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Conserved domains on  [gi|2217360331|ref|XP_047274360|]
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ankyrin repeat domain-containing protein 6 isoform X20 [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];
14-208 2.31e-43

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 157.81  E-value: 2.31e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360331  14 LLVAAYKGQTENVVQLINKGARV-AVTKHGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIA 92
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGADVnARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360331  93 ALIHEGCALDRQDKAGNTALHLACQNSHSQSTRVLLLAGSRADLKNNAGDTCLHVAARYNHLSIIRLLLTAFCSVHEKNQ 172
Cdd:COG0666   171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2217360331 173 AGDTALHVAAALNHKKVAKILLEAGADTTIVNNVLR 208
Cdd:COG0666   251 DGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLL 286
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
14-208 2.31e-43

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 157.81  E-value: 2.31e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360331  14 LLVAAYKGQTENVVQLINKGARV-AVTKHGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIA 92
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGADVnARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360331  93 ALIHEGCALDRQDKAGNTALHLACQNSHSQSTRVLLLAGSRADLKNNAGDTCLHVAARYNHLSIIRLLLTAFCSVHEKNQ 172
Cdd:COG0666   171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2217360331 173 AGDTALHVAAALNHKKVAKILLEAGADTTIVNNVLR 208
Cdd:COG0666   251 DGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLL 286
PHA03095 PHA03095
ankyrin-like protein; Provisional
 19-205 1.63e-20

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 95.09  E-value: 1.63e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360331  19 YKGQTENVVQ-LINKGARV-AVTKHGRTPLHL-AANKG-HLPVVQILLKAGCDLDVQDDGDQTALH------RATVvgnt 88
Cdd:PHA03095   92 YNATTLDVIKlLIKAGADVnAKDKVGRTPLHVyLSGFNiNPKVIRLLLRKGADVNALDLYGMTPLAvllksrNANV---- 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360331  89 EIIAALIHEGCALDRQDKAGNTALHLACQNSHSQST--RVLLLAGSRADLKNNAGDTCLHVAARYNHL--SIIRLLLTAF 164
Cdd:PHA03095  168 ELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRARivRELIRAGCDPAATDMLGNTPLHSMATGSSCkrSLVLPLLIAG 247

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2217360331 165 CSVHEKNQAGDTALHVAAALNHKKVAKILLEAGADTTIVNN 205
Cdd:PHA03095  248 ISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSS 288
Ank_2 pfam12796
Ankyrin repeats (3 copies);
112-204 1.65e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 86.32  E-value: 1.65e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360331 112 LHLACQNSHSQSTRVLLLAGSRADLKNNAGDTCLHVAARYNHLSIIRLLLtAFCSVHEKNQaGDTALHVAAALNHKKVAK 191
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKDN-GRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 2217360331 192 ILLEAGADTTIVN 204
Cdd:pfam12796  79 LLLEKGADINVKD 91
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 7-154 2.82e-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: 53.86  E-value: 2.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360331   7 VAALSERLLVAayKGQTENVVQLINkgarVAVTKH---GRTPLHLAANKGHLPVVQILLKAGCDLdvqddgdQTAlhRAT 83
Cdd:cd22192    57 VAALYDNLEAA--VVLMEAAPELVN----EPMTSDlyqGETALHIAVVNQNLNLVRELIARGADV-------VSP--RAT 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360331  84 -----------------------VVGNTEIIAALIHEGCALDRQDKAGNTALH-LACQNSHSQSTRV--LLLAGSRAD-- 135
Cdd:cd22192   122 gtffrpgpknliyygehplsfaaCVGNEEIVRLLIEHGADIRAQDSLGNTVLHiLVLQPNKTFACQMydLILSYDKEDdl 201

                         170       180       190
                  ....*....|....*....|....*....|
gi 2217360331 136 -----LKNNAGDTCLHVAAR------YNHL 154
Cdd:cd22192   202 qpldlVPNNQGLTPFKLAAKegnivmFQHL 231
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 41-70 3.87e-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: 3.87e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 2217360331   41 HGRTPLHLAANKGHLPVVQILLKAGCDLDV 70
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 41-161 4.95e-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: 46.61  E-value: 4.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360331  41 HGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGD--------------QTALHRATVVGNTEIIAALIHEGCALDRQDK 106
Cdd:TIGR00870 127 PGITALHLAAHRQNYEIVKLLLERGASVPARACGDffvksqgvdsfyhgESPLNAAACLGSPSIVALLSEDPADILTADS 206

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217360331 107 AGNTALHLACQNS-----------HSQSTRVLLLAGSR-----ADLKNNAGDTCLHVAARYNHLSIIRLLL 161
Cdd:TIGR00870 207 LGNTLLHLLVMENefkaeyeelscQMYNFALSLLDKLRdskelEVILNHQGLTPLKLAAKEGRIVLFRLKL 277
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
14-208 2.31e-43

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 157.81  E-value: 2.31e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360331  14 LLVAAYKGQTENVVQLINKGARV-AVTKHGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIA 92
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGADVnARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360331  93 ALIHEGCALDRQDKAGNTALHLACQNSHSQSTRVLLLAGSRADLKNNAGDTCLHVAARYNHLSIIRLLLTAFCSVHEKNQ 172
Cdd:COG0666   171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2217360331 173 AGDTALHVAAALNHKKVAKILLEAGADTTIVNNVLR 208
Cdd:COG0666   251 DGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLL 286
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
14-205 3.12e-43

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 157.42  E-value: 3.12e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360331  14 LLVAAYKGQTENVVQLINKGARV-AVTKHGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIA 92
Cdd:COG0666    58 LLAAALAGDLLVALLLLAAGADInAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVK 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360331  93 ALIHEGCALDRQDKAGNTALHLACQNSHSQSTRVLLLAGSRADLKNNAGDTCLHVAARYNHLSIIRLLLTAFCSVHEKNQ 172
Cdd:COG0666   138 LLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN 217

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2217360331 173 AGDTALHVAAALNHKKVAKILLEAGADTTIVNN 205
Cdd:COG0666   218 DGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-205 1.51e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 144.33  E-value: 1.51e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360331   1 MSQQDAVAALSERLLVAAYKGQTENVVQLINKGARVAVTKHGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALH 80
Cdd:COG0666    13 AALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLH 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360331  81 RATVVGNTEIIAALIHEGCALDRQDKAGNTALHLACQNSHSQSTRVLLLAGSRADLKNNAGDTCLHVAARYNHLSIIRLL 160
Cdd:COG0666    93 AAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLL 172

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2217360331 161 LTAFCSVHEKNQAGDTALHVAAALNHKKVAKILLEAGADTTIVNN 205
Cdd:COG0666   173 LEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN 217
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
14-178 1.41e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 130.46  E-value: 1.41e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360331  14 LLVAAYKGQTENVVQLINKGARV-AVTKHGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIA 92
Cdd:COG0666   124 LHLAAYNGNLEIVKLLLEAGADVnAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVK 203

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360331  93 ALIHEGCALDRQDKAGNTALHLACQNSHSQSTRVLLLAGSRADLKNNAGDTCLHVAARYNHLSIIRLLLTAFCSVHEKNQ 172
Cdd:COG0666   204 LLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283


                  ....*.
gi 2217360331 173 AGDTAL 178
Cdd:COG0666   284 DLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
24-205 1.11e-27

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 113.51  E-value: 1.11e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360331  24 ENVVQLINKGARVAVTKHGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIAALIHEGCALDR 103
Cdd:COG0666     3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360331 104 QDKAGNTALHLACQNSHSQSTRVLLLAGSRADLKNNAGDTCLHVAARYNHLSIIRLLLTAFCSVHEKNQAGDTALHVAAA 183
Cdd:COG0666    83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162

                         170       180
                  ....*....|....*....|..
gi 2217360331 184 LNHKKVAKILLEAGADTTIVNN 205
Cdd:COG0666   163 NGNLEIVKLLLEAGADVNARDN 184
PHA03095 PHA03095
ankyrin-like protein; Provisional
 19-205 1.63e-20

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 95.09  E-value: 1.63e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360331  19 YKGQTENVVQ-LINKGARV-AVTKHGRTPLHL-AANKG-HLPVVQILLKAGCDLDVQDDGDQTALH------RATVvgnt 88
Cdd:PHA03095   92 YNATTLDVIKlLIKAGADVnAKDKVGRTPLHVyLSGFNiNPKVIRLLLRKGADVNALDLYGMTPLAvllksrNANV---- 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360331  89 EIIAALIHEGCALDRQDKAGNTALHLACQNSHSQST--RVLLLAGSRADLKNNAGDTCLHVAARYNHL--SIIRLLLTAF 164
Cdd:PHA03095  168 ELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRARivRELIRAGCDPAATDMLGNTPLHSMATGSSCkrSLVLPLLIAG 247

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2217360331 165 CSVHEKNQAGDTALHVAAALNHKKVAKILLEAGADTTIVNN 205
Cdd:PHA03095  248 ISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSS 288
Ank_2 pfam12796
Ankyrin repeats (3 copies);
112-204 1.65e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 86.32  E-value: 1.65e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360331 112 LHLACQNSHSQSTRVLLLAGSRADLKNNAGDTCLHVAARYNHLSIIRLLLtAFCSVHEKNQaGDTALHVAAALNHKKVAK 191
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKDN-GRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 2217360331 192 ILLEAGADTTIVN 204
Cdd:pfam12796  79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
46-138 5.16e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.17  E-value: 5.16e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360331  46 LHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIAALIhEGCALDRQDKaGNTALHLACQNSHSQSTR 125
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKDN-GRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 2217360331 126 VLLLAGSRADLKN 138
Cdd:pfam12796  79 LLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
55-205 2.22e-18

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 86.16  E-value: 2.22e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360331  55 LPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIAALIHEGCALDRQDKAGNTALHLACQNSHSQSTRVLLLAGSRA 134
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217360331 135 DLKNNAGDTCLHVAARYNHLSIIRLLLTAFCSVHEKNQAGDTALHVAAALNHKKVAKILLEAGADTTIVNN 205
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDN 151
Ank_2 pfam12796
Ankyrin repeats (3 copies);
14-105 3.59e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.77  E-value: 3.59e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360331  14 LLVAAYKGQTENVVQLINKGARV-AVTKHGRTPLHLAANKGHLPVVQILLKaGCDLDVQDDGdQTALHRATVVGNTEIIA 92
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADAnLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDNG-RTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 2217360331  93 ALIHEGCALDRQD 105
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 26-208 2.77e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 84.72  E-value: 2.77e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360331  26 VVQLINKGARVAV-TKHGRTPLHLAANKGH-----LPVVQILLKAGCDLDVQDDGDQTALHRA--TVVGNTEIIAALIHE 97
Cdd:PHA03100   51 VKILLDNGADINSsTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVNAPDNNGITPLLYAisKKSNSYSIVEYLLDN 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360331  98 GCALDRQDKAGNTALHLACQNSHS----------------QSTRV--LLLAGSRADLKNNAGDTCLHVAARYNHLSIIRL 159
Cdd:PHA03100  131 GANVNIKNSDGENLLHLYLESNKIdlkilkllidkgvdinAKNRVnyLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKY 210

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2217360331 160 LLTAFCSVHEKNQAGDTALHVAAALNHKKVAKILLEAGADTTIVNNVLR 208
Cdd:PHA03100  211 LLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIETLL 259
PHA03095 PHA03095
ankyrin-like protein; Provisional
 24-205 2.86e-17

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 85.08  E-value: 2.86e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360331  24 ENVVQLINKGARVAVTK-HGRTPLHLAANKGHLP---VVQILLKAGCDLDVQDDGDQTALHRATVVGNTE-IIAALIHEG 98
Cdd:PHA03095   28 EEVRRLLAAGADVNFRGeYGKTPLHLYLHYSSEKvkdIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAG 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360331  99 CALDRQDKAGNTALH--LACQNSHSQSTRVLLLAGsrADL--KNNAGDTCLHVAARYNH--LSIIRLLLTAFCSVHEKNQ 172
Cdd:PHA03095  108 ADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKG--ADVnaLDLYGMTPLAVLLKSRNanVELLRLLIDAGADVYAVDD 185

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2217360331 173 AGDTALHVaAALNHKKVAKI---LLEAGADTTIVNN 205
Cdd:PHA03095  186 RFRSLLHH-HLQSFKPRARIvreLIRAGCDPAATDM 220
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 49-323 3.98e-17

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 85.69  E-value: 3.98e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360331  49 AANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIAALIHEGCALDRQDKAGNTALHLACQNSHSQSTRVLL 128
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILY 611

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360331 129 LAGSRADlKNNAGDTcLHVAARYNHLSIIRLLLTAFCSVHEKNQAGDTALHVAAALNHKKVAKILLEAGADTTIVNNVLR 208
Cdd:PLN03192  612 HFASISD-PHAAGDL-LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDDD 689

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360331 209 FSRgrslRKKRERLKEERRAQSVprdevaqskgsVSAGDTPSSEQAVARKEEAREEFLSASPEprakddrRRKSRPKVSA 288
Cdd:PLN03192  690 FSP----TELRELLQKRELGHSI-----------TIVDSVPADEPDLGRDGGSRPGRLQGTSS-------DNQCRPRVSI 747

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 2217360331 289 FSdptppadqqpghqknlhahNHPKKRNRHRCSSP 323
Cdd:PLN03192  748 YK-------------------GHPLLRNERCCNEA 763
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 40-205 4.63e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 83.95  E-value: 4.63e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360331  40 KHGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVG-----NTEIIAALIHEGCALDRQDKAGNTALHL 114
Cdd:PHA03100   33 KKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKynltdVKEIVKLLLEYGANVNAPDNNGITPLLY 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360331 115 ACQNSHSQSTRV--LLLAGSRADLKNNAGDTCLHVAARYNH--LSIIRLL----------------LTAFCSVHEKNQAG 174
Cdd:PHA03100  113 AISKKSNSYSIVeyLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLidkgvdinaknrvnylLSYGVPINIKDVYG 192

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2217360331 175 DTALHVAAALNHKKVAKILLEAGADTTIVNN 205
Cdd:PHA03100  193 FTPLHYAVYNNNPEFVKYLLDLGANPNLVNK 223
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 22-205 5.47e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 77.70  E-value: 5.47e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360331  22 QTENVVQLINKGARVAV-TKHGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIAALIHEGCA 100
Cdd:PHA02874  103 EKDMIKTILDCGIDVNIkDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAY 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360331 101 LDRQDKAGNTALHLACQNSHSQSTRVLLLAGSRADLKNNAGDTCLHVAARYNHlSIIRLLLTAfCSVHEKNQAGDTALHv 180
Cdd:PHA02874  183 ANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLINN-ASINDQDIDGSTPLH- 259

                         170       180
                  ....*....|....*....|....*...
gi 2217360331 181 aAALNH---KKVAKILLEAGADTTIVNN 205
Cdd:PHA02874  260 -HAINPpcdIDIIDILLYHKADISIKDN 286
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 57-204 5.90e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 78.00  E-value: 5.90e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360331  57 VVQILLKAGCDLDVQD-DGDQTALHRATVVGNTEIIAALIHEGCALDRQDKAGNTALHLACQNSHSQSTRVLLLAGSRAD 135
Cdd:PHA02878  149 ITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTD 228

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217360331 136 LKNNAGDTCLHVAARY-NHLSIIRLLLTAFCSVHEKNQA-GDTALHVAaaLNHKKVAKILLEAGADTTIVN 204
Cdd:PHA02878  229 ARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYIlGLTALHSS--IKSERKLKLLLEYGADINSLN 297
PHA03095 PHA03095
ankyrin-like protein; Provisional
 29-210 8.56e-15

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 77.37  E-value: 8.56e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360331  29 LINKGARV-AVTKHGRTPLH-LAANKG-HLPVVQILLKAGCDLDVQDDGDQTALH------RAtvvgNTEIIAALIHEGC 99
Cdd:PHA03095  138 LLRKGADVnALDLYGMTPLAvLLKSRNaNVELLRLLIDAGADVYAVDDRFRSLLHhhlqsfKP----RARIVRELIRAGC 213

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360331 100 ALDRQDKAGNTALHLACQNSHSQSTRV--LLLAGSRADLKNNAGDTCLHVAARYNHLSIIRLLLTAFCSVHEKNQAGDTA 177
Cdd:PHA03095  214 DPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTP 293

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2217360331 178 LHVAAALNHKKVAKILLEAGADT-TIVNNVLRFS 210
Cdd:PHA03095  294 LSLMVRNNNGRAVRAALAKNPSAeTVAATLNTAS 327
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 15-199 5.06e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 68.94  E-value: 5.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360331  15 LVAAYKGQTENVVQLINKGARV-AVTKHGRTPLHLAAN-KGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIA 92
Cdd:PHA02876  313 LMAKNGYDTENIRTLIMLGADVnAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIIN 392

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360331  93 ALIHEGCALDRQDKAGNTALHLA-CQNSHSQSTRVLLLAGSRADLKNNAGDTCLHVAARYN-HLSIIRLLLTAFCSVHEK 170
Cdd:PHA02876  393 TLLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAI 472

                         170       180
                  ....*....|....*....|....*....
gi 2217360331 171 NQAGDTALHVaaALNHKKVAKILLEAGAD 199
Cdd:PHA02876  473 NIQNQYPLLI--ALEYHGIVNILLHYGAE 499
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 43-207 3.47e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 65.78  E-value: 3.47e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360331  43 RTPLHLAANKGHLPVVQILLKAGCDLD--VQDDGDqTALHRATVVGNTEIIAALIHEGCALDRQDKAGNTALHLACQNSH 120
Cdd:PHA02875   69 ESELHDAVEEGDVKAVEELLDLGKFADdvFYKDGM-TPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGD 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360331 121 SQSTRVLLLAGSRADLKNNAGDTCLHVAARYNHLSIIRLLLTAFCSVHEKNQAGDTALHVAAALNHK-KVAKILLEAGAD 199
Cdd:PHA02875  148 IKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKiDIVRLFIKRGAD 227


                  ....*...
gi 2217360331 200 TTIVNNVL 207
Cdd:PHA02875  228 CNIMFMIE 235
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 17-162 6.06e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 65.01  E-value: 6.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360331  17 AAYKGQTENVVQLI--NKGARVAVTKHGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIAAL 94
Cdd:PHA02875   75 AVEEGDVKAVEELLdlGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELL 154

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217360331  95 IHEGCALDRQDKAGNTALHLACQNSHSQSTRVLLLAGSRADLKNNAGD-TCLHVAARYNHLSIIRLLLT 162
Cdd:PHA02875  155 IDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIK 223
Ank_4 pfam13637
Ankyrin repeats (many copies);
42-95 7.86e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 57.67  E-value: 7.86e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2217360331  42 GRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIAALI 95
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 88-223 2.16e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 63.36  E-value: 2.16e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360331  88 TEIIAALIHEGCALDRQDK-AGNTALHLACQNSHSQSTRVLLLAGSRADLKNNAGDTCLHVAARYNHLSIIRLLLTAFCS 166
Cdd:PHA02878  147 AEITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAS 226

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2217360331 167 VHEKNQAGDTALHVAAA-LNHKKVAKILLEAGADTTIVNNVLRFSRGRSLRKKRERLK 223
Cdd:PHA02878  227 TDARDKCGNTPLHISVGyCKDYDILKLLLEHGVDVNAKSYILGLTALHSSIKSERKLK 284
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 42-199 4.94e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 61.93  E-value: 4.94e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360331  42 GRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIAALIHEGC-ALDRQDKAGNTALHLACQNSH 120
Cdd:PHA02875   35 GISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKfADDVFYKDGMTPLHLATILKK 114

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217360331 121 SQSTRVLLLAGSRADLKNNAGDTCLHVAARYNHLSIIRLLLTAFCSVHEKNQAGDTALHVAAALNHKKVAKILLEAGAD 199
Cdd:PHA02875  115 LDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGAN 193
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 10-197 5.63e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 61.90  E-value: 5.63e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360331  10 LSERLLVAAYKGQTENVVQLI-NKGARVAVT-KHGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGN 87
Cdd:PHA02874    1 ASQDLRMCIYSGDIEAIEKIIkNKGNCINISvDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360331  88 TEIIAALIHEG---------------------CALD--RQDKAGNTALHLACQNSHSQSTRVLLLAGSRADLKNNAGDTC 144
Cdd:PHA02874   81 HDIIKLLIDNGvdtsilpipciekdmiktildCGIDvnIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYP 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2217360331 145 LHVAARYNHLSIIRLLLTAFCSVHEKNQAGDTALHVAAALNHKKVAKILLEAG 197
Cdd:PHA02874  161 IHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHG 213
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 26-204 5.91e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 62.39  E-value: 5.91e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360331  26 VVQLINKGARV-AVTKHGRTPLHLAANKGH-LPVVQILLKAGCDLDVQDDGDQTALHRATVVG-NTEIIAALIHEGCALD 102
Cdd:PHA02876  290 VPKLLERGADVnAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGANVN 369

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360331 103 RQDKAGNTALHLACQNSHSQSTRVLLLAGSRADLKNNAGDTCLHVA-ARYNHLSIIRLLLTAFCSVHEKNQAGDTALHVA 181
Cdd:PHA02876  370 ARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYA 449

                         170       180
                  ....*....|....*....|....
gi 2217360331 182 AALNHK-KVAKILLEAGADTTIVN 204
Cdd:PHA02876  450 CKKNCKlDVIEMLLDNGADVNAIN 473
Ank_5 pfam13857
Ankyrin repeats (many copies);
40-82 4.98e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 52.73  E-value: 4.98e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2217360331  40 KHGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRA 82
Cdd:pfam13857  14 GEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 29-199 1.08e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 58.54  E-value: 1.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360331  29 LINKGARV-AVTKHGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIAALIHE---------- 97
Cdd:PHA02876  164 LLEGGADVnAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNrsninkndls 243

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360331  98 -------------------GCALDRQDKAGNTALHLACQN-SHSQSTRVLLLAGSRADLKNNAGDTCLHVAARYNH-LSI 156
Cdd:PHA02876  244 llkairnedletslllydaGFSVNSIDDCKNTPLHHASQApSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTEN 323

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2217360331 157 IRLLLTAFCSVHEKNQAGDTALHVAAALN-HKKVAKILLEAGAD 199
Cdd:PHA02876  324 IRTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGAN 367
Ank_4 pfam13637
Ankyrin repeats (many copies);
141-194 2.96e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.35  E-value: 2.96e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2217360331 141 GDTCLHVAARYNHLSIIRLLLTAFCSVHEKNQAGDTALHVAAALNHKKVAKILL 194
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
108-161 4.38e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.97  E-value: 4.38e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2217360331 108 GNTALHLACQNSHSQSTRVLLLAGSRADLKNNAGDTCLHVAARYNHLSIIRLLL 161
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 14-206 6.29e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 55.35  E-value: 6.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360331  14 LLVAAYKGQTENVVQLINKGARVAVTK-HGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIA 92
Cdd:PHA02874  128 LHYAIKKGDLESIKMLFEYGADVNIEDdNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIK 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360331  93 ALIHEGCALDRQDKAGNTALHLACqnSHSQSTRVLLLAGSRADLKNNAGDTCLHVAARYN-HLSIIRLLLTAFCSVHEKN 171
Cdd:PHA02874  208 LLIDHGNHIMNKCKNGFTPLHNAI--IHNRSAIELLINNASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKD 285

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2217360331 172 QAGDTALHVAAA-LNHKKVAKILL-------EAG--ADTTIVNNV 206
Cdd:PHA02874  286 NKGENPIDTAFKyINKDPVIKDIIanavlikEADklKDSDFLEHI 330
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 41-73 7.67e-08

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 48.44  E-value: 7.67e-08
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2217360331  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 ...
 7-154 2.82e-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: 53.86  E-value: 2.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360331   7 VAALSERLLVAayKGQTENVVQLINkgarVAVTKH---GRTPLHLAANKGHLPVVQILLKAGCDLdvqddgdQTAlhRAT 83
Cdd:cd22192    57 VAALYDNLEAA--VVLMEAAPELVN----EPMTSDlyqGETALHIAVVNQNLNLVRELIARGADV-------VSP--RAT 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360331  84 -----------------------VVGNTEIIAALIHEGCALDRQDKAGNTALH-LACQNSHSQSTRV--LLLAGSRAD-- 135
Cdd:cd22192   122 gtffrpgpknliyygehplsfaaCVGNEEIVRLLIEHGADIRAQDSLGNTVLHiLVLQPNKTFACQMydLILSYDKEDdl 201

                         170       180       190
                  ....*....|....*....|....*....|
gi 2217360331 136 -----LKNNAGDTCLHVAAR------YNHL 154
Cdd:cd22192   202 qpldlVPNNQGLTPFKLAAKegnivmFQHL 231
Ank_4 pfam13637
Ankyrin repeats (many copies);
77-128 3.43e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.27  E-value: 3.43e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2217360331  77 TALHRATVVGNTEIIAALIHEGCALDRQDKAGNTALHLACQNSHSQSTRVLL 128
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 44-191 1.16e-06

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 51.55  E-value: 1.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360331  44 TPLHLAANKGHLPVVQILLK-AGCDLDVQDDGDQTALHRATVVGNTEIIAALIHEGCALDRQDK-----AGNTALHLACQ 117
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEPMtsdlyQGETALHIAVV 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360331 118 NSHSQSTRVLLLAGsrADLKN----------NAGDTC------LHVAARYNHLSIIRLLLTAFCSVHEKNQAGDTALHVA 181
Cdd:cd22192    99 NQNLNLVRELIARG--ADVVSpratgtffrpGPKNLIyygehpLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHIL 176

                         170
                  ....*....|
gi 2217360331 182 AALNHKKVAK 191
Cdd:cd22192   177 VLQPNKTFAC 186
Ank_5 pfam13857
Ankyrin repeats (many copies);
127-181 1.68e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.42  E-value: 1.68e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2217360331 127 LLLAGSRA-DLKNNAGDTCLHVAARYNHLSIIRLLLTAFCSVHEKNQAGDTALHVA 181
Cdd:pfam13857   1 LLEHGPIDlNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 71-169 1.88e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.05  E-value: 1.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360331  71 QDDGDQTALHRATV-------VGNTEIIAALIHEGCALDRQDKAGNTALHLACQNSHSQSTRVLLLAGSRADLKNNAGDT 143
Cdd:PTZ00322   71 EEVIDPVVAHMLTVelcqlaaSGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKT 150

                          90       100
                  ....*....|....*....|....*.
gi 2217360331 144 CLHVAARYNHLSIIRLLLTAFCSVHE 169
Cdd:PTZ00322  151 PLELAEENGFREVVQLLSRHSQCHFE 176
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 41-70 3.87e-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: 3.87e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 2217360331   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 6.26e-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: 6.26e-06
                          10        20        30
                  ....*....|....*....|....*....|
gi 2217360331  41 HGRTPLHLAANKGHLPVVQILLKAGCDLDV 70
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 42-161 6.29e-06

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: 49.37  E-value: 6.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360331  42 GRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGD--------------QTALHRATVVGNTEIIaALIHEGCALD--RQD 105
Cdd:cd22194   141 GQTALNIAIERRQGDIVKLLIAKGADVNAHAKGVffnpkykhegfyfgETPLALAACTNQPEIV-QLLMEKESTDitSQD 219

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217360331 106 KAGNTALH---LACQNSHSQSTRV------LLLAGSRADL---KNNAGDTCLHVAARYNHLSIIRLLL 161
Cdd:cd22194   220 SRGNTVLHalvTVAEDSKTQNDFVkrmydmILLKSENKNLetiRNNEGLTPLQLAAKMGKAEILKYIL 287
Ank_5 pfam13857
Ankyrin repeats (many copies);
96-148 7.40e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.49  E-value: 7.40e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2217360331  96 HEGCALDRQDKAGNTALHLACQNSHSQSTRVLLLAGSRADLKNNAGDTCLHVA 148
Cdd:pfam13857   4 HGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 13-204 1.31e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 48.34  E-value: 1.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360331  13 RLLVAAYKGQTENVVQLINkgaRVAVTKHGRT--------PLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATV 84
Cdd:PHA02878    3 KLYKSMYTDNYETILKYIE---YIDHTENYSTsaslipfiPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360331  85 VGNTEIIAALIHE--GCALDRQDKAGNTALH------------------------LACQNSHSQS-----TRVLLLAGSR 133
Cdd:PHA02878   80 EPNKLGMKEMIRSinKCSVFYTLVAIKDAFNnrnveifkiiltnrykniqtidlvYIDKKSKDDIieaeiTKLLLSYGAD 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217360331 134 ADLKN-NAGDTCLHVAARYNHLSIIRLLLTAFCSVHEKNQAGDTALHVAAALNHKKVAKILLEAGADTTIVN 204
Cdd:PHA02878  160 INMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARD 231
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 174-205 2.05e-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: 2.05e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2217360331 174 GDTALHVAAA-LNHKKVAKILLEAGADTTIVNN 205
Cdd:pfam00023   2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 142-207 3.67e-05

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 46.93  E-value: 3.67e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217360331 142 DTCLHVAARYNHL-SIIRLLLTAFCSVHEKNQAGDTALHVAAALNHKKVAKILLEagADTTIVNNVL 207
Cdd:cd22192    18 ESPLLLAAKENDVqAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPELVNEPM 82
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 10-94 4.04e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.82  E-value: 4.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360331  10 LSERLLVAAYKGQTENVVQLINKGARV-AVTKHGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNT 88
Cdd:PTZ00322   82 LTVELCQLAASGDAVGARILLTGGADPnCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFR 161


                  ....*.
gi 2217360331  89 EIIAAL 94
Cdd:PTZ00322  162 EVVQLL 167
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 41-161 4.95e-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: 46.61  E-value: 4.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360331  41 HGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGD--------------QTALHRATVVGNTEIIAALIHEGCALDRQDK 106
Cdd:TIGR00870 127 PGITALHLAAHRQNYEIVKLLLERGASVPARACGDffvksqgvdsfyhgESPLNAAACLGSPSIVALLSEDPADILTADS 206

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217360331 107 AGNTALHLACQNS-----------HSQSTRVLLLAGSR-----ADLKNNAGDTCLHVAARYNHLSIIRLLL 161
Cdd:TIGR00870 207 LGNTLLHLLVMENefkaeyeelscQMYNFALSLLDKLRdskelEVILNHQGLTPLKLAAKEGRIVLFRLKL 277
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 42-161 8.31e-05

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: 45.62  E-value: 8.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360331  42 GRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGD-------------QTALHRATVVGNTEIIAALI---HEGCALDRQD 105
Cdd:cd22197    94 GHSALHIAIEKRSLQCVKLLVENGADVHARACGRffqkkqgtcfyfgELPLSLAACTKQWDVVNYLLenpHQPASLQAQD 173

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217360331 106 KAGNTALH---LACQNSHSQSTRV------LLLAGSRAD-------LKNNAGDTCLHVAARYNHLSIIRLLL 161
Cdd:cd22197   174 SLGNTVLHalvMIADNSPENSALVikmydgLLQAGARLCptvqleeISNHEGLTPLKLAAKEGKIEIFRHIL 245
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 174-202 1.86e-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: 1.86e-04
                           10        20
                   ....*....|....*....|....*....
gi 2217360331  174 GDTALHVAAALNHKKVAKILLEAGADTTI 202
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 141-169 3.29e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 38.34  E-value: 3.29e-04
                           10        20
                   ....*....|....*....|....*....
gi 2217360331  141 GDTCLHVAARYNHLSIIRLLLTAFCSVHE 169
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 55-204 3.56e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 43.90  E-value: 3.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360331  55 LPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIAALIHEGCALDRQDKAGNTALHLACQNSHSQSTRVLLlaGSRA 134
Cdd:PHA02876  158 LLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAII--DNRS 235

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217360331 135 DLKNNagDTCLHVAARYNHLSIIRLLLTAFCSVHEKNQAGDTALHVAA-ALNHKKVAKILLEAGADTTIVN 204
Cdd:PHA02876  236 NINKN--DLSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASqAPSLSRLVPKLLERGADVNAKN 304
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 141-171 5.67e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 37.65  E-value: 5.67e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2217360331 141 GDTCLHVAA-RYNHLSIIRLLLTAFCSVHEKN 171
Cdd:pfam00023   2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PHA02791 PHA02791
ankyrin-like protein; Provisional
 26-171 7.92e-04

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 41.95  E-value: 7.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360331  26 VVQLINKGARVAVTKHgRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIAALIHEGCALDRQD 105
Cdd:PHA02791   46 VCTLLNAGALKNLLEN-EFPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDSGNMQTVKLFVKKNWRLMFYG 124

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217360331 106 KAG--NTALHLACQNSHSQSTRVLLLAGSRADLKNNAgdTCLHVAARYNHLSIIRLLLTAFCSVHEKN 171
Cdd:PHA02791  125 KTGwkTSFYHAVMLNDVSIVSYFLSEIPSTFDLAILL--SCIHITIKNGHVDMMILLLDYMTSTNTNN 190
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 22-161 8.55e-04

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: 42.48  E-value: 8.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360331  22 QTENVVQLINKGARVAVTKhGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGD--------------QTALHRATVVGN 87
Cdd:cd22193    57 KTDNLKRFINAEYTDEYYE-GQTALHIAIERRQGDIVALLVENGADVHAHAKGRffqpkyqgegfyfgELPLSLAACTNQ 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360331  88 TEIIAALI---HEGCALDRQDKAGNTALH---LACQNSHSQSTRV------LLLAGSR-------ADLKNNAGDTCLHVA 148
Cdd:cd22193   136 PDIVQYLLeneHQPADIEAQDSRGNTVLHalvTVADNTKENTKFVtrmydmILIRGAKlcptvelEEIRNNDGLTPLQLA 215

                         170
                  ....*....|...
gi 2217360331 149 ARYNHLSIIRLLL 161
Cdd:cd22193   216 AKMGKIEILKYIL 228
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 29-113 9.67e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 40.96  E-value: 9.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360331  29 LINKGARV-AVTKH-GRTPLH--LAANKGHLP-VVQILLKAGCDLDVQDDGDQTALHR--ATVVGNTEIIAALIHEGCAL 101
Cdd:PHA02859   72 LIENGADVnFKTRDnNLSALHhyLSFNKNVEPeILKILIDSGSSITEEDEDGKNLLHMymCNFNVRINVIKLLIDSGVSF 151

                          90
                  ....*....|..
gi 2217360331 102 DRQDKAGNTALH 113
Cdd:PHA02859  152 LNKDFDNNNILY 163
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 109-199 9.70e-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: 42.31  E-value: 9.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360331 109 NTALHLACQNSHSQSTRVLLLAgSRADL--KNNAGDTCLHVAARYNHLSIIRLLLTAfcsVHE-KNQA-------GDTAL 178
Cdd:cd22192    18 ESPLLLAAKENDVQAIKKLLKC-PSCDLfqRGALGETALHVAALYDNLEAAVVLMEA---APElVNEPmtsdlyqGETAL 93

                          90       100
                  ....*....|....*....|.
gi 2217360331 179 HVAAALNHKKVAKILLEAGAD 199
Cdd:cd22192    94 HIAVVNQNLNLVRELIARGAD 114
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 47-128 1.60e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.81  E-value: 1.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360331  47 HLAANkGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIAALIHEGCALDRQDKAGNTALHLACQNSHSQSTRV 126
Cdd:PTZ00322   88 QLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                  ..
gi 2217360331 127 LL 128
Cdd:PTZ00322  167 LS 168
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 157-204 2.94e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 40.65  E-value: 2.94e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2217360331 157 IRLLLTAFCSVHEKNQAGDTALHVAAALNHKKVAKILLEAGADTTIVN 204
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLD 145
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 127-206 3.07e-03

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 40.67  E-value: 3.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360331 127 LLLAGSRADLKNNAGDTCLH--VAARYNHLSIIRLLLTAFCSVHEKNQAGDTALH-------VAAALNHK-------KVA 190
Cdd:PHA02716  303 FLQPGVKLHYKDSAGRTCLHqyILRHNISTDIIKLLHEYGNDLNEPDNIGNTVLHtylsmlsVVNILDPEtdndirlDVI 382

                          90
                  ....*....|....*.
gi 2217360331 191 KILLEAGADTTIVNNV 206
Cdd:PHA02716  383 QCLISLGADITAVNCL 398
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 141-169 3.42e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 35.31  E-value: 3.42e-03
                          10        20
                  ....*....|....*....|....*....
gi 2217360331 141 GDTCLHVAARYNHLSIIRLLLTAFCSVHE 169
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA03095 PHA03095
ankyrin-like protein; Provisional
 125-206 3.95e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 40.01  E-value: 3.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360331 125 RVLLLAGSRADLKNNAGDTCLHVAARYNH---LSIIRLLLTAFCSVHEKNQAGDTALHVAAALNHK-KVAKILLEAGADT 200
Cdd:PHA03095   31 RRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKAGADV 110


                  ....*.
gi 2217360331 201 TIVNNV 206
Cdd:PHA03095  111 NAKDKV 116
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 4-161 3.97e-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: 40.25  E-value: 3.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360331   4 QDAVAALSERLLVAAYKgqTENVVQLINKGARVAVTKhGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGD-------- 75
Cdd:cd21882    38 NDGVNEAIMLLLEAAPD--SGNPKELVNAPCTDEFYQ-GQTALHIAIENRNLNLVRLLVENGADVSARATGRffrkspgn 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360331  76 -----QTALHRATVVGNTEIIAALI---HEGCALDRQDKAGNTALH---LACQNSHSQSTRV------LLLAGSRAD--- 135
Cdd:cd21882   115 lfyfgELPLSLAACTNQEEIVRLLLengAQPAALEAQDSLGNTVLHalvLQADNTPENSAFVcqmynlLLSYGAHLDptq 194

                         170       180       190
                  ....*....|....*....|....*....|
gi 2217360331 136 ----LKNNAGDTCLHVAARYNHLSIIRLLL 161
Cdd:cd21882   195 qleeIPNHQGLTPLKLAAVEGKIVMFQHIL 224
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 116-194 4.92e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 39.88  E-value: 4.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360331 116 CQNSHSQST---RVLLLAGSRADLKNNAGDTCLHVAARYNHLSIIRLLLTAFCSVHEKNQAGDTALHVAAALNHKKVAKI 192
Cdd:PTZ00322   87 CQLAASGDAvgaRILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                  ..
gi 2217360331 193 LL 194
Cdd:PTZ00322  167 LS 168
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 174-199 5.07e-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: 5.07e-03
                          10        20
                  ....*....|....*....|....*.
gi 2217360331 174 GDTALHVAAALNHKKVAKILLEAGAD 199
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGAD 27
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 112-199 7.53e-03

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 39.68  E-value: 7.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360331 112 LHLACQNSHSQSTRVLLLAGSRADLknnaGDTCLHVAARYNHL---SIIRLLLTAF---CSVHEKN-------QAGDTAL 178
Cdd:TIGR00870  57 FVAAIENENLELTELLLNLSCRGAV----GDTLLHAISLEYVDaveAILLHLLAAFrksGPLELANdqytsefTPGITAL 132

                          90       100
                  ....*....|....*....|.
gi 2217360331 179 HVAAALNHKKVAKILLEAGAD 199
Cdd:TIGR00870 133 HLAAHRQNYEIVKLLLERGAS 153
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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