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Conserved domains on  [gi|1720397239|ref|XP_030103388|]
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GA-binding protein subunit beta-1 isoform X13 [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];
18-187 9.65e-47

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 159.35  E-value: 9.65e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397239  18 LLEAARAGQDDEVRILMANGA-PFTTDWLGTSPLHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHANIVE 96
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGAdVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397239  97 VLLKHGADVNAKDMLKMTALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEDLAEILQIAMQNQINTNP 176
Cdd:COG0666   171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250

                         170
                  ....*....|.
gi 1720397239 177 ESPDTVTIHAA 187
Cdd:COG0666   251 DGLTALLLAAA 261
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
18-187 9.65e-47

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 159.35  E-value: 9.65e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397239  18 LLEAARAGQDDEVRILMANGA-PFTTDWLGTSPLHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHANIVE 96
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGAdVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397239  97 VLLKHGADVNAKDMLKMTALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEDLAEILQIAMQNQINTNP 176
Cdd:COG0666   171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250

                         170
                  ....*....|.
gi 1720397239 177 ESPDTVTIHAA 187
Cdd:COG0666   251 DGLTALLLAAA 261
Ank_2 pfam12796
Ankyrin repeats (3 copies);
50-141 3.36e-26

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 99.03  E-value: 3.36e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397239  50 LHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHANIVEVLLKHgADVNAKDMlKMTALHWATEHNHQEVVE 129
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78

                          90
                  ....*....|..
gi 1720397239 130 LLIKYGADVHTQ 141
Cdd:pfam12796  79 LLLEKGADINVK 90
PHA03095 PHA03095
ankyrin-like protein; Provisional
 28-151 3.00e-18

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 84.69  E-value: 3.00e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397239  28 DEVRILMANGAPF-TTDWLGTSPLHLaaqYGHFSTTE----VLLRAGVSRDARTKVDRTPLHMAAS--EGHANIVEVLLK 100
Cdd:PHA03095   64 DIVRLLLEAGADVnAPERCGFTPLHL---YLYNATTLdvikLLIKAGADVNAKDKVGRTPLHVYLSgfNINPKVIRLLLR 140

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720397239 101 HGADVNAKDMLKMTALHWATEhNHQ---EVVELLIKYGADVHTQSKFCKTAFDI 151
Cdd:PHA03095  141 KGADVNALDLYGMTPLAVLLK-SRNanvELLRLLIDAGADVYAVDDRFRSLLHH 193
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 18-189 3.68e-11

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: 63.49  E-value: 3.68e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397239  18 LLEAARAGQDDEVRILMANGA--PFTTDWLGTSPLHLAAQYGHFSTTEVLLRAgvsrdARTKVD----------RTPLHM 85
Cdd:cd22192    21 LLLAAKENDVQAIKKLLKCPScdLFQRGALGETALHVAALYDNLEAAVVLMEA-----APELVNepmtsdlyqgETALHI 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397239  86 AASEGHANIVEVLLKHGADVNAKD------MLKMTALHWATEH--------NHQEVVELLIKYGADVHTQSKFCKTAFDI 151
Cdd:cd22192    96 AVVNQNLNLVRELIARGADVVSPRatgtffRPGPKNLIYYGEHplsfaacvGNEEIVRLLIEHGADIRAQDSLGNTVLHI 175

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1720397239 152 SIDNGNEDLA-EILQIAMQNQINTNPESPDTVTIHAA-TP 189
Cdd:cd22192   176 LVLQPNKTFAcQMYDLILSYDKEDDLQPLDLVPNNQGlTP 215
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 79-107 1.00e-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: 47.20  E-value: 1.00e-07
                           10        20
                   ....*....|....*....|....*....
gi 1720397239   79 DRTPLHMAASEGHANIVEVLLKHGADVNA 107
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 10-147 2.51e-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: 48.92  E-value: 2.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397239  10 SLVDLGKKLLEAARAGQDDEVRILMANGAPF---TTDWLGTSPLHLAAQYG-HFSTTEVLLragvSRDARTKVDRTPLHm 85
Cdd:TIGR00870  13 PLSDEEKAFLPAAERGDLASVYRDLEEPKKLninCPDRLGRSALFVAAIENeNLELTELLL----NLSCRGAVGDTLLH- 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720397239  86 AASEGHANIVEVLLKHGADVNAKDMLK--------------MTALHWATEHNHQEVVELLIKYGADVHTQSK--FCKT 147
Cdd:TIGR00870  88 AISLEYVDAVEAILLHLLAAFRKSGPLelandqytseftpgITALHLAAHRQNYEIVKLLLERGASVPARACgdFFVK 165
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
18-187 9.65e-47

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 159.35  E-value: 9.65e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397239  18 LLEAARAGQDDEVRILMANGA-PFTTDWLGTSPLHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHANIVE 96
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGAdVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397239  97 VLLKHGADVNAKDMLKMTALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEDLAEILQIAMQNQINTNP 176
Cdd:COG0666   171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250

                         170
                  ....*....|.
gi 1720397239 177 ESPDTVTIHAA 187
Cdd:COG0666   251 DGLTALLLAAA 261
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
18-164 1.54e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 135.08  E-value: 1.54e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397239  18 LLEAARAGQDDEVRILMANGAP-FTTDWLGTSPLHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHANIVE 96
Cdd:COG0666    58 LLAAALAGDLLVALLLLAAGADiNAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVK 137

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720397239  97 VLLKHGADVNAKDMLKMTALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEDLAEIL 164
Cdd:COG0666   138 LLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
18-175 2.16e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 134.70  E-value: 2.16e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397239  18 LLEAARAGQDDEVRILMANGA-PFTTDWLGTSPLHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHANIVE 96
Cdd:COG0666   124 LHLAAYNGNLEIVKLLLEAGAdVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVK 203

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720397239  97 VLLKHGADVNAKDMLKMTALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEDLAEILQIAMQNQINTN 175
Cdd:COG0666   204 LLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
18-164 1.03e-28

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 111.58  E-value: 1.03e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397239  18 LLEAARAGQDDEVRILMANGAPFTTDWLGTSPLHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHANIVEV 97
Cdd:COG0666    26 LAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKL 105

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720397239  98 LLKHGADVNAKDMLKMTALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEDLAEIL 164
Cdd:COG0666   106 LLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLL 172
Ank_2 pfam12796
Ankyrin repeats (3 copies);
50-141 3.36e-26

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 99.03  E-value: 3.36e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397239  50 LHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHANIVEVLLKHgADVNAKDMlKMTALHWATEHNHQEVVE 129
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78

                          90
                  ....*....|..
gi 1720397239 130 LLIKYGADVHTQ 141
Cdd:pfam12796  79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
18-109 1.01e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 82.09  E-value: 1.01e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397239  18 LLEAARAGQDDEVRILMANGA-PFTTDWLGTSPLHLAAQYGHFSTTEVLLRAGVSRDarTKVDRTPLHMAASEGHANIVE 96
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGAdANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1720397239  97 VLLKHGADVNAKD 109
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 28-151 3.00e-18

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 84.69  E-value: 3.00e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397239  28 DEVRILMANGAPF-TTDWLGTSPLHLaaqYGHFSTTE----VLLRAGVSRDARTKVDRTPLHMAAS--EGHANIVEVLLK 100
Cdd:PHA03095   64 DIVRLLLEAGADVnAPERCGFTPLHL---YLYNATTLdvikLLIKAGADVNAKDKVGRTPLHVYLSgfNINPKVIRLLLR 140

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720397239 101 HGADVNAKDMLKMTALHWATEhNHQ---EVVELLIKYGADVHTQSKFCKTAFDI 151
Cdd:PHA03095  141 KGADVNALDLYGMTPLAVLLK-SRNanvELLRLLIDAGADVYAVDDRFRSLLHH 193
Ank_2 pfam12796
Ankyrin repeats (3 copies);
83-164 2.13e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.92  E-value: 2.13e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397239  83 LHMAASEGHANIVEVLLKHGADVNAKDMLKMTALHWATEHNHQEVVELLIKYgADVHTQSKFcKTAFDISIDNGNEDLAE 162
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNG-RTALHYAARSGHLEIVK 78


                  ..
gi 1720397239 163 IL 164
Cdd:pfam12796  79 LL 80
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 30-176 3.74e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 78.17  E-value: 3.74e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397239  30 VRILMANGAPFT-TDWLGTSPLHLAAQY--GHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHA--NIVEVLLKHGAD 104
Cdd:PHA03100   89 VKLLLEYGANVNaPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVD 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397239 105 ----------------VNAKDMLKMTALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEdlaEILQIAM 168
Cdd:PHA03100  169 inaknrvnyllsygvpINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNK---EIFKLLL 245


                  ....*...
gi 1720397239 169 QNQINTNP 176
Cdd:PHA03100  246 NNGPSIKT 253
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
32-164 1.82e-15

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 75.38  E-value: 1.82e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397239  32 ILMANGAPFTTDWLGTSPLHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHANIVEVLLKHGADVNAKDML 111
Cdd:COG0666     7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1720397239 112 KMTALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEDLAEIL 164
Cdd:COG0666    87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLL 139
PHA03095 PHA03095
ankyrin-like protein; Provisional
 30-182 1.40e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 70.82  E-value: 1.40e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397239  30 VRILMANGA-PFTTDWLGTSPLHLAAQYGHFSTT--EVLLRAGVSRDARTKVDRTPLHMAA--SEGHANIVEVLLKHGAD 104
Cdd:PHA03095  170 LRLLIDAGAdVYAVDDRFRSLLHHHLQSFKPRARivRELIRAGCDPAATDMLGNTPLHSMAtgSSCKRSLVLPLLIAGIS 249

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720397239 105 VNAKDMLKMTALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEDlaeilqiAMQNQINTNPeSPDTV 182
Cdd:PHA03095  250 INARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGR-------AVRAALAKNP-SAETV 319
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 31-175 5.81e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 68.92  E-value: 5.81e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397239  31 RILMANGAPFTTDWLGTSPLHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHA-----NIVEVLLKHGADV 105
Cdd:PHA03100   20 YIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANV 99

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720397239 106 NAKDMLKMTALHWA--TEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEDLaEILQIAMQNQINTN 175
Cdd:PHA03100  100 NAPDNNGITPLLYAisKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDL-KILKLLIDKGVDIN 170
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 42-170 2.36e-12

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 67.59  E-value: 2.36e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397239  42 TDWLGTSPLHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHANIVEVLLKHGADVNAKDMLKMTALHWATE 121
Cdd:PLN03192  521 DDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAIS 600

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720397239 122 HNHQEVVELLIKYGA--DVHTQSK-FCKTA-------------FDISIDNGNEDLAEILQIAMQN 170
Cdd:PLN03192  601 AKHHKIFRILYHFASisDPHAAGDlLCTAAkrndltamkellkQGLNVDSEDHQGATALQVAMAE 665
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 30-184 3.67e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 66.44  E-value: 3.67e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397239  30 VRILMANGAPFT--TDWLGTSPLHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHANIVEVLLKHGADVNA 107
Cdd:PHA02878  150 TKLLLSYGADINmkDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDA 229

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397239 108 KDMLKMTALHWATEH-NHQEVVELLIKYGADVHTQSKFCK-TAFDISIDNgNEDLAEILQI-AMQNQINTNPESPDTVTI 184
Cdd:PHA02878  230 RDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYILGlTALHSSIKS-ERKLKLLLEYgADINSLNSYKLTPLSSAV 308
Ank_4 pfam13637
Ankyrin repeats (many copies);
80-132 4.45e-12

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 59.98  E-value: 4.45e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1720397239  80 RTPLHMAASEGHANIVEVLLKHGADVNAKDMLKMTALHWATEHNHQEVVELLI 132
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 18-189 3.68e-11

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: 63.49  E-value: 3.68e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397239  18 LLEAARAGQDDEVRILMANGA--PFTTDWLGTSPLHLAAQYGHFSTTEVLLRAgvsrdARTKVD----------RTPLHM 85
Cdd:cd22192    21 LLLAAKENDVQAIKKLLKCPScdLFQRGALGETALHVAALYDNLEAAVVLMEA-----APELVNepmtsdlyqgETALHI 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397239  86 AASEGHANIVEVLLKHGADVNAKD------MLKMTALHWATEH--------NHQEVVELLIKYGADVHTQSKFCKTAFDI 151
Cdd:cd22192    96 AVVNQNLNLVRELIARGADVVSPRatgtffRPGPKNLIYYGEHplsfaacvGNEEIVRLLIEHGADIRAQDSLGNTVLHI 175

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1720397239 152 SIDNGNEDLA-EILQIAMQNQINTNPESPDTVTIHAA-TP 189
Cdd:cd22192   176 LVLQPNKTFAcQMYDLILSYDKEDDLQPLDLVPNNQGlTP 215
PHA03095 PHA03095
ankyrin-like protein; Provisional
 65-164 1.19e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 61.96  E-value: 1.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397239  65 LLRAGVSRDARTKVDRTPLHM---AASEGHANIVEVLLKHGADVNAKDMLKMTALHWATEHNHQE-VVELLIKYGADVHT 140
Cdd:PHA03095   33 LLAAGADVNFRGEYGKTPLHLylhYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAGADVNA 112

                          90       100
                  ....*....|....*....|....*.
gi 1720397239 141 QSKFCKTAFDI--SIDNGNEDLAEIL 164
Cdd:PHA03095  113 KDKVGRTPLHVylSGFNINPKVIRLL 138
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 46-177 1.83e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 61.62  E-value: 1.83e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397239  46 GTSPLHLAAQYGHFS-TTEVLLRAGVSRDARTKVDRTPLHMAAS-EGHANIVEVLLKHGADVNAKDMLKMTALHWATEHN 123
Cdd:PHA02876  307 GETPLYLMAKNGYDTeNIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRN 386

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720397239 124 HQEVVELLIKYGADVHTQSKFCKTAFDIS-------------IDNG------NEDLAEILQIAMQNqiNTNPE 177
Cdd:PHA02876  387 NVVIINTLLDYGADIEALSQKIGTALHFAlcgtnpymsvktlIDRGanvnskNKDLSTPLHYACKK--NCKLD 457
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 51-139 3.14e-10

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 61.07  E-value: 3.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397239  51 HLAAQyGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHANIVEVLLKHGADVNAKDMLKMTALHWATEHNHQEVVEL 130
Cdd:PTZ00322   88 QLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                  ....*....
gi 1720397239 131 LIKYGADVH 139
Cdd:PTZ00322  167 LSRHSQCHF 175
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 13-164 5.02e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 60.00  E-value: 5.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397239  13 DLGKKLLEAARAGQDDEVRILMANGApFTTDWL---GTSPLHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASE 89
Cdd:PHA02875   67 DIESELHDAVEEGDVKAVEELLDLGK-FADDVFykdGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMM 145

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720397239  90 GHANIVEVLLKHGADVNAKDMLKMTALHWATEHNHQEVVELLIKYGADVHTQSKF-CKTAFDISIDNGNEDLAEIL 164
Cdd:PHA02875  146 GDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNgCVAALCYAIENNKIDIVRLF 221
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
18-116 7.03e-10

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 58.81  E-value: 7.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397239  18 LLEAARAGQDDEVRILMANGA-PFTTDWLGTSPLHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHANIVE 96
Cdd:COG0666   190 LHLAAENGHLEIVKLLLEAGAdVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVK 269

                          90       100
                  ....*....|....*....|
gi 1720397239  97 VLLKHGADVNAKDMLKMTAL 116
Cdd:COG0666   270 LLLLALLLLAAALLDLLTLL 289
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 18-157 7.05e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 59.59  E-value: 7.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397239  18 LLEAARAGQDDEVRILMANGapfttdwLGTSPLHLAAQygHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHANIVEV 97
Cdd:PHA02874   72 LLTAIKIGAHDIIKLLIDNG-------VDTSILPIPCI--EKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKM 142

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397239  98 LLKHGADVNAKDMLKMTALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGN 157
Cdd:PHA02874  143 LFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGD 202
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 94-175 1.34e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 58.92  E-value: 1.34e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397239  94 IVEVLLKHGADVNAKDMLKMTALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEDLAEILqIAMQNQIN 173
Cdd:PHA02876  160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAI-IDNRSNIN 238


                  ..
gi 1720397239 174 TN 175
Cdd:PHA02876  239 KN 240
Ank_5 pfam13857
Ankyrin repeats (many copies);
98-151 1.46e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 53.12  E-value: 1.46e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1720397239  98 LLKHG-ADVNAKDMLKMTALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFDI 151
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 78-164 1.92e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 58.37  E-value: 1.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397239  78 VDRTPLHMAASE-------GHANIVEVLLKHGADVNAKDMLKMTALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFD 150
Cdd:PTZ00322   74 IDPVVAHMLTVElcqlaasGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLE 153

                          90
                  ....*....|....
gi 1720397239 151 ISIDNGNEDLAEIL 164
Cdd:PTZ00322  154 LAEENGFREVVQLL 167
Ank_4 pfam13637
Ankyrin repeats (many copies);
46-99 3.54e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.89  E-value: 3.54e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720397239  46 GTSPLHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHANIVEVLL 99
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 81-188 3.86e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 57.37  E-value: 3.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397239  81 TPLHMAASEGHANIVEVLLKHGADVNAKDMLKMTALHWATEHNH-----QEVVELLIKYGADVHTQSKFCKTAFDISIDN 155
Cdd:PHA03100   37 LPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVNAPDNNGITPLLYAISK 116

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1720397239 156 GNEDLaEILQIAMQNQINTNPESPDTVT-IHAAT 188
Cdd:PHA03100  117 KSNSY-SIVEYLLDNGANVNIKNSDGENlLHLYL 149
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 14-101 7.20e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.83  E-value: 7.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397239  14 LGKKLLEAARAGQDDEVRILMANGA-PFTTDWLGTSPLHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHA 92
Cdd:PTZ00322   82 LTVELCQLAASGDAVGARILLTGGAdPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFR 161


                  ....*....
gi 1720397239  93 NIVEVLLKH 101
Cdd:PTZ00322  162 EVVQLLSRH 170
Ank_4 pfam13637
Ankyrin repeats (many copies);
113-164 7.50e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.12  E-value: 7.50e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1720397239 113 MTALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEDLAEIL 164
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 28-137 1.18e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 55.77  E-value: 1.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397239  28 DEVRILMANGA-PFTTDWLGTSPLHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHANIVEVLLKHGADVN 106
Cdd:PHA02875  116 DIMKLLIARGAdPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANID 195

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1720397239 107 -AKDMLKMTALHWATEHNHQEVVELLIKYGAD 137
Cdd:PHA02875  196 yFGKNGCVAALCYAIENNKIDIVRLFIKRGAD 227
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 32-138 3.82e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 54.49  E-value: 3.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397239  32 ILMANGAPFTTDWLGTSPLHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHANIVEV-------------- 97
Cdd:PLN03192  544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIlyhfasisdphaag 623

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720397239  98 -----------------LLKHGADVNAKDMLKMTALHWATEHNHQEVVELLIKYGADV 138
Cdd:PLN03192  624 dllctaakrndltamkeLLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 46-164 4.03e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 54.23  E-value: 4.03e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397239  46 GTSPLHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHANIVEVLL---KHGADVNAKDmlKMTALHWATEH 122
Cdd:PHA02875   35 GISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLdlgKFADDVFYKD--GMTPLHLATIL 112

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1720397239 123 NHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEDLAEIL 164
Cdd:PHA02875  113 KKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELL 154
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 80-109 4.36e-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: 48.44  E-value: 4.36e-08
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1720397239  80 RTPLHMAA-SEGHANIVEVLLKHGADVNAKD 109
Cdd:pfam00023   3 NTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 55-160 7.93e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 53.53  E-value: 7.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397239  55 QYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHANIVEVLLKHGADVNAKDMLKMTALHWATEHNHQEVVELLIKY 134
Cdd:PHA02876  154 QQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDN 233

                          90       100
                  ....*....|....*....|....*...
gi 1720397239 135 GADVHTQskfcktafDISIDNG--NEDL 160
Cdd:PHA02876  234 RSNINKN--------DLSLLKAirNEDL 253
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 79-107 1.00e-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: 47.20  E-value: 1.00e-07
                           10        20
                   ....*....|....*....|....*....
gi 1720397239   79 DRTPLHMAASEGHANIVEVLLKHGADVNA 107
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 21-132 2.84e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 51.50  E-value: 2.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397239  21 AARAGQDDEVRILMANGAPFTT-DWLGTSPLHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHANIVEVLL 99
Cdd:PHA02874  131 AIKKGDLESIKMLFEYGADVNIeDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLI 210

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1720397239 100 KHGADVNAKDMLKMTALHWATEHNhQEVVELLI 132
Cdd:PHA02874  211 DHGNHIMNKCKNGFTPLHNAIIHN-RSAIELLI 242
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 80-107 1.32e-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: 44.17  E-value: 1.32e-06
                          10        20
                  ....*....|....*....|....*...
gi 1720397239  80 RTPLHMAASEGHANIVEVLLKHGADVNA 107
Cdd:pfam13606   3 NTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
65-119 1.47e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.64  E-value: 1.47e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720397239  65 LLRAG-VSRDARTKVDRTPLHMAASEGHANIVEVLLKHGADVNAKDMLKMTALHWA 119
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 28-139 2.29e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 48.91  E-value: 2.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397239  28 DEVRILMANGAPFTT-DWLGTSPLHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHANI-VEVLLKHGADV 105
Cdd:PHA02876  356 DIVITLLELGANVNArDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMsVKTLIDRGANV 435

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1720397239 106 NAKDMLKMTALHWATEHNHQ-EVVELLIKYGADVH 139
Cdd:PHA02876  436 NSKNKDLSTPLHYACKKNCKlDVIEMLLDNGADVN 470
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 10-147 2.51e-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: 48.92  E-value: 2.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397239  10 SLVDLGKKLLEAARAGQDDEVRILMANGAPF---TTDWLGTSPLHLAAQYG-HFSTTEVLLragvSRDARTKVDRTPLHm 85
Cdd:TIGR00870  13 PLSDEEKAFLPAAERGDLASVYRDLEEPKKLninCPDRLGRSALFVAAIENeNLELTELLL----NLSCRGAVGDTLLH- 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720397239  86 AASEGHANIVEVLLKHGADVNAKDMLK--------------MTALHWATEHNHQEVVELLIKYGADVHTQSK--FCKT 147
Cdd:TIGR00870  88 AISLEYVDAVEAILLHLLAAFRKSGPLelandqytseftpgITALHLAAHRQNYEIVKLLLERGASVPARACgdFFVK 165
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 14-117 4.15e-06

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 48.09  E-value: 4.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397239  14 LGKKLLEAARAGQDDEVRILMANGAP------FTTD-WLGTSPLHLAAQYGHFSTTEVLLRAGV--------------SR 72
Cdd:cd22192    50 LGETALHVAALYDNLEAAVVLMEAAPelvnepMTSDlYQGETALHIAVVNQNLNLVRELIARGAdvvspratgtffrpGP 129

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1720397239  73 DARTKVDRTPLHMAASEGHANIVEVLLKHGADVNAKDMLKMTALH 117
Cdd:cd22192   130 KNLIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 113-139 6.58e-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: 42.19  E-value: 6.58e-06
                           10        20
                   ....*....|....*....|....*..
gi 1720397239  113 MTALHWATEHNHQEVVELLIKYGADVH 139
Cdd:smart00248   3 RTPLHLAAENGNLEVVKLLLDKGADIN 29
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 28-109 8.64e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 46.97  E-value: 8.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397239  28 DEVRILMANGAPF-TTDWLGTSPLHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHANIVEVLLKHGADVN 106
Cdd:PHA03100  173 NRVNYLLSYGVPInIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252


                  ...
gi 1720397239 107 AKD 109
Cdd:PHA03100  253 TII 255
PHA02946 PHA02946
ankyin-like protein; Provisional
 63-139 1.65e-05

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 46.20  E-value: 1.65e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720397239  63 EVLLRAGVSRDARTKVDRTPLHMAASEGHANIVEVLLKHGADVNAKDMLKMTALHW--ATEHNHQEVVELLIKYGADVH 139
Cdd:PHA02946   56 EELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYlsGTDDEVIERINLLVQYGAKIN 134
PHA02741 PHA02741
hypothetical protein; Provisional
 83-165 1.69e-05

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 44.26  E-value: 1.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397239  83 LHMAAsEGH-----ANIVEVLLKHGADVNAKDMLK-MTALHWAT-EHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDN 155
Cdd:PHA02741   64 IHIAA-EKHeaqlaAEIIDHLIELGADINAQEMLEgDTALHLAAhRRDHDLAEWLCCQPGIDLHFCNADNKSPFELAIDN 142

                          90
                  ....*....|
gi 1720397239 156 GNEDLAEILQ 165
Cdd:PHA02741  143 EDVAMMQILR 152
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 113-143 1.93e-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: 40.74  E-value: 1.93e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1720397239 113 MTALHWATEH-NHQEVVELLIKYGADVHTQSK 143
Cdd:pfam00023   3 NTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
PHA03095 PHA03095
ankyrin-like protein; Provisional
 85-158 2.40e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 45.40  E-value: 2.40e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720397239  85 MAASEGHANIVEVLLKHGADVNAKDMLKMTALHWATEHNHQ---EVVELLIKYGADVHTQSKFCKTAFDISIDNGNE 158
Cdd:PHA03095   20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEkvkDIVRLLLEAGADVNAPERCGFTPLHLYLYNATT 96
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 50-149 4.44e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 44.57  E-value: 4.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397239  50 LHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHANIVEVLLKHGADVNAKDMLKMTALHWATEHNHQEVVE 129
Cdd:PHA02874  128 LHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIK 207

                          90       100
                  ....*....|....*....|
gi 1720397239 130 LLIKYGADVHTQskfCKTAF 149
Cdd:PHA02874  208 LLIDHGNHIMNK---CKNGF 224
PHA02798 PHA02798
ankyrin-like protein; Provisional
 93-175 9.40e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 43.67  E-value: 9.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397239  93 NIVEVLLKHGADVNAKDMLKMTALHWATEH---NHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEDLAEILQIAMQ 169
Cdd:PHA02798   90 DIVKILIENGADINKKNSDGETPLYCLLSNgyiNNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHHIDIEIIKLLLE 169


                  ....*.
gi 1720397239 170 NQINTN 175
Cdd:PHA02798  170 KGVDIN 175
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 74-164 9.79e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 43.43  E-value: 9.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397239  74 ARTKVDRTPLHMAASEGH-ANIVEVLLKHGADVNAK----DMLKMTALHWATEHNHQEVVELLIKYGADVHTQSKFCK-T 147
Cdd:PHA02884   27 KKNKICIANILYSSIKFHyTDIIDAILKLGADPEAPfplsENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKiT 106

                          90
                  ....*....|....*..
gi 1720397239 148 AFDISIDNGNEDLAEIL 164
Cdd:PHA02884  107 PLYISVLHGCLKCLEIL 123
Ank_4 pfam13637
Ankyrin repeats (many copies);
18-66 1.40e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.18  E-value: 1.40e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1720397239  18 LLEAARAGQDDEVRILMANGAPF-TTDWLGTSPLHLAAQYGHFSTTEVLL 66
Cdd:pfam13637   5 LHAAAASGHLELLRLLLEKGADInAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 45-138 1.43e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 43.51  E-value: 1.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397239  45 LGTSpLHLAAqYGH--FSTTEVLLRAGVSRDARTKVDRTPLHMAASEG-HANIVEVLLKHGADVNAKDMLKMTALHWATE 121
Cdd:PHA02876  408 IGTA-LHFAL-CGTnpYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIALE 485

                          90
                  ....*....|....*..
gi 1720397239 122 HNhqEVVELLIKYGADV 138
Cdd:PHA02876  486 YH--GIVNILLHYGAEL 500
Ank_5 pfam13857
Ankyrin repeats (many copies);
38-86 2.40e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.48  E-value: 2.40e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1720397239  38 APFTTDWLGTSPLHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMA 86
Cdd:pfam13857   8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02798 PHA02798
ankyrin-like protein; Provisional
 62-170 3.43e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 42.13  E-value: 3.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397239  62 TEVLLRAGVSRDARTKVDRTPLHMAASEGHANIVEVLL---KHGADVNAKDMLKMTALHWATEHNHQ---EVVELLIKYG 135
Cdd:PHA02798   92 VKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLfmiENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEKG 171

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1720397239 136 ADVHTQS-KFCKTAFDISID-NGNEDLAEILQIAMQN 170
Cdd:PHA02798  172 VDINTHNnKEKYDTLHCYFKyNIDRIDADILKLFVDN 208
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 59-147 4.97e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 41.59  E-value: 4.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397239  59 FSTTEVLLRAGVSRDARTKVDRTPLHMAA-SEGHANIVEVLLKHGADVNAKDMLKMTALHWATEHNHQ-EVVELLIKYGA 136
Cdd:PHA02876  253 LETSLLLYDAGFSVNSIDDCKNTPLHHASqAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYDtENIRTLIMLGA 332

                          90
                  ....*....|.
gi 1720397239 137 DVHTQSKFCKT 147
Cdd:PHA02876  333 DVNAADRLYIT 343
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 81-179 5.12e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 41.49  E-value: 5.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397239  81 TPLHMAASEGHANIVEVLLKHGADVN-----------------AKDMLKM------------------------------ 113
Cdd:PHA02874   37 TPLIDAIRSGDAKIVELFIKHGADINhintkiphplltaikigAHDIIKLlidngvdtsilpipciekdmiktildcgid 116

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720397239 114 ---------TALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEDLAEIL--QIAMQNQINTNPESP 179
Cdd:PHA02874  117 vnikdaelkTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLleKGAYANVKDNNGESP 193
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 113-140 7.33e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 36.47  E-value: 7.33e-04
                          10        20
                  ....*....|....*....|....*...
gi 1720397239 113 MTALHWATEHNHQEVVELLIKYGADVHT 140
Cdd:pfam13606   3 NTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 54-138 9.11e-04

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 41.05  E-value: 9.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397239  54 AQYGHFSTTEVLLRAGVSRDARTKVDRTPLH--MAASEGHANIVEVLLKHGADVNAKDMLKMTALH-----------WAT 120
Cdd:PHA02716  292 ARNIDISVVYSFLQPGVKLHYKDSAGRTCLHqyILRHNISTDIIKLLHEYGNDLNEPDNIGNTVLHtylsmlsvvniLDP 371

                          90       100
                  ....*....|....*....|.
gi 1720397239 121 EHNHQ---EVVELLIKYGADV 138
Cdd:PHA02716  372 ETDNDirlDVIQCLISLGADI 392
PHA02798 PHA02798
ankyrin-like protein; Provisional
 93-157 1.57e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 39.82  E-value: 1.57e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720397239  93 NIVEVLLKHgADVNAKDMLKMTALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGN 157
Cdd:PHA02798  240 NILDFIFSY-IDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENES 303
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 81-157 1.72e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 39.03  E-value: 1.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397239  81 TPLHMAASEGHAN--IVEVLLKHGADVNAKDM-LKMTALHWATEHN---HQEVVELLIKYGADVHTQSKFCKTAFDISID 154
Cdd:PHA02859   53 TPIFSCLEKDKVNveILKFLIENGADVNFKTRdNNLSALHHYLSFNknvEPEILKILIDSGSSITEEDEDGKNLLHMYMC 132


                  ...
gi 1720397239 155 NGN 157
Cdd:PHA02859  133 NFN 135
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 94-185 1.77e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 39.65  E-value: 1.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397239  94 IVEVLLKHGADVNAKDMLKMTALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGN--EDLAEILQIAMQNq 171
Cdd:PHA03100   17 NIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnlTDVKEIVKLLLEY- 95

                          90
                  ....*....|....
gi 1720397239 172 iNTNPESPDTVTIH 185
Cdd:PHA03100   96 -GANVNAPDNNGIT 108
PHA02791 PHA02791
ankyrin-like protein; Provisional
 26-133 2.62e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 38.87  E-value: 2.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720397239  26 QDDEVRILMANGAPFTTDWLGTSPLHLAAQYGHFSTTEVLLRAGVSRDARTkvDRTPLHMAASEGHANIVEVLLKHGADV 105
Cdd:PHA02791   10 KSKQLKSFLSSKDAFKADVHGHSALYYAIADNNVRLVCTLLNAGALKNLLE--NEFPLHQAATLEDTKIVKILLFSGMDD 87

                          90       100
                  ....*....|....*....|....*...
gi 1720397239 106 NAKDMLKMTALHWATEHNHQEVVELLIK 133
Cdd:PHA02791   88 SQFDDKGNTALYYAVDSGNMQTVKLFVK 115
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 46-77 2.81e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 34.96  E-value: 2.81e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1720397239  46 GTSPLHLAA-QYGHFSTTEVLLRAGVSRDARTK 77
Cdd:pfam00023   2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 50-107 4.27e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 38.70  E-value: 4.27e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720397239  50 LHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHANIVEVLLKHGADVNA 107
Cdd:PLN03192  626 LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDK 683
PHA02743 PHA02743
Viral ankyrin protein; Provisional
 63-136 7.54e-03

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 36.72  E-value: 7.54e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720397239  63 EVLLRAGVSRDAR-TKVDRTPLHMAASEGHANIVEVLLKH-GADVNAKDMLKMTALHWATEHNHQEVVELLIKYGA 136
Cdd:PHA02743   77 ELLVNMGADINAReLGTGNTLLHIAASTKNYELAEWLCRQlGVNLGAINYQHETAYHIAYKMRDRRMMEILRANGA 152
 
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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