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Conserved domains on  [gi|1958777944|ref|XP_038966477|]
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ankyrin repeat domain-containing protein 6 isoform X1 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
5-244 4.22e-48

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 171.29  E-value: 4.22e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944   5 DAVAALSERLLIAAYKGQTENVVQLINKGAKV--AVTKHGRTPLHLAANKGHLSVVQILLKAGCDLDVQDDGDQTALHRA 82
Cdd:COG0666    48 ALADALGALLLLAAALAGDLLVALLLLAAGADinAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLA 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944  83 TVVGNTEILTALIREGCALDRQDKDGNTALHEAAWHGFSQSAKLLVKAGANVLARNKAGNTALHLACQNSHSQSTRVLLL 162
Cdd:COG0666   128 AYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLE 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944 163 GGSRADLKNNAGDTCLHVAARYNHLSVVRLLLSAFCSVHEKNQAGDTALHVAAALNHKKVVKILLEAGADTTLVNNAGQT 242
Cdd:COG0666   208 AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287


                  ..
gi 1958777944 243 PL 244
Cdd:COG0666   288 LL 289
PLN02847 super family cl27225
triacylglycerol lipase
 545-706 2.09e-03

triacylglycerol lipase


The actual alignment was detected with superfamily member PLN02847:

Pssm-ID: 178439 [Multi-domain]  Cd Length: 633  Bit Score: 41.40  E-value: 2.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944 545 AGPGA---ASDSSSQVVRPKDKALnATAVPRHQQELLPSDCTGSGLRKVKAPAASRLGDQQTGSCVNRGTQTKKSARGGQ 621
Cdd:PLN02847  373 AGAGAllrPVSSSTQVVMKRAQNV-AQAVVRTRSSLSSWSCMGPRRRSVGSVANSKKEDLPEATHVTSSVNSESLVTEVK 451

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944 622 TKHRGQQPTASSPS-GQQPSAASSDARDASQALELTQYFFEAVSaQMEKWYE--RKIEEARSQASQKAQQDEATLKEHIR 698
Cdd:PLN02847  452 TTKSVEHKSESSSSdGSGHDDEEEEEPLLSEDRVITSSVEEEVT-EGELWYEleKELQRQETEVDAQAQEEEAAAAKEIT 530


                  ....*...
gi 1958777944 699 SLEEEVAK 706
Cdd:PLN02847  531 EEENVLAK 538
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
5-244 4.22e-48

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 171.29  E-value: 4.22e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944   5 DAVAALSERLLIAAYKGQTENVVQLINKGAKV--AVTKHGRTPLHLAANKGHLSVVQILLKAGCDLDVQDDGDQTALHRA 82
Cdd:COG0666    48 ALADALGALLLLAAALAGDLLVALLLLAAGADinAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLA 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944  83 TVVGNTEILTALIREGCALDRQDKDGNTALHEAAWHGFSQSAKLLVKAGANVLARNKAGNTALHLACQNSHSQSTRVLLL 162
Cdd:COG0666   128 AYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLE 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944 163 GGSRADLKNNAGDTCLHVAARYNHLSVVRLLLSAFCSVHEKNQAGDTALHVAAALNHKKVVKILLEAGADTTLVNNAGQT 242
Cdd:COG0666   208 AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287


                  ..
gi 1958777944 243 PL 244
Cdd:COG0666   288 LL 289
PHA03095 PHA03095
ankyrin-like protein; Provisional
 29-265 2.78e-29

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 122.06  E-value: 2.78e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944  29 LINKGAKV-AVTKHGRTPLHL-AANKGHLSVVQILLKAGCDLDVQDDGDQTALHR--ATVVGNTEILTALIREGCALDRQ 104
Cdd:PHA03095   69 LLEAGADVnAPERCGFTPLHLyLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNAL 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944 105 DKDGNTALHeaawhGFSQSA-------KLLVKAGANVLARNKAGNTALHLACQNSHSQST--RVLLLGGSRADLKNNAGD 175
Cdd:PHA03095  149 DLYGMTPLA-----VLLKSRnanvellRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRARivRELIRAGCDPAATDMLGN 223

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944 176 TCLHVAARYNHL--SVVRLLLSAFCSVHEKNQAGDTALHVAAALNHKKVVKILLEAGADTTLVNNAGQTPLETARYHDNP 253
Cdd:PHA03095  224 TPLHSMATGSSCkrSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNG 303

                         250
                  ....*....|...
gi 1958777944 254 E-VALLLTKAPQI 265
Cdd:PHA03095  304 RaVRAALAKNPSA 316
Ank_2 pfam12796
Ankyrin repeats (3 copies);
46-138 5.84e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.86  E-value: 5.84e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944  46 LHLAANKGHLSVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEILTALIrEGCALDRQDkDGNTALHEAAWHGFSQSAK 125
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1958777944 126 LLVKAGANVLARN 138
Cdd:pfam12796  79 LLLEKGADINVKD 91
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 109-244 1.88e-09

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: 60.80  E-value: 1.88e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944 109 NTALHEAAWHGFSQSAK-LLVKAGANVLARNKAGNTALHLACQNSHSQSTRVLLLGGSRadLKNNA-------GDTCLHV 180
Cdd:cd22192    18 ESPLLLAAKENDVQAIKkLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPE--LVNEPmtsdlyqGETALHI 95

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958777944 181 AARYNHLSVVRLLLS------------AFCSVHEKNQA--GDTALHVAAALNHKKVVKILLEAGADTTLVNNAGQTPL 244
Cdd:cd22192    96 AVVNQNLNLVRELIArgadvvspratgTFFRPGPKNLIyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 41-70 1.37e-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: 44.89  E-value: 1.37e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 1958777944   41 HGRTPLHLAANKGHLSVVQILLKAGCDLDV 70
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 41-194 5.85e-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: 5.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944  41 HGRTPLHLAANKGHLSVVQILLKAGCDLDVQDDGD--------------QTALHRATVVGNTEILTALIREGCALDRQDK 106
Cdd:TIGR00870 127 PGITALHLAAHRQNYEIVKLLLERGASVPARACGDffvksqgvdsfyhgESPLNAAACLGSPSIVALLSEDPADILTADS 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944 107 DGNTALHeaawhgfsqsakLLVkaganVLARNKAGNTALHLACQNShsqstrVLLLGGSRADLK------NNAGDTCLHV 180
Cdd:TIGR00870 207 LGNTLLH------------LLV-----MENEFKAEYEELSCQMYNF------ALSLLDKLRDSKelevilNHQGLTPLKL 263

                         170
                  ....*....|....
gi 1958777944 181 AARYNHLSVVRLLL 194
Cdd:TIGR00870 264 AAKEGRIVLFRLKL 277
PLN02847 PLN02847
triacylglycerol lipase
 545-706 2.09e-03

triacylglycerol lipase


Pssm-ID: 178439 [Multi-domain]  Cd Length: 633  Bit Score: 41.40  E-value: 2.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944 545 AGPGA---ASDSSSQVVRPKDKALnATAVPRHQQELLPSDCTGSGLRKVKAPAASRLGDQQTGSCVNRGTQTKKSARGGQ 621
Cdd:PLN02847  373 AGAGAllrPVSSSTQVVMKRAQNV-AQAVVRTRSSLSSWSCMGPRRRSVGSVANSKKEDLPEATHVTSSVNSESLVTEVK 451

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944 622 TKHRGQQPTASSPS-GQQPSAASSDARDASQALELTQYFFEAVSaQMEKWYE--RKIEEARSQASQKAQQDEATLKEHIR 698
Cdd:PLN02847  452 TTKSVEHKSESSSSdGSGHDDEEEEEPLLSEDRVITSSVEEEVT-EGELWYEleKELQRQETEVDAQAQEEEAAAAKEIT 530


                  ....*...
gi 1958777944 699 SLEEEVAK 706
Cdd:PLN02847  531 EEENVLAK 538
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
5-244 4.22e-48

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 171.29  E-value: 4.22e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944   5 DAVAALSERLLIAAYKGQTENVVQLINKGAKV--AVTKHGRTPLHLAANKGHLSVVQILLKAGCDLDVQDDGDQTALHRA 82
Cdd:COG0666    48 ALADALGALLLLAAALAGDLLVALLLLAAGADinAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLA 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944  83 TVVGNTEILTALIREGCALDRQDKDGNTALHEAAWHGFSQSAKLLVKAGANVLARNKAGNTALHLACQNSHSQSTRVLLL 162
Cdd:COG0666   128 AYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLE 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944 163 GGSRADLKNNAGDTCLHVAARYNHLSVVRLLLSAFCSVHEKNQAGDTALHVAAALNHKKVVKILLEAGADTTLVNNAGQT 242
Cdd:COG0666   208 AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287


                  ..
gi 1958777944 243 PL 244
Cdd:COG0666   288 LL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-262 2.26e-47

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 169.36  E-value: 2.26e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944   1 MSQQDAVAALSERLLIAAYKGQTENVVQLINKGAKVAVTKHGRTPLHLAANKGHLSVVQILLKAGCDLDVQDDGDQTALH 80
Cdd:COG0666    13 AALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLH 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944  81 RATVVGNTEILTALIREGCALDRQDKDGNTALHEAAWHGFSQSAKLLVKAGANVLARNKAGNTALHLACQNSHSQSTRVL 160
Cdd:COG0666    93 AAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLL 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944 161 LLGGSRADLKNNAGDTCLHVAARYNHLSVVRLLLSAFCSVHEKNQAGDTALHVAAALNHKKVVKILLEAGADTTLVNNAG 240
Cdd:COG0666   173 LEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDG 252

                         250       260
                  ....*....|....*....|..
gi 1958777944 241 QTPLETARYHDNPEVALLLTKA 262
Cdd:COG0666   253 LTALLLAAAAGAALIVKLLLLA 274
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
24-262 8.06e-47

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 167.82  E-value: 8.06e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944  24 ENVVQLINKGAKVAVTKHGRTPLHLAANKGHLSVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEILTALIREGCALDR 103
Cdd:COG0666     3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944 104 QDKDGNTALHEAAWHGFSQSAKLLVKAGANVLARNKAGNTALHLACQNSHSQSTRVLLLGGSRADLKNNAGDTCLHVAAR 183
Cdd:COG0666    83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958777944 184 YNHLSVVRLLLSAFCSVHEKNQAGDTALHVAAALNHKKVVKILLEAGADTTLVNNAGQTPLETARYHDNPEVALLLTKA 262
Cdd:COG0666   163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
55-262 9.79e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 133.93  E-value: 9.79e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944  55 LSVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEILTALIREGCALDRQDKDGNTALHEAAWHGFSQSAKLLVKAGANV 134
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944 135 LARNKAGNTALHLACQNSHSQSTRVLLLGGSRADLKNNAGDTCLHVAARYNHLSVVRLLLSAFCSVHEKNQAGDTALHVA 214
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1958777944 215 AALNHKKVVKILLEAGADTTLVNNAGQTPLETARYHDNPEVALLLTKA 262
Cdd:COG0666   161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA 208
PHA03095 PHA03095
ankyrin-like protein; Provisional
 29-265 2.78e-29

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 122.06  E-value: 2.78e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944  29 LINKGAKV-AVTKHGRTPLHL-AANKGHLSVVQILLKAGCDLDVQDDGDQTALHR--ATVVGNTEILTALIREGCALDRQ 104
Cdd:PHA03095   69 LLEAGADVnAPERCGFTPLHLyLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNAL 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944 105 DKDGNTALHeaawhGFSQSA-------KLLVKAGANVLARNKAGNTALHLACQNSHSQST--RVLLLGGSRADLKNNAGD 175
Cdd:PHA03095  149 DLYGMTPLA-----VLLKSRnanvellRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRARivRELIRAGCDPAATDMLGN 223

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944 176 TCLHVAARYNHL--SVVRLLLSAFCSVHEKNQAGDTALHVAAALNHKKVVKILLEAGADTTLVNNAGQTPLETARYHDNP 253
Cdd:PHA03095  224 TPLHSMATGSSCkrSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNG 303

                         250
                  ....*....|...
gi 1958777944 254 E-VALLLTKAPQI 265
Cdd:PHA03095  304 RaVRAALAKNPSA 316
PHA03095 PHA03095
ankyrin-like protein; Provisional
 24-262 3.47e-28

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 118.59  E-value: 3.47e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944  24 ENVVQLINKGAKVAVTK-HGRTPLHLAANKGH---LSVVQILLKAGCDLDVQDDGDQTALHRATVVGNTE-ILTALIREG 98
Cdd:PHA03095   28 EEVRRLLAAGADVNFRGeYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAG 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944  99 CALDRQDKDGNTALHeAAWHGFSQSAK---LLVKAGANVLARNKAGNTALH--LACQNSHSQSTRVLLLGGSRADLKNNA 173
Cdd:PHA03095  108 ADVNAKDKVGRTPLH-VYLSGFNINPKvirLLLRKGADVNALDLYGMTPLAvlLKSRNANVELLRLLIDAGADVYAVDDR 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944 174 GDTCLHVAARYNHLS--VVRLLLSAFCSVHEKNQAGDTALHVAAALNHKKVVKI--LLEAGADTTLVNNAGQTPLETARY 249
Cdd:PHA03095  187 FRSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAV 266

                         250
                  ....*....|...
gi 1958777944 250 HDNPEVALLLTKA 262
Cdd:PHA03095  267 FNNPRACRRLIAL 279
Ank_2 pfam12796
Ankyrin repeats (3 copies);
46-138 5.84e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.86  E-value: 5.84e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944  46 LHLAANKGHLSVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEILTALIrEGCALDRQDkDGNTALHEAAWHGFSQSAK 125
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1958777944 126 LLVKAGANVLARN 138
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 40-265 8.28e-21

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 95.50  E-value: 8.28e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944  40 KHGRTPLHLAANKGHLSVVQILLKAGCDLDVQDDGDQTALHRATVVG-----NTEILTALIREGCALDRQDKDGNTALHE 114
Cdd:PHA03100   33 KKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKynltdVKEIVKLLLEYGANVNAPDNNGITPLLY 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944 115 AAWHGFSQSA--KLLVKAGANVLARNKAGNTALHLACQNSHSQS--TRVLLLGGSRADLKNNagdtclhvaarynhlsvV 190
Cdd:PHA03100  113 AISKKSNSYSivEYLLDNGANVNIKNSDGENLLHLYLESNKIDLkiLKLLIDKGVDINAKNR-----------------V 175

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958777944 191 RLLLSAFCSVHEKNQAGDTALHVAAALNHKKVVKILLEAGADTTLVNNAGQTPLETARYHDNPE-VALLLTKAPQI 265
Cdd:PHA03100  176 NYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEiFKLLLNNGPSI 251
Ank_2 pfam12796
Ankyrin repeats (3 copies);
145-237 1.46e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 86.71  E-value: 1.46e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944 145 LHLACQNSHSQSTRVLLLGGSRADLKNNAGDTCLHVAARYNHLSVVRLLLSAFCSvhEKNQAGDTALHVAAALNHKKVVK 224
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1958777944 225 ILLEAGADTTLVN 237
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 19-248 1.67e-19

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 92.01  E-value: 1.67e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944  19 YKGQTENVVQ-LINKGAKV-AVTKHGRTPLHL-AANKG-HLSVVQILLKAGCDLDVQDDGDQTALH------RATVvgnt 88
Cdd:PHA03095   92 YNATTLDVIKlLIKAGADVnAKDKVGRTPLHVyLSGFNiNPKVIRLLLRKGADVNALDLYGMTPLAvllksrNANV---- 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944  89 EILTALIREGCALDRQDKDGNTALHEaawhgFSQSAK-------LLVKAGANVLARNKAGNTALHLACQNSHSQSTRV-- 159
Cdd:PHA03095  168 ELLRLLIDAGADVYAVDDRFRSLLHH-----HLQSFKprarivrELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlp 242

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944 160 LLLGGSRADLKNNAGDTCLHVAARYNHLSVVRLLLSAFCSVHEKNQAGDTALHVAAALNHKKVVKILLE--------AGA 231
Cdd:PHA03095  243 LLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAknpsaetvAAT 322

                         250
                  ....*....|....*..
gi 1958777944 232 DTTLVNNAGQTPLETAR 248
Cdd:PHA03095  323 LNTASVAGGDIPSDATR 339
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 57-247 7.42e-19

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 89.64  E-value: 7.42e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944  57 VVQILLKAGCDLDVQDDGDQTALHRATVVGNTEILTALIREGCALDRQDKDGNTALHEAAWHGFSQSAKLLVKAGANVLA 136
Cdd:PHA02874  106 MIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANV 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944 137 RNKAGNTALHLACQNSHSQSTRVLLLGGSRADLKNNAGDTCLHVAARYNHlSVVRLLLSAfCSVHEKNQAGDTALHvaAA 216
Cdd:PHA02874  186 KDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLINN-ASINDQDIDGSTPLH--HA 261

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1958777944 217 LNH---KKVVKILLEAGADTTLVNNAGQTPLETA 247
Cdd:PHA02874  262 INPpcdIDIIDILLYHKADISIKDNKGENPIDTA 295
Ank_2 pfam12796
Ankyrin repeats (3 copies);
112-204 2.79e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.16  E-value: 2.79e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944 112 LHEAAWHGFSQSAKLLVKAGANVLARNKAGNTALHLACQNSHSQSTRvLLLGGSRADLKNNaGDTCLHVAARYNHLSVVR 191
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVK-LLLEHADVNLKDN-GRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1958777944 192 LLLSAFCSVHEKN 204
Cdd:pfam12796  79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
14-105 1.39e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 78.23  E-value: 1.39e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944  14 LLIAAYKGQTENVVQLINKGAKV-AVTKHGRTPLHLAANKGHLSVVQILLKaGCDLDVQDDGdQTALHRATVVGNTEILT 92
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADAnLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDNG-RTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1958777944  93 ALIREGCALDRQD 105
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 88-247 2.11e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 82.62  E-value: 2.11e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944  88 TEILTALIREGCALDRQDKD-GNTALHEAAWHGFSQSAKLLVKAGANVLARNKAGNTALHLACQNSHSQSTRVLLLGGSR 166
Cdd:PHA02878  147 AEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAS 226

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944 167 ADLKNNAGDTCLHVAARY-NHLSVVRLLLSAFCSVHEKNQA-GDTALHVAaaLNHKKVVKILLEAGADTTLVNNAGQTPL 244
Cdd:PHA02878  227 TDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYIlGLTALHSS--IKSERKLKLLLEYGADINSLNSYKLTPL 304


                  ...
gi 1958777944 245 ETA 247
Cdd:PHA02878  305 SSA 307
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 26-200 3.95e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 81.25  E-value: 3.95e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944  26 VVQLINKGAKVAV-TKHGRTPLHLAANKGH-----LSVVQILLKAGCDLDVQDDGDQTALHRA--TVVGNTEILTALIRE 97
Cdd:PHA03100   51 VKILLDNGADINSsTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVNAPDNNGITPLLYAisKKSNSYSIVEYLLDN 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944  98 GCALDRQDKDGNTALHEAAWHGFSQS--AKLLVKAGANV----------------LARNKAGNTALHLACQNSHSQSTRV 159
Cdd:PHA03100  131 GANVNIKNSDGENLLHLYLESNKIDLkiLKLLIDKGVDInaknrvnyllsygvpiNIKDVYGFTPLHYAVYNNNPEFVKY 210

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1958777944 160 LLLGGSRADLKNNAGDTCLHVAARYNHLSVVRLLLSAFCSV 200
Cdd:PHA03100  211 LLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSI 251
Ank_2 pfam12796
Ankyrin repeats (3 copies);
178-259 7.98e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 73.23  E-value: 7.98e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944 178 LHVAARYNHLSVVRLLLSAFCSVHEKNQAGDTALHVAAALNHKKVVKILLEaGADTTLVNNaGQTPLETARYHDNPEVAL 257
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIVK 78


                  ..
gi 1958777944 258 LL 259
Cdd:pfam12796  79 LL 80
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 10-262 1.26e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 79.62  E-value: 1.26e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944  10 LSERLLIAAYKGQTENVVQLI-NKGAKVAVT-KHGRTPLHLAANKGHLSVVQILLKAGCDLDVQDDGDQTALHRATVVGN 87
Cdd:PHA02874    1 ASQDLRMCIYSGDIEAIEKIIkNKGNCINISvDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944  88 TEILTALIREGC---ALDRQDKDGNTAlheaawhgfsqsaKLLVKAGANVLARNKAGNTALHLACQNSHSQSTRVLLLGG 164
Cdd:PHA02874   81 HDIIKLLIDNGVdtsILPIPCIEKDMI-------------KTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYG 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944 165 SRADLKNNAGDTCLHVAARYNHLSVVRLLLSAFCSVHEKNQAGDTALHVAAALNHKKVVKILLEAGADTTLVNNAGQTPL 244
Cdd:PHA02874  148 ADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPL 227

                         250
                  ....*....|....*...
gi 1958777944 245 ETARYHDNPEVALLLTKA 262
Cdd:PHA02874  228 HNAIIHNRSAIELLINNA 245
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 14-250 2.66e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 76.64  E-value: 2.66e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944  14 LLIAAYKGQTENVVQLINKGAKV-AVTKHGRTPLHLAANKGHLS-VVQILLKAGCDLDVQDDGDQTALHRATVVG-NTEI 90
Cdd:PHA02876  244 LLKAIRNEDLETSLLLYDAGFSVnSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMAKNGyDTEN 323

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944  91 LTALIREGCALDRQDKDGNTALHEAA-WHGFSQSAKLLVKAGANVLARNKAGNTALHLACQNSHSQSTRVLLLGGSRADL 169
Cdd:PHA02876  324 IRTLIMLGADVNAADRLYITPLHQAStLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEA 403

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944 170 KNNAGDTCLHVA-ARYNHLSVVRLLLSAFCSVHEKNQAGDTALHVAAALNHK-KVVKILLEAGADTTLVNNAGQTPLETA 247
Cdd:PHA02876  404 LSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNCKlDVIEMLLDNGADVNAINIQNQYPLLIA 483


                  ....
gi 1958777944 248 -RYH 250
Cdd:PHA02876  484 lEYH 487
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 29-253 3.28e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 76.26  E-value: 3.28e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944  29 LINKGAKV-AVTKHGRTPLHLAANKGHLSVVQILLKAGCDLDVQDDGDQTALHRAT------------------------ 83
Cdd:PHA02876  164 LLEGGADVnAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVdsknidtikaiidnrsninkndls 243

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944  84 ---VVGNTEILTALI--REGCALDRQDKDGNTALHEAAWH-GFSQSAKLLVKAGANVLARNKAGNTALHLACQNSH-SQS 156
Cdd:PHA02876  244 llkAIRNEDLETSLLlyDAGFSVNSIDDCKNTPLHHASQApSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTEN 323

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944 157 TRVLLLGGSRADLKNNAGDTCLHVAA---RYNHLSVVRLLLSAfcSVHEKNQAGDTALHVAAALNHKKVVKILLEAGADT 233
Cdd:PHA02876  324 IRTLIMLGADVNAADRLYITPLHQAStldRNKDIVITLLELGA--NVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADI 401

                         250       260
                  ....*....|....*....|
gi 1958777944 234 TLVNNAGQTPLETARYHDNP 253
Cdd:PHA02876  402 EALSQKIGTALHFALCGTNP 421
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 42-171 1.41e-13

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 74.52  E-value: 1.41e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944  42 GRTPLHLAANKGHLSVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEILTALIREGCALDRQdkDGNTALHEAAWHGFS 121
Cdd:PLN03192  558 GRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPH--AAGDLLCTAAKRNDL 635

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958777944 122 QSAKLLVKAGANVLARNKAGNTALHLACQNSHSQSTRVLLLGGSRADLKN 171
Cdd:PLN03192  636 TAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAN 685
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 42-254 2.53e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 72.33  E-value: 2.53e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944  42 GRTPLHLAANKGHLSVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEILTALIREGC-ALDRQDKDGNTALHEAAWHGF 120
Cdd:PHA02875   35 GISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKfADDVFYKDGMTPLHLATILKK 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944 121 SQSAKLLVKAGANVLARNKAGNTALHLACQNSHSQSTRVLLLGGSRADLKNNAGDTCLHVAARYNHLSVVRLLLSAFCSV 200
Cdd:PHA02875  115 LDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANI 194

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958777944 201 HEKNQAGDTALHVAAALNHK-KVVKILLEAGADT---TLVNNAGQTPLETARYHD-NPE 254
Cdd:PHA02875  195 DYFGKNGCVAALCYAIENNKiDIVRLFIKRGADCnimFMIEGEECTILDMICNMCtNLE 253
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 22-198 5.16e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 71.83  E-value: 5.16e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944  22 QTENVVQLINKGAKV-AVTKH-GRTPLHLAANKGHLSVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEILTALIREGC 99
Cdd:PHA02878  146 EAEITKLLLSYGADInMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA 225

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944 100 ALDRQDKDGNTALHEAAWHGFSQSA-KLLVKAGANVLARNKA-GNTALHLACQNshSQSTRVLLLGGSRADLKNNAGDTC 177
Cdd:PHA02878  226 STDARDKCGNTPLHISVGYCKDYDIlKLLLEHGVDVNAKSYIlGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTP 303

                         170       180
                  ....*....|....*....|..
gi 1958777944 178 LHVAAR-YNHLSVVRLLLSAFC 198
Cdd:PHA02878  304 LSSAVKqYLCINIGRILISNIC 325
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 49-237 1.35e-12

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 71.05  E-value: 1.35e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944  49 AANKGHLSVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEILTALIREGCALDRQDKDGNTALHEAawhgfsqsakllV 128
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNA------------I 599

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944 129 KAGanvlaRNKAGNTALHLAcqnshsqstrvlllggsRADLKNNAGDTcLHVAARYNHLSVVRLLLSAFCSVHEKNQAGD 208
Cdd:PLN03192  600 SAK-----HHKIFRILYHFA-----------------SISDPHAAGDL-LCTAAKRNDLTAMKELLKQGLNVDSEDHQGA 656

                         170       180
                  ....*....|....*....|....*....
gi 1958777944 209 TALHVAAALNHKKVVKILLEAGADTTLVN 237
Cdd:PLN03192  657 TALQVAMAEDHVDMVRLLIMNGADVDKAN 685
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 15-194 1.81e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 70.48  E-value: 1.81e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944  15 LIAAYKGQTENVVQLINKGAKV-AVTKHGRTPLHLAAN-KGHLSVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEILT 92
Cdd:PHA02876  313 LMAKNGYDTENIRTLIMLGADVnAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIIN 392

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944  93 ALIREGCALDRQDKDGNTALHeAAWHGFS--QSAKLLVKAGANVLARNKAGNTALHLACQ-NSHSQSTRVLLLGGSRADL 169
Cdd:PHA02876  393 TLLDYGADIEALSQKIGTALH-FALCGTNpyMSVKTLIDRGANVNSKNKDLSTPLHYACKkNCKLDVIEMLLDNGADVNA 471

                         170       180
                  ....*....|....*....|....*
gi 1958777944 170 KNNAGDTCLHVAARYNhlSVVRLLL 194
Cdd:PHA02876  472 INIQNQYPLLIALEYH--GIVNILL 494
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 17-169 2.04e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 63.47  E-value: 2.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944  17 AAYKGQTENVVQLI--NKGAKVAVTKHGRTPLHLAANKGHLSVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEILTAL 94
Cdd:PHA02875   75 AVEEGDVKAVEELLdlGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELL 154

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958777944  95 IREGCALDRQDKDGNTALHEAAWHGFSQSAKLLVKAGANVLARNKAGN-TALHLACQNSHSQSTRVLLLGGSRADL 169
Cdd:PHA02875  155 IDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGADCNI 230
Ank_4 pfam13637
Ankyrin repeats (many copies);
42-95 2.63e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 56.13  E-value: 2.63e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958777944  42 GRTPLHLAANKGHLSVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEILTALI 95
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 55-252 1.75e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 61.23  E-value: 1.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944  55 LSVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEILTALIREG---------------CALDRQDKD------------ 107
Cdd:PHA02876  158 LLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGadvniialddlsvleCAVDSKNIDtikaiidnrsni 237

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944 108 --GNTALHEAAWHGFSQSAKLLVKAGANVLARNKAGNTALHLACQN-SHSQSTRVLLLGGSRADLKNNAGDTCLHVAARY 184
Cdd:PHA02876  238 nkNDLSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQApSLSRLVPKLLERGADVNAKNIKGETPLYLMAKN 317

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944 185 NH-LSVVRLLLSAFCSVHEKNQAGDTALHVAAALN-HKKVVKILLEAGADTTLVNNAGQTPLETARYHDN 252
Cdd:PHA02876  318 GYdTENIRTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYAAVRNN 387
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 109-244 1.88e-09

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: 60.80  E-value: 1.88e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944 109 NTALHEAAWHGFSQSAK-LLVKAGANVLARNKAGNTALHLACQNSHSQSTRVLLLGGSRadLKNNA-------GDTCLHV 180
Cdd:cd22192    18 ESPLLLAAKENDVQAIKkLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPE--LVNEPmtsdlyqGETALHI 95

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958777944 181 AARYNHLSVVRLLLS------------AFCSVHEKNQA--GDTALHVAAALNHKKVVKILLEAGADTTLVNNAGQTPL 244
Cdd:cd22192    96 AVVNQNLNLVRELIArgadvvspratgTFFRPGPKNLIyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
Ank_4 pfam13637
Ankyrin repeats (many copies);
174-227 2.73e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.43  E-value: 2.73e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958777944 174 GDTCLHVAARYNHLSVVRLLLSAFCSVHEKNQAGDTALHVAAALNHKKVVKILL 227
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 13-247 3.65e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 59.51  E-value: 3.65e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944  13 RLLIAAYKGQTENVVQLINKGAKvavTKHGRT--------PLHLAANKGHLSVVQILLKAGCDLDVQDDGDQTALHRATV 84
Cdd:PHA02878    3 KLYKSMYTDNYETILKYIEYIDH---TENYSTsaslipfiPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944  85 VGNTEILTALIREgcalDRQDKDGNT--ALHEAAWHGFSQSAKLLVkaganvLARNKAGNTA-LHLACQNSHSQS----- 156
Cdd:PHA02878   80 EPNKLGMKEMIRS----INKCSVFYTlvAIKDAFNNRNVEIFKIIL------TNRYKNIQTIdLVYIDKKSKDDIieaei 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944 157 TRVLLLGGSRADLKN-NAGDTCLHVAARYNHLSVVRLLLSAFCSVHEKNQAGDTALHVAAALNHKKVVKILLEAGADTTL 235
Cdd:PHA02878  150 TKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDA 229

                         250
                  ....*....|..
gi 1958777944 236 VNNAGQTPLETA 247
Cdd:PHA02878  230 RDKCGNTPLHIS 241
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 190-264 1.02e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 58.76  E-value: 1.02e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958777944 190 VRLLLSAFCSVHEKNQAGDTALHVAAALNHKKVVKILLEAGADTTLVNNAGQTPLETARYHDNPEVALLLTKAPQ 264
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQ 172
Ank_5 pfam13857
Ankyrin repeats (many copies);
40-82 1.11e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 51.58  E-value: 1.11e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1958777944  40 KHGRTPLHLAANKGHLSVVQILLKAGCDLDVQDDGDQTALHRA 82
Cdd:pfam13857  14 GEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 11-187 1.24e-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: 58.10  E-value: 1.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944  11 SERLLIAAYKgqtENVVQLINKGAKVAVTK------HGRTPLHLAANKGHLSVVQILLKAGCDL-DVQDDGD----QTAL 79
Cdd:cd22192    17 SESPLLLAAK---ENDVQAIKKLLKCPSCDlfqrgaLGETALHVAALYDNLEAAVVLMEAAPELvNEPMTSDlyqgETAL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944  80 HRATVVGNTEILTALIREG-----------CALDRQDKD---GNTALHEAAWHGFSQSAKLLVKAGANVLARNKAGNTAL 145
Cdd:cd22192    94 HIAVVNQNLNLVRELIARGadvvspratgtFFRPGPKNLiyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958777944 146 H-LACQNSHSQSTRV--LLLGGSRAD-------LKNNAGDTCLHVAAR------YNHL 187
Cdd:cd22192   174 HiLVLQPNKTFACQMydLILSYDKEDdlqpldlVPNNQGLTPFKLAAKegnivmFQHL 231
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 53-261 8.60e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 55.00  E-value: 8.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944  53 GHLSVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEILTALIREGCALDRQDKDGNTALHEAAWHGFSQSAKLLVKAGA 132
Cdd:PHA02875   13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGK 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944 133 ---NVLArnKAGNTALHLACQNSHSQSTRVLLLGGSRADLKNNAGDTCLHVAARYNHLSVVRLLLSAFCSVHEKNQAGDT 209
Cdd:PHA02875   93 fadDVFY--KDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCT 170

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958777944 210 ALHVAAALNHKKVVKILLEAGADTTLVNNAGQ-TPLETARYHDNPEVALLLTK 261
Cdd:PHA02875  171 PLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIK 223
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 41-73 9.27e-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: 9.27e-08
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1958777944  41 HGRTPLHLAANK-GHLSVVQILLKAGCDLDVQDD 73
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 44-255 1.19e-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: 55.02  E-value: 1.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944  44 TPLHLAANKGHLSVVQILLK-AGCDLDVQDDGDQTALHRATVVGNTEILTALIREGCALDRQDK-----DGNTALHEAAW 117
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEPMtsdlyQGETALHIAVV 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944 118 HGFSQSAKLLVKAGANVlARNKAGNTALHLacqnshsqstrvlllggsRADLKNNAGDTCLHVAARYNHLSVVRLLLSAF 197
Cdd:cd22192    99 NQNLNLVRELIARGADV-VSPRATGTFFRP------------------GPKNLIYYGEHPLSFAACVGNEEIVRLLIEHG 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958777944 198 CSVHEKNQAGDTALHVAAALNHKKVVK-----IL-LEAGADT----TLVNNAGQTPLETARYHDNPEV 255
Cdd:cd22192   160 ADIRAQDSLGNTVLHILVLQPNKTFACqmydlILsYDKEDDLqpldLVPNNQGLTPFKLAAKEGNIVM 227
Ank_4 pfam13637
Ankyrin repeats (many copies);
108-161 1.93e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.04  E-value: 1.93e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958777944 108 GNTALHEAAWHGFSQSAKLLVKAGANVLARNKAGNTALHLACQNSHSQSTRVLL 161
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 57-251 2.29e-07

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 54.15  E-value: 2.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944  57 VVQILLKAGCDLDVQDDGDQTALHRATVVGN--TEILTALIREGCALDRQDKDGNTALHEAAWHGFSQSAKLlVKAGANV 134
Cdd:PHA02716  194 ILEWLCNNGVNVNLQNNHLITPLHTYLITGNvcASVIKKIIELGGDMDMKCVNGMSPIMTYIINIDNINPEI-TNIYIES 272

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944 135 LARNKAGNTA--LHLACQNSHSQSTRVL---LLGGSRADLKNNAGDTCLH--VAARYNHLSVVRLLLSAFCSVHEKNQAG 207
Cdd:PHA02716  273 LDGNKVKNIPmiLHSYITLARNIDISVVysfLQPGVKLHYKDSAGRTCLHqyILRHNISTDIIKLLHEYGNDLNEPDNIG 352

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958777944 208 DTALH-------VAAALNHK-------KVVKILLEAGADTTLVNNAGQTPLE----TAR---YHD 251
Cdd:PHA02716  353 NTVLHtylsmlsVVNILDPEtdndirlDVIQCLISLGADITAVNCLGYTPLTsyicTAQnymYYD 417
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 75-270 3.00e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 53.46  E-value: 3.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944  75 DQTALHRATVVGNTEILTALIREGCALDRQDKDGNTALHEAAWHGFSQSAKLLVKAGANVLARNKAGNTALHLACQNSHS 154
Cdd:PHA02875    2 DQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944 155 QSTRVLLLGGSRA-DLKNNAGDTCLHVAARYNHLSVVRLLLSAFCSVHEKNQAGDTALHVAAALNHKKVVKILLEAGADT 233
Cdd:PHA02875   82 KAVEELLDLGKFAdDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACL 161

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1958777944 234 TLVNNAGQTPLETARYHDNPEVA-LLLTKAPQILRFSR 270
Cdd:PHA02875  162 DIEDCCGCTPLIIAMAKGDIAICkMLLDSGANIDYFGK 199
Ank_4 pfam13637
Ankyrin repeats (many copies);
141-194 3.00e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.65  E-value: 3.00e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958777944 141 GNTALHLACQNSHSQSTRVLLLGGSRADLKNNAGDTCLHVAARYNHLSVVRLLL 194
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 71-202 3.05e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 53.75  E-value: 3.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944  71 QDDGDQTALHRATVvgnteiltalirEGCALdrqdkdgntalheaAWHGFSQSAKLLVKAGANVLARNKAGNTALHLACQ 150
Cdd:PTZ00322   71 EEVIDPVVAHMLTV------------ELCQL--------------AASGDAVGARILLTGGADPNCRDYDGRTPLHIACA 124

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958777944 151 NSHSQSTRVLLLGGSRADLKNNAGDTCLHVAARYNHLSVVRLLLSAFCSVHE 202
Cdd:PTZ00322  125 NGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFE 176
Ank_4 pfam13637
Ankyrin repeats (many copies);
207-259 3.38e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.27  E-value: 3.38e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958777944 207 GDTALHVAAALNHKKVVKILLEAGADTTLVNNAGQTPLETARYHDNPEVALLL 259
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 175-247 6.67e-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: 52.71  E-value: 6.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944 175 DTCLHVAARYNHL-SVVRLLLSAFCSVHEKNQAGDTALHVAAALNHKKVVKILLEagADTTLVNNA-------GQTPLET 246
Cdd:cd22192    18 ESPLLLAAKENDVqAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPELVNEPmtsdlyqGETALHI 95


                  .
gi 1958777944 247 A 247
Cdd:cd22192    96 A 96
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 41-70 1.37e-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: 44.89  E-value: 1.37e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 1958777944   41 HGRTPLHLAANKGHLSVVQILLKAGCDLDV 70
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02791 PHA02791
ankyrin-like protein; Provisional
 41-204 1.57e-06

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 50.43  E-value: 1.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944  41 HGRTPLHLAANKGHLSVVQILLKAGCDLDVQDDgdQTALHRATVVGNTEILTALIREGCALDRQDKDGNTALHEAAWHGF 120
Cdd:PHA02791   29 HGHSALYYAIADNNVRLVCTLLNAGALKNLLEN--EFPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDSGN 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944 121 SQSAKLLVKAGANVLARNKAG--NTALHLACQNSHSQSTRVLLLGGSRADLKNNAgdTCLHVAARYNHLSVVRLLLSAFC 198
Cdd:PHA02791  107 MQTVKLFVKKNWRLMFYGKTGwkTSFYHAVMLNDVSIVSYFLSEIPSTFDLAILL--SCIHITIKNGHVDMMILLLDYMT 184


                  ....*.
gi 1958777944 199 SVHEKN 204
Cdd:PHA02791  185 STNTNN 190
Ank_5 pfam13857
Ankyrin repeats (many copies);
163-214 1.96e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.42  E-value: 1.96e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958777944 163 GGSRADLKNNAGDTCLHVAARYNHLSVVRLLLSAFCSVHEKNQAGDTALHVA 214
Cdd:pfam13857   5 GPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
94-148 2.29e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.03  E-value: 2.29e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958777944  94 LIREG-CALDRQDKDGNTALHEAAWHGFSQSAKLLVKAGANVLARNKAGNTALHLA 148
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_2 pfam12796
Ankyrin repeats (3 copies);
211-273 2.64e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 46.26  E-value: 2.64e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958777944 211 LHVAAALNHKKVVKILLEAGADTTLVNNAGQTPLETARYHDNPEVALLLTKAPQILRFSRGRS 273
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGRT 63
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 79-259 3.15e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 50.26  E-value: 3.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944  79 LHRATVVGNTEILTALIREGCALDRQDKDGNTALHEAAWHGFSQSAKLLVKaganVLARNKAGNT--ALHLACQNSHSQS 156
Cdd:PHA02878   41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIR----SINKCSVFYTlvAIKDAFNNRNVEI 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944 157 TRVLLLGGSRADLKNNAGDTCLHVAARYNHLSVVRLLLSAFCSVHEKNQ-AGDTALHVAAALNHKKVVKILLEAGADTTL 235
Cdd:PHA02878  117 FKIILTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNI 196

                         170       180
                  ....*....|....*....|....*
gi 1958777944 236 VNNAGQTPLETA-RYHDNPEVALLL 259
Cdd:PHA02878  197 PDKTNNSPLHHAvKHYNKPIVHILL 221
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 10-96 4.96e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.90  E-value: 4.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944  10 LSERLLIAAYKGQTENVVQLINKGAKV-AVTKHGRTPLHLAANKGHLSVVQILLKAGCDLDVQDDGDQTALHRATVVGNT 88
Cdd:PTZ00322   82 LTVELCQLAASGDAVGARILLTGGADPnCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFR 161


                  ....*...
gi 1958777944  89 EILTALIR 96
Cdd:PTZ00322  162 EVVQLLSR 169
Ank_5 pfam13857
Ankyrin repeats (many copies);
193-247 7.08e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.87  E-value: 7.08e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958777944 193 LLSAF-CSVHEKNQAGDTALHVAAALNHKKVVKILLEAGADTTLVNNAGQTPLETA 247
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 41-70 1.25e-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.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 42.24  E-value: 1.25e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 1958777944  41 HGRTPLHLAANKGHLSVVQILLKAGCDLDV 70
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 107-139 2.12e-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: 2.12e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1958777944 107 DGNTALHEAAWH-GFSQSAKLLVKAGANVLARNK 139
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 207-238 2.27e-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: 2.27e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1958777944 207 GDTALHVAAA-LNHKKVVKILLEAGADTTLVNN 238
Cdd:pfam00023   2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
Ank_5 pfam13857
Ankyrin repeats (many copies);
127-181 3.72e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.56  E-value: 3.72e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958777944 127 LVKAG-ANVLARNKAGNTALHLACQNSHSQSTRVLLLGGSRADLKNNAGDTCLHVA 181
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 29-147 4.32e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 45.20  E-value: 4.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944  29 LINKGAKV-AVTKH-GRTPLH--LAANKG-HLSVVQILLKAGCDLDVQDDGDQTALHR--ATVVGNTEILTALIREGCAL 101
Cdd:PHA02859   72 LIENGADVnFKTRDnNLSALHhyLSFNKNvEPEILKILIDSGSSITEEDEDGKNLLHMymCNFNVRINVIKLLIDSGVSF 151

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1958777944 102 DRQDKDGNTALHE-AAWHGFSQSAKLLVKAGANVLARNKAGNTALHL 147
Cdd:PHA02859  152 LNKDFDNNNILYSyILFHSDKKIFDFLTSLGIDINETNKSGYNCYDL 198
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 41-194 5.85e-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: 5.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944  41 HGRTPLHLAANKGHLSVVQILLKAGCDLDVQDDGD--------------QTALHRATVVGNTEILTALIREGCALDRQDK 106
Cdd:TIGR00870 127 PGITALHLAAHRQNYEIVKLLLERGASVPARACGDffvksqgvdsfyhgESPLNAAACLGSPSIVALLSEDPADILTADS 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944 107 DGNTALHeaawhgfsqsakLLVkaganVLARNKAGNTALHLACQNShsqstrVLLLGGSRADLK------NNAGDTCLHV 180
Cdd:TIGR00870 207 LGNTLLH------------LLV-----MENEFKAEYEELSCQMYNF------ALSLLDKLRDSKelevilNHQGLTPLKL 263

                         170
                  ....*....|....
gi 1958777944 181 AARYNHLSVVRLLL 194
Cdd:TIGR00870 264 AAKEGRIVLFRLKL 277
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 207-232 5.92e-05

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: 40.26  E-value: 5.92e-05
                           10        20
                   ....*....|....*....|....*.
gi 1958777944  207 GDTALHVAAALNHKKVVKILLEAGAD 232
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGAD 27
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 47-127 6.84e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.04  E-value: 6.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944  47 HLAANkGHLSVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEILTALIREGCALDRQDKDGNTALHEAAWHGFSQSAKL 126
Cdd:PTZ00322   88 QLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                  .
gi 1958777944 127 L 127
Cdd:PTZ00322  167 L 167
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 174-202 1.66e-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: 1.66e-04
                           10        20
                   ....*....|....*....|....*....
gi 1958777944  174 GDTCLHVAARYNHLSVVRLLLSAFCSVHE 202
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 174-204 1.76e-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: 39.19  E-value: 1.76e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1958777944 174 GDTCLHVAA-RYNHLSVVRLLLSAFCSVHEKN 204
Cdd:pfam00023   2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PHA03095 PHA03095
ankyrin-like protein; Provisional
 187-262 2.19e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 44.25  E-value: 2.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944 187 LSVVRLLLSAFCSVHEKNQAGDTALHVAAALNH---KKVVKILLEAGADTTLVNNAGQTPLETARYHDN-PEVALLLTKA 262
Cdd:PHA03095   27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKA 106
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 145-232 4.75e-04

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 43.53  E-value: 4.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944 145 LHLACQNSHSQSTRVLLLGGSRADLknnaGDTCLHvAARYNHLSVVRLLLSAFCSVHEKN--------------QAGDTA 210
Cdd:TIGR00870  57 FVAAIENENLELTELLLNLSCRGAV----GDTLLH-AISLEYVDAVEAILLHLLAAFRKSgplelandqytsefTPGITA 131

                          90       100
                  ....*....|....*....|..
gi 1958777944 211 LHVAAALNHKKVVKILLEAGAD 232
Cdd:TIGR00870 132 LHLAAHRQNYEIVKLLLERGAS 153
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 125-251 5.06e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 42.11  E-value: 5.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944 125 KLLVKAGANVLARNKAGN-TALHLAC---QNSHSQSTRVLLLGGSRADLKNNAGDTCLHV-AARYN-HLSVVRLLLSAFC 198
Cdd:PHA02859   70 KFLIENGADVNFKTRDNNlSALHHYLsfnKNVEPEILKILIDSGSSITEEDEDGKNLLHMyMCNFNvRINVIKLLIDSGV 149

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958777944 199 SVHEKNQAGDTALHVAAAL-NHKKVVKILLEAGADTTLVNNAGQTPLETARYHD 251
Cdd:PHA02859  150 SFLNKDFDNNNILYSYILFhSDKKIFDFLTSLGIDINETNKSGYNCYDLIKFRN 203
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 207-232 1.26e-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: 36.85  E-value: 1.26e-03
                          10        20
                  ....*....|....*....|....*.
gi 1958777944 207 GDTALHVAAALNHKKVVKILLEAGAD 232
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGAD 27
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 42-150 1.98e-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: 41.67  E-value: 1.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944  42 GRTPLHLAANKGHLSVVQILLKAGCDLDVQDDGD--------------QTALHRATVVGNTEILTaLIREGCALD--RQD 105
Cdd:cd22194   141 GQTALNIAIERRQGDIVKLLIAKGADVNAHAKGVffnpkykhegfyfgETPLALAACTNQPEIVQ-LLMEKESTDitSQD 219

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958777944 106 KDGNTALH---EAAWHGFSQSA-------KLLVKAGANVL--ARNKAGNTALHLACQ 150
Cdd:cd22194   220 SRGNTVLHalvTVAEDSKTQNDfvkrmydMILLKSENKNLetIRNNEGLTPLQLAAK 276
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 107-134 2.07e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.03  E-value: 2.07e-03
                           10        20
                   ....*....|....*....|....*...
gi 1958777944  107 DGNTALHEAAWHGFSQSAKLLVKAGANV 134
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
PLN02847 PLN02847
triacylglycerol lipase
 545-706 2.09e-03

triacylglycerol lipase


Pssm-ID: 178439 [Multi-domain]  Cd Length: 633  Bit Score: 41.40  E-value: 2.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944 545 AGPGA---ASDSSSQVVRPKDKALnATAVPRHQQELLPSDCTGSGLRKVKAPAASRLGDQQTGSCVNRGTQTKKSARGGQ 621
Cdd:PLN02847  373 AGAGAllrPVSSSTQVVMKRAQNV-AQAVVRTRSSLSSWSCMGPRRRSVGSVANSKKEDLPEATHVTSSVNSESLVTEVK 451

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944 622 TKHRGQQPTASSPS-GQQPSAASSDARDASQALELTQYFFEAVSaQMEKWYE--RKIEEARSQASQKAQQDEATLKEHIR 698
Cdd:PLN02847  452 TTKSVEHKSESSSSdGSGHDDEEEEEPLLSEDRVITSSVEEEVT-EGELWYEleKELQRQETEVDAQAQEEEAAAAKEIT 530


                  ....*...
gi 1958777944 699 SLEEEVAK 706
Cdd:PLN02847  531 EEENVLAK 538
PHA02741 PHA02741
hypothetical protein; Provisional
 171-267 2.91e-03

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 39.26  E-value: 2.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944 171 NNAGDTCLHVAARYNH----LSVVRLLLSAFCSVHEKNQA-GDTALHVAA-ALNHKKVVKILLEAGADTTLVNNAGQTPL 244
Cdd:PHA02741   57 DDAGQMCIHIAAEKHEaqlaAEIIDHLIELGADINAQEMLeGDTALHLAAhRRDHDLAEWLCCQPGIDLHFCNADNKSPF 136

                          90       100
                  ....*....|....*....|...
gi 1958777944 245 ETARyhDNPEVALLltkapQILR 267
Cdd:PHA02741  137 ELAI--DNEDVAMM-----QILR 152
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 174-202 3.17e-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: 35.70  E-value: 3.17e-03
                          10        20
                  ....*....|....*....|....*....
gi 1958777944 174 GDTCLHVAARYNHLSVVRLLLSAFCSVHE 202
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 137-232 4.58e-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: 4.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944 137 RNKAGNTALHLACQNSHSQ--STRVLLL-----GGSRADLKNNA-------GDTCLHVAARYNHLSVVRLLLSAFCSVH- 201
Cdd:cd21882    22 RGATGKTCLHKAALNLNDGvnEAIMLLLeaapdSGNPKELVNAPctdefyqGQTALHIAIENRNLNLVRLLVENGADVSa 101

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1958777944 202 -------EKNQA-----GDTALHVAAALNHKKVVKILLEAGAD 232
Cdd:cd21882   102 ratgrffRKSPGnlfyfGELPLSLAACTNQEEIVRLLLENGAQ 144
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 202-263 4.83e-03

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 40.13  E-value: 4.83e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958777944 202 EKNQAGDTALHVAAALNHKKVVKILLEAGADT------TLVNNA--------GQTPLETARYHDNPE-VALLLTKAP 263
Cdd:cd22194   136 EEAYEGQTALNIAIERRQGDIVKLLIAKGADVnahakgVFFNPKykhegfyfGETPLALAACTNQPEiVQLLMEKES 212
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 4-113 6.40e-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: 39.86  E-value: 6.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944   4 QDAVAALSERLLIAAYKgqTENVVQLINKGAKVAVTKhGRTPLHLAANKGHLSVVQILLKAGCDLDVQDDGD-------- 75
Cdd:cd21882    38 NDGVNEAIMLLLEAAPD--SGNPKELVNAPCTDEFYQ-GQTALHIAIENRNLNLVRLLVENGADVSARATGRffrkspgn 114

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1958777944  76 -----QTALHRATVVGNTEILTALIREG---CALDRQDKDGNTALH 113
Cdd:cd21882   115 lfyfgELPLSLAACTNQEEIVRLLLENGaqpAALEAQDSLGNTVLH 160
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 137-264 8.24e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 37.55  E-value: 8.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958777944 137 RNKAGNTALHLAC-----------QNSHSQSTRVLLLGgsradlKNNAGDTCLHVAARYNHL---SVVRLLLSAFCSVHE 202
Cdd:PHA02736   13 PDIEGENILHYLCrnggvtdllafKNAISDENRYLVLE------YNRHGKQCVHIVSNPDKAdpqEKLKLLMEWGADING 86

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958777944 203 KNQA-GDTALHVAAALNHKKVVKILL-EAGADTTLVNNAGQTPLETA-RYHDNPEVALLLTKAPQ 264
Cdd:PHA02736   87 KERVfGNTPLHIAVYTQNYELATWLCnQPGVNMEILNYAFKTPYYVAcERHDAKMMNILRAKGAQ 151
 
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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