NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|27369712|ref|NP_766100|]
View 

GA-binding protein subunit beta-2 [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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
10-173 3.62e-43

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 152.80  E-value: 3.62e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369712  10 LLEAARKGQDDEVRTLMANGA-PFTTDWLGTSPLHLAAQYGHYSTAEVLLRAGVSRDARTKVDRTPLHMAAADGHVHIVE 88
Cdd:COG0666  91 LHAAARNGDLEIVKLLLEAGAdVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369712  89 LLVRSGADVNAKDMLQMTALHWATEHHHRDVVELLIKYGADVYAFSKFDKSAFDIAMEKNNTEILVMLQEAMQNQVNTNH 168
Cdd:COG0666 171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250


                ....*
gi 27369712 169 ERANP 173
Cdd:COG0666 251 DGLTA 255
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
10-173 3.62e-43

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 152.80  E-value: 3.62e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369712  10 LLEAARKGQDDEVRTLMANGA-PFTTDWLGTSPLHLAAQYGHYSTAEVLLRAGVSRDARTKVDRTPLHMAAADGHVHIVE 88
Cdd:COG0666  91 LHAAARNGDLEIVKLLLEAGAdVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369712  89 LLVRSGADVNAKDMLQMTALHWATEHHHRDVVELLIKYGADVYAFSKFDKSAFDIAMEKNNTEILVMLQEAMQNQVNTNH 168
Cdd:COG0666 171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250


                ....*
gi 27369712 169 ERANP 173
Cdd:COG0666 251 DGLTA 255
Ank_2 pfam12796
Ankyrin repeats (3 copies);
42-130 9.58e-24

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 94.41  E-value: 9.58e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369712    42 LHLAAQYGHYSTAEVLLRAGVSRDARTKVDRTPLHMAAADGHVHIVELLVrSGADVNAKDMlQMTALHWATEHHHRDVVE 121
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKDN-GRTALHYAARSGHLEIVK 78


                  ....*....
gi 27369712   122 LLIKYGADV 130
Cdd:pfam12796  79 LLLEKGADI 87
PHA03095 PHA03095
ankyrin-like protein; Provisional
 20-185 4.77e-17

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 82.77  E-value: 4.77e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369712   20 DEVRTLMANGAPF-TTDWLGTSPLHLAAQYGhySTAEV---LLRAGVSRDARTKVDRTPLHMAAADGHVH--IVELLVRS 93
Cdd:PHA03095  64 DIVRLLLEAGADVnAPERCGFTPLHLYLYNA--TTLDViklLIKAGADVNAKDKVGRTPLHVYLSGFNINpkVIRLLLRK 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369712   94 GADVNAKDMLQMTALHWATEHHHRDV--VELLIKYGADVYAFSKFDKSAFDIAME--KNNTEILVMLQEAMQNQVNTN-- 167
Cdd:PHA03095 142 GADVNALDLYGMTPLAVLLKSRNANVelLRLLIDAGADVYAVDDRFRSLLHHHLQsfKPRARIVRELIRAGCDPAATDml 221

                        170       180
                 ....*....|....*....|...
gi 27369712  168 -----HERANPVANPVTVTAPFI 185
Cdd:PHA03095 222 gntplHSMATGSSCKRSLVLPLL 244
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 10-168 1.67e-10

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: 62.72  E-value: 1.67e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369712  10 LLEAARKGQDDEVRTLMANGA--PFTTDWLGTSPLHLAAQYGHYSTAEVLLRAgvsrdARTKVD----------RTPLHM 77
Cdd:cd22192  21 LLLAAKENDVQAIKKLLKCPScdLFQRGALGETALHVAALYDNLEAAVVLMEA-----APELVNepmtsdlyqgETALHI 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369712  78 AAADGHVHIVELLVRSGADVNAKD------MLQMTALHWATEH--------HHRDVVELLIKYGADVYAFSKFDKSAFDI 143
Cdd:cd22192  96 AVVNQNLNLVRELIARGADVVSPRatgtffRPGPKNLIYYGEHplsfaacvGNEEIVRLLIEHGADIRAQDSLGNTVLHI 175

                       170       180       190
                ....*....|....*....|....*....|.
gi 27369712 144 AMEKNNTEI------LVMLQEAMQNQVNTNH 168
Cdd:cd22192 176 LVLQPNKTFacqmydLILSYDKEDDLQPLDL 206
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 71-99 8.06e-07

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: 44.89  E-value: 8.06e-07
                           10        20
                   ....*....|....*....|....*....
gi 27369712     71 DRTPLHMAAADGHVHIVELLVRSGADVNA 99
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 3-109 8.89e-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: 47.77  E-value: 8.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369712     3 LVDLGKRLLEAARKGQDDEVRTL---------------MANGAPFTTDWLGTSPLHLAAQYGHYSTAEVLLRAGVSRDAR 67
Cdd:TIGR00870  78 RGAVGDTLLHAISLEYVDAVEAIllhllaafrksgpleLANDQYTSEFTPGITALHLAAHRQNYEIVKLLLERGASVPAR 157

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 27369712    68 TKVD--------------RTPLHMAAADGHVHIVELLVRSGADVNAKDMLQMTALH 109
Cdd:TIGR00870 158 ACGDffvksqgvdsfyhgESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLH 213
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
10-173 3.62e-43

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 152.80  E-value: 3.62e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369712  10 LLEAARKGQDDEVRTLMANGA-PFTTDWLGTSPLHLAAQYGHYSTAEVLLRAGVSRDARTKVDRTPLHMAAADGHVHIVE 88
Cdd:COG0666  91 LHAAARNGDLEIVKLLLEAGAdVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369712  89 LLVRSGADVNAKDMLQMTALHWATEHHHRDVVELLIKYGADVYAFSKFDKSAFDIAMEKNNTEILVMLQEAMQNQVNTNH 168
Cdd:COG0666 171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250


                ....*
gi 27369712 169 ERANP 173
Cdd:COG0666 251 DGLTA 255
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
10-172 5.62e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 130.84  E-value: 5.62e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369712  10 LLEAARKGQDDEVRTLMANGA-PFTTDWLGTSPLHLAAQYGHYSTAEVLLRAGVSRDARTKVDRTPLHMAAADGHVHIVE 88
Cdd:COG0666 124 LHLAAYNGNLEIVKLLLEAGAdVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVK 203

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369712  89 LLVRSGADVNAKDMLQMTALHWATEHHHRDVVELLIKYGADVYAFSKFDKSAFDIAMEKNNTEILVMLQEAMQNQVNTNH 168
Cdd:COG0666 204 LLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283


                ....
gi 27369712 169 ERAN 172
Cdd:COG0666 284 DLLT 287
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
5-159 3.41e-34

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 128.92  E-value: 3.41e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369712   5 DLGKRLLEAARKGQDDEVRTLMANGAPF--TTDWLGTSPLHLAAQYGHYSTAEVLLRAGVSRDARTKVDRTPLHMAAADG 82
Cdd:COG0666  52 ALGALLLLAAALAGDLLVALLLLAAGADinAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNG 131

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27369712  83 HVHIVELLVRSGADVNAKDMLQMTALHWATEHHHRDVVELLIKYGADVYAFSKFDKSAFDIAMEKNNTEILVMLQEA 159
Cdd:COG0666 132 NLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA 208
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
8-156 5.94e-25

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 103.50  E-value: 5.94e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369712   8 KRLLEAARKGQDDEVRTLMANGAPFTTDWLGTSPLHLAAQYGHYSTAEVLLRAGVSRDARTKVDRTPLHMAAADGHVHIV 87
Cdd:COG0666  24 LLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIV 103

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27369712  88 ELLVRSGADVNAKDMLQMTALHWATEHHHRDVVELLIKYGADVYAFSKFDKSAFDIAMEKNNTEILVML 156
Cdd:COG0666 104 KLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLL 172
Ank_2 pfam12796
Ankyrin repeats (3 copies);
42-130 9.58e-24

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 94.41  E-value: 9.58e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369712    42 LHLAAQYGHYSTAEVLLRAGVSRDARTKVDRTPLHMAAADGHVHIVELLVrSGADVNAKDMlQMTALHWATEHHHRDVVE 121
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKDN-GRTALHYAARSGHLEIVK 78


                  ....*....
gi 27369712   122 LLIKYGADV 130
Cdd:pfam12796  79 LLLEKGADI 87
PHA03095 PHA03095
ankyrin-like protein; Provisional
 20-185 4.77e-17

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 82.77  E-value: 4.77e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369712   20 DEVRTLMANGAPF-TTDWLGTSPLHLAAQYGhySTAEV---LLRAGVSRDARTKVDRTPLHMAAADGHVH--IVELLVRS 93
Cdd:PHA03095  64 DIVRLLLEAGADVnAPERCGFTPLHLYLYNA--TTLDViklLIKAGADVNAKDKVGRTPLHVYLSGFNINpkVIRLLLRK 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369712   94 GADVNAKDMLQMTALHWATEHHHRDV--VELLIKYGADVYAFSKFDKSAFDIAME--KNNTEILVMLQEAMQNQVNTN-- 167
Cdd:PHA03095 142 GADVNALDLYGMTPLAVLLKSRNANVelLRLLIDAGADVYAVDDRFRSLLHHHLQsfKPRARIVRELIRAGCDPAATDml 221

                        170       180
                 ....*....|....*....|...
gi 27369712  168 -----HERANPVANPVTVTAPFI 185
Cdd:PHA03095 222 gntplHSMATGSSCKRSLVLPLL 244
Ank_2 pfam12796
Ankyrin repeats (3 copies);
10-101 4.88e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.92  E-value: 4.88e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369712    10 LLEAARKGQDDEVRTLMANGA-PFTTDWLGTSPLHLAAQYGHYSTAEVLLRAGVSRDarTKVDRTPLHMAAADGHVHIVE 88
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGAdANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 27369712    89 LLVRSGADVNAKD 101
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 20-159 1.78e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 80.84  E-value: 1.78e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369712   20 DEVRTLMANGAPFT-TDWLGTSPLHLaaqYGHYSTAEV------LLRAGVSRDARTKVDRTPLHMAAADGHV-HIVELLV 91
Cdd:PHA03095  28 EEVRRLLAAGADVNfRGEYGKTPLHL---YLHYSSEKVkdivrlLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLI 104

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27369712   92 RSGADVNAKDMLQMTALH--WATEHHHRDVVELLIKYGADVYAFSKFDKSAFDIAMEKNNT--EILVMLQEA 159
Cdd:PHA03095 105 KAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNAnvELLRLLIDA 176
Ank_2 pfam12796
Ankyrin repeats (3 copies);
75-156 7.33e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 66.68  E-value: 7.33e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369712    75 LHMAAADGHVHIVELLVRSGADVNAKDMLQMTALHWATEHHHRDVVELLIKYgADVYAFSKfDKSAFDIAMEKNNTEILV 154
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78


                  ..
gi 27369712   155 ML 156
Cdd:pfam12796  79 LL 80
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 22-156 1.88e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 71.62  E-value: 1.88e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369712   22 VRTLMANGAPFT-TDWLGTSPLHLAAQY--GHYSTAEVLLRAGVSRDARTKVDRTPLHMAAADGHV--HIVELLVRSGAD 96
Cdd:PHA03100  89 VKLLLEYGANVNaPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVD 168

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27369712   97 VNAKDMLQM----------------TALHWATEHHHRDVVELLIKYGADVYAFSKFDKSAFDIAMEKNNTEILVML 156
Cdd:PHA03100 169 INAKNRVNYllsygvpinikdvygfTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLL 244
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
25-159 3.89e-13

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 69.60  E-value: 3.89e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369712  25 LMANGAPFTTDWLGTSPLHLAAQYGHYSTAEVLLRAGVSRDARTKVDRTPLHMAAADGHVHIVELLVRSGADVNAKDMLQ 104
Cdd:COG0666   8 LLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGG 87

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 27369712 105 MTALHWATEHHHRDVVELLIKYGADVYAFSKFDKSAFDIAMEKNNTEILVMLQEA 159
Cdd:COG0666  88 NTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA 142
Ank_4 pfam13637
Ankyrin repeats (many copies);
72-124 3.23e-12

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 61.14  E-value: 3.23e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 27369712    72 RTPLHMAAADGHVHIVELLVRSGADVNAKDMLQMTALHWATEHHHRDVVELLI 124
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 5-147 8.90e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 66.44  E-value: 8.90e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369712    5 DLGKRLLEAARKGQD-DEVRTLMANGA-PFTTDWLGTSPLHLAAQYGHYSTAEVLLRAGVSRDARTKVDRTPLHMAAAD- 81
Cdd:PHA02878 166 HKGNTALHYATENKDqRLTELLLSYGAnVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYc 245

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27369712   82 GHVHIVELLVRSGADVNAKD-MLQMTALHWATehHHRDVVELLIKYGADVYAFSKFDKSAFDIAMEK 147
Cdd:PHA02878 246 KDYDILKLLLEHGVDVNAKSyILGLTALHSSI--KSERKLKLLLEYGADINSLNSYKLTPLSSAVKQ 310
PHA03095 PHA03095
ankyrin-like protein; Provisional
 22-155 3.22e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 64.66  E-value: 3.22e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369712   22 VRTLMANGA-PFTTDWLGTSPLHLAAQYGHYSTA--EVLLRAGVSRDARTKVDRTPLHMAAADGHVH--IVELLVRSGAD 96
Cdd:PHA03095 170 LRLLIDAGAdVYAVDDRFRSLLHHHLQSFKPRARivRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIAGIS 249

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 27369712   97 VNAKDMLQMTALHWATEHHHRDVVELLIKYGADVYAFSKFDKSAFDIAMEKNNTEILVM 155
Cdd:PHA03095 250 INARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRA 308
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 14-169 5.13e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 64.70  E-value: 5.13e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369712   14 ARKGQDDE-VRTLMANGAPFT-TDWLGTSPLHLAAQYGHYS-TAEVLLRAGVSRDARTKVDRTPLHMAAADGHVHIVELL 90
Cdd:PHA02876 315 AKNGYDTEnIRTLIMLGADVNaADRLYITPLHQASTLDRNKdIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTL 394

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369712   91 VRSGADVNAKDMLQMTALHWA---TEHHHRdvVELLIKYGADVYAFSKFDKSAFDIAMEKN-NTEILVMLQE--AMQNQV 164
Cdd:PHA02876 395 LDYGADIEALSQKIGTALHFAlcgTNPYMS--VKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDngADVNAI 472


                 ....*
gi 27369712  165 NTNHE 169
Cdd:PHA02876 473 NIQNQ 477
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 10-168 1.67e-10

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: 62.72  E-value: 1.67e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369712  10 LLEAARKGQDDEVRTLMANGA--PFTTDWLGTSPLHLAAQYGHYSTAEVLLRAgvsrdARTKVD----------RTPLHM 77
Cdd:cd22192  21 LLLAAKENDVQAIKKLLKCPScdLFQRGALGETALHVAALYDNLEAAVVLMEA-----APELVNepmtsdlyqgETALHI 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369712  78 AAADGHVHIVELLVRSGADVNAKD------MLQMTALHWATEH--------HHRDVVELLIKYGADVYAFSKFDKSAFDI 143
Cdd:cd22192  96 AVVNQNLNLVRELIARGADVVSPRatgtffRPGPKNLIYYGEHplsfaacvGNEEIVRLLIEHGADIRAQDSLGNTVLHI 175

                       170       180       190
                ....*....|....*....|....*....|.
gi 27369712 144 AMEKNNTEI------LVMLQEAMQNQVNTNH 168
Cdd:cd22192 176 LVLQPNKTFacqmydLILSYDKEDDLQPLDL 206
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 43-133 7.49e-10

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 60.68  E-value: 7.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369712   43 HLAAQyGHYSTAEVLLRAGVSRDARTKVDRTPLHMAAADGHVHIVELLVRSGADVNAKDMLQMTALHWATEHHHRDVVEL 122
Cdd:PTZ00322  88 QLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166

                         90
                 ....*....|.
gi 27369712  123 LIKYGADVYAF 133
Cdd:PTZ00322 167 LSRHSQCHFEL 177
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 86-193 7.86e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 60.85  E-value: 7.86e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369712   86 IVELLVRSGADVNAKDMLQMTALHWATEHHHRDVVELLIKYGADVYAFSKFDKSAFDIAMEKNNTEILVMLQEAMQNQVN 165
Cdd:PHA02876 160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINK 239

                         90       100
                 ....*....|....*....|....*...
gi 27369712  166 TNHERANPVANPVTVTAPFIFTSGEVIN 193
Cdd:PHA02876 240 NDLSLLKAIRNEDLETSLLLYDAGFSVN 267
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 22-132 1.05e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 60.06  E-value: 1.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369712   22 VRTLMANGAPFT-TDWLGTSPLHLAAQYGHYST--AEVLLRAGVSRDARTKVDR----------------TPLHMAAADG 82
Cdd:PHA03100 124 VEYLLDNGANVNiKNSDGENLLHLYLESNKIDLkiLKLLIDKGVDINAKNRVNYllsygvpinikdvygfTPLHYAVYNN 203

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 27369712   83 HVHIVELLVRSGADVNAKDMLQMTALHWATEHHHRDVVELLIKYGADVYA 132
Cdd:PHA03100 204 NPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 22-134 2.52e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 58.74  E-value: 2.52e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369712   22 VRTLMANGAPFT--TDWLGTSPLHLAAQYGHYSTAEVLLRAGVSRDARTKVDRTPLHMAAADGHVHIVELLVRSGADVNA 99
Cdd:PHA02878 150 TKLLLSYGADINmkDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDA 229

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 27369712  100 KDMLQMTALHWATEH-HHRDVVELLIKYGADVYAFS 134
Cdd:PHA02878 230 RDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKS 265
Ank_4 pfam13637
Ankyrin repeats (many copies);
38-91 2.58e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.66  E-value: 2.58e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 27369712    38 GTSPLHLAAQYGHYSTAEVLLRAGVSRDARTKVDRTPLHMAAADGHVHIVELLV 91
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 23-167 2.62e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 58.52  E-value: 2.62e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369712   23 RTLMANGAPFTTDWLGTSPLHLAAQYGHYSTAEVLLRAGVSRDARTKVDRTPLHMAAADGHV-----HIVELLVRSGADV 97
Cdd:PHA03100  20 YIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANV 99

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27369712   98 NAKDMLQMTALHWATEHH--HRDVVELLIKYGADVYAFSKFDKSAFDIAME--KNNTEILVMLqeaMQNQVNTN 167
Cdd:PHA03100 100 NAPDNNGITPLLYAISKKsnSYSIVEYLLDNGANVNIKNSDGENLLHLYLEsnKIDLKILKLL---IDKGVDIN 170
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
10-108 2.80e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 58.04  E-value: 2.80e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369712  10 LLEAARKGQDDEVRTLMANGA-PFTTDWLGTSPLHLAAQYGHYSTAEVLLRAGVSRDARTKVDRTPLHMAAADGHVHIVE 88
Cdd:COG0666 190 LHLAAENGHLEIVKLLLEAGAdVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVK 269

                        90       100
                ....*....|....*....|
gi 27369712  89 LLVRSGADVNAKDMLQMTAL 108
Cdd:COG0666 270 LLLLALLLLAAALLDLLTLL 289
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 5-156 2.37e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 55.77  E-value: 2.37e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369712    5 DLGKRLLEAARKGQDDEVRTLMANGApFTTDWL---GTSPLHLAAQYGHYSTAEVLLRAGVSRDARTKVDRTPLHMAAAD 81
Cdd:PHA02875  67 DIESELHDAVEEGDVKAVEELLDLGK-FADDVFykdGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMM 145

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27369712   82 GHVHIVELLVRSGADVNAKDMLQMTALHWATEHHHRDVVELLIKYGADVYAFSKF-DKSAFDIAMEKNNTEILVML 156
Cdd:PHA02875 146 GDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNgCVAALCYAIENNKIDIVRLF 221
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 70-156 2.44e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.06  E-value: 2.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369712   70 VDRTPLHMA-------AADGHVHIVELLVRSGADVNAKDMLQMTALHWATEHHHRDVVELLIKYGADVYAFSKFDKSAFD 142
Cdd:PTZ00322  74 IDPVVAHMLtvelcqlAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLE 153

                         90
                 ....*....|....
gi 27369712  143 IAMEKNNTEILVML 156
Cdd:PTZ00322 154 LAEENGFREVVQLL 167
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 55-158 2.89e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 55.66  E-value: 2.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369712   55 EVLLRAGVSRDARTK-VDRTPLHMAAADGHVHIVELLVRSGADVNAKDMLQMTALHWATEHHHRDVVELLIKYGADVYAF 133
Cdd:PHA02878 151 KLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDAR 230

                         90       100
                 ....*....|....*....|....*.
gi 27369712  134 SKFDKSAFDIAMEK-NNTEILVMLQE 158
Cdd:PHA02878 231 DKCGNTPLHISVGYcKDYDILKLLLE 256
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 20-129 6.75e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 54.23  E-value: 6.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369712   20 DEVRTLMANGA-PFTTDWLGTSPLHLAAQYGHYSTAEVLLRAGVSRDARTKVDRTPLHMAAADGHVHIVELLVRSGADVN 98
Cdd:PHA02875 116 DIMKLLIARGAdPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANID 195

                         90       100       110
                 ....*....|....*....|....*....|..
gi 27369712   99 -AKDMLQMTALHWATEHHHRDVVELLIKYGAD 129
Cdd:PHA02875 196 yFGKNGCVAALCYAIENNKIDIVRLFIKRGAD 227
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 38-129 6.87e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 54.23  E-value: 6.87e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369712   38 GTSPLHLAAQYGHYSTAEVLLRAGVSRDARTKVDRTPLHMAAADGHVHIVELLVRSGA---DVNAKDmlQMTALHWATEH 114
Cdd:PHA02875  35 GISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKfadDVFYKD--GMTPLHLATIL 112

                         90
                 ....*....|....*
gi 27369712  115 HHRDVVELLIKYGAD 129
Cdd:PHA02875 113 KKLDIMKLLIARGAD 127
Ank_5 pfam13857
Ankyrin repeats (many copies);
89-144 1.34e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.11  E-value: 1.34e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 27369712    89 LLVRSGADVNAKDMLQMTALHWATEHHHRDVVELLIKYGADVYAFSKFDKSAFDIA 144
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 72-101 1.53e-07

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: 47.28  E-value: 1.53e-07
                          10        20        30
                  ....*....|....*....|....*....|.
gi 27369712    72 RTPLHMAAAD-GHVHIVELLVRSGADVNAKD 101
Cdd:pfam00023   3 NTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 10-128 5.10e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 51.50  E-value: 5.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369712   10 LLEAARKGQDDEVRTLMANGapfttdwLGTSPLHLAAQygHYSTAEVLLRAGVSRDARTKVDRTPLHMAAADGHVHIVEL 89
Cdd:PHA02874  72 LLTAIKIGAHDIIKLLIDNG-------VDTSILPIPCI--EKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKM 142

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 27369712   90 LVRSGADVNAKDMLQMTALHWATEHHHRDVVELLIKYGA 128
Cdd:PHA02874 143 LFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGA 181
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 13-124 5.37e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 51.50  E-value: 5.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369712   13 AARKGQDDEVRTLMANGAPFTT-DWLGTSPLHLAAQYGHYSTAEVLLRAGVSRDARTKVDRTPLHMAAADGHVHIVELLV 91
Cdd:PHA02874 131 AIKKGDLESIKMLFEYGADVNIeDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLI 210

                         90       100       110
                 ....*....|....*....|....*....|...
gi 27369712   92 RSGADVNAKDMLQMTALHWATeHHHRDVVELLI 124
Cdd:PHA02874 211 DHGNHIMNKCKNGFTPLHNAI-IHNRSAIELLI 242
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 6-92 5.64e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.82  E-value: 5.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369712    6 LGKRLLEAARKGQDDEVRTLMANGA-PFTTDWLGTSPLHLAAQYGHYSTAEVLLRAGVSRDARTKVDRTPLHMAAADGHV 84
Cdd:PTZ00322  82 LTVELCQLAASGDAVGARILLTGGAdPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFR 161


                 ....*...
gi 27369712   85 HIVELLVR 92
Cdd:PTZ00322 162 EVVQLLSR 169
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 25-158 7.00e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 51.41  E-value: 7.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369712   25 LMANGAPFTTDWLGTSPLHLAAQYGHYSTAEVLLRAGVSRDARTKVDRTPLHMAAADGHVHIVELL-------------- 90
Cdd:PLN03192 545 LKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILyhfasisdphaagd 624

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369712   91 -----------------VRSGADVNAKDMLQMTALHWATEHHHRDVVELLIKYGADVyafskfDKSAFDIAMekNNTEIL 153
Cdd:PLN03192 625 llctaakrndltamkelLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV------DKANTDDDF--SPTELR 696


                 ....*
gi 27369712  154 VMLQE 158
Cdd:PLN03192 697 ELLQK 701
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 71-99 8.06e-07

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: 44.89  E-value: 8.06e-07
                           10        20
                   ....*....|....*....|....*....
gi 27369712     71 DRTPLHMAAADGHVHIVELLVRSGADVNA 99
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
104-156 8.22e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.73  E-value: 8.22e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 27369712   104 QMTALHWATEHHHRDVVELLIKYGADVYAFSKFDKSAFDIAMEKNNTEILVML 156
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 8-128 8.25e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 51.41  E-value: 8.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369712    8 KRLLEAARKGQDDEVRTLMANGAPFTTDWLGTSPLHLAAQYGHYSTAEVLLRAGVSRDARTKVDRTPLHMAAADGHVHIV 87
Cdd:PLN03192 495 KNFLQHHKELHDLNVGDLLGDNGGEHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCV 574

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 27369712   88 ELLVRSGADVNAKDMLQMTALHWATEHHHRDVVELLIKYGA 128
Cdd:PLN03192 575 LVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFAS 615
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 54-124 1.41e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 50.45  E-value: 1.41e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27369712   54 AEVLLRAGVSRDARTKVDRTPLHMAAADGHVHIVELLVRSGADVNAKDMLQMTALHWATEHHHRDVVELLI 124
Cdd:PHA02876 161 AEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAII 231
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 3-109 8.89e-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: 47.77  E-value: 8.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369712     3 LVDLGKRLLEAARKGQDDEVRTL---------------MANGAPFTTDWLGTSPLHLAAQYGHYSTAEVLLRAGVSRDAR 67
Cdd:TIGR00870  78 RGAVGDTLLHAISLEYVDAVEAIllhllaafrksgpleLANDQYTSEFTPGITALHLAAHRQNYEIVKLLLERGASVPAR 157

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 27369712    68 TKVD--------------RTPLHMAAADGHVHIVELLVRSGADVNAKDMLQMTALH 109
Cdd:TIGR00870 158 ACGDffvksqgvdsfyhgESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLH 213
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 22-130 1.31e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 47.37  E-value: 1.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369712   22 VRTLMANGAPFT--TDWLGTSpLHLAAqYGH--YSTAEVLLRAGVSRDARTKVDRTPLHMAAADG-HVHIVELLVRSGAD 96
Cdd:PHA02876 391 INTLLDYGADIEalSQKIGTA-LHFAL-CGTnpYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGAD 468

                         90       100       110
                 ....*....|....*....|....*....|....
gi 27369712   97 VNAKDMLQMTALHWATEHHhrDVVELLIKYGADV 130
Cdd:PHA02876 469 VNAINIQNQYPLLIALEYH--GIVNILLHYGAEL 500
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 105-132 1.34e-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: 41.80  E-value: 1.34e-05
                           10        20
                   ....*....|....*....|....*...
gi 27369712    105 MTALHWATEHHHRDVVELLIKYGADVYA 132
Cdd:smart00248   3 RTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 72-99 1.53e-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: 41.47  E-value: 1.53e-05
                          10        20
                  ....*....|....*....|....*...
gi 27369712    72 RTPLHMAAADGHVHIVELLVRSGADVNA 99
Cdd:pfam13606   3 NTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 10-168 4.57e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 45.34  E-value: 4.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369712   10 LLEAARKGQDDEVRTLMANGApfTTDWLGTS---PLHLAAQYGHYSTAEVLLRAGVSrdarTKVDRTPlhmaaaDGHVHI 86
Cdd:PHA02874  39 LIDAIRSGDAKIVELFIKHGA--DINHINTKiphPLLTAIKIGAHDIIKLLIDNGVD----TSILPIP------CIEKDM 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369712   87 VELLVRSGADVNAKDMLQMTALHWATEHHHRDVVELLIKYGADVYAFSKFDKSAFDIAMEKNNTEIL-VMLQEAMQNQVN 165
Cdd:PHA02874 107 IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIkLLLEKGAYANVK 186


                 ...
gi 27369712  166 TNH 168
Cdd:PHA02874 187 DNN 189
PHA03095 PHA03095
ankyrin-like protein; Provisional
 77-156 5.93e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 45.02  E-value: 5.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369712   77 MAAADGHVHIVELLVRSGADVNAKDMLQMTALHW--ATEHHHR-DVVELLIKYGADVYAFSKFDKSAFDIAMEKNNTEIL 153
Cdd:PHA03095  20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHLylHYSSEKVkDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDV 99


                 ...
gi 27369712  154 VML 156
Cdd:PHA03095 100 IKL 102
Ank_4 pfam13637
Ankyrin repeats (many copies);
10-58 6.69e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 40.34  E-value: 6.69e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 27369712    10 LLEAARKGQDDEVRTLMANGAPF-TTDWLGTSPLHLAAQYGHYSTAEVLL 58
Cdd:pfam13637   5 LHAAAASGHLELLRLLLEKGADInAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 20-101 8.34e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 44.66  E-value: 8.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369712   20 DEVRTLMANGAPF-TTDWLGTSPLHLAAQYGHYSTAEVLLRAGVSRDARTKVDRTPLHMAAADGHVHIVELLVRSGADVN 98
Cdd:PHA03100 173 NRVNYLLSYGVPInIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252


                 ...
gi 27369712   99 AKD 101
Cdd:PHA03100 253 TII 255
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 105-132 9.25e-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. 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: 39.19  E-value: 9.25e-05
                          10        20
                  ....*....|....*....|....*....
gi 27369712   105 MTALHWATEHH-HRDVVELLIKYGADVYA 132
Cdd:pfam00023   3 NTPLHLAAGRRgNLEIVKLLLSKGADVNA 31
Ank_2 pfam12796
Ankyrin repeats (3 copies);
108-168 9.31e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 40.87  E-value: 9.31e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27369712   108 LHWATEHHHRDVVELLIKYGADVYAFSKFDKSAFDIAMEKNNTEIL-VMLQEAMQNQVNTNH 168
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVkLLLEHADVNLKDNGR 62
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 105-132 1.69e-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: 38.39  E-value: 1.69e-04
                          10        20
                  ....*....|....*....|....*...
gi 27369712   105 MTALHWATEHHHRDVVELLIKYGADVYA 132
Cdd:pfam13606   3 NTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
30-78 2.81e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.48  E-value: 2.81e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 27369712    30 APFTTDWLGTSPLHLAAQYGHYSTAEVLLRAGVSRDARTKVDRTPLHMA 78
Cdd:pfam13857   8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02741 PHA02741
hypothetical protein; Provisional
 84-158 3.67e-04

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 41.18  E-value: 3.67e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27369712   84 VHIVELLVRSGADVNAKDMLQ-MTALHWATEHHHRDVVELLIKY-GADVYAFSKFDKSAFDIAMEKNNTEILVMLQE 158
Cdd:PHA02741  77 AEIIDHLIELGADINAQEMLEgDTALHLAAHRRDHDLAEWLCCQpGIDLHFCNADNKSPFELAIDNEDVAMMQILRE 153
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 38-69 5.48e-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: 37.27  E-value: 5.48e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 27369712    38 GTSPLHLAA-QYGHYSTAEVLLRAGVSRDARTK 69
Cdd:pfam00023   2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 18-167 6.44e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 41.87  E-value: 6.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369712   18 QDDEVRTLMANGAPFTT-DWLGTSPLHLAAQYGHYSTAEVLLRAGVSRDARTKVDRTPLHMAAADGHVHIVELLVRSGAD 96
Cdd:PHA02874 103 EKDMIKTILDCGIDVNIkDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAY 182

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27369712   97 VNAKDMLQMTALHWATEHHHRDVVELLIKYGADVYAFSKFDKSAFDIAMEKNNTEILVMLQEAMQNQVNTN 167
Cdd:PHA02874 183 ANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAIELLINNASINDQDID 253
PHA02743 PHA02743
Viral ankyrin protein; Provisional
 43-128 1.75e-03

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 39.03  E-value: 1.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369712   43 HLAAQYGHYSTA---EVLLRAGVSRDAR-TKVDRTPLHMAAADGHVHIVELLVRS-GADVNAKDMLQMTALHWATEHHHR 117
Cdd:PHA02743  62 HMVAWYDRANAVmkiELLVNMGADINAReLGTGNTLLHIAASTKNYELAEWLCRQlGVNLGAINYQHETAYHIAYKMRDR 141

                         90
                 ....*....|.
gi 27369712  118 DVVELLIKYGA 128
Cdd:PHA02743 142 RMMEILRANGA 152
PHA02946 PHA02946
ankyin-like protein; Provisional
 16-98 2.62e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 40.04  E-value: 2.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369712   16 KGQDDE-VRTLMANG-APFTTDWLGTSPLHLAAQYGHYSTAEVLLRAGVSRDARTKVDRTPLHMAAA--DGHVHIVELLV 91
Cdd:PHA02946  48 KGLDERfVEELLHRGySPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGtdDEVIERINLLV 127


                 ....*..
gi 27369712   92 RSGADVN 98
Cdd:PHA02946 128 QYGAKIN 134
Ank_5 pfam13857
Ankyrin repeats (many copies);
57-111 3.29e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.40  E-value: 3.29e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 27369712    57 LLRAG-VSRDARTKVDRTPLHMAAADGHVHIVELLVRSGADVNAKDMLQMTALHWA 111
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 2-135 3.69e-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: 39.68  E-value: 3.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369712     2 SLVDLGKRLLEAARKGQDDEVRTLMANGAPF---TTDWLGTSPLHLAAQYG-HYSTAEVLLragvSRDARTKVDRTPLHm 77
Cdd:TIGR00870  13 PLSDEEKAFLPAAERGDLASVYRDLEEPKKLninCPDRLGRSALFVAAIENeNLELTELLL----NLSCRGAVGDTLLH- 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27369712    78 AAADGHVHIVELLVRSGADVNAKDM-LQM-------------TALHWATEHHHRDVVELLIKYGADVYAFSK 135
Cdd:TIGR00870  88 AISLEYVDAVEAILLHLLAAFRKSGpLELandqytseftpgiTALHLAAHRQNYEIVKLLLERGASVPARAC 159
PHA02946 PHA02946
ankyin-like protein; Provisional
 55-130 3.81e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 39.27  E-value: 3.81e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27369712   55 EVLLRAGVSRDARTKVDRTPLHMAAADGHVHIVELLVRSGADVNAKDMLQMTALHW--ATEHHHRDVVELLIKYGADV 130
Cdd:PHA02946  56 EELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYlsGTDDEVIERINLLVQYGAKI 133
PHA02791 PHA02791
ankyrin-like protein; Provisional
 18-153 4.98e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 38.48  E-value: 4.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27369712   18 QDDEVRTLMANGAPFTTDWLGTSPLHLAAQYGHYSTAEVLLRAGVSRDARTkvDRTPLHMAAADGHVHIVELLVRSGADV 97
Cdd:PHA02791  10 KSKQLKSFLSSKDAFKADVHGHSALYYAIADNNVRLVCTLLNAGALKNLLE--NEFPLHQAATLEDTKIVKILLFSGMDD 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 27369712   98 NAKDMLQMTALHWATEHHHRDVVELLIKYGADVYAFSKFD-KSAFDIAMEKNNTEIL 153
Cdd:PHA02791  88 SQFDDKGNTALYYAVDSGNMQTVKLFVKKNWRLMFYGKTGwKTSFYHAVMLNDVSIV 144
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 38-63 9.21e-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: 33.72  E-value: 9.21e-03
                           10        20
                   ....*....|....*....|....*.
gi 27369712     38 GTSPLHLAAQYGHYSTAEVLLRAGVS 63
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGAD 27
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH