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Conserved domains on  [gi|1907093835|ref|XP_036013957|]
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ankyrin repeat and death domain-containing protein 1B isoform X4 [Mus musculus]

Protein Classification

ankyrin repeat domain-containing protein( domain architecture ID 12356329)

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];
142-415 1.95e-37

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 138.55  E-value: 1.95e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 142 IMLMLVKAGADQRAKNQEGMNALHLAAQNNNLHIVDYLIHDLHLHDLNQPNERGRKPFHLAAERGHVEMIEKLIFLNLHT 221
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 222 SEKDKDGNTALHLAAMHGHSPAVQVLLTQWSEVNESNENGETPFLLAVVGGHEECSRVLLAGGSDVNIPNKLNVSALQTA 301
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 302 TRNGHTALVNFLLGENADLQQQKESKEPPLHLAVINNRPAVVNSLLSARHDVDVLDQRRQTPLHVAADLGNVELVETLLK 381
Cdd:COG0666   161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1907093835 382 AGCNLKITDKQGKTALAVAARSQHSLVVDMLIKA 415
Cdd:COG0666   241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLA 274
Ank_2 pfam12796
Ankyrin repeats (3 copies);
68-157 6.19e-15

Ankyrin repeats (3 copies);


:

Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.14  E-value: 6.19e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835  68 AAKSSNLDLMEKLFEKKVNINAVNNMNRTALHFAVGRNSLSAVDFLLSHkARVDVADkHGLTVIHLAAWSGSFEIMLMLV 147
Cdd:pfam12796   4 AAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKLLL 81

                          90
                  ....*....|
gi 1907093835 148 KAGADQRAKN 157
Cdd:pfam12796  82 EKGADINVKD 91
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
142-415 1.95e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 138.55  E-value: 1.95e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 142 IMLMLVKAGADQRAKNQEGMNALHLAAQNNNLHIVDYLIHDLHLHDLNQPNERGRKPFHLAAERGHVEMIEKLIFLNLHT 221
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 222 SEKDKDGNTALHLAAMHGHSPAVQVLLTQWSEVNESNENGETPFLLAVVGGHEECSRVLLAGGSDVNIPNKLNVSALQTA 301
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 302 TRNGHTALVNFLLGENADLQQQKESKEPPLHLAVINNRPAVVNSLLSARHDVDVLDQRRQTPLHVAADLGNVELVETLLK 381
Cdd:COG0666   161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1907093835 382 AGCNLKITDKQGKTALAVAARSQHSLVVDMLIKA 415
Cdd:COG0666   241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLA 274
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 63-413 1.80e-20

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 94.36  E-value: 1.80e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835  63 RSFQNAAKSSNLDLMEKLFEKKVNINAVNNMNRTALHFAVGRNSLSAVDFLLSHKARVDVADKHGLTVIHLAAWSGSFEI 142
Cdd:PHA02876  147 KLIKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDT 226

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 143 mlmlVKAGADQRAKNQEGMNALHLAAQNNNLHiVDYLIHDLHLhDLNQPNERGRKPFHLAAERGHVemiekliflnlhts 222
Cdd:PHA02876  227 ----IKAIIDNRSNINKNDLSLLKAIRNEDLE-TSLLLYDAGF-SVNSIDDCKNTPLHHASQAPSL-------------- 286

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 223 ekdkdgntalhlaamhghSPAVQVLLTQWSEVNESNENGETP-FLLAVVGGHEECSRVLLAGGSDVNIPNKLNVSALQTA 301
Cdd:PHA02876  287 ------------------SRLVPKLLERGADVNAKNIKGETPlYLMAKNGYDTENIRTLIMLGADVNAADRLYITPLHQA 348

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 302 T---RNGHTALVNFLLGENADLQQQKEskEPPLHLAVINNRPAVVNSLLSARHDVDVLDQRRQTPLHVAADLGNVEL-VE 377
Cdd:PHA02876  349 StldRNKDIVITLLELGANVNARDYCD--KTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMsVK 426

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1907093835 378 TLLKAGCNLKITDKQGKTALAVAARSQHSL-VVDMLI 413
Cdd:PHA02876  427 TLIDRGANVNSKNKDLSTPLHYACKKNCKLdVIEMLL 463
Ank_2 pfam12796
Ankyrin repeats (3 copies);
199-291 1.08e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.15  E-value: 1.08e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 199 FHLAAERGHVEMIEKLIFLNLHTSEKDKDGNTALHLAAMHGHSPAVQVLLTQWSevNESNENGETPFLLAVVGGHEECSR 278
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1907093835 279 VLLAGGSDVNIPN 291
Cdd:pfam12796  79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
68-157 6.19e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.14  E-value: 6.19e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835  68 AAKSSNLDLMEKLFEKKVNINAVNNMNRTALHFAVGRNSLSAVDFLLSHkARVDVADkHGLTVIHLAAWSGSFEIMLMLV 147
Cdd:pfam12796   4 AAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKLLL 81

                          90
                  ....*....|
gi 1907093835 148 KAGADQRAKN 157
Cdd:pfam12796  82 EKGADINVKD 91
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 183-381 1.81e-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: 60.03  E-value: 1.81e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 183 LHLHDLNQPNErgrKPFHLAAERGHVEMIEKLIfLNLHTS--EKDKDGNTALHLAAMHGHSPAVQVLLTQWSE-VNESNE 259
Cdd:cd22192     8 LHLLQQKRISE---SPLLLAAKENDVQAIKKLL-KCPSCDlfQRGALGETALHVAALYDNLEAAVVLMEAAPElVNEPMT 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 260 N----GETPFLLAVVGGHEECSRVLLAGGSDVNIP---------NKLNV-----SALQTATRNGHTALVNFLLGENADLQ 321
Cdd:cd22192    84 SdlyqGETALHIAVVNQNLNLVRELIARGADVVSPratgtffrpGPKNLiyygeHPLSFAACVGNEEIVRLLIEHGADIR 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 322 QQKESKEPPLHLAVI--NNRPA--VVNSLLSA-----RHDVD-VLDQRRQTPLHVAADLGNVELVETLLK 381
Cdd:cd22192   164 AQDSLGNTVLHILVLqpNKTFAcqMYDLILSYdkeddLQPLDlVPNNQGLTPFKLAAKEGNIVMFQHLVQ 233
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 58-282 9.54e-09

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: 57.78  E-value: 9.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835  58 LLAIERSFQNAAKSSNLDLMEKLFE--KKVNINAVNNMNRTALHFAVGRNSLSAV-DFLLSHKARVDVADkhglTVIHLA 134
Cdd:TIGR00870  14 LSDEEKAFLPAAERGDLASVYRDLEepKKLNINCPDRLGRSALFVAAIENENLELtELLLNLSCRGAVGD----TLLHAI 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 135 A---WSGSFEIMLMLVKAGADQRAKN----------QEGMNALHLAAQNNNLHIVDYLIH------------DLHLHDLN 189
Cdd:TIGR00870  90 SleyVDAVEAILLHLLAAFRKSGPLElandqytsefTPGITALHLAAHRQNYEIVKLLLErgasvparacgdFFVKSQGV 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 190 QPNERGRKPFHLAAERGHVEMIEKLIFLNLHTSEKDKDGNTALHLAAM-------------HGHSPAVQVL-----LTQW 251
Cdd:TIGR00870 170 DSFYHGESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVMenefkaeyeelscQMYNFALSLLdklrdSKEL 249

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1907093835 252 SEVneSNENGETPFLLAVVGGHEECSRVLLA 282
Cdd:TIGR00870 250 EVI--LNHQGLTPLKLAAKEGRIVLFRLKLA 278
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 65-180 6.67e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 42.04  E-value: 6.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835  65 FQNAAKSSNLDLMEKLFEKKVNINAVNNMNRTAL------HFAVGRNSLSAVDFLLSHkARVDVADKHGLTVIHLAAWSG 138
Cdd:PHA02989  189 LRNDIDVISIKVIKYLIKKGVNIETNNNGSESVLesfldnNKILSKKEFKVLNFILKY-IKINKKDKKGFNPLLISAKVD 267

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1907093835 139 SFEIMLMLVKAGADQRAKNQEGMNALHLAAQNNNLHIVDYLI 180
Cdd:PHA02989  268 NYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHGNIDMLNRIL 309
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 18-184 3.70e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 39.79  E-value: 3.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835  18 AARGLKANLRDVATRPWRSLARMPKPEVQDPETaaagheGLLAIERSFQNAAKSSN------LDLMEKLFEKKVNINAVN 91
Cdd:cd22196    14 VAKGDCKELDGLLEYLMRTKKRLTDSEFKDPET------GKTCLLKAMLNLHNGQNdtisllLDIAEKTGNLKEFVNAAY 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835  92 NMN----RTALHFAVGRNSLSAVDFLLSHKARVDvadkhgltvihlAAWSGSFEimlmlvkagadQRAKNQEGMN----A 163
Cdd:cd22196    88 TDSyykgQTALHIAIERRNMHLVELLVQNGADVH------------ARASGEFF-----------KKKKGGPGFYfgelP 144

                         170       180
                  ....*....|....*....|.
gi 1907093835 164 LHLAAQNNNLHIVDYLIHDLH 184
Cdd:cd22196   145 LSLAACTNQLDIVKFLLENPH 165
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
142-415 1.95e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 138.55  E-value: 1.95e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 142 IMLMLVKAGADQRAKNQEGMNALHLAAQNNNLHIVDYLIHDLHLHDLNQPNERGRKPFHLAAERGHVEMIEKLIFLNLHT 221
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 222 SEKDKDGNTALHLAAMHGHSPAVQVLLTQWSEVNESNENGETPFLLAVVGGHEECSRVLLAGGSDVNIPNKLNVSALQTA 301
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 302 TRNGHTALVNFLLGENADLQQQKESKEPPLHLAVINNRPAVVNSLLSARHDVDVLDQRRQTPLHVAADLGNVELVETLLK 381
Cdd:COG0666   161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1907093835 382 AGCNLKITDKQGKTALAVAARSQHSLVVDMLIKA 415
Cdd:COG0666   241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLA 274
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
74-364 5.80e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 134.31  E-value: 5.80e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835  74 LDLMEKLFEKKVNINAVNNMNRTALHFAVGRNSLSAVDFLLSHKARVDVADKHGLTVIHLAAWSGSFEIMLMLVKAGADQ 153
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 154 RAKNQEGMNALHLAAQNNNLHIVDYLIHdlHLHDLNQPNERGRKPFHLAAERGHVEMIEKLIFLNLHTSEKDKDGNTALH 233
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLE--AGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLH 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 234 LAAMHGHSPAVQVLLTQWSEVNESNENGETPFLLAVVGGHEECSRVLLAGGSDVNIPNKLNVSALQTATRNGHTALVNFL 313
Cdd:COG0666   159 LAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLL 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907093835 314 LGENADLQQQKESKEPPLHLAVINNRPAVVNSLLSARHDVDVLDQRRQTPL 364
Cdd:COG0666   239 LEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
58-331 5.92e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 134.31  E-value: 5.92e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835  58 LLAIERSFQNAAKSSNLDLMEKLFEKKVNINAVNNMNRTALHFAVGRNSLSAVDFLLSHKARVDVADKHGLTVIHLAAWS 137
Cdd:COG0666    18 LLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARN 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 138 GSFEIMLMLVKAGADQRAKNQEGMNALHLAAQNNNLHIVDYLIHdlHLHDLNQPNERGRKPFHLAAERGHVEMIEKLIFL 217
Cdd:COG0666    98 GDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLE--AGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEA 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 218 NLHTSEKDKDGNTALHLAAMHGHSPAVQVLLTQWSEVNESNENGETPFLLAVVGGHEECSRVLLAGGSDVNIPNKLNVSA 297
Cdd:COG0666   176 GADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTA 255

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1907093835 298 LQTATRNGHTALVNFLLGENADLQQQKESKEPPL 331
Cdd:COG0666   256 LLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
107-397 3.11e-34

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 129.69  E-value: 3.11e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 107 LSAVDFLLSHKARVDVADKHGLTVIHLAAWSGSFEIMLMLVKAGADQRAKNQEGMNALHLAAQNNNLHIVDYLIHdlHLH 186
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLA--AGA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 187 DLNQPNERGRKPFHLAAERGHVEMIEKLIFLNLHTSEKDKDGNTALHLAAMHGHSPAVQVLLTQWSEVNESNENGETPFL 266
Cdd:COG0666    79 DINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLH 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 267 LAVVGGHEECSRVLLAGGSDVNIPNKLNVSALQTATRNGHTALVNFLLGENADLQQQKESKEPPLHLAVINNRPAVVNSL 346
Cdd:COG0666   159 LAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLL 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907093835 347 LSARHDVDVLDQRRQTPLHVAADLGNVELVETLLKAGCNLKITDKQGKTAL 397
Cdd:COG0666   239 LEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 63-413 1.80e-20

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 94.36  E-value: 1.80e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835  63 RSFQNAAKSSNLDLMEKLFEKKVNINAVNNMNRTALHFAVGRNSLSAVDFLLSHKARVDVADKHGLTVIHLAAWSGSFEI 142
Cdd:PHA02876  147 KLIKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDT 226

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 143 mlmlVKAGADQRAKNQEGMNALHLAAQNNNLHiVDYLIHDLHLhDLNQPNERGRKPFHLAAERGHVemiekliflnlhts 222
Cdd:PHA02876  227 ----IKAIIDNRSNINKNDLSLLKAIRNEDLE-TSLLLYDAGF-SVNSIDDCKNTPLHHASQAPSL-------------- 286

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 223 ekdkdgntalhlaamhghSPAVQVLLTQWSEVNESNENGETP-FLLAVVGGHEECSRVLLAGGSDVNIPNKLNVSALQTA 301
Cdd:PHA02876  287 ------------------SRLVPKLLERGADVNAKNIKGETPlYLMAKNGYDTENIRTLIMLGADVNAADRLYITPLHQA 348

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 302 T---RNGHTALVNFLLGENADLQQQKEskEPPLHLAVINNRPAVVNSLLSARHDVDVLDQRRQTPLHVAADLGNVEL-VE 377
Cdd:PHA02876  349 StldRNKDIVITLLELGANVNARDYCD--KTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMsVK 426

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1907093835 378 TLLKAGCNLKITDKQGKTALAVAARSQHSL-VVDMLI 413
Cdd:PHA02876  427 TLIDRGANVNSKNKDLSTPLHYACKKNCKLdVIEMLL 463
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 68-289 1.83e-20

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 93.19  E-value: 1.83e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835  68 AAKSSNLDLMEKLFEKKVNINAVNNMNRTALHF-----AVGRNSLSAVDFLLSHKARVDVADKHGLTVIHLAAW--SGSF 140
Cdd:PHA03100   42 AKEARNIDVVKILLDNGADINSSTKNNSTPLHYlsnikYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISkkSNSY 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 141 EIMLMLVKAGADQRAKNQEGMNALHLAAQNN--NLHIVDYLIhdLHLHDLNQPNErgrkpfhlaaerghvemIEKLIFLN 218
Cdd:PHA03100  122 SIVEYLLDNGANVNIKNSDGENLLHLYLESNkiDLKILKLLI--DKGVDINAKNR-----------------VNYLLSYG 182

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907093835 219 LHTSEKDKDGNTALHLAAMHGHSPAVQVLLTQWSEVNESNENGETPFLLAVVGGHEECSRVLLAGGSDVNI 289
Cdd:PHA03100  183 VPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
PHA03095 PHA03095
ankyrin-like protein; Provisional
 69-357 5.39e-18

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 86.23  E-value: 5.39e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835  69 AKSSNLDL--MEKLFEKKVNINAVNNMNRTALHFAVGRNS---LSAVDFLLSHKARVDVADKHGLTVIHLAAWSGS-FEI 142
Cdd:PHA03095   20 LNASNVTVeeVRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDV 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 143 MLMLVKAGADQRAKNQEGMNALH--LAAQNNNLHIVDYLIHdlHLHDLNQPNERGRKPFH--LAAERGHVEMIEKLIFLN 218
Cdd:PHA03095  100 IKLLIKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLR--KGADVNALDLYGMTPLAvlLKSRNANVELLRLLIDAG 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 219 LHTSEKDKDGNTALHLAAMHGHSPA--VQVLLTQWSEVNESNENGETPFLLAVVGGHEECSRV--LLAGGSDVNIPNKLN 294
Cdd:PHA03095  178 ADVYAVDDRFRSLLHHHLQSFKPRAriVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYG 257

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907093835 295 VSALQTATRNGHTALVNFLLGENADLQQQKESKEPPLHLAVINNRPAVVNSLLSARHDVDVLD 357
Cdd:PHA03095  258 QTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVA 320
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 170-414 5.74e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 82.79  E-value: 5.74e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 170 NNNLHIVDYLIHDLHLhdlnqpnergrkPFHLAAERGHVEMIEKLIFLNLHTSEKDKDGNTALHLAAMHGHS-----PAV 244
Cdd:PHA03100   22 IMEDDLNDYSYKKPVL------------PLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIV 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 245 QVLLTQWSEVNESNENGETPFLLAVVGGHEECSRV--LLAGGSDVNIPNKLNVSALQTATRNGHTAL--VNFLLGENADL 320
Cdd:PHA03100   90 KLLLEYGANVNAPDNNGITPLLYAISKKSNSYSIVeyLLDNGANVNIKNSDGENLLHLYLESNKIDLkiLKLLIDKGVDI 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 321 QqqkeskepplhlaVINNrpavVNSLLSARHDVDVLDQRRQTPLHVAADLGNVELVETLLKAGCNLKITDKQGKTALAVA 400
Cdd:PHA03100  170 N-------------AKNR----VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIA 232

                         250
                  ....*....|....
gi 1907093835 401 ARSQHSLVVDMLIK 414
Cdd:PHA03100  233 ILNNNKEIFKLLLN 246
Ank_2 pfam12796
Ankyrin repeats (3 copies);
199-291 1.08e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.15  E-value: 1.08e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 199 FHLAAERGHVEMIEKLIFLNLHTSEKDKDGNTALHLAAMHGHSPAVQVLLTQWSevNESNENGETPFLLAVVGGHEECSR 278
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1907093835 279 VLLAGGSDVNIPN 291
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 73-268 1.22e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 81.55  E-value: 1.22e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835  73 NLDLMEKLFEKKVNINAVNNMNRTALHFAVGRNSLSAVDFLLSHKARVDVADKHGLTVIHLAAWSGSFEIMLMLVKAGAD 152
Cdd:PHA02874  103 EKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAY 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 153 QRAKNQEGMNALHLAAQNNNLHIVDYLIHdlHLHDLNQPNERGRKPFHLAA--ERGHVEmiekLIFLNLHTSEKDKDGNT 230
Cdd:PHA02874  183 ANVKDNNGESPLHNAAEYGDYACIKLLID--HGNHIMNKCKNGFTPLHNAIihNRSAIE----LLINNASINDQDIDGST 256

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1907093835 231 ALHLAAMHGHS-PAVQVLLTQWSEVNESNENGETPFLLA 268
Cdd:PHA02874  257 PLHHAINPPCDiDIIDILLYHKADISIKDNKGENPIDTA 295
Ank_2 pfam12796
Ankyrin repeats (3 copies);
131-225 1.74e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 71.69  E-value: 1.74e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 131 IHLAAWSGSFEIMLMLVKAGADQRAKNQEGMNALHLAAQNNNLHIVDYLIhdlhLHDLNQPNERGRKPFHLAAERGHVEM 210
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL----EHADVNLKDNGRTALHYAARSGHLEI 76

                          90
                  ....*....|....*
gi 1907093835 211 IEKLIFLNLHTSEKD 225
Cdd:pfam12796  77 VKLLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 71-415 4.96e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 76.93  E-value: 4.96e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835  71 SSNLDLMEKLFEKKVN-INAVNNMNRTALHFAVGRNSLSAVDFLLSHKARVDVADKHGLTVIHLAAWSGSFEIMLMLVKA 149
Cdd:PHA02874   11 SGDIEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDN 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 150 GADQraknqegmNALHLAAQNNNL--HIVDYLIhdlhlhDLNQPNERGRKPFHLAAERGHVEMIEKLIFLNLHTSEKDKD 227
Cdd:PHA02874   91 GVDT--------SILPIPCIEKDMikTILDCGI------DVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDN 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 228 GNTALHLAAMHGHSPAVQVLLTQWSEVNESNENGETPFLLAVVGGHEECSRVLLAGGSdvNIPNKLNvsalqtatrNGHT 307
Cdd:PHA02874  157 GCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGN--HIMNKCK---------NGFT 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 308 alvnfllgenadlqqqkeskepPLHLAVINNRPAVvnSLLSARHDVDVLDQRRQTPLHVAADLG-NVELVETLLKAGCNL 386
Cdd:PHA02874  226 ----------------------PLHNAIIHNRSAI--ELLINNASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADI 281

                         330       340       350
                  ....*....|....*....|....*....|.
gi 1907093835 387 KITDKQGKTALAVAAR--SQHSLVVDMLIKA 415
Cdd:PHA02874  282 SIKDNKGENPIDTAFKyiNKDPVIKDIIANA 312
Ank_2 pfam12796
Ankyrin repeats (3 copies);
68-157 6.19e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.14  E-value: 6.19e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835  68 AAKSSNLDLMEKLFEKKVNINAVNNMNRTALHFAVGRNSLSAVDFLLSHkARVDVADkHGLTVIHLAAWSGSFEIMLMLV 147
Cdd:pfam12796   4 AAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKLLL 81

                          90
                  ....*....|
gi 1907093835 148 KAGADQRAKN 157
Cdd:pfam12796  82 EKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
331-414 1.38e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 68.99  E-value: 1.38e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 331 LHLAVINNRPAVVNSLLSARHDVDVLDQRRQTPLHVAADLGNVELVETLLKaGCNLKITDkQGKTALAVAARSQHSLVVD 410
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78


                  ....
gi 1907093835 411 MLIK 414
Cdd:pfam12796  79 LLLE 82
Ank_2 pfam12796
Ankyrin repeats (3 copies);
298-390 7.55e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.06  E-value: 7.55e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 298 LQTATRNGHTALVNFLLGENADLQQQKESKEPPLHLAVINNRPAVVnSLLSARHDVDVLDQRRqTPLHVAADLGNVELVE 377
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIV-KLLLEHADVNLKDNGR-TALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1907093835 378 TLLKAGCNLKITD 390
Cdd:pfam12796  79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
98-181 1.08e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 66.68  E-value: 1.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835  98 LHFAVGRNSLSAVDFLLSHKARVDVADKHGLTVIHLAAWSGSFEIMLMLVKaGADQRAKNqEGMNALHLAAQNNNLHIVD 177
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78


                  ....
gi 1907093835 178 YLIH 181
Cdd:pfam12796  79 LLLE 82
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 64-248 1.26e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 69.31  E-value: 1.26e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835  64 SFQNAAKSSNLDLMEKLFEKKVNINAVNNMNRTALHFAVGR--NSLSAVDFLLSHKARVDVADKHGLTVIHLAAWSGS-- 139
Cdd:PHA03100   76 SNIKYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKid 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 140 FEIMLMLVKAGADQRAKNQegmnalhlaaqnnnlhiVDYLIHdlHLHDLNQPNERGRKPFHLAAERGHVEMIEKLIFLNL 219
Cdd:PHA03100  156 LKILKLLIDKGVDINAKNR-----------------VNYLLS--YGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGA 216

                         170       180
                  ....*....|....*....|....*....
gi 1907093835 220 HTSEKDKDGNTALHLAAMHGHSPAVQVLL 248
Cdd:PHA03100  217 NPNLVNKYGDTPLHIAILNNNKEIFKLLL 245
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 65-335 4.83e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 67.60  E-value: 4.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835  65 FQNAAKSSNLDLMEKLFEKKVNINAVNNMNRTALHFAVGRNSLSAVDFLLSHKARVDVAdkHGLTVIHLAAWSGSFEIML 144
Cdd:PHA02878   41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVF--YTLVAIKDAFNNRNVEIFK 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 145 MLVKagadQRAKNQEGMNALHLAAQNNNLHIVDYLIHDLHLH--DLNQPNE-RGRKPFHLAAERGHVEMIEKLIFLNLHT 221
Cdd:PHA02878  119 IILT----NRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYgaDINMKDRhKGNTALHYATENKDQRLTELLLSYGANV 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 222 SEKDKDGNTALHLAAMHGHSPAVQVLLTQWSEVNESNENGETPFLLAVVGGHE-ECSRVLLAGGSDVNIPNK-LNVSALQ 299
Cdd:PHA02878  195 NIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDyDILKLLLEHGVDVNAKSYiLGLTALH 274

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1907093835 300 TATRNGHTalVNFLLGENADLQQQKESKEPPLHLAV 335
Cdd:PHA02878  275 SSIKSERK--LKLLLEYGADINSLNSYKLTPLSSAV 308
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 93-319 5.33e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 67.32  E-value: 5.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835  93 MNRTALHFAVGRNSLSAVDFLLSHKARVDVADKHGLTVIHLAAWSGSFEIMLMLVKAGADQRAKNQEGMNALHLAAQNNN 172
Cdd:PHA02875    1 MDQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 173 LHIVDYLIhDLHLHDLNQPNERGRKPFHLAAERGHVEMIEKLIFLNLHTSEKDKDGNTALHLAAMHGHSPAVQVLLTQWS 252
Cdd:PHA02875   81 VKAVEELL-DLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKA 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907093835 253 EVNESNENGETPFLLAVVGGHEECSRVLLAGGSDVN-IPNKLNVSALQTATRNGHTALVNFLLGENAD 319
Cdd:PHA02875  160 CLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDyFGKNGCVAALCYAIENNKIDIVRLFIKRGAD 227
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 171-414 1.16e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 66.17  E-value: 1.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 171 NNLHIVDYLihdlhLHDLNQPN---ERGRKPFHLAAERGHVEMIEKLIFLNLHTSEKDKDGNTALHLAAMHGHSPAVQVL 247
Cdd:PHA02875   13 GELDIARRL-----LDIGINPNfeiYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEEL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 248 LTQWSEVNES-NENGETPFLLAVVGGHEECSRVLLAGGSDVNIPNKlnvsalqtatrnghtalvnfllgenadlqqqkeS 326
Cdd:PHA02875   88 LDLGKFADDVfYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNT---------------------------------D 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 327 KEPPLHLAVINNRPAVVNSLLSARHDVDVLDQRRQTPLHVAADLGNVELVETLLKAGCNLKITDKQGK-TALAVAARSQH 405
Cdd:PHA02875  135 KFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNK 214


                  ....*....
gi 1907093835 406 SLVVDMLIK 414
Cdd:PHA02875  215 IDIVRLFIK 223
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 154-413 1.42e-11

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 66.82  E-value: 1.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 154 RAKNQEGMNALHLAAQNNNLHIVDYLIHDLHLHDLNqpnergrkpfhlaaerghvemIEKLIFLNlhtSEKDKDGNTALH 233
Cdd:PLN03192  473 RLKTSTLIEAMQTRQEDNVVILKNFLQHHKELHDLN---------------------VGDLLGDN---GGEHDDPNMASN 528

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 234 L--AAMHGHSPAVQVLLTQWSEVNESNENGETPFLLAVVGGHEECSRVLLAGGSDVNIPNKLNVSALQTATRNGHTALVN 311
Cdd:PLN03192  529 LltVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFR 608

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 312 FLLgenadlqqqkeskepplHLAVINNrPAVVNSLLSarhdvdvldqrrqtplhVAADLGNVELVETLLKAGCNLKITDK 391
Cdd:PLN03192  609 ILY-----------------HFASISD-PHAAGDLLC-----------------TAAKRNDLTAMKELLKQGLNVDSEDH 653

                         250       260
                  ....*....|....*....|..
gi 1907093835 392 QGKTALAVAARSQHSLVVDMLI 413
Cdd:PLN03192  654 QGATALQVAMAEDHVDMVRLLI 675
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 55-258 1.78e-11

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 66.43  E-value: 1.78e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835  55 HEGLLAIERSFQNAAKSSNLDLMEKLFE---KKVNINAVNNMNRTAlhfAVGRNSLsaVDFLLSHKARVDVADKHGLTVI 131
Cdd:PLN03192  488 EDNVVILKNFLQHHKELHDLNVGDLLGDnggEHDDPNMASNLLTVA---STGNAAL--LEELLKAKLDPDIGDSKGRTPL 562

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 132 HLAAWSGSFEIMLMLVKAGADQRAKNQEGMNALHLAAQNNNLHIVDYLIHDLHLHDlnqPNERGrKPFHLAAERGHVEMI 211
Cdd:PLN03192  563 HIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISD---PHAAG-DLLCTAAKRNDLTAM 638

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1907093835 212 EKLIFLNLHTSEKDKDGNTALHLAAMHGHSPAVQVLLTQWSEVNESN 258
Cdd:PLN03192  639 KELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAN 685
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 152-413 2.52e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 65.86  E-value: 2.52e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 152 DQRAKNQEGMNALHLAAQNNNLHIVDYLIHDLHlhDLNQPNERGRKPFHLAAERGHVEMIEKLIFLNLHTSEKDKDGNTA 231
Cdd:PHA02876  137 DKINESIEYMKLIKERIQQDELLIAEMLLEGGA--DVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSV 214

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 232 LHLAAMHGHSPAVQVLLTQWSEVNESnengETPFLLAVVGGHEECSRVLLAGGSDVNIPNKLNVSALQTATRNGH-TALV 310
Cdd:PHA02876  215 LECAVDSKNIDTIKAIIDNRSNINKN----DLSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLV 290

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 311 NFLLGENADLQQQKESKEPPLHLAVINNRPAV-VNSLLSARHDVDVLDQRRQTPLHVAADLG-NVELVETLLKAGCNLKI 388
Cdd:PHA02876  291 PKLLERGADVNAKNIKGETPLYLMAKNGYDTEnIRTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGANVNA 370

                         250       260
                  ....*....|....*....|....*
gi 1907093835 389 TDKQGKTALAVAARSQHSLVVDMLI 413
Cdd:PHA02876  371 RDYCDKTPIHYAAVRNNVVIINTLL 395
Ank_2 pfam12796
Ankyrin repeats (3 copies);
265-357 4.28e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 58.97  E-value: 4.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 265 FLLAVVGGHEECSRVLLAGGSDVNIPNKLNVSALQTATRNGHTALVNFLLgENADLQQQkESKEPPLHLAVINNRPAVVN 344
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLK-DNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1907093835 345 SLLSARHDVDVLD 357
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 164-407 6.40e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 64.13  E-value: 6.40e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 164 LHLAAQNNNLHIVDYLIHdlHLHDLNQPNERGRKPFHLAAERGHVEMIEKLIflnlHTSEKDKDGNT--ALHLAAMHGHS 241
Cdd:PHA02878   41 LHQAVEARNLDVVKSLLT--RGHNVNQPDHRDLTPLHIICKEPNKLGMKEMI----RSINKCSVFYTlvAIKDAFNNRNV 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 242 PAVQVLLTQWSEVNESNENGETPFLLAVVGGHEECSRVLLAGGSDVNI--PNKLNvSALQTATRNGHTALVNFLLGENAD 319
Cdd:PHA02878  115 EIFKIILTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMkdRHKGN-TALHYATENKDQRLTELLLSYGAN 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 320 LQQQKESKEPPLHLAVINNRPAVVNSLLSARHDVDVLDQRRQTPLHVAAD-LGNVELVETLLKAGCNLKITDK-QGKTAL 397
Cdd:PHA02878  194 VNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGyCKDYDILKLLLEHGVDVNAKSYiLGLTAL 273

                         250
                  ....*....|
gi 1907093835 398 AVAARSQHSL 407
Cdd:PHA02878  274 HSSIKSERKL 283
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 67-289 1.66e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 62.70  E-value: 1.66e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835  67 NAAKSSNLDLMEKLFEKKVNINAVNNMNRTALHFAVGRNSLSAVDFLLSHKARVDVADKHGLTVIHLAAWSG---SFEIM 143
Cdd:PHA02875    8 DAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGdvkAVEEL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 144 LMLVKAGADQRAKnqEGMNALHLAAQNNNLHIVDYLIHdlHLHDLNQPNERGRKPFHLAAERGHVEMIEKLIFLNLHTSE 223
Cdd:PHA02875   88 LDLGKFADDVFYK--DGMTPLHLATILKKLDIMKLLIA--RGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDI 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907093835 224 KDKDGNTALHLAAMHGHSPAVQVLLTQWSEVNESNENGETPFL-LAVVGGHEECSRVLLAGGSDVNI 289
Cdd:PHA02875  164 EDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALcYAIENNKIDIVRLFIKRGADCNI 230
PHA03095 PHA03095
ankyrin-like protein; Provisional
 187-415 2.42e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 62.35  E-value: 2.42e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 187 DLNQPNERGRKPFHLAAERGHVE-------MIEKLIFLNLhtseKDKDGNTALHLAAMHGHS-PAVQVLLTQWSEVNESN 258
Cdd:PHA03095   39 DVNFRGEYGKTPLHLYLHYSSEKvkdivrlLLEAGADVNA----PERCGFTPLHLYLYNATTlDVIKLLIKAGADVNAKD 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 259 ENGETPF--LLAVVGGHEECSRVLLAGGSDVNIPNKLNVSALQTATRNGHT--ALVNFLLGENADLQQQKESKEPPLH-- 332
Cdd:PHA03095  115 KVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNAnvELLRLLIDAGADVYAVDDRFRSLLHhh 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 333 LAVINNRPAVVNSLLSARHDVDVLDQRRQTPLHVAADLGNVE--LVETLLKAGCNLKITDKQGKTALAVAARSQHSLVVD 410
Cdd:PHA03095  195 LQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACR 274


                  ....*
gi 1907093835 411 MLIKA 415
Cdd:PHA03095  275 RLIAL 279
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 183-381 1.81e-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: 60.03  E-value: 1.81e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 183 LHLHDLNQPNErgrKPFHLAAERGHVEMIEKLIfLNLHTS--EKDKDGNTALHLAAMHGHSPAVQVLLTQWSE-VNESNE 259
Cdd:cd22192     8 LHLLQQKRISE---SPLLLAAKENDVQAIKKLL-KCPSCDlfQRGALGETALHVAALYDNLEAAVVLMEAAPElVNEPMT 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 260 N----GETPFLLAVVGGHEECSRVLLAGGSDVNIP---------NKLNV-----SALQTATRNGHTALVNFLLGENADLQ 321
Cdd:cd22192    84 SdlyqGETALHIAVVNQNLNLVRELIARGADVVSPratgtffrpGPKNLiyygeHPLSFAACVGNEEIVRLLIEHGADIR 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 322 QQKESKEPPLHLAVI--NNRPA--VVNSLLSA-----RHDVD-VLDQRRQTPLHVAADLGNVELVETLLK 381
Cdd:cd22192   164 AQDSLGNTVLHILVLqpNKTFAcqMYDLILSYdkeddLQPLDlVPNNQGLTPFKLAAKEGNIVMFQHLVQ 233
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 96-215 2.77e-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: 59.26  E-value: 2.77e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835  96 TALHFAVGRNSLSAVDFLLSHKArvDVAD-----------KHGLT-----VIHLAAWSGSFEIMLMLVKAGADQRAKNQE 159
Cdd:cd22192    91 TALHIAVVNQNLNLVRELIARGA--DVVSpratgtffrpgPKNLIyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSL 168

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907093835 160 GMNALH-LAAQNNNL---HIVDYLIH---DLHLHDLNQ-PNERGRKPFHLAAERGHVEMIEKLI 215
Cdd:cd22192   169 GNTVLHiLVLQPNKTfacQMYDLILSydkEDDLQPLDLvPNNQGLTPFKLAAKEGNIVMFQHLV 232
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 58-282 9.54e-09

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: 57.78  E-value: 9.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835  58 LLAIERSFQNAAKSSNLDLMEKLFE--KKVNINAVNNMNRTALHFAVGRNSLSAV-DFLLSHKARVDVADkhglTVIHLA 134
Cdd:TIGR00870  14 LSDEEKAFLPAAERGDLASVYRDLEepKKLNINCPDRLGRSALFVAAIENENLELtELLLNLSCRGAVGD----TLLHAI 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 135 A---WSGSFEIMLMLVKAGADQRAKN----------QEGMNALHLAAQNNNLHIVDYLIH------------DLHLHDLN 189
Cdd:TIGR00870  90 SleyVDAVEAILLHLLAAFRKSGPLElandqytsefTPGITALHLAAHRQNYEIVKLLLErgasvparacgdFFVKSQGV 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 190 QPNERGRKPFHLAAERGHVEMIEKLIFLNLHTSEKDKDGNTALHLAAM-------------HGHSPAVQVL-----LTQW 251
Cdd:TIGR00870 170 DSFYHGESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVMenefkaeyeelscQMYNFALSLLdklrdSKEL 249

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1907093835 252 SEVneSNENGETPFLLAVVGGHEECSRVLLA 282
Cdd:TIGR00870 250 EVI--LNHQGLTPLKLAAKEGRIVLFRLKLA 278
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 198-400 1.38e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 56.81  E-value: 1.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 198 PFHLAAERGHVEMIEKLIFLNLHTSEKDKDGNTALHLAAMHGHSPAVQVLLTQWSEVNESNEngETPFLLAVVGGHEECS 277
Cdd:PHA02878   40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVFYT--LVAIKDAFNNRNVEIF 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 278 RVLLAGGSDVNipNKLNVSALQTATRNG--HTALVNFLLGENADLQQQKESK-EPPLHLAVINNRPAVVNSLLSARHDVD 354
Cdd:PHA02878  118 KIILTNRYKNI--QTIDLVYIDKKSKDDiiEAEITKLLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVN 195

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1907093835 355 VLDQRRQTPLHVAADLGNVELVETLLKAGCNLKITDKQGKTALAVA 400
Cdd:PHA02878  196 IPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHIS 241
Ank_4 pfam13637
Ankyrin repeats (many copies);
94-147 1.81e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.35  E-value: 1.81e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907093835  94 NRTALHFAVGRNSLSAVDFLLSHKARVDVADKHGLTVIHLAAWSGSFEIMLMLV 147
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
228-281 2.10e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.35  E-value: 2.10e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907093835 228 GNTALHLAAMHGHSPAVQVLLTQWSEVNESNENGETPFLLAVVGGHEECSRVLL 281
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 68-266 3.28e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 55.74  E-value: 3.28e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835  68 AAKSSNLDLMEKLFEKKVNINAVNNMNRTALHFAVGRNSLSAVDFLLSHKARVDVADKHGLTVIHLAAWSGSFEIMLMLV 147
Cdd:PHA02874  131 AIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLI 210

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 148 KAGADQRAKNQEGMNALHLAAQNNNlHIVDYLIHDlhlHDLNQPNERGRKPFHLAAERG-HVEMIEKLIFLNLHTSEKDK 226
Cdd:PHA02874  211 DHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLINN---ASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDN 286

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1907093835 227 DGNTALHLAAMH-GHSPAVQVLLTQWSEVNESNENGETPFL 266
Cdd:PHA02874  287 KGENPIDTAFKYiNKDPVIKDIIANAVLIKEADKLKDSDFL 327
Ank_4 pfam13637
Ankyrin repeats (many copies);
195-248 4.21e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.58  E-value: 4.21e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907093835 195 GRKPFHLAAERGHVEMIEKLIFLNLHTSEKDKDGNTALHLAAMHGHSPAVQVLL 248
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
68-114 5.76e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.20  E-value: 5.76e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1907093835  68 AAKSSNLDLMEKLFEKKVNINAVNNMNRTALHFAVGRNSLSAVDFLL 114
Cdd:pfam13637   8 AAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
127-180 7.81e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.81  E-value: 7.81e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907093835 127 GLTVIHLAAWSGSFEIMLMLVKAGADQRAKNQEGMNALHLAAQNNNLHIVDYLI 180
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 254-418 8.05e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 54.20  E-value: 8.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 254 VNESNENGETPFLLAVVGGHEECSRVLLAGGSDVNIPNKLNVSALQTATRNGHTALVNFLLGENADLQQqkeskeppLHL 333
Cdd:PHA02874   28 INISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSI--------LPI 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 334 AVINNRpaVVNSLLSARHDVDVLDQRRQTPLHVAADLGNVELVETLLKAGCNLKITDKQGKTALAVAARSQHSLVVDMLI 413
Cdd:PHA02874  100 PCIEKD--MIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLL 177


                  ....*
gi 1907093835 414 KAERY 418
Cdd:PHA02874  178 EKGAY 182
Ank_5 pfam13857
Ankyrin repeats (many copies);
346-400 8.12e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.88  E-value: 8.12e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907093835 346 LLSARH-DVDVLDQRRQTPLHVAADLGNVELVETLLKAGCNLKITDKQGKTALAVA 400
Cdd:pfam13857   1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
160-215 9.59e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.42  E-value: 9.59e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907093835 160 GMNALHLAAQNNNLHIVDYLIHdlHLHDLNQPNERGRKPFHLAAERGHVEMIEKLI 215
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLE--KGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 95-215 1.07e-07

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: 54.12  E-value: 1.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835  95 RTALHFAVGRNSLSAVDFLLSHKARVDVA------DKHGLTVIH-------LAAWSGSFEIMLMLVKAGADQRAKNQE-- 159
Cdd:cd21882    74 QTALHIAIENRNLNLVRLLVENGADVSARatgrffRKSPGNLFYfgelplsLAACTNQEEIVRLLLENGAQPAALEAQds 153

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907093835 160 -GMNALH-LAAQNNN--------LHIVD-YLIHDLHLHDLNQ----PNERGRKPFHLAAERGHVEMIEKLI 215
Cdd:cd21882   154 lGNTVLHaLVLQADNtpensafvCQMYNlLLSYGAHLDPTQQleeiPNHQGLTPLKLAAVEGKIVMFQHIL 224
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 346-414 3.76e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.59  E-value: 3.76e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907093835 346 LLSARHDVDVLDQRRQTPLHVAADLGNVELVETLLKAGCNLKITDKQGKTALAVAARSQHSLVVDMLIK 414
Cdd:PTZ00322  101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
Ank_5 pfam13857
Ankyrin repeats (many copies);
180-235 6.49e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.19  E-value: 6.49e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907093835 180 IHDLHLHDLNQPNERGRKPFHLAAERGHVEMIEKLIFLNLHTSEKDKDGNTALHLA 235
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 268-414 1.05e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 50.76  E-value: 1.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 268 AVVGGHEECSRVLLAGGSDVNIPNKLNVSALQTATRNGHTALVNFLLGENADLQQQKESKEPPLHLAVINNRPAVVNSLL 347
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907093835 348 -SARHDVDVLDQRRQTPLHVAADLGNVELVETLLKAGCNLKITDKQGKTALAVAARSQHSLVVDMLIK 414
Cdd:PHA02875   89 dLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLID 156
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 94-272 2.93e-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: 49.63  E-value: 2.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835  94 NRTALHFAVGRNSLSAVDFLLSHKaRVDVADK--HGLTVIHLAAWSGSFEIMLMLVKAgaDQRAKNQ-------EGMNAL 164
Cdd:cd22192    17 SESPLLLAAKENDVQAIKKLLKCP-SCDLFQRgaLGETALHVAALYDNLEAAVVLMEA--APELVNEpmtsdlyQGETAL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 165 HLAAQNNNLHIVDYLIHdlHLHDLNQPN------ERGRK--------PFHLAAERGHVEMIEKLIFLNLHTSEKDKDGNT 230
Cdd:cd22192    94 HIAVVNQNLNLVRELIA--RGADVVSPRatgtffRPGPKnliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNT 171

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907093835 231 ALHLAAMHGHS-PAVQV---LLTQWSEVNE------SNENGETPFLLAVVGG 272
Cdd:cd22192   172 VLHILVLQPNKtFACQMydlILSYDKEDDLqpldlvPNNQGLTPFKLAAKEG 223
PHA02798 PHA02798
ankyrin-like protein; Provisional
 72-314 5.16e-06

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 48.68  E-value: 5.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835  72 SNLDLMEKLFEKKVNINAVNNMNRTALHFAVGR---NSLSAVDFLLSHKARVDVADKHGLTVIHLAAWSG---SFEIMLM 145
Cdd:PHA02798   87 HMLDIVKILIENGADINKKNSDGETPLYCLLSNgyiNNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNhhiDIEIIKL 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 146 LVKAGAD-QRAKNQEGMNALHLAAQNN----NLHIVDYLIHDLHLhdLNQPNERGRKPFhlaaerghVEMIEKLIFLNlh 220
Cdd:PHA02798  167 LLEKGVDiNTHNNKEKYDTLHCYFKYNidriDADILKLFVDNGFI--INKENKSHKKKF--------MEYLNSLLYDN-- 234

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 221 tseKDKDGNtalhlaamhghspaVQVLLTQWSEVNESNENGETPFLLAVVGGHEECSRVLLAGGSDVNIPNKLNVSALQT 300
Cdd:PHA02798  235 ---KRFKKN--------------ILDFIFSYIDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFT 297

                         250
                  ....*....|....
gi 1907093835 301 ATRNGHTALVNFLL 314
Cdd:PHA02798  298 AFENESKFIFNSIL 311
Ank_4 pfam13637
Ankyrin repeats (many copies);
362-413 1.02e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.65  E-value: 1.02e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907093835 362 TPLHVAADLGNVELVETLLKAGCNLKITDKQGKTALAVAARSQHSLVVDMLI 413
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02741 PHA02741
hypothetical protein; Provisional
 156-270 3.58e-05

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 44.26  E-value: 3.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 156 KNQEGMNALHLAAQNNNLHIV----DYLIHDLHLHDLNQPNERGRKPFHLAAERGH----VEMIEKLIFLNLHTSEKDK- 226
Cdd:PHA02741   17 KNSEGENFFHEAARCGCFDIIarftPFIRGDCHAAALNATDDAGQMCIHIAAEKHEaqlaAEIIDHLIELGADINAQEMl 96

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1907093835 227 DGNTALHLAAMHGHSPAVQVLLTQWS-EVNESNENGETPFLLAVV 270
Cdd:PHA02741   97 EGDTALHLAAHRRDHDLAEWLCCQPGiDLHFCNADNKSPFELAID 141
PHA02946 PHA02946
ankyin-like protein; Provisional
 76-269 5.83e-05

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 45.43  E-value: 5.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835  76 LMEKLFEKKVNINAVNNMNRTALHFAVGRNSLSAVDFLLSHKARVDVADKHGLTVIHLAAWSGS--FEIMLMLVKAGAD- 152
Cdd:PHA02946   54 FVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYGAKi 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 153 QRAKNQEGMNALhLAAQNNNLHIVDYLIH---DLHLHDLNQPNERGRkpfHLAAERGHVEMIEKLIFLNLHTSEKDKDGN 229
Cdd:PHA02946  134 NNSVDEEGCGPL-LACTDPSERVFKKIMSigfEARIVDKFGKNHIHR---HLMSDNPKASTISWMMKLGISPSKPDHDGN 209

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1907093835 230 TALHLAAMHG-HSPAVQVLLTQWSEVNESNENGETPFLLAV 269
Cdd:PHA02946  210 TPLHIVCSKTvKNVDIINLLLPSTDVNKQNKFGDSPLTLLI 250
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 233-315 6.00e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 45.66  E-value: 6.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 233 HLAAmHGHSPAVQVLLTQWSEVNESNENGETPFLLAVVGGHEECSRVLLAGGSDVNIPNKLNVSALQTATRNGHTALVNF 312
Cdd:PTZ00322   88 QLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                  ...
gi 1907093835 313 LLG 315
Cdd:PTZ00322  167 LSR 169
Ank_5 pfam13857
Ankyrin repeats (many copies);
224-268 1.24e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.64  E-value: 1.24e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1907093835 224 KDKDGNTALHLAAMHGHSPAVQVLLTQWSEVNESNENGETPFLLA 268
Cdd:pfam13857  12 LDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 139-267 1.52e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 42.88  E-value: 1.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 139 SFEIMLMLVKAGADQRAKNQ-EGMNALH--LAAQNN-NLHIVDYLIHDLHlhDLNQPNERGRKPFHLAAERGHV--EMIE 212
Cdd:PHA02859   65 NVEILKFLIENGADVNFKTRdNNLSALHhyLSFNKNvEPEILKILIDSGS--SITEEDEDGKNLLHMYMCNFNVriNVIK 142

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907093835 213 KLIFLNLHTSEKDKDGNTALHLAAM-HGHSPAVQVLLTQWSEVNESNENGETPFLL 267
Cdd:PHA02859  143 LLIDSGVSFLNKDFDNNNILYSYILfHSDKKIFDFLTSLGIDINETNKSGYNCYDL 198
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 320-414 1.67e-04

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 43.85  E-value: 1.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 320 LQQQKESKEPPLHLAVINNRPAVVNSLLSArHDVDVLdQRR---QTPLHVAADLGNVELVETLLKAG---CNLKITDK-- 391
Cdd:cd22192    10 LLQQKRISESPLLLAAKENDVQAIKKLLKC-PSCDLF-QRGalgETALHVAALYDNLEAAVVLMEAApelVNEPMTSDly 87

                          90       100
                  ....*....|....*....|...
gi 1907093835 392 QGKTALAVAARSQHSLVVDMLIK 414
Cdd:cd22192    88 QGETALHIAVVNQNLNLVRELIA 110
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 286-381 1.96e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 43.73  E-value: 1.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 286 DVNIPNKLNVSALQTATrNGHTALVNFLLGENADLQQQKESKEPPLHLAVINNRPAVVNSLLSARHDVDVLDQRRQTPLH 365
Cdd:PTZ00322   75 DPVVAHMLTVELCQLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLE 153

                          90
                  ....*....|....*.
gi 1907093835 366 VAADLGNVELVETLLK 381
Cdd:PTZ00322  154 LAEENGFREVVQLLSR 169
Ank_5 pfam13857
Ankyrin repeats (many copies);
113-167 2.13e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.25  E-value: 2.13e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907093835 113 LLSHK-ARVDVADKHGLTVIHLAAWSGSFEIMLMLVKAGADQRAKNQEGMNALHLA 167
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
85-134 2.28e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.87  E-value: 2.28e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907093835  85 VNINAVNNMNRTALHFAVGRNSLSAVDFLLSHKARVDVADKHGLTVIHLA 134
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 221-281 2.61e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 43.35  E-value: 2.61e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907093835 221 TSEKDKDGNTALHLAAMHGHSPAVQVLLTQWSEVNESNENGETPFLLAVVGGHEECSRVLL 281
Cdd:PTZ00322  108 PNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 187-261 3.63e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 42.96  E-value: 3.63e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907093835 187 DLNQPNERGRKPFHLAAERGHVEMIEKLIFLNLHTSEKDKDGNTALHLAAMHGHSPAVQVLLTQWSEVNESNENG 261
Cdd:PTZ00322  107 DPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELGANA 181
Ank_4 pfam13637
Ankyrin repeats (many copies);
263-314 5.18e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.02  E-value: 5.18e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907093835 263 TPFLLAVVGGHEECSRVLLAGGSDVNIPNKLNVSALQTATRNGHTALVNFLL 314
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 65-180 6.67e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 42.04  E-value: 6.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835  65 FQNAAKSSNLDLMEKLFEKKVNINAVNNMNRTAL------HFAVGRNSLSAVDFLLSHkARVDVADKHGLTVIHLAAWSG 138
Cdd:PHA02989  189 LRNDIDVISIKVIKYLIKKGVNIETNNNGSESVLesfldnNKILSKKEFKVLNFILKY-IKINKKDKKGFNPLLISAKVD 267

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1907093835 139 SFEIMLMLVKAGADQRAKNQEGMNALHLAAQNNNLHIVDYLI 180
Cdd:PHA02989  268 NYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHGNIDMLNRIL 309
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 113-188 6.77e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 42.19  E-value: 6.77e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907093835 113 LLSHKARVDVADKHGLTVIHLAAWSGSFEIMLMLVKAGADQRAKNQEGMNALHLAAQNNNLHIVDYLI-HDLHLHDL 188
Cdd:PTZ00322  101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSrHSQCHFEL 177
PHA02791 PHA02791
ankyrin-like protein; Provisional
 160-314 7.84e-04

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 41.18  E-value: 7.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 160 GMNALHLAAQNNNLHIVDYLIHDLHLHDLNQpNERgrkPFHLAAERGHVEMIEKLIFLNLHTSEKDKDGNTALHLAAMHG 239
Cdd:PHA02791   30 GHSALYYAIADNNVRLVCTLLNAGALKNLLE-NEF---PLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDSG 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 240 HSPAVQVLLTQ-WSEVNESNENGETPFLLAVVGGHEECSRVLLAggsdvNIPNKLN----VSALQTATRNGHTALVNFLL 314
Cdd:PHA02791  106 NMQTVKLFVKKnWRLMFYGKTGWKTSFYHAVMLNDVSIVSYFLS-----EIPSTFDlailLSCIHITIKNGHVDMMILLL 180
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 156-236 8.52e-04

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 39.86  E-value: 8.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 156 KNQEGMNALHLAAQNNNlhIVDYL-----IHDLHLHDLNQPNERGRKPFHLAAERGHVEMIEKLIFL-----NLHTSEKd 225
Cdd:PHA02736   13 PDIEGENILHYLCRNGG--VTDLLafknaISDENRYLVLEYNRHGKQCVHIVSNPDKADPQEKLKLLmewgaDINGKER- 89

                          90
                  ....*....|.
gi 1907093835 226 KDGNTALHLAA 236
Cdd:PHA02736   90 VFGNTPLHIAV 100
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 361-391 8.75e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.88  E-value: 8.75e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1907093835 361 QTPLHVAAD-LGNVELVETLLKAGCNLKITDK 391
Cdd:pfam00023   3 NTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
Ank_4 pfam13637
Ankyrin repeats (many copies);
329-380 8.81e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 37.25  E-value: 8.81e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907093835 329 PPLHLAVINNRPAVVNSLLSARHDVDVLDQRRQTPLHVAADLGNVELVETLL 380
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 296-403 1.03e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 41.72  E-value: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 296 SALQTAT--RNGHtaLVNFLLGENADLQ--------QQKESK------EPPLHLAVINNRPAVVNSLLSARH---DVDVL 356
Cdd:cd22196    96 TALHIAIerRNMH--LVELLVQNGADVHarasgeffKKKKGGpgfyfgELPLSLAACTNQLDIVKFLLENPHspaDISAR 173

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907093835 357 DQRRQTPLHVAADLGNVELVET---------LLKAGCNLK-------ITDKQGKTALAVAARS 403
Cdd:cd22196   174 DSMGNTVLHALVEVADNTPENTkfvtkmyneILILGAKIRpllkleeITNKKGLTPLKLAAKT 236
Ank_5 pfam13857
Ankyrin repeats (many copies);
146-202 1.07e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.94  E-value: 1.07e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907093835 146 LVKAG-ADQRAKNQEGMNALHLAAQNNNLHIVDYLIhdLHLHDLNQPNERGRKPFHLA 202
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLL--AYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 278-348 1.10e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.42  E-value: 1.10e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907093835 278 RVLLAGGSDVNIPNKLNVSALQTATRNGHTALVNFLLGENADLQQQKESKEPPLHLAVINNRPAVVNSLLS 348
Cdd:PTZ00322   99 RILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 367-414 1.39e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 41.39  E-value: 1.39e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1907093835 367 AADLGNVELVETLLKAGCNLKITDKQGKTALAVAARSQHSLVVDMLIK 414
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLK 579
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 252-403 1.40e-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: 40.93  E-value: 1.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 252 SEVNESnENGETPFLLAVV---GGHEECSRVLLAGGSDVNIPNKLNVSALQTATRNGHTAL-----------VNFLLGEN 317
Cdd:cd22193    21 SEFTES-STGKTCLMKALLnlnPGTNDTIRILLDIAEKTDNLKRFINAEYTDEYYEGQTALhiaierrqgdiVALLVENG 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 318 ADLQQQKESK--------------EPPLHLAVINNRPAVVNSLLSARH---DVDVLDQRRQTPLH----VAADL-GNVEL 375
Cdd:cd22193   100 ADVHAHAKGRffqpkyqgegfyfgELPLSLAACTNQPDIVQYLLENEHqpaDIEAQDSRGNTVLHalvtVADNTkENTKF 179

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1907093835 376 V----ETLLKAGCNL-------KITDKQGKTALAVAARS 403
Cdd:cd22193   180 VtrmyDMILIRGAKLcptveleEIRNNDGLTPLQLAAKM 218
PHA02743 PHA02743
Viral ankyrin protein; Provisional
 124-215 2.64e-03

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 38.64  E-value: 2.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 124 DKHGLTVIHLAAW---SGSFEIMLMLVKAGADQRAKNQE-GMNALHLAAQNNNLHIVDYLIHDLHLhDLNQPNERGRKPF 199
Cdd:PHA02743   54 DHHGRQCTHMVAWydrANAVMKIELLVNMGADINARELGtGNTLLHIAASTKNYELAEWLCRQLGV-NLGAINYQHETAY 132

                          90
                  ....*....|....*.
gi 1907093835 200 HLAAERGHVEMIEKLI 215
Cdd:PHA02743  133 HIAYKMRDRRMMEILR 148
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 66-126 3.70e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 39.65  E-value: 3.70e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907093835  66 QNAAKSSNLDLMEKLFEKKVNINAVNNMNRTALHFAVGRNSLSAVDFLLSHKARVDVADKH 126
Cdd:PHA03100  197 HYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 18-184 3.70e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 39.79  E-value: 3.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835  18 AARGLKANLRDVATRPWRSLARMPKPEVQDPETaaagheGLLAIERSFQNAAKSSN------LDLMEKLFEKKVNINAVN 91
Cdd:cd22196    14 VAKGDCKELDGLLEYLMRTKKRLTDSEFKDPET------GKTCLLKAMLNLHNGQNdtisllLDIAEKTGNLKEFVNAAY 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835  92 NMN----RTALHFAVGRNSLSAVDFLLSHKARVDvadkhgltvihlAAWSGSFEimlmlvkagadQRAKNQEGMN----A 163
Cdd:cd22196    88 TDSyykgQTALHIAIERRNMHLVELLVQNGADVH------------ARASGEFF-----------KKKKGGPGFYfgelP 144

                         170       180
                  ....*....|....*....|.
gi 1907093835 164 LHLAAQNNNLHIVDYLIHDLH 184
Cdd:cd22196   145 LSLAACTNQLDIVKFLLENPH 165
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 227-256 3.94e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 34.93  E-value: 3.94e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1907093835 227 DGNTALHLAAMHGHSPAVQVLLTQWSEVNE 256
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 151-233 4.64e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 39.36  E-value: 4.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 151 ADQRAKNQEGMNALHLAAQNNNLHIVDYLIH---DLHLH---DLNQPNER------GRKPFHLAAERGHVEMIEkLIFLN 218
Cdd:cd22194   132 AEYTEEAYEGQTALNIAIERRQGDIVKLLIAkgaDVNAHakgVFFNPKYKhegfyfGETPLALAACTNQPEIVQ-LLMEK 210

                          90
                  ....*....|....*..
gi 1907093835 219 LHT--SEKDKDGNTALH 233
Cdd:cd22194   211 ESTdiTSQDSRGNTVLH 227
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 241-417 6.02e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 38.97  E-value: 6.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 241 SPAVQVLLTQWSEVNESNE------NGETPFLLAVVGGHEECSRVLLAGGSDVN-IPNKLNVSALQ----TATRNGHTAL 309
Cdd:cd22194    19 SPQSPQDDTPSNPNSPSAElakeeqRDKKKRLKKVSEAAVEELGELLKELKDLSrRRRKTDVPDFLmhklTASDTGKTCL 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 310 VNFLLGENadlqqqkeskepplhlaviNNRPAVVNSLLSARHDVDVLDQ-----------RRQTPLHVAADLGNVELVET 378
Cdd:cd22194    99 MKALLNIN-------------------ENTKEIVRILLAFAEENGILDRfinaeyteeayEGQTALNIAIERRQGDIVKL 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907093835 379 LLKAGCNLKITDKQ--------------GKTALAVAARSQHSLVVDMLIKAER 417
Cdd:cd22194   160 LIAKGADVNAHAKGvffnpkykhegfyfGETPLALAACTNQPEIVQLLMEKES 212
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 361-388 8.00e-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: 33.77  E-value: 8.00e-03
                          10        20
                  ....*....|....*....|....*...
gi 1907093835 361 QTPLHVAADLGNVELVETLLKAGCNLKI 388
Cdd:pfam13606   3 NTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02791 PHA02791
ankyrin-like protein; Provisional
 331-434 8.36e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 38.10  E-value: 8.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 331 LHLAVINNRPAVVNSLLSARHDVDVLDQrrQTPLHVAADLGNVELVETLLKAGCNLKITDKQGKTALAVAARSQHSLVVD 410
Cdd:PHA02791   34 LYYAIADNNVRLVCTLLNAGALKNLLEN--EFPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDSGNMQTVK 111

                          90       100
                  ....*....|....*....|....
gi 1907093835 411 MLIKAEryyaWREKRFGSSKAKLT 434
Cdd:PHA02791  112 LFVKKN----WRLMFYGKTGWKTS 131
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 337-414 9.40e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 38.11  E-value: 9.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907093835 337 NNRPAVVNSLLSARHDVDVLDQRRQTPLHVAADLGNVELVETLLKAGCNLKITDKQGKTALAVAARSQHSL-----VVDM 411
Cdd:PHA03100   12 IIKVKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLtdvkeIVKL 91


                  ...
gi 1907093835 412 LIK 414
Cdd:PHA03100   92 LLE 94
 
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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