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Conserved domains on  [gi|17136842|ref|NP_476943|]
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cactus, isoform C [Drosophila melanogaster]

Protein Classification

ankyrin repeat domain-containing protein( domain architecture ID 11429852)

ankyrin repeat domain-containing protein; ANK proteins mediate specific protein-protein interactions without necessarily recognizing specific primary sequences which allows for one ankyrin repeat domain to recognize and bind to a variety of intracellular substrates and may be involved in a wide array of functions

Gene Ontology:  GO:0005515
PubMed:  17176038
SCOP:  4000366

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
225-464 1.42e-33

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 128.53  E-value: 1.42e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136842 225 QQNDDGDTPLHLACISGSVDVVAALIRmapHPCLLNIQNDVAQTPLHLAALTAQPNIMRILLLAGAEPTVRDRHGNTALH 304
Cdd:COG0666  82 AKDDGGNTLLHAAARNGDLEIVKLLLE---AGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLH 158
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136842 305 LSCIAGEKQCVRALTEKfgateiheahrqyghrsndkavsslsyaclPADLEIRNYDGERCVHLAAEAGHIDILRILVSH 384
Cdd:COG0666 159 LAAANGNLEIVKLLLEA------------------------------GADVNARDNDGETPLHLAAENGHLEIVKLLLEA 208
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136842 385 GADINAREgKSGRTPLHIAIEGCNEDLANFLLDecEKLNLETATYAGLTAYQFACIMNKSRMQNILEKRGAETVTPPDSD 464
Cdd:COG0666 209 GADVNAKD-NDGKTALDLAAENGNLEIVKLLLE--AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDL 285
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
225-464 1.42e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 128.53  E-value: 1.42e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136842 225 QQNDDGDTPLHLACISGSVDVVAALIRmapHPCLLNIQNDVAQTPLHLAALTAQPNIMRILLLAGAEPTVRDRHGNTALH 304
Cdd:COG0666  82 AKDDGGNTLLHAAARNGDLEIVKLLLE---AGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLH 158
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136842 305 LSCIAGEKQCVRALTEKfgateiheahrqyghrsndkavsslsyaclPADLEIRNYDGERCVHLAAEAGHIDILRILVSH 384
Cdd:COG0666 159 LAAANGNLEIVKLLLEA------------------------------GADVNARDNDGETPLHLAAENGHLEIVKLLLEA 208
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136842 385 GADINAREgKSGRTPLHIAIEGCNEDLANFLLDecEKLNLETATYAGLTAYQFACIMNKSRMQNILEKRGAETVTPPDSD 464
Cdd:COG0666 209 GADVNAKD-NDGKTALDLAAENGNLEIVKLLLE--AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDL 285
PHA02736 PHA02736
Viral ankyrin protein; Provisional
359-456 3.62e-18

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 81.46  E-value: 3.62e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136842  359 NYDGERCVHLAAEAGHID---ILRILVSHGADINAREGKSGRTPLHIAIEGCNEDLANFLLDEcEKLNLETATYAGLTAY 435
Cdd:PHA02736  52 NRHGKQCVHIVSNPDKADpqeKLKLLMEWGADINGKERVFGNTPLHIAVYTQNYELATWLCNQ-PGVNMEILNYAFKTPY 130
                         90       100
                 ....*....|....*....|.
gi 17136842  436 QFACIMNKSRMQNILEKRGAE 456
Cdd:PHA02736 131 YVACERHDAKMMNILRAKGAQ 151
Ank_2 pfam12796
Ankyrin repeats (3 copies);
270-391 2.05e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 71.30  E-value: 2.05e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136842   270 LHLAALTAQPNIMRILLLAGAEPTVRDRHGNTALHLSCIAGEKQCVRALTEKfgateiheahrqyghrsndkavsslsya 349
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH---------------------------- 52
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 17136842   350 clpADLEIRNYdGERCVHLAAEAGHIDILRILVSHGADINAR 391
Cdd:pfam12796  53 ---ADVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINVK 90
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
221-475 6.96e-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: 58.10  E-value: 6.96e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136842 221 EQFYQQNDDG-DTPLHLACISGSVDVVAALIRmAPHpCLLNIQNDVAQTPLHLAALTAQPNIMRILLLAGAE----PTVR 295
Cdd:cd22192   7 ELHLLQQKRIsESPLLLAAKENDVQAIKKLLK-CPS-CDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElvnePMTS 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136842 296 DRH-GNTALHLSCIAGEKQCVRALTEKfGATEIH-EAHRQYGHRSNDKAVsslsyaclpadleirnYDGERCVHLAAEAG 373
Cdd:cd22192  85 DLYqGETALHIAVVNQNLNLVRELIAR-GADVVSpRATGTFFRPGPKNLI----------------YYGEHPLSFAACVG 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136842 374 HIDILRILVSHGADINAREgKSGRTPLHIAIEGCNEDLA----NFLLDECEKLN---LETAT-YAGLTAYQFACIMNKSR 445
Cdd:cd22192 148 NEEIVRLLIEHGADIRAQD-SLGNTVLHILVLQPNKTFAcqmyDLILSYDKEDDlqpLDLVPnNQGLTPFKLAAKEGNIV 226
                       250       260       270
                ....*....|....*....|....*....|....
gi 17136842 446 M-QNILEKRGAE--TVTPPDSD-YDSSDIEDLDD 475
Cdd:cd22192 227 MfQHLVQKRRHIqwTYGPLTSTlYDLTEIDSWGD 260
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
218-382 1.08e-07

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: 54.32  E-value: 1.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136842   218 NAWEQFYQQNDD---GDTPLHLACISGSVDVVAALI-RMAPHP-------CLLNIQNDVA---QTPLHLAALTAQPNIMR 283
Cdd:TIGR00870 113 PLELANDQYTSEftpGITALHLAAHRQNYEIVKLLLeRGASVParacgdfFVKSQGVDSFyhgESPLNAAACLGSPSIVA 192
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136842   284 ILLLAGAEPTVRDRHGNTALHLSCIagekqcvraltekfgATEIHEAHRQYGHRSNDKAVSSLSYACLPADLE-IRNYDG 362
Cdd:TIGR00870 193 LLSEDPADILTADSLGNTLLHLLVM---------------ENEFKAEYEELSCQMYNFALSLLDKLRDSKELEvILNHQG 257
                         170       180
                  ....*....|....*....|
gi 17136842   363 ERCVHLAAEAGHIDILRILV 382
Cdd:TIGR00870 258 LTPLKLAAKEGRIVLFRLKL 277
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
361-390 6.38e-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: 42.57  E-value: 6.38e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 17136842    361 DGERCVHLAAEAGHIDILRILVSHGADINA 390
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
225-464 1.42e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 128.53  E-value: 1.42e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136842 225 QQNDDGDTPLHLACISGSVDVVAALIRmapHPCLLNIQNDVAQTPLHLAALTAQPNIMRILLLAGAEPTVRDRHGNTALH 304
Cdd:COG0666  82 AKDDGGNTLLHAAARNGDLEIVKLLLE---AGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLH 158
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136842 305 LSCIAGEKQCVRALTEKfgateiheahrqyghrsndkavsslsyaclPADLEIRNYDGERCVHLAAEAGHIDILRILVSH 384
Cdd:COG0666 159 LAAANGNLEIVKLLLEA------------------------------GADVNARDNDGETPLHLAAENGHLEIVKLLLEA 208
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136842 385 GADINAREgKSGRTPLHIAIEGCNEDLANFLLDecEKLNLETATYAGLTAYQFACIMNKSRMQNILEKRGAETVTPPDSD 464
Cdd:COG0666 209 GADVNAKD-NDGKTALDLAAENGNLEIVKLLLE--AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDL 285
PHA02736 PHA02736
Viral ankyrin protein; Provisional
359-456 3.62e-18

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 81.46  E-value: 3.62e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136842  359 NYDGERCVHLAAEAGHID---ILRILVSHGADINAREGKSGRTPLHIAIEGCNEDLANFLLDEcEKLNLETATYAGLTAY 435
Cdd:PHA02736  52 NRHGKQCVHIVSNPDKADpqeKLKLLMEWGADINGKERVFGNTPLHIAVYTQNYELATWLCNQ-PGVNMEILNYAFKTPY 130
                         90       100
                 ....*....|....*....|.
gi 17136842  436 QFACIMNKSRMQNILEKRGAE 456
Cdd:PHA02736 131 YVACERHDAKMMNILRAKGAQ 151
Ank_2 pfam12796
Ankyrin repeats (3 copies);
270-391 2.05e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 71.30  E-value: 2.05e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136842   270 LHLAALTAQPNIMRILLLAGAEPTVRDRHGNTALHLSCIAGEKQCVRALTEKfgateiheahrqyghrsndkavsslsya 349
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH---------------------------- 52
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 17136842   350 clpADLEIRNYdGERCVHLAAEAGHIDILRILVSHGADINAR 391
Cdd:pfam12796  53 ---ADVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINVK 90
PHA02743 PHA02743
Viral ankyrin protein; Provisional
360-464 2.89e-13

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 67.53  E-value: 2.89e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136842  360 YD--GERCVHLAAE---AGHIDILRILVSHGADINAREGKSGRTPLHIAIEGCNEDLANFLldeCEKL--NLETATYAGL 432
Cdd:PHA02743  53 YDhhGRQCTHMVAWydrANAVMKIELLVNMGADINARELGTGNTLLHIAASTKNYELAEWL---CRQLgvNLGAINYQHE 129
                         90       100       110
                 ....*....|....*....|....*....|..
gi 17136842  433 TAYQFACIMNKSRMQNILEKRGAETVTPPDSD 464
Cdd:PHA02743 130 TAYHIAYKMRDRRMMEILRANGAVCDDPLSIG 161
PHA03100 PHA03100
ankyrin repeat protein; Provisional
232-455 3.41e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 71.23  E-value: 3.41e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136842  232 TPLHLACISGSVDVVAALIRmapHPCLLNIQNDVAQTPLHLAA-----LTAQPNIMRILLLAGAEPTVRDRHGNTALHLs 306
Cdd:PHA03100  37 LPLYLAKEARNIDVVKILLD---NGADINSSTKNNSTPLHYLSnikynLTDVKEIVKLLLEYGANVNAPDNNGITPLLY- 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136842  307 ciagekqcvrALTEKFGATEIHEAHRQYGhrsndkavsslsyaclpADLEIRNYDGERCVHLAAEAGHID--ILRILVSH 384
Cdd:PHA03100 113 ----------AISKKSNSYSIVEYLLDNG-----------------ANVNIKNSDGENLLHLYLESNKIDlkILKLLIDK 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136842  385 GADINARE---------------GKSGRTPLHIAIEGCNEDLANFLLDECEKLNleTATYAGLTAYQFACIMNKSRMQNI 449
Cdd:PHA03100 166 GVDINAKNrvnyllsygvpinikDVYGFTPLHYAVYNNNPEFVKYLLDLGANPN--LVNKYGDTPLHIAILNNNKEIFKL 243

                 ....*.
gi 17136842  450 LEKRGA 455
Cdd:PHA03100 244 LLNNGP 249
Ank_2 pfam12796
Ankyrin repeats (3 copies);
216-296 7.22e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 64.37  E-value: 7.22e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136842   216 IMNAWEQFYQQNDDGDTPLHLACISGSVDVVAALIRMAPhpclLNIQNDvAQTPLHLAALTAQPNIMRILLLAGAEPTVR 295
Cdd:pfam12796  16 LLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD----VNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINVK 90

                  .
gi 17136842   296 D 296
Cdd:pfam12796  91 D 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
230-403 1.62e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 66.20  E-value: 1.62e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136842  230 GDTPLHL-ACISGSVDVVAALIRMAPHpclLNIQNDVAQTPLH--LAALTAQPNIMRILLLAGAEPTVRDRHGNTALHls 306
Cdd:PHA03095  83 GFTPLHLyLYNATTLDVIKLLIKAGAD---VNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLA-- 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136842  307 CIAGEKQC----VRALTEK---------FGATEIHEaHRQYGHRSNDKAVSSLSYACLPADleiRNYDGERCVHLAAEAG 373
Cdd:PHA03095 158 VLLKSRNAnvelLRLLIDAgadvyavddRFRSLLHH-HLQSFKPRARIVRELIRAGCDPAA---TDMLGNTPLHSMATGS 233
                        170       180       190
                 ....*....|....*....|....*....|..
gi 17136842  374 HIDILRI--LVSHGADINAREgKSGRTPLHIA 403
Cdd:PHA03095 234 SCKRSLVlpLLIAGISINARN-RYGQTPLHYA 264
Ank_2 pfam12796
Ankyrin repeats (3 copies);
367-456 2.28e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 60.13  E-value: 2.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136842   367 HLAAEAGHIDILRILVSHGADINAREgKSGRTPLHIAIEGCNEDLANFLLDECEKlnleTATYAGLTAYQFACIMNKSRM 446
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENGADANLQD-KNGRTALHLAAKNGHLEIVKLLLEHADV----NLKDNGRTALHYAARSGHLEI 76
                          90
                  ....*....|
gi 17136842   447 QNILEKRGAE 456
Cdd:pfam12796  77 VKLLLEKGAD 86
Ank_2 pfam12796
Ankyrin repeats (3 copies);
352-417 2.79e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 59.74  E-value: 2.79e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17136842   352 PADLEIRNYDGERCVHLAAEAGHIDILRILVSHgadINAREGKSGRTPLHIAIEGCNEDLANFLLD 417
Cdd:pfam12796  20 GADANLQDKNGRTALHLAAKNGHLEIVKLLLEH---ADVNLKDNGRTALHYAARSGHLEIVKLLLE 82
PHA03095 PHA03095
ankyrin-like protein; Provisional
226-446 2.82e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 65.43  E-value: 2.82e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136842  226 QNDDGDTPLHlACISG---SVDVVAALIRMAPHPCLLNIQNdvaQTPLH--LAALTAQPNIMRILLLAGAEPTVRDRHGN 300
Cdd:PHA03095 113 KDKVGRTPLH-VYLSGfniNPKVIRLLLRKGADVNALDLYG---MTPLAvlLKSRNANVELLRLLIDAGADVYAVDDRFR 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136842  301 TALHLSC--IAGEKQCVRALTEK---------FGATEIHEAHRQyghrSNDKAVSSLSYACLPADLEIRNYDGERCVHLA 369
Cdd:PHA03095 189 SLLHHHLqsFKPRARIVRELIRAgcdpaatdmLGNTPLHSMATG----SSCKRSLVLPLLIAGISINARNRYGQTPLHYA 264
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17136842  370 AEAGHIDILRILVSHGADINAREgKSGRTPLHIAIEGCNEDLANFLLDECEKLNLETATYAGLTAYQFACIMNKSRM 446
Cdd:PHA03095 265 AVFNNPRACRRLIALGADINAVS-SDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAATLNTASVAGGDIPSDATRL 340
Ank_4 pfam13637
Ankyrin repeats (many copies);
364-416 3.16e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.44  E-value: 3.16e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 17136842   364 RCVHLAAEAGHIDILRILVSHGADINAREGkSGRTPLHIAIEGCNEDLANFLL 416
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDG-NGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
264-440 1.96e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 62.98  E-value: 1.96e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136842  264 DVAQTPLHLAALTAQPNIMRILLLAGAEPTVRDRHGNTALHLSCIAGEKQCVRALTekfgateiheahrQYGhrsndkav 343
Cdd:PHA02878 166 HKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILL-------------ENG-------- 224
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136842  344 sslsyaclpADLEIRNYDGERCVHLA-AEAGHIDILRILVSHGADINAREGKSGRTPLHIAIEgcNEDLANFLLD---EC 419
Cdd:PHA02878 225 ---------ASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSYILGLTALHSSIK--SERKLKLLLEygaDI 293
                        170       180
                 ....*....|....*....|.
gi 17136842  420 EKLNLETATYAGLTAYQFACI 440
Cdd:PHA02878 294 NSLNSYKLTPLSSAVKQYLCI 314
PHA02874 PHA02874
ankyrin repeat protein; Provisional
226-422 2.33e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 62.29  E-value: 2.33e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136842  226 QNDDGDTPLHLACISGSVDVVAALIRMAPHpclLNIQNDVAQTPLHLAALTAQPNIMRILLLAGAEPTVRDRHGNTALHL 305
Cdd:PHA02874 120 KDAELKTFLHYAIKKGDLESIKMLFEYGAD---VNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHN 196
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136842  306 SCIAGEKQCVRALTE---------KFGATEIHEAHRQyghrsNDKAVSSLSYAclpADLEIRNYDGERCVHLAAE-AGHI 375
Cdd:PHA02874 197 AAEYGDYACIKLLIDhgnhimnkcKNGFTPLHNAIIH-----NRSAIELLINN---ASINDQDIDGSTPLHHAINpPCDI 268
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 17136842  376 DILRILVSHGADINAREGKsGRTPLHIAIEGCNED------LAN-FLLDECEKL 422
Cdd:PHA02874 269 DIIDILLYHKADISIKDNK-GENPIDTAFKYINKDpvikdiIANaVLIKEADKL 321
PHA02875 PHA02875
ankyrin repeat protein; Provisional
229-389 6.87e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 60.78  E-value: 6.87e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136842  229 DGDTPLHLACISGSVDVVAALIRMAPHPcllniqNDV----AQTPLHLAALTAQPNIMRILLLAGAEPTVRDRHGNTALH 304
Cdd:PHA02875  67 DIESELHDAVEEGDVKAVEELLDLGKFA------DDVfykdGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLH 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136842  305 LSCIAGEKQCVRALTEKFGATEIHEAhrqYGHrsndkavSSLSYACLPADLEI----------RNYDGER-CVHL---AA 370
Cdd:PHA02875 141 LAVMMGDIKGIELLIDHKACLDIEDC---CGC-------TPLIIAMAKGDIAIckmlldsganIDYFGKNgCVAAlcyAI 210
                        170
                 ....*....|....*....
gi 17136842  371 EAGHIDILRILVSHGADIN 389
Cdd:PHA02875 211 ENNKIDIVRLFIKRGADCN 229
PHA02741 PHA02741
hypothetical protein; Provisional
350-452 9.45e-10

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 57.75  E-value: 9.45e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136842  350 CLPADLEIRNYDGERCVHLAAEAGH----IDILRILVSHGADINAREGKSGRTPLHIAIEGCNEDLANFLLDEcEKLNLE 425
Cdd:PHA02741  48 CHAAALNATDDAGQMCIHIAAEKHEaqlaAEIIDHLIELGADINAQEMLEGDTALHLAAHRRDHDLAEWLCCQ-PGIDLH 126
                         90       100
                 ....*....|....*....|....*..
gi 17136842  426 TATYAGLTAYQFACIMNKSRMQNILEK 452
Cdd:PHA02741 127 FCNADNKSPFELAIDNEDVAMMQILRE 153
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
221-475 6.96e-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: 58.10  E-value: 6.96e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136842 221 EQFYQQNDDG-DTPLHLACISGSVDVVAALIRmAPHpCLLNIQNDVAQTPLHLAALTAQPNIMRILLLAGAE----PTVR 295
Cdd:cd22192   7 ELHLLQQKRIsESPLLLAAKENDVQAIKKLLK-CPS-CDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElvnePMTS 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136842 296 DRH-GNTALHLSCIAGEKQCVRALTEKfGATEIH-EAHRQYGHRSNDKAVsslsyaclpadleirnYDGERCVHLAAEAG 373
Cdd:cd22192  85 DLYqGETALHIAVVNQNLNLVRELIAR-GADVVSpRATGTFFRPGPKNLI----------------YYGEHPLSFAACVG 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136842 374 HIDILRILVSHGADINAREgKSGRTPLHIAIEGCNEDLA----NFLLDECEKLN---LETAT-YAGLTAYQFACIMNKSR 445
Cdd:cd22192 148 NEEIVRLLIEHGADIRAQD-SLGNTVLHILVLQPNKTFAcqmyDLILSYDKEDDlqpLDLVPnNQGLTPFKLAAKEGNIV 226
                       250       260       270
                ....*....|....*....|....*....|....
gi 17136842 446 M-QNILEKRGAE--TVTPPDSD-YDSSDIEDLDD 475
Cdd:cd22192 227 MfQHLVQKRRHIqwTYGPLTSTlYDLTEIDSWGD 260
Ank_5 pfam13857
Ankyrin repeats (many copies);
349-403 5.53e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 49.27  E-value: 5.53e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 17136842   349 ACLPADLEIRNYDGERCVHLAAEAGHIDILRILVSHGADINAREgKSGRTPLHIA 403
Cdd:pfam13857   3 EHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKD-EEGLTALDLA 56
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
218-382 1.08e-07

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: 54.32  E-value: 1.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136842   218 NAWEQFYQQNDD---GDTPLHLACISGSVDVVAALI-RMAPHP-------CLLNIQNDVA---QTPLHLAALTAQPNIMR 283
Cdd:TIGR00870 113 PLELANDQYTSEftpGITALHLAAHRQNYEIVKLLLeRGASVParacgdfFVKSQGVDSFyhgESPLNAAACLGSPSIVA 192
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136842   284 ILLLAGAEPTVRDRHGNTALHLSCIagekqcvraltekfgATEIHEAHRQYGHRSNDKAVSSLSYACLPADLE-IRNYDG 362
Cdd:TIGR00870 193 LLSEDPADILTADSLGNTLLHLLVM---------------ENEFKAEYEELSCQMYNFALSLLDKLRDSKELEvILNHQG 257
                         170       180
                  ....*....|....*....|
gi 17136842   363 ERCVHLAAEAGHIDILRILV 382
Cdd:TIGR00870 258 LTPLKLAAKEGRIVLFRLKL 277
Ank_5 pfam13857
Ankyrin repeats (many copies);
256-305 1.78e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 47.73  E-value: 1.78e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 17136842   256 PCLLNIQNDVAQTPLHLAALTAQPNIMRILLLAGAEPTVRDRHGNTALHL 305
Cdd:pfam13857   6 PIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
PHA02878 PHA02878
ankyrin repeat protein; Provisional
269-423 2.78e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 52.96  E-value: 2.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136842  269 PLHLAALTAQPNIMRILLLAGAEPTVRDRHGNTALHLSCIAGEKQCVRALTekfgateiheahRQYGHRSNDKAVSSLSY 348
Cdd:PHA02878  40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMI------------RSINKCSVFYTLVAIKD 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136842  349 ACLPADLEI------RNYDGERCVHLA-----AEAGHID--ILRILVSHGADINAREGKSGRTPLHIAIEGCNEDLANFL 415
Cdd:PHA02878 108 AFNNRNVEIfkiiltNRYKNIQTIDLVyidkkSKDDIIEaeITKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELL 187

                 ....*...
gi 17136842  416 LDECEKLN 423
Cdd:PHA02878 188 LSYGANVN 195
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
221-460 7.98e-07

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: 51.42  E-value: 7.98e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136842 221 EQFYQQNDDGDTPLHLAcisgsvdvvaalirmaphpcLLNIQNDVAQTPLHLaaLTAQPNIMRILLLAGAEPTVRDRHGN 300
Cdd:cd21882  17 DSAYQRGATGKTCLHKA--------------------ALNLNDGVNEAIMLL--LEAAPDSGNPKELVNAPCTDEFYQGQ 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136842 301 TALHLSCIAGEKQCVRALTEKfGAtEIHEahrqyghRSNDKAVSSLSYACLpadleirnYDGERCVHLAAEAGHIDILRI 380
Cdd:cd21882  75 TALHIAIENRNLNLVRLLVEN-GA-DVSA-------RATGRFFRKSPGNLF--------YFGELPLSLAACTNQEEIVRL 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136842 381 LVSHGADINAREGKS--GRTPLHIAIEGCNEDLAN-----------FLLDE--CEKLNLETAT-YAGLTAYQFACIMNKS 444
Cdd:cd21882 138 LLENGAQPAALEAQDslGNTVLHALVLQADNTPENsafvcqmynllLSYGAhlDPTQQLEEIPnHQGLTPLKLAAVEGKI 217
                       250
                ....*....|....*..
gi 17136842 445 RM-QNILEKRGAETVTP 460
Cdd:cd21882 218 VMfQHILQREFSGPYQP 234
PHA02875 PHA02875
ankyrin repeat protein; Provisional
229-457 8.05e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 51.15  E-value: 8.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136842  229 DGDTPLHLACISGSVDVVAALIRMAPHPcllNIQNDVAQTPLHLAALTAQPNIMRILLLAGA-EPTVRDRHGNTALHLSC 307
Cdd:PHA02875  34 DGISPIKLAMKFRDSEAIKLLMKHGAIP---DVKYPDIESELHDAVEEGDVKAVEELLDLGKfADDVFYKDGMTPLHLAT 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136842  308 IAGEKQCVRALTekfgateiheahrQYGhrsndkavsslsyaclpADLEIRNYDGERCVHLAAEAGHIDILRILVSHGAD 387
Cdd:PHA02875 111 ILKKLDIMKLLI-------------ARG-----------------ADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKAC 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17136842  388 INAREGkSGRTPLHIAIEGCNEDLANFLLDECEKLNletatYAG----LTAYQFACIMNKSRMQNILEKRGAET 457
Cdd:PHA02875 161 LDIEDC-CGCTPLIIAMAKGDIAICKMLLDSGANID-----YFGkngcVAALCYAIENNKIDIVRLFIKRGADC 228
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
191-324 8.52e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.44  E-value: 8.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136842  191 STASTANANPSGSGATSS----APPSSINIMNAWEQFYQQNDDgdtplHLACISGSVDVVAAlirmAPHPclLNIQNDVA 266
Cdd:PTZ00322   7 SVASSAFAAQLFFGTEGSrkrrAKPISFERMAAIQEEIARIDT-----HLEALEATENKDAT----PDHN--LTTEEVID 75
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17136842  267 QTPLH-----LAALTAQPNIM--RILLLAGAEPTVRDRHGNTALHLSCIAGEKQCVRALTEkFGA 324
Cdd:PTZ00322  76 PVVAHmltveLCQLAASGDAVgaRILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLE-FGA 139
PHA02876 PHA02876
ankyrin repeat protein; Provisional
259-456 1.34e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 50.83  E-value: 1.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136842  259 LNIQNDVAQTPLHLAALTaqPNIMRI---LLLAGAEPTVRDRHGNTALHLSCIAG-EKQCVRAL---------TEKFGAT 325
Cdd:PHA02876 266 VNSIDDCKNTPLHHASQA--PSLSRLvpkLLERGADVNAKNIKGETPLYLMAKNGyDTENIRTLimlgadvnaADRLYIT 343
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136842  326 EIHEAHRQygHRSNDKAVSSLSyacLPADLEIRNYDGERCVHLAAEAGHIDILRILVSHGADINAREGKSGrTPLHIAIE 405
Cdd:PHA02876 344 PLHQASTL--DRNKDIVITLLE---LGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIG-TALHFALC 417
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 17136842  406 GCNEDLA-NFLLDECEKLNLETATYAglTAYQFACIMN-KSRMQNILEKRGAE 456
Cdd:PHA02876 418 GTNPYMSvKTLIDRGANVNSKNKDLS--TPLHYACKKNcKLDVIEMLLDNGAD 468
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
353-419 2.12e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.28  E-value: 2.12e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17136842  353 ADLEIRNYDGERCVHLAAEAGHIDILRILVSHGADINAREgKSGRTPLHIAIEGCNEDLANFLLDEC 419
Cdd:PTZ00322 106 ADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLD-KDGKTPLELAEENGFREVVQLLSRHS 171
PHA02791 PHA02791
ankyrin-like protein; Provisional
224-389 3.78e-06

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 48.50  E-value: 3.78e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136842  224 YQQNDDGDTPLHLACISGSVDVVAALIRMAPHPCLLNiqndvAQTPLHLAALTAQPNIMRILLLAGAEPTVRDRHGNTAL 303
Cdd:PHA02791  24 FKADVHGHSALYYAIADNNVRLVCTLLNAGALKNLLE-----NEFPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTAL 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136842  304 HLSCIAGEKQCVRALTEK------FGATEIHEAHrQYGHRSNDKAVSSLSYACLPADLEIRNYdgERCVHLAAEAGHIDI 377
Cdd:PHA02791  99 YYAVDSGNMQTVKLFVKKnwrlmfYGKTGWKTSF-YHAVMLNDVSIVSYFLSEIPSTFDLAIL--LSCIHITIKNGHVDM 175
                        170
                 ....*....|..
gi 17136842  378 LRILVSHGADIN 389
Cdd:PHA02791 176 MILLLDYMTSTN 187
PHA02874 PHA02874
ankyrin repeat protein; Provisional
233-404 4.17e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 49.19  E-value: 4.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136842  233 PLHLACISGSVDVVAALI------RMAPHPCL--------------LNIQNDVAQTPLHLAALTAQPNIMRILLLAGAEP 292
Cdd:PHA02874  71 PLLTAIKIGAHDIIKLLIdngvdtSILPIPCIekdmiktildcgidVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADV 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136842  293 TVRDRHGNTALHLSCIAGEKQCVRALTEKfgateiheahrqyghrsndkavsslsyaclPADLEIRNYDGERCVHLAAEA 372
Cdd:PHA02874 151 NIEDDNGCYPIHIAIKHNFFDIIKLLLEK------------------------------GAYANVKDNNGESPLHNAAEY 200
                        170       180       190
                 ....*....|....*....|....*....|..
gi 17136842  373 GHIDILRILVSHGADINAReGKSGRTPLHIAI 404
Cdd:PHA02874 201 GDYACIKLLIDHGNHIMNK-CKNGFTPLHNAI 231
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
267-390 5.61e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 49.10  E-value: 5.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136842  267 QTPLHLAALTAQPNIMRILLLAGAEPTVRDRHGNTALHLSCIAGEKQCVRALTEKFGATEIHEAHR---QYGHRSNDKAV 343
Cdd:PLN03192 559 RTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAGDllcTAAKRNDLTAM 638
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 17136842  344 SSLSYACLPADLEirNYDGERCVHLAAEAGHIDILRILVSHGADINA 390
Cdd:PLN03192 639 KELLKQGLNVDSE--DHQGATALQVAMAEDHVDMVRLLIMNGADVDK 683
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
361-390 6.38e-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: 42.57  E-value: 6.38e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 17136842    361 DGERCVHLAAEAGHIDILRILVSHGADINA 390
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
267-383 3.62e-05

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 46.29  E-value: 3.62e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136842 267 QTPLHLAALTAQPNIMRILLLAGAEP-TVRDRHGNTALHlsciagekqcvrALTEkfgATEIHEAHRQYGHRSNDKAVSs 345
Cdd:cd22194 189 ETPLALAACTNQPEIVQLLMEKESTDiTSQDSRGNTVLH------------ALVT---VAEDSKTQNDFVKRMYDMILL- 252
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 17136842 346 lsyACLPADLE-IRNYDGERCVHLAAEAGHIDILRILVS 383
Cdd:cd22194 253 ---KSENKNLEtIRNNEGLTPLQLAAKMGKAEILKYILS 288
PHA02875 PHA02875
ankyrin repeat protein; Provisional
227-324 4.28e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 45.75  E-value: 4.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136842  227 NDDGDTPLHLACISGSVDVVAALIRmapHPCLLNIQNDVAQTPLHLAALTAQPNIMRILLLAGAEPTVRDRHGNTALHLS 306
Cdd:PHA02875 132 NTDKFSPLHLAVMMGDIKGIELLID---HKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCY 208
                         90
                 ....*....|....*...
gi 17136842  307 CIAGEKQCVRALTEKFGA 324
Cdd:PHA02875 209 AIENNKIDIVRLFIKRGA 226
Ank_4 pfam13637
Ankyrin repeats (many copies);
230-286 5.07e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 40.72  E-value: 5.07e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 17136842   230 GDTPLHLACISGSVDVVAALIrmaPHPCLLNIQNDVAQTPLHLAALTAQPNIMRILL 286
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLL---EKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
273-416 6.33e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 45.63  E-value: 6.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136842  273 AALTAQPNIMRILLLAGAEPTVRDRHGNTALHLSCIAGEKQCVRALTEKFGATEIHEAHrqyGHRSNDKAVSS------- 345
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDAN---GNTALWNAISAkhhkifr 608
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17136842  346 LSYACLPADleiRNYDGERCVHLAAEAGHIDILRILVSHGADINArEGKSGRTPLHIAIEGCNEDLANFLL 416
Cdd:PLN03192 609 ILYHFASIS---DPHAAGDLLCTAAKRNDLTAMKELLKQGLNVDS-EDHQGATALQVAMAEDHVDMVRLLI 675
Ank_4 pfam13637
Ankyrin repeats (many copies);
268-318 7.22e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 40.34  E-value: 7.22e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 17136842   268 TPLHLAALTAQPNIMRILLLAGAEPTVRDRHGNTALHLSCIAGEKQCVRAL 318
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PHA03100 PHA03100
ankyrin repeat protein; Provisional
227-327 7.32e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 45.04  E-value: 7.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136842  227 NDDGDTPLHLA--CISGSVDVVAALI-------------RMAPHPCLLNIQNDVAQTPLHLAALTAQPNIMRILLLAGAE 291
Cdd:PHA03100 138 NSDGENLLHLYleSNKIDLKILKLLIdkgvdinaknrvnYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGAN 217
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 17136842  292 PTVRDRHGNTALHLSCIAGEKQCVRALTEKFGATEI 327
Cdd:PHA03100 218 PNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
361-391 1.23e-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: 1.23e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 17136842   361 DGERCVHLAAE-AGHIDILRILVSHGADINAR 391
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNAR 32
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
264-452 1.38e-04

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: 44.36  E-value: 1.38e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136842 264 DVAQTPLHLAALTAQPN---IMRILL-----------LAGAEPTVRDRHGNTALHlscIAGEKQC---VRALTEKFGATE 326
Cdd:cd22194  92 DTGKTCLMKALLNINENtkeIVRILLafaeengildrFINAEYTEEAYEGQTALN---IAIERRQgdiVKLLIAKGADVN 168
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136842 327 IHEAHRQYGHRSNDKAVsslsyaclpadleirnYDGERCVHLAAEAGHIDILRILVSHGADINAREGKSGRTPLHiAIEG 406
Cdd:cd22194 169 AHAKGVFFNPKYKHEGF----------------YFGETPLALAACTNQPEIVQLLMEKESTDITSQDSRGNTVLH-ALVT 231
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 17136842 407 CNEDLANF----------LLDECEKLNLETAT-YAGLTAYQFACIMNKSRM-QNILEK 452
Cdd:cd22194 232 VAEDSKTQndfvkrmydmILLKSENKNLETIRnNEGLTPLQLAAKMGKAEIlKYILSR 289
PHA02741 PHA02741
hypothetical protein; Provisional
215-318 2.65e-04

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 41.57  E-value: 2.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136842  215 NIMNAWEQ-FYQQNDDGDTPLHLACISGSVDVVAAL---IRMAPHPCLLNIQNDVAQTPLHLAALTAQP----NIMRILL 286
Cdd:PHA02741   5 HFMTCLEEmIAEKNSEGENFFHEAARCGCFDIIARFtpfIRGDCHAAALNATDDAGQMCIHIAAEKHEAqlaaEIIDHLI 84
                         90       100       110
                 ....*....|....*....|....*....|...
gi 17136842  287 LAGAEPTVRDR-HGNTALHLSCIAGEKQCVRAL 318
Cdd:PHA02741  85 ELGADINAQEMlEGDTALHLAAHRRDHDLAEWL 117
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
361-390 5.77e-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.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.24  E-value: 5.77e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 17136842   361 DGERCVHLAAEAGHIDILRILVSHGADINA 390
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
229-256 5.89e-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.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.24  E-value: 5.89e-04
                          10        20
                  ....*....|....*....|....*...
gi 17136842   229 DGDTPLHLACISGSVDVVAALIRMAPHP 256
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADI 28
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
229-251 6.05e-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: 37.18  E-value: 6.05e-04
                           10        20
                   ....*....|....*....|...
gi 17136842    229 DGDTPLHLACISGSVDVVAALIR 251
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLD 23
Ank_5 pfam13857
Ankyrin repeats (many copies);
226-273 1.17e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.94  E-value: 1.17e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 17136842   226 QNDDGDTPLHLACISGSVDVVAALIRmapHPCLLNIQNDVAQTPLHLA 273
Cdd:pfam13857  12 LDGEGYTPLHVAAKYGALEIVRVLLA---YGVDLNLKDEEGLTALDLA 56
PHA02876 PHA02876
ankyrin repeat protein; Provisional
226-405 2.09e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 40.82  E-value: 2.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136842  226 QNDDGDTPLHLACISG-SVDVVAALIRMAPHpclLNIQNDVAQTPLHLAA-LTAQPNIMRILLLAGAEPTVRDRHGNTAL 303
Cdd:PHA02876 303 KNIKGETPLYLMAKNGyDTENIRTLIMLGAD---VNAADRLYITPLHQAStLDRNKDIVITLLELGANVNARDYCDKTPI 379
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136842  304 HLSCIAGEKQCVRALTEkFGAtEIHEAHRQYGHRSNDKAVSSLSYACLP------ADLEIRNYDGERCVHLAAEAG-HID 376
Cdd:PHA02876 380 HYAAVRNNVVIINTLLD-YGA-DIEALSQKIGTALHFALCGTNPYMSVKtlidrgANVNSKNKDLSTPLHYACKKNcKLD 457
                        170       180
                 ....*....|....*....|....*....
gi 17136842  377 ILRILVSHGADINAREGKSgRTPLHIAIE 405
Cdd:PHA02876 458 VIEMLLDNGADVNAINIQN-QYPLLIALE 485
PHA02874 PHA02874
ankyrin repeat protein; Provisional
228-425 2.60e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 40.33  E-value: 2.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136842  228 DDGDTPLHLACISGSVDVVAALIRmapHPCLLNIQNDVAQTPLHLAALTAQPNIMRILLLAGAEPTVrdrhgntaLHLSC 307
Cdd:PHA02874  33 DETTTPLIDAIRSGDAKIVELFIK---HGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSI--------LPIPC 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136842  308 IagEKQCVRALTEKfgateiheahrqyghrsndkavsslsyaclPADLEIRNYDGERCVHLAAEAGHIDILRILVSHGAD 387
Cdd:PHA02874 102 I--EKDMIKTILDC------------------------------GIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGAD 149
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 17136842  388 INArEGKSGRTPLHIAIEGCNEDLANFLLDECEKLNLE 425
Cdd:PHA02874 150 VNI-EDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVK 186
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
396-424 2.72e-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: 35.26  E-value: 2.72e-03
                           10        20
                   ....*....|....*....|....*....
gi 17136842    396 GRTPLHIAIEGCNEDLANFLLDECEKLNL 424
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
381-438 3.32e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.79  E-value: 3.32e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 17136842   381 LVSHG-ADINAREGKsGRTPLHIAIEGCNEDLANFLLDECEKLNLETAtyAGLTAYQFA 438
Cdd:pfam13857   1 LLEHGpIDLNRLDGE-GYTPLHVAAKYGALEIVRVLLAYGVDLNLKDE--EGLTALDLA 56
PHA03095 PHA03095
ankyrin-like protein; Provisional
359-417 3.43e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 39.62  E-value: 3.43e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17136842  359 NYDGER-------CVHLAAEAGhIDILRILVSHGADINAREgKSGRTPLHIAIE-GCNEDLANFLLD 417
Cdd:PHA03095  41 NFRGEYgktplhlYLHYSSEKV-KDIVRLLLEAGADVNAPE-RCGFTPLHLYLYnATTLDVIKLLIK 105
Ank_4 pfam13637
Ankyrin repeats (many copies);
325-382 5.45e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 34.94  E-value: 5.45e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 17136842   325 TEIHEAHrqygHRSNDKAVSSLsyACLPADLEIRNYDGERCVHLAAEAGHIDILRILV 382
Cdd:pfam13637   3 TALHAAA----ASGHLELLRLL--LEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
267-297 6.00e-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: 34.57  E-value: 6.00e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 17136842   267 QTPLHLAALTA-QPNIMRILLLAGAEPTVRDR 297
Cdd:pfam00023   3 NTPLHLAAGRRgNLEIVKLLLSKGADVNARDK 34
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
229-286 6.16e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 39.11  E-value: 6.16e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 17136842  229 DGDTPLHLACISGSVDVVAALIRMAPHPCLLNIQNdvaQTPLHLAALTAQPNIMRILL 286
Cdd:PTZ00322 114 DGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDG---KTPLELAEENGFREVVQLLS 168
PHA02946 PHA02946
ankyin-like protein; Provisional
225-405 6.43e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 38.88  E-value: 6.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136842  225 QQNDDGDTPLHLACISGSVDVVAALIRMAPHPCLLNIQNdvaQTPLHLAALTAQPNIMRILLLAGAEPTVR---DRHGNT 301
Cdd:PHA02946  67 ETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQH---KTPLYYLSGTDDEVIERINLLVQYGAKINnsvDEEGCG 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136842  302 ALHLSCIAGEKQCVRALTEKFGATEIHEAHRQYGHR---SNDKAVSSLSYAC-LPADLEIRNYDGERCVHL--AAEAGHI 375
Cdd:PHA02946 144 PLLACTDPSERVFKKIMSIGFEARIVDKFGKNHIHRhlmSDNPKASTISWMMkLGISPSKPDHDGNTPLHIvcSKTVKNV 223
                        170       180       190
                 ....*....|....*....|....*....|
gi 17136842  376 DILRILVShGADINaREGKSGRTPLHIAIE 405
Cdd:PHA02946 224 DIINLLLP-STDVN-KQNKFGDSPLTLLIK 251
PHA02876 PHA02876
ankyrin repeat protein; Provisional
232-438 6.92e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 38.89  E-value: 6.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136842  232 TPLHLACISGSVDVVAALIRMAPHpcLLNIQNDVAQTPLHLAALTaqPNIMRILLLAGAEPTVRDRHGNTALHLSCIAGE 311
Cdd:PHA02876  43 TAIHQALQLRQIDIVEEIIQQNPE--LIYITDHKCHSTLHTICII--PNVMDIVISLTLDCDIILDIKYASIILNKHKLD 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136842  312 KQCVRALTEKFGATEIHEahrqyghrsnDKAVSSLSYAclpadleirnydgeRCVHLAAEAGHIDILRILVSHGADINAR 391
Cdd:PHA02876 119 EACIHILKEAISGNDIHY----------DKINESIEYM--------------KLIKERIQQDELLIAEMLLEGGADVNAK 174
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 17136842  392 EGKSgRTPLHIAIEGCNEDLANFLLDECEKLNLetATYAGLTAYQFA 438
Cdd:PHA02876 175 DIYC-ITPIHYAAERGNAKMVNLLLSYGADVNI--IALDDLSVLECA 218
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
230-439 7.04e-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: 38.91  E-value: 7.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136842   230 GDTPLHLACISGSVDVVAALirmaphpcLLNIQNDVA--QTPLHLAALTAQPN---IMRILL----------LAGAEPTV 294
Cdd:TIGR00870  52 GRSALFVAAIENENLELTEL--------LLNLSCRGAvgDTLLHAISLEYVDAveaILLHLLaafrksgpleLANDQYTS 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136842   295 RDRHGNTALHLSCIAGEKQCVRALTEKfGATEIHEAHRQYGHRSNDkaVSSLSYaclpadleirnydGERCVHLAAEAGH 374
Cdd:TIGR00870 124 EFTPGITALHLAAHRQNYEIVKLLLER-GASVPARACGDFFVKSQG--VDSFYH-------------GESPLNAAACLGS 187
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17136842   375 IDILRILVSHGADINAREgKSGRTPLHIAIE-----GCNEDLA----NFLLDECEKL----NLETAT-YAGLTAYQFAC 439
Cdd:TIGR00870 188 PSIVALLSEDPADILTAD-SLGNTLLHLLVMenefkAEYEELScqmyNFALSLLDKLrdskELEVILnHQGLTPLKLAA 265
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
229-260 7.10e-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: 34.19  E-value: 7.10e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 17136842   229 DGDTPLHLACIS-GSVDVVAALIRMAPHPCLLN 260
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
Ank_4 pfam13637
Ankyrin repeats (many copies);
222-250 7.77e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 34.56  E-value: 7.77e-03
                          10        20
                  ....*....|....*....|....*....
gi 17136842   222 QFYQQNDDGDTPLHLACISGSVDVVAALI 250
Cdd:pfam13637  26 DINAVDGNGETALHFAASNGNVEVLKLLL 54
 
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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