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Conserved domains on  [gi|530383065|ref|XP_005248739|]
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ankyrin repeat domain-containing protein 6 isoform X3 [Homo sapiens]

Protein Classification

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

ankyrin repeat domain-containing protein; ANK proteins mediate specific protein-protein interactions without necessarily recognizing specific primary sequences which allows for one ankyrin repeat domain to recognize and bind to a variety of intracellular substrates and may be involved in a wide array of functions

Gene Ontology:  GO:0005515
PubMed:  17176038
SCOP:  4000366

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
95-263 3.40e-41

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 152.42  E-value: 3.40e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383065  95 REKEGDQTALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKAGNTALHLAC 174
Cdd:COG0666   82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383065 175 QNSHSQSTRVLLLAGSRADLKNNAGDTCLHVAARYNHLSIIRLLLTAFCSVHEKNQAGDTALHVAAALNHKKVAKILLEA 254
Cdd:COG0666  162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241


                 ....*....
gi 530383065 255 GADTTIVNN 263
Cdd:COG0666  242 GADLNAKDK 250
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
95-263 3.40e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 152.42  E-value: 3.40e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383065  95 REKEGDQTALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKAGNTALHLAC 174
Cdd:COG0666   82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383065 175 QNSHSQSTRVLLLAGSRADLKNNAGDTCLHVAARYNHLSIIRLLLTAFCSVHEKNQAGDTALHVAAALNHKKVAKILLEA 254
Cdd:COG0666  162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241


                 ....*....
gi 530383065 255 GADTTIVNN 263
Cdd:COG0666  242 GADLNAKDK 250
Ank_2 pfam12796
Ankyrin repeats (3 copies);
170-262 7.16e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.48  E-value: 7.16e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383065  170 LHLACQNSHSQSTRVLLLAGSRADLKNNAGDTCLHVAARYNHLSIIRLLLtAFCSVHEKNQaGDTALHVAAALNHKKVAK 249
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKDN-GRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 530383065  250 ILLEAGADTTIVN 262
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 113-262 8.35e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 80.69  E-value: 8.35e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383065 113 TEIIAALIHEGCALDRQDKD-GNTALHEASWHGFSQSAKLLIKAGANVLAKNKAGNTALHLACQNSHSQSTRVLLLAGSR 191
Cdd:PHA02878 147 AEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAS 226

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530383065 192 ADLKNNAGDTCLHVAARY-NHLSIIRLLLTAFCSVHEKNQA-GDTALHVAaaLNHKKVAKILLEAGADTTIVN 262
Cdd:PHA02878 227 TDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYIlGLTALHSS--IKSERKLKLLLEYGADINSLN 297
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 150-258 2.20e-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: 51.17  E-value: 2.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383065 150 KLLIKAGANVLAKNKAGNTALHLACQNSHSQSTRVLLLAGSRadLKNNA-------GDTCLHVAARYNHLSIIRLLL--- 219
Cdd:cd22192   35 KLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPE--LVNEPmtsdlyqGETALHIAVVNQNLNLVRELIarg 112

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 530383065 220 ----------TAFcSVHEKNQA--GDTALHVAAALNHKKVAKILLEAGADT 258
Cdd:cd22192  113 advvspratgTFF-RPGPKNLIyyGEHPLSFAACVGNEEIVRLLIEHGADI 162
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 232-260 2.04e-04

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: 39.11  E-value: 2.04e-04
                           10        20
                   ....*....|....*....|....*....
gi 530383065   232 GDTALHVAAALNHKKVAKILLEAGADTTI 260
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 59-219 1.93e-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: 41.61  E-value: 1.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383065   59 ASEIVQDAVATVKAMKEDKNKKNHRGKVRKDPRRSEREKegDQTALHRATVVGNTEIIAALIHEG-------CALDRQDK 131
Cdd:TIGR00870  89 ISLEYVDAVEAILLHLLAAFRKSGPLELANDQYTSEFTP--GITALHLAAHRQNYEIVKLLLERGasvparaCGDFFVKS 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383065  132 DGNTALHeaswHG---------FSQSA--KLLIKAGANVLAKNKAGNTALHLACQNS-----------HSQSTRVLLLAG 189
Cdd:TIGR00870 167 QGVDSFY----HGesplnaaacLGSPSivALLSEDPADILTADSLGNTLLHLLVMENefkaeyeelscQMYNFALSLLDK 242

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 530383065  190 SR-----ADLKNNAGDTCLHVAARYNHLSIIRLLL 219
Cdd:TIGR00870 243 LRdskelEVILNHQGLTPLKLAAKEGRIVLFRLKL 277
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
95-263 3.40e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 152.42  E-value: 3.40e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383065  95 REKEGDQTALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKAGNTALHLAC 174
Cdd:COG0666   82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383065 175 QNSHSQSTRVLLLAGSRADLKNNAGDTCLHVAARYNHLSIIRLLLTAFCSVHEKNQAGDTALHVAAALNHKKVAKILLEA 254
Cdd:COG0666  162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241


                 ....*....
gi 530383065 255 GADTTIVNN 263
Cdd:COG0666  242 GADLNAKDK 250
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
97-263 5.18e-40

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 148.95  E-value: 5.18e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383065  97 KEGDQTALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKAGNTALHLACQN 176
Cdd:COG0666   51 DALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYN 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383065 177 SHSQSTRVLLLAGSRADLKNNAGDTCLHVAARYNHLSIIRLLLTAFCSVHEKNQAGDTALHVAAALNHKKVAKILLEAGA 256
Cdd:COG0666  131 GNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGA 210


                 ....*..
gi 530383065 257 DTTIVNN 263
Cdd:COG0666  211 DVNAKDN 217
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
98-266 4.47e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 137.78  E-value: 4.47e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383065  98 EGDQTALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKAGNTALHLACQNS 177
Cdd:COG0666  118 KDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENG 197

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383065 178 HSQSTRVLLLAGSRADLKNNAGDTCLHVAARYNHLSIIRLLLTAFCSVHEKNQAGDTALHVAAALNHKKVAKILLEAGAD 257
Cdd:COG0666  198 HLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLL 277


                 ....*....
gi 530383065 258 TTIVNNVLR 266
Cdd:COG0666  278 LAAALLDLL 286
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
102-263 2.94e-28

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 115.05  E-value: 2.94e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383065 102 TALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKAGNTALHLACQNSHSQS 181
Cdd:COG0666   23 LLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEI 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383065 182 TRVLLLAGSRADLKNNAGDTCLHVAARYNHLSIIRLLLTAFCSVHEKNQAGDTALHVAAALNHKKVAKILLEAGADTTIV 261
Cdd:COG0666  103 VKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNAR 182


                 ..
gi 530383065 262 NN 263
Cdd:COG0666  183 DN 184
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
101-236 1.17e-25

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 107.73  E-value: 1.17e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383065 101 QTALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKAGNTALHLACQNSHSQ 180
Cdd:COG0666  154 NTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLE 233

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 530383065 181 STRVLLLAGSRADLKNNAGDTCLHVAARYNHLSIIRLLLTAFCSVHEKNQAGDTAL 236
Cdd:COG0666  234 IVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
Ank_2 pfam12796
Ankyrin repeats (3 copies);
170-262 7.16e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.48  E-value: 7.16e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383065  170 LHLACQNSHSQSTRVLLLAGSRADLKNNAGDTCLHVAARYNHLSIIRLLLtAFCSVHEKNQaGDTALHVAAALNHKKVAK 249
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKDN-GRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 530383065  250 ILLEAGADTTIVN 262
Cdd:pfam12796  79 LLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
114-263 4.99e-20

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 91.17  E-value: 4.99e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383065 114 EIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKAGNTALHLACQNSHSQSTRVLLLAGSRAD 193
Cdd:COG0666    2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383065 194 LKNNAGDTCLHVAARYNHLSIIRLLLTAFCSVHEKNQAGDTALHVAAALNHKKVAKILLEAGADTTIVNN 263
Cdd:COG0666   82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDN 151
Ank_2 pfam12796
Ankyrin repeats (3 copies);
137-229 1.68e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.93  E-value: 1.68e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383065  137 LHEASWHGFSQSAKLLIKAGANVLAKNKAGNTALHLACQNSHSQSTRvLLLAGSRADLKNNaGDTCLHVAARYNHLSIIR 216
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVK-LLLEHADVNLKDN-GRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 530383065  217 LLLTAFCSVHEKN 229
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 113-262 8.35e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 80.69  E-value: 8.35e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383065 113 TEIIAALIHEGCALDRQDKD-GNTALHEASWHGFSQSAKLLIKAGANVLAKNKAGNTALHLACQNSHSQSTRVLLLAGSR 191
Cdd:PHA02878 147 AEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAS 226

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530383065 192 ADLKNNAGDTCLHVAARY-NHLSIIRLLLTAFCSVHEKNQA-GDTALHVAaaLNHKKVAKILLEAGADTTIVN 262
Cdd:PHA02878 227 TDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYIlGLTALHSS--IKSERKLKLLLEYGADINSLN 297
PHA03095 PHA03095
ankyrin-like protein; Provisional
 112-263 1.09e-15

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 80.45  E-value: 1.09e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383065 112 NTEIIAALIHEGCALDRQDKDGNTALHeaswhGFSQSA-------KLLIKAGANVLAKNKAGNTALHLACQNSHSQST-- 182
Cdd:PHA03095 131 NPKVIRLLLRKGADVNALDLYGMTPLA-----VLLKSRnanvellRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRARiv 205

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383065 183 RVLLLAGSRADLKNNAGDTCLHVAARYNHL--SIIRLLLTAFCSVHEKNQAGDTALHVAAALNHKKVAKILLEAGADTTI 260
Cdd:PHA03095 206 RELIRAGCDPAATDMLGNTPLHSMATGSSCkrSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINA 285


                 ...
gi 530383065 261 VNN 263
Cdd:PHA03095 286 VSS 288
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 64-381 1.90e-15

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 80.30  E-value: 1.90e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383065  64 QDAVATVKAMKEdKNKKNHRGKVRKDPRRSEREKEGDQTALHRATVV--GNTEIIAALIHEGCALDRQDKDGNTALHEAS 141
Cdd:PLN03192 488 EDNVVILKNFLQ-HHKELHDLNVGDLLGDNGGEHDDPNMASNLLTVAstGNAALLEELLKAKLDPDIGDSKGRTPLHIAA 566

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383065 142 WHGFSQSAKLLIKAGANVLAKNKAGNTALHLACQNSHSQSTRVLLLAGSRADlKNNAGDTcLHVAARYNHLSIIRLLLTA 221
Cdd:PLN03192 567 SKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISD-PHAAGDL-LCTAAKRNDLTAMKELLKQ 644

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383065 222 FCSVHEKNQAGDTALHVAAALNHKKVAKILLEAGADTTIVNNVLRFSRgrslRKKRERLKEERRAQSVprdevaqskgsV 301
Cdd:PLN03192 645 GLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDDDFSP----TELRELLQKRELGHSI-----------T 709

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383065 302 SAGDTPSSEQAVARKEEAREEFLSASPEprakddrRRKSRPKVSAFSdptppadqqpghqknlhahNHPKKRNRHRCSSP 381
Cdd:PLN03192 710 IVDSVPADEPDLGRDGGSRPGRLQGTSS-------DNQCRPRVSIYK-------------------GHPLLRNERCCNEA 763
Ank_2 pfam12796
Ankyrin repeats (3 copies);
104-196 4.43e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.92  E-value: 4.43e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383065  104 LHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKaGANVLAKNKaGNTALHLACQNSHSQSTR 183
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 530383065  184 VLLLAGSRADLKN 196
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 32-263 1.63e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 76.54  E-value: 1.63e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383065  32 LLPANRVNSHWSANAISDWSMSNHIAPASEIVQDAVATVKAMKEDKNKKNHRGKvrkdprrserekegdqTALHRATVVG 111
Cdd:PHA02874  72 LLTAIKIGAHDIIKLLIDNGVDTSILPIPCIEKDMIKTILDCGIDVNIKDAELK----------------TFLHYAIKKG 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383065 112 NTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKAGNTALHLACQNSHSQSTRVLLLAGSR 191
Cdd:PHA02874 136 DLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNH 215

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530383065 192 ADLKNNAGDTCLHVAARYNHlSIIRLLLTAfCSVHEKNQAGDTALHvaAALNH---KKVAKILLEAGADTTIVNN 263
Cdd:PHA02874 216 IMNKCKNGFTPLHNAIIHNR-SAIELLINN-ASINDQDIDGSTPLH--HAINPpcdIDIIDILLYHKADISIKDN 286
PHA03095 PHA03095
ankyrin-like protein; Provisional
 97-263 2.13e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 76.22  E-value: 2.13e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383065  97 KEGDQTALH---RATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQS-AKLLIKAGANVLAKNKAGNTALH- 171
Cdd:PHA03095  44 GEYGKTPLHlylHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDvIKLLIKAGADVNAKDKVGRTPLHv 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383065 172 -LACQNSHSQSTRVLLLAGsrADL--KNNAGDTCLHVAARYNH--LSIIRLLLTAFCSVHEKNQAGDTALHVaAALNHKK 246
Cdd:PHA03095 124 yLSGFNINPKVIRLLLRKG--ADVnaLDLYGMTPLAVLLKSRNanVELLRLLIDAGADVYAVDDRFRSLLHH-HLQSFKP 200

                        170       180
                 ....*....|....*....|
gi 530383065 247 VAKI---LLEAGADTTIVNN 263
Cdd:PHA03095 201 RARIvreLIRAGCDPAATDM 220
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 112-266 1.40e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 73.55  E-value: 1.40e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383065 112 NTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSA--KLLIKAGANVLAKNKAGNTALHLACQNSHS---------- 179
Cdd:PHA03100  85 VKEIVKLLLEYGANVNAPDNNGITPLLYAISKKSNSYSivEYLLDNGANVNIKNSDGENLLHLYLESNKIdlkilkllid 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383065 180 ------QSTRV--LLLAGSRADLKNNAGDTCLHVAARYNHLSIIRLLLTAFCSVHEKNQAGDTALHVAAALNHKKVAKIL 251
Cdd:PHA03100 165 kgvdinAKNRVnyLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLL 244

                        170
                 ....*....|....*
gi 530383065 252 LEAGADTTIVNNVLR 266
Cdd:PHA03100 245 LNNGPSIKTIIETLL 259
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
100-201 2.03e-13

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 71.52  E-value: 2.03e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383065 100 DQTALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKAGNTALHLACQNSHS 179
Cdd:COG0666  186 GETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAA 265

                         90       100
                 ....*....|....*....|..
gi 530383065 180 QSTRVLLLAGSRADLKNNAGDT 201
Cdd:COG0666  266 LIVKLLLLALLLLAAALLDLLT 287
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 112-263 2.23e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 72.78  E-value: 2.23e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383065 112 NTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQS-----AKLLIKAGANVLAKNKAGNTALHLACQNSHSQSTRV-- 184
Cdd:PHA03100  47 NIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLTdvkeiVKLLLEYGANVNAPDNNGITPLLYAISKKSNSYSIVey 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383065 185 LLLAGSRADLKNNAGDTCLHVAARYNH--LSIIRLL----------------LTAFCSVHEKNQAGDTALHVAAALNHKK 246
Cdd:PHA03100 127 LLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLidkgvdinaknrvnylLSYGVPINIKDVYGFTPLHYAVYNNNPE 206

                        170
                 ....*....|....*..
gi 530383065 247 VAKILLEAGADTTIVNN 263
Cdd:PHA03100 207 FVKYLLDLGANPNLVNK 223
PHA03095 PHA03095
ankyrin-like protein; Provisional
 150-263 8.50e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 71.21  E-value: 8.50e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383065 150 KLLIKAGANVLAKNKAGNTALHLACQNSHSQSTRV---LLLAGSRADLKNNAGDTCLHVAARY-NHLSIIRLLLTAFCSV 225
Cdd:PHA03095  31 RRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIvrlLLEAGADVNAPERCGFTPLHLYLYNaTTLDVIKLLIKAGADV 110

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 530383065 226 HEKNQAGDTALHV-AAALN-HKKVAKILLEAGADTTIVNN 263
Cdd:PHA03095 111 NAKDKVGRTPLHVyLSGFNiNPKVIRLLLRKGADVNALDL 150
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 102-219 6.74e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 65.07  E-value: 6.74e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383065 102 TALHRA--TVVGNTEIIAALIHEGCALDRQDKDGNTALHEA--SWHGFSQSAKLLIKAGANVLAKNKA------------ 165
Cdd:PHA03100 108 TPLLYAisKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYleSNKIDLKILKLLIDKGVDINAKNRVnyllsygvpini 187

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 530383065 166 ----GNTALHLACQNSHSQSTRVLLLAGSRADLKNNAGDTCLHVAARYNHLSIIRLLL 219
Cdd:PHA03100 188 kdvyGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLL 245
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 150-281 7.84e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 64.90  E-value: 7.84e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383065 150 KLLIKAGANVLAKNK-AGNTALHLACQNSHSQSTRVLLLAGSRADLKNNAGDTCLHVAARYNHLSIIRLLLTAFCSVHEK 228
Cdd:PHA02878 151 KLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDAR 230

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 530383065 229 NQAGDTALHVAAA-LNHKKVAKILLEAGADTTIVNNVLRFSRGRSLRKKRERLK 281
Cdd:PHA02878 231 DKCGNTPLHISVGyCKDYDILKLLLEHGVDVNAKSYILGLTALHSSIKSERKLK 284
Ank_2 pfam12796
Ankyrin repeats (3 copies);
101-163 5.47e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 56.66  E-value: 5.47e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530383065  101 QTALHRATVVGNTEIIAALIhEGCALDRQDkDGNTALHEASWHGFSQSAKLLIKAGANVLAKN 163
Cdd:pfam12796  31 RTALHLAAKNGHLEIVKLLL-EHADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 99-265 7.42e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 61.55  E-value: 7.42e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383065  99 GDQTALHRATVVGNTEIIAALIHEGC-ALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKAGNTALHLACQNS 177
Cdd:PHA02875  67 DIESELHDAVEEGDVKAVEELLDLGKfADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMG 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383065 178 HSQSTRVLLLAGSRADLKNNAGDTCLHVAARYNHLSIIRLLLTAFCSVHEKNQAGDTALHVAAALNHK-KVAKILLEAGA 256
Cdd:PHA02875 147 DIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKiDIVRLFIKRGA 226


                 ....*....
gi 530383065 257 DTTIVNNVL 265
Cdd:PHA02875 227 DCNIMFMIE 235
Ank_4 pfam13637
Ankyrin repeats (many copies);
102-153 5.78e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.28  E-value: 5.78e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 530383065  102 TALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLI 153
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 105-268 1.51e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 57.73  E-value: 1.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383065 105 HRATVvgntEIIAALIHEGCALDRQDKDGNTALHEaswhgFSQSAK-------LLIKAGANVLAKNKAGNTALHLACQNS 177
Cdd:PHA03095 163 RNANV----ELLRLLIDAGADVYAVDDRFRSLLHH-----HLQSFKprarivrELIRAGCDPAATDMLGNTPLHSMATGS 233

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383065 178 HSQSTRV--LLLAGSRADLKNNAGDTCLHVAARYNHLSIIRLLLTAFCSVHEKNQAGDTALHVAAALNHKKVAKILLEAG 255
Cdd:PHA03095 234 SCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKN 313

                        170
                 ....*....|....
gi 530383065 256 ADT-TIVNNVLRFS 268
Cdd:PHA03095 314 PSAeTVAATLNTAS 327
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 114-264 2.11e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 56.98  E-value: 2.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383065 114 EIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKAGNTALHLACQNSHSQS-----TRVLLLA 188
Cdd:PHA03100  16 KNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLTdvkeiVKLLLEY 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383065 189 GSRADLKNNAGDTCLHVAA--RYNHLSIIRLLLTAFCSVHEKNQAGDTALHVAAALNH--KKVAKILLEAGADTTIVNNV 264
Cdd:PHA03100  96 GANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAKNRV 175
Ank_4 pfam13637
Ankyrin repeats (many copies);
199-252 2.46e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.74  E-value: 2.46e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 530383065  199 GDTCLHVAARYNHLSIIRLLLTAFCSVHEKNQAGDTALHVAAALNHKKVAKILL 252
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
166-219 3.83e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.97  E-value: 3.83e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 530383065  166 GNTALHLACQNSHSQSTRVLLLAGSRADLKNNAGDTCLHVAARYNHLSIIRLLL 219
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 39-262 1.15e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 55.07  E-value: 1.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383065  39 NSHWSANAISDWSMSN-HIAPASEIVQDAVATVKAMKEDKNKKNHRGkvrkdprrserekegdQTALHRATVVG-NTEII 116
Cdd:PHA02876 261 DAGFSVNSIDDCKNTPlHHASQAPSLSRLVPKLLERGADVNAKNIKG----------------ETPLYLMAKNGyDTENI 324

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383065 117 AALIHEGCALDRQDKDGNTALHEAS-WHGFSQSAKLLIKAGANVLAKNKAGNTALHLACQNSHSQSTRVLLLAGSRADLK 195
Cdd:PHA02876 325 RTLIMLGADVNAADRLYITPLHQAStLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEAL 404

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530383065 196 NNAGDTCLHVA-ARYNHLSIIRLLLTAFCSVHEKNQAGDTALHVAAALNHK-KVAKILLEAGADTTIVN 262
Cdd:PHA02876 405 SQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNCKlDVIEMLLDNGADVNAIN 473
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 112-257 1.31e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 54.61  E-value: 1.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383065 112 NTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGA---NVLAKNkaGNTALHLACQNSHSQSTRVLLLA 188
Cdd:PHA02875  47 DSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKfadDVFYKD--GMTPLHLATILKKLDIMKLLIAR 124

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530383065 189 GSRADLKNNAGDTCLHVAARYNHLSIIRLLLTAFCSVHEKNQAGDTALHVAAALNHKKVAKILLEAGAD 257
Cdd:PHA02875 125 GADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGAN 193
Ank_4 pfam13637
Ankyrin repeats (many copies);
133-186 5.73e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.88  E-value: 5.73e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 530383065  133 GNTALHEASWHGFSQSAKLLIKAGANVLAKNKAGNTALHLACQNSHSQSTRVLL 186
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 102-265 7.32e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 52.76  E-value: 7.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383065 102 TALHRATVVGN-TEIIAALIHEGCALDRQDKDGNTALHEASWHGF-SQSAKLLIKAGANVLAKNKAGNTALHLACQNSHS 179
Cdd:PHA02876 275 TPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDRN 354

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383065 180 QSTRVLLLA-GSRADLKNNAGDTCLHVAARYNHLSIIRLLLTAFCSVHEKNQAGDTALHVA-AALNHKKVAKILLEAGAD 257
Cdd:PHA02876 355 KDIVITLLElGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGAN 434


                 ....*...
gi 530383065 258 TTIVNNVL 265
Cdd:PHA02876 435 VNSKNKDL 442
Ank_5 pfam13857
Ankyrin repeats (many copies);
121-173 8.41e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.57  E-value: 8.41e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 530383065  121 HEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKAGNTALHLA 173
Cdd:pfam13857   4 HGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
185-239 1.24e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.80  E-value: 1.24e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 530383065  185 LLLAGSRA-DLKNNAGDTCLHVAARYNHLSIIRLLLTAFCSVHEKNQAGDTALHVA 239
Cdd:pfam13857   1 LLEHGPIDlNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 150-258 2.20e-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: 51.17  E-value: 2.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383065 150 KLLIKAGANVLAKNKAGNTALHLACQNSHSQSTRVLLLAGSRadLKNNA-------GDTCLHVAARYNHLSIIRLLL--- 219
Cdd:cd22192   35 KLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPE--LVNEPmtsdlyqGETALHIAVVNQNLNLVRELIarg 112

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 530383065 220 ----------TAFcSVHEKNQA--GDTALHVAAALNHKKVAKILLEAGADT 258
Cdd:cd22192  113 advvspratgTFF-RPGPKNLIyyGEHPLSFAACVGNEEIVRLLIEHGADI 162
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 100-219 2.60e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 50.83  E-value: 2.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383065 100 DQTALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEAsWHGFS--QSAKLLIKAGANVLAKNKAGNTALHLACQ-N 176
Cdd:PHA02876 375 DKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFA-LCGTNpyMSVKTLIDRGANVNSKNKDLSTPLHYACKkN 453

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 530383065 177 SHSQSTRVLLLAGSRADLKNNAGDTCLHVAARYNhlSIIRLLL 219
Cdd:PHA02876 454 CKLDVIEMLLDNGADVNAINIQNQYPLLIALEYH--GIVNILL 494
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 104-262 3.43e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 50.26  E-value: 3.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383065 104 LHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKaganVLAKNKAGNT--ALHLACQNSH--- 178
Cdd:PHA02878  41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIR----SINKCSVFYTlvAIKDAFNNRNvei 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383065 179 ------------------------------SQSTRVLLLAGSRADLKN-NAGDTCLHVAARYNHLSIIRLLLTAFCSVHE 227
Cdd:PHA02878 117 fkiiltnrykniqtidlvyidkkskddiieAEITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNI 196

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 530383065 228 KNQAGDTALHVAAALNHKKVAKILLEAGADTTIVN 262
Cdd:PHA02878 197 PDKTNNSPLHHAVKHYNKPIVHILLENGASTDARD 231
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 137-227 8.80e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.13  E-value: 8.80e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383065 137 LHEASWHGFSQSAKLLIKAGANVLAKNKAGNTALHLACQNSHSQSTRVLLLAGSRADLKNNAGDTCLHVAARYNHLSIIR 216
Cdd:PTZ00322  86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165

                         90
                 ....*....|.
gi 530383065 217 LLLTAFCSVHE 227
Cdd:PTZ00322 166 LLSRHSQCHFE 176
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 97-220 1.08e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 48.45  E-value: 1.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383065  97 KEGDqTALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKAGNTALHLACQN 176
Cdd:PHA02875 100 KDGM-TPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAK 178

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 530383065 177 SHSQSTRVLLLAGSRADLKNNAGD-TCLHVAARYNHLSIIRLLLT 220
Cdd:PHA02875 179 GDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIK 223
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 232-263 1.39e-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: 42.28  E-value: 1.39e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 530383065  232 GDTALHVAAA-LNHKKVAKILLEAGADTTIVNN 263
Cdd:pfam00023   2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
Ank_5 pfam13857
Ankyrin repeats (many copies);
152-206 1.41e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.10  E-value: 1.41e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 530383065  152 LIKAG-ANVLAKNKAGNTALHLACQNSHSQSTRVLLLAGSRADLKNNAGDTCLHVA 206
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 132-164 2.50e-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: 41.51  E-value: 2.50e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 530383065  132 DGNTALHEASWH-GFSQSAKLLIKAGANVLAKNK 164
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 200-265 4.15e-05

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: 46.93  E-value: 4.15e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530383065 200 DTCLHVAARYNHL-SIIRLLLTAFCSVHEKNQAGDTALHVAAALNHKKVAKILLEagADTTIVNNVL 265
Cdd:cd22192   18 ESPLLLAAKENDVqAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPELVNEPM 82
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 90-186 1.65e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.89  E-value: 1.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383065  90 PRRSEREKEGDQTALHRATV-------VGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAK 162
Cdd:PTZ00322  65 DHNLTTEEVIDPVVAHMLTVelcqlaaSGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLL 144

                         90       100
                 ....*....|....*....|....
gi 530383065 163 NKAGNTALHLACQNSHSQSTRVLL 186
Cdd:PTZ00322 145 DKDGKTPLELAEENGFREVVQLLS 168
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 232-260 2.04e-04

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: 39.11  E-value: 2.04e-04
                           10        20
                   ....*....|....*....|....*....
gi 530383065   232 GDTALHVAAALNHKKVAKILLEAGADTTI 260
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 156-257 2.19e-04

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: 44.62  E-value: 2.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383065 156 GANVLAKNKAGNTALHLACQNSHSQSTRVLLLAgSRADL--KNNAGDTCLHVAARYNHLSIIRLLLTAfcsVHE-KNQA- 231
Cdd:cd22192    7 ELHLLQQKRISESPLLLAAKENDVQAIKKLLKC-PSCDLfqRGALGETALHVAALYDNLEAAVVLMEA---APElVNEPm 82

                         90       100       110
                 ....*....|....*....|....*....|..
gi 530383065 232 ------GDTALHVAAALNHKKVAKILLEAGAD 257
Cdd:cd22192   83 tsdlyqGETALHIAVVNQNLNLVRELIARGAD 114
PHA02791 PHA02791
ankyrin-like protein; Provisional
 100-229 2.30e-04

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 43.88  E-value: 2.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383065 100 DQTALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKAG--NTALHLACQNS 177
Cdd:PHA02791  61 NEFPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDSGNMQTVKLFVKKNWRLMFYGKTGwkTSFYHAVMLND 140

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 530383065 178 HSQSTRVLLLAGSRADLKNNAgdTCLHVAARYNHLSIIRLLLTAFCSVHEKN 229
Cdd:PHA02791 141 VSIVSYFLSEIPSTFDLAILL--SCIHITIKNGHVDMMILLLDYMTSTNTNN 190
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 101-212 3.49e-04

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: 43.85  E-value: 3.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383065 101 QTALHRATVVGNTEIIAALIHEG-----------CALDRQDKD---GNTALHEASWHGFSQSAKLLIKAGANVLAKNKAG 166
Cdd:cd22192   90 ETALHIAVVNQNLNLVRELIARGadvvspratgtFFRPGPKNLiyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLG 169

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530383065 167 NTALH-LACQNSHSQSTRV--LLLAGSRAD-------LKNNAGDTCLHVAAR------YNHL 212
Cdd:cd22192  170 NTVLHiLVLQPNKTFACQMydLILSYDKEDdlqpldlVPNNQGLTPFKLAAKegnivmFQHL 231
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 133-249 3.58e-04

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: 43.85  E-value: 3.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383065 133 GNTALHEASWHGFSQSAKLLIKAgANVLAKNK------AGNTALHLACQNSHSQSTRVLLLAGsrADLKN---------- 196
Cdd:cd22192   51 GETALHVAALYDNLEAAVVLMEA-APELVNEPmtsdlyQGETALHIAVVNQNLNLVRELIARG--ADVVSpratgtffrp 127

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 530383065 197 NAGDTC------LHVAARYNHLSIIRLLLTAFCSVHEKNQAGDTALHVAAALNHKKVAK 249
Cdd:cd22192  128 GPKNLIyygehpLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTFAC 186
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 199-227 3.60e-04

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: 38.34  E-value: 3.60e-04
                           10        20
                   ....*....|....*....|....*....
gi 530383065   199 GDTCLHVAARYNHLSIIRLLLTAFCSVHE 227
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 199-229 3.91e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.42  E-value: 3.91e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 530383065  199 GDTCLHVAA-RYNHLSIIRLLLTAFCSVHEKN 229
Cdd:pfam00023   2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PHA02798 PHA02798
ankyrin-like protein; Provisional
 101-269 1.38e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 41.74  E-value: 1.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383065 101 QTALHRATVvgNTEIIAALIHEGCALDRQDKDGNTAL-----HEASWHGFSQSAKLLIKAGANVLAKNKAGNTALHLACQ 175
Cdd:PHA02798  41 QKYLQRDSP--STDIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLS 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383065 176 NSHSQSTRVLLLA---GSRADLKNNAGDTCLHVAARYNH---LSIIRLLLTAFCSVHE-KNQAGDTALHVAAALNHKK-- 246
Cdd:PHA02798 119 NGYINNLEILLFMienGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDINThNNKEKYDTLHCYFKYNIDRid 198

                        170       180
                 ....*....|....*....|....*
gi 530383065 247 --VAKILLEAGadtTIVNNVLRFSR 269
Cdd:PHA02798 199 adILKLFVDNG---FIINKENKSHK 220
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 59-219 1.93e-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: 41.61  E-value: 1.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383065   59 ASEIVQDAVATVKAMKEDKNKKNHRGKVRKDPRRSEREKegDQTALHRATVVGNTEIIAALIHEG-------CALDRQDK 131
Cdd:TIGR00870  89 ISLEYVDAVEAILLHLLAAFRKSGPLELANDQYTSEFTP--GITALHLAAHRQNYEIVKLLLERGasvparaCGDFFVKS 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383065  132 DGNTALHeaswHG---------FSQSA--KLLIKAGANVLAKNKAGNTALHLACQNS-----------HSQSTRVLLLAG 189
Cdd:TIGR00870 167 QGVDSFY----HGesplnaaacLGSPSivALLSEDPADILTADSLGNTLLHLLVMENefkaeyeelscQMYNFALSLLDK 242

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 530383065  190 SR-----ADLKNNAGDTCLHVAARYNHLSIIRLLL 219
Cdd:TIGR00870 243 LRdskelEVILNHQGLTPLKLAAKEGRIVLFRLKL 277
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 215-262 2.81e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.04  E-value: 2.81e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 530383065 215 IRLLLTAFCSVHEKNQAGDTALHVAAALNHKKVAKILLEAGADTTIVN 262
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLD 145
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 152-264 2.91e-03

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 41.05  E-value: 2.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383065 152 LIKAGANVLAKNKAGNTA--LHLACQNSHSQSTRVL---LLAGSRADLKNNAGDTCLH--VAARYNHLSIIRLLLTAFCS 224
Cdd:PHA02716 265 ITNIYIESLDGNKVKNIPmiLHSYITLARNIDISVVysfLQPGVKLHYKDSAGRTCLHqyILRHNISTDIIKLLHEYGND 344

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 530383065 225 VHEKNQAGDTALH-------VAAALNHK-------KVAKILLEAGADTTIVNNV 264
Cdd:PHA02716 345 LNEPDNIGNTVLHtylsmlsVVNILDPEtdndirlDVIQCLISLGADITAVNCL 398
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 199-227 3.74e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 35.31  E-value: 3.74e-03
                          10        20
                  ....*....|....*....|....*....
gi 530383065  199 GDTCLHVAARYNHLSIIRLLLTAFCSVHE 227
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
86-140 3.79e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.17  E-value: 3.79e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 530383065   86 VRKDPRRSEREKEGDQTALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEA 140
Cdd:pfam13857   2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 132-159 4.08e-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: 35.26  E-value: 4.08e-03
                           10        20
                   ....*....|....*....|....*...
gi 530383065   132 DGNTALHEASWHGFSQSAKLLIKAGANV 159
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 174-252 4.65e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 40.27  E-value: 4.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383065 174 CQNSHSQST---RVLLLAGSRADLKNNAGDTCLHVAARYNHLSIIRLLLTAFCSVHEKNQAGDTALHVAAALNHKKVAKI 250
Cdd:PTZ00322  87 CQLAASGDAvgaRILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                 ..
gi 530383065 251 LL 252
Cdd:PTZ00322 167 LS 168
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 232-257 5.54e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 34.93  E-value: 5.54e-03
                          10        20
                  ....*....|....*....|....*.
gi 530383065  232 GDTALHVAAALNHKKVAKILLEAGAD 257
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGAD 27
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 170-257 8.45e-03

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 39.68  E-value: 8.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530383065  170 LHLACQNSHSQSTRVLLLAGSRADLknnaGDTCLHVAARYNHL---SIIRLLLTAF---CSVHEKN-------QAGDTAL 236
Cdd:TIGR00870  57 FVAAIENENLELTELLLNLSCRGAV----GDTLLHAISLEYVDaveAILLHLLAAFrksGPLELANdqytsefTPGITAL 132

                          90       100
                  ....*....|....*....|.
gi 530383065  237 HVAAALNHKKVAKILLEAGAD 257
Cdd:TIGR00870 133 HLAAHRQNYEIVKLLLERGAS 153
 
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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