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Conserved domains on  [gi|201066352|ref|NP_001128441|]
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ankyrin repeat domain-containing protein 6 [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 201066352   5 DAVAALSERLLIAAYKGQTENVVQLINKGAKV--AVTKHGRTPLHLAANKGHLSVVQILLKAGCDLDVQDDGDQTALHRA 82
Cdd:COG0666   48 ALADALGALLLLAAALAGDLLVALLLLAAGADinAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLA 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201066352  83 TVVGNTEILTALIREGCALDRQDKDGNTALHEAAWHGFSQSAKLLVKAGANVLARNKAGNTALHLACQNSHSQSTRVLLL 162
Cdd:COG0666  128 AYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLE 207

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201066352 163 GGSRADLKNNAGDTCLHVAARYNHLSVVRLLLSAFCSVHEKNQAGDTALHVAAALNHKKVVKILLEAGADTTLVNNAGQT 242
Cdd:COG0666  208 AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287


                 ..
gi 201066352 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 201066352 545 AGPGA---ASDSSSQVVRPKDKALnATAVPRHQQELLPSDCTGSGLRKVKAPAASRLGDQQTGSCVNRGTQTKKSARGGQ 621
Cdd:PLN02847 373 AGAGAllrPVSSSTQVVMKRAQNV-AQAVVRTRSSLSSWSCMGPRRRSVGSVANSKKEDLPEATHVTSSVNSESLVTEVK 451

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201066352 622 TKHRGQQPTASSPS-GQQPSAASSDARDASQALELTQYFFEAVSaQMEKWYE--RKIEEARSQASQKAQQDEATLKEHIR 698
Cdd:PLN02847 452 TTKSVEHKSESSSSdGSGHDDEEEEEPLLSEDRVITSSVEEEVT-EGELWYEleKELQRQETEVDAQAQEEEAAAAKEIT 530


                 ....*...
gi 201066352 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 201066352   5 DAVAALSERLLIAAYKGQTENVVQLINKGAKV--AVTKHGRTPLHLAANKGHLSVVQILLKAGCDLDVQDDGDQTALHRA 82
Cdd:COG0666   48 ALADALGALLLLAAALAGDLLVALLLLAAGADinAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLA 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201066352  83 TVVGNTEILTALIREGCALDRQDKDGNTALHEAAWHGFSQSAKLLVKAGANVLARNKAGNTALHLACQNSHSQSTRVLLL 162
Cdd:COG0666  128 AYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLE 207

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201066352 163 GGSRADLKNNAGDTCLHVAARYNHLSVVRLLLSAFCSVHEKNQAGDTALHVAAALNHKKVVKILLEAGADTTLVNNAGQT 242
Cdd:COG0666  208 AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287


                 ..
gi 201066352 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 201066352  29 LINKGAKV-AVTKHGRTPLHL-AANKGHLSVVQILLKAGCDLDVQDDGDQTALHR--ATVVGNTEILTALIREGCALDRQ 104
Cdd:PHA03095  69 LLEAGADVnAPERCGFTPLHLyLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNAL 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201066352 105 DKDGNTALHeaawhGFSQSA-------KLLVKAGANVLARNKAGNTALHLACQNSHSQST--RVLLLGGSRADLKNNAGD 175
Cdd:PHA03095 149 DLYGMTPLA-----VLLKSRnanvellRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRARivRELIRAGCDPAATDMLGN 223

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201066352 176 TCLHVAARYNHL--SVVRLLLSAFCSVHEKNQAGDTALHVAAALNHKKVVKILLEAGADTTLVNNAGQTPLETARYHDNP 253
Cdd:PHA03095 224 TPLHSMATGSSCkrSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNG 303

                        250
                 ....*....|...
gi 201066352 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 201066352   46 LHLAANKGHLSVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEILTALIrEGCALDRQDkDGNTALHEAAWHGFSQSAK 125
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 201066352  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 201066352 109 NTALHEAAWHGFSQSAK-LLVKAGANVLARNKAGNTALHLACQNSHSQSTRVLLLGGSRadLKNNA-------GDTCLHV 180
Cdd:cd22192   18 ESPLLLAAKENDVQAIKkLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPE--LVNEPmtsdlyqGETALHI 95

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 201066352 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 201066352    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 201066352   41 HGRTPLHLAANKGHLSVVQILLKAGCDLDVQDDGD--------------QTALHRATVVGNTEILTALIREGCALDRQDK 106
Cdd:TIGR00870 127 PGITALHLAAHRQNYEIVKLLLERGASVPARACGDffvksqgvdsfyhgESPLNAAACLGSPSIVALLSEDPADILTADS 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201066352  107 DGNTALHeaawhgfsqsakLLVkaganVLARNKAGNTALHLACQNShsqstrVLLLGGSRADLK------NNAGDTCLHV 180
Cdd:TIGR00870 207 LGNTLLH------------LLV-----MENEFKAEYEELSCQMYNF------ALSLLDKLRDSKelevilNHQGLTPLKL 263

                         170
                  ....*....|....
gi 201066352  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 201066352 545 AGPGA---ASDSSSQVVRPKDKALnATAVPRHQQELLPSDCTGSGLRKVKAPAASRLGDQQTGSCVNRGTQTKKSARGGQ 621
Cdd:PLN02847 373 AGAGAllrPVSSSTQVVMKRAQNV-AQAVVRTRSSLSSWSCMGPRRRSVGSVANSKKEDLPEATHVTSSVNSESLVTEVK 451

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201066352 622 TKHRGQQPTASSPS-GQQPSAASSDARDASQALELTQYFFEAVSaQMEKWYE--RKIEEARSQASQKAQQDEATLKEHIR 698
Cdd:PLN02847 452 TTKSVEHKSESSSSdGSGHDDEEEEEPLLSEDRVITSSVEEEVT-EGELWYEleKELQRQETEVDAQAQEEEAAAAKEIT 530


                 ....*...
gi 201066352 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 201066352   5 DAVAALSERLLIAAYKGQTENVVQLINKGAKV--AVTKHGRTPLHLAANKGHLSVVQILLKAGCDLDVQDDGDQTALHRA 82
Cdd:COG0666   48 ALADALGALLLLAAALAGDLLVALLLLAAGADinAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLA 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201066352  83 TVVGNTEILTALIREGCALDRQDKDGNTALHEAAWHGFSQSAKLLVKAGANVLARNKAGNTALHLACQNSHSQSTRVLLL 162
Cdd:COG0666  128 AYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLE 207

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201066352 163 GGSRADLKNNAGDTCLHVAARYNHLSVVRLLLSAFCSVHEKNQAGDTALHVAAALNHKKVVKILLEAGADTTLVNNAGQT 242
Cdd:COG0666  208 AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287


                 ..
gi 201066352 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 201066352   1 MSQQDAVAALSERLLIAAYKGQTENVVQLINKGAKVAVTKHGRTPLHLAANKGHLSVVQILLKAGCDLDVQDDGDQTALH 80
Cdd:COG0666   13 AALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLH 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201066352  81 RATVVGNTEILTALIREGCALDRQDKDGNTALHEAAWHGFSQSAKLLVKAGANVLARNKAGNTALHLACQNSHSQSTRVL 160
Cdd:COG0666   93 AAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLL 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201066352 161 LLGGSRADLKNNAGDTCLHVAARYNHLSVVRLLLSAFCSVHEKNQAGDTALHVAAALNHKKVVKILLEAGADTTLVNNAG 240
Cdd:COG0666  173 LEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDG 252

                        250       260
                 ....*....|....*....|..
gi 201066352 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 201066352  24 ENVVQLINKGAKVAVTKHGRTPLHLAANKGHLSVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEILTALIREGCALDR 103
Cdd:COG0666    3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201066352 104 QDKDGNTALHEAAWHGFSQSAKLLVKAGANVLARNKAGNTALHLACQNSHSQSTRVLLLGGSRADLKNNAGDTCLHVAAR 183
Cdd:COG0666   83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 201066352 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 201066352  55 LSVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEILTALIREGCALDRQDKDGNTALHEAAWHGFSQSAKLLVKAGANV 134
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201066352 135 LARNKAGNTALHLACQNSHSQSTRVLLLGGSRADLKNNAGDTCLHVAARYNHLSVVRLLLSAFCSVHEKNQAGDTALHVA 214
Cdd:COG0666   81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 201066352 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 201066352  29 LINKGAKV-AVTKHGRTPLHL-AANKGHLSVVQILLKAGCDLDVQDDGDQTALHR--ATVVGNTEILTALIREGCALDRQ 104
Cdd:PHA03095  69 LLEAGADVnAPERCGFTPLHLyLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNAL 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201066352 105 DKDGNTALHeaawhGFSQSA-------KLLVKAGANVLARNKAGNTALHLACQNSHSQST--RVLLLGGSRADLKNNAGD 175
Cdd:PHA03095 149 DLYGMTPLA-----VLLKSRnanvellRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRARivRELIRAGCDPAATDMLGN 223

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201066352 176 TCLHVAARYNHL--SVVRLLLSAFCSVHEKNQAGDTALHVAAALNHKKVVKILLEAGADTTLVNNAGQTPLETARYHDNP 253
Cdd:PHA03095 224 TPLHSMATGSSCkrSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNG 303

                        250
                 ....*....|...
gi 201066352 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 201066352  24 ENVVQLINKGAKVAVTK-HGRTPLHLAANKGH---LSVVQILLKAGCDLDVQDDGDQTALHRATVVGNTE-ILTALIREG 98
Cdd:PHA03095  28 EEVRRLLAAGADVNFRGeYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAG 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201066352  99 CALDRQDKDGNTALHeAAWHGFSQSAK---LLVKAGANVLARNKAGNTALH--LACQNSHSQSTRVLLLGGSRADLKNNA 173
Cdd:PHA03095 108 ADVNAKDKVGRTPLH-VYLSGFNINPKvirLLLRKGADVNALDLYGMTPLAvlLKSRNANVELLRLLIDAGADVYAVDDR 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201066352 174 GDTCLHVAARYNHLS--VVRLLLSAFCSVHEKNQAGDTALHVAAALNHKKVVKI--LLEAGADTTLVNNAGQTPLETARY 249
Cdd:PHA03095 187 FRSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAV 266

                        250
                 ....*....|...
gi 201066352 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 201066352   46 LHLAANKGHLSVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEILTALIrEGCALDRQDkDGNTALHEAAWHGFSQSAK 125
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 201066352  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 201066352  40 KHGRTPLHLAANKGHLSVVQILLKAGCDLDVQDDGDQTALHRATVVG-----NTEILTALIREGCALDRQDKDGNTALHE 114
Cdd:PHA03100  33 KKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKynltdVKEIVKLLLEYGANVNAPDNNGITPLLY 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201066352 115 AAWHGFSQSA--KLLVKAGANVLARNKAGNTALHLACQNSHSQS--TRVLLLGGSRADLKNNagdtclhvaarynhlsvV 190
Cdd:PHA03100 113 AISKKSNSYSivEYLLDNGANVNIKNSDGENLLHLYLESNKIDLkiLKLLIDKGVDINAKNR-----------------V 175

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 201066352 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 201066352  145 LHLACQNSHSQSTRVLLLGGSRADLKNNAGDTCLHVAARYNHLSVVRLLLSAFCSvhEKNQAGDTALHVAAALNHKKVVK 224
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 201066352  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 201066352  19 YKGQTENVVQ-LINKGAKV-AVTKHGRTPLHL-AANKG-HLSVVQILLKAGCDLDVQDDGDQTALH------RATVvgnt 88
Cdd:PHA03095  92 YNATTLDVIKlLIKAGADVnAKDKVGRTPLHVyLSGFNiNPKVIRLLLRKGADVNALDLYGMTPLAvllksrNANV---- 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201066352  89 EILTALIREGCALDRQDKDGNTALHEaawhgFSQSAK-------LLVKAGANVLARNKAGNTALHLACQNSHSQSTRV-- 159
Cdd:PHA03095 168 ELLRLLIDAGADVYAVDDRFRSLLHH-----HLQSFKprarivrELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlp 242

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201066352 160 LLLGGSRADLKNNAGDTCLHVAARYNHLSVVRLLLSAFCSVHEKNQAGDTALHVAAALNHKKVVKILLE--------AGA 231
Cdd:PHA03095 243 LLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAknpsaetvAAT 322

                        250
                 ....*....|....*..
gi 201066352 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 201066352  57 VVQILLKAGCDLDVQDDGDQTALHRATVVGNTEILTALIREGCALDRQDKDGNTALHEAAWHGFSQSAKLLVKAGANVLA 136
Cdd:PHA02874 106 MIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANV 185

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201066352 137 RNKAGNTALHLACQNSHSQSTRVLLLGGSRADLKNNAGDTCLHVAARYNHlSVVRLLLSAfCSVHEKNQAGDTALHvaAA 216
Cdd:PHA02874 186 KDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLINN-ASINDQDIDGSTPLH--HA 261

                        170       180       190
                 ....*....|....*....|....*....|....
gi 201066352 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 201066352  112 LHEAAWHGFSQSAKLLVKAGANVLARNKAGNTALHLACQNSHSQSTRvLLLGGSRADLKNNaGDTCLHVAARYNHLSVVR 191
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVK-LLLEHADVNLKDN-GRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 201066352  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 201066352   14 LLIAAYKGQTENVVQLINKGAKV-AVTKHGRTPLHLAANKGHLSVVQILLKaGCDLDVQDDGdQTALHRATVVGNTEILT 92
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADAnLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDNG-RTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 201066352   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 201066352  88 TEILTALIREGCALDRQDKD-GNTALHEAAWHGFSQSAKLLVKAGANVLARNKAGNTALHLACQNSHSQSTRVLLLGGSR 166
Cdd:PHA02878 147 AEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAS 226

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201066352 167 ADLKNNAGDTCLHVAARY-NHLSVVRLLLSAFCSVHEKNQA-GDTALHVAaaLNHKKVVKILLEAGADTTLVNNAGQTPL 244
Cdd:PHA02878 227 TDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYIlGLTALHSS--IKSERKLKLLLEYGADINSLNSYKLTPL 304


                 ...
gi 201066352 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 201066352  26 VVQLINKGAKVAV-TKHGRTPLHLAANKGH-----LSVVQILLKAGCDLDVQDDGDQTALHRA--TVVGNTEILTALIRE 97
Cdd:PHA03100  51 VKILLDNGADINSsTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVNAPDNNGITPLLYAisKKSNSYSIVEYLLDN 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201066352  98 GCALDRQDKDGNTALHEAAWHGFSQS--AKLLVKAGANV----------------LARNKAGNTALHLACQNSHSQSTRV 159
Cdd:PHA03100 131 GANVNIKNSDGENLLHLYLESNKIDLkiLKLLIDKGVDInaknrvnyllsygvpiNIKDVYGFTPLHYAVYNNNPEFVKY 210

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 201066352 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 201066352  178 LHVAARYNHLSVVRLLLSAFCSVHEKNQAGDTALHVAAALNHKKVVKILLEaGADTTLVNNaGQTPLETARYHDNPEVAL 257
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIVK 78


                  ..
gi 201066352  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 201066352  10 LSERLLIAAYKGQTENVVQLI-NKGAKVAVT-KHGRTPLHLAANKGHLSVVQILLKAGCDLDVQDDGDQTALHRATVVGN 87
Cdd:PHA02874   1 ASQDLRMCIYSGDIEAIEKIIkNKGNCINISvDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201066352  88 TEILTALIREGC---ALDRQDKDGNTAlheaawhgfsqsaKLLVKAGANVLARNKAGNTALHLACQNSHSQSTRVLLLGG 164
Cdd:PHA02874  81 HDIIKLLIDNGVdtsILPIPCIEKDMI-------------KTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYG 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201066352 165 SRADLKNNAGDTCLHVAARYNHLSVVRLLLSAFCSVHEKNQAGDTALHVAAALNHKKVVKILLEAGADTTLVNNAGQTPL 244
Cdd:PHA02874 148 ADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPL 227

                        250
                 ....*....|....*...
gi 201066352 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 201066352  14 LLIAAYKGQTENVVQLINKGAKV-AVTKHGRTPLHLAANKGHLS-VVQILLKAGCDLDVQDDGDQTALHRATVVG-NTEI 90
Cdd:PHA02876 244 LLKAIRNEDLETSLLLYDAGFSVnSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMAKNGyDTEN 323

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201066352  91 LTALIREGCALDRQDKDGNTALHEAA-WHGFSQSAKLLVKAGANVLARNKAGNTALHLACQNSHSQSTRVLLLGGSRADL 169
Cdd:PHA02876 324 IRTLIMLGADVNAADRLYITPLHQAStLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEA 403

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201066352 170 KNNAGDTCLHVA-ARYNHLSVVRLLLSAFCSVHEKNQAGDTALHVAAALNHK-KVVKILLEAGADTTLVNNAGQTPLETA 247
Cdd:PHA02876 404 LSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNCKlDVIEMLLDNGADVNAINIQNQYPLLIA 483


                 ....
gi 201066352 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 201066352  29 LINKGAKV-AVTKHGRTPLHLAANKGHLSVVQILLKAGCDLDVQDDGDQTALHRAT------------------------ 83
Cdd:PHA02876 164 LLEGGADVnAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVdsknidtikaiidnrsninkndls 243

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201066352  84 ---VVGNTEILTALI--REGCALDRQDKDGNTALHEAAWH-GFSQSAKLLVKAGANVLARNKAGNTALHLACQNSH-SQS 156
Cdd:PHA02876 244 llkAIRNEDLETSLLlyDAGFSVNSIDDCKNTPLHHASQApSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTEN 323

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201066352 157 TRVLLLGGSRADLKNNAGDTCLHVAA---RYNHLSVVRLLLSAfcSVHEKNQAGDTALHVAAALNHKKVVKILLEAGADT 233
Cdd:PHA02876 324 IRTLIMLGADVNAADRLYITPLHQAStldRNKDIVITLLELGA--NVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADI 401

                        250       260
                 ....*....|....*....|
gi 201066352 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 201066352  42 GRTPLHLAANKGHLSVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEILTALIREGCALDRQdkDGNTALHEAAWHGFS 121
Cdd:PLN03192 558 GRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPH--AAGDLLCTAAKRNDL 635

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 201066352 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 201066352  42 GRTPLHLAANKGHLSVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEILTALIREGC-ALDRQDKDGNTALHEAAWHGF 120
Cdd:PHA02875  35 GISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKfADDVFYKDGMTPLHLATILKK 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201066352 121 SQSAKLLVKAGANVLARNKAGNTALHLACQNSHSQSTRVLLLGGSRADLKNNAGDTCLHVAARYNHLSVVRLLLSAFCSV 200
Cdd:PHA02875 115 LDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANI 194

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 201066352 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 201066352  22 QTENVVQLINKGAKV-AVTKH-GRTPLHLAANKGHLSVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEILTALIREGC 99
Cdd:PHA02878 146 EAEITKLLLSYGADInMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA 225

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201066352 100 ALDRQDKDGNTALHEAAWHGFSQSA-KLLVKAGANVLARNKA-GNTALHLACQNshSQSTRVLLLGGSRADLKNNAGDTC 177
Cdd:PHA02878 226 STDARDKCGNTPLHISVGYCKDYDIlKLLLEHGVDVNAKSYIlGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTP 303

                        170       180
                 ....*....|....*....|..
gi 201066352 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 201066352  49 AANKGHLSVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEILTALIREGCALDRQDKDGNTALHEAawhgfsqsakllV 128
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNA------------I 599

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201066352 129 KAGanvlaRNKAGNTALHLAcqnshsqstrvlllggsRADLKNNAGDTcLHVAARYNHLSVVRLLLSAFCSVHEKNQAGD 208
Cdd:PLN03192 600 SAK-----HHKIFRILYHFA-----------------SISDPHAAGDL-LCTAAKRNDLTAMKELLKQGLNVDSEDHQGA 656

                        170       180
                 ....*....|....*....|....*....
gi 201066352 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 201066352  15 LIAAYKGQTENVVQLINKGAKV-AVTKHGRTPLHLAAN-KGHLSVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEILT 92
Cdd:PHA02876 313 LMAKNGYDTENIRTLIMLGADVnAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIIN 392

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201066352  93 ALIREGCALDRQDKDGNTALHeAAWHGFS--QSAKLLVKAGANVLARNKAGNTALHLACQ-NSHSQSTRVLLLGGSRADL 169
Cdd:PHA02876 393 TLLDYGADIEALSQKIGTALH-FALCGTNpyMSVKTLIDRGANVNSKNKDLSTPLHYACKkNCKLDVIEMLLDNGADVNA 471

                        170       180
                 ....*....|....*....|....*
gi 201066352 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 201066352  17 AAYKGQTENVVQLI--NKGAKVAVTKHGRTPLHLAANKGHLSVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEILTAL 94
Cdd:PHA02875  75 AVEEGDVKAVEELLdlGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELL 154

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 201066352  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 201066352   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 201066352  55 LSVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEILTALIREG---------------CALDRQDKD------------ 107
Cdd:PHA02876 158 LLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGadvniialddlsvleCAVDSKNIDtikaiidnrsni 237

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201066352 108 --GNTALHEAAWHGFSQSAKLLVKAGANVLARNKAGNTALHLACQN-SHSQSTRVLLLGGSRADLKNNAGDTCLHVAARY 184
Cdd:PHA02876 238 nkNDLSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQApSLSRLVPKLLERGADVNAKNIKGETPLYLMAKN 317

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201066352 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 201066352 109 NTALHEAAWHGFSQSAK-LLVKAGANVLARNKAGNTALHLACQNSHSQSTRVLLLGGSRadLKNNA-------GDTCLHV 180
Cdd:cd22192   18 ESPLLLAAKENDVQAIKkLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPE--LVNEPmtsdlyqGETALHI 95

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 201066352 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 201066352  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 201066352  13 RLLIAAYKGQTENVVQLINKGAKvavTKHGRT--------PLHLAANKGHLSVVQILLKAGCDLDVQDDGDQTALHRATV 84
Cdd:PHA02878   3 KLYKSMYTDNYETILKYIEYIDH---TENYSTsaslipfiPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201066352  85 VGNTEILTALIREgcalDRQDKDGNT--ALHEAAWHGFSQSAKLLVkaganvLARNKAGNTA-LHLACQNSHSQS----- 156
Cdd:PHA02878  80 EPNKLGMKEMIRS----INKCSVFYTlvAIKDAFNNRNVEIFKIIL------TNRYKNIQTIdLVYIDKKSKDDIieaei 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201066352 157 TRVLLLGGSRADLKN-NAGDTCLHVAARYNHLSVVRLLLSAFCSVHEKNQAGDTALHVAAALNHKKVVKILLEAGADTTL 235
Cdd:PHA02878 150 TKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDA 229

                        250
                 ....*....|..
gi 201066352 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 201066352 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 201066352   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 201066352  11 SERLLIAAYKgqtENVVQLINKGAKVAVTK------HGRTPLHLAANKGHLSVVQILLKAGCDL-DVQDDGD----QTAL 79
Cdd:cd22192   17 SESPLLLAAK---ENDVQAIKKLLKCPSCDlfqrgaLGETALHVAALYDNLEAAVVLMEAAPELvNEPMTSDlyqgETAL 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201066352  80 HRATVVGNTEILTALIREG-----------CALDRQDKD---GNTALHEAAWHGFSQSAKLLVKAGANVLARNKAGNTAL 145
Cdd:cd22192   94 HIAVVNQNLNLVRELIARGadvvspratgtFFRPGPKNLiyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 201066352 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 201066352  53 GHLSVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEILTALIREGCALDRQDKDGNTALHEAAWHGFSQSAKLLVKAGA 132
Cdd:PHA02875  13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGK 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201066352 133 ---NVLArnKAGNTALHLACQNSHSQSTRVLLLGGSRADLKNNAGDTCLHVAARYNHLSVVRLLLSAFCSVHEKNQAGDT 209
Cdd:PHA02875  93 fadDVFY--KDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCT 170

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 201066352 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 201066352   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 201066352  44 TPLHLAANKGHLSVVQILLK-AGCDLDVQDDGDQTALHRATVVGNTEILTALIREGCALDRQDK-----DGNTALHEAAW 117
Cdd:cd22192   19 SPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEPMtsdlyQGETALHIAVV 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201066352 118 HGFSQSAKLLVKAGANVlARNKAGNTALHLacqnshsqstrvlllggsRADLKNNAGDTCLHVAARYNHLSVVRLLLSAF 197
Cdd:cd22192   99 NQNLNLVRELIARGADV-VSPRATGTFFRP------------------GPKNLIYYGEHPLSFAACVGNEEIVRLLIEHG 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 201066352 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 201066352  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 201066352  57 VVQILLKAGCDLDVQDDGDQTALHRATVVGN--TEILTALIREGCALDRQDKDGNTALHEAAWHGFSQSAKLlVKAGANV 134
Cdd:PHA02716 194 ILEWLCNNGVNVNLQNNHLITPLHTYLITGNvcASVIKKIIELGGDMDMKCVNGMSPIMTYIINIDNINPEI-TNIYIES 272

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201066352 135 LARNKAGNTA--LHLACQNSHSQSTRVL---LLGGSRADLKNNAGDTCLH--VAARYNHLSVVRLLLSAFCSVHEKNQAG 207
Cdd:PHA02716 273 LDGNKVKNIPmiLHSYITLARNIDISVVysfLQPGVKLHYKDSAGRTCLHqyILRHNISTDIIKLLHEYGNDLNEPDNIG 352

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 201066352 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 201066352  75 DQTALHRATVVGNTEILTALIREGCALDRQDKDGNTALHEAAWHGFSQSAKLLVKAGANVLARNKAGNTALHLACQNSHS 154
Cdd:PHA02875   2 DQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201066352 155 QSTRVLLLGGSRA-DLKNNAGDTCLHVAARYNHLSVVRLLLSAFCSVHEKNQAGDTALHVAAALNHKKVVKILLEAGADT 233
Cdd:PHA02875  82 KAVEELLDLGKFAdDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACL 161

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 201066352 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 201066352  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 201066352  71 QDDGDQTALHRATVvgnteiltalirEGCALdrqdkdgntalheaAWHGFSQSAKLLVKAGANVLARNKAGNTALHLACQ 150
Cdd:PTZ00322  71 EEVIDPVVAHMLTV------------ELCQL--------------AASGDAVGARILLTGGADPNCRDYDGRTPLHIACA 124

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 201066352 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 201066352  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 201066352 175 DTCLHVAARYNHL-SVVRLLLSAFCSVHEKNQAGDTALHVAAALNHKKVVKILLEagADTTLVNNA-------GQTPLET 246
Cdd:cd22192   18 ESPLLLAAKENDVqAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPELVNEPmtsdlyqGETALHI 95


                 .
gi 201066352 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 201066352    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 201066352  41 HGRTPLHLAANKGHLSVVQILLKAGCDLDVQDDgdQTALHRATVVGNTEILTALIREGCALDRQDKDGNTALHEAAWHGF 120
Cdd:PHA02791  29 HGHSALYYAIADNNVRLVCTLLNAGALKNLLEN--EFPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDSGN 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201066352 121 SQSAKLLVKAGANVLARNKAG--NTALHLACQNSHSQSTRVLLLGGSRADLKNNAgdTCLHVAARYNHLSVVRLLLSAFC 198
Cdd:PHA02791 107 MQTVKLFVKKNWRLMFYGKTGwkTSFYHAVMLNDVSIVSYFLSEIPSTFDLAILL--SCIHITIKNGHVDMMILLLDYMT 184


                 ....*.
gi 201066352 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 201066352  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 201066352   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 201066352  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 201066352  79 LHRATVVGNTEILTALIREGCALDRQDKDGNTALHEAAWHGFSQSAKLLVKaganVLARNKAGNT--ALHLACQNSHSQS 156
Cdd:PHA02878  41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIR----SINKCSVFYTlvAIKDAFNNRNVEI 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201066352 157 TRVLLLGGSRADLKNNAGDTCLHVAARYNHLSVVRLLLSAFCSVHEKNQ-AGDTALHVAAALNHKKVVKILLEAGADTTL 235
Cdd:PHA02878 117 FKIILTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNI 196

                        170       180
                 ....*....|....*....|....*
gi 201066352 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 201066352  10 LSERLLIAAYKGQTENVVQLINKGAKV-AVTKHGRTPLHLAANKGHLSVVQILLKAGCDLDVQDDGDQTALHRATVVGNT 88
Cdd:PTZ00322  82 LTVELCQLAASGDAVGARILLTGGADPnCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFR 161


                 ....*...
gi 201066352  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 201066352  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 201066352   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 201066352  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 201066352  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 201066352  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 201066352  29 LINKGAKV-AVTKH-GRTPLH--LAANKG-HLSVVQILLKAGCDLDVQDDGDQTALHR--ATVVGNTEILTALIREGCAL 101
Cdd:PHA02859  72 LIENGADVnFKTRDnNLSALHhyLSFNKNvEPEILKILIDSGSSITEEDEDGKNLLHMymCNFNVRINVIKLLIDSGVSF 151

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 201066352 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 201066352   41 HGRTPLHLAANKGHLSVVQILLKAGCDLDVQDDGD--------------QTALHRATVVGNTEILTALIREGCALDRQDK 106
Cdd:TIGR00870 127 PGITALHLAAHRQNYEIVKLLLERGASVPARACGDffvksqgvdsfyhgESPLNAAACLGSPSIVALLSEDPADILTADS 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201066352  107 DGNTALHeaawhgfsqsakLLVkaganVLARNKAGNTALHLACQNShsqstrVLLLGGSRADLK------NNAGDTCLHV 180
Cdd:TIGR00870 207 LGNTLLH------------LLV-----MENEFKAEYEELSCQMYNF------ALSLLDKLRDSKelevilNHQGLTPLKL 263

                         170
                  ....*....|....
gi 201066352  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 201066352   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 201066352  47 HLAANkGHLSVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEILTALIREGCALDRQDKDGNTALHEAAWHGFSQSAKL 126
Cdd:PTZ00322  88 QLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                 .
gi 201066352 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 201066352   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 201066352  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 201066352 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 201066352  145 LHLACQNSHSQSTRVLLLGGSRADLknnaGDTCLHvAARYNHLSVVRLLLSAFCSVHEKN--------------QAGDTA 210
Cdd:TIGR00870  57 FVAAIENENLELTELLLNLSCRGAV----GDTLLH-AISLEYVDAVEAILLHLLAAFRKSgplelandqytsefTPGITA 131

                          90       100
                  ....*....|....*....|..
gi 201066352  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 201066352 125 KLLVKAGANVLARNKAGN-TALHLAC---QNSHSQSTRVLLLGGSRADLKNNAGDTCLHV-AARYN-HLSVVRLLLSAFC 198
Cdd:PHA02859  70 KFLIENGADVNFKTRDNNlSALHHYLsfnKNVEPEILKILIDSGSSITEEDEDGKNLLHMyMCNFNvRINVIKLLIDSGV 149

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 201066352 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 201066352  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 201066352  42 GRTPLHLAANKGHLSVVQILLKAGCDLDVQDDGD--------------QTALHRATVVGNTEILTaLIREGCALD--RQD 105
Cdd:cd22194  141 GQTALNIAIERRQGDIVKLLIAKGADVNAHAKGVffnpkykhegfyfgETPLALAACTNQPEIVQ-LLMEKESTDitSQD 219

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 201066352 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 201066352   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 201066352 545 AGPGA---ASDSSSQVVRPKDKALnATAVPRHQQELLPSDCTGSGLRKVKAPAASRLGDQQTGSCVNRGTQTKKSARGGQ 621
Cdd:PLN02847 373 AGAGAllrPVSSSTQVVMKRAQNV-AQAVVRTRSSLSSWSCMGPRRRSVGSVANSKKEDLPEATHVTSSVNSESLVTEVK 451

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 201066352 622 TKHRGQQPTASSPS-GQQPSAASSDARDASQALELTQYFFEAVSaQMEKWYE--RKIEEARSQASQKAQQDEATLKEHIR 698
Cdd:PLN02847 452 TTKSVEHKSESSSSdGSGHDDEEEEEPLLSEDRVITSSVEEEVT-EGELWYEleKELQRQETEVDAQAQEEEAAAAKEIT 530


                 ....*...
gi 201066352 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 201066352 171 NNAGDTCLHVAARYNH----LSVVRLLLSAFCSVHEKNQA-GDTALHVAA-ALNHKKVVKILLEAGADTTLVNNAGQTPL 244
Cdd:PHA02741  57 DDAGQMCIHIAAEKHEaqlaAEIIDHLIELGADINAQEMLeGDTALHLAAhRRDHDLAEWLCCQPGIDLHFCNADNKSPF 136

                         90       100
                 ....*....|....*....|...
gi 201066352 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 201066352  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 201066352 137 RNKAGNTALHLACQNSHSQ--STRVLLL-----GGSRADLKNNA-------GDTCLHVAARYNHLSVVRLLLSAFCSVH- 201
Cdd:cd21882   22 RGATGKTCLHKAALNLNDGvnEAIMLLLeaapdSGNPKELVNAPctdefyqGQTALHIAIENRNLNLVRLLVENGADVSa 101

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 201066352 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 201066352 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 201066352   4 QDAVAALSERLLIAAYKgqTENVVQLINKGAKVAVTKhGRTPLHLAANKGHLSVVQILLKAGCDLDVQDDGD-------- 75
Cdd:cd21882   38 NDGVNEAIMLLLEAAPD--SGNPKELVNAPCTDEFYQ-GQTALHIAIENRNLNLVRLLVENGADVSARATGRffrkspgn 114

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 201066352  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 201066352 137 RNKAGNTALHLAC-----------QNSHSQSTRVLLLGgsradlKNNAGDTCLHVAARYNHL---SVVRLLLSAFCSVHE 202
Cdd:PHA02736  13 PDIEGENILHYLCrnggvtdllafKNAISDENRYLVLE------YNRHGKQCVHIVSNPDKAdpqEKLKLLMEWGADING 86

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 201066352 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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