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Conserved domains on  [gi|1021589237|ref|NP_001310838|]
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GA-binding protein subunit beta-2 isoform d [Homo sapiens]

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 7.80e-44

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 154.34  E-value: 7.80e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589237  10 LLEAARKGQDDEVRTLMANGA-PFTTDWLGTSPLHLAAQYGHYSTAEVLLRAGVSRDARTKVDRTPLHMAAADGHAHIVE 88
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGAdVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589237  89 LLVRNGADVNAKDMLKMTALHWATERHHRDVVELLIKYGADVHAFSKFDKSAFDIALEKNNAEILVILQEAMQNQVNVNP 168
Cdd:COG0666   171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250


                  ....*
gi 1021589237 169 ERANP 173
Cdd:COG0666   251 DGLTA 255
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
10-173 7.80e-44

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 154.34  E-value: 7.80e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589237  10 LLEAARKGQDDEVRTLMANGA-PFTTDWLGTSPLHLAAQYGHYSTAEVLLRAGVSRDARTKVDRTPLHMAAADGHAHIVE 88
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGAdVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589237  89 LLVRNGADVNAKDMLKMTALHWATERHHRDVVELLIKYGADVHAFSKFDKSAFDIALEKNNAEILVILQEAMQNQVNVNP 168
Cdd:COG0666   171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250


                  ....*
gi 1021589237 169 ERANP 173
Cdd:COG0666   251 DGLTA 255
Ank_2 pfam12796
Ankyrin repeats (3 copies);
42-132 5.72e-24

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 94.80  E-value: 5.72e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589237  42 LHLAAQYGHYSTAEVLLRAGVSRDARTKVDRTPLHMAAADGHAHIVELLVRNgADVNAKDMlKMTALHWATERHHRDVVE 121
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78

                          90
                  ....*....|.
gi 1021589237 122 LLIKYGADVHA 132
Cdd:pfam12796  79 LLLEKGADINV 89
PHA03095 PHA03095
ankyrin-like protein; Provisional
 20-153 1.63e-17

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 83.92  E-value: 1.63e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589237  20 DEVRTLMANGAPF-TTDWLGTSPLHLAAQYGhySTAEV---LLRAGVSRDARTKVDRTPLH--MAAADGHAHIVELLVRN 93
Cdd:PHA03095   64 DIVRLLLEAGADVnAPERCGFTPLHLYLYNA--TTLDViklLIKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRK 141

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1021589237  94 GADVNAKDMLKMTALHWATERHHRDV--VELLIKYGADVHAFSKFDKSAFDIALE--KNNAEIL 153
Cdd:PHA03095  142 GADVNALDLYGMTPLAVLLKSRNANVelLRLLIDAGADVYAVDDRFRSLLHHHLQsfKPRARIV 205
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 10-132 5.98e-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: 61.18  E-value: 5.98e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589237  10 LLEAARKGQDDEVRTLMANGA--PFTTDWLGTSPLHLAAQYGHYSTAEVLLRAgvsrdARTKVD----------RTPLHM 77
Cdd:cd22192    21 LLLAAKENDVQAIKKLLKCPScdLFQRGALGETALHVAALYDNLEAAVVLMEA-----APELVNepmtsdlyqgETALHI 95

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1021589237  78 AAADGHAHIVELLVRNGADV------------NAKDMLKMT--ALHWATERHHRDVVELLIKYGADVHA 132
Cdd:cd22192    96 AVVNQNLNLVRELIARGADVvspratgtffrpGPKNLIYYGehPLSFAACVGNEEIVRLLIEHGADIRA 164
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 3-109 6.13e-07

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: 51.62  E-value: 6.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589237   3 LVDLGKRLLEAARKGQDDEVRTL---------------MANGAPFTTDWLGTSPLHLAAQYGHYSTAEVLLRAGVSRDAR 67
Cdd:TIGR00870  78 RGAVGDTLLHAISLEYVDAVEAIllhllaafrksgpleLANDQYTSEFTPGITALHLAAHRQNYEIVKLLLERGASVPAR 157

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1021589237  68 TKVD--------------RTPLHMAAADGHAHIVELLVRNGADVNAKDMLKMTALH 109
Cdd:TIGR00870 158 ACGDffvksqgvdsfyhgESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLH 213
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 71-99 7.10e-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: 45.27  E-value: 7.10e-07
                           10        20
                   ....*....|....*....|....*....
gi 1021589237   71 DRTPLHMAAADGHAHIVELLVRNGADVNA 99
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
10-173 7.80e-44

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 154.34  E-value: 7.80e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589237  10 LLEAARKGQDDEVRTLMANGA-PFTTDWLGTSPLHLAAQYGHYSTAEVLLRAGVSRDARTKVDRTPLHMAAADGHAHIVE 88
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGAdVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589237  89 LLVRNGADVNAKDMLKMTALHWATERHHRDVVELLIKYGADVHAFSKFDKSAFDIALEKNNAEILVILQEAMQNQVNVNP 168
Cdd:COG0666   171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250


                  ....*
gi 1021589237 169 ERANP 173
Cdd:COG0666   251 DGLTA 255
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
10-172 8.50e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 133.16  E-value: 8.50e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589237  10 LLEAARKGQDDEVRTLMANGA-PFTTDWLGTSPLHLAAQYGHYSTAEVLLRAGVSRDARTKVDRTPLHMAAADGHAHIVE 88
Cdd:COG0666   124 LHLAAYNGNLEIVKLLLEAGAdVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVK 203

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589237  89 LLVRNGADVNAKDMLKMTALHWATERHHRDVVELLIKYGADVHAFSKFDKSAFDIALEKNNAEILVILQEAMQNQVNVNP 168
Cdd:COG0666   204 LLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283


                  ....
gi 1021589237 169 ERAN 172
Cdd:COG0666   284 DLLT 287
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
5-159 2.26e-34

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 129.30  E-value: 2.26e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589237   5 DLGKRLLEAARKGQDDEVRTLMANGAPF--TTDWLGTSPLHLAAQYGHYSTAEVLLRAGVSRDARTKVDRTPLHMAAADG 82
Cdd:COG0666    52 ALGALLLLAAALAGDLLVALLLLAAGADinAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNG 131

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1021589237  83 HAHIVELLVRNGADVNAKDMLKMTALHWATERHHRDVVELLIKYGADVHAFSKFDKSAFDIALEKNNAEILVILQEA 159
Cdd:COG0666   132 NLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA 208
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
8-156 1.33e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 102.34  E-value: 1.33e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589237   8 KRLLEAARKGQDDEVRTLMANGAPFTTDWLGTSPLHLAAQYGHYSTAEVLLRAGVSRDARTKVDRTPLHMAAADGHAHIV 87
Cdd:COG0666    24 LLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIV 103

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1021589237  88 ELLVRNGADVNAKDMLKMTALHWATERHHRDVVELLIKYGADVHAFSKFDKSAFDIALEKNNAEILVIL 156
Cdd:COG0666   104 KLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLL 172
Ank_2 pfam12796
Ankyrin repeats (3 copies);
42-132 5.72e-24

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 94.80  E-value: 5.72e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589237  42 LHLAAQYGHYSTAEVLLRAGVSRDARTKVDRTPLHMAAADGHAHIVELLVRNgADVNAKDMlKMTALHWATERHHRDVVE 121
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78

                          90
                  ....*....|.
gi 1021589237 122 LLIKYGADVHA 132
Cdd:pfam12796  79 LLLEKGADINV 89
PHA03095 PHA03095
ankyrin-like protein; Provisional
 20-153 1.63e-17

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 83.92  E-value: 1.63e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589237  20 DEVRTLMANGAPF-TTDWLGTSPLHLAAQYGhySTAEV---LLRAGVSRDARTKVDRTPLH--MAAADGHAHIVELLVRN 93
Cdd:PHA03095   64 DIVRLLLEAGADVnAPERCGFTPLHLYLYNA--TTLDViklLIKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRK 141

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1021589237  94 GADVNAKDMLKMTALHWATERHHRDV--VELLIKYGADVHAFSKFDKSAFDIALE--KNNAEIL 153
Cdd:PHA03095  142 GADVNALDLYGMTPLAVLLKSRNANVelLRLLIDAGADVYAVDDRFRSLLHHHLQsfKPRARIV 205
Ank_2 pfam12796
Ankyrin repeats (3 copies);
10-101 3.42e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 76.31  E-value: 3.42e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589237  10 LLEAARKGQDDEVRTLMANGA-PFTTDWLGTSPLHLAAQYGHYSTAEVLLRAGVSRDarTKVDRTPLHMAAADGHAHIVE 88
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGAdANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1021589237  89 LLVRNGADVNAKD 101
Cdd:pfam12796  79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
75-156 9.47e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 69.37  E-value: 9.47e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589237  75 LHMAAADGHAHIVELLVRNGADVNAKDMLKMTALHWATERHHRDVVELLIKYgADVHAFSKfDKSAFDIALEKNNAEILV 154
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78


                  ..
gi 1021589237 155 IL 156
Cdd:pfam12796  79 LL 80
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
25-159 2.44e-13

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 69.98  E-value: 2.44e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589237  25 LMANGAPFTTDWLGTSPLHLAAQYGHYSTAEVLLRAGVSRDARTKVDRTPLHMAAADGHAHIVELLVRNGADVNAKDMLK 104
Cdd:COG0666     8 LLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGG 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1021589237 105 MTALHWATERHHRDVVELLIKYGADVHAFSKFDKSAFDIALEKNNAEILVILQEA 159
Cdd:COG0666    88 NTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA 142
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 22-156 4.81e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 70.08  E-value: 4.81e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589237  22 VRTLMANGAPFT-TDWLGTSPLHLAAQY--GHYSTAEVLLRAGVSRDARTKVDRTPLHMAAADGHA--HIVELLVRNGAD 96
Cdd:PHA03100   89 VKLLLEYGANVNaPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVD 168

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1021589237  97 VNAKDMLKM----------------TALHWATERHHRDVVELLIKYGADVHAFSKFDKSAFDIALEKNNAEILVIL 156
Cdd:PHA03100  169 INAKNRVNYllsygvpinikdvygfTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLL 244
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 5-147 4.37e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 67.60  E-value: 4.37e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589237   5 DLGKRLLEAARKGQD-DEVRTLMANGA-PFTTDWLGTSPLHLAAQYGHYSTAEVLLRAGVSRDARTKVDRTPLHMAAADG 82
Cdd:PHA02878  166 HKGNTALHYATENKDqRLTELLLSYGAnVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYC 245

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1021589237  83 HAH-IVELLVRNGADVNAKD-MLKMTALHWATerHHRDVVELLIKYGADVHAFSKFDKSAFDIALEK 147
Cdd:PHA02878  246 KDYdILKLLLEHGVDVNAKSyILGLTALHSSI--KSERKLKLLLEYGADINSLNSYKLTPLSSAVKQ 310
PHA03095 PHA03095
ankyrin-like protein; Provisional
 22-153 2.56e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 65.05  E-value: 2.56e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589237  22 VRTLMANGA-PFTTDWLGTSPLHLAAQYGHYSTA--EVLLRAGVSRDARTKVDRTPLHMAAADG--HAHIVELLVRNGAD 96
Cdd:PHA03095  170 LRLLIDAGAdVYAVDDRFRSLLHHHLQSFKPRARivRELIRAGCDPAATDMLGNTPLHSMATGSscKRSLVLPLLIAGIS 249

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1021589237  97 VNAKDMLKMTALHWATERHHRDVVELLIKYGADVHAFSKFDKSAFDIALEKNNAEIL 153
Cdd:PHA03095  250 INARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAV 306
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 22-181 2.65e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 64.90  E-value: 2.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589237  22 VRTLMANGAPFT--TDWLGTSPLHLAAQYGHYSTAEVLLRAGVSRDARTKVDRTPLHMAAADGHAHIVELLVRNGADVNA 99
Cdd:PHA02878  150 TKLLLSYGADINmkDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDA 229

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589237 100 KDMLKMTALHWATER-HHRDVVELLIKYGADVHAFSKF-DKSAFDIALEKNNAEILVILQEAMQNQVNVNPEranpvtDP 177
Cdd:PHA02878  230 RDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYIlGLTALHSSIKSERKLKLLLEYGADINSLNSYKL------TP 303


                  ....
gi 1021589237 178 VSMA 181
Cdd:PHA02878  304 LSSA 307
Ank_4 pfam13637
Ankyrin repeats (many copies);
72-124 3.15e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.05  E-value: 3.15e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1021589237  72 RTPLHMAAADGHAHIVELLVRNGADVNAKDMLKMTALHWATERHHRDVVELLI 124
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 38-149 1.16e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 63.54  E-value: 1.16e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589237  38 GTSPLHLAAQYGhYSTAEV--LLRAGVSRDARTKVDRTPLHMAAA-DGHAHIVELLVRNGADVNAKDMLKMTALHWATER 114
Cdd:PHA02876  307 GETPLYLMAKNG-YDTENIrtLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVR 385

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1021589237 115 HHRDVVELLIKYGADVHAFSKFDKSAFDIALEKNN 149
Cdd:PHA02876  386 NNVVIINTLLDYGADIEALSQKIGTALHFALCGTN 420
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 23-167 1.62e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 62.38  E-value: 1.62e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589237  23 RTLMANGAPFTTDWLGTSPLHLAAQYGHYSTAEVLLRAGVSRDARTKVDRTPLHMAAADGHA-----HIVELLVRNGADV 97
Cdd:PHA03100   20 YIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANV 99

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1021589237  98 NAKDMLKMTALHWA--TERHHRDVVELLIKYGADVHAFSKFDKSAFDIALEKNNAEiLVILQEAMQNQVNVN 167
Cdd:PHA03100  100 NAPDNNGITPLLYAisKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKID-LKILKLLIDKGVDIN 170
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 14-146 2.60e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 62.39  E-value: 2.60e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589237  14 ARKGQDDE-VRTLMANGAPFT-TDWLGTSPLHLAAQYGHYS-TAEVLLRAGVSRDARTKVDRTPLHMAAADGHAHI---- 86
Cdd:PHA02876  315 AKNGYDTEnIRTLIMLGADVNaADRLYITPLHQASTLDRNKdIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIintl 394

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589237  87 ------------------------------VELLVRNGADVNAKDMLKMTALHWATERHHR-DVVELLIKYGADVHAFSK 135
Cdd:PHA02876  395 ldygadiealsqkigtalhfalcgtnpymsVKTLIDRGANVNSKNKDLSTPLHYACKKNCKlDVIEMLLDNGADVNAINI 474

                         170
                  ....*....|.
gi 1021589237 136 FDKSAFDIALE 146
Cdd:PHA02876  475 QNQYPLLIALE 485
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 86-167 3.51e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 62.00  E-value: 3.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589237  86 IVELLVRNGADVNAKDMLKMTALHWATERHHRDVVELLIKYGADVHAFSKFDKSAFDIALEKNNAEilvILQEAMQNQVN 165
Cdd:PHA02876  160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNID---TIKAIIDNRSN 236


                  ..
gi 1021589237 166 VN 167
Cdd:PHA02876  237 IN 238
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 40-156 4.37e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 61.62  E-value: 4.37e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589237  40 SPLHLAAQYGHYST-AEVLLRAGVSRDARTKVDRTPLHMAAADGH-AHIVELLVRNGADVNAKDMLKMTALHWA-TERHH 116
Cdd:PHA02876  275 TPLHHASQAPSLSRlVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQAsTLDRN 354

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1021589237 117 RDVVELLIKYGADVHAFSKFDKSAFDIALEKNNAEILVIL 156
Cdd:PHA02876  355 KDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTL 394
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 10-132 5.98e-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: 61.18  E-value: 5.98e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589237  10 LLEAARKGQDDEVRTLMANGA--PFTTDWLGTSPLHLAAQYGHYSTAEVLLRAgvsrdARTKVD----------RTPLHM 77
Cdd:cd22192    21 LLLAAKENDVQAIKKLLKCPScdLFQRGALGETALHVAALYDNLEAAVVLMEA-----APELVNepmtsdlyqgETALHI 95

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1021589237  78 AAADGHAHIVELLVRNGADV------------NAKDMLKMT--ALHWATERHHRDVVELLIKYGADVHA 132
Cdd:cd22192    96 AVVNQNLNLVRELIARGADVvspratgtffrpGPKNLIYYGehPLSFAACVGNEEIVRLLIEHGADIRA 164
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
10-108 6.86e-10

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 59.58  E-value: 6.86e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589237  10 LLEAARKGQDDEVRTLMANGA-PFTTDWLGTSPLHLAAQYGHYSTAEVLLRAGVSRDARTKVDRTPLHMAAADGHAHIVE 88
Cdd:COG0666   190 LHLAAENGHLEIVKLLLEAGAdVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVK 269

                          90       100
                  ....*....|....*....|
gi 1021589237  89 LLVRNGADVNAKDMLKMTAL 108
Cdd:COG0666   270 LLLLALLLLAAALLDLLTLL 289
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 43-133 1.12e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 60.30  E-value: 1.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589237  43 HLAAQyGHYSTAEVLLRAGVSRDARTKVDRTPLHMAAADGHAHIVELLVRNGADVNAKDMLKMTALHWATERHHRDVVEL 122
Cdd:PTZ00322   88 QLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166

                          90
                  ....*....|.
gi 1021589237 123 LIKYGADVHAF 133
Cdd:PTZ00322  167 LSRHSQCHFEL 177
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 70-183 2.86e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 59.14  E-value: 2.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589237  70 VDRTPLHMA-------AADGHAHIVELLVRNGADVNAKDMLKMTALHWATERHHRDVVELLIKYGADVHAFSKFDKSAFD 142
Cdd:PTZ00322   74 IDPVVAHMLtvelcqlAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLE 153

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1021589237 143 IALEKNNAEILVIL----QEAMQNQVNVNPERANPV-----TDPVSMAAP 183
Cdd:PTZ00322  154 LAEENGFREVVQLLsrhsQCHFELGANAKPDSFTGKppsleDSPISSHHP 203
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 84-167 6.53e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 57.58  E-value: 6.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589237  84 AHIVELLVRNGADVNAKDMLKM-TALHWATERHHRDVVELLIKYGADVHAFSKFDKSAFDIALEKNNAEILVILqeaMQN 162
Cdd:PHA02878  147 AEITKLLLSYGADINMKDRHKGnTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHIL---LEN 223


                  ....*
gi 1021589237 163 QVNVN 167
Cdd:PHA02878  224 GASTD 228
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 22-130 6.82e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 57.37  E-value: 6.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589237  22 VRTLMANGAPFT-TDWLGTSPLHLAAQYGHYST--AEVLLRAGVSRDARTKVDR----------------TPLHMAAADG 82
Cdd:PHA03100  124 VEYLLDNGANVNiKNSDGENLLHLYLESNKIDLkiLKLLIDKGVDINAKNRVNYllsygvpinikdvygfTPLHYAVYNN 203

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1021589237  83 HAHIVELLVRNGADVNAKDMLKMTALHWATERHHRDVVELLIKYGADV 130
Cdd:PHA03100  204 NPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSI 251
Ank_4 pfam13637
Ankyrin repeats (many copies);
38-91 8.79e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.12  E-value: 8.79e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1021589237  38 GTSPLHLAAQYGHYSTAEVLLRAGVSRDARTKVDRTPLHMAAADGHAHIVELLV 91
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 8-197 2.72e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 56.03  E-value: 2.72e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589237   8 KRLLEAARKGQDDEVRTLMANGAPFTTDWLGTSPLHLAAQYGHYSTAEVLLRAGVSRDARTKVDRTPLHMAAADGHAHIV 87
Cdd:PLN03192  495 KNFLQHHKELHDLNVGDLLGDNGGEHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCV 574

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589237  88 ELLVRNGADVNAKDMLKMTALHWATERHHRDVVELLIKYGA--DVHAfskfdksAFDIALEKNNAEILVILQEAMQNQVN 165
Cdd:PLN03192  575 LVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASisDPHA-------AGDLLCTAAKRNDLTAMKELLKQGLN 647

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1021589237 166 VNPERANPVTD-PVSMA------APFIFTSGEVVNLASL 197
Cdd:PLN03192  648 VDSEDHQGATAlQVAMAedhvdmVRLLIMNGADVDKANT 686
Ank_5 pfam13857
Ankyrin repeats (many copies);
89-144 4.21e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 49.27  E-value: 4.21e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1021589237  89 LLVRNGADVNAKDMLKMTALHWATERHHRDVVELLIKYGADVHAFSKFDKSAFDIA 144
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 5-156 9.19e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 53.84  E-value: 9.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589237   5 DLGKRLLEAARKGQDDEVRTLMANGApFTTDWL---GTSPLHLAAQYGHYSTAEVLLRAGVSRDARTKVDRTPLHMAAAD 81
Cdd:PHA02875   67 DIESELHDAVEEGDVKAVEELLDLGK-FADDVFykdGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMM 145

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1021589237  82 GHAHIVELLVRNGADVNAKDMLKMTALHWATERHHRDVVELLIKYGADVHAFSKF-DKSAFDIALEKNNAEILVIL 156
Cdd:PHA02875  146 GDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNgCVAALCYAIENNKIDIVRLF 221
PHA03095 PHA03095
ankyrin-like protein; Provisional
 22-125 9.55e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 53.88  E-value: 9.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589237  22 VRTLMANGA-PFTTDWLGTSPLHLAAQYGHYSTAEV--LLRAGVSRDARTKVDRTPLHMAAADGHAHIVELLVRNGADVN 98
Cdd:PHA03095  205 VRELIRAGCdPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADIN 284

                          90       100
                  ....*....|....*....|....*..
gi 1021589237  99 AKDMLKMTALHWATERHHRDVVELLIK 125
Cdd:PHA03095  285 AVSSDGNTPLSLMVRNNNGRAVRAALA 311
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 72-101 9.77e-08

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: 47.67  E-value: 9.77e-08
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1021589237  72 RTPLHMAAAD-GHAHIVELLVRNGADVNAKD 101
Cdd:pfam00023   3 NTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 13-124 1.13e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 53.43  E-value: 1.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589237  13 AARKGQDDEVRTLMANGAPFTT-DWLGTSPLHLAAQYGHYSTAEVLLRAGVSRDARTKVDRTPLHMAAADGHAHIVELLV 91
Cdd:PHA02874  131 AIKKGDLESIKMLFEYGADVNIeDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLI 210

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1021589237  92 RNGADVNAKDMLKMTALHWATeRHHRDVVELLI 124
Cdd:PHA02874  211 DHGNHIMNKCKNGFTPLHNAI-IHNRSAIELLI 242
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 6-92 2.08e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.98  E-value: 2.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589237   6 LGKRLLEAARKGQDDEVRTLMANGA-PFTTDWLGTSPLHLAAQYGHYSTAEVLLRAGVSRDARTKVDRTPLHMAAADGHA 84
Cdd:PTZ00322   82 LTVELCQLAASGDAVGARILLTGGAdPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFR 161


                  ....*...
gi 1021589237  85 HIVELLVR 92
Cdd:PTZ00322  162 EVVQLLSR 169
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 3-109 6.13e-07

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: 51.62  E-value: 6.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589237   3 LVDLGKRLLEAARKGQDDEVRTL---------------MANGAPFTTDWLGTSPLHLAAQYGHYSTAEVLLRAGVSRDAR 67
Cdd:TIGR00870  78 RGAVGDTLLHAISLEYVDAVEAIllhllaafrksgpleLANDQYTSEFTPGITALHLAAHRQNYEIVKLLLERGASVPAR 157

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1021589237  68 TKVD--------------RTPLHMAAADGHAHIVELLVRNGADVNAKDMLKMTALH 109
Cdd:TIGR00870 158 ACGDffvksqgvdsfyhgESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLH 213
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 54-124 6.37e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 51.60  E-value: 6.37e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1021589237  54 AEVLLRAGVSRDARTKVDRTPLHMAAADGHAHIVELLVRNGADVNAKDMLKMTALHWATERHHRDVVELLI 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 7.10e-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: 45.27  E-value: 7.10e-07
                           10        20
                   ....*....|....*....|....*....
gi 1021589237   71 DRTPLHMAAADGHAHIVELLVRNGADVNA 99
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 20-129 7.16e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 51.15  E-value: 7.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589237  20 DEVRTLMANGA-PFTTDWLGTSPLHLAAQYGHYSTAEVLLRAGVSRDARTKVDRTPLHMAAADGHAHIVELLVRNGADVN 98
Cdd:PHA02875  116 DIMKLLIARGAdPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANID 195

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1021589237  99 -AKDMLKMTALHWATERHHRDVVELLIKYGAD 129
Cdd:PHA02875  196 yFGKNGCVAALCYAIENNKIDIVRLFIKRGAD 227
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 38-129 8.62e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 50.76  E-value: 8.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589237  38 GTSPLHLAAQYGHYSTAEVLLRAGVSRDARTKVDRTPLHMAAADGHAHIVELLVRNGA---DVNAKDmlKMTALHWATER 114
Cdd:PHA02875   35 GISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKfadDVFYKD--GMTPLHLATIL 112

                          90
                  ....*....|....*
gi 1021589237 115 HHRDVVELLIKYGAD 129
Cdd:PHA02875  113 KKLDIMKLLIARGAD 127
PHA02741 PHA02741
hypothetical protein; Provisional
 79-158 1.26e-06

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 48.12  E-value: 1.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589237  79 AADGH-----AHIVELLVRNGADVNAKDMLK-MTALHWATERHHRDVVELLIKY-GADVHAFSKFDKSAFDIALEKNNAE 151
Cdd:PHA02741   67 AAEKHeaqlaAEIIDHLIELGADINAQEMLEgDTALHLAAHRRDHDLAEWLCCQpGIDLHFCNADNKSPFELAIDNEDVA 146


                  ....*..
gi 1021589237 152 ILVILQE 158
Cdd:PHA02741  147 MMQILRE 153
Ank_4 pfam13637
Ankyrin repeats (many copies);
105-156 2.03e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.57  E-value: 2.03e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1021589237 105 MTALHWATERHHRDVVELLIKYGADVHAFSKFDKSAFDIALEKNNAEILVIL 156
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 25-137 2.13e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 49.87  E-value: 2.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589237  25 LMANGAPFTTDWLGTSPLHLAAQYGHYSTAEVLLRAGVSRDARTKVDRTPLHMAAADGHAHIVELL-------------- 90
Cdd:PLN03192  545 LKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILyhfasisdphaagd 624

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1021589237  91 -----------------VRNGADVNAKDMLKMTALHWATERHHRDVVELLIKYGADVHAFSKFD 137
Cdd:PLN03192  625 llctaakrndltamkelLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDD 688
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 22-139 7.84e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 48.14  E-value: 7.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589237  22 VRTLMANGAPFT--TDWLGTSpLHLAAqYGH--YSTAEVLLRAGVSRDARTKVDRTPLHMAAADG-HAHIVELLVRNGAD 96
Cdd:PHA02876  391 INTLLDYGADIEalSQKIGTA-LHFAL-CGTnpYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGAD 468

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1021589237  97 VNAKDMLKMTALHWATERHhrDVVELLIKYGADVHAFSKFDKS 139
Cdd:PHA02876  469 VNAINIQNQYPLLIALEYH--GIVNILLHYGAELRDSRVLHKS 509
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 73-172 8.64e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 47.74  E-value: 8.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589237  73 TPLHMAAADGHAHIVELLVRNGADVNAKDMLKMTALHWAT-----ERHHRDVVELLIKYGADVHAFSKFDKSAFDIALEK 147
Cdd:PHA03100   37 LPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSnikynLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISK 116

                          90       100
                  ....*....|....*....|....*..
gi 1021589237 148 --NNAEILVILqeaMQNQVNVNPERAN 172
Cdd:PHA03100  117 ksNSYSIVEYL---LDNGANVNIKNSD 140
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 10-128 9.08e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 47.65  E-value: 9.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589237  10 LLEAARKGQDDEVRTLMANGapfttdwLGTSPLHLAAQygHYSTAEVLLRAGVSRDARTKVDRTPLHMAAADGHAHIVEL 89
Cdd:PHA02874   72 LLTAIKIGAHDIIKLLIDNG-------VDTSILPIPCI--EKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKM 142

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1021589237  90 LVRNGADVNAKDMLKMTALHWATERHHRDVVELLIKYGA 128
Cdd:PHA02874  143 LFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGA 181
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 72-99 9.53e-06

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 41.86  E-value: 9.53e-06
                          10        20
                  ....*....|....*....|....*...
gi 1021589237  72 RTPLHMAAADGHAHIVELLVRNGADVNA 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 1.78e-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: 41.42  E-value: 1.78e-05
                           10        20
                   ....*....|....*....|....*...
gi 1021589237  105 MTALHWATERHHRDVVELLIKYGADVHA 132
Cdd:smart00248   3 RTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 105-132 2.44e-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: 41.12  E-value: 2.44e-05
                          10        20
                  ....*....|....*....|....*....
gi 1021589237 105 MTALHWATERH-HRDVVELLIKYGADVHA 132
Cdd:pfam00023   3 NTPLHLAAGRRgNLEIVKLLLSKGADVNA 31
Ank_4 pfam13637
Ankyrin repeats (many copies);
10-58 4.83e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 40.72  E-value: 4.83e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1021589237  10 LLEAARKGQDDEVRTLMANGAPF-TTDWLGTSPLHLAAQYGHYSTAEVLL 58
Cdd:pfam13637   5 LHAAAASGHLELLRLLLEKGADInAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 20-101 6.25e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 45.04  E-value: 6.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589237  20 DEVRTLMANGAPF-TTDWLGTSPLHLAAQYGHYSTAEVLLRAGVSRDARTKVDRTPLHMAAADGHAHIVELLVRNGADVN 98
Cdd:PHA03100  173 NRVNYLLSYGVPInIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252


                  ...
gi 1021589237  99 AKD 101
Cdd:PHA03100  253 TII 255
Ank_5 pfam13857
Ankyrin repeats (many copies);
57-111 1.16e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.64  E-value: 1.16e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1021589237  57 LLRAG-VSRDARTKVDRTPLHMAAADGHAHIVELLVRNGADVNAKDMLKMTALHWA 111
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 18-167 1.62e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 43.80  E-value: 1.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589237  18 QDDEVRTLMANGAPFTT-DWLGTSPLHLAAQYGHYSTAEVLLRAGVSRDARTKVDRTPLHMAAADGHAHIVELLVRNGAD 96
Cdd:PHA02874  103 EKDMIKTILDCGIDVNIkDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAY 182

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1021589237  97 VNAKDMLKMTALHWATERHHRDVVELLIKYGADVHAFSKFDKSAFDIALEKNNAEILVILQEAMQNQVNVN 167
Cdd:PHA02874  183 ANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAIELLINNASINDQDID 253
Ank_5 pfam13857
Ankyrin repeats (many copies);
30-78 1.91e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.87  E-value: 1.91e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1021589237  30 APFTTDWLGTSPLHLAAQYGHYSTAEVLLRAGVSRDARTKVDRTPLHMA 78
Cdd:pfam13857   8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA03095 PHA03095
ankyrin-like protein; Provisional
 86-151 2.70e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 43.09  E-value: 2.70e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1021589237  86 IVELLVRNGADVNAKDMLKMTALHWATERHH---RDVVELLIKYGADVHAFSKFDKSAFDIALEKNNAE 151
Cdd:PHA03095   29 EVRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTL 97
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 106-132 3.47e-04

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


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 42.87  E-value: 3.47e-04
                          10        20
                  ....*....|....*....|....*..
gi 1021589237 106 TALHWATERHHRDVVELLIKYGADVHA 132
Cdd:cd22196    96 TALHIAIERRNMHLVELLVQNGADVHA 122
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 38-69 4.16e-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: 37.65  E-value: 4.16e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1021589237  38 GTSPLHLAA-QYGHYSTAEVLLRAGVSRDARTK 69
Cdd:pfam00023   2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 105-132 4.29e-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: 37.24  E-value: 4.29e-04
                          10        20
                  ....*....|....*....|....*...
gi 1021589237 105 MTALHWATERHHRDVVELLIKYGADVHA 132
Cdd:pfam13606   3 NTPLHLAARNGRLEIVKLLLENGADINA 30
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 86-223 6.63e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 41.57  E-value: 6.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589237  86 IVELLVRNGADVNAKDMLKMTALHWATERHHRDVVELLIKYGADVHAFSKFDKSAF-----DIALEKNNAEILVILqeaM 160
Cdd:PHA03100   17 NIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLhylsnIKYNLTDVKEIVKLL---L 93

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1021589237 161 QNQVNVNPERANPVTdPVSMAAPFIFTSGEVVNLasLIS-STNTKTTSANTEEII----EGNSVDSSI 223
Cdd:PHA03100   94 EYGANVNAPDNNGIT-PLLYAISKKSNSYSIVEY--LLDnGANVNIKNSDGENLLhlylESNKIDLKI 158
PHA02743 PHA02743
Viral ankyrin protein; Provisional
 43-128 6.99e-04

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 40.18  E-value: 6.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589237  43 HLAAQYGHYSTA---EVLLRAGVSRDAR-TKVDRTPLHMAAADGHAHIVELLVRN-GADVNAKDMLKMTALHWATERHHR 117
Cdd:PHA02743   62 HMVAWYDRANAVmkiELLVNMGADINAReLGTGNTLLHIAASTKNYELAEWLCRQlGVNLGAINYQHETAYHIAYKMRDR 141

                          90
                  ....*....|.
gi 1021589237 118 DVVELLIKYGA 128
Cdd:PHA02743  142 RMMEILRANGA 152
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 95-182 8.00e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 41.67  E-value: 8.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589237  95 ADVNAKDMLKMTALHWATERHHRDVVELLIKYGADVHAFSK--------------FDKSAFDIALEKNNAEILVILQEAM 160
Cdd:cd22194   132 AEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKgvffnpkykhegfyFGETPLALAACTNQPEIVQLLMEKE 211

                          90       100
                  ....*....|....*....|..
gi 1021589237 161 QNQVNVNPERANPVTDPVSMAA 182
Cdd:cd22194   212 STDITSQDSRGNTVLHALVTVA 233
PHA02946 PHA02946
ankyin-like protein; Provisional
 55-131 1.64e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 40.42  E-value: 1.64e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1021589237  55 EVLLRAGVSRDARTKVDRTPLHMAAADGHAHIVELLVRNGADVNAKDMLKMTALHW--ATERHHRDVVELLIKYGADVH 131
Cdd:PHA02946   56 EELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYlsGTDDEVIERINLLVQYGAKIN 134
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 106-135 3.76e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 39.39  E-value: 3.76e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1021589237 106 TALHWATERHHRDVVELLIKYGADVHAFSK 135
Cdd:cd22193    78 TALHIAIERRQGDIVALLVENGADVHAHAK 107
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 72-100 4.08e-03

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


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 39.40  E-value: 4.08e-03
                          10        20
                  ....*....|....*....|....*....
gi 1021589237  72 RTPLHMAAADGHAHIVELLVRNGADVNAK 100
Cdd:cd22196    95 QTALHIAIERRNMHLVELLVQNGADVHAR 123
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 89-158 4.38e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 37.55  E-value: 4.38e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1021589237  89 LLVRNGADVNAKDMLK-MTALHWATERHHRDVVELLIKY-GADVHAFSKFDKSAFDIALEKNNAEILVILQE 158
Cdd:PHA02736   76 LLMEWGADINGKERVFgNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYVACERHDAKMMNILRA 147
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 106-132 4.84e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely related to TRPV1, sharing high sequence identity (>50%), but TRPV2 shows a higher temperature threshold and sensitivity for activation than TRPV1. TRPV2 can be stimulated by ligands or lipids, and is involved in osmosensation and mechanosensation. TRPV2 is expressed in both neuronal and non-neuronal tissues, and it has been implicated in diverse physiological and pathophysiological processes, including cardiac-structure maintenance, innate immunity, and cancer. TRPV2 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 39.07  E-value: 4.84e-03
                          10        20
                  ....*....|....*....|....*..
gi 1021589237 106 TALHWATERHHRDVVELLIKYGADVHA 132
Cdd:cd22197    96 SALHIAIEKRSLQCVKLLVENGADVHA 122
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 2-135 5.41e-03

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 38.91  E-value: 5.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589237   2 SLVDLGKRLLEAARKGQDDEVRTLMANGAPF---TTDWLGTSPLHLAAQYG-HYSTAEVLLragvSRDARTKVDRTPLHm 77
Cdd:TIGR00870  13 PLSDEEKAFLPAAERGDLASVYRDLEEPKKLninCPDRLGRSALFVAAIENeNLELTELLL----NLSCRGAVGDTLLH- 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1021589237  78 AAADGHAHIVELLVR----------NGADVNAKDMLK----MTALHWATERHHRDVVELLIKYGADVHAFSK 135
Cdd:TIGR00870  88 AISLEYVDAVEAILLhllaafrksgPLELANDQYTSEftpgITALHLAAHRQNYEIVKLLLERGASVPARAC 159
PHA02798 PHA02798
ankyrin-like protein; Provisional
 86-167 6.38e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 38.66  E-value: 6.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589237  86 IVELLVRNGADVNAKDMLKMTALHWATER---HHRDVVELLIKYGADVHAFSKFDKSAFDIALEKNNAEILVILQEAMQN 162
Cdd:PHA02798   91 IVKILIENGADINKKNSDGETPLYCLLSNgyiNNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHHIDIEIIKLLLEK 170


                  ....*
gi 1021589237 163 QVNVN 167
Cdd:PHA02798  171 GVDIN 175
PHA02946 PHA02946
ankyin-like protein; Provisional
 16-98 8.24e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 38.11  E-value: 8.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589237  16 KGQDDE-VRTLMANG-APFTTDWLGTSPLHLAAQYGHYSTAEVLLRAGVSRDARTKVDRTPLHMAAADGHAHI--VELLV 91
Cdd:PHA02946   48 KGLDERfVEELLHRGySPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIerINLLV 127


                  ....*..
gi 1021589237  92 RNGADVN 98
Cdd:PHA02946  128 QYGAKIN 134
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 38-63 8.26e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 33.72  E-value: 8.26e-03
                           10        20
                   ....*....|....*....|....*.
gi 1021589237   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.
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