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Conserved domains on  [gi|568939838|ref|XP_006505254|]
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ankyrin repeat domain-containing protein 7 isoform X1 [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];
23-201 1.18e-39

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 137.78  E-value: 1.18e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939838  23 GLLTPLHLACANGYTNIVSLLIENQCKINVQDSENRTPLIKqAVECQQESCATVLLLHGADPNLVDVYSNTALHYAVCGQ 102
Cdd:COG0666   86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHL-AAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANG 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939838 103 NISLANKLLQYKANLEAKNKDGHTPLLLAVAENNENMVKFLLKKGADVNASDKNHRTAIMIALIVEPTSSVKLLLQQDTD 182
Cdd:COG0666  165 NLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD 244

                        170
                 ....*....|....*....
gi 568939838 183 LAHKDIYGFTAEEYASFNG 201
Cdd:COG0666  245 LNAKDKDGLTALLLAAAAG 263
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
23-201 1.18e-39

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 137.78  E-value: 1.18e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939838  23 GLLTPLHLACANGYTNIVSLLIENQCKINVQDSENRTPLIKqAVECQQESCATVLLLHGADPNLVDVYSNTALHYAVCGQ 102
Cdd:COG0666   86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHL-AAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANG 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939838 103 NISLANKLLQYKANLEAKNKDGHTPLLLAVAENNENMVKFLLKKGADVNASDKNHRTAIMIALIVEPTSSVKLLLQQDTD 182
Cdd:COG0666  165 NLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD 244

                        170
                 ....*....|....*....
gi 568939838 183 LAHKDIYGFTAEEYASFNG 201
Cdd:COG0666  245 LNAKDKDGLTALLLAAAAG 263
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 25-178 4.79e-19

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 84.72  E-value: 4.79e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939838  25 LTPLHLACANGYT-----NIVSLLIENQCKINVQDSENRTPLIKQAVEC-QQESCATVLLLHGADPNLVDVYSNTALHYA 98
Cdd:PHA03100  69 STPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKKsNSYSIVEYLLDNGANVNIKNSDGENLLHLY 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939838  99 V--CGQNISLANKLLQYKANLEAKN--------------KD--GHTPLLLAVAENNENMVKFLLKKGADVNASDKNHRTA 160
Cdd:PHA03100 149 LesNKIDLKILKLLIDKGVDINAKNrvnyllsygvpiniKDvyGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTP 228

                        170
                 ....*....|....*...
gi 568939838 161 IMIALIVEPTSSVKLLLQ 178
Cdd:PHA03100 229 LHIAILNNNKEIFKLLLN 246
Ank_2 pfam12796
Ankyrin repeats (3 copies);
28-154 5.46e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.83  E-value: 5.46e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939838   28 LHLACANGYTNIVSLLIENqckinvqdsenrtplikqavecqqescatvlllhGADPNLVDVYSNTALHYAVCGQNISLA 107
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLEN----------------------------------GADANLQDKNGRTALHLAAKNGHLEIV 46

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 568939838  108 nKLLQYKANLEAKNkDGHTPLLLAVAENNENMVKFLLKKGADVNASD 154
Cdd:pfam12796  47 -KLLLEHADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 74-184 1.03e-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: 1.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939838  74 ATVLLLHGAdPNLV------DVYSN-TALHYAVCGQNISLANKLLQYKANLEA---------KNKD-----GHTPLLLAV 132
Cdd:cd22192   66 AAVVLMEAA-PELVnepmtsDLYQGeTALHIAVVNQNLNLVRELIARGADVVSpratgtffrPGPKnliyyGEHPLSFAA 144

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568939838 133 AENNENMVKFLLKKGADVNASDKNHRTAIMIaliveptssvkLLLQQDTDLA 184
Cdd:cd22192  145 CVGNEEIVRLLIEHGADIRAQDSLGNTVLHI-----------LVLQPNKTFA 185
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 50-152 6.80e-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: 46.23  E-value: 6.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939838   50 INVQDSENRTPLIKQAVECQQESCATVLLLHGADPNLVDvysnTALHYA----VCGQNISLANKLLQYK-------ANLE 118
Cdd:TIGR00870  45 INCPDRLGRSALFVAAIENENLELTELLLNLSCRGAVGD----TLLHAIsleyVDAVEAILLHLLAAFRksgplelANDQ 120

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 568939838  119 AKNK--DGHTPLLLAVAENNENMVKFLLKKGADVNA 152
Cdd:TIGR00870 121 YTSEftPGITALHLAAHRQNYEIVKLLLERGASVPA 156
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 123-152 1.40e-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: 40.65  E-value: 1.40e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 568939838   123 DGHTPLLLAVAENNENMVKFLLKKGADVNA 152
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
23-201 1.18e-39

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 137.78  E-value: 1.18e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939838  23 GLLTPLHLACANGYTNIVSLLIENQCKINVQDSENRTPLIKqAVECQQESCATVLLLHGADPNLVDVYSNTALHYAVCGQ 102
Cdd:COG0666   86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHL-AAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANG 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939838 103 NISLANKLLQYKANLEAKNKDGHTPLLLAVAENNENMVKFLLKKGADVNASDKNHRTAIMIALIVEPTSSVKLLLQQDTD 182
Cdd:COG0666  165 NLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD 244

                        170
                 ....*....|....*....
gi 568939838 183 LAHKDIYGFTAEEYASFNG 201
Cdd:COG0666  245 LNAKDKDGLTALLLAAAAG 263
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
23-201 3.45e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 120.83  E-value: 3.45e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939838  23 GLLTPLHLACANGYTNIVSLLIENQCKINVQDSENRTPLIkQAVECQQESCATVLLLHGADPNLVDVYSNTALHYAVCGQ 102
Cdd:COG0666   53 LGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLH-AAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNG 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939838 103 NISLANKLLQYKANLEAKNKDGHTPLLLAVAENNENMVKFLLKKGADVNASDKNHRTAIMIALIVEPTSSVKLLLQQDTD 182
Cdd:COG0666  132 NLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGAD 211

                        170
                 ....*....|....*....
gi 568939838 183 LAHKDIYGFTAEEYASFNG 201
Cdd:COG0666  212 VNAKDNDGKTALDLAAENG 230
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
26-193 7.55e-31

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 114.67  E-value: 7.55e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939838  26 TPLHLACANGYTNIVSLLIENQCKINVQDSENRTPLIKqAVECQQESCATVLLLHGADPNLVDVYSNTALHYAVCGQNIS 105
Cdd:COG0666  122 TPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHL-AAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLE 200

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939838 106 LANKLLQYKANLEAKNKDGHTPLLLAVAENNENMVKFLLKKGADVNASDKNHRTAIMIALIVEPTSSVKLLLQQDTDLAH 185
Cdd:COG0666  201 IVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAA 280


                 ....*...
gi 568939838 186 KDIYGFTA 193
Cdd:COG0666  281 ALLDLLTL 288
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
24-201 3.39e-26

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 102.34  E-value: 3.39e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939838  24 LLTPLHLACANGYTNIVSLLIENQCKINVQDSENRTPLIKQAVECQQESCATVLLLHGADPNLVDVYSNTALHYAVCGQN 103
Cdd:COG0666   20 LLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGD 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939838 104 ISLANKLLQYKANLEAKNKDGHTPLLLAVAENNENMVKFLLKKGADVNASDKNHRTAIMIALIVEPTSSVKLLLQQDTDL 183
Cdd:COG0666  100 LEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADV 179

                        170
                 ....*....|....*...
gi 568939838 184 AHKDIYGFTAEEYASFNG 201
Cdd:COG0666  180 NARDNDGETPLHLAAENG 197
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
26-161 5.83e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 91.17  E-value: 5.83e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939838  26 TPLHLACANGYTNIVSLLIENQCKINVQDSENRTPLIkQAVECQQESCATVLLLHGADPNLVDVYSNTALHYAVCGQNIS 105
Cdd:COG0666  155 TPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLH-LAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLE 233

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568939838 106 LANKLLQYKANLEAKNKDGHTPLLLAVAENNENMVKFLLKKGADVNASDKNHRTAI 161
Cdd:COG0666  234 IVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 25-178 4.79e-19

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 84.72  E-value: 4.79e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939838  25 LTPLHLACANGYT-----NIVSLLIENQCKINVQDSENRTPLIKQAVEC-QQESCATVLLLHGADPNLVDVYSNTALHYA 98
Cdd:PHA03100  69 STPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKKsNSYSIVEYLLDNGANVNIKNSDGENLLHLY 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939838  99 V--CGQNISLANKLLQYKANLEAKN--------------KD--GHTPLLLAVAENNENMVKFLLKKGADVNASDKNHRTA 160
Cdd:PHA03100 149 LesNKIDLKILKLLIDKGVDINAKNrvnyllsygvpiniKDvyGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTP 228

                        170
                 ....*....|....*...
gi 568939838 161 IMIALIVEPTSSVKLLLQ 178
Cdd:PHA03100 229 LHIAILNNNKEIFKLLLN 246
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
39-201 3.53e-18

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 80.77  E-value: 3.53e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939838  39 IVSLLIENQCKINVQDSENRTPLIKQAVECQQESCATVLLLHGADPNLVDVYSNTALHYAVCGQNISLANKLLQYKANLE 118
Cdd:COG0666    2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939838 119 AKNKDGHTPLLLAVAENNENMVKFLLKKGADVNASDKNHRTAIMIALIVEPTSSVKLLLQQDTDLAHKDIYGFTAEEYAS 198
Cdd:COG0666   82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161


                 ...
gi 568939838 199 FNG 201
Cdd:COG0666  162 ANG 164
PHA03095 PHA03095
ankyrin-like protein; Provisional
 30-193 4.17e-17

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 79.30  E-value: 4.17e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939838  30 LACANGYTNIVSLLIENQCKINVQDSENRTPLiKQAVECQQESCATV---LLLHGADPNLVDVYSNTALHYAVCGQN-IS 105
Cdd:PHA03095  20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPL-HLYLHYSSEKVKDIvrlLLEAGADVNAPERCGFTPLHLYLYNATtLD 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939838 106 LANKLLQYKANLEAKNKDGHTPL--LLAVAENNENMVKFLLKKGADVNASDKNHRTAIMIALI---VEPtSSVKLLLQQD 180
Cdd:PHA03095  99 VIKLLIKAGADVNAKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKsrnANV-ELLRLLIDAG 177

                        170
                 ....*....|...
gi 568939838 181 TDLAHKDIYGFTA 193
Cdd:PHA03095 178 ADVYAVDDRFRSL 190
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 25-166 1.13e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 77.78  E-value: 1.13e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939838  25 LTPLHLACAN--GYTNIVSLLIENQCKINVQDSENRTPLiKQAVECQQESCATV------------------LLLHGADP 84
Cdd:PHA03100 107 ITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLL-HLYLESNKIDLKILkllidkgvdinaknrvnyLLSYGVPI 185

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939838  85 NLVDVYSNTALHYAVCGQNISLANKLLQYKANLEAKNKDGHTPLLLAVAENNENMVKFLLKKGADVNA--------SDKN 156
Cdd:PHA03100 186 NIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTiietllyfKDKD 265

                        170
                 ....*....|
gi 568939838 157 HRTAIMIALI 166
Cdd:PHA03100 266 LNTITKIKML 275
Ank_2 pfam12796
Ankyrin repeats (3 copies);
28-154 5.46e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.83  E-value: 5.46e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939838   28 LHLACANGYTNIVSLLIENqckinvqdsenrtplikqavecqqescatvlllhGADPNLVDVYSNTALHYAVCGQNISLA 107
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLEN----------------------------------GADANLQDKNGRTALHLAAKNGHLEIV 46

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 568939838  108 nKLLQYKANLEAKNkDGHTPLLLAVAENNENMVKFLLKKGADVNASD 154
Cdd:pfam12796  47 -KLLLEHADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
95-187 2.02e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 66.29  E-value: 2.02e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939838   95 LHYAVCGQNISLANKLLQYKANLEAKNKDGHTPLLLAVAENNENMVKFLLKKgADVNASDkNHRTAIMIALIVEPTSSVK 174
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 568939838  175 LLLQQDTDLAHKD 187
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 26-183 4.27e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 70.48  E-value: 4.27e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939838  26 TPLHLACA-NGYTNIVSLLIENQCKINVQDSENRTPLIKQAVEcQQESCATVLLLHGADPNLVDVYSNTALHYAVCGQNI 104
Cdd:PHA02876 343 TPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVR-NNVVIINTLLDYGADIEALSQKIGTALHFALCGTNP 421

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939838 105 SLANK-LLQYKANLEAKNKDGHTPLLLAVAENNE-NMVKFLLKKGADVNASDKNHRTAIMIALivEPTSSVKLLLQQDTD 182
Cdd:PHA02876 422 YMSVKtLIDRGANVNSKNKDLSTPLHYACKKNCKlDVIEMLLDNGADVNAINIQNQYPLLIAL--EYHGIVNILLHYGAE 499


                 .
gi 568939838 183 L 183
Cdd:PHA02876 500 L 500
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 37-200 7.18e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 69.69  E-value: 7.18e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939838  37 TNIVSLLIENQCKINVQDSENRTPLIKQAVECQQESCATVLLLHGADPNLVDVYSNTALHYAVCGQNISLANK-----LL 111
Cdd:PHA03100  14 KVKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLTDVKeivklLL 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939838 112 QYKANLEAKNKDGHTPLLLAVAE--NNENMVKFLLKKGADVNASDKNHRTAIMIALI------------------VEPTS 171
Cdd:PHA03100  94 EYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLEsnkidlkilkllidkgvdINAKN 173

                        170       180
                 ....*....|....*....|....*....
gi 568939838 172 SVKLLLQQDTDLAHKDIYGFTAEEYASFN 200
Cdd:PHA03100 174 RVNYLLSYGVPINIKDVYGFTPLHYAVYN 202
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 26-164 1.29e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 69.32  E-value: 1.29e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939838  26 TPLHLACANGY-TNIVSLLIENQCKINVQDSENRTPLIKQAVECQQESCATVLLLHGADPNLVDVYSNTALHYAVCGQNI 104
Cdd:PHA02876 309 TPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNV 388

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568939838 105 SLANKLLQYKANLEAKNKDGHTPLLLAVAENNENM-VKFLLKKGADVNASDKNHRTAIMIA 164
Cdd:PHA02876 389 VIINTLLDYGADIEALSQKIGTALHFALCGTNPYMsVKTLIDRGANVNSKNKDLSTPLHYA 449
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 37-192 2.21e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 68.37  E-value: 2.21e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939838  37 TNIVSLLIENQCKINVQDSENRTPLIKQAVECQQESCATVLLLHGADPNLVDVYSNTALHYAVCGQNISLANKLLQYKAN 116
Cdd:PHA02878 147 AEITKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAS 226

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568939838 117 LEAKNKDGHTPLLLAVAE-NNENMVKFLLKKGADVNA-SDKNHRTAIMIALIVEptSSVKLLLQQDTDLAHKDIYGFT 192
Cdd:PHA02878 227 TDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAkSYILGLTALHSSIKSE--RKLKLLLEYGADINSLNSYKLT 302
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 51-195 2.65e-13

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 68.36  E-value: 2.65e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939838  51 NVQDSENRTPLiKQAVECQQESCATVLLLHGADPNLVDVYSNTALHYAVCGQNISLANKLLQYkanleAKNKDGHTP--- 127
Cdd:PLN03192 552 DIGDSKGRTPL-HIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHF-----ASISDPHAAgdl 625

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568939838 128 LLLAVAENNENMVKFLLKKGADVNASDKNHRTAIMIALIVEPTSSVKLLLQQDTDLAHKDIY-GFTAEE 195
Cdd:PLN03192 626 LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDdDFSPTE 694
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 26-154 1.50e-12

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 66.04  E-value: 1.50e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939838  26 TPLHLACANGYTNIVSLLIENQCKINVQDSENRTPLIkQAVECQQESCATVL--LLHGADPNLvdvySNTALHYAVCGQN 103
Cdd:PLN03192 560 TPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALW-NAISAKHHKIFRILyhFASISDPHA----AGDLLCTAAKRND 634

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568939838 104 ISLANKLLQYKANLEAKNKDGHTPLLLAVAENNENMVKFLLKKGADVNASD 154
Cdd:PLN03192 635 LTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAN 685
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 25-198 4.14e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 64.70  E-value: 4.14e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939838  25 LTPLHLACANGYTNIVSLLIENQCKINvqdsENRTPLIKQaveCQQESCATVLLLH--GADPNLVDVYSNTALHYAVCGQ 102
Cdd:PHA02876 212 LSVLECAVDSKNIDTIKAIIDNRSNIN----KNDLSLLKA---IRNEDLETSLLLYdaGFSVNSIDDCKNTPLHHASQAP 284

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939838 103 NIS-LANKLLQYKANLEAKNKDGHTPLLLaVAEN---NENmVKFLLKKGADVNASDKNHRTAIMIALIVEPTSSVKL-LL 177
Cdd:PHA02876 285 SLSrLVPKLLERGADVNAKNIKGETPLYL-MAKNgydTEN-IRTLIMLGADVNAADRLYITPLHQASTLDRNKDIVItLL 362

                        170       180
                 ....*....|....*....|.
gi 568939838 178 QQDTDLAHKDIYGFTAEEYAS 198
Cdd:PHA02876 363 ELGANVNARDYCDKTPIHYAA 383
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 26-165 5.96e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 64.13  E-value: 5.96e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939838  26 TPLHLACANGYTNIVSLLIENQCKINVQDSENRTPLIKqAVECQQESCATVLLLHGADPNLVDVYSNTALHYAVCG-QNI 104
Cdd:PHA02878 170 TALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHH-AVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDY 248

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568939838 105 SLANKLLQYKANLEAKNK-DGHTPLLLAVaeNNENMVKFLLKKGADVNASDKNHRTAIMIAL 165
Cdd:PHA02878 249 DILKLLLEHGVDVNAKSYiLGLTALHSSI--KSERKLKLLLEYGADINSLNSYKLTPLSSAV 308
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 26-200 6.04e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 64.31  E-value: 6.04e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939838  26 TPLHLAC-ANGYTNIVSLLIENQCKINVQDSENRTPLIKQAVECQQESCATVLLLHGADPNLVDVYSNTALHYA-VCGQN 103
Cdd:PHA02876 275 TPLHHASqAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYDTENIRTLIMLGADVNAADRLYITPLHQAsTLDRN 354

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939838 104 ISLANKLLQYKANLEAKNKDGHTPLLLAVAENNENMVKFLLKKGADVNASDKNHRTAIMIALI-VEPTSSVKLLLQQDTD 182
Cdd:PHA02876 355 KDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCgTNPYMSVKTLIDRGAN 434

                        170
                 ....*....|....*...
gi 568939838 183 LAHKDIYGFTAEEYASFN 200
Cdd:PHA02876 435 VNSKNKDLSTPLHYACKK 452
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 25-194 1.68e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 62.70  E-value: 1.68e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939838  25 LTPLHLACANGYTNIVSLLIENQCKINVQDSENRTPLiKQAVECQQESCATVLLLHGADPNLVDVYSNTALHYAVCGQNI 104
Cdd:PHA02875 103 MTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPL-HLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDI 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939838 105 SLANKLLQYKANLEAKNKDGHTPLLLAVAENNE-NMVKFLLKKGADVNasdknhrtaIMIALIVEPTSSVKLLLQQDTDL 183
Cdd:PHA02875 182 AICKMLLDSGANIDYFGKNGCVAALCYAIENNKiDIVRLFIKRGADCN---------IMFMIEGEECTILDMICNMCTNL 252

                        170
                 ....*....|.
gi 568939838 184 AHKDIYGFTAE 194
Cdd:PHA02875 253 ESEAIDALIAD 263
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 26-192 1.69e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 62.67  E-value: 1.69e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939838  26 TPLHLACANGYTNIVSLLIENQCKINVQDSENRTPLIKQ----------------------AVECQQESCATVLLLHGAD 83
Cdd:PHA02874  37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAikigahdiikllidngvdtsilPIPCIEKDMIKTILDCGID 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939838  84 PNLVDVYSNTALHYAVCGQNISLANKLLQYKANLEAKNKDGHTPLLLAVAENNENMVKFLLKKGADVNASDKNHRTAIMI 163
Cdd:PHA02874 117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHN 196

                        170       180
                 ....*....|....*....|....*....
gi 568939838 164 ALIVEPTSSVKLLLQQDTDLAHKDIYGFT 192
Cdd:PHA02874 197 AAEYGDYACIKLLIDHGNHIMNKCKNGFT 225
PHA03095 PHA03095
ankyrin-like protein; Provisional
 25-217 2.66e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 62.35  E-value: 2.66e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939838  25 LTPLH--LACANGYTNIVSLLIENQCKINVQDSENRTPLIKQAVECQ-QESCATVLLLHGADPNLVDVYSNTALHYAV-- 99
Cdd:PHA03095 153 MTPLAvlLKSRNANVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKpRARIVRELIRAGCDPAATDMLGNTPLHSMAtg 232

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939838 100 CGQNISLANKLLQYKANLEAKNKDGHTPLLLAVAENNENMVKFLLKKGADVNASDKNHRTAIMIALIVEPTSSVKLLLQQ 179
Cdd:PHA03095 233 SSCKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAK 312

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 568939838 180 DTDLahkdiygftAEEYASFNGFTMYHHITANNENKKK 217
Cdd:PHA03095 313 NPSA---------ETVAATLNTASVAGGDIPSDATRLC 341
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 23-182 3.66e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 61.93  E-value: 3.66e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939838  23 GLLTPLHLACANGYTNIVSLLIENQCKIN-VQDSENRTPLiKQAVECQQESCATVLLLHGADPNLVDVYSNTALHYAVCG 101
Cdd:PHA02875  67 DIESELHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPL-HLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMM 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939838 102 QNISLANKLLQYKANLEAKNKDGHTPLLLAVAENNENMVKFLLKKGADVNASDKNHRTAIM-IALIVEPTSSVKLLLQQD 180
Cdd:PHA02875 146 GDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALcYAIENNKIDIVRLFIKRG 225


                 ..
gi 568939838 181 TD 182
Cdd:PHA02875 226 AD 227
Ank_2 pfam12796
Ankyrin repeats (3 copies);
25-88 2.77e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 55.12  E-value: 2.77e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568939838   25 LTPLHLACANGYTNIVSLLIENqCKINVQDsENRTPLIkQAVECQQESCATVLLLHGADPNLVD 88
Cdd:pfam12796  31 RTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALH-YAARSGHLEIVKLLLEKGADINVKD 91
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 31-197 3.08e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 56.15  E-value: 3.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939838  31 ACANGYTNIVSLLIENQCKINVQDSENRTPlIKQAVECQQESCATVLLLHGADPNLVDVYSNTALHYAVCGQNISLANKL 110
Cdd:PHA02875   9 AILFGELDIARRLLDIGINPNFEIYDGISP-IKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEEL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939838 111 LQYKANL-EAKNKDGHTPLLLAVAENNENMVKFLLKKGADVNASDKNHRTAIMIALIVEPTSSVKLLLQQDTDLAHKDIY 189
Cdd:PHA02875  88 LDLGKFAdDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCC 167


                 ....*...
gi 568939838 190 GFTAEEYA 197
Cdd:PHA02875 168 GCTPLIIA 175
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 61-161 1.38e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 54.30  E-value: 1.38e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939838  61 LIKQAVECQQESCATVLLLHGADPNLVDVYSNTALHYAVCGQNISLANKLLQYKANLEAKNKDGHTPLLLAVAENNENMV 140
Cdd:PHA02876 148 LIKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTI 227

                         90       100
                 ....*....|....*....|.
gi 568939838 141 KFLLKKGADVNASDKNHRTAI 161
Cdd:PHA02876 228 KAIIDNRSNINKNDLSLLKAI 248
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 74-145 3.71e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.98  E-value: 3.71e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568939838  74 ATVLLLHGADPNLVDVYSNTALHYAVCGQNISLANKLLQYKANLEAKNKDGHTPLLLAVAENNENMVKFLLK 145
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
Ank_4 pfam13637
Ankyrin repeats (many copies);
124-177 1.39e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.88  E-value: 1.39e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568939838  124 GHTPLLLAVAENNENMVKFLLKKGADVNASDKNHRTAIMIALIVEPTSSVKLLL 177
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 38-197 1.90e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 50.73  E-value: 1.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939838  38 NIVSLLIENQCKINVQDSENRTpLIKQAVECQQESCATVLLLHGADPNLVDVYSNTALHYAVCGQNISLANKLLQYKANL 117
Cdd:PHA02874 105 DMIKTILDCGIDVNIKDAELKT-FLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYA 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939838 118 EAKNKDGHTPLLLAVAENNENMVKFLLKKGADVNASDKNHRTAIMIAlIVEPTSSVKLLLQQDTdLAHKDIYGFTAEEYA 197
Cdd:PHA02874 184 NVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNA-IIHNRSAIELLINNAS-INDQDIDGSTPLHHA 261
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 31-198 4.43e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 49.88  E-value: 4.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939838  31 ACANGYTNIVSLLIENQCKiNVQDSENRTPLIKQAVECQQESCATVLLLHGADPNLVDVYS-NTALHYAVCGQNISLANK 109
Cdd:PHA02878 108 AFNNRNVEIFKIILTNRYK-NIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDRHKgNTALHYATENKDQRLTEL 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939838 110 LLQYKANLEAKNKDGHTPLLLAVAENNENMVKFLLKKGADVNasdknhrtaimialiveptssvklllqqdtdlaHKDIY 189
Cdd:PHA02878 187 LLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTD---------------------------------ARDKC 233


                 ....*....
gi 568939838 190 GFTAEEYAS 198
Cdd:PHA02878 234 GNTPLHISV 242
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 74-184 1.03e-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: 1.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939838  74 ATVLLLHGAdPNLV------DVYSN-TALHYAVCGQNISLANKLLQYKANLEA---------KNKD-----GHTPLLLAV 132
Cdd:cd22192   66 AAVVLMEAA-PELVnepmtsDLYQGeTALHIAVVNQNLNLVRELIARGADVVSpratgtffrPGPKnliyyGEHPLSFAA 144

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568939838 133 AENNENMVKFLLKKGADVNASDKNHRTAIMIaliveptssvkLLLQQDTDLA 184
Cdd:cd22192  145 CVGNEEIVRLLIEHGADIRAQDSLGNTVLHI-----------LVLQPNKTFA 185
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 26-146 1.18e-06

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 48.72  E-value: 1.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939838  26 TPLHLACANGYTNIVSLLIENQCKINVQ---DSENRTPL---------IKQAVECQQESCATVLLLHGADP---NLVDVY 90
Cdd:cd21882   75 TALHIAIENRNLNLVRLLVENGADVSARatgRFFRKSPGnlfyfgelpLSLAACTNQEEIVRLLLENGAQPaalEAQDSL 154

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568939838  91 SNTALHYAVCGQN---------ISLANKLLQYKANL-------EAKNKDGHTPLLLAVAENNENMVKFLLKK 146
Cdd:cd21882  155 GNTVLHALVLQADntpensafvCQMYNLLLSYGAHLdptqqleEIPNHQGLTPLKLAAVEGKIVMFQHILQR 226
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 57-150 1.19e-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: 48.47  E-value: 1.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939838  57 NRTPLIKQAVECQQESCATVLLLHGADPNLVDVYSNTALHYAVCGQNISLANKLLQYKANL--EAKNKD---GHTPLLLA 131
Cdd:cd22192   17 SESPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELvnEPMTSDlyqGETALHIA 96

                         90
                 ....*....|....*....
gi 568939838 132 VAENNENMVKFLLKKGADV 150
Cdd:cd22192   97 VVNQNLNLVRELIARGADV 115
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 26-146 1.82e-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: 1.82e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939838  26 TPLHLACANGYTNIVSLLIENQCkiNVQD--------SENRTPLI-------KQAVECQQESCATVLLLHGADPNLVDVY 90
Cdd:cd22192   91 TALHIAVVNQNLNLVRELIARGA--DVVSpratgtffRPGPKNLIyygehplSFAACVGNEEIVRLLIEHGADIRAQDSL 168

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568939838  91 SNTALHYAVCGQNISLA----NKLLQYKANLEA------KNKDGHTPLLLAVAENNENMVKFLLKK 146
Cdd:cd22192  169 GNTVLHILVLQPNKTFAcqmyDLILSYDKEDDLqpldlvPNNQGLTPFKLAAKEGNIVMFQHLVQK 234
Ank_4 pfam13637
Ankyrin repeats (many copies);
92-144 1.88e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.80  E-value: 1.88e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568939838   92 NTALHYAVCGQNISLANKLLQYKANLEAKNKDGHTPLLLAVAENNENMVKFLL 144
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 123-155 4.06e-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: 42.28  E-value: 4.06e-06
                          10        20        30
                  ....*....|....*....|....*....|....
gi 568939838  123 DGHTPLLLAVAE-NNENMVKFLLKKGADVNASDK 155
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 50-152 6.80e-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: 46.23  E-value: 6.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939838   50 INVQDSENRTPLIKQAVECQQESCATVLLLHGADPNLVDvysnTALHYA----VCGQNISLANKLLQYK-------ANLE 118
Cdd:TIGR00870  45 INCPDRLGRSALFVAAIENENLELTELLLNLSCRGAVGD----TLLHAIsleyVDAVEAILLHLLAAFRksgplelANDQ 120

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 568939838  119 AKNK--DGHTPLLLAVAENNENMVKFLLKKGADVNA 152
Cdd:TIGR00870 121 YTSEftPGITALHLAAHRQNYEIVKLLLERGASVPA 156
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 123-152 1.40e-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: 40.65  E-value: 1.40e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 568939838   123 DGHTPLLLAVAENNENMVKFLLKKGADVNA 152
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
77-131 2.21e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.79  E-value: 2.21e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568939838   77 LLLHG-ADPNLVDVYSNTALHYAVCGQNISLANKLLQYKANLEAKNKDGHTPLLLA 131
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 97-214 2.36e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 44.27  E-value: 2.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939838  97 YAVCGQNISLANKLLQYKANLEA----KNKDGHTPLLLAVAENNENMVKFLLKKGADVNASDKNHRTAIMIALIVEPTSS 172
Cdd:PHA03100   4 YIVLTKSRIIKVKNIKYIIMEDDlndySYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLT 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 568939838 173 -----VKLLLQQDTDLAHKDIYGFTAEEYA---SFNGFTMYHHITANNEN 214
Cdd:PHA03100  84 dvkeiVKLLLEYGANVNAPDNNGITPLLYAiskKSNSYSIVEYLLDNGAN 133
Ank_4 pfam13637
Ankyrin repeats (many copies);
57-111 6.41e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.57  E-value: 6.41e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568939838   57 NRTPLIKQAVECQQESCATvLLLHGADPNLVDVYSNTALHYAVCGQNISLANKLL 111
Cdd:pfam13637   1 ELTALHAAAASGHLELLRL-LLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02798 PHA02798
ankyrin-like protein; Provisional
 38-213 7.72e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 42.90  E-value: 7.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939838  38 NIVSLLIENQCKINVQDSENRTPLIKQAVECQQESCATVLLL--HGADPNLVDVYSNTALHYAV---CGQNISLANKLLQ 112
Cdd:PHA02798  90 DIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLFMieNGADTTLLDKDGFTMLQVYLqsnHHIDIEIIKLLLE 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939838 113 YKANLEA-KNKDGHTPLLLAVAEN----NENMVKFLLKKGADVNASDKNHRTAIMIALIVeptssvkllLQQDTDLAHKD 187
Cdd:PHA02798 170 KGVDINThNNKEKYDTLHCYFKYNidriDADILKLFVDNGFIINKENKSHKKKFMEYLNS---------LLYDNKRFKKN 240

                        170       180       190
                 ....*....|....*....|....*....|.
gi 568939838 188 IYGF-----TAEEYASFNGFTMYHHITANNE 213
Cdd:PHA02798 241 ILDFifsyiDINQVDELGFNPLYYSVSHNNR 271
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 123-152 7.72e-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: 38.78  E-value: 7.72e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 568939838  123 DGHTPLLLAVAENNENMVKFLLKKGADVNA 152
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 58-185 9.96e-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: 42.56  E-value: 9.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939838  58 RTPLIKQAVECQQESCATVLLLHGADPNLVDVY-------------SNTALHYAVCGQNISLANKLLQYKANLEAK---- 120
Cdd:cd21882   27 KTCLHKAALNLNDGVNEAIMLLLEAAPDSGNPKelvnapctdefyqGQTALHIAIENRNLNLVRLLVENGADVSARatgr 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939838 121 --NKDGHT-------PLLLAVAENNENMVKFLLKKGAD---VNASDKNHRTaIMIALIVEPTSSVK----------LLLQ 178
Cdd:cd21882  107 ffRKSPGNlfyfgelPLSLAACTNQEEIVRLLLENGAQpaaLEAQDSLGNT-VLHALVLQADNTPEnsafvcqmynLLLS 185


                 ....*..
gi 568939838 179 QDTDLAH 185
Cdd:cd21882  186 YGAHLDP 192
Ank_5 pfam13857
Ankyrin repeats (many copies);
26-61 9.99e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.87  E-value: 9.99e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 568939838   26 TPLHLACANGYTNIVSLLIENQCKINVQDSENRTPL 61
Cdd:pfam13857  18 TPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 26-162 1.32e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 42.26  E-value: 1.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939838  26 TPLHLACANGYTNIVSLLIENQCKINVQDSENRTPLIKQAVecqQESCATVLLLHGADPNLVDVYSNTALHYAV---Cgq 102
Cdd:PHA02874 192 SPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII---HNRSAIELLINNASINDQDIDGSTPLHHAInppC-- 266

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568939838 103 NISLANKLLQYKANLEAKNKDGHTPLLLAVAE-NNENMVKFLLKKGADVNASDKNHRTAIM 162
Cdd:PHA02874 267 DIDIIDILLYHKADISIKDNKGENPIDTAFKYiNKDPVIKDIIANAVLIKEADKLKDSDFL 327
Ank_4 pfam13637
Ankyrin repeats (many copies);
25-78 1.79e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.41  E-value: 1.79e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568939838   25 LTPLHLACANGYTNIVSLLIENQCKINVQDSENRTPLIKqAVECQQESCATVLL 78
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHF-AASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 26-80 6.00e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 40.27  E-value: 6.00e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568939838  26 TPLHLACANGYTNIVSLLIENQCKINVQDSENRTPLiKQAVECQQESCATVLLLH 80
Cdd:PTZ00322 117 TPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPL-ELAEENGFREVVQLLSRH 170
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 28-148 8.24e-04

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 38.70  E-value: 8.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939838  28 LHLACANGytNIVSLLIENqckiNVQDSENR---TPLIKQAVEC-----------QQESCaTVLLLHGADPNLVD-VYSN 92
Cdd:PHA02736  21 LHYLCRNG--GVTDLLAFK----NAISDENRylvLEYNRHGKQCvhivsnpdkadPQEKL-KLLMEWGADINGKErVFGN 93

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568939838  93 TALHYAVCGQNISLANKLL-QYKANLEAKNKDGHTPLLLAVAENNENMVKFLLKKGA 148
Cdd:PHA02736  94 TPLHIAVYTQNYELATWLCnQPGVNMEILNYAFKTPYYVACERHDAKMMNILRAKGA 150
Ank_5 pfam13857
Ankyrin repeats (many copies);
110-164 9.00e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.17  E-value: 9.00e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568939838  110 LLQYK-ANLEAKNKDGHTPLLLAVAENNENMVKFLLKKGADVNASDKNHRTAIMIA 164
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 26-54 1.28e-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: 1.28e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 568939838   26 TPLHLACA-NGYTNIVSLLIENQCKINVQD 54
Cdd:pfam00023   4 TPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 26-52 1.30e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 35.31  E-value: 1.30e-03
                          10        20
                  ....*....|....*....|....*..
gi 568939838   26 TPLHLACANGYTNIVSLLIENQCKINV 52
Cdd:pfam13606   4 TPLHLAARNGRLEIVKLLLENGADINA 30
PHA02946 PHA02946
ankyin-like protein; Provisional
 51-155 1.39e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 39.27  E-value: 1.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939838  51 NVQDSENRTPLiKQAVECQQESCATVLLLHGADPNLVDVYSNTALHY--AVCGQNISLANKLLQYKANL-EAKNKDGHTP 127
Cdd:PHA02946  66 NETDDDGNYPL-HIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYlsGTDDEVIERINLLVQYGAKInNSVDEEGCGP 144

                         90       100
                 ....*....|....*....|....*...
gi 568939838 128 lLLAVAENNENMVKFLLKKGADVNASDK 155
Cdd:PHA02946 145 -LLACTDPSERVFKKIMSIGFEARIVDK 171
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 36-139 1.98e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 38.43  E-value: 1.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939838  36 YTNIVSLLIENQCKINVQ--DSENR--TPLIkQAVECQQESCATVLLLHGADpnlVDVYSN----TALHYAVCGQNISLA 107
Cdd:PHA02884  45 YTDIIDAILKLGADPEAPfpLSENSktNPLI-YAIDCDNDDAAKLLIRYGAD---VNRYAEeakiTPLYISVLHGCLKCL 120

                         90       100       110
                 ....*....|....*....|....*....|..
gi 568939838 108 NKLLQYKANLEAKNKDGHTPLLLAVAENNENM 139
Cdd:PHA02884 121 EILLSYGADINIQTNDMVTPIELALMICNNFL 152
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 26-52 2.26e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.49  E-value: 2.26e-03
                           10        20
                   ....*....|....*....|....*..
gi 568939838    26 TPLHLACANGYTNIVSLLIENQCKINV 52
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02798 PHA02798
ankyrin-like protein; Provisional
 37-192 2.85e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 38.28  E-value: 2.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939838  37 TNIVSLLIENQCKINVQDSENRTPLikqavecqqescATVLllhgadPNLVDVysNTALhyavcgqNISLAnkLLQYKAN 116
Cdd:PHA02798  51 TDIVKLFINLGANVNGLDNEYSTPL------------CTIL------SNIKDY--KHML-------DIVKI--LIENGAD 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939838 117 LEAKNKDGHTPLLLAVAE---NNENMVKFLLKKGADVNASDKNHRTAIMIALIVE---PTSSVKLLLQQDTDL-AHKDIY 189
Cdd:PHA02798 102 INKKNSDGETPLYCLLSNgyiNNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNhhiDIEIIKLLLEKGVDInTHNNKE 181


                 ...
gi 568939838 190 GFT 192
Cdd:PHA02798 182 KYD 184
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 83-164 3.21e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 38.34  E-value: 3.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939838  83 DPNLVDVYSNTALHYAVCGQNISlANKLLQYKANLEAKNKDGHTPLLLAVAENNENMVKFLLKKGADVNASDKNHRTAIM 162
Cdd:PTZ00322  75 DPVVAHMLTVELCQLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLE 153


                 ..
gi 568939838 163 IA 164
Cdd:PTZ00322 154 LA 155
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 26-144 3.27e-03

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 38.14  E-value: 3.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939838   26 TPLHLACANGYTNIVSLLIENQCKINV------------QDS--ENRTPLikQAVEC-QQESCATVLLLHGADPNLVDVY 90
Cdd:TIGR00870 130 TALHLAAHRQNYEIVKLLLERGASVPAracgdffvksqgVDSfyHGESPL--NAAAClGSPSIVALLSEDPADILTADSL 207

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939838   91 SNTALHYAV-----CGQNISLA----NKLLQYKA------NLEA-KNKDGHTPLLLAVAENNENMVKFLL 144
Cdd:TIGR00870 208 GNTLLHLLVmenefKAEYEELScqmyNFALSLLDklrdskELEViLNHQGLTPLKLAAKEGRIVLFRLKL 277
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 103-166 5.07e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 37.54  E-value: 5.07e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568939838 103 NISLANKLLQYKANLEAKNKDGHTPLLLAVAENNENMVKFLLKKGADVNASDKNHRTAIMIALI 166
Cdd:PLN03192 537 NAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAIS 600
PHA02946 PHA02946
ankyin-like protein; Provisional
 92-161 5.90e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 37.34  E-value: 5.90e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568939838  92 NTALHYAVCG---QNISLANKLLQYKANLEAKNKDGHTPLLLAVAENNENMVKFLLKKGADVNASDKNHRTAI 161
Cdd:PHA02946  37 NYHILHAYCGikgLDERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPL 109
Ank_5 pfam13857
Ankyrin repeats (many copies);
43-98 5.92e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 34.24  E-value: 5.92e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568939838   43 LIEN-QCKINVQDSENRTPLIKqAVECQQESCATVLLLHGADPNLVDVYSNTALHYA 98
Cdd:pfam13857   1 LLEHgPIDLNRLDGEGYTPLHV-AAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 93-154 7.97e-03

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


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 37.09  E-value: 7.97e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568939838  93 TALHYAVCGQNISLANKLLQYKANLEA--------KNKD------GHTPLLLAVAENNENMVKFLLK---KGADVNASD 154
Cdd:cd22196   96 TALHIAIERRNMHLVELLVQNGADVHArasgeffkKKKGgpgfyfGELPLSLAACTNQLDIVKFLLEnphSPADISARD 174
 
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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