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Conserved domains on  [gi|1370507653|ref|XP_024302133|]
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ankyrin repeat domain-containing protein 6 isoform X26 [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 1.42e-44

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 160.89  E-value: 1.42e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507653  14 LLVAAYKGQTENVVQLINKGARV-AVTKHGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIA 92
Cdd:COG0666    58 LLAAALAGDLLVALLLLAAGADInAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVK 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507653  93 ALIHEGCALDRQDKAGNTALHLACQNSHSQSTRVLLLAGSRADLKNNAGDTALHVAAALNHKKVAKILLEAGADTTIVNN 172
Cdd:COG0666   138 LLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN 217

                         170       180
                  ....*....|....*....|....
gi 1370507653 173 AGQTPLETARYHNNPEVALLLTKA 196
Cdd:COG0666   218 DGKTALDLAAENGNLEIVKLLLEA 241
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
14-196 1.42e-44

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 160.89  E-value: 1.42e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507653  14 LLVAAYKGQTENVVQLINKGARV-AVTKHGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIA 92
Cdd:COG0666    58 LLAAALAGDLLVALLLLAAGADInAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVK 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507653  93 ALIHEGCALDRQDKAGNTALHLACQNSHSQSTRVLLLAGSRADLKNNAGDTALHVAAALNHKKVAKILLEAGADTTIVNN 172
Cdd:COG0666   138 LLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN 217

                         170       180
                  ....*....|....*....|....
gi 1370507653 173 AGQTPLETARYHNNPEVALLLTKA 196
Cdd:COG0666   218 DGKTALDLAAENGNLEIVKLLLEA 241
PHA03095 PHA03095
ankyrin-like protein; Provisional
 29-199 2.71e-21

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 97.40  E-value: 2.71e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507653  29 LINKGARV-AVTKHGRTPLH-LAANKG-HLPVVQILLKAGCDLDVQDDGDQTALH------RAtvvgNTEIIAALIHEGC 99
Cdd:PHA03095  138 LLRKGADVnALDLYGMTPLAvLLKSRNaNVELLRLLIDAGADVYAVDDRFRSLLHhhlqsfKP----RARIVRELIRAGC 213

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507653 100 ALDRQDKAGNTALHLACQNSHSQSTRV--LLLAGSRADLKNNAGDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQTP 177
Cdd:PHA03095  214 DPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTP 293

                         170       180
                  ....*....|....*....|...
gi 1370507653 178 LETARYHNNPE-VALLLTKAPQV 199
Cdd:PHA03095  294 LSLMVRNNNGRaVRAALAKNPSA 316
Ank_2 pfam12796
Ankyrin repeats (3 copies);
79-171 1.73e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 86.32  E-value: 1.73e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507653  79 LHRATVVGNTEIIAALIHEGCALDRQDKAGNTALHLACQNSHSQSTRvLLLAGSRADLKNNaGDTALHVAAALNHKKVAK 158
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVK-LLLEHADVNLKDN-GRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1370507653 159 ILLEAGADTTIVN 171
Cdd:pfam12796  79 LLLEKGADINVKD 91
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 7-150 6.19e-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: 55.79  E-value: 6.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507653   7 VAALSERLLVAayKGQTENVVQLINkgarVAVTKH---GRTPLHLAANKGHLPVVQILLKAGCDLdvqddgdQTAlhRAT 83
Cdd:cd22192    57 VAALYDNLEAA--VVLMEAAPELVN----EPMTSDlyqGETALHIAVVNQNLNLVRELIARGADV-------VSP--RAT 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507653  84 -----------------------VVGNTEIIAALIHEGCALDRQDKAGNTALH-LACQNSHSQSTRV--LLLAGSRAD-- 135
Cdd:cd22192   122 gtffrpgpknliyygehplsfaaCVGNEEIVRLLIEHGADIRAQDSLGNTVLHiLVLQPNKTFACQMydLILSYDKEDdl 201

                         170       180
                  ....*....|....*....|
gi 1370507653 136 -----LKNNAGDTALHVAAA 150
Cdd:cd22192   202 qpldlVPNNQGLTPFKLAAK 221
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 1370507653   41 HGRTPLHLAANKGHLPVVQILLKAGCDLDV 70
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 41-162 1.02e-05

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 48.92  E-value: 1.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507653  41 HGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGD--------------QTALHRATVVGNTEIIAALIHEGCALDRQDK 106
Cdd:TIGR00870 127 PGITALHLAAHRQNYEIVKLLLERGASVPARACGDffvksqgvdsfyhgESPLNAAACLGSPSIVALLSEDPADILTADS 206

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370507653 107 AGNTALHLACQNS-----------HSQSTRVLLLAGSR-----ADLKNNAGDTALHVAAALNHKKVAKILLE 162
Cdd:TIGR00870 207 LGNTLLHLLVMENefkaeyeelscQMYNFALSLLDKLRdskelEVILNHQGLTPLKLAAKEGRIVLFRLKLA 278
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
14-196 1.42e-44

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 160.89  E-value: 1.42e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507653  14 LLVAAYKGQTENVVQLINKGARV-AVTKHGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIA 92
Cdd:COG0666    58 LLAAALAGDLLVALLLLAAGADInAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVK 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507653  93 ALIHEGCALDRQDKAGNTALHLACQNSHSQSTRVLLLAGSRADLKNNAGDTALHVAAALNHKKVAKILLEAGADTTIVNN 172
Cdd:COG0666   138 LLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN 217

                         170       180
                  ....*....|....*....|....
gi 1370507653 173 AGQTPLETARYHNNPEVALLLTKA 196
Cdd:COG0666   218 DGKTALDLAAENGNLEIVKLLLEA 241
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
14-196 1.63e-43

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 158.19  E-value: 1.63e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507653  14 LLVAAYKGQTENVVQLINKGARV-AVTKHGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIA 92
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGADVnARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507653  93 ALIHEGCALDRQDKAGNTALHLACQNSHSQSTRVLLLAGSRADLKNNAGDTALHVAAALNHKKVAKILLEAGADTTIVNN 172
Cdd:COG0666   171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250

                         170       180
                  ....*....|....*....|....
gi 1370507653 173 AGQTPLETARYHNNPEVALLLTKA 196
Cdd:COG0666   251 DGLTALLLAAAAGAALIVKLLLLA 274
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
14-178 1.17e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 136.24  E-value: 1.17e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507653  14 LLVAAYKGQTENVVQLINKGARV-AVTKHGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIA 92
Cdd:COG0666   124 LHLAAYNGNLEIVKLLLEAGADVnAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVK 203

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507653  93 ALIHEGCALDRQDKAGNTALHLACQNSHSQSTRVLLLAGSRADLKNNAGDTALHVAAALNHKKVAKILLEAGADTTIVNN 172
Cdd:COG0666   204 LLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283


                  ....*.
gi 1370507653 173 AGQTPL 178
Cdd:COG0666   284 DLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-196 1.38e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 135.85  E-value: 1.38e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507653   1 MSQQDAVAALSERLLVAAYKGQTENVVQLINKGARVAVTKHGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALH 80
Cdd:COG0666    13 AALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLH 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507653  81 RATVVGNTEIIAALIHEGCALDRQDKAGNTALHLACQNSHSQSTRVLLLAGSRADLKNNAGDTALHVAAALNHKKVAKIL 160
Cdd:COG0666    93 AAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLL 172

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1370507653 161 LEAGADTTIVNNAGQTPLETARYHNNPEVALLLTKA 196
Cdd:COG0666   173 LEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA 208
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
24-193 3.60e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 103.11  E-value: 3.60e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507653  24 ENVVQLINKGARVAVTKHGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIAALIHEGCALDR 103
Cdd:COG0666     3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507653 104 QDKAGNTALHLACQNSHSQSTRVLLLAGSRADLKNNAGDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQTPLETARY 183
Cdd:COG0666    83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162

                         170
                  ....*....|
gi 1370507653 184 HNNPEVALLL 193
Cdd:COG0666   163 NGNLEIVKLL 172
PHA03095 PHA03095
ankyrin-like protein; Provisional
 29-199 2.71e-21

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 97.40  E-value: 2.71e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507653  29 LINKGARV-AVTKHGRTPLH-LAANKG-HLPVVQILLKAGCDLDVQDDGDQTALH------RAtvvgNTEIIAALIHEGC 99
Cdd:PHA03095  138 LLRKGADVnALDLYGMTPLAvLLKSRNaNVELLRLLIDAGADVYAVDDRFRSLLHhhlqsfKP----RARIVRELIRAGC 213

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507653 100 ALDRQDKAGNTALHLACQNSHSQSTRV--LLLAGSRADLKNNAGDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQTP 177
Cdd:PHA03095  214 DPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTP 293

                         170       180
                  ....*....|....*....|...
gi 1370507653 178 LETARYHNNPE-VALLLTKAPQV 199
Cdd:PHA03095  294 LSLMVRNNNGRaVRAALAKNPSA 316
Ank_2 pfam12796
Ankyrin repeats (3 copies);
79-171 1.73e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 86.32  E-value: 1.73e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507653  79 LHRATVVGNTEIIAALIHEGCALDRQDKAGNTALHLACQNSHSQSTRvLLLAGSRADLKNNaGDTALHVAAALNHKKVAK 158
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVK-LLLEHADVNLKDN-GRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1370507653 159 ILLEAGADTTIVN 171
Cdd:pfam12796  79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
46-138 2.71e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.94  E-value: 2.71e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507653  46 LHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIAALIhEGCALDRQDKaGNTALHLACQNSHSQSTR 125
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKDN-GRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1370507653 126 VLLLAGSRADLKN 138
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 19-196 2.91e-20

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 94.32  E-value: 2.91e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507653  19 YKGQTENVVQ-LINKGARV-AVTKHGRTPLHL-AANKG-HLPVVQILLKAGCDLDVQDDGDQTALH------RATVvgnt 88
Cdd:PHA03095   92 YNATTLDVIKlLIKAGADVnAKDKVGRTPLHVyLSGFNiNPKVIRLLLRKGADVNALDLYGMTPLAvllksrNANV---- 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507653  89 EIIAALIHEGCALDRQDKAGNTALHLACQNSHSQST--RVLLLAGSRADLKNNAGDTALHVAAALNHKKVAKI--LLEAG 164
Cdd:PHA03095  168 ELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRARivRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAG 247

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1370507653 165 ADTTIVNNAGQTPLETARYHNNPEVALLLTKA 196
Cdd:PHA03095  248 ISINARNRYGQTPLHYAAVFNNPRACRRLIAL 279
Ank_2 pfam12796
Ankyrin repeats (3 copies);
14-105 1.91e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.55  E-value: 1.91e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507653  14 LLVAAYKGQTENVVQLINKGARV-AVTKHGRTPLHLAANKGHLPVVQILLKaGCDLDVQDDGdQTALHRATVVGNTEIIA 92
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADAnLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDNG-RTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1370507653  93 ALIHEGCALDRQD 105
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 26-199 7.80e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 83.18  E-value: 7.80e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507653  26 VVQLINKGARVAV-TKHGRTPLHLAANKGH-----LPVVQILLKAGCDLDVQDDGDQTALHRA--TVVGNTEIIAALIHE 97
Cdd:PHA03100   51 VKILLDNGADINSsTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVNAPDNNGITPLLYAisKKSNSYSIVEYLLDN 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507653  98 GCALDRQDKAGNTALHLACQNSHS----------------QSTRV--LLLAGSRADLKNNAGDTALHVAAALNHKKVAKI 159
Cdd:PHA03100  131 GANVNIKNSDGENLLHLYLESNKIdlkilkllidkgvdinAKNRVnyLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKY 210

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1370507653 160 LLEAGADTTIVNNAGQTPLETARYHNNPE-VALLLTKAPQV 199
Cdd:PHA03100  211 LLDLGANPNLVNKYGDTPLHIAILNNNKEiFKLLLNNGPSI 251
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 42-171 1.10e-15

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 81.07  E-value: 1.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507653  42 GRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIAALIHEGCALDRQdkAGNTALHLACQNSHS 121
Cdd:PLN03192  558 GRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPH--AAGDLLCTAAKRNDL 635

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1370507653 122 QSTRVLLLAGSRADLKNNAGDTALHVAAALNHKKVAKILLEAGADTTIVN 171
Cdd:PLN03192  636 TAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAN 685
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
55-196 2.22e-15

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 77.30  E-value: 2.22e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507653  55 LPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIAALIHEGCALDRQDKAGNTALHLACQNSHSQSTRVLLLAGSRA 134
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370507653 135 DLKNNAGDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQTPLETARYHNNPEVALLLTKA 196
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA 142
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 22-181 8.61e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 77.23  E-value: 8.61e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507653  22 QTENVVQLINKGARV-AVTKH-GRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIAALIHEGC 99
Cdd:PHA02878  146 EAEITKLLLSYGADInMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA 225

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507653 100 ALDRQDKAGNTALHLACQNSHSQST-RVLLLAGSRADLKNNA-GDTALHVaaALNHKKVAKILLEAGADTTIVNNAGQTP 177
Cdd:PHA02878  226 STDARDKCGNTPLHISVGYCKDYDIlKLLLEHGVDVNAKSYIlGLTALHS--SIKSERKLKLLLEYGADINSLNSYKLTP 303


                  ....
gi 1370507653 178 LETA 181
Cdd:PHA02878  304 LSSA 307
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 15-185 2.77e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 76.26  E-value: 2.77e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507653  15 LVAAYKGQTENVVQLINKGARV-AVTKHGRTPLHLAAN-KGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIA 92
Cdd:PHA02876  313 LMAKNGYDTENIRTLIMLGADVnAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIIN 392

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507653  93 ALIHEGCALDRQDKAGNTALHLA-CQNSHSQSTRVLLLAGSRADLKNNAGDTALHVAAALNHK-KVAKILLEAGADTTIV 170
Cdd:PHA02876  393 TLLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNCKlDVIEMLLDNGADVNAI 472

                         170
                  ....*....|....*.
gi 1370507653 171 NNAGQTPLETA-RYHN 185
Cdd:PHA02876  473 NIQNQYPLLIAlEYHG 488
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 57-196 4.79e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 74.61  E-value: 4.79e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507653  57 VVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIAALIHEGCALDRQDKAGNTALHLACQNSHSQSTRVLLLAGSRADL 136
Cdd:PHA02874  106 MIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANV 185

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507653 137 KNNAGDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQTPLETARYHNNPEVALLLTKA 196
Cdd:PHA02874  186 KDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAIELLINNA 245
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 40-195 6.40e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 74.32  E-value: 6.40e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507653  40 KHGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVG-----NTEIIAALIHEGCALDRQDKAGNTALHL 114
Cdd:PHA03100   33 KKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKynltdVKEIVKLLLEYGANVNAPDNNGITPLLY 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507653 115 ACQNSHSQSTRV--LLLAGSRADLKNNAGDTALHVAAALNH--KKVAKILLEAGAD----------------TTIVNNAG 174
Cdd:PHA03100  113 AISKKSNSYSIVeyLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDinaknrvnyllsygvpINIKDVYG 192

                         170       180
                  ....*....|....*....|..
gi 1370507653 175 QTPLETARYHNNPE-VALLLTK 195
Cdd:PHA03100  193 FTPLHYAVYNNNPEfVKYLLDL 214
Ank_2 pfam12796
Ankyrin repeats (3 copies);
112-193 6.77e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.45  E-value: 6.77e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507653 112 LHLACQNSHSQSTRVLLLAGSRADLKNNAGDTALHVAAALNHKKVAKILLEaGADTTIVNNaGQTPLETARYHNNPEVAL 191
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIVK 78


                  ..
gi 1370507653 192 LL 193
Cdd:pfam12796  79 LL 80
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 17-217 7.40e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 73.87  E-value: 7.40e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507653  17 AAYKGQTENVVQLI--NKGARVAVTKHGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIAAL 94
Cdd:PHA02875   75 AVEEGDVKAVEELLdlGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELL 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507653  95 IHEGCALDRQDKAGNTALHLACQNSHSQSTRVLLLAGSRADLKNNAGDTALHVAAALNHK-KVAKILLEAGADTTI---V 170
Cdd:PHA02875  155 IDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKiDIVRLFIKRGADCNImfmI 234

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507653 171 NNAGQTPLETAR-YHNNPEV-ALLLTKAPQVLR-----------FSRGRSLRKKRERLKE 217
Cdd:PHA02875  235 EGEECTILDMICnMCTNLESeAIDALIADIAIRihkktirrdegFKNNMSTIEDKEEFKD 294
PHA03095 PHA03095
ankyrin-like protein; Provisional
 24-178 1.13e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 70.44  E-value: 1.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507653  24 ENVVQLINKGARVAVTK-HGRTPLHLAANKGHLP---VVQILLKAGCDLDVQDDGDQTALHRATVVGNTE-IIAALIHEG 98
Cdd:PHA03095   28 EEVRRLLAAGADVNFRGeYGKTPLHLYLHYSSEKvkdIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAG 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507653  99 CALDRQDKAGNTALHlACqnshsqstrvllLAGSRAdlknnagdtalhvaaalnHKKVAKILLEAGADTTIVNNAGQTPL 178
Cdd:PHA03095  108 ADVNAKDKVGRTPLH-VY------------LSGFNI------------------NPKVIRLLLRKGADVNALDLYGMTPL 156
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 22-235 1.13e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 70.38  E-value: 1.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507653  22 QTENVVQLINKGARVAV-TKHGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIAALIHEGCA 100
Cdd:PHA02874  103 EKDMIKTILDCGIDVNIkDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAY 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507653 101 LDRQDKAGNTALHLACQNSHSQSTRVLLLAGSRADLKNNAGDTALHVAAALNHKKVAKILLEAGADTTIVNnaGQTPLET 180
Cdd:PHA02874  183 ANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAIELLINNASINDQDID--GSTPLHH 260

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370507653 181 A-RYHNNPEV--ALLLTKAPQVLRFSRGRSLRK------KRERLKEERRAQSVPRDEVAQSKGS 235
Cdd:PHA02874  261 AiNPPCDIDIidILLYHKADISIKDNKGENPIDtafkyiNKDPVIKDIIANAVLIKEADKLKDS 324
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 29-172 3.57e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 68.92  E-value: 3.57e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507653  29 LINKGARV-AVTKHGRTPLHLAANK--GHLPVVQILLKAGCDLDVQDDGDQTALHRATVVG--NTEIIAALIHEG----- 98
Cdd:PHA03100   92 LLEYGANVnAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNkiDLKILKLLIDKGvdina 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507653  99 -----------CALDRQDKAGNTALHLACQNSHSQSTRVLLLAGSRADLKNNAGDTALHVAAALNHKKVAKILLEAGADT 167
Cdd:PHA03100  172 knrvnyllsygVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSI 251


                  ....*
gi 1370507653 168 TIVNN 172
Cdd:PHA03100  252 KTIIE 256
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 14-181 1.98e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 66.53  E-value: 1.98e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507653  14 LLVAAYKGQTENVVQLINKGARVAVTK-HGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIA 92
Cdd:PHA02874  128 LHYAIKKGDLESIKMLFEYGADVNIEDdNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIK 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507653  93 ALIHEGCALDRQDKAGNTALHLACqnSHSQSTRVLLLAGSRADLKNNAGDTALHvaAALNH---KKVAKILLEAGADTTI 169
Cdd:PHA02874  208 LLIDHGNHIMNKCKNGFTPLHNAI--IHNRSAIELLINNASINDQDIDGSTPLH--HAINPpcdIDIIDILLYHKADISI 283

                         170
                  ....*....|..
gi 1370507653 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 1370507653  42 GRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIAALI 95
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 10-194 3.67e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 62.67  E-value: 3.67e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507653  10 LSERLLVAAYKGQTENVVQLI-NKGARVAVT-KHGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGN 87
Cdd:PHA02874    1 ASQDLRMCIYSGDIEAIEKIIkNKGNCINISvDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507653  88 TEIIAALIHEG---------------------CALD--RQDKAGNTALHLACQNSHSQSTRVLLLAGSRADLKNNAGDTA 144
Cdd:PHA02874   81 HDIIKLLIDNGvdtsilpipciekdmiktildCGIDvnIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYP 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1370507653 145 LHVAAALNHKKVAKILLEAGADTTIVNNAGQTPLE-TARYHNNPEVALLLT 194
Cdd:PHA02874  161 IHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHnAAEYGDYACIKLLID 211
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 42-204 6.11e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 61.55  E-value: 6.11e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507653  42 GRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIAALIHEGC-ALDRQDKAGNTALHLACQNSH 120
Cdd:PHA02875   35 GISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKfADDVFYKDGMTPLHLATILKK 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507653 121 SQSTRVLLLAGSRADLKNNAGDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQTPLETARYHNNPEVA-LLLTKAPQV 199
Cdd:PHA02875  115 LDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICkMLLDSGANI 194


                  ....*
gi 1370507653 200 LRFSR 204
Cdd:PHA02875  195 DYFGK 199
Ank_5 pfam13857
Ankyrin repeats (many copies);
40-82 3.93e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 52.73  E-value: 3.93e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1370507653  40 KHGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRA 82
Cdd:pfam13857  14 GEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 116-198 4.24e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 59.53  E-value: 4.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507653 116 CQNSHSQST---RVLLLAGSRADLKNNAGDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQTPLETARYHNNPEVALL 192
Cdd:PTZ00322   87 CQLAASGDAvgaRILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                  ....*.
gi 1370507653 193 LTKAPQ 198
Cdd:PTZ00322  167 LSRHSQ 172
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 29-178 7.69e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 58.92  E-value: 7.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507653  29 LINKGARV-AVTKHGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIAALIHEGCALDRQDka 107
Cdd:PHA02876  164 LLEGGADVnAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKND-- 241

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370507653 108 gnTALHLACQNSHSQSTRVLLLAGSRADLKNNAGDTALHVAA-ALNHKKVAKILLEAGADTTIVNNAGQTPL 178
Cdd:PHA02876  242 --LSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASqAPSLSRLVPKLLERGADVNAKNIKGETPL 311
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 41-73 5.55e-08

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 48.82  E-value: 5.55e-08
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1370507653  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 ...
 7-150 6.19e-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: 55.79  E-value: 6.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507653   7 VAALSERLLVAayKGQTENVVQLINkgarVAVTKH---GRTPLHLAANKGHLPVVQILLKAGCDLdvqddgdQTAlhRAT 83
Cdd:cd22192    57 VAALYDNLEAA--VVLMEAAPELVN----EPMTSDlyqGETALHIAVVNQNLNLVRELIARGADV-------VSP--RAT 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507653  84 -----------------------VVGNTEIIAALIHEGCALDRQDKAGNTALH-LACQNSHSQSTRV--LLLAGSRAD-- 135
Cdd:cd22192   122 gtffrpgpknliyygehplsfaaCVGNEEIVRLLIEHGADIRAQDSLGNTVLHiLVLQPNKTFACQMydLILSYDKEDdl 201

                         170       180
                  ....*....|....*....|
gi 1370507653 136 -----LKNNAGDTALHVAAA 150
Cdd:cd22192   202 qpldlVPNNQGLTPFKLAAK 221
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 14-187 6.39e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 55.84  E-value: 6.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507653  14 LLVAAYKGQTENVVQLINKGARV-AVTKHGRTPLHLAANKGHLP-VVQILLKAGCDLDVQDDGDQTALHRATVVG-NTEI 90
Cdd:PHA02876  244 LLKAIRNEDLETSLLLYDAGFSVnSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMAKNGyDTEN 323

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507653  91 IAALIHEGCALDRQDKAGNTALHLACQNSHSQSTRVLLLA-GSRADLKNNAGDTALHVAAALNHKKVAKILLEAGADTTI 169
Cdd:PHA02876  324 IRTLIMLGADVNAADRLYITPLHQASTLDRNKDIVITLLElGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEA 403

                         170
                  ....*....|....*...
gi 1370507653 170 VNNAGQTPLETARYHNNP 187
Cdd:PHA02876  404 LSQKIGTALHFALCGTNP 421
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 1370507653 141 GDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQTPLETARYHNNPEVALLL 193
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 44-178 2.14e-07

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: 54.25  E-value: 2.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507653  44 TPLHLAANKGHLPVVQILLK-AGCDLDVQDDGDQTALHRATVVGNTEIIAALIHEGCALDRQDK-----AGNTALHLACQ 117
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEPMtsdlyQGETALHIAVV 98

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370507653 118 NSHSQSTRVLLLAGsrADLKNNA----------------GDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQTPL 178
Cdd:cd22192    99 NQNLNLVRELIARG--ADVVSPRatgtffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
Ank_5 pfam13857
Ankyrin repeats (many copies);
96-148 2.36e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 47.73  E-value: 2.36e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1370507653  96 HEGCALDRQDKAGNTALHLACQNSHSQSTRVLLLAGSRADLKNNAGDTALHVA 148
Cdd:pfam13857   4 HGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
77-128 2.73e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.65  E-value: 2.73e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1370507653  77 TALHRATVVGNTEIIAALIHEGCALDRQDKAGNTALHLACQNSHSQSTRVLL 128
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 89-180 6.61e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 52.33  E-value: 6.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507653  89 EIIAALIHEGCALDRQDKAGNTALHLACQNSHSQSTRV---LLLAGSRADLKNNAGDTALHVAAALNHK-KVAKILLEAG 164
Cdd:PHA03095   28 EEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIvrlLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKAG 107

                          90
                  ....*....|....*.
gi 1370507653 165 ADTTIVNNAGQTPLET 180
Cdd:PHA03095  108 ADVNAKDKVGRTPLHV 123
Ank_4 pfam13637
Ankyrin repeats (many copies);
108-161 1.34e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.73  E-value: 1.34e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1370507653 108 GNTALHLACQNSHSQSTRVLLLAGSRADLKNNAGDTALHVAAALNHKKVAKILL 161
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
145-207 1.62e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 46.65  E-value: 1.62e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370507653 145 LHVAAALNHKKVAKILLEAGADTTIVNNAGQTPLETARYHNNPEVALLLTKAPQVLRFSRGRS 207
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGRT 63
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 71-161 3.33e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.28  E-value: 3.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507653  71 QDDGDQTALHRATV-------VGNTEIIAALIHEGCALDRQDKAGNTALHLACQNSHSQSTRVLLLAGSRADLKNNAGDT 143
Cdd:PTZ00322   71 EEVIDPVVAHMLTVelcqlaaSGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKT 150

                          90
                  ....*....|....*...
gi 1370507653 144 ALHVAAALNHKKVAKILL 161
Cdd:PTZ00322  151 PLELAEENGFREVVQLLS 168
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 1370507653   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 1370507653  41 HGRTPLHLAANKGHLPVVQILLKAGCDLDV 70
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
127-181 6.25e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.87  E-value: 6.25e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1370507653 127 LLLAGSRA-DLKNNAGDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQTPLETA 181
Cdd:pfam13857   1 LLEHGPIDlNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 41-162 1.02e-05

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 48.92  E-value: 1.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507653  41 HGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGD--------------QTALHRATVVGNTEIIAALIHEGCALDRQDK 106
Cdd:TIGR00870 127 PGITALHLAAHRQNYEIVKLLLERGASVPARACGDffvksqgvdsfyhgESPLNAAACLGSPSIVALLSEDPADILTADS 206

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370507653 107 AGNTALHLACQNS-----------HSQSTRVLLLAGSR-----ADLKNNAGDTALHVAAALNHKKVAKILLE 162
Cdd:TIGR00870 207 LGNTLLHLLVMENefkaeyeelscQMYNFALSLLDKLRdskelEVILNHQGLTPLKLAAKEGRIVLFRLKLA 278
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 141-172 1.57e-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: 41.89  E-value: 1.57e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1370507653 141 GDTALHVAAA-LNHKKVAKILLEAGADTTIVNN 172
Cdd:pfam00023   2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 13-193 1.62e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 47.95  E-value: 1.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507653  13 RLLVAAYKGQTENVVQLINkgaRVAVTKHGRT--------PLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATV 84
Cdd:PHA02878    3 KLYKSMYTDNYETILKYIE---YIDHTENYSTsaslipfiPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507653  85 VGNTEIIAALIHE--GCALDRQDKAGNTALH------------------------LACQNSHSQS-----TRVLLLAGSR 133
Cdd:PHA02878   80 EPNKLGMKEMIRSinKCSVFYTLVAIKDAFNnrnveifkiiltnrykniqtidlvYIDKKSKDDIieaeiTKLLLSYGAD 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370507653 134 ADLKN-NAGDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQTPLETA-RYHNNPEVALLL 193
Cdd:PHA02878  160 INMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAvKHYNKPIVHILL 221
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 42-162 1.93e-05

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: 47.83  E-value: 1.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507653  42 GRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGD--------------QTALHRATVVGNTEIIaALIHEGCALD--RQD 105
Cdd:cd22194   141 GQTALNIAIERRQGDIVKLLIAKGADVNAHAKGVffnpkykhegfyfgETPLALAACTNQPEIV-QLLMEKESTDitSQD 219

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370507653 106 KAGNTALH---LACQNSHSQSTRV------LLLAGSRADL---KNNAGDTALHVAAALNHKKVAKILLE 162
Cdd:cd22194   220 SRGNTVLHalvTVAEDSKTQNDFVkrmydmILLKSENKNLetiRNNEGLTPLQLAAKMGKAEILKYILS 288
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 10-94 4.12e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.82  E-value: 4.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507653  10 LSERLLVAAYKGQTENVVQLINKGARV-AVTKHGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNT 88
Cdd:PTZ00322   82 LTVELCQLAASGDAVGARILLTGGADPnCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFR 161


                  ....*.
gi 1370507653  89 EIIAAL 94
Cdd:PTZ00322  162 EVVQLL 167
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 29-185 1.17e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 43.65  E-value: 1.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507653  29 LINKGARV-AVTKH-GRTPLH--LAANKGHLP-VVQILLKAGCDLDVQDDGDQTALHR--ATVVGNTEIIAALIHEGCAL 101
Cdd:PHA02859   72 LIENGADVnFKTRDnNLSALHhyLSFNKNVEPeILKILIDSGSSITEEDEDGKNLLHMymCNFNVRINVIKLLIDSGVSF 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507653 102 DRQDKAGNTALHlacqnshsqsTRVLLlagsRADlknnagdtalhvaaalnhKKVAKILLEAGADTTIVNNAGQTPLETA 181
Cdd:PHA02859  152 LNKDFDNNNILY----------SYILF----HSD------------------KKIFDFLTSLGIDINETNKSGYNCYDLI 199


                  ....
gi 1370507653 182 RYHN 185
Cdd:PHA02859  200 KFRN 203
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 57-178 1.61e-04

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 44.90  E-value: 1.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507653  57 VVQILLKAGCDLDVQDDGDQTALHRATVVGN--TEIIAALIHEGCALDRQDKAGNTALHlacqnshSQSTRVLLLAGSRA 134
Cdd:PHA02716  299 VVYSFLQPGVKLHYKDSAGRTCLHQYILRHNisTDIIKLLHEYGNDLNEPDNIGNTVLH-------TYLSMLSVVNILDP 371

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1370507653 135 DLKNNAgdtalhvaaalnHKKVAKILLEAGADTTIVNNAGQTPL 178
Cdd:PHA02716  372 ETDNDI------------RLDVIQCLISLGADITAVNCLGYTPL 403
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 1370507653  141 GDTALHVAAALNHKKVAKILLEAGADTTI 169
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 42-149 5.90e-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: 42.92  E-value: 5.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507653  42 GRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGD-------------QTALHRATVVGNTEIIAALI---HEGCALDRQD 105
Cdd:cd22197    94 GHSALHIAIEKRSLQCVKLLVENGADVHARACGRffqkkqgtcfyfgELPLSLAACTKQWDVVNYLLenpHQPASLQAQD 173

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507653 106 KAGNTALH---LACQNSHSQSTRV------LLLAGSRAD-------LKNNAGDTALHVAA 149
Cdd:cd22197   174 SLGNTVLHalvMIADNSPENSALVikmydgLLQAGARLCptvqleeISNHEGLTPLKLAA 233
PHA02798 PHA02798
ankyrin-like protein; Provisional
 47-172 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 1370507653  47 HLAANKGHLPVVQILLKAGCDLDVQDDGDQTALhrATVVGN-------TEIIAALIHEGCALDRQDKAGNTALHLACQNS 119
Cdd:PHA02798   43 YLQRDSPSTDIVKLFINLGANVNGLDNEYSTPL--CTILSNikdykhmLDIVKILIENGADINKKNSDGETPLYCLLSNG 120

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1370507653 120 HSQSTRVLLLA---GSRADLKNNAGDTALHVAAALNHK---KVAKILLEAGADTTIVNN 172
Cdd:PHA02798  121 YINNLEILLFMienGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEKGVDINTHNN 179
PHA02791 PHA02791
ankyrin-like protein; Provisional
 41-161 1.11e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 41.57  E-value: 1.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507653  41 HGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDgdQTALHRATVVGNTEIIAALIHEGCALDRQDKAGNTALHLACQNSH 120
Cdd:PHA02791   29 HGHSALYYAIADNNVRLVCTLLNAGALKNLLEN--EFPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDSGN 106

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1370507653 121 SQSTRVLLLAGSRADLKNNAG-DTALHVAAALNHKKVAKILL 161
Cdd:PHA02791  107 MQTVKLFVKKNWRLMFYGKTGwKTSFYHAVMLNDVSIVSYFL 148
PHA02791 PHA02791
ankyrin-like protein; Provisional
 103-202 1.13e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 41.57  E-value: 1.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507653 103 RQDKAGNTALHLACQNSHSQSTRVLLLAGSRADLKNNagDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQTPLETAR 182
Cdd:PHA02791   25 KADVHGHSALYYAIADNNVRLVCTLLNAGALKNLLEN--EFPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAV 102

                          90       100
                  ....*....|....*....|
gi 1370507653 183 YHNNPEVALLLTKAPQVLRF 202
Cdd:PHA02791  103 DSGNMQTVKLFVKKNWRLMF 122
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 109-199 1.40e-03

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: 41.92  E-value: 1.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507653 109 NTALHLACQNSHSQSTRVLLLAgSRADL--KNNAGDTALHVAAALNHKKVAKILLEagADTTIVNNA-------GQTPLE 179
Cdd:cd22192    18 ESPLLLAAKENDVQAIKKLLKC-PSCDLfqRGALGETALHVAALYDNLEAAVVLME--AAPELVNEPmtsdlyqGETALH 94

                          90       100
                  ....*....|....*....|.
gi 1370507653 180 TARYHNNPE-VALLLTKAPQV 199
Cdd:cd22192    95 IAVVNQNLNlVRELIARGADV 115
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 47-128 1.57e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.81  E-value: 1.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507653  47 HLAANkGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIAALIHEGCALDRQDKAGNTALHLACQNSHSQSTRV 126
Cdd:PTZ00322   88 QLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                  ..
gi 1370507653 127 LL 128
Cdd:PTZ00322  167 LS 168
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 22-162 2.60e-03

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


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 40.93  E-value: 2.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507653  22 QTENVVQLINKGARVAVTKhGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGD--------------QTALHRATVVGN 87
Cdd:cd22193    57 KTDNLKRFINAEYTDEYYE-GQTALHIAIERRQGDIVALLVENGADVHAHAKGRffqpkyqgegfyfgELPLSLAACTNQ 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507653  88 TEIIAALI---HEGCALDRQDKAGNTALH---LACQNSHSQSTRV------LLLAGSR-------ADLKNNAGDTALHVA 148
Cdd:cd22193   136 PDIVQYLLeneHQPADIEAQDSRGNTVLHalvTVADNTKENTKFVtrmydmILIRGAKlcptvelEEIRNNDGLTPLQLA 215

                         170
                  ....*....|....
gi 1370507653 149 AALNHKKVAKILLE 162
Cdd:cd22193   216 AKMGKIEILKYILQ 229
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 1370507653 141 GDTALHVAAALNHKKVAKILLEAGAD 166
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGAD 27
PHA03095 PHA03095
ankyrin-like protein; Provisional
 125-196 8.05e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 39.24  E-value: 8.05e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370507653 125 RVLLLAGSRADLKNNAGDTALHVAAALNHKKVAKI---LLEAGADTTIVNNAGQTPLETARYHNN-PEVALLLTKA 196
Cdd:PHA03095   31 RRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIvrlLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKA 106
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 4-149 8.47e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. 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. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 39.09  E-value: 8.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507653   4 QDAVAALSERLLVAAYKgqTENVVQLINKGARVAVTKhGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGD-------- 75
Cdd:cd21882    38 NDGVNEAIMLLLEAAPD--SGNPKELVNAPCTDEFYQ-GQTALHIAIENRNLNLVRLLVENGADVSARATGRffrkspgn 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507653  76 -----QTALHRATVVGNTEIIAALI---HEGCALDRQDKAGNTALH---LACQNSHSQSTRV------LLLAGSRAD--- 135
Cdd:cd21882   115 lfyfgELPLSLAACTNQEEIVRLLLengAQPAALEAQDSLGNTVLHalvLQADNTPENSAFVcqmynlLLSYGAHLDptq 194

                         170
                  ....*....|....*...
gi 1370507653 136 ----LKNNAGDTALHVAA 149
Cdd:cd21882   195 qleeIPNHQGLTPLKLAA 212
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 137-197 8.84e-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: 39.36  E-value: 8.84e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370507653 137 KNNAGDTALHVAAALNHKKVAKILLEAGADTTI---------VNNA-----GQTPLETARYHNNPE-VALLLTKAP 197
Cdd:cd22194   137 EAYEGQTALNIAIERRQGDIVKLLIAKGADVNAhakgvffnpKYKHegfyfGETPLALAACTNQPEiVQLLMEKES 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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