKMLLDSGAniDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCNI 230
Ank_4 pfam13637
Ankyrin repeats (many copies);
157-207 7.06e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.42  E-value: 7.06e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1205974750 157 PLHIAAERGLYEVAELLLSREAEVDLMCENGGAPIHIAAENGHAKFLKLLL 207
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 149-246 1.86e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 52.96  E-value: 1.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205974750 149 KADNSGVAPLHIAAERGLYEVAELLLSREAEVDLMCENGGAPIHIAAENGHAKFLKLLLQHEADYNAGDPV--TALVIAA 226
Cdd:PHA02878  163 KDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCgnTPLHISV 242

                          90       100
                  ....*....|....*....|.
gi 1205974750 227 GKGLT-DCIKCLLKAGADANI 246
Cdd:PHA02878  243 GYCKDyDILKLLLEHGVDVNA 263
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 81-269 7.07e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 51.03  E-value: 7.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205974750  81 VTGTKRRGPLHLAAANGNAEMCRFLIkvgdvdvdaadSDGATPLIfaiqglgsttvvrlllnnganLNKADNSgvaPLHI 160
Cdd:PHA02878  163 KDRHKGNTALHYATENKDQRLTELLL-----------SYGANVNI---------------------PDKTNNS---PLHH 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205974750 161 AAERGLYEVAELLLSREAEVDLMCENGGAPIHIAAenGHAK---FLKLLLQHEADYNAGDPV---TALVIAAGKglTDCI 234
Cdd:PHA02878  208 AVKHYNKPIVHILLENGASTDARDKCGNTPLHISV--GYCKdydILKLLLEHGVDVNAKSYIlglTALHSSIKS--ERKL 283

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1205974750 235 KCLLKAGADANIPDEDGKLPVQIAACQgwKECVEI 269
Cdd:PHA02878  284 KLLLEYGADINSLNSYKLTPLSSAVKQ--YLCINI 316
Ank_5 pfam13857
Ankyrin repeats (many copies);
206-258 5.23e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.49  E-value: 5.23e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1205974750 206 LLQH---EADYNAGDPVTALVIAAGKGLTDCIKCLLKAGADANIPDEDGKLPVQIA 258
Cdd:pfam13857   1 LLEHgpiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 79-258 8.32e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 47.65  E-value: 8.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205974750  79 VGVTGTKRRGPLHLAAANGNAEMCRFLIKVGDVDVDAADSdGATPLIFAIQGlGSTTVVRLLLNNGANLNKADNSGVAPL 158
Cdd:PHA02874  117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDN-GCYPIHIAIKH-NFFDIIKLLLEKGAYANVKDNNGESPL 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205974750 159 HIAAERGLYEVAELLLSREAEVDLMCENGGAPIHIAAENGHAKfLKLLLQHEA----DYNAGDPV-TALVIAAGKgltDC 233
Cdd:PHA02874  195 HNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSA-IELLINNASindqDIDGSTPLhHAINPPCDI---DI 270

                         170       180
                  ....*....|....*....|....*
gi 1205974750 234 IKCLLKAGADANIPDEDGKLPVQIA 258
Cdd:PHA02874  271 IDILLYHKADISIKDNKGENPIDTA 295
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 181-271 1.37e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 47.17  E-value: 1.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205974750 181 DLMCENGG--------APIHIAAENGHAKFLKLLLQHEADYNAGDPV--TALVIAAGKGLTDCIKCLLKAGADANIPDED 250
Cdd:PLN03192  511 DLLGDNGGehddpnmaSNLLTVASTGNAALLEELLKAKLDPDIGDSKgrTPLHIAASKGYEDCVLVLLKHACNVHIRDAN 590

                          90       100
                  ....*....|....*....|.
gi 1205974750 251 GKLPVQIAACQGWKECVEILF 271
Cdd:PLN03192  591 GNTALWNAISAKHHKIFRILY 611
Ank_4 pfam13637
Ankyrin repeats (many copies);
190-238 9.51e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.95  E-value: 9.51e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1205974750 190 PIHIAAENGHAKFLKLLLQHEADYNA--GDPVTALVIAAGKGLTDCIKCLL 238
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKGADINAvdGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 192-270 9.89e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.50  E-value: 9.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205974750 192 HIAAeNGHAKFLKLLLQHEADYNAGD--PVTALVIAAGKGLTDCIKCLLKAGADANIPDEDGKLPVQIAACQGWKECVEI 269
Cdd:PTZ00322   88 QLAA-SGDAVGARILLTGGADPNCRDydGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                  .
gi 1205974750 270 L 270
Cdd:PTZ00322  167 L 167
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 151-217 1.20e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.12  E-value: 1.20e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1205974750 151 DNSGVAPLHIAAERGLYEVAELLLSREAEVDLMCENGGAPIHIAAENGHAKFLKLLLQHEADYNAGD 217
Cdd:PTZ00322  112 DYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELG 178
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 155-270 4.02e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 42.26  E-value: 4.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205974750 155 VAPLHIAAERGLYEVAELLLSREAEVDLMCENGGAPIHIAAENGHAKFLKLLLQHEAD-----------------YNAGD 217
Cdd:PHA02874   36 TTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDtsilpipciekdmiktiLDCGI 115

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1205974750 218 PV--------TALVIAAGKGLTDCIKCLLKAGADANIPDEDGKLPVQIAACQGWKECVEIL 270
Cdd:PHA02874  116 DVnikdaelkTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLL 176
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 190-215 4.68e-04

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: 37.18  E-value: 4.68e-04
                           10        20
                   ....*....|....*....|....*.
gi 1205974750  190 PIHIAAENGHAKFLKLLLQHEADYNA 215
Cdd:smart00248   5 PLHLAAENGNLEVVKLLLDKGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
220-270 4.77e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 37.64  E-value: 4.77e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1205974750 220 TALVIAAGKGLTDCIKCLLKAGADANIPDEDGKLPVQIAACQGWKECVEIL 270
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
Ank_5 pfam13857
Ankyrin repeats (many copies);
151-194 7.00e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.33  E-value: 7.00e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1205974750 151 DNSGVAPLHIAAERGLYEVAELLLSREAEVDLMCENGGAPIHIA 194
Cdd:pfam13857  13 DGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 186-215 1.30e-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: 36.08  E-value: 1.30e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1205974750 186 NGGAPIHIAAENGHAKFLKLLLQHEADYNA 215
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 87-259 1.68e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 40.43  E-value: 1.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205974750  87 RGPLHLAAANGNAEMCRFLIKVGdVDVDAADSDGATPLIFAIQGLGSTTvVRLLLNNGANLNKAD--------------- 151
Cdd:PHA02876  179 ITPIHYAAERGNAKMVNLLLSYG-ADVNIIALDDLSVLECAVDSKNIDT-IKAIIDNRSNINKNDlsllkairnedlets 256

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205974750 152 ----NSGVA----------PLHIAAER-GLYEVAELLLSREAEVDLMCENGGAPIHIAAENGH-AKFLKLLLQHEADYNA 215
Cdd:PHA02876  257 lllyDAGFSvnsiddckntPLHHASQApSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNA 336

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1205974750 216 GDPVTALVIAAGKGL---TDCIKCLLKAGADANIPDEDGKLPVQIAA 259
Cdd:PHA02876  337 ADRLYITPLHQASTLdrnKDIVITLLELGANVNARDYCDKTPIHYAA 383
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 154-217 2.12e-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: 40.06  E-value: 2.12e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1205974750 154 GVAPLHIAAERGLYEVAELLLSREAEVDLMCE--------------NGGAPIHIAAENGHAKFLKLLLQHEADYNAGD 217
Cdd:TIGR00870 128 GITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAAACLGSPSIVALLSEDPADILTAD 205
PHA03095 PHA03095
ankyrin-like protein; Provisional
 77-255 2.22e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 40.01  E-value: 2.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205974750  77 AAVGVTGTKRRGPLH--LAAANGNAEMCRFLIKVGDVDVDAADSdGATPL-IFAIQGLGSTTVVRLLLNNGANLNKADNS 153
Cdd:PHA03095  108 ADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLY-GMTPLaVLLKSRNANVELLRLLIDAGADVYAVDDR 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205974750 154 GVAPLHIAAE--RGLYEVAELLLSREAEVDLMCENGGAPIHIAAENGHAKFLKL--LLQHEADYNAGDPV--TALVIAAG 227
Cdd:PHA03095  187 FRSLLHHHLQsfKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYgqTPLHYAAV 266

                         170       180
                  ....*....|....*....|....*...
gi 1205974750 228 KGLTDCIKCLLKAGADANIPDEDGKLPV 255
Cdd:PHA03095  267 FNNPRACRRLIALGADINAVSSDGNTPL 294
PHA02743 PHA02743
Viral ankyrin protein; Provisional
 152-221 4.50e-03

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 37.49  E-value: 4.50e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1205974750 152 NSGVAPLHIAAERGLYEVAElLLSREAEVDLMCENGG--APIHIAAENGHAKFLKLLLQHEADYNagDPVTA 221
Cdd:PHA02743   92 GTGNTLLHIAASTKNYELAE-WLCRQLGVNLGAINYQheTAYHIAYKMRDRRMMEILRANGAVCD--DPLSI 160
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 151-215 5.07e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 38.88  E-value: 5.07e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1205974750 151 DNSGVAPLHIAAERGLYEVAELLLSREAEVDLMCENGGAPIHIAAENGHAKFLKLLLQHEADYNA 215
Cdd:PHA03100  189 DVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 44-262 5.26e-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: 5.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205974750  44 LLNAALEGDLSRVKELVEElneegKGVDeVVTAAAVGVTGtkrrgpLHLAAANGNAEMCRFLIKvgdvdvdaadsdGATP 123
Cdd:cd22192    21 LLLAAKENDVQAIKKLLKC-----PSCD-LFQRGALGETA------LHVAALYDNLEAAVVLME------------AAPE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205974750 124 LIFaiQGLGSTTVVrlllnnganlnkadnsGVAPLHIAAERGLYEVAELLLSREAEV--------------DLMCENGGA 189
Cdd:cd22192    77 LVN--EPMTSDLYQ----------------GETALHIAVVNQNLNLVRELIARGADVvspratgtffrpgpKNLIYYGEH 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205974750 190 PIHIAAENGHAKFLKLLLQHEADYNAGD-----PVTALVIAAGKGL-TDCIKCLLKAGADAN------IPDEDGKLPVQI 257
Cdd:cd22192   139 PLSFAACVGNEEIVRLLIEHGADIRAQDslgntVLHILVLQPNKTFaCQMYDLILSYDKEDDlqpldlVPNNQGLTPFKL 218


                  ....*
gi 1205974750 258 AACQG 262
Cdd:cd22192   219 AAKEG 223
PHA03095 PHA03095
ankyrin-like protein; Provisional
 136-243 5.70e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 38.85  E-value: 5.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205974750 136 VVRLLLNNGANLNKADNSGVAPLHiaaergLY-------EVAELLLSREAEVDLMCENGGAPIHI--AAENGHAKFLKLL 206
Cdd:PHA03095   65 IVRLLLEAGADVNAPERCGFTPLH------LYlynattlDVIKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLL 138

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1205974750 207 LQHEADYNAGD-----PVTALVIAAGKGLtDCIKCLLKAGAD 243
Cdd:PHA03095  139 LRKGADVNALDlygmtPLAVLLKSRNANV-ELLRLLIDAGAD 179
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 157-182 6.40e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.10  E-value: 6.40e-03
                           10        20
                   ....*....|....*....|....*.
gi 1205974750  157 PLHIAAERGLYEVAELLLSREAEVDL 182
Cdd:smart00248   5 PLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 186-217 6.74e-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: 34.19  E-value: 6.74e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1205974750 186 NGGAPIHIAA-ENGHAKFLKLLLQHEADYNAGD 217
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 220-249 8.54e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 33.80  E-value: 8.54e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1205974750 220 TALVIAAGK-GLTDCIKCLLKAGADANIPDE 249
Cdd:pfam00023   4 TPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
 
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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