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Conserved domains on  [gi|504697848|ref|WP_014884950|]
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MULTISPECIES: ankyrin repeat domain-containing protein [Enterobacter]

Protein Classification

ankyrin repeat domain-containing protein( domain architecture ID 11429852)

ankyrin repeat domain-containing protein; ANK proteins mediate specific protein-protein interactions without necessarily recognizing specific primary sequences which allows for one ankyrin repeat domain to recognize and bind to a variety of intracellular substrates and may be involved in a wide array of functions

Gene Ontology:  GO:0005515
PubMed:  17176038
SCOP:  4000366

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
8-201 4.42e-29

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 109.27  E-value: 4.42e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697848   8 TEFLLAAEEGNVDALKACLEKGVDINATNRQKRTAIIIASLKKHYACVEFLIAAGADIDKQDQTCFNPFLIscltndltl 87
Cdd:COG0666   89 TLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHL--------- 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697848  88 lrivlpanpdldrltrfggvgitpASEKGHVEIVRELLAKtDINVNHTNFVGWTPLLEAIVLNDggekqQEIVKLLLDNG 167
Cdd:COG0666  160 ------------------------AAANGNLEIVKLLLEA-GADVNARDNDGETPLHLAAENGH-----LEIVKLLLEAG 209

                        170       180       190
                 ....*....|....*....|....*....|....
gi 504697848 168 ANPHMTDKYGKTPLELAREKGYHAIADLLLAAGA 201
Cdd:COG0666  210 ADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
8-201 4.42e-29

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 109.27  E-value: 4.42e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697848   8 TEFLLAAEEGNVDALKACLEKGVDINATNRQKRTAIIIASLKKHYACVEFLIAAGADIDKQDQTCFNPFLIscltndltl 87
Cdd:COG0666   89 TLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHL--------- 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697848  88 lrivlpanpdldrltrfggvgitpASEKGHVEIVRELLAKtDINVNHTNFVGWTPLLEAIVLNDggekqQEIVKLLLDNG 167
Cdd:COG0666  160 ------------------------AAANGNLEIVKLLLEA-GADVNARDNDGETPLHLAAENGH-----LEIVKLLLEAG 209

                        170       180       190
                 ....*....|....*....|....*....|....
gi 504697848 168 ANPHMTDKYGKTPLELAREKGYHAIADLLLAAGA 201
Cdd:COG0666  210 ADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 18-201 1.49e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 73.93  E-value: 1.49e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697848  18 NVDALKACLEKGVDINATNRQKRTAIIIASLKK--HYACVEFLIAAGADIDKQDQTCFNP---FLISClTNDLTLLRIVL 92
Cdd:PHA03100  85 VKEIVKLLLEYGANVNAPDNNGITPLLYAISKKsnSYSIVEYLLDNGANVNIKNSDGENLlhlYLESN-KIDLKILKLLI 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697848  93 PANPDLDRLTRFggvgitpasekghveivrELLAKTDINVNHTNFVGWTPLLEAIVLNDggekqQEIVKLLLDNGANPHM 172
Cdd:PHA03100 164 DKGVDINAKNRV------------------NYLLSYGVPINIKDVYGFTPLHYAVYNNN-----PEFVKYLLDLGANPNL 220

                        170       180
                 ....*....|....*....|....*....
gi 504697848 173 TDKYGKTPLELAREKGYHAIADLLLAAGA 201
Cdd:PHA03100 221 VNKYGDTPLHIAILNNNKEIFKLLLNNGP 249
Ank_2 pfam12796
Ankyrin repeats (3 copies);
43-174 8.69e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 56.28  E-value: 8.69e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697848   43 IIIASLKKHYACVEFLIAAGADIDKQDQTCFNPFLISCltndltllrivlpanpdldrltrfggvgitpasEKGHVEIVR 122
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAA---------------------------------KNGHLEIVK 47

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 504697848  123 ELLAKTDINVNHTnfvGWTPLLEAIVLNdggekQQEIVKLLLDNGANPHMTD 174
Cdd:pfam12796  48 LLLEHADVNLKDN---GRTALHYAARSG-----HLEIVKLLLEKGADINVKD 91
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 11-198 1.33e-04

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 41.99  E-value: 1.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697848   11 LLAAEEGNVDALKACL-------EKGVDINATNRQK-------RTAIIIASLKKHYACVEFLIAAGADIdkQDQTCFNPF 76
Cdd:TIGR00870  86 LHAISLEYVDAVEAILlhllaafRKSGPLELANDQYtseftpgITALHLAAHRQNYEIVKLLLERGASV--PARACGDFF 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697848   77 LISCLTNDLtllrivlpanpdldrltRFGGVGITPASEKGHVEIVReLLAKTDINVNHTNFVGWTpLLEAIVL-----ND 151
Cdd:TIGR00870 164 VKSQGVDSF-----------------YHGESPLNAAACLGSPSIVA-LLSEDPADILTADSLGNT-LLHLLVMenefkAE 224

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 504697848  152 GGEKQQEIVKLLLDNGANP-------HMTDKYGKTPLELAREKGYHAIADLLLA 198
Cdd:TIGR00870 225 YEELSCQMYNFALSLLDKLrdskeleVILNHQGLTPLKLAAKEGRIVLFRLKLA 278
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 11-181 3.26e-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: 40.77  E-value: 3.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697848  11 LLAAEEGNVDALKACLE-KGVDINATNRQKRTAIIIASLKKHYACVEFLIAAGADIDKQDQTcfnpfliSCLTNDLTLLR 89
Cdd:cd22192   22 LLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEPMT-------SDLYQGETALH 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697848  90 IvlpanpdldrltrfggvgitpASEKGHVEIVRELLAK-TDIN---VNHTNFV---------GWTPL-LEAIVLNdggek 155
Cdd:cd22192   95 I---------------------AVVNQNLNLVRELIARgADVVsprATGTFFRpgpknliyyGEHPLsFAACVGN----- 148

                        170       180
                 ....*....|....*....|....*.
gi 504697848 156 qQEIVKLLLDNGANPHMTDKYGKTPL 181
Cdd:cd22192  149 -EEIVRLLIEHGADIRAQDSLGNTVL 173
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
8-201 4.42e-29

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 109.27  E-value: 4.42e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697848   8 TEFLLAAEEGNVDALKACLEKGVDINATNRQKRTAIIIASLKKHYACVEFLIAAGADIDKQDQTCFNPFLIscltndltl 87
Cdd:COG0666   89 TLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHL--------- 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697848  88 lrivlpanpdldrltrfggvgitpASEKGHVEIVRELLAKtDINVNHTNFVGWTPLLEAIVLNDggekqQEIVKLLLDNG 167
Cdd:COG0666  160 ------------------------AAANGNLEIVKLLLEA-GADVNARDNDGETPLHLAAENGH-----LEIVKLLLEAG 209

                        170       180       190
                 ....*....|....*....|....*....|....
gi 504697848 168 ANPHMTDKYGKTPLELAREKGYHAIADLLLAAGA 201
Cdd:COG0666  210 ADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
5-201 2.07e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 96.95  E-value: 2.07e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697848   5 ALVTEFLLAAEEGNVDALKACLEKGVDINATNRQKRTAIIIASLKKHYACVEFLIAAGADIDKQDQTCFNPFLISCLTND 84
Cdd:COG0666   20 LLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGD 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697848  85 LTLLRIVLPANPDLDRLTRFGGVGITPASEKGHVEIVRELLAKtDINVNHTNFVGWTPLLEAIVLNDggekqQEIVKLLL 164
Cdd:COG0666  100 LEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA-GADVNAQDNDGNTPLHLAAANGN-----LEIVKLLL 173

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 504697848 165 DNGANPHMTDKYGKTPLELAREKGYHAIADLLLAAGA 201
Cdd:COG0666  174 EAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGA 210
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
8-201 1.18e-19

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 84.24  E-value: 1.18e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697848   8 TEFLLAAEEGNVDALKACLEKGVDINATNRQKRTAIIIASLKKHYACVEFLIAAGADIDKQDQtcfnpfliscltNDLTL 87
Cdd:COG0666  122 TPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDN------------DGETP 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697848  88 LRIvlpanpdldrltrfggvgitpASEKGHVEIVRELLAKtDINVNHTNFVGWTPLLEAIVLNDggekqQEIVKLLLDNG 167
Cdd:COG0666  190 LHL---------------------AAENGHLEIVKLLLEA-GADVNAKDNDGKTALDLAAENGN-----LEIVKLLLEAG 242

                        170       180       190
                 ....*....|....*....|....*....|....
gi 504697848 168 ANPHMTDKYGKTPLELAREKGYHAIADLLLAAGA 201
Cdd:COG0666  243 ADLNAKDKDGLTALLLAAAAGAALIVKLLLLALL 276
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
26-201 4.51e-18

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 80.00  E-value: 4.51e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697848  26 LEKGVDINATNRQKRTAIIIASLKKHYACVEFLIAAGADIDKQDQTCFNPFLISCLTNDLTLLRIVLPANPDLDRLTRFG 105
Cdd:COG0666    8 LLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGG 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697848 106 GVGITPASEKGHVEIVRELLAKtDINVNHTNFVGWTPLLEAIVLNDggekqQEIVKLLLDNGANPHMTDKYGKTPLELAR 185
Cdd:COG0666   88 NTLLHAAARNGDLEIVKLLLEA-GADVNARDKDGETPLHLAAYNGN-----LEIVKLLLEAGADVNAQDNDGNTPLHLAA 161

                        170
                 ....*....|....*.
gi 504697848 186 EKGYHAIADLLLAAGA 201
Cdd:COG0666  162 ANGNLEIVKLLLEAGA 177
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 18-201 1.49e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 73.93  E-value: 1.49e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697848  18 NVDALKACLEKGVDINATNRQKRTAIIIASLKK--HYACVEFLIAAGADIDKQDQTCFNP---FLISClTNDLTLLRIVL 92
Cdd:PHA03100  85 VKEIVKLLLEYGANVNAPDNNGITPLLYAISKKsnSYSIVEYLLDNGANVNIKNSDGENLlhlYLESN-KIDLKILKLLI 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697848  93 PANPDLDRLTRFggvgitpasekghveivrELLAKTDINVNHTNFVGWTPLLEAIVLNDggekqQEIVKLLLDNGANPHM 172
Cdd:PHA03100 164 DKGVDINAKNRV------------------NYLLSYGVPINIKDVYGFTPLHYAVYNNN-----PEFVKYLLDLGANPNL 220

                        170       180
                 ....*....|....*....|....*....
gi 504697848 173 TDKYGKTPLELAREKGYHAIADLLLAAGA 201
Cdd:PHA03100 221 VNKYGDTPLHIAILNNNKEIFKLLLNNGP 249
Ank_2 pfam12796
Ankyrin repeats (3 copies);
43-174 8.69e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 56.28  E-value: 8.69e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697848   43 IIIASLKKHYACVEFLIAAGADIDKQDQTCFNPFLISCltndltllrivlpanpdldrltrfggvgitpasEKGHVEIVR 122
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAA---------------------------------KNGHLEIVK 47

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 504697848  123 ELLAKTDINVNHTnfvGWTPLLEAIVLNdggekQQEIVKLLLDNGANPHMTD 174
Cdd:pfam12796  48 LLLEHADVNLKDN---GRTALHYAARSG-----HLEIVKLLLEKGADINVKD 91
Ank_4 pfam13637
Ankyrin repeats (many copies);
13-59 3.96e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.43  E-value: 3.96e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 504697848   13 AAEEGNVDALKACLEKGVDINATNRQKRTAIIIASLKKHYACVEFLI 59
Cdd:pfam13637   8 AAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
112-201 5.52e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 53.97  E-value: 5.52e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697848  112 ASEKGHVEIVRELLaKTDINVNHTNFVGWTPLLEAIVLNdggekQQEIVKLLLDNgANPHMTDkYGKTPLELAREKGYHA 191
Cdd:pfam12796   4 AAKNGNLELVKLLL-ENGADANLQDKNGRTALHLAAKNG-----HLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLE 75

                          90
                  ....*....|
gi 504697848  192 IADLLLAAGA 201
Cdd:pfam12796  76 IVKLLLEKGA 85
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 10-201 7.93e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 57.38  E-value: 7.93e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697848  10 FLLAAEEGNVDALKACLEKGVDINATNRQKRTAIIIAS-LKKHYACVEFLIAAGADIDKQDQTCFNPFLISCLTNDLTLL 88
Cdd:PHA02876 312 YLMAKNGYDTENIRTLIMLGADVNAADRLYITPLHQAStLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVII 391

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697848  89 RIVLPANPDLDRLTRFGGVGITPASEKGHVEIVRELLAKTDINVNHTNFVGWTPLLEAIVLNdggeKQQEIVKLLLDNGA 168
Cdd:PHA02876 392 NTLLDYGADIEALSQKIGTALHFALCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKN----CKLDVIEMLLDNGA 467

                        170       180       190
                 ....*....|....*....|....*....|...
gi 504697848 169 NPHMTDKYGKTPLELARekGYHAIADLLLAAGA 201
Cdd:PHA02876 468 DVNAINIQNQYPLLIAL--EYHGIVNILLHYGA 498
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 1-200 1.60e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 53.43  E-value: 1.60e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697848   1 MSATALVTEFLLAAEEGNVDALKACLEKGVDINATNRQKRTAIIIASLKKHYACVEFLIAAGADidkqdqTCFNPflISC 80
Cdd:PHA02874  30 ISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVD------TSILP--IPC 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697848  81 LTNDLtlLRIVLPANPDLDRLTRFGGVGITPASEKGHVEIVRELLA-KTDINVNHTNfvGWTPLLEAIVLNdggekQQEI 159
Cdd:PHA02874 102 IEKDM--IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEyGADVNIEDDN--GCYPIHIAIKHN-----FFDI 172

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 504697848 160 VKLLLDNGANPHMTDKYGKTPLELAREKGYHAIADLLLAAG 200
Cdd:PHA02874 173 IKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHG 213
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 18-184 3.81e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 52.27  E-value: 3.81e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697848  18 NVDALKACLEKGVDINATNRQKRTAIIIASLKKHYACVEFLIAAGADIDKQDQTCFNPFLISCLTNDLTLLRIVLPANPD 97
Cdd:PHA02874 103 EKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAY 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697848  98 LDRLTRFGGVGITPASEKGHVEIVRELLAKTDINVNHTNfVGWTPLLEAIVLNdggekqQEIVKLLLDNgANPHMTDKYG 177
Cdd:PHA02874 183 ANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCK-NGFTPLHNAIIHN------RSAIELLINN-ASINDQDIDG 254


                 ....*..
gi 504697848 178 KTPLELA 184
Cdd:PHA02874 255 STPLHHA 261
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 12-67 3.98e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 52.56  E-value: 3.98e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 504697848  12 LAAEEGNVDALKACLEKGVDINATNRQKRTAIIIASLKKHYACVEFLIAAGADIDK 67
Cdd:PLN03192 628 TAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDK 683
Ank_2 pfam12796
Ankyrin repeats (3 copies);
10-100 4.06e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 48.96  E-value: 4.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697848   10 FLLAAEEGNVDALKACLEKGVDINATNRQKRTAIIIASLKKHYACVEFLIaAGADIDKQDQTcFNPFLISCLTNDLTLLR 89
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKDNG-RTALHYAARSGHLEIVK 78

                          90
                  ....*....|.
gi 504697848   90 IVLPANPDLDR 100
Cdd:pfam12796  79 LLLEKGADINV 89
PHA03095 PHA03095
ankyrin-like protein; Provisional
 18-198 1.39e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 50.79  E-value: 1.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697848  18 NVDALKACLEKGVDINATNRQKRTAIIIAsLKKHYACVE---FLIAAGADI---DKQDQTCFNPFLISCLTNDlTLLRIV 91
Cdd:PHA03095 131 NPKVIRLLLRKGADVNALDLYGMTPLAVL-LKSRNANVEllrLLIDAGADVyavDDRFRSLLHHHLQSFKPRA-RIVREL 208

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697848  92 LPANPDLDRLTRFGGVGITPASEKGHVE--IVRELLAKtDINVNHTNFVGWTPLLEAIVLNdggekQQEIVKLLLDNGAN 169
Cdd:PHA03095 209 IRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIA-GISINARNRYGQTPLHYAAVFN-----NPRACRRLIALGAD 282

                        170       180
                 ....*....|....*....|....*....
gi 504697848 170 PHMTDKYGKTPLELAREKGYHAIADLLLA 198
Cdd:PHA03095 283 INAVSSDGNTPLSLMVRNNNGRAVRAALA 311
PHA03095 PHA03095
ankyrin-like protein; Provisional
 118-201 2.53e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 50.02  E-value: 2.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697848 118 VEIVRELLAKtDINVNHTNFVGWTPLleAIVLNDGGEKQQEIVKLLLDNGANPHMTDKYGKTPLELAREKGYHA-IADLL 196
Cdd:PHA03095  27 VEEVRRLLAA-GADVNFRGEYGKTPL--HLYLHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLL 103


                 ....*
gi 504697848 197 LAAGA 201
Cdd:PHA03095 104 IKAGA 108
PHA03095 PHA03095
ankyrin-like protein; Provisional
 10-182 6.05e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 48.87  E-value: 6.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697848  10 FLLAAEEGNVDALKACLEKGVDINATNRQKRTAIiiaSLKKHYAC------VEFLIAAGADIDKQDQTCFNPfLISCLTN 83
Cdd:PHA03095  18 YLLNASNVTVEEVRRLLAAGADVNFRGEYGKTPL---HLYLHYSSekvkdiVRLLLEAGADVNAPERCGFTP-LHLYLYN 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697848  84 DLTL--LRIVLPANPDldrLTRFGGVGITP-----ASEKGHVEIVRELLAKtDINVNHTNFVGWTPLLEAIVLNDGgekQ 156
Cdd:PHA03095  94 ATTLdvIKLLIKAGAD---VNAKDKVGRTPlhvylSGFNINPKVIRLLLRK-GADVNALDLYGMTPLAVLLKSRNA---N 166

                        170       180
                 ....*....|....*....|....*.
gi 504697848 157 QEIVKLLLDNGANPHMTDKYGKTPLE 182
Cdd:PHA03095 167 VELLRLLIDAGADVYAVDDRFRSLLH 192
Ank_2 pfam12796
Ankyrin repeats (3 copies);
4-69 9.41e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 45.49  E-value: 9.41e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504697848    4 TALvtefLLAAEEGNVDALKACLEKgVDINATNrQKRTAIIIASLKKHYACVEFLIAAGADIDKQD 69
Cdd:pfam12796  32 TAL----HLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 19-201 2.32e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.94  E-value: 2.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697848  19 VDALKACLEKGVDINATNRQKRTAIII--ASLKKHYACVEFLIAAGADIDKQDQTCFNP---FLISclTN-DLTLLRIVL 92
Cdd:PHA03095  97 LDVIKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPlavLLKS--RNaNVELLRLLI 174

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697848  93 -----PANPDLDRLTRFGgvgITPASEKGHVEIVRELLAKtDINVNHTNFVGWTPLLeaiVLNDGGEKQQEIVKLLLDNG 167
Cdd:PHA03095 175 dagadVYAVDDRFRSLLH---HHLQSFKPRARIVRELIRA-GCDPAATDMLGNTPLH---SMATGSSCKRSLVLPLLIAG 247

                        170       180       190
                 ....*....|....*....|....*....|....
gi 504697848 168 ANPHMTDKYGKTPLELAREKGYHAIADLLLAAGA 201
Cdd:PHA03095 248 ISINARNRYGQTPLHYAAVFNNPRACRRLIALGA 281
Ank_5 pfam13857
Ankyrin repeats (many copies);
124-184 4.58e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.33  E-value: 4.58e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504697848  124 LLAKTDINVNHTNFVGWTPLLEAIVLNDggekqQEIVKLLLDNGANPHMTDKYGKTPLELA 184
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGA-----LEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 159-197 5.44e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.04  E-value: 5.44e-06
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 504697848 159 IVKLLLDNGANPHMTDKYGKTPLELAREKGYHAIADLLL 197
Cdd:PTZ00322 130 VVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 22-189 7.27e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 45.64  E-value: 7.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697848  22 LKACLEKGVDINATNRQK-RTAIIIASLKKHYACVEFLIAAGADIDKQDQTCFNPFLISCLTNDLTLLRIVLPANPDLDR 100
Cdd:PHA02878 150 TKLLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDA 229

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697848 101 LTRFGGVGITPASEK-GHVEIVRELLAK-TDINVNHTnFVGWTPLLEAIvlndggeKQQEIVKLLLDNGANPHMTDKYGK 178
Cdd:PHA02878 230 RDKCGNTPLHISVGYcKDYDILKLLLEHgVDVNAKSY-ILGLTALHSSI-------KSERKLKLLLEYGADINSLNSYKL 301

                        170
                 ....*....|.
gi 504697848 179 TPLELAREKGY 189
Cdd:PHA02878 302 TPLSSAVKQYL 312
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 17-201 7.44e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 45.75  E-value: 7.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697848  17 GNVDALKACLEKGVDINATNRQKRTAIIIASLKKHYACVEFLIAAGADIDKQDQTCFNPFLISCLTNDLTLLRIVLPANP 96
Cdd:PHA02875  13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGK 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697848  97 DLDRLtrFGGVGITP---ASEKGHVEIVRELLA-KTDINVNHTNfvGWTPLLEAIVLNDggekqQEIVKLLLDNGANPHM 172
Cdd:PHA02875  93 FADDV--FYKDGMTPlhlATILKKLDIMKLLIArGADPDIPNTD--KFSPLHLAVMMGD-----IKGIELLIDHKACLDI 163

                        170       180
                 ....*....|....*....|....*....
gi 504697848 173 TDKYGKTPLELAREKGYHAIADLLLAAGA 201
Cdd:PHA02875 164 EDCCGCTPLIIAMAKGDIAICKMLLDSGA 192
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 8-165 1.61e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 44.60  E-value: 1.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697848   8 TEFLLAAEEGNVDALKACLEKGVDINATNRQKRTAIIIASLKKHYACVEFLIAAGADIDKQDQTCFNPFLISCLTNDLTL 87
Cdd:PHA02875 104 TPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAI 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697848  88 LRIVLPANPDLDRLTRFGGVG-ITPASEKGHVEIVRELLAK-TDINVNHTNFVGWTPLLEAIVLNDGGEKQQEIVKLLLD 165
Cdd:PHA02875 184 CKMLLDSGANIDYFGKNGCVAaLCYAIENNKIDIVRLFIKRgADCNIMFMIEGEECTILDMICNMCTNLESEAIDALIAD 263
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 11-185 1.81e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 44.47  E-value: 1.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697848  11 LLAAEEGNVDALKACLEKGVDINATNRQKRTAIIIASLKKHYACVEFLIAAGADIDKQDQTCFNPFLISCLTNDLTLLRI 90
Cdd:PLN03192 530 LTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRI 609

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697848  91 VL----PANPDLdrltrfGGVGITPASEKGHVEIVRELLaKTDINVNHTNFVGWTPLLEAIvlndgGEKQQEIVKLLLDN 166
Cdd:PLN03192 610 LYhfasISDPHA------AGDLLCTAAKRNDLTAMKELL-KQGLNVDSEDHQGATALQVAM-----AEDHVDMVRLLIMN 677

                        170       180
                 ....*....|....*....|
gi 504697848 167 GANPHMTDKYGK-TPLELAR 185
Cdd:PLN03192 678 GADVDKANTDDDfSPTELRE 697
PHA03095 PHA03095
ankyrin-like protein; Provisional
 26-99 3.17e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 43.86  E-value: 3.17e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504697848  26 LEKGVDINATNRQKRTAIIIASLKKHYACVEFLIAAGADIDKQDQTCFNPFLISCLTNDLTLLRIVLPANPDLD 99
Cdd:PHA03095 244 LIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAE 317
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 13-201 1.19e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 41.90  E-value: 1.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697848  13 AAEEGNVDALKACLEKGVDINATNRQK-RTAIIIASLKKHYACVEFLIAAGADIDKQDQTCFNPFLISCLTNDLTLLriv 91
Cdd:PHA02875  75 AVEEGDVKAVEELLDLGKFADDVFYKDgMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGI--- 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697848  92 lpanpdldrltrfggvgitpasekghveivrELLAKTDINVNHTNFVGWTPLLEAIvlndgGEKQQEIVKLLLDNGANPH 171
Cdd:PHA02875 152 -------------------------------ELLIDHKACLDIEDCCGCTPLIIAM-----AKGDIAICKMLLDSGANID 195

                        170       180       190
                 ....*....|....*....|....*....|.
gi 504697848 172 MTDKYGK-TPLELAREKGYHAIADLLLAAGA 201
Cdd:PHA02875 196 YFGKNGCvAALCYAIENNKIDIVRLFIKRGA 226
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 11-198 1.33e-04

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 41.99  E-value: 1.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697848   11 LLAAEEGNVDALKACL-------EKGVDINATNRQK-------RTAIIIASLKKHYACVEFLIAAGADIdkQDQTCFNPF 76
Cdd:TIGR00870  86 LHAISLEYVDAVEAILlhllaafRKSGPLELANDQYtseftpgITALHLAAHRQNYEIVKLLLERGASV--PARACGDFF 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697848   77 LISCLTNDLtllrivlpanpdldrltRFGGVGITPASEKGHVEIVReLLAKTDINVNHTNFVGWTpLLEAIVL-----ND 151
Cdd:TIGR00870 164 VKSQGVDSF-----------------YHGESPLNAAACLGSPSIVA-LLSEDPADILTADSLGNT-LLHLLVMenefkAE 224

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 504697848  152 GGEKQQEIVKLLLDNGANP-------HMTDKYGKTPLELAREKGYHAIADLLLA 198
Cdd:TIGR00870 225 YEELSCQMYNFALSLLDKLrdskeleVILNHQGLTPLKLAAKEGRIVLFRLKLA 278
Ank_4 pfam13637
Ankyrin repeats (many copies);
139-197 1.97e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.02  E-value: 1.97e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 504697848  139 GWTPLLEAIVLNDggekqQEIVKLLLDNGANPHMTDKYGKTPLELAREKGYHAIADLLL 197
Cdd:pfam13637   1 ELTALHAAAASGH-----LELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 11-181 3.26e-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: 40.77  E-value: 3.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697848  11 LLAAEEGNVDALKACLE-KGVDINATNRQKRTAIIIASLKKHYACVEFLIAAGADIDKQDQTcfnpfliSCLTNDLTLLR 89
Cdd:cd22192   22 LLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEPMT-------SDLYQGETALH 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697848  90 IvlpanpdldrltrfggvgitpASEKGHVEIVRELLAK-TDIN---VNHTNFV---------GWTPL-LEAIVLNdggek 155
Cdd:cd22192   95 I---------------------AVVNQNLNLVRELIARgADVVsprATGTFFRpgpknliyyGEHPLsFAACVGN----- 148

                        170       180
                 ....*....|....*....|....*.
gi 504697848 156 qQEIVKLLLDNGANPHMTDKYGKTPL 181
Cdd:cd22192  149 -EEIVRLLIEHGADIRAQDSLGNTVL 173
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 13-201 3.80e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 40.63  E-value: 3.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697848  13 AAEEGNVDALKACLEKGVDINATNRQKRTAIIIASLKKHYACVEFLIAagadIDKQDQTCFNPFLIS--CLTNDLTLLRI 90
Cdd:PHA02878  44 AVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIR----SINKCSVFYTLVAIKdaFNNRNVEIFKI 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697848  91 VLPANPDLDRLTRFGGVGITPASEKGHVEIVRELLAK-TDINVNHTNfVGWTPLLEAivlndGGEKQQEIVKLLLDNGAN 169
Cdd:PHA02878 120 ILTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYgADINMKDRH-KGNTALHYA-----TENKDQRLTELLLSYGAN 193

                        170       180       190
                 ....*....|....*....|....*....|..
gi 504697848 170 PHMTDKYGKTPLELAREKGYHAIADLLLAAGA 201
Cdd:PHA02878 194 VNIPDKTNNSPLHHAVKHYNKPIVHILLENGA 225
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 7-201 5.01e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 40.43  E-value: 5.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697848   7 VTEFLLAAEEGNVDALKACLEKGVDINATNRQKRTAIIIASLKKHYACVEFLIAAGADIDKQDQTCFNPFLISCLTNDLT 86
Cdd:PHA02876 179 ITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKNDLSLLKAIRNEDLETSLL 258

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697848  87 LLRIVLPAN----------------PDLDRLTRF---GGVGITPASEKGHV------------EIVRELLAKtDINVNHT 135
Cdd:PHA02876 259 LYDAGFSVNsiddckntplhhasqaPSLSRLVPKlleRGADVNAKNIKGETplylmakngydtENIRTLIML-GADVNAA 337

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504697848 136 NFVGWTPLLEAIVLndggEKQQEIVKLLLDNGANPHMTDKYGKTPLELAREKGYHAIADLLLAAGA 201
Cdd:PHA02876 338 DRLYITPLHQASTL----DRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGA 399
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 4-188 7.51e-04

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: 39.74  E-value: 7.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697848   4 TALVTEFLLAAEEGNvdalkACLEKGVDINATNRQKR--TAIIIASLKKHYACVEFLIAAGADIDKQDQ-TCFNPflisc 80
Cdd:cd22194  109 TKEIVRILLAFAEEN-----GILDRFINAEYTEEAYEgqTALNIAIERRQGDIVKLLIAKGADVNAHAKgVFFNP----- 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697848  81 ltndltllrivlpanPDLDRLTRFGGVGITPASEKGHVEIVRELLAKTDINVNHTNFVGWTPLLEAIVLNDGGEKQQEIV 160
Cdd:cd22194  179 ---------------KYKHEGFYFGETPLALAACTNQPEIVQLLMEKESTDITSQDSRGNTVLHALVTVAEDSKTQNDFV 243

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 504697848 161 KLLLD------NGAN-PHMTDKYGKTPLELAREKG 188
Cdd:cd22194  244 KRMYDmillksENKNlETIRNNEGLTPLQLAAKMG 278
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 139-175 1.20e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 35.34  E-value: 1.20e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 504697848  139 GWTPLLEAIVLNDggekQQEIVKLLLDNGANPHMTDK 175
Cdd:pfam00023   2 GNTPLHLAAGRRG----NLEIVKLLLSKGADVNARDK 34
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 28-201 1.22e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 38.79  E-value: 1.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697848  28 KGVDINATNRQKRTAIIIASLKKHYACVEFLIAAGADIDKQDQTCFNPFL--ISCLTNDLTLLRI-------VLPAnPDL 98
Cdd:PHA02874  24 KGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLtaIKIGAHDIIKLLIdngvdtsILPI-PCI 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697848  99 DRltrfggvgitpasekghvEIVRELLaKTDINVNHTNFVGWTPLLEAIVLNDggekqQEIVKLLLDNGANPHMTDKYGK 178
Cdd:PHA02874 103 EK------------------DMIKTIL-DCGIDVNIKDAELKTFLHYAIKKGD-----LESIKMLFEYGADVNIEDDNGC 158

                        170       180
                 ....*....|....*....|...
gi 504697848 179 TPLELAREKGYHAIADLLLAAGA 201
Cdd:PHA02874 159 YPIHIAIKHNFFDIIKLLLEKGA 181
Ank_4 pfam13637
Ankyrin repeats (many copies);
40-89 2.63e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 34.94  E-value: 2.63e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 504697848   40 RTAIIIASLKKHYACVEFLIAAGADIDKQDQTCFNPFLISCLTNDLTLLR 89
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLK 51
PHA03095 PHA03095
ankyrin-like protein; Provisional
 118-201 3.32e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 37.70  E-value: 3.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697848 118 VEIVRELLAKtDINVNHTNFVGWTPLlEAIVLNDGGEkqqEIVKLLLDNGANPHMTDKYGKTPLEL-AREKGYHA-IADL 195
Cdd:PHA03095  63 KDIVRLLLEA-GADVNAPERCGFTPL-HLYLYNATTL---DVIKLLIKAGADVNAKDKVGRTPLHVyLSGFNINPkVIRL 137


                 ....*.
gi 504697848 196 LLAAGA 201
Cdd:PHA03095 138 LLRKGA 143
PHA02798 PHA02798
ankyrin-like protein; Provisional
 18-133 3.49e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 37.51  E-value: 3.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697848  18 NVDALKACLEKGVDINATNRQKRT-------AIIIASLKKHYACVEFlIAAGADIDKQDQTCFNPFLISCLTNDLTLLRI 90
Cdd:PHA02798 198 DADILKLFVDNGFIINKENKSHKKkfmeylnSLLYDNKRFKKNILDF-IFSYIDINQVDELGFNPLYYSVSHNNRKIFEY 276

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 504697848  91 VLPANPDLDRLTRFGGVGITPASEKGHVEIVRELLAKtDINVN 133
Cdd:PHA02798 277 LLQLGGDINIITELGNTCLFTAFENESKFIFNSILNK-KPNKN 318
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 8-71 3.94e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 37.34  E-value: 3.94e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504697848   8 TEFLLAAEEGNVDALKACLEKGVDINATNRQKRTAIIIASLKKHYACVEFLIAAGADIDKQDQT 71
Cdd:PHA03100 194 TPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 114-181 5.71e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 36.34  E-value: 5.71e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504697848 114 EKGHVEIVrELLAKTDINVNH-TNFVGWTPLLEAIVLNDGGEkqQEIVKLLLDNGANPHMTDKYGKTPL 181
Cdd:PHA02859  62 DKVNVEIL-KFLIENGADVNFkTRDNNLSALHHYLSFNKNVE--PEILKILIDSGSSITEEDEDGKNLL 127
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 158-201 6.35e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 36.57  E-value: 6.35e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 504697848 158 EIVKLLLDNGANPHMTDKYGKTPLELAREKGYHA-----IADLLLAAGA 201
Cdd:PHA03100  49 DVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLtdvkeIVKLLLEYGA 97
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 118-201 8.65e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 36.58  E-value: 8.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504697848 118 VEIVRELLAKTDINVNHTN-FVGWTPLLEAIVLNDggekQQEIVKLLLDNGANPHMTDKYGKTPLELAREKGYHAIADLL 196
Cdd:PHA02876 122 IHILKEAISGNDIHYDKINeSIEYMKLIKERIQQD----ELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLL 197


                 ....*
gi 504697848 197 LAAGA 201
Cdd:PHA02876 198 LSYGA 202
 
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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