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Conserved domains on  [gi|26345898|dbj|BAC36600|]
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unnamed protein product [Mus musculus]

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];
25-258 8.66e-43

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 147.79  E-value: 8.66e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345898  25 ISLAKTAPPSLSIGGGYHLRDKHLKKLHKAATIGNEQKLKDYLERKKYNVNGRDKRSRTPLHLACANGYTNIVSLLIENQ 104
Cdd:COG0666  31 LLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAG 110

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345898 105 CKINVQDSENRTPLIKqAVECQQESCATVLLLHGADPNLVDVYSNTALHYAVCGQNISLANKLLQYKANLEAKNKDGHTP 184
Cdd:COG0666 111 ADVNARDKDGETPLHL-AAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETP 189

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 26345898 185 LLLAVAENNENMVKFLLKKGADVNASDKNHRTAIMIALIVEPTSSVKLLLQQDTDLAHKDIYGFTAEEYASFNG 258
Cdd:COG0666 190 LHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAG 263
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
25-258 8.66e-43

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 147.79  E-value: 8.66e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345898  25 ISLAKTAPPSLSIGGGYHLRDKHLKKLHKAATIGNEQKLKDYLERKKYNVNGRDKRSRTPLHLACANGYTNIVSLLIENQ 104
Cdd:COG0666  31 LLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAG 110

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345898 105 CKINVQDSENRTPLIKqAVECQQESCATVLLLHGADPNLVDVYSNTALHYAVCGQNISLANKLLQYKANLEAKNKDGHTP 184
Cdd:COG0666 111 ADVNARDKDGETPLHL-AAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETP 189

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 26345898 185 LLLAVAENNENMVKFLLKKGADVNASDKNHRTAIMIALIVEPTSSVKLLLQQDTDLAHKDIYGFTAEEYASFNG 258
Cdd:COG0666 190 LHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAG 263
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 51-235 1.03e-19

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 88.18  E-value: 1.03e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345898   51 LHKAATIGNEQKLKdYLERKKYNVNGRDKRSRTPLHLACANGYT-----NIVSLLIENQCKINVQDSENRTPLIKQAVEC 125
Cdd:PHA03100  39 LYLAKEARNIDVVK-ILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKK 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345898  126 -QQESCATVLLLHGADPNLVDVYSNTALHYAV--CGQNISLANKLLQYKANLEAKN--------------KD--GHTPLL 186
Cdd:PHA03100 118 sNSYSIVEYLLDNGANVNIKNSDGENLLHLYLesNKIDLKILKLLIDKGVDINAKNrvnyllsygvpiniKDvyGFTPLH 197

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 26345898  187 LAVAENNENMVKFLLKKGADVNASDKNHRTAIMIALIVEPTSSVKLLLQ 235
Cdd:PHA03100 198 YAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLN 246
Ank_2 pfam12796
Ankyrin repeats (3 copies);
85-211 2.66e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 69.76  E-value: 2.66e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345898    85 LHLACANGYTNIVSLLIENqckinvqdsenrtplikqavecqqescatvlllhGADPNLVDVYSNTALHYAVCGQNISLA 164
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLEN----------------------------------GADANLQDKNGRTALHLAAKNGHLEIV 46

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 26345898   165 nKLLQYKANLEAKNkDGHTPLLLAVAENNENMVKFLLKKGADVNASD 211
Cdd:pfam12796  47 -KLLLEHADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 131-241 1.59e-06

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 48.86  E-value: 1.59e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345898 131 ATVLLLHGAdPNLV------DVYSN-TALHYAVCGQNISLANKLLQYKANLEA---------KNKD-----GHTPLLLAV 189
Cdd:cd22192  66 AAVVLMEAA-PELVnepmtsDLYQGeTALHIAVVNQNLNLVRELIARGADVVSpratgtffrPGPKnliyyGEHPLSFAA 144

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 26345898 190 AENNENMVKFLLKKGADVNASDKNHRTAIMIaliveptssvkLLLQQDTDLA 241
Cdd:cd22192 145 CVGNEEIVRLLIEHGADIRAQDSLGNTVLHI-----------LVLQPNKTFA 185
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 49-209 6.31e-06

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: 47.38  E-value: 6.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345898    49 KKLHKAATIGNEQKLKDYL-ERKKYNVNGRDKRSRTPL-HLACANGYTNIVSLLIENQCKINVQDSenrtplikqavecq 126
Cdd:TIGR00870  19 KAFLPAAERGDLASVYRDLeEPKKLNINCPDRLGRSALfVAAIENENLELTELLLNLSCRGAVGDT-------------- 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345898   127 qescatvlLLHGADPNLVDVYSNTALH---YAVCGQNISLANKllQYKANLEAknkdGHTPLLLAVAENNENMVKFLLKK 203
Cdd:TIGR00870  85 --------LLHAISLEYVDAVEAILLHllaAFRKSGPLELAND--QYTSEFTP----GITALHLAAHRQNYEIVKLLLER 150


                  ....*.
gi 26345898   204 GADVNA 209
Cdd:TIGR00870 151 GASVPA 156
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 180-209 1.64e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.03  E-value: 1.64e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 26345898    180 DGHTPLLLAVAENNENMVKFLLKKGADVNA 209
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
25-258 8.66e-43

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 147.79  E-value: 8.66e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345898  25 ISLAKTAPPSLSIGGGYHLRDKHLKKLHKAATIGNEQKLKDYLERKKYNVNGRDKRSRTPLHLACANGYTNIVSLLIENQ 104
Cdd:COG0666  31 LLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAG 110

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345898 105 CKINVQDSENRTPLIKqAVECQQESCATVLLLHGADPNLVDVYSNTALHYAVCGQNISLANKLLQYKANLEAKNKDGHTP 184
Cdd:COG0666 111 ADVNARDKDGETPLHL-AAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETP 189

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 26345898 185 LLLAVAENNENMVKFLLKKGADVNASDKNHRTAIMIALIVEPTSSVKLLLQQDTDLAHKDIYGFTAEEYASFNG 258
Cdd:COG0666 190 LHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAG 263
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
51-250 3.01e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 130.84  E-value: 3.01e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345898  51 LHKAATIGNEQKLKdYLERKKYNVNGRDKRSRTPLHLACANGYTNIVSLLIENQCKINVQDSENRTPLIKqAVECQQESC 130
Cdd:COG0666  91 LHAAARNGDLEIVK-LLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHL-AAANGNLEI 168

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345898 131 ATVLLLHGADPNLVDVYSNTALHYAVCGQNISLANKLLQYKANLEAKNKDGHTPLLLAVAENNENMVKFLLKKGADVNAS 210
Cdd:COG0666 169 VKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAK 248

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 26345898 211 DKNHRTAIMIALIVEPTSSVKLLLQQDTDLAHKDIYGFTA 250
Cdd:COG0666 249 DKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
43-258 1.21e-34

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 126.61  E-value: 1.21e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345898  43 LRDKHLKKLHKAATIGNEQKLKDYLERKKYNVNGRDKRSRTPLHLACANGYTNIVSLLIENQCKINVQDSENRTPLIkQA 122
Cdd:COG0666  16 LLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLH-AA 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345898 123 VECQQESCATVLLLHGADPNLVDVYSNTALHYAVCGQNISLANKLLQYKANLEAKNKDGHTPLLLAVAENNENMVKFLLK 202
Cdd:COG0666  95 ARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLE 174

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 26345898 203 KGADVNASDKNHRTAIMIALIVEPTSSVKLLLQQDTDLAHKDIYGFTAEEYASFNG 258
Cdd:COG0666 175 AGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENG 230
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
51-218 2.84e-26

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 104.27  E-value: 2.84e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345898  51 LHKAATIGNEQKLKdYLERKKYNVNGRDKRSRTPLHLACANGYTNIVSLLIENQCKINVQDSENRTPLIkQAVECQQESC 130
Cdd:COG0666 124 LHLAAYNGNLEIVK-LLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLH-LAAENGHLEI 201

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345898 131 ATVLLLHGADPNLVDVYSNTALHYAVCGQNISLANKLLQYKANLEAKNKDGHTPLLLAVAENNENMVKFLLKKGADVNAS 210
Cdd:COG0666 202 VKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAA 281


                ....*...
gi 26345898 211 DKNHRTAI 218
Cdd:COG0666 282 LLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
67-258 4.03e-26

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 103.88  E-value: 4.03e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345898  67 LERKKYNVNGRDKRSRTPLHLACANGYTNIVSLLIENQCKINVQDSENRTPLIKQAVECQQESCATVLLLHGADPNLVDV 146
Cdd:COG0666   6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345898 147 YSNTALHYAVCGQNISLANKLLQYKANLEAKNKDGHTPLLLAVAENNENMVKFLLKKGADVNASDKNHRTAIMIALIVEP 226
Cdd:COG0666  86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGN 165

                       170       180       190
                ....*....|....*....|....*....|..
gi 26345898 227 TSSVKLLLQQDTDLAHKDIYGFTAEEYASFNG 258
Cdd:COG0666 166 LEIVKLLLEAGADVNARDNDGETPLHLAAENG 197
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 51-235 1.03e-19

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 88.18  E-value: 1.03e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345898   51 LHKAATIGNEQKLKdYLERKKYNVNGRDKRSRTPLHLACANGYT-----NIVSLLIENQCKINVQDSENRTPLIKQAVEC 125
Cdd:PHA03100  39 LYLAKEARNIDVVK-ILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKK 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345898  126 -QQESCATVLLLHGADPNLVDVYSNTALHYAV--CGQNISLANKLLQYKANLEAKN--------------KD--GHTPLL 186
Cdd:PHA03100 118 sNSYSIVEYLLDNGANVNIKNSDGENLLHLYLesNKIDLKILKLLIDKGVDINAKNrvnyllsygvpiniKDvyGFTPLH 197

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 26345898  187 LAVAENNENMVKFLLKKGADVNASDKNHRTAIMIALIVEPTSSVKLLLQ 235
Cdd:PHA03100 198 YAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLN 246
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
96-258 8.60e-18

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 81.15  E-value: 8.60e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345898  96 IVSLLIENQCKINVQDSENRTPLIKQAVECQQESCATVLLLHGADPNLVDVYSNTALHYAVCGQNISLANKLLQYKANLE 175
Cdd:COG0666   2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345898 176 AKNKDGHTPLLLAVAENNENMVKFLLKKGADVNASDKNHRTAIMIALIVEPTSSVKLLLQQDTDLAHKDIYGFTAEEYAS 255
Cdd:COG0666  82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161


                ...
gi 26345898 256 FNG 258
Cdd:COG0666 162 ANG 164
PHA03095 PHA03095
ankyrin-like protein; Provisional
 73-254 3.54e-17

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 80.84  E-value: 3.54e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345898   73 NVNGRDKRSRTPLH--LACANG-YTNIVSLLIENQCKINVQDSENRTPLIKQAVECQQESCATVLLLHGADPNLVDVYSN 149
Cdd:PHA03095  39 DVNFRGEYGKTPLHlyLHYSSEkVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDVIKLLIKAGADVNAKDKVGR 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345898  150 TALHYAVCGQNI--SLANKLLQYKANLEAKNKDGHTPLLLAVAENNEN--MVKFLLKKGADVNASDKNHRTAI-MIALIV 224
Cdd:PHA03095 119 TPLHVYLSGFNInpKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANveLLRLLIDAGADVYAVDDRFRSLLhHHLQSF 198

                        170       180       190
                 ....*....|....*....|....*....|.
gi 26345898  225 EPTSSV-KLLLQQDTDLAHKDIYGFTAEEYA 254
Cdd:PHA03095 199 KPRARIvRELIRAGCDPAATDMLGNTPLHSM 229
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 73-223 9.33e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 79.32  E-value: 9.33e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345898   73 NVNGRDKRSRTPLHLACAN--GYTNIVSLLIENQCKINVQDSENRTPLiKQAVECQQESCATV----------------- 133
Cdd:PHA03100  98 NVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLL-HLYLESNKIDLKILkllidkgvdinaknrvn 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345898  134 -LLLHGADPNLVDVYSNTALHYAVCGQNISLANKLLQYKANLEAKNKDGHTPLLLAVAENNENMVKFLLKKGADVNA--- 209
Cdd:PHA03100 177 yLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTiie 256

                        170
                 ....*....|....*....
gi 26345898  210 -----SDKNHRTAIMIALI 223
Cdd:PHA03100 257 tllyfKDKDLNTITKIKML 275
PHA03095 PHA03095
ankyrin-like protein; Provisional
 87-250 2.22e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 78.53  E-value: 2.22e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345898   87 LACANGYTNIVSLLIENQCKINVQDSENRTPLiKQAVECQQESCATV---LLLHGADPNLVDVYSNTALHYAVCGQN-IS 162
Cdd:PHA03095  20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPL-HLYLHYSSEKVKDIvrlLLEAGADVNAPERCGFTPLHLYLYNATtLD 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345898  163 LANKLLQYKANLEAKNKDGHTPL--LLAVAENNENMVKFLLKKGADVNASDKNHRTAIMIALI---VEPtSSVKLLLQQD 237
Cdd:PHA03095  99 VIKLLIKAGADVNAKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKsrnANV-ELLRLLIDAG 177

                        170
                 ....*....|...
gi 26345898  238 TDLAHKDIYGFTA 250
Cdd:PHA03095 178 ADVYAVDDRFRSL 190
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 51-221 9.72e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 77.03  E-value: 9.72e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345898   51 LHKAATIGNEQKLKDYLERKKYNVNGRDKRSRTPLHLACANGY-TNIVSLLIENQCKINVQDSENRTPLIKQAVECQQES 129
Cdd:PHA02876 277 LHHASQAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKD 356

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345898  130 CATVLLLHGADPNLVDVYSNTALHYAVCGQNISLANKLLQYKANLEAKNKDGHTPLLLAVAENNENM-VKFLLKKGADVN 208
Cdd:PHA02876 357 IVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMsVKTLIDRGANVN 436

                        170
                 ....*....|...
gi 26345898  209 ASDKNHRTAIMIA 221
Cdd:PHA02876 437 SKNKDLSTPLHYA 449
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 54-211 1.03e-15

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 76.83  E-value: 1.03e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345898   54 AATIGNEQKLKDYLeRKKYNVNGRDKRSRTPLHLACANGYTNIVSLLIENQCKINVQDSENRTPLIkQAVECQQESCATV 133
Cdd:PLN03192 532 VASTGNAALLEELL-KAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALW-NAISAKHHKIFRI 609

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345898  134 L--LLHGADPNLvdvySNTALHYAVCGQNISLANKLLQYKANLEAKNKDGHTPLLLAVAENNENMVKFLLKKGADVNASD 211
Cdd:PLN03192 610 LyhFASISDPHA----AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAN 685
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 19-240 1.56e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 76.26  E-value: 1.56e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345898   19 HSSEVPiSLAKTAPPSLSIGGGYHLRD-KHLKKLHKAATIGNEQKLKDYLERKKYNVNGRDKRSRTPLHLACA-NGYTNI 96
Cdd:PHA02876 279 HASQAP-SLSRLVPKLLERGADVNAKNiKGETPLYLMAKNGYDTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDI 357

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345898   97 VSLLIENQCKINVQDSENRTPLIKQAVEcQQESCATVLLLHGADPNLVDVYSNTALHYAVCGQNISLANK-LLQYKANLE 175
Cdd:PHA02876 358 VITLLELGANVNARDYCDKTPIHYAAVR-NNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMSVKtLIDRGANVN 436

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 26345898  176 AKNKDGHTPLLLAVAENNE-NMVKFLLKKGADVNASDKNHRTAIMIALivEPTSSVKLLLQQDTDL 240
Cdd:PHA02876 437 SKNKDLSTPLHYACKKNCKlDVIEMLLDNGADVNAINIQNQYPLLIAL--EYHGIVNILLHYGAEL 500
Ank_2 pfam12796
Ankyrin repeats (3 copies);
85-211 2.66e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 69.76  E-value: 2.66e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345898    85 LHLACANGYTNIVSLLIENqckinvqdsenrtplikqavecqqescatvlllhGADPNLVDVYSNTALHYAVCGQNISLA 164
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLEN----------------------------------GADANLQDKNGRTALHLAAKNGHLEIV 46

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 26345898   165 nKLLQYKANLEAKNkDGHTPLLLAVAENNENMVKFLLKKGADVNASD 211
Cdd:pfam12796  47 -KLLLEHADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 50-255 3.82e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 75.10  E-value: 3.82e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345898   50 KLHKAATIGNEQKLKDYLERKKYNVNGRDKRSRTPLHLACANGYTNIVSLLIENQCKINV------------QDS----- 112
Cdd:PHA02876 147 KLIKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIialddlsvlecaVDSknidt 226

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345898  113 -----ENRTPLIKQAVE----CQQESCATVLLLH--GADPNLVDVYSNTALHYAVCGQNIS-LANKLLQYKANLEAKNKD 180
Cdd:PHA02876 227 ikaiiDNRSNINKNDLSllkaIRNEDLETSLLLYdaGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIK 306

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 26345898  181 GHTPLLLaVAEN---NENmVKFLLKKGADVNASDKNHRTAIMIALIVEPTSSVKL-LLQQDTDLAHKDIYGFTAEEYAS 255
Cdd:PHA02876 307 GETPLYL-MAKNgydTEN-IRTLIMLGADVNAADRLYITPLHQASTLDRNKDIVItLLELGANVNARDYCDKTPIHYAA 383
Ank_2 pfam12796
Ankyrin repeats (3 copies);
51-145 7.18e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 68.60  E-value: 7.18e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345898    51 LHKAATIGNEQKLKDYLErKKYNVNGRDKRSRTPLHLACANGYTNIVSLLIENqCKINVQDsENRTPLIkQAVECQQESC 130
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLE-NGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALH-YAARSGHLEI 76

                          90
                  ....*....|....*
gi 26345898   131 ATVLLLHGADPNLVD 145
Cdd:pfam12796  77 VKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
152-244 1.33e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.83  E-value: 1.33e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345898   152 LHYAVCGQNISLANKLLQYKANLEAKNKDGHTPLLLAVAENNENMVKFLLKKgADVNASDkNHRTAIMIALIVEPTSSVK 231
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 26345898   232 LLLQQDTDLAHKD 244
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 66-274 4.05e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 71.98  E-value: 4.05e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345898   66 YLERKKYNVNGRDKRSRTPLH--LACANGYTNIVSLLIENQCKINVQDSENRTPLIKQAVECQ-QESCATVLLLHGADPN 142
Cdd:PHA03095 137 LLLRKGADVNALDLYGMTPLAvlLKSRNANVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKpRARIVRELIRAGCDPA 216

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345898  143 LVDVYSNTALHYAV--CGQNISLANKLLQYKANLEAKNKDGHTPLLLAVAENNENMVKFLLKKGADVNASDKNHRTAIMI 220
Cdd:PHA03095 217 ATDMLGNTPLHSMAtgSSCKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSL 296

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 26345898  221 ALIVEPTSSVKLLLQQDTDLahkdiygftAEEYASFNGFTMYHHITANNENKKK 274
Cdd:PHA03095 297 MVRNNNGRAVRAALAKNPSA---------ETVAATLNTASVAGGDIPSDATRLC 341
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 51-250 4.62e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 71.83  E-value: 4.62e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345898   51 LHKAATIGNEQKLKDYLERKkYNVNGRDKRSRTPLHLACAN------------------GYT-------------NIVSL 99
Cdd:PHA02878  41 LHQAVEARNLDVVKSLLTRG-HNVNQPDHRDLTPLHIICKEpnklgmkemirsinkcsvFYTlvaikdafnnrnvEIFKI 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345898  100 LIENQCKiNVQDSENRTPLIKQAVECQQESCATVLLLHGADPNLVDVYS-NTALHYAVCGQNISLANKLLQYKANLEAKN 178
Cdd:PHA02878 120 ILTNRYK-NIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPD 198

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 26345898  179 KDGHTPLLLAVAENNENMVKFLLKKGADVNASDKNHRTAIMIAL-IVEPTSSVKLLLQQDTDL-AHKDIYGFTA 250
Cdd:PHA02878 199 KTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVgYCKDYDILKLLLEHGVDVnAKSYILGLTA 272
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 51-251 2.19e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 69.63  E-value: 2.19e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345898   51 LHKAATIGNEQKLKDYLERKKYNVNGRDKRSRTPLHLACANGYTNIVSLLIENQCKINVQDSENRTPLiKQAVECQQESC 130
Cdd:PHA02875  72 LHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPL-HLAVMMGDIKG 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345898  131 ATVLLLHGADPNLVDVYSNTALHYAVCGQNISLANKLLQYKANLEAKNKDGHTPLLLAVAENNE-NMVKFLLKKGADVNa 209
Cdd:PHA02875 151 IELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKiDIVRLFIKRGADCN- 229

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 26345898  210 sdknhrtaIMIALIVEPTSSVKLLLQQDTDLAHKDIYGFTAE 251
Cdd:PHA02875 230 --------IMFMIEGEECTILDMICNMCTNLESEAIDALIAD 263
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 72-257 9.10e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 68.17  E-value: 9.10e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345898   72 YNVNGRDKRSRTPLHLAC-ANGYTNIVSLLIENQCKINVQDSENRTPLIKQAVECQQESCATVLLLHGADPNLVDVYSNT 150
Cdd:PHA02876 264 FSVNSIDDCKNTPLHHASqAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYDTENIRTLIMLGADVNAADRLYIT 343

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345898  151 ALHYA-VCGQNISLANKLLQYKANLEAKNKDGHTPLLLAVAENNENMVKFLLKKGADVNASDKNHRTAIMIALI-VEPTS 228
Cdd:PHA02876 344 PLHQAsTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCgTNPYM 423

                        170       180
                 ....*....|....*....|....*....
gi 26345898  229 SVKLLLQQDTDLAHKDIYGFTAEEYASFN 257
Cdd:PHA02876 424 SVKTLIDRGANVNSKNKDLSTPLHYACKK 452
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 94-257 1.32e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 67.38  E-value: 1.32e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345898   94 TNIVSLLIENQCKINVQDSENRTPLIKQAVECQQESCATVLLLHGADPNLVDVYSNTALHYAVCGQNISLANK-----LL 168
Cdd:PHA03100  14 KVKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLTDVKeivklLL 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345898  169 QYKANLEAKNKDGHTPLLLAVAE--NNENMVKFLLKKGADVNASDKNHRTAIMIALI------------------VEPTS 228
Cdd:PHA03100  94 EYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLEsnkidlkilkllidkgvdINAKN 173

                        170       180
                 ....*....|....*....|....*....
gi 26345898  229 SVKLLLQQDTDLAHKDIYGFTAEEYASFN 257
Cdd:PHA03100 174 RVNYLLSYGVPINIKDVYGFTPLHYAVYN 202
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 94-249 1.76e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 66.83  E-value: 1.76e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345898   94 TNIVSLLIENQCKINVQDSENRTPLIKQAVECQQESCATVLLLHGADPNLVDVYSNTALHYAVCGQNISLANKLLQYKAN 173
Cdd:PHA02878 147 AEITKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAS 226

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 26345898  174 LEAKNKDGHTPLLLAVAE-NNENMVKFLLKKGADVNA-SDKNHRTAIMIALIVEptSSVKLLLQQDTDLAHKDIYGFT 249
Cdd:PHA02878 227 TDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAkSYILGLTALHSSIKSE--RKLKLLLEYGADINSLNSYKLT 302
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 39-222 1.54e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 64.13  E-value: 1.54e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345898   39 GGYHLRDKHLKKLHKAATIgnEQKLKDYLERKKYNVNGRDKRS-RTPLHLACANGYTNIVSLLIENQCKINVQDSENRTP 117
Cdd:PHA02878 127 NIQTIDLVYIDKKSKDDII--EAEITKLLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSP 204

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345898  118 LIKqAVECQQESCATVLLLHGADPNLVDVYSNTALHYAVCG-QNISLANKLLQYKANLEAKNK-DGHTPLLLAVaeNNEN 195
Cdd:PHA02878 205 LHH-AVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYiLGLTALHSSI--KSER 281

                        170       180
                 ....*....|....*....|....*..
gi 26345898  196 MVKFLLKKGADVNASDKNHRTAIMIAL 222
Cdd:PHA02878 282 KLKLLLEYGADINSLNSYKLTPLSSAV 308
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 35-189 1.58e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 64.13  E-value: 1.58e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345898   35 LSIGGGYHLRDKHLKK--LHKAATiGNEQKLKDYLERKKYNVNGRDKRSRTPLHLACANGYTNIVSLLIENQCKINVQDS 112
Cdd:PHA02878 154 LSYGADINMKDRHKGNtaLHYATE-NKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDK 232

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 26345898  113 ENRTPLIKQAVECQQESCATVLLLHGADPNLVDVYSN-TALHYAVCGQNISlaNKLLQYKANLEAKNKDGHTPLLLAV 189
Cdd:PHA02878 233 CGNTPLHISVGYCKDYDILKLLLEHGVDVNAKSYILGlTALHSSIKSERKL--KLLLEYGADINSLNSYKLTPLSSAV 308
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 73-239 4.78e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 62.70  E-value: 4.78e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345898   73 NVNGRDKRSrtPLHLACANGYTNIVSLLIENQCKIN-VQDSENRTPLiKQAVECQQESCATVLLLHGADPNLVDVYSNTA 151
Cdd:PHA02875  62 DVKYPDIES--ELHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPL-HLATILKKLDIMKLLIARGADPDIPNTDKFSP 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345898  152 LHYAVCGQNISLANKLLQYKANLEAKNKDGHTPLLLAVAENNENMVKFLLKKGADVNASDKNHRTAIM-IALIVEPTSSV 230
Cdd:PHA02875 139 LHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALcYAIENNKIDIV 218


                 ....*....
gi 26345898  231 KLLLQQDTD 239
Cdd:PHA02875 219 RLFIKRGAD 227
PHA03095 PHA03095
ankyrin-like protein; Provisional
 62-203 5.98e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 62.35  E-value: 5.98e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345898   62 KLKDYLERKKYNVNGRDKRSRTPLHLACAN--GYTNIVSLLIENQCKINVQDSENRTPLIKQAVECqqeSCATV----LL 135
Cdd:PHA03095 168 ELLRLLIDAGADVYAVDDRFRSLLHHHLQSfkPRARIVRELIRAGCDPAATDMLGNTPLHSMATGS---SCKRSlvlpLL 244

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 26345898  136 LHGADPNLVDVYSNTALHYAVCGQNISLANKLLQYKANLEAKNKDGHTPLLLAVAENNENMVKFLLKK 203
Cdd:PHA03095 245 IAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAK 312
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 83-249 8.71e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 61.90  E-value: 8.71e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345898   83 TPLHLACANGYTNIVSLLIENQCKINVQDSENRTPLIKQ----------------------AVECQQESCATVLLLHGAD 140
Cdd:PHA02874  37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAikigahdiikllidngvdtsilPIPCIEKDMIKTILDCGID 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345898  141 PNLVDVYSNTALHYAVCGQNISLANKLLQYKANLEAKNKDGHTPLLLAVAENNENMVKFLLKKGADVNASDKNHRTAIMI 220
Cdd:PHA02874 117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHN 196

                        170       180
                 ....*....|....*....|....*....
gi 26345898  221 ALIVEPTSSVKLLLQQDTDLAHKDIYGFT 249
Cdd:PHA02874 197 AAEYGDYACIKLLIDHGNHIMNKCKNGFT 225
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 88-254 8.64e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 55.77  E-value: 8.64e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345898   88 ACANGYTNIVSLLIENQCKINVQDSENRTPlIKQAVECQQESCATVLLLHGADPNLVDVYSNTALHYAVCGQNISLANKL 167
Cdd:PHA02875   9 AILFGELDIARRLLDIGINPNFEIYDGISP-IKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEEL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345898  168 LQYKANL-EAKNKDGHTPLLLAVAENNENMVKFLLKKGADVNASDKNHRTAIMIALIVEPTSSVKLLLQQDTDLAHKDIY 246
Cdd:PHA02875  88 LDLGKFAdDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCC 167


                 ....*...
gi 26345898  247 GFTAEEYA 254
Cdd:PHA02875 168 GCTPLIIA 175
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 35-222 7.67e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 53.04  E-value: 7.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345898   35 LSIGGGYHLRDKHLKK-LHKAATIGNEQKLKDYLERKKyNVNGRDKRSRTPLHLACANGYTNIVSLLIENQCKINVQDSE 113
Cdd:PHA02874 111 LDCGIDVNIKDAELKTfLHYAIKKGDLESIKMLFEYGA-DVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNN 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345898  114 NRTPLiKQAVECQQESCATVLLLHGADPNLVDVYSNTALHYAVCgQNISlANKLLQYKANLEAKNKDGHTPLLLAVAEN- 192
Cdd:PHA02874 190 GESPL-HNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII-HNRS-AIELLINNASINDQDIDGSTPLHHAINPPc 266

                        170       180       190
                 ....*....|....*....|....*....|
gi 26345898  193 NENMVKFLLKKGADVNASDKNHRTAIMIAL 222
Cdd:PHA02874 267 DIDIIDILLYHKADISIKDNKGENPIDTAF 296
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 131-202 8.66e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.98  E-value: 8.66e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 26345898  131 ATVLLLHGADPNLVDVYSNTALHYAVCGQNISLANKLLQYKANLEAKNKDGHTPLLLAVAENNENMVKFLLK 202
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
Ank_4 pfam13637
Ankyrin repeats (many copies);
181-234 1.09e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.65  E-value: 1.09e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 26345898   181 GHTPLLLAVAENNENMVKFLLKKGADVNASDKNHRTAIMIALIVEPTSSVKLLL 234
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
66-118 1.83e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.96  E-value: 1.83e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 26345898    66 YLERKKYNVNGRDKRSRTPLHLACANGYTNIVSLLIENQCKINVQDSENRTPL 118
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 95-254 6.70e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 49.96  E-value: 6.70e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345898   95 NIVSLLIENQCKINVQDSENRTpLIKQAVECQQESCATVLLLHGADPNLVDVYSNTALHYAVCGQNISLANKLLQYKANL 174
Cdd:PHA02874 105 DMIKTILDCGIDVNIKDAELKT-FLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYA 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345898  175 EAKNKDGHTPLLLAVAENNENMVKFLLKKGADVNASDKNHRTAIMIAlIVEPTSSVKLLLQQDTdLAHKDIYGFTAEEYA 254
Cdd:PHA02874 184 NVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNA-IIHNRSAIELLINNAS-INDQDIDGSTPLHHA 261
Ank_4 pfam13637
Ankyrin repeats (many copies);
149-201 1.48e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.57  E-value: 1.48e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 26345898   149 NTALHYAVCGQNISLANKLLQYKANLEAKNKDGHTPLLLAVAENNENMVKFLL 201
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 131-241 1.59e-06

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 48.86  E-value: 1.59e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345898 131 ATVLLLHGAdPNLV------DVYSN-TALHYAVCGQNISLANKLLQYKANLEA---------KNKD-----GHTPLLLAV 189
Cdd:cd22192  66 AAVVLMEAA-PELVnepmtsDLYQGeTALHIAVVNQNLNLVRELIARGADVVSpratgtffrPGPKnliyyGEHPLSFAA 144

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 26345898 190 AENNENMVKFLLKKGADVNASDKNHRTAIMIaliveptssvkLLLQQDTDLA 241
Cdd:cd22192 145 CVGNEEIVRLLIEHGADIRAQDSLGNTVLHI-----------LVLQPNKTFA 185
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 114-207 2.03e-06

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 48.86  E-value: 2.03e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345898 114 NRTPLIKQAVECQQESCATVLLLHGADPNLVDVYSNTALHYAVCGQNISLANKLLQYKANL--EAKNKD---GHTPLLLA 188
Cdd:cd22192  17 SESPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELvnEPMTSDlyqGETALHIA 96

                        90
                ....*....|....*....
gi 26345898 189 VAENNENMVKFLLKKGADV 207
Cdd:cd22192  97 VVNQNLNLVRELIARGADV 115
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 83-203 2.94e-06

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 48.09  E-value: 2.94e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345898  83 TPLHLACANGYTNIVSLLIENQCkiNVQD--------SENRTPLI-------KQAVECQQESCATVLLLHGADPNLVDVY 147
Cdd:cd22192  91 TALHIAVVNQNLNLVRELIARGA--DVVSpratgtffRPGPKNLIyygehplSFAACVGNEEIVRLLIEHGADIRAQDSL 168

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 26345898 148 SNTALHYAVCGQNISLA----NKLLQYKANLEA------KNKDGHTPLLLAVAENNENMVKFLLKK 203
Cdd:cd22192 169 GNTVLHILVLQPNKTFAcqmyDLILSYDKEDDLqpldlvPNNQGLTPFKLAAKEGNIVMFQHLVQK 234
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 180-212 3.61e-06

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: 42.66  E-value: 3.61e-06
                          10        20        30
                  ....*....|....*....|....*....|....
gi 26345898   180 DGHTPLLLAVAE-NNENMVKFLLKKGADVNASDK 212
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
Ank_4 pfam13637
Ankyrin repeats (many copies);
51-101 6.25e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.65  E-value: 6.25e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 26345898    51 LHKAATIGNEQKLKDYLErKKYNVNGRDKRSRTPLHLACANGYTNIVSLLI 101
Cdd:pfam13637   5 LHAAAASGHLELLRLLLE-KGADINAVDGNGETALHFAASNGNVEVLKLLL 54
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 49-209 6.31e-06

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: 47.38  E-value: 6.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345898    49 KKLHKAATIGNEQKLKDYL-ERKKYNVNGRDKRSRTPL-HLACANGYTNIVSLLIENQCKINVQDSenrtplikqavecq 126
Cdd:TIGR00870  19 KAFLPAAERGDLASVYRDLeEPKKLNINCPDRLGRSALfVAAIENENLELTELLLNLSCRGAVGDT-------------- 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345898   127 qescatvlLLHGADPNLVDVYSNTALH---YAVCGQNISLANKllQYKANLEAknkdGHTPLLLAVAENNENMVKFLLKK 203
Cdd:TIGR00870  85 --------LLHAISLEYVDAVEAILLHllaAFRKSGPLELAND--QYTSEFTP----GITALHLAAHRQNYEIVKLLLER 150


                  ....*.
gi 26345898   204 GADVNA 209
Cdd:TIGR00870 151 GASVPA 156
PHA02798 PHA02798
ankyrin-like protein; Provisional
 73-270 6.60e-06

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 47.14  E-value: 6.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345898   73 NVNGRDKRSRTPLHLACAN-----GYTNIVSLLIENQCKINVQDSENRTPLIKQAVECQQESCATVLLL--HGADPNLVD 145
Cdd:PHA02798  63 NVNGLDNEYSTPLCTILSNikdykHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLFMieNGADTTLLD 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345898  146 VYSNTALHYAV---CGQNISLANKLLQYKANLEA-KNKDGHTPLLLAVAEN----NENMVKFLLKKGADVNASDKNHRTA 217
Cdd:PHA02798 143 KDGFTMLQVYLqsnHHIDIEIIKLLLEKGVDINThNNKEKYDTLHCYFKYNidriDADILKLFVDNGFIINKENKSHKKK 222

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 26345898  218 IMIALIVeptssvkllLQQDTDLAHKDIYGF-----TAEEYASFNGFTMYHHITANNE 270
Cdd:PHA02798 223 FMEYLNS---------LLYDNKRFKKNILDFifsyiDINQVDELGFNPLYYSVSHNNR 271
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 75-137 7.97e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.82  E-value: 7.97e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 26345898   75 NGRDKRSRTPLHLACANGYTNIVSLLIENQCKINVQDSENRTPLiKQAVECQQESCATVLLLH 137
Cdd:PTZ00322 109 NCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPL-ELAEENGFREVVQLLSRH 170
Ank_5 pfam13857
Ankyrin repeats (many copies);
134-188 1.45e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.56  E-value: 1.45e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 26345898   134 LLLHG-ADPNLVDVYSNTALHYAVCGQNISLANKLLQYKANLEAKNKDGHTPLLLA 188
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 180-209 1.64e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.03  E-value: 1.64e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 26345898    180 DGHTPLLLAVAENNENMVKFLLKKGADVNA 209
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
114-168 4.71e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 40.34  E-value: 4.71e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 26345898   114 NRTPLIKQAVECQQESCATvLLLHGADPNLVDVYSNTALHYAVCGQNISLANKLL 168
Cdd:pfam13637   1 ELTALHAAAASGHLELLRL-LLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 180-209 6.63e-05

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: 39.16  E-value: 6.63e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 26345898   180 DGHTPLLLAVAENNENMVKFLLKKGADVNA 209
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 57-242 7.88e-05

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: 43.72  E-value: 7.88e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345898  57 IGNEQKLKDYLERKKYNvngRDKRSRTPLHLACAN---GYTNIVSLLIENQckinvQDSENRTPLIKQAVECQqescatv 133
Cdd:cd21882   5 LGLLECLRWYLTDSAYQ---RGATGKTCLHKAALNlndGVNEAIMLLLEAA-----PDSGNPKELVNAPCTDE------- 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345898 134 lLLHGadpnlvdvysNTALHYAVCGQNISLANKLLQYKANLEAK------NKDGHT-------PLLLAVAENNENMVKFL 200
Cdd:cd21882  70 -FYQG----------QTALHIAIENRNLNLVRLLVENGADVSARatgrffRKSPGNlfyfgelPLSLAACTNQEEIVRLL 138

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 26345898 201 LKKGAD---VNASDKNHRTaIMIALIVEPTSSVK----------LLLQQDTDLAH 242
Cdd:cd21882 139 LENGAQpaaLEAQDSLGNT-VLHALVLQADNTPEnsafvcqmynLLLSYGAHLDP 192
Ank_4 pfam13637
Ankyrin repeats (many copies);
82-135 1.03e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.18  E-value: 1.03e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 26345898    82 RTPLHLACANGYTNIVSLLIENQCKINVQDSENRTPLIKqAVECQQESCATVLL 135
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHF-AASNGNVEVLKLLL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 154-271 1.34e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 42.73  E-value: 1.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345898  154 YAVCGQNISLANKLLQYKANLEA----KNKDGHTPLLLAVAENNENMVKFLLKKGADVNASDKNHRTAIMIALIVEPTSS 229
Cdd:PHA03100   4 YIVLTKSRIIKVKNIKYIIMEDDlndySYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLT 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 26345898  230 -----VKLLLQQDTDLAHKDIYGFTAEEYA---SFNGFTMYHHITANNEN 271
Cdd:PHA03100  84 dvkeiVKLLLEYGANVNAPDNNGITPLLYAiskKSNSYSIVEYLLDNGAN 133
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 82-109 4.46e-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.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 36.85  E-value: 4.46e-04
                          10        20
                  ....*....|....*....|....*...
gi 26345898    82 RTPLHLACANGYTNIVSLLIENQCKINV 109
Cdd:pfam13606   3 NTPLHLAARNGRLEIVKLLLENGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 82-111 5.41e-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: 5.41e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 26345898    82 RTPLHLACA-NGYTNIVSLLIENQCKINVQD 111
Cdd:pfam00023   3 NTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 77-205 5.60e-04

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 39.47  E-value: 5.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345898   77 RDKRSRTPLHLACANGytNIVSLLIENqckiNVQDSENR---TPLIKQAVEC-----------QQESCaTVLLLHGADPN 142
Cdd:PHA02736  13 PDIEGENILHYLCRNG--GVTDLLAFK----NAISDENRylvLEYNRHGKQCvhivsnpdkadPQEKL-KLLMEWGADIN 85

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 26345898  143 LVD-VYSNTALHYAVCGQNISLANKLL-QYKANLEAKNKDGHTPLLLAVAENNENMVKFLLKKGA 205
Cdd:PHA02736  86 GKErVFGNTPLHIAVYTQNYELATWLCnQPGVNMEILNYAFKTPYYVACERHDAKMMNILRAKGA 150
Ank_5 pfam13857
Ankyrin repeats (many copies);
167-221 5.74e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.33  E-value: 5.74e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 26345898   167 LLQYK-ANLEAKNKDGHTPLLLAVAENNENMVKFLLKKGADVNASDKNHRTAIMIA 221
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 82-109 1.19e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.64  E-value: 1.19e-03
                           10        20
                   ....*....|....*....|....*...
gi 26345898     82 RTPLHLACANGYTNIVSLLIENQCKINV 109
Cdd:smart00248   3 RTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 93-196 3.05e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 38.43  E-value: 3.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345898   93 YTNIVSLLIENQCKINVQ--DSENR--TPLIkQAVECQQESCATVLLLHGADpnlVDVYSN----TALHYAVCGQNISLA 164
Cdd:PHA02884  45 YTDIIDAILKLGADPEAPfpLSENSktNPLI-YAIDCDNDDAAKLLIRYGAD---VNRYAEeakiTPLYISVLHGCLKCL 120

                         90       100       110
                 ....*....|....*....|....*....|..
gi 26345898  165 NKLLQYKANLEAKNKDGHTPLLLAVAENNENM 196
Cdd:PHA02884 121 EILLSYGADINIQTNDMVTPIELALMICNNFL 152
PHA02946 PHA02946
ankyin-like protein; Provisional
 108-212 3.81e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 38.50  E-value: 3.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345898  108 NVQDSENRTPLiKQAVECQQESCATVLLLHGADPNLVDVYSNTALHY--AVCGQNISLANKLLQYKANL-EAKNKDGHTP 184
Cdd:PHA02946  66 NETDDDGNYPL-HIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYlsGTDDEVIERINLLVQYGAKInNSVDEEGCGP 144

                         90       100
                 ....*....|....*....|....*...
gi 26345898  185 lLLAVAENNENMVKFLLKKGADVNASDK 212
Cdd:PHA02946 145 -LLACTDPSERVFKKIMSIGFEARIVDK 171
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 140-221 5.39e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 37.96  E-value: 5.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345898  140 DPNLVDVYSNTALHYAVCGQNISlANKLLQYKANLEAKNKDGHTPLLLAVAENNENMVKFLLKKGADVNASDKNHRTAIM 219
Cdd:PTZ00322  75 DPVVAHMLTVELCQLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLE 153


                 ..
gi 26345898  220 IA 221
Cdd:PTZ00322 154 LA 155
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 160-223 8.32e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 37.54  E-value: 8.32e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 26345898  160 NISLANKLLQYKANLEAKNKDGHTPLLLAVAENNENMVKFLLKKGADVNASDKNHRTAIMIALI 223
Cdd:PLN03192 537 NAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAIS 600
PHA02798 PHA02798
ankyrin-like protein; Provisional
 94-249 9.07e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 37.12  E-value: 9.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345898   94 TNIVSLLIENQCKINVQDSENRTPLikqavecqqescATVLllhgadPNLVDVYSntalhyavcgqNISLANKLLQYKAN 173
Cdd:PHA02798  51 TDIVKLFINLGANVNGLDNEYSTPL------------CTIL------SNIKDYKH-----------MLDIVKILIENGAD 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26345898  174 LEAKNKDGHTPLLLAVAE---NNENMVKFLLKKGADVNASDKNHRTAIMIALIVE---PTSSVKLLLQQDTDL-AHKDIY 246
Cdd:PHA02798 102 INKKNSDGETPLYCLLSNgyiNNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNhhiDIEIIKLLLEKGVDInTHNNKE 181


                 ...
gi 26345898  247 GFT 249
Cdd:PHA02798 182 KYD 184
 
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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