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Conserved domains on  [gi|1039764056|ref|XP_017175004|]
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GA-binding protein subunit beta-2 isoform X2 [Mus musculus]

Protein Classification

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

ankyrin repeat (ANK) domain-containing protein is involved in mediating protein-protein interactions

Gene Ontology:  GO:0005515
PubMed:  33435370|17176038

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
10-173 2.17e-41

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 146.25  E-value: 2.17e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764056  10 LLEAARKGQDDEVRTLMANGA-PFTTDWLGTSPLHLAAQYGHYSTAEVLLRAGVSRDARTKVDRTPLHMAAADGHVHIVE 88
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGAdVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764056  89 LLVRSGADVNAKDMLQMTALHWATEHHHRDVVELLIKYGADVYAFSKFDKSAFDIAMEKNNTEILVMLQEAMQNQVNTNH 168
Cdd:COG0666   171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250


                  ....*
gi 1039764056 169 ERANP 173
Cdd:COG0666   251 DGLTA 255
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
10-173 2.17e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 146.25  E-value: 2.17e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764056  10 LLEAARKGQDDEVRTLMANGA-PFTTDWLGTSPLHLAAQYGHYSTAEVLLRAGVSRDARTKVDRTPLHMAAADGHVHIVE 88
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGAdVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764056  89 LLVRSGADVNAKDMLQMTALHWATEHHHRDVVELLIKYGADVYAFSKFDKSAFDIAMEKNNTEILVMLQEAMQNQVNTNH 168
Cdd:COG0666   171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250


                  ....*
gi 1039764056 169 ERANP 173
Cdd:COG0666   251 DGLTA 255
Ank_2 pfam12796
Ankyrin repeats (3 copies);
42-130 2.74e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.10  E-value: 2.74e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764056  42 LHLAAQYGHYSTAEVLLRAGVSRDARTKVDRTPLHMAAADGHVHIVELLVrSGADVNAKDMlQMTALHWATEHHHRDVVE 121
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKDN-GRTALHYAARSGHLEIVK 78


                  ....*....
gi 1039764056 122 LLIKYGADV 130
Cdd:pfam12796  79 LLLEKGADI 87
PHA03095 PHA03095
ankyrin-like protein; Provisional
 20-185 5.86e-17

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 81.61  E-value: 5.86e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764056  20 DEVRTLMANGAPF-TTDWLGTSPLHLAAQYGhySTAEV---LLRAGVSRDARTKVDRTPLHMAAADGHVH--IVELLVRS 93
Cdd:PHA03095   64 DIVRLLLEAGADVnAPERCGFTPLHLYLYNA--TTLDViklLIKAGADVNAKDKVGRTPLHVYLSGFNINpkVIRLLLRK 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764056  94 GADVNAKDMLQMTALHWATEHHHRDV--VELLIKYGADVYAFSKFDKSAFDIAME--KNNTEILVMLQEAMQNQVNTN-- 167
Cdd:PHA03095  142 GADVNALDLYGMTPLAVLLKSRNANVelLRLLIDAGADVYAVDDRFRSLLHHHLQsfKPRARIVRELIRAGCDPAATDml 221

                         170       180
                  ....*....|....*....|...
gi 1039764056 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 1.07e-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: 1.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764056  10 LLEAARKGQDDEVRTLMANGA--PFTTDWLGTSPLHLAAQYGHYSTAEVLLRAgvsrdARTKVD----------RTPLHM 77
Cdd:cd22192    21 LLLAAKENDVQAIKKLLKCPScdLFQRGALGETALHVAALYDNLEAAVVLMEA-----APELVNepmtsdlyqgETALHI 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764056  78 AAADGHVHIVELLVRSGADVNAKD------MLQMTALHWATEH--------HHRDVVELLIKYGADVYAFSKFDKSAFDI 143
Cdd:cd22192    96 AVVNQNLNLVRELIARGADVVSPRatgtffRPGPKNLIYYGEHplsfaacvGNEEIVRLLIEHGADIRAQDSLGNTVLHI 175

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1039764056 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 1.29e-06

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: 44.12  E-value: 1.29e-06
                           10        20
                   ....*....|....*....|....*....
gi 1039764056   71 DRTPLHMAAADGHVHIVELLVRSGADVNA 99
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 3-109 6.50e-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: 6.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764056   3 LVDLGKRLLEAARKGQDDEVRTL---------------MANGAPFTTDWLGTSPLHLAAQYGHYSTAEVLLRAGVSRDAR 67
Cdd:TIGR00870  78 RGAVGDTLLHAISLEYVDAVEAIllhllaafrksgpleLANDQYTSEFTPGITALHLAAHRQNYEIVKLLLERGASVPAR 157

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039764056  68 TKVD--------------RTPLHMAAADGHVHIVELLVRSGADVNAKDMLQMTALH 109
Cdd:TIGR00870 158 ACGDffvksqgvdsfyhgESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLH 213
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
10-173 2.17e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 146.25  E-value: 2.17e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764056  10 LLEAARKGQDDEVRTLMANGA-PFTTDWLGTSPLHLAAQYGHYSTAEVLLRAGVSRDARTKVDRTPLHMAAADGHVHIVE 88
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGAdVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764056  89 LLVRSGADVNAKDMLQMTALHWATEHHHRDVVELLIKYGADVYAFSKFDKSAFDIAMEKNNTEILVMLQEAMQNQVNTNH 168
Cdd:COG0666   171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250


                  ....*
gi 1039764056 169 ERANP 173
Cdd:COG0666   251 DGLTA 255
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
10-172 1.65e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 125.45  E-value: 1.65e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764056  10 LLEAARKGQDDEVRTLMANGA-PFTTDWLGTSPLHLAAQYGHYSTAEVLLRAGVSRDARTKVDRTPLHMAAADGHVHIVE 88
Cdd:COG0666   124 LHLAAYNGNLEIVKLLLEAGAdVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVK 203

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764056  89 LLVRSGADVNAKDMLQMTALHWATEHHHRDVVELLIKYGADVYAFSKFDKSAFDIAMEKNNTEILVMLQEAMQNQVNTNH 168
Cdd:COG0666   204 LLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283


                  ....
gi 1039764056 169 ERAN 172
Cdd:COG0666   284 DLLT 287
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
5-159 9.64e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 123.53  E-value: 9.64e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764056   5 DLGKRLLEAARKGQDDEVRTLMANGAPF--TTDWLGTSPLHLAAQYGHYSTAEVLLRAGVSRDARTKVDRTPLHMAAADG 82
Cdd:COG0666    52 ALGALLLLAAALAGDLLVALLLLAAGADinAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNG 131

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039764056  83 HVHIVELLVRSGADVNAKDMLQMTALHWATEHHHRDVVELLIKYGADVYAFSKFDKSAFDIAMEKNNTEILVMLQEA 159
Cdd:COG0666   132 NLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA 208
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
8-156 6.84e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 99.64  E-value: 6.84e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764056   8 KRLLEAARKGQDDEVRTLMANGAPFTTDWLGTSPLHLAAQYGHYSTAEVLLRAGVSRDARTKVDRTPLHMAAADGHVHIV 87
Cdd:COG0666    24 LLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIV 103

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039764056  88 ELLVRSGADVNAKDMLQMTALHWATEHHHRDVVELLIKYGADVYAFSKFDKSAFDIAMEKNNTEILVML 156
Cdd:COG0666   104 KLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLL 172
Ank_2 pfam12796
Ankyrin repeats (3 copies);
42-130 2.74e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.10  E-value: 2.74e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764056  42 LHLAAQYGHYSTAEVLLRAGVSRDARTKVDRTPLHMAAADGHVHIVELLVrSGADVNAKDMlQMTALHWATEHHHRDVVE 121
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKDN-GRTALHYAARSGHLEIVK 78


                  ....*....
gi 1039764056 122 LLIKYGADV 130
Cdd:pfam12796  79 LLLEKGADI 87
PHA03095 PHA03095
ankyrin-like protein; Provisional
 20-185 5.86e-17

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 81.61  E-value: 5.86e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764056  20 DEVRTLMANGAPF-TTDWLGTSPLHLAAQYGhySTAEV---LLRAGVSRDARTKVDRTPLHMAAADGHVH--IVELLVRS 93
Cdd:PHA03095   64 DIVRLLLEAGADVnAPERCGFTPLHLYLYNA--TTLDViklLIKAGADVNAKDKVGRTPLHVYLSGFNINpkVIRLLLRK 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764056  94 GADVNAKDMLQMTALHWATEHHHRDV--VELLIKYGADVYAFSKFDKSAFDIAME--KNNTEILVMLQEAMQNQVNTN-- 167
Cdd:PHA03095  142 GADVNALDLYGMTPLAVLLKSRNANVelLRLLIDAGADVYAVDDRFRSLLHHHLQsfKPRARIVRELIRAGCDPAATDml 221

                         170       180
                  ....*....|....*....|...
gi 1039764056 168 -----HERANPVANPVTVTAPFI 185
Cdd:PHA03095  222 gntplHSMATGSSCKRSLVLPLL 244
Ank_2 pfam12796
Ankyrin repeats (3 copies);
10-101 1.34e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 74.00  E-value: 1.34e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764056  10 LLEAARKGQDDEVRTLMANGA-PFTTDWLGTSPLHLAAQYGHYSTAEVLLRAGVSRDarTKVDRTPLHMAAADGHVHIVE 88
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGAdANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1039764056  89 LLVRSGADVNAKD 101
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 20-159 1.89e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 80.07  E-value: 1.89e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764056  20 DEVRTLMANGAPFT-TDWLGTSPLHLaaqYGHYSTAEV------LLRAGVSRDARTKVDRTPLHMAAADGHV-HIVELLV 91
Cdd:PHA03095   28 EEVRRLLAAGADVNfRGEYGKTPLHL---YLHYSSEKVkdivrlLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLI 104

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039764056  92 RSGADVNAKDMLQMTALH--WATEHHHRDVVELLIKYGADVYAFSKFDKSAFDIAMEKNNT--EILVMLQEA 159
Cdd:PHA03095  105 KAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNAnvELLRLLIDA 176
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 22-156 1.15e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 71.62  E-value: 1.15e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764056  22 VRTLMANGAPFT-TDWLGTSPLHLAAQY--GHYSTAEVLLRAGVSRDARTKVDRTPLHMAAADGHV--HIVELLVRSGAD 96
Cdd:PHA03100   89 VKLLLEYGANVNaPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVD 168

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039764056  97 VNAKDMLQM----------------TALHWATEHHHRDVVELLIKYGADVYAFSKFDKSAFDIAMEKNNTEILVML 156
Cdd:PHA03100  169 INAKNRVNYllsygvpinikdvygfTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLL 244
Ank_2 pfam12796
Ankyrin repeats (3 copies);
75-156 1.95e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.14  E-value: 1.95e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764056  75 LHMAAADGHVHIVELLVRSGADVNAKDMLQMTALHWATEHHHRDVVELLIKYgADVYAFSKfDKSAFDIAMEKNNTEILV 154
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78


                  ..
gi 1039764056 155 ML 156
Cdd:pfam12796  79 LL 80
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
25-159 2.24e-12

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 66.90  E-value: 2.24e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764056  25 LMANGAPFTTDWLGTSPLHLAAQYGHYSTAEVLLRAGVSRDARTKVDRTPLHMAAADGHVHIVELLVRSGADVNAKDMLQ 104
Cdd:COG0666     8 LLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGG 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1039764056 105 MTALHWATEHHHRDVVELLIKYGADVYAFSKFDKSAFDIAMEKNNTEILVMLQEA 159
Cdd:COG0666    88 NTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA 142
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 5-147 5.64e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 66.44  E-value: 5.64e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764056   5 DLGKRLLEAARKGQD-DEVRTLMANGA-PFTTDWLGTSPLHLAAQYGHYSTAEVLLRAGVSRDARTKVDRTPLHMAAAD- 81
Cdd:PHA02878  166 HKGNTALHYATENKDqRLTELLLSYGAnVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYc 245

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039764056  82 GHVHIVELLVRSGADVNAKD-MLQMTALHWATehHHRDVVELLIKYGADVYAFSKFDKSAFDIAMEK 147
Cdd:PHA02878  246 KDYDILKLLLEHGVDVNAKSyILGLTALHSSI--KSERKLKLLLEYGADINSLNSYKLTPLSSAVKQ 310
Ank_4 pfam13637
Ankyrin repeats (many copies);
72-124 8.92e-12

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 59.60  E-value: 8.92e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1039764056  72 RTPLHMAAADGHVHIVELLVRSGADVNAKDMLQMTALHWATEHHHRDVVELLI 124
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 22-155 3.34e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 64.28  E-value: 3.34e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764056  22 VRTLMANGA-PFTTDWLGTSPLHLAAQYGHYSTA--EVLLRAGVSRDARTKVDRTPLHMAAADGHVH--IVELLVRSGAD 96
Cdd:PHA03095  170 LRLLIDAGAdVYAVDDRFRSLLHHHLQSFKPRARivRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIAGIS 249

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039764056  97 VNAKDMLQMTALHWATEHHHRDVVELLIKYGADVYAFSKFDKSAFDIAMEKNNTEILVM 155
Cdd:PHA03095  250 INARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRA 308
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 14-169 3.85e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 64.31  E-value: 3.85e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764056  14 ARKGQDDE-VRTLMANGAPFT-TDWLGTSPLHLAAQYGHYS-TAEVLLRAGVSRDARTKVDRTPLHMAAADGHVHIVELL 90
Cdd:PHA02876  315 AKNGYDTEnIRTLIMLGADVNaADRLYITPLHQASTLDRNKdIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTL 394

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764056  91 VRSGADVNAKDMLQMTALHWA---TEHHHRdvVELLIKYGADVYAFSKFDKSAFDIAMEKN-NTEILVMLQE--AMQNQV 164
Cdd:PHA02876  395 LDYGADIEALSQKIGTALHFAlcgTNPYMS--VKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDngADVNAI 472


                  ....*
gi 1039764056 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 1.07e-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: 1.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764056  10 LLEAARKGQDDEVRTLMANGA--PFTTDWLGTSPLHLAAQYGHYSTAEVLLRAgvsrdARTKVD----------RTPLHM 77
Cdd:cd22192    21 LLLAAKENDVQAIKKLLKCPScdLFQRGALGETALHVAALYDNLEAAVVLMEA-----APELVNepmtsdlyqgETALHI 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764056  78 AAADGHVHIVELLVRSGADVNAKD------MLQMTALHWATEH--------HHRDVVELLIKYGADVYAFSKFDKSAFDI 143
Cdd:cd22192    96 AVVNQNLNLVRELIARGADVVSPRatgtffRPGPKNLIYYGEHplsfaacvGNEEIVRLLIEHGADIRAQDSLGNTVLHI 175

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1039764056 144 AMEKNNTEI------LVMLQEAMQNQVNTNH 168
Cdd:cd22192   176 LVLQPNKTFacqmydLILSYDKEDDLQPLDL 206
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 86-193 5.88e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 60.46  E-value: 5.88e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764056  86 IVELLVRSGADVNAKDMLQMTALHWATEHHHRDVVELLIKYGADVYAFSKFDKSAFDIAMEKNNTEILVMLQEAMQNQVN 165
Cdd:PHA02876  160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINK 239

                          90       100
                  ....*....|....*....|....*...
gi 1039764056 166 TNHERANPVANPVTVTAPFIFTSGEVIN 193
Cdd:PHA02876  240 NDLSLLKAIRNEDLETSLLLYDAGFSVN 267
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 43-133 6.23e-10

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 60.68  E-value: 6.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764056  43 HLAAQyGHYSTAEVLLRAGVSRDARTKVDRTPLHMAAADGHVHIVELLVRSGADVNAKDMLQMTALHWATEHHHRDVVEL 122
Cdd:PTZ00322   88 QLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166

                          90
                  ....*....|.
gi 1039764056 123 LIKYGADVYAF 133
Cdd:PTZ00322  167 LSRHSQCHFEL 177
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 22-132 7.16e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 60.06  E-value: 7.16e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764056  22 VRTLMANGAPFT-TDWLGTSPLHLAAQYGHYST--AEVLLRAGVSRDARTKVDR----------------TPLHMAAADG 82
Cdd:PHA03100  124 VEYLLDNGANVNiKNSDGENLLHLYLESNKIDLkiLKLLIDKGVDINAKNRVNYllsygvpinikdvygfTPLHYAVYNN 203

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039764056  83 HVHIVELLVRSGADVNAKDMLQMTALHWATEHHHRDVVELLIKYGADVYA 132
Cdd:PHA03100  204 NPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 22-134 1.72e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 58.74  E-value: 1.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764056  22 VRTLMANGAPFT--TDWLGTSPLHLAAQYGHYSTAEVLLRAGVSRDARTKVDRTPLHMAAADGHVHIVELLVRSGADVNA 99
Cdd:PHA02878  150 TKLLLSYGADINmkDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDA 229

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1039764056 100 KDMLQMTALHWATEH-HHRDVVELLIKYGADVYAFS 134
Cdd:PHA02878  230 RDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKS 265
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 23-167 1.81e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 58.52  E-value: 1.81e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764056  23 RTLMANGAPFTTDWLGTSPLHLAAQYGHYSTAEVLLRAGVSRDARTKVDRTPLHMAAADGHV-----HIVELLVRSGADV 97
Cdd:PHA03100   20 YIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANV 99

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039764056  98 NAKDMLQMTALHWATEHH--HRDVVELLIKYGADVYAFSKFDKSAFDIAME--KNNTEILVMLqeaMQNQVNTN 167
Cdd:PHA03100  100 NAPDNNGITPLLYAISKKsnSYSIVEYLLDNGANVNIKNSDGENLLHLYLEsnKIDLKILKLL---IDKGVDIN 170
Ank_4 pfam13637
Ankyrin repeats (many copies);
38-91 6.26e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.51  E-value: 6.26e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039764056  38 GTSPLHLAAQYGHYSTAEVLLRAGVSRDARTKVDRTPLHMAAADGHVHIVELLV 91
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
10-108 1.20e-08

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 55.73  E-value: 1.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764056  10 LLEAARKGQDDEVRTLMANGA-PFTTDWLGTSPLHLAAQYGHYSTAEVLLRAGVSRDARTKVDRTPLHMAAADGHVHIVE 88
Cdd:COG0666   190 LHLAAENGHLEIVKLLLEAGAdVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVK 269

                          90       100
                  ....*....|....*....|
gi 1039764056  89 LLVRSGADVNAKDMLQMTAL 108
Cdd:COG0666   270 LLLLALLLLAAALLDLLTLL 289
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 55-158 2.02e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 55.66  E-value: 2.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764056  55 EVLLRAGVSRDARTK-VDRTPLHMAAADGHVHIVELLVRSGADVNAKDMLQMTALHWATEHHHRDVVELLIKYGADVYAF 133
Cdd:PHA02878  151 KLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDAR 230

                          90       100
                  ....*....|....*....|....*.
gi 1039764056 134 SKFDKSAFDIAMEK-NNTEILVMLQE 158
Cdd:PHA02878  231 DKCGNTPLHISVGYcKDYDILKLLLE 256
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 70-156 2.06e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 55.67  E-value: 2.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764056  70 VDRTPLHMA-------AADGHVHIVELLVRSGADVNAKDMLQMTALHWATEHHHRDVVELLIKYGADVYAFSKFDKSAFD 142
Cdd:PTZ00322   74 IDPVVAHMLtvelcqlAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLE 153

                          90
                  ....*....|....
gi 1039764056 143 IAMEKNNTEILVML 156
Cdd:PTZ00322  154 LAEENGFREVVQLL 167
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 5-156 2.26e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 55.38  E-value: 2.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764056   5 DLGKRLLEAARKGQDDEVRTLMANGApFTTDWL---GTSPLHLAAQYGHYSTAEVLLRAGVSRDARTKVDRTPLHMAAAD 81
Cdd:PHA02875   67 DIESELHDAVEEGDVKAVEELLDLGK-FADDVFykdGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMM 145

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039764056  82 GHVHIVELLVRSGADVNAKDMLQMTALHWATEHHHRDVVELLIKYGADVYAFSKF-DKSAFDIAMEKNNTEILVML 156
Cdd:PHA02875  146 GDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNgCVAALCYAIENNKIDIVRLF 221
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 20-129 6.72e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 53.84  E-value: 6.72e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764056  20 DEVRTLMANGA-PFTTDWLGTSPLHLAAQYGHYSTAEVLLRAGVSRDARTKVDRTPLHMAAADGHVHIVELLVRSGADVN 98
Cdd:PHA02875  116 DIMKLLIARGAdPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANID 195

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1039764056  99 -AKDMLQMTALHWATEHHHRDVVELLIKYGAD 129
Cdd:PHA02875  196 yFGKNGCVAALCYAIENNKIDIVRLFIKRGAD 227
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 38-129 6.91e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 53.84  E-value: 6.91e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764056  38 GTSPLHLAAQYGHYSTAEVLLRAGVSRDARTKVDRTPLHMAAADGHVHIVELLVRSGA---DVNAKDmlQMTALHWATEH 114
Cdd:PHA02875   35 GISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKfadDVFYKD--GMTPLHLATIL 112

                          90
                  ....*....|....*
gi 1039764056 115 HHRDVVELLIKYGAD 129
Cdd:PHA02875  113 KKLDIMKLLIARGAD 127
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 72-101 2.52e-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: 46.51  E-value: 2.52e-07
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1039764056  72 RTPLHMAAAD-GHVHIVELLVRSGADVNAKD 101
Cdd:pfam00023   3 NTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
Ank_5 pfam13857
Ankyrin repeats (many copies);
89-144 2.98e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.96  E-value: 2.98e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039764056  89 LLVRSGADVNAKDMLQMTALHWATEHHHRDVVELLIKYGADVYAFSKFDKSAFDIA 144
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 10-128 3.70e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 51.50  E-value: 3.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764056  10 LLEAARKGQDDEVRTLMANGapfttdwLGTSPLHLAAQygHYSTAEVLLRAGVSRDARTKVDRTPLHMAAADGHVHIVEL 89
Cdd:PHA02874   72 LLTAIKIGAHDIIKLLIDNG-------VDTSILPIPCI--EKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKM 142

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1039764056  90 LVRSGADVNAKDMLQMTALHWATEHHHRDVVELLIKYGA 128
Cdd:PHA02874  143 LFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGA 181
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 13-124 3.90e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 51.50  E-value: 3.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764056  13 AARKGQDDEVRTLMANGAPFTT-DWLGTSPLHLAAQYGHYSTAEVLLRAGVSRDARTKVDRTPLHMAAADGHVHIVELLV 91
Cdd:PHA02874  131 AIKKGDLESIKMLFEYGADVNIeDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLI 210

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1039764056  92 RSGADVNAKDMLQMTALHWATeHHHRDVVELLI 124
Cdd:PHA02874  211 DHGNHIMNKCKNGFTPLHNAI-IHNRSAIELLI 242
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 6-92 4.88e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.44  E-value: 4.88e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764056   6 LGKRLLEAARKGQDDEVRTLMANGA-PFTTDWLGTSPLHLAAQYGHYSTAEVLLRAGVSRDARTKVDRTPLHMAAADGHV 84
Cdd:PTZ00322   82 LTVELCQLAASGDAVGARILLTGGAdPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFR 161


                  ....*...
gi 1039764056  85 HIVELLVR 92
Cdd:PTZ00322  162 EVVQLLSR 169
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 25-158 6.71e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 51.02  E-value: 6.71e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764056  25 LMANGAPFTTDWLGTSPLHLAAQYGHYSTAEVLLRAGVSRDARTKVDRTPLHMAAADGHVHIVELL-------------- 90
Cdd:PLN03192  545 LKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILyhfasisdphaagd 624

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764056  91 -----------------VRSGADVNAKDMLQMTALHWATEHHHRDVVELLIKYGADVyafskfDKSAFDIAMekNNTEIL 153
Cdd:PLN03192  625 llctaakrndltamkelLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV------DKANTDDDF--SPTELR 696


                  ....*
gi 1039764056 154 VMLQE 158
Cdd:PLN03192  697 ELLQK 701
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 8-128 7.13e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 51.02  E-value: 7.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764056   8 KRLLEAARKGQDDEVRTLMANGAPFTTDWLGTSPLHLAAQYGHYSTAEVLLRAGVSRDARTKVDRTPLHMAAADGHVHIV 87
Cdd:PLN03192  495 KNFLQHHKELHDLNVGDLLGDNGGEHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCV 574

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1039764056  88 ELLVRSGADVNAKDMLQMTALHWATEHHHRDVVELLIKYGA 128
Cdd:PLN03192  575 LVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFAS 615
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 54-124 1.09e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 50.45  E-value: 1.09e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039764056  54 AEVLLRAGVSRDARTKVDRTPLHMAAADGHVHIVELLVRSGADVNAKDMLQMTALHWATEHHHRDVVELLI 124
Cdd:PHA02876  161 AEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAII 231
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 71-99 1.29e-06

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: 44.12  E-value: 1.29e-06
                           10        20
                   ....*....|....*....|....*....
gi 1039764056   71 DRTPLHMAAADGHVHIVELLVRSGADVNA 99
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
104-156 1.75e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.57  E-value: 1.75e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1039764056 104 QMTALHWATEHHHRDVVELLIKYGADVYAFSKFDKSAFDIAMEKNNTEILVML 156
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 3-109 6.50e-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: 6.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764056   3 LVDLGKRLLEAARKGQDDEVRTL---------------MANGAPFTTDWLGTSPLHLAAQYGHYSTAEVLLRAGVSRDAR 67
Cdd:TIGR00870  78 RGAVGDTLLHAISLEYVDAVEAIllhllaafrksgpleLANDQYTSEFTPGITALHLAAHRQNYEIVKLLLERGASVPAR 157

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039764056  68 TKVD--------------RTPLHMAAADGHVHIVELLVRSGADVNAKDMLQMTALH 109
Cdd:TIGR00870 158 ACGDffvksqgvdsfyhgESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLH 213
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 22-130 1.14e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 46.98  E-value: 1.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764056  22 VRTLMANGAPFT--TDWLGTSpLHLAAqYGH--YSTAEVLLRAGVSRDARTKVDRTPLHMAAADG-HVHIVELLVRSGAD 96
Cdd:PHA02876  391 INTLLDYGADIEalSQKIGTA-LHFAL-CGTnpYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGAD 468

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1039764056  97 VNAKDMLQMTALHWATEHHhrDVVELLIKYGADV 130
Cdd:PHA02876  469 VNAINIQNQYPLLIALEYH--GIVNILLHYGAEL 500
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 72-99 1.30e-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: 1.30e-05
                          10        20
                  ....*....|....*....|....*...
gi 1039764056  72 RTPLHMAAADGHVHIVELLVRSGADVNA 99
Cdd:pfam13606   3 NTPLHLAARNGRLEIVKLLLENGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 105-132 2.00e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.03  E-value: 2.00e-05
                           10        20
                   ....*....|....*....|....*...
gi 1039764056  105 MTALHWATEHHHRDVVELLIKYGADVYA 132
Cdd:smart00248   3 RTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 10-168 3.44e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 45.34  E-value: 3.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764056  10 LLEAARKGQDDEVRTLMANGApfTTDWLGTS---PLHLAAQYGHYSTAEVLLRAGVSrdarTKVDRTPlhmaaaDGHVHI 86
Cdd:PHA02874   39 LIDAIRSGDAKIVELFIKHGA--DINHINTKiphPLLTAIKIGAHDIIKLLIDNGVD----TSILPIP------CIEKDM 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764056  87 VELLVRSGADVNAKDMLQMTALHWATEHHHRDVVELLIKYGADVYAFSKFDKSAFDIAMEKNNTEIL-VMLQEAMQNQVN 165
Cdd:PHA02874  107 IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIkLLLEKGAYANVK 186


                  ...
gi 1039764056 166 TNH 168
Cdd:PHA02874  187 DNN 189
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 20-101 6.31e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 44.66  E-value: 6.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764056  20 DEVRTLMANGAPF-TTDWLGTSPLHLAAQYGHYSTAEVLLRAGVSRDARTKVDRTPLHMAAADGHVHIVELLVRSGADVN 98
Cdd:PHA03100  173 NRVNYLLSYGVPInIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252


                  ...
gi 1039764056  99 AKD 101
Cdd:PHA03100  253 TII 255
PHA03095 PHA03095
ankyrin-like protein; Provisional
 77-156 6.40e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 44.63  E-value: 6.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764056  77 MAAADGHVHIVELLVRSGADVNAKDMLQMTALHW--ATEHHHR-DVVELLIKYGADVYAFSKFDKSAFDIAMEKNNTEIL 153
Cdd:PHA03095   20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHLylHYSSEKVkDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDV 99


                  ...
gi 1039764056 154 VML 156
Cdd:PHA03095  100 IKL 102
Ank_4 pfam13637
Ankyrin repeats (many copies);
10-58 1.36e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.18  E-value: 1.36e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039764056  10 LLEAARKGQDDEVRTLMANGAPF-TTDWLGTSPLHLAAQYGHYSTAEVLL 58
Cdd:pfam13637   5 LHAAAASGHLELLRLLLEKGADInAVDGNGETALHFAASNGNVEVLKLLL 54
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 105-132 1.39e-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: 38.81  E-value: 1.39e-04
                          10        20
                  ....*....|....*....|....*....
gi 1039764056 105 MTALHWATEHH-HRDVVELLIKYGADVYA 132
Cdd:pfam00023   3 NTPLHLAAGRRgNLEIVKLLLSKGADVNA 31
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 105-132 1.44e-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: 1.44e-04
                          10        20
                  ....*....|....*....|....*...
gi 1039764056 105 MTALHWATEHHHRDVVELLIKYGADVYA 132
Cdd:pfam13606   3 NTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_2 pfam12796
Ankyrin repeats (3 copies);
108-168 1.57e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 40.10  E-value: 1.57e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039764056 108 LHWATEHHHRDVVELLIKYGADVYAFSKFDKSAFDIAMEKNNTEIL-VMLQEAMQNQVNTNH 168
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVkLLLEHADVNLKDNGR 62
PHA02741 PHA02741
hypothetical protein; Provisional
 84-158 4.40e-04

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 40.41  E-value: 4.40e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039764056  84 VHIVELLVRSGADVNAKDMLQ-MTALHWATEHHHRDVVELLIKY-GADVYAFSKFDKSAFDIAMEKNNTEILVMLQE 158
Cdd:PHA02741   77 AEIIDHLIELGADINAQEMLEgDTALHLAAHRRDHDLAEWLCCQpGIDLHFCNADNKSPFELAIDNEDVAMMQILRE 153
Ank_5 pfam13857
Ankyrin repeats (many copies);
30-78 4.87e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.71  E-value: 4.87e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1039764056  30 APFTTDWLGTSPLHLAAQYGHYSTAEVLLRAGVSRDARTKVDRTPLHMA 78
Cdd:pfam13857   8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 18-167 4.95e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 41.87  E-value: 4.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764056  18 QDDEVRTLMANGAPFTT-DWLGTSPLHLAAQYGHYSTAEVLLRAGVSRDARTKVDRTPLHMAAADGHVHIVELLVRSGAD 96
Cdd:PHA02874  103 EKDMIKTILDCGIDVNIkDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAY 182

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039764056  97 VNAKDMLQMTALHWATEHHHRDVVELLIKYGADVYAFSKFDKSAFDIAMEKNNTEILVMLQEAMQNQVNTN 167
Cdd:PHA02874  183 ANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAIELLINNASINDQDID 253
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 38-69 7.86e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.50  E-value: 7.86e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1039764056  38 GTSPLHLAA-QYGHYSTAEVLLRAGVSRDARTK 69
Cdd:pfam00023   2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PHA02946 PHA02946
ankyin-like protein; Provisional
 16-98 2.03e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 40.04  E-value: 2.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764056  16 KGQDDE-VRTLMANG-APFTTDWLGTSPLHLAAQYGHYSTAEVLLRAGVSRDARTKVDRTPLHMAAA--DGHVHIVELLV 91
Cdd:PHA02946   48 KGLDERfVEELLHRGySPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGtdDEVIERINLLV 127


                  ....*..
gi 1039764056  92 RSGADVN 98
Cdd:PHA02946  128 QYGAKIN 134
PHA02743 PHA02743
Viral ankyrin protein; Provisional
 55-128 2.18e-03

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 38.26  E-value: 2.18e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039764056  55 EVLLRAGVSRDAR-TKVDRTPLHMAAADGHVHIVELLVRS-GADVNAKDMLQMTALHWATEHHHRDVVELLIKYGA 128
Cdd:PHA02743   77 ELLVNMGADINAReLGTGNTLLHIAASTKNYELAEWLCRQlGVNLGAINYQHETAYHIAYKMRDRRMMEILRANGA 152
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 2-135 2.84e-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: 2.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764056   2 SLVDLGKRLLEAARKGQDDEVRTLMANGAPF---TTDWLGTSPLHLAAQYG-HYSTAEVLLragvSRDARTKVDRTPLHm 77
Cdd:TIGR00870  13 PLSDEEKAFLPAAERGDLASVYRDLEEPKKLninCPDRLGRSALFVAAIENeNLELTELLL----NLSCRGAVGDTLLH- 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039764056  78 AAADGHVHIVELLVRSGADVNAKDM-LQM-------------TALHWATEHHHRDVVELLIKYGADVYAFSK 135
Cdd:TIGR00870  88 AISLEYVDAVEAILLHLLAAFRKSGpLELandqytseftpgiTALHLAAHRQNYEIVKLLLERGASVPARAC 159
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 53-185 2.85e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 39.66  E-value: 2.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764056  53 TAEVLLRAGVSRDARTKVDRTPLHMAA-ADGHVHIVELLVRSGADVNAK------------------------------- 100
Cdd:PHA02876  255 TSLLLYDAGFSVNSIDDCKNTPLHHASqAPSLSRLVPKLLERGADVNAKnikgetplylmakngydtenirtlimlgadv 334

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764056 101 ---DMLQMTALHWA-TEHHHRDVVELLIKYGADVYAFSKFDKSAFDIAMEKNNTEILVMLQ------EAMQNQVNTNHER 170
Cdd:PHA02876  335 naaDRLYITPLHQAsTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLdygadiEALSQKIGTALHF 414

                         170
                  ....*....|....*
gi 1039764056 171 ANPVANPVTVTAPFI 185
Cdd:PHA02876  415 ALCGTNPYMSVKTLI 429
PHA02946 PHA02946
ankyin-like protein; Provisional
 55-130 2.96e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 39.27  E-value: 2.96e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039764056  55 EVLLRAGVSRDARTKVDRTPLHMAAADGHVHIVELLVRSGADVNAKDMLQMTALHW--ATEHHHRDVVELLIKYGADV 130
Cdd:PHA02946   56 EELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYlsGTDDEVIERINLLVQYGAKI 133
Ank_5 pfam13857
Ankyrin repeats (many copies);
57-111 6.31e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 34.63  E-value: 6.31e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039764056  57 LLRAG-VSRDARTKVDRTPLHMAAADGHVHIVELLVRSGADVNAKDMLQMTALHWA 111
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02791 PHA02791
ankyrin-like protein; Provisional
 18-153 6.52e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 37.71  E-value: 6.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039764056  18 QDDEVRTLMANGAPFTTDWLGTSPLHLAAQYGHYSTAEVLLRAGVSRDARTkvDRTPLHMAAADGHVHIVELLVRSGADV 97
Cdd:PHA02791   10 KSKQLKSFLSSKDAFKADVHGHSALYYAIADNNVRLVCTLLNAGALKNLLE--NEFPLHQAATLEDTKIVKILLFSGMDD 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039764056  98 NAKDMLQMTALHWATEHHHRDVVELLIKYGADVYAFSKFD-KSAFDIAMEKNNTEIL 153
Cdd:PHA02791   88 SQFDDKGNTALYYAVDSGNMQTVKLFVKKNWRLMFYGKTGwKTSFYHAVMLNDVSIV 144
 
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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