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Conserved domains on  [gi|1498473183|gb|AYO90349|]
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ankyrin repeat protein [Fowlpox virus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PHA02875 PHA02875
ankyrin repeat protein; Provisional
1-410 0e+00

ankyrin repeat protein; Provisional


:

Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 718.70  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183   1 MDRVELCNAILFGELDVARRLLDSYINPNFTI-NGYSPIKMAVRLRDVEMIKLLMSYNTYPDYNYPDIESELHEAVEEGD 79
Cdd:PHA02875    1 MDQVALCDAILFGELDIARRLLDIGINPNFEIyDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183  80 VVKVEELLDSGKFINDVIYKKGNTPLHLATISKNLDMMRLLIARGADTDVPNTDRFTPLHLAVMSKDIKGIELLLDHRAC 159
Cdd:PHA02875   81 VKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKAC 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183 160 TNIEDCYGCTPLIIAMSKGDTEVCRMLLDSGANIDYFSKRPCVTAMCYAIQNNKIDMVSMFLKRGADSNIVFTVMNEEHT 239
Cdd:PHA02875  161 LDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLFIKRGADCNIMFMIEGEECT 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183 240 TLEMICNMDTNPESESVDMLIADIALRQYTNTISSDKGFSRNMTVINSKSRLKDVFEKCKIELRRINSESIRTYNILDLC 319
Cdd:PHA02875  241 ILDMICNMCTNLESEAIDALIADIAIRIHKKTIRRDEGFKNNMSTIEDKEEFKDVFEKCIIELRRIKSEKIGKKNILDLC 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183 320 L--KPSKNLDENILARHSRKILGLYDNAIFYKYLLKELADTASQRAEAIESAMRVIDEKITGDETKWNWLPHEIKYNILE 397
Cdd:PHA02875  321 IleKNSHNLDENILARHSKKILGLNDEAHFYKYLLKEAADIALKRAEAIESAIRVIDDEITGDESKWNILPHEIKYLILE 400
                         410
                  ....*....|...
gi 1498473183 398 YIGNKELDIASMK 410
Cdd:PHA02875  401 KIGNKDIDIAIMK 413
 
Name Accession Description Interval E-value
PHA02875 PHA02875
ankyrin repeat protein; Provisional
1-410 0e+00

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 718.70  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183   1 MDRVELCNAILFGELDVARRLLDSYINPNFTI-NGYSPIKMAVRLRDVEMIKLLMSYNTYPDYNYPDIESELHEAVEEGD 79
Cdd:PHA02875    1 MDQVALCDAILFGELDIARRLLDIGINPNFEIyDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183  80 VVKVEELLDSGKFINDVIYKKGNTPLHLATISKNLDMMRLLIARGADTDVPNTDRFTPLHLAVMSKDIKGIELLLDHRAC 159
Cdd:PHA02875   81 VKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKAC 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183 160 TNIEDCYGCTPLIIAMSKGDTEVCRMLLDSGANIDYFSKRPCVTAMCYAIQNNKIDMVSMFLKRGADSNIVFTVMNEEHT 239
Cdd:PHA02875  161 LDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLFIKRGADCNIMFMIEGEECT 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183 240 TLEMICNMDTNPESESVDMLIADIALRQYTNTISSDKGFSRNMTVINSKSRLKDVFEKCKIELRRINSESIRTYNILDLC 319
Cdd:PHA02875  241 ILDMICNMCTNLESEAIDALIADIAIRIHKKTIRRDEGFKNNMSTIEDKEEFKDVFEKCIIELRRIKSEKIGKKNILDLC 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183 320 L--KPSKNLDENILARHSRKILGLYDNAIFYKYLLKELADTASQRAEAIESAMRVIDEKITGDETKWNWLPHEIKYNILE 397
Cdd:PHA02875  321 IleKNSHNLDENILARHSKKILGLNDEAHFYKYLLKEAADIALKRAEAIESAIRVIDDEITGDESKWNILPHEIKYLILE 400
                         410
                  ....*....|...
gi 1498473183 398 YIGNKELDIASMK 410
Cdd:PHA02875  401 KIGNKDIDIAIMK 413
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
8-229 3.62e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 139.32  E-value: 3.62e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183   8 NAILFGELDVARRLLDSYINPNFTINGYSPIKMAVRLRDVEMIKLLMSYNTYPDYNYPDIESELHEAVEEGDVVKVEELL 87
Cdd:COG0666    28 AALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLL 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183  88 DSGKFINDViYKKGNTPLHLATISKNLDMMRLLIARGADTDVPNTDRFTPLHLAVMSKDIKGIELLLDHRACTNIEDCYG 167
Cdd:COG0666   108 EAGADVNAR-DKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDG 186
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1498473183 168 CTPLIIAMSKGDTEVCRMLLDSGANIDYFSKRPCvTAMCYAIQNNKIDMVSMFLKRGADSNI 229
Cdd:COG0666   187 ETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGK-TALDLAAENGNLEIVKLLLEAGADLNA 247
Ank_2 pfam12796
Ankyrin repeats (3 copies);
105-194 6.92e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 78.23  E-value: 6.92e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183 105 LHLATISKNLDMMRLLIARGADTDVPNTDRFTPLHLAVMSKDIKGIELLLDHRACTNieDCYGCTPLIIAMSKGDTEVCR 184
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLEIVK 78
                          90
                  ....*....|
gi 1498473183 185 MLLDSGANID 194
Cdd:pfam12796  79 LLLEKGADIN 88
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
36-185 3.17e-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: 61.95  E-value: 3.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183  36 SPIKMAVRLRDVEMIKLLMSYNTYpdynypDI-------ESELHEAVEEGDVVKVEELLDSG-KFINDVI----YKkGNT 103
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKCPSC------DLfqrgalgETALHVAALYDNLEAAVVLMEAApELVNEPMtsdlYQ-GET 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183 104 PLHLATISKNLDMMRLLIARGADTDVPntdRFT-----------------PLHLA--VMSKDIkgIELLLDHRACTNIED 164
Cdd:cd22192    92 ALHIAVVNQNLNLVRELIARGADVVSP---RATgtffrpgpknliyygehPLSFAacVGNEEI--VRLLIEHGADIRAQD 166
                         170       180
                  ....*....|....*....|..
gi 1498473183 165 CYGCTPL-IIAMSKGDTEVCRM 185
Cdd:cd22192   167 SLGNTVLhILVLQPNKTFACQM 188
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
6-126 8.44e-05

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 44.69  E-value: 8.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183   6 LCNAILFGELDVARRLLD----SYINPNFTINGYSPIKMAVRLRDVEMIKLLMSYNTYPDYNypdiESELHEAVEEgDVV 81
Cdd:TIGR00870  21 FLPAAERGDLASVYRDLEepkkLNINCPDRLGRSALFVAAIENENLELTELLLNLSCRGAVG----DTLLHAISLE-YVD 95
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1498473183  82 KVEELL----------DSGKFINDVI---YKKGNTPLHLATISKNLDMMRLLIARGAD 126
Cdd:TIGR00870  96 AVEAILlhllaafrksGPLELANDQYtseFTPGITALHLAAHRQNYEIVKLLLERGAS 153
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
166-195 2.57e-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: 37.95  E-value: 2.57e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 1498473183  166 YGCTPLIIAMSKGDTEVCRMLLDSGANIDY 195
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
PHA02875 PHA02875
ankyrin repeat protein; Provisional
1-410 0e+00

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 718.70  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183   1 MDRVELCNAILFGELDVARRLLDSYINPNFTI-NGYSPIKMAVRLRDVEMIKLLMSYNTYPDYNYPDIESELHEAVEEGD 79
Cdd:PHA02875    1 MDQVALCDAILFGELDIARRLLDIGINPNFEIyDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183  80 VVKVEELLDSGKFINDVIYKKGNTPLHLATISKNLDMMRLLIARGADTDVPNTDRFTPLHLAVMSKDIKGIELLLDHRAC 159
Cdd:PHA02875   81 VKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKAC 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183 160 TNIEDCYGCTPLIIAMSKGDTEVCRMLLDSGANIDYFSKRPCVTAMCYAIQNNKIDMVSMFLKRGADSNIVFTVMNEEHT 239
Cdd:PHA02875  161 LDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLFIKRGADCNIMFMIEGEECT 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183 240 TLEMICNMDTNPESESVDMLIADIALRQYTNTISSDKGFSRNMTVINSKSRLKDVFEKCKIELRRINSESIRTYNILDLC 319
Cdd:PHA02875  241 ILDMICNMCTNLESEAIDALIADIAIRIHKKTIRRDEGFKNNMSTIEDKEEFKDVFEKCIIELRRIKSEKIGKKNILDLC 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183 320 L--KPSKNLDENILARHSRKILGLYDNAIFYKYLLKELADTASQRAEAIESAMRVIDEKITGDETKWNWLPHEIKYNILE 397
Cdd:PHA02875  321 IleKNSHNLDENILARHSKKILGLNDEAHFYKYLLKEAADIALKRAEAIESAIRVIDDEITGDESKWNILPHEIKYLILE 400
                         410
                  ....*....|...
gi 1498473183 398 YIGNKELDIASMK 410
Cdd:PHA02875  401 KIGNKDIDIAIMK 413
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
8-229 3.62e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 139.32  E-value: 3.62e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183   8 NAILFGELDVARRLLDSYINPNFTINGYSPIKMAVRLRDVEMIKLLMSYNTYPDYNYPDIESELHEAVEEGDVVKVEELL 87
Cdd:COG0666    28 AALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLL 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183  88 DSGKFINDViYKKGNTPLHLATISKNLDMMRLLIARGADTDVPNTDRFTPLHLAVMSKDIKGIELLLDHRACTNIEDCYG 167
Cdd:COG0666   108 EAGADVNAR-DKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDG 186
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1498473183 168 CTPLIIAMSKGDTEVCRMLLDSGANIDYFSKRPCvTAMCYAIQNNKIDMVSMFLKRGADSNI 229
Cdd:COG0666   187 ETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGK-TALDLAAENGNLEIVKLLLEAGADLNA 247
PHA02878 PHA02878
ankyrin repeat protein; Provisional
33-404 1.04e-35

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 136.93  E-value: 1.04e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183  33 NGYSPIKMAVRLRDVEMIKLLMSYNTYPDYNYPDIESELHEAVEEGDVVKVEELLDSGKFINDVIYKKGNTPLHLATISK 112
Cdd:PHA02878  100 YTLVAIKDAFNNRNVEIFKIILTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDRHKGNTALHYATENK 179
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183 113 NLDMMRLLIARGADTDVPNTDRFTPLHLAVMSKDIKGIELLLDHRACTNIEDCYGCTPLIIAMSK-GDTEVCRMLLDSGA 191
Cdd:PHA02878  180 DQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGV 259
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183 192 NIDYFSKRPCVTAMCYAIQNNkiDMVSMFLKRGADSNIVFTvmnEEHTTLEMIcnMDTNPESESVDMLIADIALRQYTNT 271
Cdd:PHA02878  260 DVNAKSYILGLTALHSSIKSE--RKLKLLLEYGADINSLNS---YKLTPLSSA--VKQYLCINIGRILISNICLLKRIKP 332
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183 272 -ISSDKGFSRNMTVINSKSRLKDVFEKCKIELRRINSESIRTYNILDLCLKPSKNLDENILARHSRKILGLYDNAIFYKY 350
Cdd:PHA02878  333 dIKNSEGFIDNMDCITSNKRLNQIKDKCEDELNRLASIKITNTYSFDDFLKCDNSTLLCKLVNNSIIDDILIDSFNIYGN 412
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1498473183 351 LLKELADTASQRAEAIESAMRVIDEKITGDETK-WNWLPHEIKYNILEYIGNKEL 404
Cdd:PHA02878  413 IIKKNIYRARKRLLLIEGAIYSLDNIFFEKQNYmWNRLPLEIKHYIMELLDDASL 467
PHA03100 PHA03100
ankyrin repeat protein; Provisional
14-404 1.01e-33

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 130.17  E-value: 1.01e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183  14 ELDVARRLLDSYINPNFTINGYS------PIKMAVRLRDVEMIKLLMSYNTYPDYNYPDIESELHEAVEE--GDVVKVEE 85
Cdd:PHA03100   47 NIDVVKILLDNGADINSSTKNNStplhylSNIKYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEY 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183  86 LLDSGKFINDViYKKGNTPLHLATISK--NLDMMRLLIARGADTDVPNTdrftplhlavmskdikgIELLLDHRACTNIE 163
Cdd:PHA03100  127 LLDNGANVNIK-NSDGENLLHLYLESNkiDLKILKLLIDKGVDINAKNR-----------------VNYLLSYGVPINIK 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183 164 DCYGCTPLIIAMSKGDTEVCRMLLDSGANIDYFSKRpCVTAMCYAIQNNKIDMVSMFLKRGADSNIVftvmneeHTTLEM 243
Cdd:PHA03100  189 DVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKY-GDTPLHIAILNNNKEIFKLLLNNGPSIKTI-------IETLLY 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183 244 icNMDTNPESE-SVDMLIADIALrqytnTISSDKGFSRNMTVINSKSRLKDVFEKCKIELRRINSESIRTYNILDLClkp 322
Cdd:PHA03100  261 --FKDKDLNTItKIKMLKKSIMY-----MFLLDPGFYKNRKLIENSKSLKDVINECEKEIERMKEIKLNKVTVYDII--- 330
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183 323 sKNLDENILARHSR-KILGLYDNAIFYKYLLKELADTASQRAEAIESAMRVIDEKITgdETKWNWLPHEIKYNILEYIGN 401
Cdd:PHA03100  331 -FNKNINFLSRYVNnKSVTKYTTSKIYGKYIKKVINKAIERKKLIKKIIKKLNNLCK--NTYWNILPIEIKYKILEYLSN 407

                  ...
gi 1498473183 402 KEL 404
Cdd:PHA03100  408 RDL 410
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
15-270 4.18e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 125.84  E-value: 4.18e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183  15 LDVARRLLDSYINPNFTINGYSPIKMAVRLRDVEMIKLLMSYNTYPDYNYPDIESELHEAVEEGDVVKVEELLDSGKFIN 94
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183  95 DVIYKKGNTPLHLATISKNLDMMRLLIARGADTDVPNTDRFTPLHLAVMSKDIKGIELLLDHRACTNIEDCYGCTPLIIA 174
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183 175 MSKGDTEVCRMLLDSGANIDYFSKRPCvTAMCYAIQNNKIDMVSMFLKRGADSNIvftVMNEEHTTLEMICNMDTNPESE 254
Cdd:COG0666   161 AANGNLEIVKLLLEAGADVNARDNDGE-TPLHLAAENGHLEIVKLLLEAGADVNA---KDNDGKTALDLAAENGNLEIVK 236
                         250
                  ....*....|....*.
gi 1498473183 255 SVDMLIADIALRQYTN 270
Cdd:COG0666   237 LLLEAGADLNAKDKDG 252
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
9-228 1.90e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 123.91  E-value: 1.90e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183   9 AILFGELDVARRLLDSYINPN-FTINGYSPIKMAVRLRDVEMIKLLMSYNTYPDYNYPDIESELHEAVEEGDVVKVEELL 87
Cdd:COG0666    61 AALAGDLLVALLLLAAGADINaKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLL 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183  88 DSGKFINdVIYKKGNTPLHLATISKNLDMMRLLIARGADTDVPNTDRFTPLHLAVMSKDIKGIELLLDHRACTNIEDCYG 167
Cdd:COG0666   141 EAGADVN-AQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDG 219
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1498473183 168 CTPLIIAMSKGDTEVCRMLLDSGANIDYfSKRPCVTAMCYAIQNNKIDMVSMFLKRGADSN 228
Cdd:COG0666   220 KTALDLAAENGNLEIVKLLLEAGADLNA-KDKDGLTALLLAAAAGAALIVKLLLLALLLLA 279
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
6-195 5.71e-26

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 106.19  E-value: 5.71e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183   6 LCNAILFGELDVARRLLDSYINPNFT-INGYSPIKMAVRLRDVEMIKLLMSYNTYPDYNYPDIESELHEAVEEGDVVKVE 84
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGADVNARdKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183  85 ELLDSGKFINdVIYKKGNTPLHLATISKNLDMMRLLIARGADTDVPNTDRFTPLHLAVMSKDIKGIELLLDHRACTNIED 164
Cdd:COG0666   171 LLLEAGADVN-ARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKD 249
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1498473183 165 CYGCTPLIIAMSKGDTEVCRMLLDSGANIDY 195
Cdd:COG0666   250 KDGLTALLLAAAAGAALIVKLLLLALLLLAA 280
Ank_2 pfam12796
Ankyrin repeats (3 copies);
105-194 6.92e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 78.23  E-value: 6.92e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183 105 LHLATISKNLDMMRLLIARGADTDVPNTDRFTPLHLAVMSKDIKGIELLLDHRACTNieDCYGCTPLIIAMSKGDTEVCR 184
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLEIVK 78
                          90
                  ....*....|
gi 1498473183 185 MLLDSGANID 194
Cdd:pfam12796  79 LLLEKGADIN 88
PHA02876 PHA02876
ankyrin repeat protein; Provisional
15-404 2.13e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 84.34  E-value: 2.13e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183  15 LDVARRLLDSYINPNftINGYSPIKmAVRLRDVEMIKLL----MSYNTYPDYNypdiESELHEAVEEGDVVK-VEELLDS 89
Cdd:PHA02876  224 IDTIKAIIDNRSNIN--KNDLSLLK-AIRNEDLETSLLLydagFSVNSIDDCK----NTPLHHASQAPSLSRlVPKLLER 296
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183  90 GKFINdVIYKKGNTPLHL-ATISKNLDMMRLLIARGADTDVPNTDRFTPLHLAVMSKDIKGIEL-LLDHRACTNIEDCYG 167
Cdd:PHA02876  297 GADVN-AKNIKGETPLYLmAKNGYDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKDIVItLLELGANVNARDYCD 375
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183 168 CTPLIIAMSKGDTEVCRMLLDSGANIDYFSKR---------------------------------PCVTAMCYAIQNN-K 213
Cdd:PHA02876  376 KTPIHYAAVRNNVVIINTLLDYGADIEALSQKigtalhfalcgtnpymsvktlidrganvnsknkDLSTPLHYACKKNcK 455
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183 214 IDMVSMFLKRGADSNIV-------FTVMNEEHTTLEM------------ICNMDTNPESESVDMLIADIALRQYT----- 269
Cdd:PHA02876  456 LDVIEMLLDNGADVNAIniqnqypLLIALEYHGIVNIllhygaelrdsrVLHKSLNDNMFSFRYIIAHICIQDFIrhdir 535
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183 270 NTISSDKGFSRNMT--------VINSKSRLKDVFEKCKIELRRINSESIRTYNILDLCLKpSKNLdeNILARH-SRKILG 340
Cdd:PHA02876  536 NEVNPLKRVPTRFTslresfkeIIQSDDTFKRIWLRCKEELKDISKIRINMFYSLDIFII-SKNM--NLLHHLvNNPIIK 612
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1498473183 341 LYDNAIFYKY--LLKELADTASQRAEAIESAMRVIDEKItgDETKWNWLPHEIKYNILEYIGNKEL 404
Cdd:PHA02876  613 EINTWHFCNYgdRLKTSISLASDRHEILEKSRSKLDEIL--DSSDWSKLPPDIKLSILEFIDNNEL 676
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
6-171 2.88e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 81.54  E-value: 2.88e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183   6 LCNAILFGELDVARRLLDSYINPNFT-INGYSPIKMAVRLRDVEMIKLLMSYNTYPDYNYPDIESELHEAVEEGDVVKVE 84
Cdd:COG0666   124 LHLAAYNGNLEIVKLLLEAGADVNAQdNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVK 203
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183  85 ELLDSGKFINdVIYKKGNTPLHLATISKNLDMMRLLIARGADTDVPNTDRFTPLHLAVMSKDIKGIELLLDHRACTNIED 164
Cdd:COG0666   204 LLLEAGADVN-AKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282

                  ....*..
gi 1498473183 165 CYGCTPL 171
Cdd:COG0666   283 LDLLTLL 289
PRANC pfam09372
PRANC domain; This presumed domain is found at the C-terminus of a variety of Pox virus ...
311-406 1.76e-15

PRANC domain; This presumed domain is found at the C-terminus of a variety of Pox virus proteins. The PRANC (Pox proteins Repeats of ANkyrin - C terminal) domain is also found on its own in some proteins. The function of this domain is unknown, but it appears to be related to the F-box domain and may play a similar role.


Pssm-ID: 286461 [Multi-domain]  Cd Length: 95  Bit Score: 71.51  E-value: 1.76e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183 311 RTYNILDLCL-KPSKNLDENILARHSRKIlglYDNAIFYKYLLKELADTASQRAEAIESAMRVIDEKITGDeTKWNWLPH 389
Cdd:pfam09372   1 DNVSLYDILFnKNNINILVRYVNNDSLIK---LKSFPIYGDIIKKIIKSSKERYKLINKAIDVLNNICSNN-SLWNLLPI 76
                          90
                  ....*....|....*..
gi 1498473183 390 EIKYNILEYIGNKELDI 406
Cdd:pfam09372  77 EIKYNILEYLNDDDLKN 93
Ank_2 pfam12796
Ankyrin repeats (3 copies);
71-164 8.75e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 69.37  E-value: 8.75e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183  71 LHEAVEEGDVVKVEELLDSGKFINdVIYKKGNTPLHLATISKNLDMMRLLIARgADTDVpNTDRFTPLHLAVMSKDIKGI 150
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADAN-LQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNL-KDNGRTALHYAARSGHLEIV 77
                          90
                  ....*....|....
gi 1498473183 151 ELLLDHRACTNIED 164
Cdd:pfam12796  78 KLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
79-404 1.26e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 75.45  E-value: 1.26e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183  79 DVVKVeeLLDSGKFINdVIYKKGNTPLHLATISKN-LDMMRLLIARGADTDVPNTDRFTPLH--LAVMSKDIKGIELLLD 155
Cdd:PHA03095   64 DIVRL--LLEAGADVN-APERCGFTPLHLYLYNATtLDVIKLLIKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLR 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183 156 HRACTNIEDCYGCTPLIIAMSKG--DTEVCRMLLDSGANI---------------DYFSKRPCV---------------- 202
Cdd:PHA03095  141 KGADVNALDLYGMTPLAVLLKSRnaNVELLRLLIDAGADVyavddrfrsllhhhlQSFKPRARIvreliragcdpaatdm 220
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183 203 ---TAMCYA----------IQNNKIDMVSM-------------------------FLKRGADSNIV---------FTVMN 235
Cdd:PHA03095  221 lgnTPLHSMatgssckrslVLPLLIAGISInarnrygqtplhyaavfnnpracrrLIALGADINAVssdgntplsLMVRN 300
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183 236 EEHTTLEMIcnMDTNPESESVDMLIAdiALRQYTNTISSDKGFSRNMTVI----------NSKSRLKDVFEKCKIELRRI 305
Cdd:PHA03095  301 NNGRAVRAA--LAKNPSAETVAATLN--TASVAGGDIPSDATRLCVAKVVlrgafsllpePIRAYHADFIRECEAEIAVM 376
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183 306 NSESIRT----YNILdlclkpsknLDENILARH-SRKILGLYDNAIFYKYLLKELADTASQRAEAIESAMRVIDekitgd 380
Cdd:PHA03095  377 RTTRIGTgvslLDIL---------FARNPDILLvSNASLRKKARLTVYGKALRARIEEMRKRSKLVERIIKLIC------ 441
                         410       420
                  ....*....|....*....|....
gi 1498473183 381 etkWNWLPHEIKYNILEYIGNKEL 404
Cdd:PHA03095  442 ---PCALPPEIVMRILDFLPDDDL 462
Ank_2 pfam12796
Ankyrin repeats (3 copies);
138-229 8.54e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 66.68  E-value: 8.54e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183 138 LHLAVMSKDIKGIELLLDHRACTNIEDCYGCTPLIIAMSKGDTEVCRMLLDSgANIDYFSKRpcVTAMCYAIQNNKIDMV 217
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNG--RTALHYAARSGHLEIV 77
                          90
                  ....*....|..
gi 1498473183 218 SMFLKRGADSNI 229
Cdd:pfam12796  78 KLLLEKGADINV 89
PHA03095 PHA03095
ankyrin-like protein; Provisional
68-246 1.30e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 68.90  E-value: 1.30e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183  68 ESELHEAVEEGDVVKVEELLDSGKFINDVIYKK--GNTPLHL---ATISKNLDMMRLLIARGADTDVPNTDRFTPLHLAV 142
Cdd:PHA03095   12 EAALYDYLLNASNVTVEEVRRLLAAGADVNFRGeyGKTPLHLylhYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183 143 MSKD-IKGIELLLDHRACTNIEDCYGCTPLIIAMS--KGDTEVCRMLLDSGANIDYFSKRPCVTAMCYAIQNN-KIDMVS 218
Cdd:PHA03095   92 YNATtLDVIKLLIKAGADVNAKDKVGRTPLHVYLSgfNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNaNVELLR 171
                         170       180
                  ....*....|....*....|....*...
gi 1498473183 219 MFLKRGADsniVFTVMNEEHTTLEMICN 246
Cdd:PHA03095  172 LLIDAGAD---VYAVDDRFRSLLHHHLQ 196
PHA02874 PHA02874
ankyrin repeat protein; Provisional
6-364 3.23e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 64.60  E-value: 3.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183   6 LCNAILFGELDVARRLLDSYINPN-FTINGYSPIKMAVRLRDVEMIKLLMSYNTYPD-YNYPDIESELheaveegdvvkV 83
Cdd:PHA02874   39 LIDAIRSGDAKIVELFIKHGADINhINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSiLPIPCIEKDM-----------I 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183  84 EELLDSGKFINdVIYKKGNTPLHLATISKNLDMMRLLIARGADTDVPNTDRFTPLHLAVMSKDIKGIELLLDHRACTNIE 163
Cdd:PHA02874  108 KTILDCGIDVN-IKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVK 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183 164 DCYGCTPLIIAMSKGDTEVCRMLLDSGANIDYFSKRPcVTAMCYAIQNNKiDMVSMFLKRGADSNIVFTVMNEEHTTLEM 243
Cdd:PHA02874  187 DNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNG-FTPLHNAIIHNR-SAIELLINNASINDQDIDGSTPLHHAINP 264
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183 244 ICNMDTnpesesVDMLI---ADIALR------------QYTNTISSDKGFSRNMTVINSKSRLKD--VFEKCKIELRRIN 306
Cdd:PHA02874  265 PCDIDI------IDILLyhkADISIKdnkgenpidtafKYINKDPVIKDIIANAVLIKEADKLKDsdFLEHIEIKDNKEF 338
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183 307 SESIR----------------TYNILDLCL----------KPSKNLDENILARHSRKILGLYDNA---IFYKYLLKELAD 357
Cdd:PHA02874  339 SDFIKecneeiedmkktkcgcDKNIFDLCLirikhkfdgnEDSIKDYLNCLDDNSHRMLKTIDINefpIYSMYISRCISD 418

                  ....*..
gi 1498473183 358 TASQRAE 364
Cdd:PHA02874  419 NGKILKD 425
Ank_2 pfam12796
Ankyrin repeats (3 copies);
40-131 6.30e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 58.59  E-value: 6.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183  40 MAVRLRDVEMIKLLMSYNTYPDYNYPDIESELHEAVEEGDVVKVEELLDSGKfINDVIYkkGNTPLHLATISKNLDMMRL 119
Cdd:pfam12796   3 LAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD-VNLKDN--GRTALHYAARSGHLEIVKL 79
                          90
                  ....*....|..
gi 1498473183 120 LIARGADTDVPN 131
Cdd:pfam12796  80 LLEKGADINVKD 91
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
36-185 3.17e-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: 61.95  E-value: 3.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183  36 SPIKMAVRLRDVEMIKLLMSYNTYpdynypDI-------ESELHEAVEEGDVVKVEELLDSG-KFINDVI----YKkGNT 103
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKCPSC------DLfqrgalgETALHVAALYDNLEAAVVLMEAApELVNEPMtsdlYQ-GET 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183 104 PLHLATISKNLDMMRLLIARGADTDVPntdRFT-----------------PLHLA--VMSKDIkgIELLLDHRACTNIED 164
Cdd:cd22192    92 ALHIAVVNQNLNLVRELIARGADVVSP---RATgtffrpgpknliyygehPLSFAacVGNEEI--VRLLIEHGADIRAQD 166
                         170       180
                  ....*....|....*....|..
gi 1498473183 165 CYGCTPL-IIAMSKGDTEVCRM 185
Cdd:cd22192   167 SLGNTVLhILVLQPNKTFACQM 188
PHA02876 PHA02876
ankyrin repeat protein; Provisional
71-228 1.88e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 59.69  E-value: 1.88e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183  71 LHEAVEEGDVVKVEELLDSGKFIN-DVIYKKgnTPLHLATISKNLDMMRLLIARGADTDVPNTDRFTPLHLAVMSKDIKG 149
Cdd:PHA02876  149 IKERIQQDELLIAEMLLEGGADVNaKDIYCI--TPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDT 226
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183 150 IELLLDHRACTNIEDcygcTPLIIAMSKGDTEVCRMLLDSG---ANIDYFSKRPcvtaMCYAIQNNKID-MVSMFLKRGA 225
Cdd:PHA02876  227 IKAIIDNRSNINKND----LSLLKAIRNEDLETSLLLYDAGfsvNSIDDCKNTP----LHHASQAPSLSrLVPKLLERGA 298

                  ...
gi 1498473183 226 DSN 228
Cdd:PHA02876  299 DVN 301
PHA02989 PHA02989
ankyrin repeat protein; Provisional
21-406 2.20e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 52.82  E-value: 2.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183  21 LLDSYINPNF-TINGYSPIKMAV---RLRDVEMIKLLMSYNTypdyNYPDIESE-----LHEAVEEGDVVK--VEELLDS 89
Cdd:PHA02989   94 LLKFGADINLkTFNGVSPIVCFIynsNINNCDMLRFLLSKGI----NVNDVKNSrgynlLHMYLESFSVKKdvIKILLSF 169
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183  90 GKFINDVIYKKGNTPLHL---ATISK-NLDMMRLLIARGADTDVPNT------DRFTPLHLAVMSKDIKGIELLLDHRAc 159
Cdd:PHA02989  170 GVNLFEKTSLYGLTPMNIylrNDIDViSIKVIKYLIKKGVNIETNNNgsesvlESFLDNNKILSKKEFKVLNFILKYIK- 248
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183 160 TNIEDCYGCTPLIIAMSKGDTEVCRMLLDSGANIDYFSKRPcVTAMCYAIQNNKIDMVSMFLKRGADSNIVFTVMN--EE 237
Cdd:PHA02989  249 INKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDG-DTVLTYAIKHGNIDMLNRILQLKPGKYLIKKTFEyfSE 327
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183 238 HTTLEMICNMdtnpesESVDMLIAdiaLRQYTNTISSDkgFSRNmtVINSKSRLKDVFEKCKIELRRINSESI-RTYNIL 316
Cdd:PHA02989  328 HGINDLFFNE------KKMLMMIL---LMQYSFTIYPI--FYKN--CYEVRLAFPNIIERYEKDLLLMKKETVgKNLSVY 394
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183 317 DLCLKPSKNLDENILARHsrKILGLYDNAIFYKYLLKELADTASQRAEAIESAMRVIdEKITGDETKWNWLPHEIKYNIL 396
Cdd:PHA02989  395 DLVFNREKEIIPVKFLKN--ENFLKFKSSILYGEKIKQIILNSYEYYNCLNKAIDVL-NKYCNKKNYWMYLPIEIQINIL 471
                         410
                  ....*....|
gi 1498473183 397 EYIGNKELDI 406
Cdd:PHA02989  472 EYLTFSDFKT 481
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
70-159 2.21e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.98  E-value: 2.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183  70 ELHEAVEEGDVVKVEELLDSGKFINDVIYKkGNTPLHLATISKNLDMMRLLIARGADTDVPNTDRFTPLHLAVMSKDIKG 149
Cdd:PTZ00322   85 ELCQLAASGDAVGARILLTGGADPNCRDYD-GRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREV 163
                          90
                  ....*....|
gi 1498473183 150 IELLLDHRAC 159
Cdd:PTZ00322  164 VQLLSRHSQC 173
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
38-226 2.66e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 52.95  E-value: 2.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183  38 IKMAVRLRDVEMIKLLMSyNTYPDYNyPDIESELHEAVEEGDVVKVEELLDSGKfINDVIYKKGNTPLHLATISKNLDMM 117
Cdd:PLN03192  498 LQHHKELHDLNVGDLLGD-NGGEHDD-PNMASNLLTVASTGNAALLEELLKAKL-DPDIGDSKGRTPLHIAASKGYEDCV 574
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183 118 RLLIARGADTDVPNTDRFTPLHLAVMSKDIKgIELLLDHraCTNIEDCY-GCTPLIIAMSKGDTEVCRMLLDSGANIDYf 196
Cdd:PLN03192  575 LVLLKHACNVHIRDANGNTALWNAISAKHHK-IFRILYH--FASISDPHaAGDLLCTAAKRNDLTAMKELLKQGLNVDS- 650
                         170       180       190
                  ....*....|....*....|....*....|
gi 1498473183 197 SKRPCVTAMCYAIQNNKIDMVSMFLKRGAD 226
Cdd:PLN03192  651 EDHQGATALQVAMAEDHVDMVRLLIMNGAD 680
Ank_4 pfam13637
Ankyrin repeats (many copies);
101-154 7.90e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.73  E-value: 7.90e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1498473183 101 GNTPLHLATISKNLDMMRLLIARGADTDVPNTDRFTPLHLAVMSKDIKGIELLL 154
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
70-229 1.05e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 50.35  E-value: 1.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183  70 ELHEAVEEGDVVKVEELLDS-GKFINdVIYKKGNTPLHLATISKNLDMMRLLIARGADTDVPNTDRFTPLHLAVMSKDIK 148
Cdd:PHA02874    4 DLRMCIYSGDIEAIEKIIKNkGNCIN-ISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183 149 GIELLLDHractniedcyGCTPLIIAMSKGDTEVCRMLLDSGANIDyFSKRPCVTAMCYAIQNNKIDMVSMFLKRGADSN 228
Cdd:PHA02874   83 IIKLLIDN----------GVDTSILPIPCIEKDMIKTILDCGIDVN-IKDAELKTFLHYAIKKGDLESIKMLFEYGADVN 151

                  .
gi 1498473183 229 I 229
Cdd:PHA02874  152 I 152
PHA03095 PHA03095
ankyrin-like protein; Provisional
146-251 1.29e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 50.41  E-value: 1.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183 146 DIKGIELLLDHRACTNIEDCYGCTPLIIAMSKG---DTEVCRMLLDSGANIDYFSKRPCVTAMCYAIQNNKIDMVSMFLK 222
Cdd:PHA03095   26 TVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSsekVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDVIKLLIK 105
                          90       100       110
                  ....*....|....*....|....*....|
gi 1498473183 223 RGADSNIVFTV-MNEEHTTLemiCNMDTNP 251
Cdd:PHA03095  106 AGADVNAKDKVgRTPLHVYL---SGFNINP 132
Ank_4 pfam13637
Ankyrin repeats (many copies);
169-221 1.40e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.96  E-value: 1.40e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1498473183 169 TPLIIAMSKGDTEVCRMLLDSGANIDYFSKRpCVTAMCYAIQNNKIDMVSMFL 221
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGN-GETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
136-187 4.40e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.42  E-value: 4.40e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1498473183 136 TPLHLAVMSKDIKGIELLLDHRACTNIEDCYGCTPLIIAMSKGDTEVCRMLL 187
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02798 PHA02798
ankyrin-like protein; Provisional
161-406 5.97e-06

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 48.29  E-value: 5.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183 161 NIEDCYGCTPLIIAMSKGDTEVCRMLLDSGANIDYFSKRPcVTAMCYAIQNNKIDMVSMFLKRGADSNIVFTVMNEEHTT 240
Cdd:PHA02798  252 NQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELG-NTCLFTAFENESKFIFNSILNKKPNKNTISYTYYKLRKH 330
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183 241 LemicnmdTNPESESVDMLIADIALRQYTNTISSDKGFS-RNMTVINSKSRLKDVFEKCKIELRRINSESIRTYNILDLC 319
Cdd:PHA02798  331 I-------LNVEGDFINQLEFDIIKKFIAYVILYVKNFSiRNLTYPFIFTYFDDFIEKCTKSINEIHNTYVNNETIFQIC 403
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183 320 LK----PSKNLDENILARHSRkilglydnAIFYKYLLKELADTASQRAEAIESAMRVIdEKITGDETK-WNWLPHEIKYN 394
Cdd:PHA02798  404 FNkkyiPIKYINNKKLKKYTK--------LFYYGNIIKKIIEKSKKRYENIYKVSCYI-TKICSNELSyWNYIPNEIKFK 474
                         250
                  ....*....|..
gi 1498473183 395 ILEYIGNKELDI 406
Cdd:PHA02798  475 IINNLSNNDILE 486
Ank_5 pfam13857
Ankyrin repeats (many copies);
86-141 3.10e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.18  E-value: 3.10e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1498473183  86 LLDSGKFINDVIYKKGNTPLHLATISKNLDMMRLLIARGADTDVPNTDRFTPLHLA 141
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02743 PHA02743
Viral ankyrin protein; Provisional
80-179 6.24e-05

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 43.27  E-value: 6.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183  80 VVKVEELLDSGKFINDVIYKKGNTPLHLATISKNLDMMRLLIAR-GADTDVPNTDRFTPLHLAVMSKDIKGIELLLDHRA 158
Cdd:PHA02743   73 VMKIELLVNMGADINARELGTGNTLLHIAASTKNYELAEWLCRQlGVNLGAINYQHETAYHIAYKMRDRRMMEILRANGA 152
                          90       100
                  ....*....|....*....|.
gi 1498473183 159 CTNiedcygcTPLIIAMSKGD 179
Cdd:PHA02743  153 VCD-------DPLSIGLSDET 166
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
100-131 6.89e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.58  E-value: 6.89e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1498473183 100 KGNTPLHLATIS-KNLDMMRLLIARGADTDVPN 131
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
6-126 8.44e-05

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 44.69  E-value: 8.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183   6 LCNAILFGELDVARRLLD----SYINPNFTINGYSPIKMAVRLRDVEMIKLLMSYNTYPDYNypdiESELHEAVEEgDVV 81
Cdd:TIGR00870  21 FLPAAERGDLASVYRDLEepkkLNINCPDRLGRSALFVAAIENENLELTELLLNLSCRGAVG----DTLLHAISLE-YVD 95
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1498473183  82 KVEELL----------DSGKFINDVI---YKKGNTPLHLATISKNLDMMRLLIARGAD 126
Cdd:TIGR00870  96 AVEAILlhllaafrksGPLELANDQYtseFTPGITALHLAAHRQNYEIVKLLLERGAS 153
Ank_4 pfam13637
Ankyrin repeats (many copies);
71-121 1.09e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.57  E-value: 1.09e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1498473183  71 LHEAVEEGDVVKVEELLDSGKFINDVIyKKGNTPLHLATISKNLDMMRLLI 121
Cdd:pfam13637   5 LHAAAASGHLELLRLLLEKGADINAVD-GNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
118-187 1.72e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 43.73  E-value: 1.72e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183 118 RLLIARGADTDVPNTDRFTPLHLAVMSKDIKGIELLLDHRACTNIEDCYGCTPLIIAMSKGDTEVCRMLL 187
Cdd:PTZ00322   99 RILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
166-195 2.57e-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: 37.95  E-value: 2.57e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 1498473183  166 YGCTPLIIAMSKGDTEVCRMLLDSGANIDY 195
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
100-129 4.42e-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: 4.42e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1498473183 100 KGNTPLHLATISKNLDMMRLLIARGADTDV 129
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
98-223 5.23e-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: 42.17  E-value: 5.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183  98 YKKGNTPLHLATISKNLDMMRLLIARGADTDVPNTDRF-------------TPLHLAVMSKDIKGIELLLDHR---ACTN 161
Cdd:cd21882    70 FYQGQTALHIAIENRNLNLVRLLVENGADVSARATGRFfrkspgnlfyfgeLPLSLAACTNQEEIVRLLLENGaqpAALE 149
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1498473183 162 IEDCYGCTPLIIAMSKGDTE------VCRM---LLDSGANIDY------FSKRPCVTAMCYAIQNNKIDMVSMFLKR 223
Cdd:cd21882   150 AQDSLGNTVLHALVLQADNTpensafVCQMynlLLSYGAHLDPtqqleeIPNHQGLTPLKLAAVEGKIVMFQHILQR 226
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
100-129 5.70e-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: 5.70e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 1498473183  100 KGNTPLHLATISKNLDMMRLLIARGADTDV 129
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_2 pfam12796
Ankyrin repeats (3 copies);
6-66 7.83e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 38.17  E-value: 7.83e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1498473183   6 LCNAILFGELDVARRLLDsYINPNFTINGYSPIKMAVRLRDVEMIKLLMSYNTypDYNYPD 66
Cdd:pfam12796  34 LHLAAKNGHLEIVKLLLE-HADVNLKDNGRTALHYAARSGHLEIVKLLLEKGA--DINVKD 91
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
166-194 8.62e-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: 36.50  E-value: 8.62e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1498473183 166 YGCTPLIIA-MSKGDTEVCRMLLDSGANID 194
Cdd:pfam00023   1 DGNTPLHLAaGRRGNLEIVKLLLSKGADVN 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
6-53 1.07e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.87  E-value: 1.07e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1498473183   6 LCNAILFGELDVARRLLDSYINPN-FTINGYSPIKMAVRLRDVEMIKLL 53
Cdd:pfam13637   5 LHAAAASGHLELLRLLLEKGADINaVDGNGETALHFAASNGNVEVLKLL 53
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
71-140 1.09e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 41.39  E-value: 1.09e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1498473183  71 LHEAVEEGDVVKVEELLDSGKFInDVIYKKGNTPLHLATISKNLDMMRLLIARGADTDVPNT-DRFTPLHL 140
Cdd:PLN03192  626 LCTAAKRNDLTAMKELLKQGLNV-DSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTdDDFSPTEL 695
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
139-222 1.69e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 40.65  E-value: 1.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183 139 HLAVmSKDIKGIELLLDHRACTNIEDCYGCTPLIIAMSKGDTEVCRMLLDSGANIDYFSKRPcVTAMCYAIQNNKIDMVS 218
Cdd:PTZ00322   88 QLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDG-KTPLELAEENGFREVVQ 165

                  ....
gi 1498473183 219 MFLK 222
Cdd:PTZ00322  166 LLSR 169
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
74-198 1.77e-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: 40.45  E-value: 1.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183  74 AVEEGDVVKVEELLDSGKFIN-DVIYKKGNTPLHLATI-SKNLDMMRLLIARGADTDVPNTdrftpLHLAVMSKDIKGIE 151
Cdd:TIGR00870  24 AAERGDLASVYRDLEEPKKLNiNCPDRLGRSALFVAAIeNENLELTELLLNLSCRGAVGDT-----LLHAISLEYVDAVE 98
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1498473183 152 LLLDHRA---------------CTNiEDCYGCTPLIIAMSKGDTEVCRMLLDSGANIDYFSK 198
Cdd:TIGR00870  99 AILLHLLaafrksgplelandqYTS-EFTPGITALHLAAHRQNYEIVKLLLERGASVPARAC 159
PHA02798 PHA02798
ankyrin-like protein; Provisional
83-216 2.18e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 40.20  E-value: 2.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183  83 VEELLDSGKFINDVIYKKgNTPLhlATISKN-------LDMMRLLIARGADTDVPNTDRFTPLHLAVMSKDIKGIELLL- 154
Cdd:PHA02798   54 VKLFINLGANVNGLDNEY-STPL--CTILSNikdykhmLDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLf 130
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1498473183 155 --DHRACTNIEDCYGCTPLIIAMSKG---DTEVCRMLLDSGANIDYFSKRPCVTAM-CYAIQN-NKIDM 216
Cdd:PHA02798  131 miENGADTTLLDKDGFTMLQVYLQSNhhiDIEIIKLLLEKGVDINTHNNKEKYDTLhCYFKYNiDRIDA 199
PHA02736 PHA02736
Viral ankyrin protein; Provisional
82-153 2.81e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 38.32  E-value: 2.81e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1498473183  82 KVEELLDSGKFINDVIYKKGNTPLHLATISKNLDMMRLLIAR-GADTDVPNTDRFTPLHLAVMSKDIKGIELL 153
Cdd:PHA02736   73 KLKLLMEWGADINGKERVFGNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYVACERHDAKMMNIL 145
PHA02741 PHA02741
hypothetical protein; Provisional
66-153 3.38e-03

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 38.10  E-value: 3.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183  66 DIESELHEAVEEGDVVKVeeLLDSGKFINDVIYKKGNTPLHLATISKNLDMMRLLIAR-GADTDVPNTDRFTPLHLAVMS 144
Cdd:PHA02741   65 HIAAEKHEAQLAAEIIDH--LIELGADINAQEMLEGDTALHLAAHRRDHDLAEWLCCQpGIDLHFCNADNKSPFELAIDN 142

                  ....*....
gi 1498473183 145 KDIKGIELL 153
Cdd:PHA02741  143 EDVAMMQIL 151
PHA02946 PHA02946
ankyin-like protein; Provisional
83-172 3.47e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 39.27  E-value: 3.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183  83 VEELLDSGKFINDViYKKGNTPLHLATISKNLDMMRLLIARGADTDVPNTDRFTPLHLAVMSKD--IKGIELLLDHRA-C 159
Cdd:PHA02946   55 VEELLHRGYSPNET-DDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYGAkI 133
                          90
                  ....*....|...
gi 1498473183 160 TNIEDCYGCTPLI 172
Cdd:PHA02946  134 NNSVDEEGCGPLL 146
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
98-223 3.60e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely related to TRPV1, sharing high sequence identity (>50%), but TRPV2 shows a higher temperature threshold and sensitivity for activation than TRPV1. TRPV2 can be stimulated by ligands or lipids, and is involved in osmosensation and mechanosensation. TRPV2 is expressed in both neuronal and non-neuronal tissues, and it has been implicated in diverse physiological and pathophysiological processes, including cardiac-structure maintenance, innate immunity, and cancer. TRPV2 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 39.45  E-value: 3.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183  98 YKKGNTPLHLATISKNLDMMRLLIARGADTDVPNTDRF-------------TPLHLAVMSKDIKGIELLLDHR---ACTN 161
Cdd:cd22197    91 YYRGHSALHIAIEKRSLQCVKLLVENGADVHARACGRFfqkkqgtcfyfgeLPLSLAACTKQWDVVNYLLENPhqpASLQ 170
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1498473183 162 IEDCYGCTPL-IIAMSKGDTE-----VCRM---LLDSGANID------YFSKRPCVTAMCYAIQNNKIDMVSMFLKR 223
Cdd:cd22197   171 AQDSLGNTVLhALVMIADNSPensalVIKMydgLLQAGARLCptvqleEISNHEGLTPLKLAAKEGKIEIFRHILQR 247
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
49-223 4.57e-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: 4.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183  49 MIKLLMSYNTypdyNYPDIESELHEAVEEGDVVKveelldsgKFINDVIYK---KGNTPLHLATISKNLDMMRLLIARGA 125
Cdd:cd22194    98 LMKALLNINE----NTKEIVRILLAFAEENGILD--------RFINAEYTEeayEGQTALNIAIERRQGDIVKLLIAKGA 165
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1498473183 126 DTDVPNTDRF--------------TPLHLAVMSKDIKGIELLLDhRACTNI--EDCYGCTPL-IIAMSKGDTE-----VC 183
Cdd:cd22194   166 DVNAHAKGVFfnpkykhegfyfgeTPLALAACTNQPEIVQLLME-KESTDItsQDSRGNTVLhALVTVAEDSKtqndfVK 244
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1498473183 184 RM----LLDS-GANIDYFSKRPCVTAMCYAIQNNKIDMVSMFLKR 223
Cdd:cd22194   245 RMydmiLLKSeNKNLETIRNNEGLTPLQLAAKMGKAEILKYILSR 289
Ank_5 pfam13857
Ankyrin repeats (many copies);
120-174 5.61e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.01  E-value: 5.61e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1498473183 120 LIARG-ADTDVPNTDRFTPLHLAVMSKDIKGIELLLDHRACTNIEDCYGCTPLIIA 174
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
 
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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