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Conserved domains on  [gi|1370507651|ref|XP_024302132|]
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ankyrin repeat domain-containing protein 6 isoform X25 [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];
14-196 9.33e-49

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 172.45  E-value: 9.33e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507651  14 LLVAAYKGQTENVVQLINKGARV-AVTKHGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIA 92
Cdd:COG0666    58 LLAAALAGDLLVALLLLAAGADInAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVK 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507651  93 ALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKAGDTALHVAAALNHKKVAKILLEAGADTTIVNN 172
Cdd:COG0666   138 LLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN 217

                         170       180
                  ....*....|....*....|....
gi 1370507651 173 AGQTPLETARYHNNPEVALLLTKA 196
Cdd:COG0666   218 DGKTALDLAAENGNLEIVKLLLEA 241
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
14-196 9.33e-49

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 172.45  E-value: 9.33e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507651  14 LLVAAYKGQTENVVQLINKGARV-AVTKHGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIA 92
Cdd:COG0666    58 LLAAALAGDLLVALLLLAAGADInAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVK 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507651  93 ALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKAGDTALHVAAALNHKKVAKILLEAGADTTIVNN 172
Cdd:COG0666   138 LLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN 217

                         170       180
                  ....*....|....*....|....
gi 1370507651 173 AGQTPLETARYHNNPEVALLLTKA 196
Cdd:COG0666   218 DGKTALDLAAENGNLEIVKLLLEA 241
Ank_2 pfam12796
Ankyrin repeats (3 copies);
46-138 7.41e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 90.18  E-value: 7.41e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507651  46 LHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIAALIhEGCALDRQDkDGNTALHEASWHGFSQSAK 125
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1370507651 126 LLIKAGANVLAKN 138
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 29-199 1.48e-21

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 98.17  E-value: 1.48e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507651  29 LINKGARV-AVTKHGRTPLH-LAANKG-HLPVVQILLKAGCDLDVQDDGDQTALH------RAtvvgNTEIIAALIHEGC 99
Cdd:PHA03095  138 LLRKGADVnALDLYGMTPLAvLLKSRNaNVELLRLLIDAGADVYAVDDRFRSLLHhhlqsfKP----RARIVRELIRAGC 213

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507651 100 ALDRQDKDGNTALHEASWHGFSQSAKL--LIKAGANVLAKNKAGDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQTP 177
Cdd:PHA03095  214 DPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTP 293

                         170       180
                  ....*....|....*....|...
gi 1370507651 178 LETARYHNNPE-VALLLTKAPQV 199
Cdd:PHA03095  294 LSLMVRNNNGRaVRAALAKNPSA 316
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 44-178 1.61e-08

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: 57.72  E-value: 1.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507651  44 TPLHLAANKGHLPVVQILLK-AGCDLDVQDDGDQTALHRATVVGNTEIIAALIHEGCALDRQDK-----DGNTALHEASW 117
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEPMtsdlyQGETALHIAVV 98

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370507651 118 HGFSQSAKLLIKAGANVL------------AKNKA--GDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQTPL 178
Cdd:cd22192    99 NQNLNLVRELIARGADVVspratgtffrpgPKNLIyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 41-70 3.83e-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: 43.73  E-value: 3.83e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 1370507651   41 HGRTPLHLAANKGHLPVVQILLKAGCDLDV 70
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 41-193 2.42e-04

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: 44.30  E-value: 2.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507651  41 HGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGD--------------QTALHRATVVGNTEIIAALIHEGCALDRQDK 106
Cdd:TIGR00870 127 PGITALHLAAHRQNYEIVKLLLERGASVPARACGDffvksqgvdsfyhgESPLNAAACLGSPSIVALLSEDPADILTADS 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507651 107 DGNTALHeaswhgfsqsakllikaGANVLAKNKAGDTALhvaaALNHKKVAKILLEAGADTT----IVNNAGQTPLETAR 182
Cdd:TIGR00870 207 LGNTLLH-----------------LLVMENEFKAEYEEL----SCQMYNFALSLLDKLRDSKelevILNHQGLTPLKLAA 265

                         170
                  ....*....|.
gi 1370507651 183 YHNNPEVALLL 193
Cdd:TIGR00870 266 KEGRIVLFRLK 276
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
14-196 9.33e-49

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 172.45  E-value: 9.33e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507651  14 LLVAAYKGQTENVVQLINKGARV-AVTKHGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIA 92
Cdd:COG0666    58 LLAAALAGDLLVALLLLAAGADInAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVK 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507651  93 ALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKAGDTALHVAAALNHKKVAKILLEAGADTTIVNN 172
Cdd:COG0666   138 LLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN 217

                         170       180
                  ....*....|....*....|....
gi 1370507651 173 AGQTPLETARYHNNPEVALLLTKA 196
Cdd:COG0666   218 DGKTALDLAAENGNLEIVKLLLEA 241
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
14-196 3.36e-47

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 168.21  E-value: 3.36e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507651  14 LLVAAYKGQTENVVQLINKGARV-AVTKHGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIA 92
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGADVnARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507651  93 ALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKAGDTALHVAAALNHKKVAKILLEAGADTTIVNN 172
Cdd:COG0666   171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250

                         170       180
                  ....*....|....*....|....
gi 1370507651 173 AGQTPLETARYHNNPEVALLLTKA 196
Cdd:COG0666   251 DGLTALLLAAAAGAALIVKLLLLA 274
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-196 3.81e-39

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 145.87  E-value: 3.81e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507651   1 MSQQDAVAALSERLLVAAYKGQTENVVQLINKGARVAVTKHGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALH 80
Cdd:COG0666    13 AALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLH 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507651  81 RATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKAGDTALHVAAALNHKKVAKIL 160
Cdd:COG0666    93 AAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLL 172

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1370507651 161 LEAGADTTIVNNAGQTPLETARYHNNPEVALLLTKA 196
Cdd:COG0666   173 LEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA 208
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
14-178 7.52e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 139.70  E-value: 7.52e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507651  14 LLVAAYKGQTENVVQLINKGARV-AVTKHGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIA 92
Cdd:COG0666   124 LHLAAYNGNLEIVKLLLEAGADVnAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVK 203

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507651  93 ALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKAGDTALHVAAALNHKKVAKILLEAGADTTIVNN 172
Cdd:COG0666   204 LLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283


                  ....*.
gi 1370507651 173 AGQTPL 178
Cdd:COG0666   284 DLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
24-193 2.50e-28

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 115.05  E-value: 2.50e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507651  24 ENVVQLINKGARVAVTKHGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIAALIHEGCALDR 103
Cdd:COG0666     3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507651 104 QDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKAGDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQTPLETARY 183
Cdd:COG0666    83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162

                         170
                  ....*....|
gi 1370507651 184 HNNPEVALLL 193
Cdd:COG0666   163 NGNLEIVKLL 172
Ank_2 pfam12796
Ankyrin repeats (3 copies);
46-138 7.41e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 90.18  E-value: 7.41e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507651  46 LHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIAALIhEGCALDRQDkDGNTALHEASWHGFSQSAK 125
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1370507651 126 LLIKAGANVLAKN 138
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 29-199 1.48e-21

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 98.17  E-value: 1.48e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507651  29 LINKGARV-AVTKHGRTPLH-LAANKG-HLPVVQILLKAGCDLDVQDDGDQTALH------RAtvvgNTEIIAALIHEGC 99
Cdd:PHA03095  138 LLRKGADVnALDLYGMTPLAvLLKSRNaNVELLRLLIDAGADVYAVDDRFRSLLHhhlqsfKP----RARIVRELIRAGC 213

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507651 100 ALDRQDKDGNTALHEASWHGFSQSAKL--LIKAGANVLAKNKAGDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQTP 177
Cdd:PHA03095  214 DPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTP 293

                         170       180
                  ....*....|....*....|...
gi 1370507651 178 LETARYHNNPE-VALLLTKAPQV 199
Cdd:PHA03095  294 LSLMVRNNNGRaVRAALAKNPSA 316
Ank_2 pfam12796
Ankyrin repeats (3 copies);
14-105 1.62e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.55  E-value: 1.62e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507651  14 LLVAAYKGQTENVVQLINKGARV-AVTKHGRTPLHLAANKGHLPVVQILLKaGCDLDVQDDGdQTALHRATVVGNTEIIA 92
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADAnLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDNG-RTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1370507651  93 ALIHEGCALDRQD 105
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 26-199 1.69e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 88.18  E-value: 1.69e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507651  26 VVQLINKGARVAV-TKHGRTPLHLAANKGH-----LPVVQILLKAGCDLDVQDDGDQTALHRA--TVVGNTEIIAALIHE 97
Cdd:PHA03100   51 VKILLDNGADINSsTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVNAPDNNGITPLLYAisKKSNSYSIVEYLLDN 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507651  98 GCALDRQDKDGNTALHEA--SWHGFSQSAKLLIKAGANVLAKNKA----------------GDTALHVAAALNHKKVAKI 159
Cdd:PHA03100  131 GANVNIKNSDGENLLHLYleSNKIDLKILKLLIDKGVDINAKNRVnyllsygvpinikdvyGFTPLHYAVYNNNPEFVKY 210

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1370507651 160 LLEAGADTTIVNNAGQTPLETARYHNNPE-VALLLTKAPQV 199
Cdd:PHA03100  211 LLDLGANPNLVNKYGDTPLHIAILNNNKEiFKLLLNNGPSI 251
PHA03095 PHA03095
ankyrin-like protein; Provisional
 24-180 1.15e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 83.15  E-value: 1.15e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507651  24 ENVVQLINKGARVAVTK-HGRTPLHLAANKGHLP---VVQILLKAGCDLDVQDDGDQTALHRATVVGNTE-IIAALIHEG 98
Cdd:PHA03095   28 EEVRRLLAAGADVNFRGeYGKTPLHLYLHYSSEKvkdIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAG 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507651  99 CALDRQDKDGNTALHeASWHGFSQSAK---LLIKAGANVLAKNKAGDTALHV-----AAALnhkKVAKILLEAGADTTIV 170
Cdd:PHA03095  108 ADVNAKDKVGRTPLH-VYLSGFNINPKvirLLLRKGADVNALDLYGMTPLAVllksrNANV---ELLRLLIDAGADVYAV 183

                         170
                  ....*....|
gi 1370507651 171 NNAGQTPLET 180
Cdd:PHA03095  184 DDRFRSLLHH 193
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
55-196 1.41e-16

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 80.77  E-value: 1.41e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507651  55 LPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANV 134
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370507651 135 LAKNKAGDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQTPLETARYHNNPEVALLLTKA 196
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA 142
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 22-181 2.66e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 81.85  E-value: 2.66e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507651  22 QTENVVQLINKGARV-AVTKH-GRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIAALIHEGC 99
Cdd:PHA02878  146 EAEITKLLLSYGADInMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA 225

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507651 100 ALDRQDKDGNTALHEASWHGFSQSA-KLLIKAGANVLAKNKA-GDTALHVaaALNHKKVAKILLEAGADTTIVNNAGQTP 177
Cdd:PHA02878  226 STDARDKCGNTPLHISVGYCKDYDIlKLLLEHGVDVNAKSYIlGLTALHS--SIKSERKLKLLLEYGADINSLNSYKLTP 303


                  ....
gi 1370507651 178 LETA 181
Cdd:PHA02878  304 LSSA 307
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 42-171 2.80e-16

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 82.99  E-value: 2.80e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507651  42 GRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIAALIHEGCALDRQdkDGNTALHEASWHGFS 121
Cdd:PLN03192  558 GRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPH--AAGDLLCTAAKRNDL 635

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1370507651 122 QSAKLLIKAGANVLAKNKAGDTALHVAAALNHKKVAKILLEAGADTTIVN 171
Cdd:PLN03192  636 TAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAN 685
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 15-185 9.58e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 80.88  E-value: 9.58e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507651  15 LVAAYKGQTENVVQLINKGARV-AVTKHGRTPLHLAAN-KGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIA 92
Cdd:PHA02876  313 LMAKNGYDTENIRTLIMLGADVnAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIIN 392

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507651  93 ALIHEGCALDRQDKDGNTALHEAsWHGFS--QSAKLLIKAGANVLAKNKAGDTALHVAAALNHK-KVAKILLEAGADTTI 169
Cdd:PHA02876  393 TLLDYGADIEALSQKIGTALHFA-LCGTNpyMSVKTLIDRGANVNSKNKDLSTPLHYACKKNCKlDVIEMLLDNGADVNA 471

                         170
                  ....*....|....*..
gi 1370507651 170 VNNAGQTPLETA-RYHN 185
Cdd:PHA02876  472 INIQNQYPLLIAlEYHG 488
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 22-235 1.66e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 79.24  E-value: 1.66e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507651  22 QTENVVQLINKGARVAV-TKHGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIAALIHEGCA 100
Cdd:PHA02874  103 EKDMIKTILDCGIDVNIkDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAY 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507651 101 LDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKAGDTALHVAAALNHKKVAKILLEAGADTTIVNnaGQTPLET 180
Cdd:PHA02874  183 ANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAIELLINNASINDQDID--GSTPLHH 260

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370507651 181 A-RYHNNPEV--ALLLTKAPQVLRFSRGRSLRK------KRERLKEERRAQSVPRDEVAQSKGS 235
Cdd:PHA02874  261 AiNPPCDIDIidILLYHKADISIKDNKGENPIDtafkyiNKDPVIKDIIANAVLIKEADKLKDS 324
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 29-172 2.05e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 75.86  E-value: 2.05e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507651  29 LINKGARV-AVTKHGRTPLHLAANK--GHLPVVQILLKAGCDLDVQDDGDQTALHRATVVG--NTEIIAALIHEG----- 98
Cdd:PHA03100   92 LLEYGANVnAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNkiDLKILKLLIDKGvdina 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507651  99 -----------CALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKAGDTALHVAAALNHKKVAKILLEAGADT 167
Cdd:PHA03100  172 knrvnyllsygVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSI 251


                  ....*
gi 1370507651 168 TIVNN 172
Cdd:PHA03100  252 KTIIE 256
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 40-195 2.67e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 75.47  E-value: 2.67e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507651  40 KHGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVG-----NTEIIAALIHEGCALDRQDKDGNTALHE 114
Cdd:PHA03100   33 KKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKynltdVKEIVKLLLEYGANVNAPDNNGITPLLY 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507651 115 ASWHGFSQSA--KLLIKAGANVLAKNKAGDTALHVAAALNH--KKVAKILLEAGAD----------------TTIVNNAG 174
Cdd:PHA03100  113 AISKKSNSYSivEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDinaknrvnyllsygvpINIKDVYG 192

                         170       180
                  ....*....|....*....|..
gi 1370507651 175 QTPLETARYHNNPE-VALLLTK 195
Cdd:PHA03100  193 FTPLHYAVYNNNPEfVKYLLDL 214
Ank_2 pfam12796
Ankyrin repeats (3 copies);
112-193 3.04e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 68.60  E-value: 3.04e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507651 112 LHEASWHGFSQSAKLLIKAGANVLAKNKAGDTALHVAAALNHKKVAKILLEaGADTTIVNNaGQTPLETARYHNNPEVAL 191
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIVK 78


                  ..
gi 1370507651 192 LL 193
Cdd:pfam12796  79 LL 80
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 17-217 5.51e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 74.26  E-value: 5.51e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507651  17 AAYKGQTENVVQLI--NKGARVAVTKHGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIAAL 94
Cdd:PHA02875   75 AVEEGDVKAVEELLdlGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELL 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507651  95 IHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKAGDTALHVAAALNHK-KVAKILLEAGADTTI---V 170
Cdd:PHA02875  155 IDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKiDIVRLFIKRGADCNImfmI 234

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507651 171 NNAGQTPLETAR-YHNNPEV-ALLLTKAPQVLR-----------FSRGRSLRKKRERLKE 217
Cdd:PHA02875  235 EGEECTILDMICnMCTNLESeAIDALIADIAIRihkktirrdegFKNNMSTIEDKEEFKD 294
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 57-193 3.79e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 69.14  E-value: 3.79e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507651  57 VVQILLKAGCDLDVQD-DGDQTALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVL 135
Cdd:PHA02878  149 ITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTD 228

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507651 136 AKNKAGDTALHVAAA-LNHKKVAKILLEAGADTTIVNNA-GQTPLETArYHNNPEVALLL 193
Cdd:PHA02878  229 ARDKCGNTPLHISVGyCKDYDILKLLLEHGVDVNAKSYIlGLTALHSS-IKSERKLKLLL 287
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 14-181 6.46e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 68.07  E-value: 6.46e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507651  14 LLVAAYKGQTENVVQLINKGARVAVTK-HGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIA 92
Cdd:PHA02874  128 LHYAIKKGDLESIKMLFEYGADVNIEDdNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIK 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507651  93 ALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNkaGDTALHvaAALNH---KKVAKILLEAGADTTI 169
Cdd:PHA02874  208 LLIDHGNHIMNKCKNGFTPLHNAIIHNRSAIELLINNASINDQDID--GSTPLH--HAINPpcdIDIIDILLYHKADISI 283

                         170
                  ....*....|..
gi 1370507651 170 VNNAGQTPLETA 181
Cdd:PHA02874  284 KDNKGENPIDTA 295
Ank_4 pfam13637
Ankyrin repeats (many copies);
42-95 5.63e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.05  E-value: 5.63e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1370507651  42 GRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIAALI 95
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 10-194 1.97e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 63.44  E-value: 1.97e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507651  10 LSERLLVAAYKGQTENVVQLI-NKGARVAVT-KHGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGN 87
Cdd:PHA02874    1 ASQDLRMCIYSGDIEAIEKIIkNKGNCINISvDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507651  88 TEIIAALIHEG---------------------CALD--RQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKAGDTA 144
Cdd:PHA02874   81 HDIIKLLIDNGvdtsilpipciekdmiktildCGIDvnIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYP 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1370507651 145 LHVAAALNHKKVAKILLEAGADTTIVNNAGQTPLE-TARYHNNPEVALLLT 194
Cdd:PHA02874  161 IHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHnAAEYGDYACIKLLID 211
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 14-187 1.14e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 61.62  E-value: 1.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507651  14 LLVAAYKGQTENVVQLINKGARV-AVTKHGRTPLHLAANKGHLP-VVQILLKAGCDLDVQDDGDQTALHRATVVG-NTEI 90
Cdd:PHA02876  244 LLKAIRNEDLETSLLLYDAGFSVnSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMAKNGyDTEN 323

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507651  91 IAALIHEGCALDRQDKDGNTALHEAS-WHGFSQSAKLLIKAGANVLAKNKAGDTALHVAAALNHKKVAKILLEAGADTTI 169
Cdd:PHA02876  324 IRTLIMLGADVNAADRLYITPLHQAStLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEA 403

                         170
                  ....*....|....*...
gi 1370507651 170 VNNAGQTPLETARYHNNP 187
Cdd:PHA02876  404 LSQKIGTALHFALCGTNP 421
Ank_5 pfam13857
Ankyrin repeats (many copies);
40-82 3.36e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 53.12  E-value: 3.36e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1370507651  40 KHGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRA 82
Cdd:pfam13857  14 GEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 42-204 4.35e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 58.85  E-value: 4.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507651  42 GRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIAALIHEGC-ALDRQDKDGNTALHEASWHGF 120
Cdd:PHA02875   35 GISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKfADDVFYKDGMTPLHLATILKK 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507651 121 SQSAKLLIKAGANVLAKNKAGDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQTPLETARYHNNPEVA-LLLTKAPQV 199
Cdd:PHA02875  115 LDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICkMLLDSGANI 194


                  ....*
gi 1370507651 200 LRFSR 204
Cdd:PHA02875  195 DYFGK 199
Ank_4 pfam13637
Ankyrin repeats (many copies);
77-128 5.22e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.28  E-value: 5.22e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1370507651  77 TALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLI 128
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 71-198 8.22e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 58.76  E-value: 8.22e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507651  71 QDDGDQTALHRATVvgnteiiaalihEGCALdrqdkdgntalhEASwhGFSQSAKLLIKAGANVLAKNKAGDTALHVAAA 150
Cdd:PTZ00322   71 EEVIDPVVAHMLTV------------ELCQL------------AAS--GDAVGARILLTGGADPNCRDYDGRTPLHIACA 124

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1370507651 151 LNHKKVAKILLEAGADTTIVNNAGQTPLETARYHNNPEVALLLTKAPQ 198
Cdd:PTZ00322  125 NGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQ 172
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 44-178 1.61e-08

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: 57.72  E-value: 1.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507651  44 TPLHLAANKGHLPVVQILLK-AGCDLDVQDDGDQTALHRATVVGNTEIIAALIHEGCALDRQDK-----DGNTALHEASW 117
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEPMtsdlyQGETALHIAVV 98

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370507651 118 HGFSQSAKLLIKAGANVL------------AKNKA--GDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQTPL 178
Cdd:cd22192    99 NQNLNLVRELIARGADVVspratgtffrpgPKNLIyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 29-178 1.61e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 57.77  E-value: 1.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507651  29 LINKGARV-AVTKHGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIAALIHEGCALDRQDkd 107
Cdd:PHA02876  164 LLEGGADVnAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKND-- 241

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370507651 108 gnTALHEASWHGFSQSAKLLIKAGANVLAKNKAGDTALHVAA-ALNHKKVAKILLEAGADTTIVNNAGQTPL 178
Cdd:PHA02876  242 --LSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASqAPSLSRLVPKLLERGADVNAKNIKGETPL 311
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 41-73 4.79e-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: 49.21  E-value: 4.79e-08
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1370507651  41 HGRTPLHLAANK-GHLPVVQILLKAGCDLDVQDD 73
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 11-189 7.88e-08

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: 55.40  E-value: 7.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507651  11 SERLLVAAYKgqtENVVQLINKGARVAVTK------HGRTPLHLAANKGHLPVVQILLKAGCDL-DVQDDGD----QTAL 79
Cdd:cd22192    17 SESPLLLAAK---ENDVQAIKKLLKCPSCDlfqrgaLGETALHVAALYDNLEAAVVLMEAAPELvNEPMTSDlyqgETAL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507651  80 HRATVVGNTEIIAALIHEG-----------CALDRQDKD---GNTALHEASWHGFSQSAKLLIKAGANVLAKNKAGDTAL 145
Cdd:cd22192    94 HIAVVNQNLNLVRELIARGadvvspratgtFFRPGPKNLiyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1370507651 146 HVAAALNHKKVAK-----IL-LEAGADT----TIVNNAGQTPLETARYHNNPEV 189
Cdd:cd22192   174 HILVLQPNKTFACqmydlILsYDKEDDLqpldLVPNNQGLTPFKLAAKEGNIVM 227
Ank_4 pfam13637
Ankyrin repeats (many copies);
141-193 9.67e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.81  E-value: 9.67e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1370507651 141 GDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQTPLETARYHNNPEVALLL 193
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
Ank_5 pfam13857
Ankyrin repeats (many copies);
127-181 6.42e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.57  E-value: 6.42e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1370507651 127 LIKAG-ANVLAKNKAGDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQTPLETA 181
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
108-161 7.65e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.50  E-value: 7.65e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1370507651 108 GNTALHEASWHGFSQSAKLLIKAGANVLAKNKAGDTALHVAAALNHKKVAKILL 161
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 44-185 1.37e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 49.43  E-value: 1.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507651  44 TPLH--LAANKGHLPVVQILLKAGCDLDVQDDGDQ-TALHRATVVG---NTEIIAALIHEGCALDRQDKDGNTALHeASW 117
Cdd:PHA02859   53 TPIFscLEKDKVNVEILKFLIENGADVNFKTRDNNlSALHHYLSFNknvEPEILKILIDSGSSITEEDEDGKNLLH-MYM 131

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370507651 118 HGFS---QSAKLLIKAGANVLAKNKAGDTALHVAAAL-NHKKVAKILLEAGADTTIVNNAGQTPLETARYHN 185
Cdd:PHA02859  132 CNFNvriNVIKLLIDSGVSFLNKDFDNNNILYSYILFhSDKKIFDFLTSLGIDINETNKSGYNCYDLIKFRN 203
Ank_2 pfam12796
Ankyrin repeats (3 copies);
145-207 1.59e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 46.65  E-value: 1.59e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370507651 145 LHVAAALNHKKVAKILLEAGADTTIVNNAGQTPLETARYHNNPEVALLLTKAPQVLRFSRGRS 207
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGRT 63
Ank_5 pfam13857
Ankyrin repeats (many copies);
96-148 2.64e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.03  E-value: 2.64e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1370507651  96 HEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKAGDTALHVA 148
Cdd:pfam13857   4 HGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 41-70 3.83e-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: 43.73  E-value: 3.83e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 1370507651   41 HGRTPLHLAANKGHLPVVQILLKAGCDLDV 70
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 41-70 6.19e-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: 43.01  E-value: 6.19e-06
                          10        20        30
                  ....*....|....*....|....*....|
gi 1370507651  41 HGRTPLHLAANKGHLPVVQILLKAGCDLDV 70
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 141-172 1.37e-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: 1.37e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1370507651 141 GDTALHVAAA-LNHKKVAKILLEAGADTTIVNN 172
Cdd:pfam00023   2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 10-111 2.06e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.59  E-value: 2.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507651  10 LSERLLVAAYKGQTENVVQLINKGARV-AVTKHGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNT 88
Cdd:PTZ00322   82 LTVELCQLAASGDAVGARILLTGGADPnCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFR 161

                          90       100
                  ....*....|....*....|...
gi 1370507651  89 EIIAALIheGCALDRQDKDGNTA 111
Cdd:PTZ00322  162 EVVQLLS--RHSQCHFELGANAK 182
PHA02791 PHA02791
ankyrin-like protein; Provisional
 41-161 2.17e-05

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 46.57  E-value: 2.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507651  41 HGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDgdQTALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGF 120
Cdd:PHA02791   29 HGHSALYYAIADNNVRLVCTLLNAGALKNLLEN--EFPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDSGN 106

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1370507651 121 SQSAKLLIKAGANVLAKNKAG-DTALHVAAALNHKKVAKILL 161
Cdd:PHA02791  107 MQTVKLFVKKNWRLMFYGKTGwKTSFYHAVMLNDVSIVSYFL 148
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 107-139 2.42e-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: 2.42e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1370507651 107 DGNTALHEASWH-GFSQSAKLLIKAGANVLAKNK 139
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 57-178 9.08e-05

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 45.67  E-value: 9.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507651  57 VVQILLKAGCDLDVQDDGDQTALHRATVVGN--TEIIAALIHEGCALDRQDKDGNTALHeaswhgfSQSAKLLIkagANV 134
Cdd:PHA02716  299 VVYSFLQPGVKLHYKDSAGRTCLHQYILRHNisTDIIKLLHEYGNDLNEPDNIGNTVLH-------TYLSMLSV---VNI 368

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1370507651 135 LAKNKAGDTALhvaaalnhkKVAKILLEAGADTTIVNNAGQTPL 178
Cdd:PHA02716  369 LDPETDNDIRL---------DVIQCLISLGADITAVNCLGYTPL 403
PHA03095 PHA03095
ankyrin-like protein; Provisional
 125-196 9.16e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 45.40  E-value: 9.16e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370507651 125 KLLIKAGANVLAKNKAGDTALHVAAALNHKKVAKI---LLEAGADTTIVNNAGQTPLETARYHNN-PEVALLLTKA 196
Cdd:PHA03095   31 RRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIvrlLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKA 106
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 125-199 1.18e-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: 45.39  E-value: 1.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507651 125 KLLIKAGANVLAKNKAGDTALHVAAALNHKKVAKILLEagADTTIVNNA-------GQTPLETARYHNNPE-VALLLTKA 196
Cdd:cd22192    35 KLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPELVNEPmtsdlyqGETALHIAVVNQNLNlVRELIARG 112


                  ...
gi 1370507651 197 PQV 199
Cdd:cd22192   113 ADV 115
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 47-129 1.39e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.89  E-value: 1.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507651  47 HLAANkGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKL 126
Cdd:PTZ00322   88 QLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                  ...
gi 1370507651 127 LIK 129
Cdd:PTZ00322  167 LSR 169
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 141-169 1.84e-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: 1.84e-04
                           10        20
                   ....*....|....*....|....*....
gi 1370507651  141 GDTALHVAAALNHKKVAKILLEAGADTTI 169
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 41-193 2.42e-04

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: 44.30  E-value: 2.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507651  41 HGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGD--------------QTALHRATVVGNTEIIAALIHEGCALDRQDK 106
Cdd:TIGR00870 127 PGITALHLAAHRQNYEIVKLLLERGASVPARACGDffvksqgvdsfyhgESPLNAAACLGSPSIVALLSEDPADILTADS 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507651 107 DGNTALHeaswhgfsqsakllikaGANVLAKNKAGDTALhvaaALNHKKVAKILLEAGADTT----IVNNAGQTPLETAR 182
Cdd:TIGR00870 207 LGNTLLH-----------------LLVMENEFKAEYEEL----SCQMYNFALSLLDKLRDSKelevILNHQGLTPLKLAA 265

                         170
                  ....*....|.
gi 1370507651 183 YHNNPEVALLL 193
Cdd:TIGR00870 266 KEGRIVLFRLK 276
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 125-195 2.73e-04

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 41.79  E-value: 2.73e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370507651 125 KLLIKAGANVLAKN-KAGDTALHVAAALNHKKVAKILL-EAGADTTIVNNAGQTPLETARYHNNPEVALLLTK 195
Cdd:PHA02736   75 KLLMEWGADINGKErVFGNTPLHIAVYTQNYELATWLCnQPGVNMEILNYAFKTPYYVACERHDAKMMNILRA 147
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 42-181 4.72e-04

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


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 43.30  E-value: 4.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507651  42 GRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGD-------------QTALHRATVVGNTEIIAALI---HEGCALDRQD 105
Cdd:cd22197    94 GHSALHIAIEKRSLQCVKLLVENGADVHARACGRffqkkqgtcfyfgELPLSLAACTKQWDVVNYLLenpHQPASLQAQD 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507651 106 KDGNTALHEaswhgfsqsaklLIkaganVLAKNKAGDTALHVaaalnhkKVAKILLEAGADTT-------IVNNAGQTPL 178
Cdd:cd22197   174 SLGNTVLHA------------LV-----MIADNSPENSALVI-------KMYDGLLQAGARLCptvqleeISNHEGLTPL 229


                  ...
gi 1370507651 179 ETA 181
Cdd:cd22197   230 KLA 232
PHA02798 PHA02798
ankyrin-like protein; Provisional
 76-179 6.33e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 42.90  E-value: 6.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507651  76 QTALHRATVvgNTEIIAALIHEGCALDRQDKDGNTAL-----HEASWHGFSQSAKLLIKAGANVLAKNKAGDTALHVA-- 148
Cdd:PHA02798   41 QKYLQRDSP--STDIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLls 118

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1370507651 149 -AALNHKKVAKILLEAGADTTIVNNAGQTPLE 179
Cdd:PHA02798  119 nGYINNLEILLFMIENGADTTLLDKDGFTMLQ 150
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 124-186 1.16e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 41.97  E-value: 1.16e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370507651 124 AKLLIKAGANVLAKNKAGDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQTPLETARYHNN 186
Cdd:PHA02876  161 AEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKN 223
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 42-162 1.20e-03

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 42.05  E-value: 1.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507651  42 GRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGD--------------QTALHRATVVGNTEIIaALIHEGCALD--RQD 105
Cdd:cd22194   141 GQTALNIAIERRQGDIVKLLIAKGADVNAHAKGVffnpkykhegfyfgETPLALAACTNQPEIV-QLLMEKESTDitSQD 219

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370507651 106 KDGNTALH---EASWHGFSQSA-------KLLIKAGANVLAK--NKAGDTALHVAAALNHKKVAKILLE 162
Cdd:cd22194   220 SRGNTVLHalvTVAEDSKTQNDfvkrmydMILLKSENKNLETirNNEGLTPLQLAAKMGKAEILKYILS 288
PHA02798 PHA02798
ankyrin-like protein; Provisional
 14-181 2.82e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 40.59  E-value: 2.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507651  14 LLVAAYKGQTENVVQLINKGARV-AVTKHGRTPLHLAANKGH---LPVVQILLKAGCDLDVQDDGDQ-TALH----RATV 84
Cdd:PHA02798  116 LLSNGYINNLEILLFMIENGADTtLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDINTHNNKEKyDTLHcyfkYNID 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507651  85 VGNTEIIAALIHEGCALDRQDKDGNTALHE------ASWHGFSQSAKLLIKAGANVLAKNKAGDTALHVAAALNHKKVAK 158
Cdd:PHA02798  196 RIDADILKLFVDNGFIINKENKSHKKKFMEylnsllYDNKRFKKNILDFIFSYIDINQVDELGFNPLYYSVSHNNRKIFE 275

                         170       180
                  ....*....|....*....|...
gi 1370507651 159 ILLEAGADTTIVNNAGQTPLETA 181
Cdd:PHA02798  276 YLLQLGGDINIITELGNTCLFTA 298
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 107-134 3.69e-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: 3.69e-03
                           10        20
                   ....*....|....*....|....*...
gi 1370507651  107 DGNTALHEASWHGFSQSAKLLIKAGANV 134
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 141-166 5.01e-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: 5.01e-03
                          10        20
                  ....*....|....*....|....*.
gi 1370507651 141 GDTALHVAAALNHKKVAKILLEAGAD 166
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGAD 27
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 132-197 5.11e-03

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 40.13  E-value: 5.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507651 132 ANVLAKNKAGDTALHVAAALNHKKVAKILLEAGADTTI---------VNNA-----GQTPLETARYHNNPE-VALLLTKA 196
Cdd:cd22194   132 AEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAhakgvffnpKYKHegfyfGETPLALAACTNQPEiVQLLMEKE 211


                  .
gi 1370507651 197 P 197
Cdd:cd22194   212 S 212
 
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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