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Conserved domains on  [gi|206729919|sp|O00221|]
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RecName: Full=NF-kappa-B inhibitor epsilon; Short=NF-kappa-BIE; AltName: Full=I-kappa-B-epsilon; Short=IkB-E; Short=IkB-epsilon; Short=IkappaBepsilon

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];
249-496 4.73e-36

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 135.47  E-value: 4.73e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729919 249 LEALTYISEDGDTLVHLAVIHEAPAVLLCCLALLPQEVLDIQNNLYQTALHLAVHLDQPGAVRALVLKGASRALQDRHGD 328
Cdd:COG0666   42 LALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGE 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729919 329 TALHVACQRQHLACARCLLEgrpepgrgtsHSLDLQLQNWQGLACLHIATLQKNQPLMELLLRNGADIDVQEGtSGKTAL 408
Cdd:COG0666  122 TPLHLAAYNGNLEIVKLLLE----------AGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDN-DGETPL 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729919 409 HLAVETQERGLVQFLLQAGAQVDARMLNGCTPLHLAAGRGLMGISSTLCKAGADSLLRNVEDETPQDLTEESLVLLPFDD 488
Cdd:COG0666  191 HLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKL 270


                 ....*...
gi 206729919 489 LKISGKLL 496
Cdd:COG0666  271 LLLALLLL 278
PTZ00249 super family cl25531
variable surface protein Vir28; Provisional
 77-229 7.00e-06

variable surface protein Vir28; Provisional


The actual alignment was detected with superfamily member PTZ00249:

Pssm-ID: 140276 [Multi-domain]  Cd Length: 516  Bit Score: 48.49  E-value: 7.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729919  77 TWPALRTLSSLRAGP-----SEPHSPGRRP--PRAGRPLCQADPQ-----PGKAARRSLEPDPAQTG--------PRPAR 136
Cdd:PTZ00249 226 TAHAHRRISGEARPPkhisfSSPHAHGRPPveTRPPNPVSVSSPQahgrhPGETHTPPLVTVPSSKAhdrnpvqtPTPTS 305

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729919 137 AAGMSEARKGPDEAE--ESQYDSGIESLRSLRSLPESTSAPASGPSD----------GSPQPCTHPPGPVKEPQEKEDAD 204
Cdd:PTZ00249 306 VSGYSSQAKGLEKQAggESERTSSVPSEQFPLPLPVLLPLGQSGPLEsseseetdeyAGPKGLPEPELELVELQEEDQRH 385

                        170       180
                 ....*....|....*....|....*
gi 206729919 205 GERADSTYGSSSLTYTLSLLGGPEA 229
Cdd:PTZ00249 386 GLKHDVDTFREDEEDTFLQEGDQPA 410
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
249-496 4.73e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 135.47  E-value: 4.73e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729919 249 LEALTYISEDGDTLVHLAVIHEAPAVLLCCLALLPQEVLDIQNNLYQTALHLAVHLDQPGAVRALVLKGASRALQDRHGD 328
Cdd:COG0666   42 LALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGE 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729919 329 TALHVACQRQHLACARCLLEgrpepgrgtsHSLDLQLQNWQGLACLHIATLQKNQPLMELLLRNGADIDVQEGtSGKTAL 408
Cdd:COG0666  122 TPLHLAAYNGNLEIVKLLLE----------AGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDN-DGETPL 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729919 409 HLAVETQERGLVQFLLQAGAQVDARMLNGCTPLHLAAGRGLMGISSTLCKAGADSLLRNVEDETPQDLTEESLVLLPFDD 488
Cdd:COG0666  191 HLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKL 270


                 ....*...
gi 206729919 489 LKISGKLL 496
Cdd:COG0666  271 LLLALLLL 278
Ank_2 pfam12796
Ankyrin repeats (3 copies);
374-462 3.23e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 68.22  E-value: 3.23e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729919  374 LHIATLQKNQPLMELLLRNGADIDVQEgTSGKTALHLAVETQERGLVQFLLQagaQVDARM-LNGCTPLHLAAGRGLMGI 452
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQD-KNGRTALHLAAKNGHLEIVKLLLE---HADVNLkDNGRTALHYAARSGHLEI 76

                          90
                  ....*....|
gi 206729919  453 SSTLCKAGAD 462
Cdd:pfam12796  77 VKLLLEKGAD 86
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 283-443 3.35e-10

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: 62.34  E-value: 3.35e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729919 283 PQEVLDIQNNLYQ-----TALHLAVHLDQPGAVRALvLKGASRALQDR--HGDTALHVACQRQHLACARCLLEGRPEpgr 355
Cdd:cd22192    1 WAQMLDELHLLQQkriseSPLLLAAKENDVQAIKKL-LKCPSCDLFQRgaLGETALHVAALYDNLEAAVVLMEAAPE--- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729919 356 gtshsldlqLQN-------WQGLACLHIATLQKNQPLMELLLRNGADIDVQEGTS-------------GKTALHLAVETQ 415
Cdd:cd22192   77 ---------LVNepmtsdlYQGETALHIAVVNQNLNLVRELIARGADVVSPRATGtffrpgpknliyyGEHPLSFAACVG 147

                        170       180
                 ....*....|....*....|....*...
gi 206729919 416 ERGLVQFLLQAGAQVDARMLNGCTPLHL 443
Cdd:cd22192  148 NEEIVRLLIEHGADIRAQDSLGNTVLHI 175
PHA03095 PHA03095
ankyrin-like protein; Provisional
 310-470 4.87e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 61.58  E-value: 4.87e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729919 310 VRALVLKGASRALQDRHGDTALHVACQRQHLACA---RCLLEGrpepgrgtshSLDLQLQNWQGLACLHIATLQKNQ-PL 385
Cdd:PHA03095  30 VRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKdivRLLLEA----------GADVNAPERCGFTPLHLYLYNATTlDV 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729919 386 MELLLRNGADIDVqEGTSGKTALH--LAVETQERGLVQFLLQAGAQVDARMLNGCTPLH--LAAGRGLMGISSTLCKAGA 461
Cdd:PHA03095 100 IKLLIKAGADVNA-KDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAvlLKSRNANVELLRLLIDAGA 178


                 ....*....
gi 206729919 462 DslLRNVED 470
Cdd:PHA03095 179 D--VYAVDD 185
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 259-453 3.55e-06

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: 49.69  E-value: 3.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729919  259 GDTLVHLAVIHE--------APAVLLCCLALLPQEVLDIQNNLY---QTALHLAVHLDQPGAVRALVLKGASralqdrhg 327
Cdd:TIGR00870  82 GDTLLHAISLEYvdaveailLHLLAAFRKSGPLELANDQYTSEFtpgITALHLAAHRQNYEIVKLLLERGAS-------- 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729919  328 dtaLHVACQrqhlaCARCLLEGRPEPGRGTSHSLDLqlqnwqgLACLhiatlqKNQPLMELLLRNGADIDVQEgTSGKTA 407
Cdd:TIGR00870 154 ---VPARAC-----GDFFVKSQGVDSFYHGESPLNA-------AACL------GSPSIVALLSEDPADILTAD-SLGNTL 211

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 206729919  408 LHLAVETQE---------RGLVQFLLQAGAQVDAR-----MLN--GCTPLHLAAGRGLMGIS 453
Cdd:TIGR00870 212 LHLLVMENEfkaeyeelsCQMYNFALSLLDKLRDSkelevILNhqGLTPLKLAAKEGRIVLF 273
PTZ00249 PTZ00249
variable surface protein Vir28; Provisional
 77-229 7.00e-06

variable surface protein Vir28; Provisional


Pssm-ID: 140276 [Multi-domain]  Cd Length: 516  Bit Score: 48.49  E-value: 7.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729919  77 TWPALRTLSSLRAGP-----SEPHSPGRRP--PRAGRPLCQADPQ-----PGKAARRSLEPDPAQTG--------PRPAR 136
Cdd:PTZ00249 226 TAHAHRRISGEARPPkhisfSSPHAHGRPPveTRPPNPVSVSSPQahgrhPGETHTPPLVTVPSSKAhdrnpvqtPTPTS 305

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729919 137 AAGMSEARKGPDEAE--ESQYDSGIESLRSLRSLPESTSAPASGPSD----------GSPQPCTHPPGPVKEPQEKEDAD 204
Cdd:PTZ00249 306 VSGYSSQAKGLEKQAggESERTSSVPSEQFPLPLPVLLPLGQSGPLEsseseetdeyAGPKGLPEPELELVELQEEDQRH 385

                        170       180
                 ....*....|....*....|....*
gi 206729919 205 GERADSTYGSSSLTYTLSLLGGPEA 229
Cdd:PTZ00249 386 GLKHDVDTFREDEEDTFLQEGDQPA 410
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 326-348 6.02e-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: 34.49  E-value: 6.02e-03
                           10        20
                   ....*....|....*....|...
gi 206729919   326 HGDTALHVACQRQHLACARCLLE 348
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLD 23
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
249-496 4.73e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 135.47  E-value: 4.73e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729919 249 LEALTYISEDGDTLVHLAVIHEAPAVLLCCLALLPQEVLDIQNNLYQTALHLAVHLDQPGAVRALVLKGASRALQDRHGD 328
Cdd:COG0666   42 LALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGE 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729919 329 TALHVACQRQHLACARCLLEgrpepgrgtsHSLDLQLQNWQGLACLHIATLQKNQPLMELLLRNGADIDVQEGtSGKTAL 408
Cdd:COG0666  122 TPLHLAAYNGNLEIVKLLLE----------AGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDN-DGETPL 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729919 409 HLAVETQERGLVQFLLQAGAQVDARMLNGCTPLHLAAGRGLMGISSTLCKAGADSLLRNVEDETPQDLTEESLVLLPFDD 488
Cdd:COG0666  191 HLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKL 270


                 ....*...
gi 206729919 489 LKISGKLL 496
Cdd:COG0666  271 LLLALLLL 278
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
249-476 1.70e-31

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 122.76  E-value: 1.70e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729919 249 LEALTYISEDGDTLVHLAVIHEAPAVLLCCLALLPQEVLDIQNNLYQTALHLAVHLDQPGAVRALVLKGASRALQDRHGD 328
Cdd:COG0666    9 LLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGN 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729919 329 TALHVACQRQHLACARCLLEgrpepgrgtsHSLDLQLQNWQGLACLHIATLQKNQPLMELLLRNGADIDVQeGTSGKTAL 408
Cdd:COG0666   89 TLLHAAARNGDLEIVKLLLE----------AGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQ-DNDGNTPL 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 206729919 409 HLAVETQERGLVQFLLQAGAQVDARMLNGCTPLHLAAGRGLMGISSTLCKAGADSLLRNVEDETPQDL 476
Cdd:COG0666  158 HLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDL 225
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
287-472 1.05e-29

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 117.75  E-value: 1.05e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729919 287 LDIQNNLYQTALHLAVHLDQPGAVRALVLKGASRALQDRHGDTALHVACQRQHLACARCLLEgrpepgrgtsHSLDLQLQ 366
Cdd:COG0666  113 VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLE----------AGADVNAR 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729919 367 NWQGLACLHIATLQKNQPLMELLLRNGADIDVQEgTSGKTALHLAVETQERGLVQFLLQAGAQVDARMLNGCTPLHLAAG 446
Cdd:COG0666  183 DNDGETPLHLAAENGHLEIVKLLLEAGADVNAKD-NDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAA 261

                        170       180
                 ....*....|....*....|....*.
gi 206729919 447 RGLMGISSTLCKAGADSLLRNVEDET 472
Cdd:COG0666  262 AGAALIVKLLLLALLLLAAALLDLLT 287
Ank_2 pfam12796
Ankyrin repeats (3 copies);
374-462 3.23e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 68.22  E-value: 3.23e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729919  374 LHIATLQKNQPLMELLLRNGADIDVQEgTSGKTALHLAVETQERGLVQFLLQagaQVDARM-LNGCTPLHLAAGRGLMGI 452
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQD-KNGRTALHLAAKNGHLEIVKLLLE---HADVNLkDNGRTALHYAARSGHLEI 76

                          90
                  ....*....|
gi 206729919  453 SSTLCKAGAD 462
Cdd:pfam12796  77 VKLLLEKGAD 86
Ank_2 pfam12796
Ankyrin repeats (3 copies);
298-399 3.81e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.83  E-value: 3.81e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729919  298 LHLAVHLDQPGAVRALVLKGASRALQDRHGDTALHVACQRQHLACARCLLEgrpepgrgtshSLDLQLQNwQGLACLHIA 377
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-----------HADVNLKD-NGRTALHYA 68

                          90       100
                  ....*....|....*....|..
gi 206729919  378 TLQKNQPLMELLLRNGADIDVQ 399
Cdd:pfam12796  69 ARSGHLEIVKLLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
331-433 4.80e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 64.75  E-value: 4.80e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729919  331 LHVACQRQHLACARCLLEGRPEPGrgtshsldlqLQNWQGLACLHIATLQKNQPLMELLLRNgadIDVQEGTSGKTALHL 410
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADAN----------LQDKNGRTALHLAAKNGHLEIVKLLLEH---ADVNLKDNGRTALHY 67

                          90       100
                  ....*....|....*....|...
gi 206729919  411 AVETQERGLVQFLLQAGAQVDAR 433
Cdd:pfam12796  68 AARSGHLEIVKLLLEKGADINVK 90
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 283-443 3.35e-10

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: 62.34  E-value: 3.35e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729919 283 PQEVLDIQNNLYQ-----TALHLAVHLDQPGAVRALvLKGASRALQDR--HGDTALHVACQRQHLACARCLLEGRPEpgr 355
Cdd:cd22192    1 WAQMLDELHLLQQkriseSPLLLAAKENDVQAIKKL-LKCPSCDLFQRgaLGETALHVAALYDNLEAAVVLMEAAPE--- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729919 356 gtshsldlqLQN-------WQGLACLHIATLQKNQPLMELLLRNGADIDVQEGTS-------------GKTALHLAVETQ 415
Cdd:cd22192   77 ---------LVNepmtsdlYQGETALHIAVVNQNLNLVRELIARGADVVSPRATGtffrpgpknliyyGEHPLSFAACVG 147

                        170       180
                 ....*....|....*....|....*...
gi 206729919 416 ERGLVQFLLQAGAQVDARMLNGCTPLHL 443
Cdd:cd22192  148 NEEIVRLLIEHGADIRAQDSLGNTVLHI 175
PHA03095 PHA03095
ankyrin-like protein; Provisional
 310-470 4.87e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 61.58  E-value: 4.87e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729919 310 VRALVLKGASRALQDRHGDTALHVACQRQHLACA---RCLLEGrpepgrgtshSLDLQLQNWQGLACLHIATLQKNQ-PL 385
Cdd:PHA03095  30 VRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKdivRLLLEA----------GADVNAPERCGFTPLHLYLYNATTlDV 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729919 386 MELLLRNGADIDVqEGTSGKTALH--LAVETQERGLVQFLLQAGAQVDARMLNGCTPLH--LAAGRGLMGISSTLCKAGA 461
Cdd:PHA03095 100 IKLLIKAGADVNA-KDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAvlLKSRNANVELLRLLIDAGA 178


                 ....*....
gi 206729919 462 DslLRNVED 470
Cdd:PHA03095 179 D--VYAVDD 185
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 369-462 4.42e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 58.46  E-value: 4.42e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729919 369 QGLACLHIATLQKNQPLMELLLRNGADIDVQEgTSGKTALHLAVETQERGLVQFLLQAGAQVDARMLNGCTPLHLAAGRG 448
Cdd:PHA02875 101 DGMTPLHLATILKKLDIMKLLIARGADPDIPN-TDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKG 179

                         90
                 ....*....|....
gi 206729919 449 LMGISSTLCKAGAD 462
Cdd:PHA02875 180 DIAICKMLLDSGAN 193
Ank_2 pfam12796
Ankyrin repeats (3 copies);
288-348 4.50e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 50.50  E-value: 4.50e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 206729919  288 DIQNNLYQTALHLAVHLDQPGAVRALVLKGASRAlqDRHGDTALHVACQRQHLACARCLLE 348
Cdd:pfam12796  24 NLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLEIVKLLLE 82
PHA03095 PHA03095
ankyrin-like protein; Provisional
 386-473 5.90e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 55.03  E-value: 5.90e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729919 386 MELLLRNGADIDvQEGTSGKTALHLAVET---QERGLVQFLLQAGAQVDARMLNGCTPLHLaagrgLMGISST------L 456
Cdd:PHA03095  30 VRRLLAAGADVN-FRGEYGKTPLHLYLHYsseKVKDIVRLLLEAGADVNAPERCGFTPLHL-----YLYNATTldviklL 103

                         90
                 ....*....|....*..
gi 206729919 457 CKAGADSLLRNVEDETP 473
Cdd:PHA03095 104 IKAGADVNAKDKVGRTP 120
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 367-461 8.04e-08

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 51.80  E-value: 8.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729919 367 NWQGLACLHIATLQ-KNQPL--MELLLRNGADIDVQEGTSGKTALHLAVETQERGLVQFLLQAgAQVDARMLNGC--TPL 441
Cdd:PHA02736  52 NRHGKQCVHIVSNPdKADPQekLKLLMEWGADINGKERVFGNTPLHIAVYTQNYELATWLCNQ-PGVNMEILNYAfkTPY 130

                         90       100
                 ....*....|....*....|
gi 206729919 442 HLAAGRGLMGISSTLCKAGA 461
Cdd:PHA02736 131 YVACERHDAKMMNILRAKGA 150
PHA03095 PHA03095
ankyrin-like protein; Provisional
 296-473 2.01e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 53.49  E-value: 2.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729919 296 TALHlaVHLD----QPGAVRALVLKGASRALQDRHGDTALHVACqRQHLACA---RCLLEGRPEP------GRGTSHSld 362
Cdd:PHA03095 119 TPLH--VYLSgfniNPKVIRLLLRKGADVNALDLYGMTPLAVLL-KSRNANVellRLLIDAGADVyavddrFRSLLHH-- 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729919 363 lqlqnwqglaclHIATLQKNQPLMELLLRNGADiDVQEGTSGKTALHLAV--ETQERGLVQFLLQAGAQVDARMLNGCTP 440
Cdd:PHA03095 194 ------------HLQSFKPRARIVRELIRAGCD-PAATDMLGNTPLHSMAtgSSCKRSLVLPLLIAGISINARNRYGQTP 260

                        170       180       190
                 ....*....|....*....|....*....|...
gi 206729919 441 LHLAAGRGLMGISSTLCKAGADSLLRNVEDETP 473
Cdd:PHA03095 261 LHYAAVFNNPRACRRLIALGADINAVSSDGNTP 293
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 310-444 2.35e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 53.04  E-value: 2.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729919 310 VRALVLKGASRALQDRHGDTALHVACQRQHLACARCLLEGRPepgrgtshslDLQLQNWQGLACLHIATLQKNQPLMELL 389
Cdd:PHA02874 107 IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGA----------DVNIEDDNGCYPIHIAIKHNFFDIIKLL 176

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 206729919 390 LRNGADIDVQEgTSGKTALHLAVETQERGLVQFLLQAGAQVDARMLNGCTPLHLA 444
Cdd:PHA02874 177 LEKGAYANVKD-NNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNA 230
PHA02741 PHA02741
hypothetical protein; Provisional
 355-444 3.45e-07

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 50.04  E-value: 3.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729919 355 RGTSHSLDLQLQNWQGLACLHIATLQKNQ----PLMELLLRNGADIDVQEGTSGKTALHLAVETQERGLVQFLL-QAGAQ 429
Cdd:PHA02741  45 RGDCHAAALNATDDAGQMCIHIAAEKHEAqlaaEIIDHLIELGADINAQEMLEGDTALHLAAHRRDHDLAEWLCcQPGID 124

                         90
                 ....*....|....*
gi 206729919 430 VDARMLNGCTPLHLA 444
Cdd:PHA02741 125 LHFCNADNKSPFELA 139
PHA03095 PHA03095
ankyrin-like protein; Provisional
 310-444 6.37e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 51.56  E-value: 6.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729919 310 VRALVLKGASRALQDRHGDTALHVACQRQH--------LACARCLLEGRPEPGRGTSHSLDLqlqnwqGLACLHIatlqk 381
Cdd:PHA03095 170 LRLLIDAGADVYAVDDRFRSLLHHHLQSFKprarivreLIRAGCDPAATDMLGNTPLHSMAT------GSSCKRS----- 238

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 206729919 382 nqpLMELLLRNGADIDVQEgTSGKTALHLAVETQERGLVQFLLQAGAQVDARMLNGCTPLHLA 444
Cdd:PHA03095 239 ---LVLPLLIAGISINARN-RYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLM 297
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 296-444 2.44e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 49.88  E-value: 2.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729919 296 TALHLAVHLDQPGAVRALVLKGASRALQDRHGDTALHVACQRQHLACARCLLEGrpepGRGTSHsldlqlQNWQGLACLH 375
Cdd:PHA02878 170 TALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLEN----GASTDA------RDKCGNTPLH 239

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729919 376 IATLQ-KNQPLMELLLRNGADIDVQEGTSGKTALHLAVETQERglVQFLLQAGAQVDARMLNGCTPLHLA 444
Cdd:PHA02878 240 ISVGYcKDYDILKLLLEHGVDVNAKSYILGLTALHSSIKSERK--LKLLLEYGADINSLNSYKLTPLSSA 307
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 295-471 2.51e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 49.60  E-value: 2.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729919 295 QTALHLAVHLDQPGAVRALVLKGasRALQD---RHGDTALHVACQRQHLACARCLLEGRPEPgrgtshsldlQLQNWQGL 371
Cdd:PHA02875  69 ESELHDAVEEGDVKAVEELLDLG--KFADDvfyKDGMTPLHLATILKKLDIMKLLIARGADP----------DIPNTDKF 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729919 372 ACLHIATLQKNQPLMELLLRNGADIDVQEGTsGKTALHLAVETQERGLVQFLLQAGAQVDARMLNGC-TPLHLAAGRGLM 450
Cdd:PHA02875 137 SPLHLAVMMGDIKGIELLIDHKACLDIEDCC-GCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKI 215

                        170       180
                 ....*....|....*....|..
gi 206729919 451 GISSTLCKAGADS-LLRNVEDE 471
Cdd:PHA02875 216 DIVRLFIKRGADCnIMFMIEGE 237
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 259-453 3.55e-06

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: 49.69  E-value: 3.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729919  259 GDTLVHLAVIHE--------APAVLLCCLALLPQEVLDIQNNLY---QTALHLAVHLDQPGAVRALVLKGASralqdrhg 327
Cdd:TIGR00870  82 GDTLLHAISLEYvdaveailLHLLAAFRKSGPLELANDQYTSEFtpgITALHLAAHRQNYEIVKLLLERGAS-------- 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729919  328 dtaLHVACQrqhlaCARCLLEGRPEPGRGTSHSLDLqlqnwqgLACLhiatlqKNQPLMELLLRNGADIDVQEgTSGKTA 407
Cdd:TIGR00870 154 ---VPARAC-----GDFFVKSQGVDSFYHGESPLNA-------AACL------GSPSIVALLSEDPADILTAD-SLGNTL 211

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 206729919  408 LHLAVETQE---------RGLVQFLLQAGAQVDAR-----MLN--GCTPLHLAAGRGLMGIS 453
Cdd:TIGR00870 212 LHLLVMENEfkaeyeelsCQMYNFALSLLDKLRDSkelevILNhqGLTPLKLAAKEGRIVLF 273
Ank_4 pfam13637
Ankyrin repeats (many copies);
296-347 4.05e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.80  E-value: 4.05e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 206729919  296 TALHLAVHLDQPGAVRALVLKGASRALQDRHGDTALHVACQRQHLACARCLL 347
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00249 PTZ00249
variable surface protein Vir28; Provisional
 77-229 7.00e-06

variable surface protein Vir28; Provisional


Pssm-ID: 140276 [Multi-domain]  Cd Length: 516  Bit Score: 48.49  E-value: 7.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729919  77 TWPALRTLSSLRAGP-----SEPHSPGRRP--PRAGRPLCQADPQ-----PGKAARRSLEPDPAQTG--------PRPAR 136
Cdd:PTZ00249 226 TAHAHRRISGEARPPkhisfSSPHAHGRPPveTRPPNPVSVSSPQahgrhPGETHTPPLVTVPSSKAhdrnpvqtPTPTS 305

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729919 137 AAGMSEARKGPDEAE--ESQYDSGIESLRSLRSLPESTSAPASGPSD----------GSPQPCTHPPGPVKEPQEKEDAD 204
Cdd:PTZ00249 306 VSGYSSQAKGLEKQAggESERTSSVPSEQFPLPLPVLLPLGQSGPLEsseseetdeyAGPKGLPEPELELVELQEEDQRH 385

                        170       180
                 ....*....|....*....|....*
gi 206729919 205 GERADSTYGSSSLTYTLSLLGGPEA 229
Cdd:PTZ00249 386 GLKHDVDTFREDEEDTFLQEGDQPA 410
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 373-497 7.11e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 48.51  E-value: 7.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729919 373 CLHIATLQKNQPLMELLLRNGADIDvQEGTSGKTALHL-----AVETQERGLVQFLLQAGAQVDARMLNGCTPLHLAAGR 447
Cdd:PHA03100  38 PLYLAKEARNIDVVKILLDNGADIN-SSTKNNSTPLHYlsnikYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISK 116

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 206729919 448 --GLMGISSTLCKAGADSLLRNVEDETPQDLTEESlvllPFDDLKISgKLLL 497
Cdd:PHA03100 117 ksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLES----NKIDLKIL-KLLI 163
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 409-480 7.23e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.74  E-value: 7.23e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 206729919 409 HLAVETQERGlVQFLLQAGAQVDARMLNGCTPLHLAAGRGLMGISSTLCKAGADSLLRNVEDETPQDLTEES 480
Cdd:PTZ00322  88 QLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEEN 158
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 327-442 7.28e-06

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: 48.72  E-value: 7.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729919 327 GDTALHVAC---QRQHLACARCLLEGRPEPGRGTshsldlQLQN-------WQGLACLHIATLQKNQPLMELLLRNGADI 396
Cdd:cd21882   26 GKTCLHKAAlnlNDGVNEAIMLLLEAAPDSGNPK------ELVNapctdefYQGQTALHIAIENRNLNLVRLLVENGADV 99

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 206729919 397 DVQE-GTS-----------GKTALHLAVETQERGLVQFLLQAGAQ---VDARMLNGCTPLH 442
Cdd:cd21882  100 SARAtGRFfrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQpaaLEAQDSLGNTVLH 160
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 382-473 1.44e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 47.27  E-value: 1.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729919 382 NQPLMELLLRNGADIDVQEGTSgKTALHLAVETQERGLVQFLLQAGAQVDARMLNGCTPLHLAAGRGLMGISSTLCKAGA 461
Cdd:PHA02874 103 EKDMIKTILDCGIDVNIKDAEL-KTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGA 181

                         90
                 ....*....|..
gi 206729919 462 DSLLRNVEDETP 473
Cdd:PHA02874 182 YANVKDNNGESP 193
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 385-491 2.65e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 46.80  E-value: 2.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729919 385 LMELLLRNGADIDVQEGTSGKTALHLAVETQERGLVQFLLQAGAQVDARMLNGCTPLHLAAGRGLMGISSTLCKAGADSL 464
Cdd:PHA02878 149 ITKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTD 228

                         90       100
                 ....*....|....*....|....*..
gi 206729919 465 LRNVEDETPQDLTEESlvLLPFDDLKI 491
Cdd:PHA02878 229 ARDKCGNTPLHISVGY--CKDYDILKL 253
PHA03247 PHA03247
large tegument protein UL36; Provisional
 63-250 3.63e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.86  E-value: 3.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729919   63 PAWAVRLPTVTAGWTWPALRTLSSLRAGPSEPHSPGRRPPRAGRPLCQADPQP--GKAARRSLEPDPAQTGPRPARAAGM 140
Cdd:PHA03247 2670 LGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPpgPAAARQASPALPAAPAPPAVPAGPA 2749

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729919  141 SEARKGPDEAeesqydsgieslRSLRSLPESTSAPAsGPSDGSPQPCTHPPG-PVKEPQEKEDADGERADSTYGSSSLTY 219
Cdd:PHA03247 2750 TPGGPARPAR------------PPTTAGPPAPAPPA-APAAGPPRRLTRPAVaSLSESRESLPSPWDPADPPAAVLAPAA 2816

                         170       180       190
                  ....*....|....*....|....*....|.
gi 206729919  220 TLSLLGGPEAEDPAPRLPLPHVGALSPQQLE 250
Cdd:PHA03247 2817 ALPPAASPAGPLPPPTSAQPTAPPPPPGPPP 2847
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 298-444 5.37e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 45.72  E-value: 5.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729919 298 LHLAVHLDQPGAVRALVLKGASRALQDRHGDTALHVACQRQHLACARCLLegrpepgrgtSHSLDLQLQNWQGLACLHIA 377
Cdd:PHA02874 161 IHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLI----------DHGNHIMNKCKNGFTPLHNA 230

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 206729919 378 TLQkNQPLMELLLrNGADIDVQEgTSGKTALHLAVETQ-ERGLVQFLLQAGAQVDARMLNGCTPLHLA 444
Cdd:PHA02874 231 IIH-NRSAIELLI-NNASINDQD-IDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTA 295
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 387-445 8.51e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 45.04  E-value: 8.51e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 206729919 387 ELLLRNGADIDVQEgTSGKTALHLAVETQERGLVQFLLQAGAQVDARMLNGCTPLHLAA 445
Cdd:PHA03100 176 NYLLSYGVPINIKD-VYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAI 233
Ank_4 pfam13637
Ankyrin repeats (many copies);
406-448 1.06e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.95  E-value: 1.06e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 206729919  406 TALHLAVETQERGLVQFLLQAGAQVDARMLNGCTPLHLAAGRG 448
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNG 45
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 287-475 1.27e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 44.57  E-value: 1.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729919 287 LDIQNNLYQTALHLAVHLDQPGAVRALVLKGASRALQDRHGDTALHVACQRQHLACARCLLEgrpepgRGTShsldLQLQ 366
Cdd:PHA02874 117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLE------KGAY----ANVK 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729919 367 NWQGLACLHIATLQKNQPLMELLLRNGADIDVQeGTSGKTALHLAVeTQERGLVQFLLQaGAQVDARMLNGCTPLHLAAG 446
Cdd:PHA02874 187 DNNGESPLHNAAEYGDYACIKLLIDHGNHIMNK-CKNGFTPLHNAI-IHNRSAIELLIN-NASINDQDIDGSTPLHHAIN 263

                        170       180       190
                 ....*....|....*....|....*....|
gi 206729919 447 RGL-MGISSTLCKAGADSLLRNVEDETPQD 475
Cdd:PHA02874 264 PPCdIDIIDILLYHKADISIKDNKGENPID 293
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 324-478 1.30e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 44.86  E-value: 1.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729919 324 DRHGDTALHVACQRQHLACARCLLEgrpepgrgtsHSLDLQLQNWQGLACLHIATLQKNQPLMELLLRNGADIDVQegtS 403
Cdd:PLN03192 555 DSKGRTPLHIAASKGYEDCVLVLLK----------HACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPH---A 621

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 206729919 404 GKTALHLAVETQERGLVQFLLQAGAQVDARMLNGCTPLHLAAGRGLMGISSTLCKAGADSLLRNVEDE-TPQDLTE 478
Cdd:PLN03192 622 AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDDDfSPTELRE 697
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 368-442 1.59e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 44.41  E-value: 1.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729919 368 WQGLACLHIATLQKNQPLMELLLRNGADID----------VQEGTS---GKTALHLAVETQERGLVQFLLQ---AGAQVD 431
Cdd:cd22196   92 YKGQTALHIAIERRNMHLVELLVQNGADVHarasgeffkkKKGGPGfyfGELPLSLAACTNQLDIVKFLLEnphSPADIS 171

                         90
                 ....*....|.
gi 206729919 432 ARMLNGCTPLH 442
Cdd:cd22196  172 ARDSMGNTVLH 182
PHA02741 PHA02741
hypothetical protein; Provisional
 403-476 1.68e-04

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 42.34  E-value: 1.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729919 403 SGKTALHLAVETQER----GLVQFLLQAGAQVDAR-MLNGCTPLHLAAGRGLMGISSTLC-KAGADSLLRNVEDETPQDL 476
Cdd:PHA02741  59 AGQMCIHIAAEKHEAqlaaEIIDHLIELGADINAQeMLEGDTALHLAAHRRDHDLAEWLCcQPGIDLHFCNADNKSPFEL 138
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 247-348 2.81e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 43.35  E-value: 2.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729919 247 QQLEALtYISEDGDTlvhlAVIHEAPavllcclallPQEVLDiqnnlyQTALH-LAVHLDQPGA------VRALVLKGAS 319
Cdd:PTZ00322  49 THLEAL-EATENKDA----TPDHNLT----------TEEVID------PVVAHmLTVELCQLAAsgdavgARILLTGGAD 107

                         90       100
                 ....*....|....*....|....*....
gi 206729919 320 RALQDRHGDTALHVACQRQHLACARCLLE 348
Cdd:PTZ00322 108 PNCRDYDGRTPLHIACANGHVQVVRVLLE 136
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 324-433 3.58e-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: 43.15  E-value: 3.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729919  324 DRHGDTALHVACQR-QHLACARCLL--EGRPEPGRGTSHSLDLQLQNWQGLACLHIATLQKNQPLMELLLrngaDIDVQE 400
Cdd:TIGR00870  49 DRLGRSALFVAAIEnENLELTELLLnlSCRGAVGDTLLHAISLEYVDAVEAILLHLLAAFRKSGPLELAN----DQYTSE 124

                          90       100       110
                  ....*....|....*....|....*....|...
gi 206729919  401 GTSGKTALHLAVETQERGLVQFLLQAGAQVDAR 433
Cdd:TIGR00870 125 FTPGITALHLAAHRQNYEIVKLLLERGASVPAR 157
Ank_5 pfam13857
Ankyrin repeats (many copies);
389-444 3.91e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.48  E-value: 3.91e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 206729919  389 LLRNGADIDVQEGTSGKTALHLAVETQERGLVQFLLQAGAQVDARMLNGCTPLHLA 444
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02743 PHA02743
Viral ankyrin protein; Provisional
 369-444 4.09e-04

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 40.95  E-value: 4.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729919 369 QGLACLHIATL-QKNQPLM--ELLLRNGADIDVQEGTSGKTALHLAVETQERGLVQFLLQA-GAQVDARMLNGCTPLHLA 444
Cdd:PHA02743  56 HGRQCTHMVAWyDRANAVMkiELLVNMGADINARELGTGNTLLHIAASTKNYELAEWLCRQlGVNLGAINYQHETAYHIA 135
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 370-462 4.63e-04

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: 42.94  E-value: 4.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729919 370 GLACLHIATLQKNQPLME---LLLRNGADID----------VQEGTSGKTALHLAVETQERGLVQFLLQAGAQVDARML- 435
Cdd:cd21882   26 GKTCLHKAALNLNDGVNEaimLLLEAAPDSGnpkelvnapcTDEFYQGQTALHIAIENRNLNLVRLLVENGADVSARATg 105

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 206729919 436 -----NGCT-------PLHLAAGRGLMGISSTLCKAGAD 462
Cdd:cd21882  106 rffrkSPGNlfyfgelPLSLAACTNQEEIVRLLLENGAQ 144
Ank_5 pfam13857
Ankyrin repeats (many copies);
287-334 5.97e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.10  E-value: 5.97e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 206729919  287 LDIQNNLYQTALHLAVHLDQPGAVRALVLKGASRALQDRHGDTALHVA 334
Cdd:pfam13857   9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
370-424 1.01e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 37.25  E-value: 1.01e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 206729919  370 GLACLHIATLQKNQPLMELLLRNGADIDVQEGtSGKTALHLAVETQERGLVQFLL 424
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDG-NGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 361-448 1.10e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 41.49  E-value: 1.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729919 361 LDLQLQNWQGLACLHIATLQKNQPLMELLLRNGADIDVQEgTSGKTALHLAVETQERGLVQFLLQAGAQVDARMLNGCTP 440
Cdd:PHA02874 115 IDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIED-DNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESP 193


                 ....*...
gi 206729919 441 LHLAAGRG 448
Cdd:PHA02874 194 LHNAAEYG 201
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 404-433 1.24e-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. 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: 36.50  E-value: 1.24e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 206729919  404 GKTALHLAVETQER-GLVQFLLQAGAQVDAR 433
Cdd:pfam00023   2 GNTPLHLAAGRRGNlEIVKLLLSKGADVNAR 32
PHA03095 PHA03095
ankyrin-like protein; Provisional
 287-397 1.92e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 40.78  E-value: 1.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729919 287 LDIQNNLYQTALHLAVHLDQPGAVRALVLKGASRALQDRHGDTALHVACQRQHLACARCLLEGRPEPgRGTSHSLDlQLQ 366
Cdd:PHA03095 250 INARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSA-ETVAATLN-TAS 327

                         90       100       110
                 ....*....|....*....|....*....|.
gi 206729919 367 NWqGLACLHIATLQKnqpLMELLLRNGADID 397
Cdd:PHA03095 328 VA-GGDIPSDATRLC---VAKVVLRGAFSLL 354
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 382-462 2.17e-03

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 40.83  E-value: 2.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729919  382 NQPLMELLLRNGADIDVqegtsGKTALHLAVETQERG---LVQFLLQAGAQ------VDARMLN----GCTPLHLAAGRG 448
Cdd:TIGR00870  65 NLELTELLLNLSCRGAV-----GDTLLHAISLEYVDAveaILLHLLAAFRKsgplelANDQYTSeftpGITALHLAAHRQ 139

                          90
                  ....*....|....
gi 206729919  449 LMGISSTLCKAGAD 462
Cdd:TIGR00870 140 NYEIVKLLLERGAS 153
PHA03247 PHA03247
large tegument protein UL36; Provisional
 63-197 2.47e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 40.69  E-value: 2.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729919   63 PAWAVRLPTVTAGWTWPALRTLSSLRAGPSEPHSPGRRPPRAGRPLCQADPQPGKAARRSLEPDPAQtgPRPARAAGMSE 142
Cdd:PHA03247 2717 SATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRL--TRPAVASLSES 2794

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 206729919  143 ARKGPDEAEESQYDSGIESLRSLRSLPESTSAPASGPSDGSPQPCTHPPGPVKEP 197
Cdd:PHA03247 2795 RESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPS 2849
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 368-476 3.14e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 39.97  E-value: 3.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729919 368 WQGLACLHIATLQKNQPLMELLLRNGADIDVQEgTSGKTALHLAVETQERGLVQFLLQAGAQVDARML-NGCTPLHLAAG 446
Cdd:PHA02875  33 YDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKY-PDIESELHDAVEEGDVKAVEELLDLGKFADDVFYkDGMTPLHLATI 111

                         90       100       110
                 ....*....|....*....|....*....|
gi 206729919 447 RGLMGISSTLCKAGADSLLRNVEDETPQDL 476
Cdd:PHA02875 112 LKKLDIMKLLIARGADPDIPNTDKFSPLHL 141
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 368-442 3.88e-03

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


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 39.78  E-value: 3.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729919 368 WQGLACLHIATLQKNQPLMELLLRNGADIDVQ----------EGTS---GKTALHLAVETQERGLVQFLLQ---AGAQVD 431
Cdd:cd22193   74 YEGQTALHIAIERRQGDIVALLVENGADVHAHakgrffqpkyQGEGfyfGELPLSLAACTNQPDIVQYLLEnehQPADIE 153

                         90
                 ....*....|.
gi 206729919 432 ARMLNGCTPLH 442
Cdd:cd22193  154 AQDSRGNTVLH 164
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 436-467 4.20e-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. 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: 34.96  E-value: 4.20e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 206729919  436 NGCTPLHLAAGR-GLMGISSTLCKAGADSLLRN 467
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 310-473 4.54e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 39.66  E-value: 4.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729919 310 VRALVLKGASRALQDRHGDTALHVACQ-RQHLACARCLLEgrpepgrgtsHSLDLQLQNWQGLACLHIATLQKNQPLMEL 388
Cdd:PHA02876 324 IRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLE----------LGANVNARDYCDKTPIHYAAVRNNVVIINT 393

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729919 389 LLRNGADIDVQEGTSGkTALHLAV-ETQERGLVQFLLQAGAQVDARMLNGCTPLHLAAGRGL-MGISSTLCKAGADSLLR 466
Cdd:PHA02876 394 LLDYGADIEALSQKIG-TALHFALcGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNCkLDVIEMLLDNGADVNAI 472


                 ....*..
gi 206729919 467 NVEDETP 473
Cdd:PHA02876 473 NIQNQYP 479
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 288-432 4.69e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 39.85  E-value: 4.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729919 288 DIQNNLYQTALHLAVHLDQPGAVRALVLKGASRALQDRHGDTALHVACQRQHLACARCLLEgrpepgrgTSHSLDLQLQN 367
Cdd:PLN03192 552 DIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYH--------FASISDPHAAG 623

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 206729919 368 wqGLACLhiATLQKNQPLMELLLRNGADIDvQEGTSGKTALHLAVETQERGLVQFLLQAGAQVDA 432
Cdd:PLN03192 624 --DLLCT--AAKRNDLTAMKELLKQGLNVD-SEDHQGATALQVAMAEDHVDMVRLLIMNGADVDK 683
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 70-240 5.50e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 39.58  E-value: 5.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729919  70 PTVTAGWTWPALRTLSSLRAGPSEPHSPGRRPPRAGRPLCQADPQPGKAARrslEPDPAQTGPRPARAAGMSEARKGPDE 149
Cdd:PRK07764 584 VEAVVGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAA---APAEASAAPAPGVAAPEHHPKHVAVP 660

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729919 150 AEESQYDSGIESLRslrslPESTSAPASGPSDGSPQPCTHPPGPVKEPQEKEDADGERADSTYGSSSLTYTLSLLGGPEA 229
Cdd:PRK07764 661 DASDGGDGWPAKAG-----GAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAA 735

                        170
                 ....*....|.
gi 206729919 230 EDPAPRLPLPH 240
Cdd:PRK07764 736 DDPVPLPPEPD 746
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 287-351 5.99e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 38.88  E-value: 5.99e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 206729919 287 LDIQNNLYQTALHLAVHLDQPGAVRALVLKGASRALQDRHGDTALHVACQRQHLACARCLLEGRP 351
Cdd:PHA03100 185 INIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 326-348 6.02e-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: 34.49  E-value: 6.02e-03
                           10        20
                   ....*....|....*....|...
gi 206729919   326 HGDTALHVACQRQHLACARCLLE 348
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLD 23
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 399-445 6.43e-03

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 39.36  E-value: 6.43e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 206729919 399 QEGTSGKTALHLAVETQERGLVQFLLQAGAQVDAR----MLN----------GCTPLHLAA 445
Cdd:cd22194  136 EEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHakgvFFNpkykhegfyfGETPLALAA 196
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 366-442 9.98e-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: 38.59  E-value: 9.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 206729919 366 QNWQGLACLHIATLQKNQPLMELLLRNGADIDVQ-EGT------------SGKTALHLAVETQERGLVQFLLQ----AGA 428
Cdd:cd22194  137 EAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHaKGVffnpkykhegfyFGETPLALAACTNQPEIVQLLMEkestDIT 216

                         90
                 ....*....|....
gi 206729919 429 QVDARmlnGCTPLH 442
Cdd:cd22194  217 SQDSR---GNTVLH 227
 
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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