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Conserved domains on  [gi|1958782630|ref|XP_038968000|]
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ankyrin repeat and SOCS box protein 2 isoform X2 [Rattus norvegicus]

Protein Classification

ankyrin repeat domain-containing protein( domain architecture ID 11430360)

ankyrin repeat (ANK) domain-containing protein 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

CATH:  1.25.40.20
Gene Ontology:  GO:0005515
PubMed:  33435370|15152081|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];
119-400 8.50e-46

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 163.59  E-value: 8.50e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 119 EALKAMIQDGKNLAEPNKEGWLPLHEAAYYGKLGCLKVLQRAYPGTIDQRTLQEETALYLATCREHLDCLLSLLQAGAEP 198
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 199 DISNKSRETPLYKACERKNAEAVRILVQYNADANHRCNRGWTALHESVSRNDLEVMEILVSGGAKVEAKNVYSITPLFVA 278
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 279 AQSGQLEALRFLAKHGADINTQASDSASALYEACKNEHEDVVEFLLSQGADANKANKDGLLPLHVASKKGNYRIVQMLLP 358
Cdd:COG0666   161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1958782630 359 VTSR-TRVRRSGISPLHLAAERNHDAVLEALLAARFDVNTPLA 400
Cdd:COG0666   241 AGADlNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283
Ank_2 pfam12796
Ankyrin repeats (3 copies);
373-469 5.50e-10

Ankyrin repeats (3 copies);


:

Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 56.28  E-value: 5.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 373 LHLAAERNHDAVLEALLAARFDVNtplaperarLYEDRRTSALYFAVVNNNVYATELLLlAGADPNRDVI--SPLLVAIR 450
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADAN---------LQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKDNgrTALHYAAR 70

                          90
                  ....*....|....*....
gi 1958782630 451 HGCLRTMQLLLDHGANIDA 469
Cdd:pfam12796  71 SGHLEIVKLLLEKGADINV 89
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
119-400 8.50e-46

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 163.59  E-value: 8.50e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 119 EALKAMIQDGKNLAEPNKEGWLPLHEAAYYGKLGCLKVLQRAYPGTIDQRTLQEETALYLATCREHLDCLLSLLQAGAEP 198
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 199 DISNKSRETPLYKACERKNAEAVRILVQYNADANHRCNRGWTALHESVSRNDLEVMEILVSGGAKVEAKNVYSITPLFVA 278
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 279 AQSGQLEALRFLAKHGADINTQASDSASALYEACKNEHEDVVEFLLSQGADANKANKDGLLPLHVASKKGNYRIVQMLLP 358
Cdd:COG0666   161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1958782630 359 VTSR-TRVRRSGISPLHLAAERNHDAVLEALLAARFDVNTPLA 400
Cdd:COG0666   241 AGADlNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283
PHA03095 PHA03095
ankyrin-like protein; Provisional
 199-480 1.27e-23

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 104.34  E-value: 1.27e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 199 DISNKSRETPLYK---ACERKNAEAVRILVQYNADANHRCNRGWTALHESVSRN---DLEVMEILVSGGAKVEAKNVYSI 272
Cdd:PHA03095    5 ESVDIIMEAALYDyllNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSsekVKDIVRLLLEAGADVNAPERCGF 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 273 TPLFVAAQSGQ-LEALRFLAKHGADINTQ--ASDSASALYEACKNEHEDVVEFLLSQGADANKANKDGLLPLHV--ASKK 347
Cdd:PHA03095   85 TPLHLYLYNATtLDVIKLLIKAGADVNAKdkVGRTPLHVYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVllKSRN 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 348 GNYRIVQMLLPVTSRTRVRRS-GISPLHLAAE--RNHDAVLEALLAARFDV-------NTPL------APERARL----- 406
Cdd:PHA03095  165 ANVELLRLLIDAGADVYAVDDrFRSLLHHHLQsfKPRARIVRELIRAGCDPaatdmlgNTPLhsmatgSSCKRSLvlpll 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 407 -------YEDRR-TSALYFAVVNNNVYATELLLLAGADPN---RDVISPLLVAIRHGCLRTMQLLLDHGANIDAYIATHP 475
Cdd:PHA03095  245 iagisinARNRYgQTPLHYAAVFNNPRACRRLIALGADINavsSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAATLN 324


                  ....*
gi 1958782630 476 TAFPA 480
Cdd:PHA03095  325 TASVA 329
Ank_2 pfam12796
Ankyrin repeats (3 copies);
176-268 3.44e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.77  E-value: 3.44e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 176 LYLATCREHLDCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVRILVQYnADANHRCNrGWTALHESVSRNDLEVME 255
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1958782630 256 ILVSGGAKVEAKN 268
Cdd:pfam12796  79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
373-469 5.50e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 56.28  E-value: 5.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 373 LHLAAERNHDAVLEALLAARFDVNtplaperarLYEDRRTSALYFAVVNNNVYATELLLlAGADPNRDVI--SPLLVAIR 450
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADAN---------LQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKDNgrTALHYAAR 70

                          90
                  ....*....|....*....
gi 1958782630 451 HGCLRTMQLLLDHGANIDA 469
Cdd:pfam12796  71 SGHLEIVKLLLEKGADINV 89
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 140-357 1.32e-09

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: 60.80  E-value: 1.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 140 LPLHEAAYYGKLGCLKVLQRAYPGTIDQRTLQEETALYLATCREHLDCLLSLLQAGaePDISNKSRETPLYKacerknae 219
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAA--PELVNEPMTSDLYQ-------- 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 220 avrilvqynadanhrcnrGWTALHESVSRNDLEVMEILVSGGAKV------------EAKNV--YSITPLFVAAQSGQLE 285
Cdd:cd22192    89 ------------------GETALHIAVVNQNLNLVRELIARGADVvspratgtffrpGPKNLiyYGEHPLSFAACVGNEE 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 286 ALRFLAKHGADINTQASDSASALY----EACKNEHEDVVEFLLSQGADANKA------NKDGLLPLHVASKKGNYRIVQM 355
Cdd:cd22192   151 IVRLLIEHGADIRAQDSLGNTVLHilvlQPNKTFACQMYDLILSYDKEDDLQpldlvpNNQGLTPFKLAAKEGNIVMFQH 230


                  ..
gi 1958782630 356 LL 357
Cdd:cd22192   231 LV 232
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 237-357 4.93e-07

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: 52.78  E-value: 4.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 237 RGWTALHESVSRNDLEVMEILVSGGAKVEAKNV--------------YSITPLFVAAQSGQLEALRFLAKHGADINTQAS 302
Cdd:TIGR00870 127 PGITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAAACLGSPSIVALLSEDPADILTADS 206

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958782630 303 DS-----ASALYEACKNEHEDVV----EFLLSQGADANKA-------NKDGLLPLHVASKKGNYRIVQMLL 357
Cdd:TIGR00870 207 LGntllhLLVMENEFKAEYEELScqmyNFALSLLDKLRDSkelevilNHQGLTPLKLAAKEGRIVLFRLKL 277
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 339-486 6.93e-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: 6.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 339 LPLHVASKKGNYRIVQMLLpVTSRTRVRRSGI---SPLHLAAERNHDAVLEALL-AARFDVNTPLAPErarLYEDRrtSA 414
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLL-KCPSCDLFQRGAlgeTALHVAALYDNLEAAVVLMeAAPELVNEPMTSD---LYQGE--TA 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 415 LYFAVVNNNVYATELLLLAGAD------------PNRDVI-----SPLLVAIRHGCLRTMQLLLDHGANIDA-------- 469
Cdd:cd22192    93 LHIAVVNQNLNLVRELIARGADvvspratgtffrPGPKNLiyygeHPLSFAACVGNEEIVRLLIEHGADIRAqdslgntv 172

                         170
                  ....*....|....*....
gi 1958782630 470 --YIATHPTAFPATIMFAM 486
Cdd:cd22192   173 lhILVLQPNKTFACQMYDL 191
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 406-503 1.30e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 47.29  E-value: 1.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 406 LYEDRRTSALYFAVVNNNVYATELLLLAGADPNR----DVISPLLVAIRHGCLRTMQLLLDHGANIDAYIATHPTAFPAT 481
Cdd:PHA02884   65 LSENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRyaeeAKITPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPIELA 144

                          90       100
                  ....*....|....*....|..
gi 1958782630 482 IMFamkCLSLLKFLMdlgCDGE 503
Cdd:PHA02884  145 LMI---CNNFLAFMI---CDNE 160
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 273-298 1.64e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.03  E-value: 1.64e-03
                           10        20
                   ....*....|....*....|....*.
gi 1958782630  273 TPLFVAAQSGQLEALRFLAKHGADIN 298
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADIN 29
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
119-400 8.50e-46

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 163.59  E-value: 8.50e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 119 EALKAMIQDGKNLAEPNKEGWLPLHEAAYYGKLGCLKVLQRAYPGTIDQRTLQEETALYLATCREHLDCLLSLLQAGAEP 198
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 199 DISNKSRETPLYKACERKNAEAVRILVQYNADANHRCNRGWTALHESVSRNDLEVMEILVSGGAKVEAKNVYSITPLFVA 278
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 279 AQSGQLEALRFLAKHGADINTQASDSASALYEACKNEHEDVVEFLLSQGADANKANKDGLLPLHVASKKGNYRIVQMLLP 358
Cdd:COG0666   161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1958782630 359 VTSR-TRVRRSGISPLHLAAERNHDAVLEALLAARFDVNTPLA 400
Cdd:COG0666   241 AGADlNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
110-357 3.53e-44

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 159.35  E-value: 3.53e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 110 LKAIKEGDEEALKAMIQDGKNLAEPNKEGWLPLHEAAYYGKLGCLKVLQRAYPGTIDQRTLQEETALYLATCREHLDCLL 189
Cdd:COG0666    25 LLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVK 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 190 SLLQAGAEPDISNKSRETPLYKACERKNAEAVRILVQYNADANHRCNRGWTALHESVSRNDLEVMEILVSGGAKVEAKNV 269
Cdd:COG0666   105 LLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDN 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 270 YSITPLFVAAQSGQLEALRFLAKHGADINTQASDSASALYEACKNEHEDVVEFLLSQGADANKANKDGLLPLHVASKKGN 349
Cdd:COG0666   185 DGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGA 264


                  ....*...
gi 1958782630 350 YRIVQMLL 357
Cdd:COG0666   265 ALIVKLLL 272
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
165-438 1.64e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 152.03  E-value: 1.64e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 165 IDQRTLQEETALYLATCREHLDCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVRILVQYNADANHRCNRGWTALHE 244
Cdd:COG0666    14 ALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHA 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 245 SVSRNDLEVMEILVSGGAKVEAKNVYSITPLFVAAQSGQLEALRFLAKHGADINTQASDSASALYEACKNEHEDVVEFLL 324
Cdd:COG0666    94 AARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLL 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 325 SQGADANKANKDGLLPLHVASKKGNYRIVQMLL----PVTSRTRvrrSGISPLHLAAERNHDAVLEALLAARFDVNTPLa 400
Cdd:COG0666   174 EAGADVNARDNDGETPLHLAAENGHLEIVKLLLeagaDVNAKDN---DGKTALDLAAENGNLEIVKLLLEAGADLNAKD- 249

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1958782630 401 perarlyeDRRTSALYFAVVNNNVYATELLLLAGADPN 438
Cdd:COG0666   250 --------KDGLTALLLAAAAGAALIVKLLLLALLLLA 279
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
110-341 7.66e-40

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 147.41  E-value: 7.66e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 110 LKAIKEGDEEALKAMIQDGKNLAEPNKEGWLPLHEAAYYGKLGCLKVLQRAyPGTIDQRTLQEETALYLATCREHLDCLL 189
Cdd:COG0666    59 LAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEA-GADVNARDKDGETPLHLAAYNGNLEIVK 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 190 SLLQAGAEPDISNKSRETPLYKACERKNAEAVRILVQYNADANHRCNRGWTALHESVSRNDLEVMEILVSGGAKVEAKNV 269
Cdd:COG0666   138 LLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN 217

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958782630 270 YSITPLFVAAQSGQLEALRFLAKHGADINTQASDSASALYEACKNEHEDVVEFLLSQGADANKANKDGLLPL 341
Cdd:COG0666   218 DGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
188-477 1.48e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 135.47  E-value: 1.48e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 188 LLSLLQAGAEPDISNKSRETPLYKACERKNAEAVRILVQYNADANHRCNRGWTALHESVSRNDLEVMEILVSGGAKVEAK 267
Cdd:COG0666     4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 268 NVYSITPLFVAAQSGQLEALRFLAKHGADINTQASDSASALYEACKNEHEDVVEFLLSQGADANKANKDGllplhvaskk 347
Cdd:COG0666    84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDG---------- 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 348 gnyrivqmllpvtsrtrvrrsgISPLHLAAERNHDAVLEALLAARFDVNTPlaperarlyEDRRTSALYFAVVNNNVYAT 427
Cdd:COG0666   154 ----------------------NTPLHLAAANGNLEIVKLLLEAGADVNAR---------DNDGETPLHLAAENGHLEIV 202

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958782630 428 ELLLLAGADPN---RDVISPLLVAIRHGCLRTMQLLLDHGANIDAYIATHPTA 477
Cdd:COG0666   203 KLLLEAGADVNakdNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTA 255
PHA03095 PHA03095
ankyrin-like protein; Provisional
 199-480 1.27e-23

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 104.34  E-value: 1.27e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 199 DISNKSRETPLYK---ACERKNAEAVRILVQYNADANHRCNRGWTALHESVSRN---DLEVMEILVSGGAKVEAKNVYSI 272
Cdd:PHA03095    5 ESVDIIMEAALYDyllNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSsekVKDIVRLLLEAGADVNAPERCGF 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 273 TPLFVAAQSGQ-LEALRFLAKHGADINTQ--ASDSASALYEACKNEHEDVVEFLLSQGADANKANKDGLLPLHV--ASKK 347
Cdd:PHA03095   85 TPLHLYLYNATtLDVIKLLIKAGADVNAKdkVGRTPLHVYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVllKSRN 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 348 GNYRIVQMLLPVTSRTRVRRS-GISPLHLAAE--RNHDAVLEALLAARFDV-------NTPL------APERARL----- 406
Cdd:PHA03095  165 ANVELLRLLIDAGADVYAVDDrFRSLLHHHLQsfKPRARIVRELIRAGCDPaatdmlgNTPLhsmatgSSCKRSLvlpll 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 407 -------YEDRR-TSALYFAVVNNNVYATELLLLAGADPN---RDVISPLLVAIRHGCLRTMQLLLDHGANIDAYIATHP 475
Cdd:PHA03095  245 iagisinARNRYgQTPLHYAAVFNNPRACRRLIALGADINavsSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAATLN 324


                  ....*
gi 1958782630 476 TAFPA 480
Cdd:PHA03095  325 TASVA 329
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 150-469 1.69e-23

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 105.15  E-value: 1.69e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 150 KLG--CLKVLQRAYPGTIDQRTLQEETALYLATCREHL--DCLL---SLLQAGAEPDISNKSRETPLYKACERKNAEAVR 222
Cdd:PHA02876  116 KLDeaCIHILKEAISGNDIHYDKINESIEYMKLIKERIqqDELLiaeMLLEGGADVNAKDIYCITPIHYAAERGNAKMVN 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 223 ILVQYNADAN-----------------------------HRCNRGWTALHESVSRNDLEVMEILVSGGAKVEAKNVYSIT 273
Cdd:PHA02876  196 LLLSYGADVNiialddlsvlecavdsknidtikaiidnrSNINKNDLSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNT 275

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 274 PLFVAAQSGQLEAL-RFLAKHGADINTQASDSASALYEACKNEHE-DVVEFLLSQGADANKANKDGLLPLHVASKKGNYR 351
Cdd:PHA02876  276 PLHHASQAPSLSRLvPKLLERGADVNAKNIKGETPLYLMAKNGYDtENIRTLIMLGADVNAADRLYITPLHQASTLDRNK 355

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 352 -IVQMLLPVTSRTRVRR-SGISPLHLAAERNHDAVLEALLAARFDVNTplaperarlYEDRRTSALYFAVVNNNVY-ATE 428
Cdd:PHA02876  356 dIVITLLELGANVNARDyCDKTPIHYAAVRNNVVIINTLLDYGADIEA---------LSQKIGTALHFALCGTNPYmSVK 426

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1958782630 429 LLLLAGAD---PNRDVISPLLVAIRHGC-LRTMQLLLDHGANIDA 469
Cdd:PHA02876  427 TLIDRGANvnsKNKDLSTPLHYACKKNCkLDVIEMLLDNGADVNA 471
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 176-357 2.22e-21

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 97.04  E-value: 2.22e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 176 LYLATCREHLDCLLSLLQAGAEPDISNKSRETPL-----YKACERKNAEAVRILVQYNADANHRCNRGWTALHESVSR-- 248
Cdd:PHA03100   39 LYLAKEARNIDVVKILLDNGADINSSTKNNSTPLhylsnIKYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKks 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 249 NDLEVMEILVSGGAKVEAKNVYSITPLFVAAQSGQ--LEALRFLAKHGADINtqASDSA------------------SAL 308
Cdd:PHA03100  119 NSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDIN--AKNRVnyllsygvpinikdvygfTPL 196

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1958782630 309 YEACKNEHEDVVEFLLSQGADANKANKDGLLPLHVASKKGNYRIVQMLL 357
Cdd:PHA03100  197 HYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLL 245
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
284-501 8.22e-21

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 93.09  E-value: 8.22e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 284 LEALRFLAKHGADINTQASDSASALYEACKNEHEDVVEFLLSQGADANKANKDGLLPLHVASKKGNYRIVQMLL-PVTSR 362
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLaAGADI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 363 TRVRRSGISPLHLAAERNHDAVLEALLAARFDVNTPlaperarlyEDRRTSALYFAVVNNNVYATELLLLAGADPN---R 439
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNAR---------DKDGETPLHLAAYNGNLEIVKLLLEAGADVNaqdN 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958782630 440 DVISPLLVAIRHGCLRTMQLLLDHGANIDAYIATHPTAfpatIMFAMKC--LSLLKFLMDLGCD 501
Cdd:COG0666   152 DGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETP----LHLAAENghLEIVKLLLEAGAD 211
Ank_2 pfam12796
Ankyrin repeats (3 copies);
176-268 3.44e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.77  E-value: 3.44e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 176 LYLATCREHLDCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVRILVQYnADANHRCNrGWTALHESVSRNDLEVME 255
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1958782630 256 ILVSGGAKVEAKN 268
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 198-473 3.93e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 87.03  E-value: 3.93e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 198 PDISNKSRETPLYKACERKNAEAVRILVQYNADANHRCNRGWTALH-----ESVSRNDLEVMEILVSGGAKVEAKNVYSI 272
Cdd:PHA03100   28 NDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHylsniKYNLTDVKEIVKLLLEYGANVNAPDNNGI 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 273 TPLFVAAQ--SGQLEALRFLAKHGADINTQASDSASALYEACKNEHED--VVEFLLSQGADANKANK-DGLL----PLHV 343
Cdd:PHA03100  108 TPLLYAISkkSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKGVDINAKNRvNYLLsygvPINI 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 344 ASKKGNyrivqmllpvtsrtrvrrsgiSPLHLAAERNHdavleallaarfdvntplaPErarlyedrrtsalyfaVVNnn 423
Cdd:PHA03100  188 KDVYGF---------------------TPLHYAVYNNN-------------------PE----------------FVK-- 209

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958782630 424 vyateLLLLAGADPN-RDVI--SPLLVAIRHGCLRTMQLLLDHGANIDAYIAT 473
Cdd:PHA03100  210 -----YLLDLGANPNlVNKYgdTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 108-347 7.02e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 86.86  E-value: 7.02e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 108 PVLKAIKEGDEEALKAMIQDGKNLAEPNKEGWLPLH-------------------------------EAAYYGKLGCLK- 155
Cdd:PHA02878   40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHiickepnklgmkemirsinkcsvfytlvaikDAFNNRNVEIFKi 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 156 VLQRAYPGTIDQRTLQEETALYLATCREHLDCLLslLQAGAEPDISNKSR-ETPLYKACERKNAEAVRILVQYNADAN-- 232
Cdd:PHA02878  120 ILTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLL--LSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNip 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 233 HRCNRgwTALHESVSRNDLEVMEILVSGGAKVEAKNVYSITPLFVAAQS-GQLEALRFLAKHGADINTQAS-DSASALYE 310
Cdd:PHA02878  198 DKTNN--SPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYiLGLTALHS 275

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1958782630 311 ACKNEheDVVEFLLSQGADANKANKDGLLPLHVASKK 347
Cdd:PHA02878  276 SIKSE--RKLKLLLEYGADINSLNSYKLTPLSSAVKQ 310
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 92-390 1.37e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 85.40  E-value: 1.37e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630  92 KYSSNLFKTSQMAAMDPVLKAIKEGDEEALKAMIQDGKNLAEPNKEGWLPLHEAAyygKLGCLKVLQRAYPGTIDqrtlq 171
Cdd:PHA02874   22 KNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAI---KIGAHDIIKLLIDNGVD----- 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 172 eeTALYLATCREHlDCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVRILVQYNADANHRCNRGWTALHESVSRNDL 251
Cdd:PHA02874   94 --TSILPIPCIEK-DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFF 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 252 EVMEILVSGGAKVEAKNVYSITPLFVAAQSGQLEALRFLAKHGADINTQASDSASALYEACKNeHEDVVEFLLSQgADAN 331
Cdd:PHA02874  171 DIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIH-NRSAIELLINN-ASIN 248

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958782630 332 KANKDGLLPLHVA-SKKGNYRIVQMLLPVTSRTRVR-RSGISPLHLAAER-NHDAVLEALLA 390
Cdd:PHA02874  249 DQDIDGSTPLHHAiNPPCDIDIIDILLYHKADISIKdNKGENPIDTAFKYiNKDPVIKDIIA 310
Ank_2 pfam12796
Ankyrin repeats (3 copies);
308-397 1.96e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.46  E-value: 1.96e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 308 LYEACKNEHEDVVEFLLSQGADANKANKDGLLPLHVASKKGNYRIVQMLLPvTSRTRVRRSGISPLHLAAERNHDAVLEA 387
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDNGRTALHYAARSGHLEIVKL 79

                          90
                  ....*....|
gi 1958782630 388 LLAARFDVNT 397
Cdd:pfam12796  80 LLEKGADINV 89
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 199-399 4.35e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 83.86  E-value: 4.35e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 199 DISNKSRETPLYKACERKNAEAVRILVQYNADANHRC----NRGWTALheSVSRNDL---------------------EV 253
Cdd:PHA02874   29 NISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINtkipHPLLTAI--KIGAHDIikllidngvdtsilpipciekDM 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 254 MEILVSGGAKVEAKNVYSITPLFVAAQSGQLEALRFLAKHGADINTQASDSASALYEACKNEHEDVVEFLLSQGADANKA 333
Cdd:PHA02874  107 IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVK 186

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958782630 334 NKDGLLPLHVASKKGNYRIVQMLLPVTSRTRVR-RSGISPLHLAAERNHDAVlEALLAARF----DVN--TPL 399
Cdd:PHA02874  187 DNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKcKNGFTPLHNAIIHNRSAI-ELLINNASindqDIDgsTPL 258
Ank_2 pfam12796
Ankyrin repeats (3 copies);
275-357 1.07e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.54  E-value: 1.07e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 275 LFVAAQSGQLEALRFLAKHGADINTQASDSASALYEACKNEHEDVVEFLLSQgADANKANkDGLLPLHVASKKGNYRIVQ 354
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78


                  ...
gi 1958782630 355 MLL 357
Cdd:pfam12796  79 LLL 81
Ank_2 pfam12796
Ankyrin repeats (3 copies);
242-334 1.52e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.15  E-value: 1.52e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 242 LHESVSRNDLEVMEILVSGGAKVEAKNVYSITPLFVAAQSGQLEALRFLAKHgADINTQASDSaSALYEACKNEHEDVVE 321
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGR-TALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1958782630 322 FLLSQGADANKAN 334
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 184-463 1.64e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 82.62  E-value: 1.64e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 184 HLDCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVR-ILVQYNadanhRCNRGWT--ALHESVSRNDLEVMEILVSG 260
Cdd:PHA02878   49 NLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKeMIRSIN-----KCSVFYTlvAIKDAFNNRNVEIFKIILTN 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 261 gakvEAKNVYSITPLFVAAQSG----QLEALRFLAKHGADINTQASDS-ASALYEACKNEHEDVVEFLLSQGADANKANK 335
Cdd:PHA02878  124 ----RYKNIQTIDLVYIDKKSKddiiEAEITKLLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDK 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 336 DGLLPLHVASKKGNYRIVQMLLPVTSRTRVRRS-GISPLHLAAERNHD-AVLEALLAARFDVNtplaperARLYeDRRTS 413
Cdd:PHA02878  200 TNNSPLHHAVKHYNKPIVHILLENGASTDARDKcGNTPLHISVGYCKDyDILKLLLEHGVDVN-------AKSY-ILGLT 271

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958782630 414 ALYFAVVNNNVyaTELLLLAGADPNR---DVISPLLVAIR-HGCLRTMQLLLDH 463
Cdd:PHA02878  272 ALHSSIKSERK--LKLLLEYGADINSlnsYKLTPLSSAVKqYLCINIGRILISN 323
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 109-367 4.42e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 81.65  E-value: 4.42e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 109 VLKAIKEGDEEALKAMIQDGKNLAEPNKEGWLPLHEAAYYGKLGCL--KVLQRAypGTIDQRTLQEETALYL-ATCREHL 185
Cdd:PHA02876  244 LLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLvpKLLERG--ADVNAKNIKGETPLYLmAKNGYDT 321

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 186 DCLLSLLQAGAEPDISNKSRETPLYKACE-RKNAEAVRILVQYNADANHRCNRGWTALHESVSRNDLEVMEILVSGGAKV 264
Cdd:PHA02876  322 ENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADI 401

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 265 EAKNVYSITPL-FVAAQSGQLEALRFLAKHGADINTQASDSASALYEACKNEHE-DVVEFLLSQGADANKANKDGLLPLH 342
Cdd:PHA02876  402 EALSQKIGTALhFALCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNCKlDVIEMLLDNGADVNAINIQNQYPLL 481

                         250       260
                  ....*....|....*....|....*
gi 1958782630 343 VAskKGNYRIVQMLLPVTSRTRVRR 367
Cdd:PHA02876  482 IA--LEYHGIVNILLHYGAELRDSR 504
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 108-298 8.46e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 79.65  E-value: 8.46e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 108 PVLKAIKEGDEEALKAMIQDGK--NLAEPNKEGwlPLHEAAYYGKLGCLKVLQRAYPGTIDQRTLQEETALYLATCREHL 185
Cdd:PHA02875   38 PIKLAMKFRDSEAIKLLMKHGAipDVKYPDIES--ELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKL 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 186 DCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVRILVQYNADANHRCNRGWTALHESVSRNDLEVMEILVSGGAKVE 265
Cdd:PHA02875  116 DIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANID 195

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1958782630 266 --AKNVySITPLFVAAQSGQLEALRFLAKHGADIN 298
Cdd:PHA02875  196 yfGKNG-CVAALCYAIENNKIDIVRLFIKRGADCN 229
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 185-396 2.42e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 78.49  E-value: 2.42e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 185 LDCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVRILVQYNADANHRCNRGWTALHESVSRNDLEVMEILVSGGAKv 264
Cdd:PHA02875   15 LDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKF- 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 265 eAKNVY---SITPLFVAAQSGQLEALRFLAKHGADINTQASDSASALYEACKNEHEDVVEFLLSQGADANKANKDGLLPL 341
Cdd:PHA02875   94 -ADDVFykdGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPL 172

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958782630 342 HVASKKGNYRIVQMLLPVTSRTRV--RRSGISPLHLAAERNHDAVLEALLAARFDVN 396
Cdd:PHA02875  173 IIAMAKGDIAICKMLLDSGANIDYfgKNGCVAALCYAIENNKIDIVRLFIKRGADCN 229
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 188-336 5.72e-15

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 78.37  E-value: 5.72e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 188 LLSLLQAGAEPDISNKSRETPLYKACERKNAEAVRILVQYNADANHRCNRGWTALHESVSRNDLEVMEILVSGGAkveAK 267
Cdd:PLN03192  541 LEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFAS---IS 617

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 268 NVYSITPLF-VAAQSGQLEALRFLAKHGADINTQASDSASALYEACKNEHEDVVEFLLSQGADANKANKD 336
Cdd:PLN03192  618 DPHAAGDLLcTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTD 687
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 242-501 9.72e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 77.41  E-value: 9.72e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 242 LHESVSRNDLEVMEILVSGGAKVEAKNVYSITPLFVAAQSGQLEALRFLAKHGADINTQASDSASA-------------- 307
Cdd:PHA02876  149 IKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVlecavdsknidtik 228

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 308 ------------------------------LYEA---------CKNE--HEDV--------VEFLLSQGADANKANKDGL 338
Cdd:PHA02876  229 aiidnrsninkndlsllkairnedletsllLYDAgfsvnsiddCKNTplHHASqapslsrlVPKLLERGADVNAKNIKGE 308

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 339 LPLHVASKKG----NYRIVQMLLPVTSRTrvRRSGISPLHLAA--ERNHDAVLeALLAARFDVNtplaperARLYEDRrt 412
Cdd:PHA02876  309 TPLYLMAKNGydteNIRTLIMLGADVNAA--DRLYITPLHQAStlDRNKDIVI-TLLELGANVN-------ARDYCDK-- 376

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 413 SALYFAVVNNNVYATELLLLAGADPnrDVISPLLVAIRHGCL------RTMQLLLDHGANIDA---YIAThptafPATIM 483
Cdd:PHA02876  377 TPIHYAAVRNNVVIINTLLDYGADI--EALSQKIGTALHFALcgtnpyMSVKTLIDRGANVNSknkDLST-----PLHYA 449

                         330
                  ....*....|....*....
gi 1958782630 484 FAMKC-LSLLKFLMDLGCD 501
Cdd:PHA02876  450 CKKNCkLDVIEMLLDNGAD 468
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 278-475 2.55e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 71.95  E-value: 2.55e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 278 AAQSGQLEALRFLAKHGADINTQASDSASALYEACKNEHEDVVEFLLSQGADANKANKDGLLPLHVASKKGNYRIVQMLL 357
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 358 PVTSRTR--VRRSGISPLHLAAERNHDAVLEALLAARFDVNTPlaperarlyEDRRTSALYFAVVNNNVYATELLLLAGA 435
Cdd:PHA02875   89 DLGKFADdvFYKDGMTPLHLATILKKLDIMKLLIARGADPDIP---------NTDKFSPLHLAVMMGDIKGIELLIDHKA 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1958782630 436 DPNRD---VISPLLVAIRHGCLRTMQLLLDHGANIDaYIATHP 475
Cdd:PHA02875  160 CLDIEdccGCTPLIIAMAKGDIAICKMLLDSGANID-YFGKNG 201
PHA03095 PHA03095
ankyrin-like protein; Provisional
 110-358 5.59e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 71.21  E-value: 5.59e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 110 LKAIKEGDEEALKAMIQDGKNLAEPNKEGWLPLHEAAYYG-KLGCLKVLQRA-----YPGTIDQRTLQeetaLYLATCRE 183
Cdd:PHA03095   55 LHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNAtTLDVIKLLIKAgadvnAKDKVGRTPLH----VYLSGFNI 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 184 HLDCLLSLLQAGAEPDISNKSRETPLYKACERKNA--EAVRILVQYNADANHRCNRGWTALH---ESVsRNDLEVMEILV 258
Cdd:PHA03095  131 NPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNAnvELLRLLIDAGADVYAVDDRFRSLLHhhlQSF-KPRARIVRELI 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 259 SGGAKVEAKNVYSITPLFVAAQSGQLEA--LRFLAKHGADINTQASDSASALYEACKNEHEDVVEFLLSQGADANKANKD 336
Cdd:PHA03095  210 RAGCDPAATDMLGNTPLHSMATGSSCKRslVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSD 289

                         250       260
                  ....*....|....*....|..
gi 1958782630 337 GLLPLHVASKKGNYRIVQMLLP 358
Cdd:PHA03095  290 GNTPLSLMVRNNNGRAVRAALA 311
Ank_2 pfam12796
Ankyrin repeats (3 copies);
112-202 6.89e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 58.97  E-value: 6.89e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 112 AIKEGDEEALKAMIQDGKNLAEPNKEGWLPLHEAAYYGKLGCLKVLQRAYPGtidQRTLQEETALYLATCREHLDCLLSL 191
Cdd:pfam12796   4 AAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV---NLKDNGRTALHYAARSGHLEIVKLL 80

                          90
                  ....*....|.
gi 1958782630 192 LQAGAEPDISN 202
Cdd:pfam12796  81 LEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 271-467 1.03e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 64.21  E-value: 1.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 271 SITPLFVAAQSGQLEALRFLAKHGADINTQASDSASALYEACKNEHEDVVEFLLSQGADANkankdgLLPLHVASKKGNY 350
Cdd:PHA02874   35 TTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTS------ILPIPCIEKDMIK 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 351 RIVQMLLPVTSRTRVRRSGispLHLAAERNHDAVLEALLAARFDVNtplaperarLYEDRRTSALYFAVVNNNVYATELL 430
Cdd:PHA02874  109 TILDCGIDVNIKDAELKTF---LHYAIKKGDLESIKMLFEYGADVN---------IEDDNGCYPIHIAIKHNFFDIIKLL 176

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1958782630 431 LLAGADPN---RDVISPLLVAIRHGCLRTMQLLLDHGANI 467
Cdd:PHA02874  177 LEKGAYANvkdNNGESPLHNAAEYGDYACIKLLIDHGNHI 216
Ank_4 pfam13637
Ankyrin repeats (many copies);
273-324 3.76e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.74  E-value: 3.76e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958782630 273 TPLFVAAQSGQLEALRFLAKHGADINTQASDSASALYEACKNEHEDVVEFLL 324
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
306-357 4.57e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.36  E-value: 4.57e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958782630 306 SALYEACKNEHEDVVEFLLSQGADANKANKDGLLPLHVASKKGNYRIVQMLL 357
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
373-469 5.50e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 56.28  E-value: 5.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 373 LHLAAERNHDAVLEALLAARFDVNtplaperarLYEDRRTSALYFAVVNNNVYATELLLlAGADPNRDVI--SPLLVAIR 450
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADAN---------LQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKDNgrTALHYAAR 70

                          90
                  ....*....|....*....
gi 1958782630 451 HGCLRTMQLLLDHGANIDA 469
Cdd:pfam12796  71 SGHLEIVKLLLEKGADINV 89
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 140-357 1.32e-09

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: 60.80  E-value: 1.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 140 LPLHEAAYYGKLGCLKVLQRAYPGTIDQRTLQEETALYLATCREHLDCLLSLLQAGaePDISNKSRETPLYKacerknae 219
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAA--PELVNEPMTSDLYQ-------- 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 220 avrilvqynadanhrcnrGWTALHESVSRNDLEVMEILVSGGAKV------------EAKNV--YSITPLFVAAQSGQLE 285
Cdd:cd22192    89 ------------------GETALHIAVVNQNLNLVRELIARGADVvspratgtffrpGPKNLiyYGEHPLSFAACVGNEE 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 286 ALRFLAKHGADINTQASDSASALY----EACKNEHEDVVEFLLSQGADANKA------NKDGLLPLHVASKKGNYRIVQM 355
Cdd:cd22192   151 IVRLLIEHGADIRAQDSLGNTVLHilvlQPNKTFACQMYDLILSYDKEDDLQpldlvpNNQGLTPFKLAAKEGNIVMFQH 230


                  ..
gi 1958782630 356 LL 357
Cdd:cd22192   231 LV 232
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 300-469 5.63e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 58.74  E-value: 5.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 300 QASDSASA-----LYEACKNEHEDVVEFLLSQGADANKANKDGLLPLHVASKKGNYRIVQMLLPVTSRTRV--------- 365
Cdd:PHA02878   28 NYSTSASLipfipLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVfytlvaikd 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 366 ----------------RRSGISPLHLAA--ERNHDAVLEA-----LLAARFDVNtplaperaRLYEDRRTSALYFAVVNN 422
Cdd:PHA02878  108 afnnrnveifkiiltnRYKNIQTIDLVYidKKSKDDIIEAeitklLLSYGADIN--------MKDRHKGNTALHYATENK 179

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958782630 423 NVYATELLLLAGADPN---RDVISPLLVAIRHGCLRTMQLLLDHGANIDA 469
Cdd:PHA02878  180 DQRLTELLLSYGANVNipdKTNNSPLHHAVKHYNKPIVHILLENGASTDA 229
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 202-348 1.71e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 55.21  E-value: 1.71e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 202 NKSRETPLYKACERKNA--EAVRILVQYNADANHRC-NRGWTALHESVSRN---DLEVMEILVSGGAKVEAKNVYSITPL 275
Cdd:PHA02859   48 NDLYETPIFSCLEKDKVnvEILKFLIENGADVNFKTrDNNLSALHHYLSFNknvEPEILKILIDSGSSITEEDEDGKNLL 127

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958782630 276 --FVAAQSGQLEALRFLAKHGADINTQASDSASALYEACKNEHED-VVEFLLSQGADANKANKDGLLPLHVASKKG 348
Cdd:PHA02859  128 hmYMCNFNVRINVIKLLIDSGVSFLNKDFDNNNILYSYILFHSDKkIFDFLTSLGIDINETNKSGYNCYDLIKFRN 203
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 175-299 1.98e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 56.98  E-value: 1.98e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 175 ALYLATCREHLDCLLSLLQAGAEPDISNKSRETPL--YKACERKNAEAVRILVQYNADANHRC----------------N 236
Cdd:PHA03100  111 LYAISKKSNSYSIVEYLLDNGANVNIKNSDGENLLhlYLESNKIDLKILKLLIDKGVDINAKNrvnyllsygvpinikdV 190

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958782630 237 RGWTALHESVSRNDLEVMEILVSGGAKVEAKNVYSITPLFVAAQSGQLEALRFLAKHGADINT 299
Cdd:PHA03100  191 YGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 108-292 4.53e-08

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: 56.17  E-value: 4.53e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 108 PVLKAIKEGDEEALKAMI-QDGKNLAEPNKEGWLPLHEAAYYGKLGCLKVLQRAYPGTIDQRTLQE----ETALYLATCR 182
Cdd:cd22192    20 PLLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEPMTSDlyqgETALHIAVVN 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 183 EHLDCLLSLLQAGAepDISN---------KSR-------ETPL-YKACErKNAEAVRILVQYNADANHRCNRGWTALHES 245
Cdd:cd22192   100 QNLNLVRELIARGA--DVVSpratgtffrPGPknliyygEHPLsFAACV-GNEEIVRLLIEHGADIRAQDSLGNTVLHIL 176

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958782630 246 VSRND----LEVMEILVSGGAKVEAKNVYSI------TPLFVAAQSGQLEALRFLAK 292
Cdd:cd22192   177 VLQPNktfaCQMYDLILSYDKEDDLQPLDLVpnnqglTPFKLAAKEGNIVMFQHLVQ 233
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 279-357 5.55e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 55.67  E-value: 5.55e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958782630 279 AQSGQLEALRFLAKHGADINTQASDSASALYEACKNEHEDVVEFLLSQGADANKANKDGLLPLHVASKKGNYRIVQMLL 357
Cdd:PTZ00322   90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
Ank_4 pfam13637
Ankyrin repeats (many copies);
205-258 1.96e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.04  E-value: 1.96e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958782630 205 RETPLYKACERKNAEAVRILVQYNADANHRCNRGWTALHESVSRNDLEVMEILV 258
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02798 PHA02798
ankyrin-like protein; Provisional
 221-450 3.57e-07

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 52.91  E-value: 3.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 221 VRILVQYNADANHRCNRGWTALHESVSR---NDLEVMEILVSGGAKVEAKNVYSITPLFVAAQSG---QLEALRFLAKHG 294
Cdd:PHA02798   92 VKILIENGADINKKNSDGETPLYCLLSNgyiNNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNhhiDIEIIKLLLEKG 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 295 ADINTQAS----DSASALYEACKNEHE-DVVEFLLSQGADANKANK-------DGLLPLHVASKKGNYRIVQMLLPVTSR 362
Cdd:PHA02798  172 VDINTHNNkekyDTLHCYFKYNIDRIDaDILKLFVDNGFIINKENKshkkkfmEYLNSLLYDNKRFKKNILDFIFSYIDI 251

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 363 TRVRRSGISPLHLAAERNHDAVLEALLAARFDVN--TPLAperarlyedrrTSALYFAVVNNNVYATELLLlaGADPNRD 440
Cdd:PHA02798  252 NQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINiiTELG-----------NTCLFTAFENESKFIFNSIL--NKKPNKN 318

                         250
                  ....*....|
gi 1958782630 441 VISPLLVAIR 450
Cdd:PHA02798  319 TISYTYYKLR 328
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 237-357 4.93e-07

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: 52.78  E-value: 4.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 237 RGWTALHESVSRNDLEVMEILVSGGAKVEAKNV--------------YSITPLFVAAQSGQLEALRFLAKHGADINTQAS 302
Cdd:TIGR00870 127 PGITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAAACLGSPSIVALLSEDPADILTADS 206

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958782630 303 DS-----ASALYEACKNEHEDVV----EFLLSQGADANKA-------NKDGLLPLHVASKKGNYRIVQMLL 357
Cdd:TIGR00870 207 LGntllhLLVMENEFKAEYEELScqmyNFALSLLDKLRDSkelevilNHQGLTPLKLAAKEGRIVLFRLKL 277
Ank_4 pfam13637
Ankyrin repeats (many copies);
106-157 8.88e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.11  E-value: 8.88e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958782630 106 MDPVLKAIKEGDEEALKAMIQDGKNLAEPNKEGWLPLHEAAYYGKLGCLKVL 157
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 151-357 1.18e-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: 51.42  E-value: 1.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 151 LGCLKVLQRAYPGTIDQRTLQEETALYLATCREH---LDCLLSLLQAGaepdisnksretplykacerKNAEAVRILVqy 227
Cdd:cd21882     5 LGLLECLRWYLTDSAYQRGATGKTCLHKAALNLNdgvNEAIMLLLEAA--------------------PDSGNPKELV-- 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 228 NADANHRCNRGWTALHESVSRNDLEVMEILVSGGAKVEAKNV-------------YSITPLFVAAQSGQLEALRFLAKHG 294
Cdd:cd21882    63 NAPCTDEFYQGQTALHIAIENRNLNLVRLLVENGADVSARATgrffrkspgnlfyFGELPLSLAACTNQEEIVRLLLENG 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 295 ADI-NTQASDSAS-----ALYEACKNEHED------VVEFLLSQGADANK-------ANKDGLLPLHVASKKGNYRIVQM 355
Cdd:cd21882   143 AQPaALEAQDSLGntvlhALVLQADNTPENsafvcqMYNLLLSYGAHLDPtqqleeiPNHQGLTPLKLAAVEGKIVMFQH 222


                  ..
gi 1958782630 356 LL 357
Cdd:cd21882   223 IL 224
Ank_5 pfam13857
Ankyrin repeats (many copies);
191-243 1.73e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.42  E-value: 1.73e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958782630 191 LLQAG-AEPDISNKSRETPLYKACERKNAEAVRILVQYNADANHRCNRGWTALH 243
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 242-436 2.50e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 50.64  E-value: 2.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 242 LHESVSRNDLEVMEILVSGGAkvEAKNVYSITPLFVAAQSGQLEALRFLAKHGADINTQASDSASALYEACKNEHEDVVE 321
Cdd:PLN03192  498 LQHHKELHDLNVGDLLGDNGG--EHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVL 575

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 322 FLLSQGADANKANKDGLLPLHVASKKGNYRIVQMLLPVTSRTRVRRSGiSPLHLAAERNHDAVLEALLAARFDVNTplap 401
Cdd:PLN03192  576 VLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAG-DLLCTAAKRNDLTAMKELLKQGLNVDS---- 650

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1958782630 402 erarlyEDRR-TSALYFAVVNNNVYATELLLLAGAD 436
Cdd:PLN03192  651 ------EDHQgATALQVAMAEDHVDMVRLLIMNGAD 680
PHA02946 PHA02946
ankyin-like protein; Provisional
 175-375 3.54e-06

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 49.67  E-value: 3.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 175 ALYLATCREHLDCLLSLLQAgAEPdiSNKSRETPLYKACERKNAEAVRILVQYNADANHRCNRGWTALHESVSRNDLEVM 254
Cdd:PHA02946   12 SLYAKYNSKNLDVFRNMLQA-IEP--SGNYHILHAYCGIKGLDERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIV 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 255 EILVSGGAKVEAKNVYSITPLFVAAQSGQ--LEALRFLAKHGADINTQASDSASALYEACKNEHEDVVEFLLSQGADA-- 330
Cdd:PHA02946   89 AMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYGAKINNSVDEEGCGPLLACTDPSERVFKKIMSIGFEAri 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 331 ---------------------------------NKANKDGLLPLHVASKK--GNYRIVQMLLPVTSRTRVRRSGISPLHL 375
Cdd:PHA02946  169 vdkfgknhihrhlmsdnpkastiswmmklgispSKPDHDGNTPLHIVCSKtvKNVDIINLLLPSTDVNKQNKFGDSPLTL 248
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 339-486 6.93e-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: 6.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 339 LPLHVASKKGNYRIVQMLLpVTSRTRVRRSGI---SPLHLAAERNHDAVLEALL-AARFDVNTPLAPErarLYEDRrtSA 414
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLL-KCPSCDLFQRGAlgeTALHVAALYDNLEAAVVLMeAAPELVNEPMTSD---LYQGE--TA 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 415 LYFAVVNNNVYATELLLLAGAD------------PNRDVI-----SPLLVAIRHGCLRTMQLLLDHGANIDA-------- 469
Cdd:cd22192    93 LHIAVVNQNLNLVRELIARGADvvspratgtffrPGPKNLiyygeHPLSFAACVGNEEIVRLLIEHGADIRAqdslgntv 172

                         170
                  ....*....|....*....
gi 1958782630 470 --YIATHPTAFPATIMFAM 486
Cdd:cd22192   173 lhILVLQPNKTFACQMYDL 191
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 219-357 1.04e-05

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: 48.60  E-value: 1.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 219 EAVRILVQY-----------NADANHRCNRGWTALHESVSRNDLEVMEILVSGGAKVEAKN--------------VYSIT 273
Cdd:cd22194   111 EIVRILLAFaeengildrfiNAEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAkgvffnpkykhegfYFGET 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 274 PLFVAAQSGQLEALRFLAKHGADINTqASDSAS-----ALYEACKN--EHEDVV----EFLLSQGADAN---KANKDGLL 339
Cdd:cd22194   191 PLALAACTNQPEIVQLLMEKESTDIT-SQDSRGntvlhALVTVAEDskTQNDFVkrmyDMILLKSENKNletIRNNEGLT 269

                         170
                  ....*....|....*...
gi 1958782630 340 PLHVASKKGNYRIVQMLL 357
Cdd:cd22194   270 PLQLAAKMGKAEILKYIL 287
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 406-503 1.30e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 47.29  E-value: 1.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 406 LYEDRRTSALYFAVVNNNVYATELLLLAGADPNR----DVISPLLVAIRHGCLRTMQLLLDHGANIDAYIATHPTAFPAT 481
Cdd:PHA02884   65 LSENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRyaeeAKITPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPIELA 144

                          90       100
                  ....*....|....*....|..
gi 1958782630 482 IMFamkCLSLLKFLMdlgCDGE 503
Cdd:PHA02884  145 LMI---CNNFLAFMI---CDNE 160
Ank_4 pfam13637
Ankyrin repeats (many copies);
238-290 7.90e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 40.72  E-value: 7.90e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958782630 238 GWTALHESVSRNDLEVMEILVSGGAKVEAKNVYSITPLFVAAQSGQLEALRFL 290
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 108-225 8.55e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 45.26  E-value: 8.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 108 PVLKAIKEGDEEALKAMIQDGKNLAEPNKEGWLPLHEAAYYGK-LGCLKVLQRAYPGTIDQRTLQEETALYLATCREhlD 186
Cdd:PHA02878  204 PLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKdYDILKLLLEHGVDVNAKSYILGLTALHSSIKSE--R 281

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1958782630 187 CLLSLLQAGAEPDISNKSRETPLYKAC-ERKNAEAVRILV 225
Cdd:PHA02878  282 KLKLLLEYGADINSLNSYKLTPLSSAVkQYLCINIGRILI 321
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 268-352 1.64e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 43.27  E-value: 1.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 268 NVYSITPLF--VAAQSGQLEALRFLAKHGADINTQASDSA-SALYEAC---KNEHEDVVEFLLSQGADANKANKDGLLPL 341
Cdd:PHA02859   48 NDLYETPIFscLEKDKVNVEILKFLIENGADVNFKTRDNNlSALHHYLsfnKNVEPEILKILIDSGSSITEEDEDGKNLL 127

                          90
                  ....*....|.
gi 1958782630 342 HVASKKGNYRI 352
Cdd:PHA02859  128 HMYMCNFNVRI 138
Ank_4 pfam13637
Ankyrin repeats (many copies);
174-225 1.77e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.57  E-value: 1.77e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958782630 174 TALYLATCREHLDCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVRILV 225
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 237-357 3.29e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong 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: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 43.63  E-value: 3.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 237 RGWTALHESVSRNDLEVMEILVSGGAKVEAKN--------------VYSITPLFVAAQSGQLEALRFLAKHG-ADINTQA 301
Cdd:cd22193    75 EGQTALHIAIERRQGDIVALLVENGADVHAHAkgrffqpkyqgegfYFGELPLSLAACTNQPDIVQYLLENEhQPADIEA 154

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958782630 302 SDSAS-----ALYEACKNEHED------VVEFLLSQGADANKA-------NKDGLLPLHVASKKGNYRIVQMLL 357
Cdd:cd22193   155 QDSRGntvlhALVTVADNTKENtkfvtrMYDMILIRGAKLCPTveleeirNNDGLTPLQLAAKMGKIEILKYIL 228
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 237-357 3.65e-04

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: 43.64  E-value: 3.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 237 RGWTALHESVSRNDLEVMEILVSGGAKVEAKN--------------VYSITPLFVAAQSGQLEALRFLAKH---GADINt 299
Cdd:cd22196    93 KGQTALHIAIERRNMHLVELLVQNGADVHARAsgeffkkkkggpgfYFGELPLSLAACTNQLDIVKFLLENphsPADIS- 171

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958782630 300 qASDSAS-----ALYEACKNEHEDvVEF-------LLSQGADANK-------ANKDGLLPLHVASKKGNYRIVQMLL 357
Cdd:cd22196   172 -ARDSMGntvlhALVEVADNTPEN-TKFvtkmyneILILGAKIRPllkleeiTNKKGLTPLKLAAKTGKIGIFAYIL 246
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 176-278 8.77e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 41.51  E-value: 8.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 176 LYLATCREHLDCLLSLLQAGAEPDI----SNKSRETPLYKACERKNAEAVRILVQYNADANHRCNRG-WTALHESVSRND 250
Cdd:PHA02884   37 LYSSIKFHYTDIIDAILKLGADPEApfplSENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAkITPLYISVLHGC 116

                          90       100
                  ....*....|....*....|....*...
gi 1958782630 251 LEVMEILVSGGAKVEAKNVYSITPLFVA 278
Cdd:PHA02884  117 LKCLEILLSYGADINIQTNDMVTPIELA 144
Ank_5 pfam13857
Ankyrin repeats (many copies);
290-344 9.42e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.71  E-value: 9.42e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958782630 290 LAKHG-ADINTQASDSASALYEACKNEHEDVVEFLLSQGADANKANKDGLLPLHVA 344
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02798 PHA02798
ankyrin-like protein; Provisional
 250-397 1.09e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 41.74  E-value: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 250 DLEVMEILVSGGAKVEAKNVYSITPLFVAAQSGQLEALRFLAKHGADINTQASDSASALYEACKNEHE-----DVVEFLL 324
Cdd:PHA02798   17 KLSTVKLLIKSCNPNEIVNEYSIFQKYLQRDSPSTDIVKLFINLGANVNGLDNEYSTPLCTILSNIKDykhmlDIVKILI 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 325 SQGADANKANKDGLLPLHVASKKG---NYRIVQ-MLLPVTSRTRVRRSGISPLHLAAERNHDA---VLEALLAARFDVNT 397
Cdd:PHA02798   97 ENGADINKKNSDGETPLYCLLSNGyinNLEILLfMIENGADTTLLDKDGFTMLQVYLQSNHHIdieIIKLLLEKGVDINT 176
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 256-325 1.48e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.42  E-value: 1.48e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 256 ILVSGGAKVEAKNVYSITPLFVAAQSGQLEALRFLAKHGADINTQASDSASALYEACKNEHEDVVEFLLS 325
Cdd:PTZ00322  100 ILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 273-298 1.64e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.03  E-value: 1.64e-03
                           10        20
                   ....*....|....*....|....*.
gi 1958782630  273 TPLFVAAQSGQLEALRFLAKHGADIN 298
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADIN 29
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 273-299 2.18e-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: 35.70  E-value: 2.18e-03
                          10        20
                  ....*....|....*....|....*..
gi 1958782630 273 TPLFVAAQSGQLEALRFLAKHGADINT 299
Cdd:pfam13606   4 TPLHLAARNGRLEIVKLLLENGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
323-376 3.01e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.17  E-value: 3.01e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958782630 323 LLSQG-ADANKANKDGLLPLHVASKKGNYRIVQMLL-PVTSRTRVRRSGISPLHLA 376
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLaYGVDLNLKDEEGLTALDLA 56
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
108-209 3.58e-03

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 39.94  E-value: 3.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 108 PVLKAIKEGDEEALKAMIQDGKNLAEPNKEGWLPLHEAAYYGKLGCLKVLQRAYpGTIDQRTLQEETALYLATCREHLDC 187
Cdd:COG0666   189 PLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAG-ADLNAKDKDGLTALLLAAAAGAALI 267

                          90       100
                  ....*....|....*....|..
gi 1958782630 188 LLSLLQAGAEPDISNKSRETPL 209
Cdd:COG0666   268 VKLLLLALLLLAAALLDLLTLL 289
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 171-290 3.99e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong 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: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 40.16  E-value: 3.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 171 QEETALYLATCREHLDCLLSLLQAGAEPDISNKSR--------------ETPLYKACERKNAEAVRILVQ---YNADANH 233
Cdd:cd22193    75 EGQTALHIAIERRQGDIVALLVENGADVHAHAKGRffqpkyqgegfyfgELPLSLAACTNQPDIVQYLLEnehQPADIEA 154

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958782630 234 RCNRGWTALH-------ESVSRNDL--EVMEILVSGGAKV-------EAKNVYSITPLFVAAQSGQLEALRFL 290
Cdd:cd22193   155 QDSRGNTVLHalvtvadNTKENTKFvtRMYDMILIRGAKLcptveleEIRNNDGLTPLQLAAKMGKIEILKYI 227
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 243-324 4.42e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 39.72  E-value: 4.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 243 HESVSRNDLEVMEILVSGgAKVEAKNVYSITPLFVAAQSGQLEALRFLAKHGADINTQASDSASALYEACKNEHEDVVEF 322
Cdd:PHA02989  229 NKILSKKEFKVLNFILKY-IKINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHGNIDMLNR 307


                  ..
gi 1958782630 323 LL 324
Cdd:PHA02989  308 IL 309
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 228-357 4.66e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely related to TRPV1, sharing high sequence identity (>50%), but TRPV2 shows a higher temperature threshold and sensitivity for activation than TRPV1. TRPV2 can be stimulated by ligands or lipids, and is involved in osmosensation and mechanosensation. TRPV2 is expressed in both neuronal and non-neuronal tissues, and it has been implicated in diverse physiological and pathophysiological processes, including cardiac-structure maintenance, innate immunity, and cancer. TRPV2 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 39.84  E-value: 4.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 228 NADANHRCNRGWTALHESVSRNDLEVMEILVSGGAKVEAKN-------------VYSITPLFVAAQSGQLEALRFLAKHG 294
Cdd:cd22197    84 NAQCTDEYYRGHSALHIAIEKRSLQCVKLLVENGADVHARAcgrffqkkqgtcfYFGELPLSLAACTKQWDVVNYLLENP 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782630 295 ADI-NTQASDSAS-----ALYEACKNEHED---VVEF---LLSQGADANKA-------NKDGLLPLHVASKKGNYRIVQM 355
Cdd:cd22197   164 HQPaSLQAQDSLGntvlhALVMIADNSPENsalVIKMydgLLQAGARLCPTvqleeisNHEGLTPLKLAAKEGKIEIFRH 243


                  ..
gi 1958782630 356 LL 357
Cdd:cd22197   244 IL 245
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 369-396 4.93e-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: 34.87  E-value: 4.93e-03
                           10        20
                   ....*....|....*....|....*...
gi 1958782630  369 GISPLHLAAERNHDAVLEALLAARFDVN 396
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADIN 29
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 237-266 8.06e-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: 8.06e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1958782630  237 RGWTALHESVSRNDLEVMEILVSGGAKVEA 266
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 165-236 8.89e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 38.88  E-value: 8.89e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958782630 165 IDQRTLQEETALYLATCREHLDCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVRILVQYNADANHRCN 236
Cdd:PHA03100  185 INIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256
 
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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