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Conserved domains on  [gi|9634701|ref|NP_038994|]
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Ankyrin repeat gene family protein [Fowlpox virus]

Protein Classification

ankyrin repeat domain-containing protein( domain architecture ID 1562542)

ankyrin (ANK) repeat domain-containing protein may be involved in mediating protein-protein interactions

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
23-222 9.40e-33

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 123.14  E-value: 9.40e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9634701   23 DRNSLLLVATKRNYIDVVRYLVKKGVDINFQEtiRDNLTPLMIASRFNSHQLVELLLNNGAIINQRSlTCGNTALHLAVK 102
Cdd:COG0666  86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARD--KDGETPLHLAAYNGNLEIVKLLLEAGADVNAQD-NDGNTPLHLAAA 162

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9634701  103 NDNRITVDILLFHGANTNITNNDGFTPLHKAVIYNaSIDIIKKLLRYKADVNIRDNEeentGLTPLDIAMSCNNYEIISL 182
Cdd:COG0666 163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENG-HLEIVKLLLEAGADVNAKDND----GKTALDLAAENGNLEIVKL 237

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 9634701  183 LVSHVIRLDYSTCMSNKTKGFDHNKKLVKDNKRLQRIAIH 222
Cdd:COG0666 238 LLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLL 277
PRANC pfam09372
PRANC domain; This presumed domain is found at the C-terminus of a variety of Pox virus ...
 237-336 9.20e-14

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: 66.12  E-value: 9.20e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9634701    237 SRFTLFDLFVN-NNVDLLLRCINKDNRFIVnfdKKLTVFNILYTDFIDTFMSRHVLLNKASKVLEDLFldndSNTSSWNN 315
Cdd:pfam09372   1 DNVSLYDILFNkNNINILVRYVNNDSLIKL---KSFPIYGDIIKKIIKSSKERYKLINKAIDVLNNIC----SNNSLWNL 73

                          90       100
                  ....*....|....*....|.
gi 9634701    316 LPNEIKDHIFTYINNDELKIM 336
Cdd:pfam09372  74 LPIEIKYNILEYLNDDDLKNL 94
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
23-222 9.40e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 123.14  E-value: 9.40e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9634701   23 DRNSLLLVATKRNYIDVVRYLVKKGVDINFQEtiRDNLTPLMIASRFNSHQLVELLLNNGAIINQRSlTCGNTALHLAVK 102
Cdd:COG0666  86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARD--KDGETPLHLAAYNGNLEIVKLLLEAGADVNAQD-NDGNTPLHLAAA 162

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9634701  103 NDNRITVDILLFHGANTNITNNDGFTPLHKAVIYNaSIDIIKKLLRYKADVNIRDNEeentGLTPLDIAMSCNNYEIISL 182
Cdd:COG0666 163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENG-HLEIVKLLLEAGADVNAKDND----GKTALDLAAENGNLEIVKL 237

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 9634701  183 LVSHVIRLDYSTCMSNKTKGFDHNKKLVKDNKRLQRIAIH 222
Cdd:COG0666 238 LLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLL 277
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 38-336 2.95e-30

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 119.98  E-value: 2.95e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9634701    38 DVVRYLVKKGVDINFQETIRDNlTPLMIASRFNSHQLVELLLNNGAIINQRSLtCGNTALHLAVKNDNRITVDILLFHGA 117
Cdd:PHA02878 148 EITKLLLSYGADINMKDRHKGN-TALHYATENKDQRLTELLLSYGANVNIPDK-TNNSPLHHAVKHYNKPIVHILLENGA 225

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9634701   118 NTNITNNDGFTPLHKAVIYNASIDIIKK--------------------------------LLRYKADVNIRDNEEEntgl 165
Cdd:PHA02878 226 STDARDKCGNTPLHISVGYCKDYDILKLllehgvdvnaksyilgltalhssikserklklLLEYGADINSLNSYKL---- 301

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9634701   166 TPLDIAM-SCNNYEIISLLVSHVIRLDYSTCMSNKTKGFDHNKKLVKDNKRLQRIAIHCLKDIEKMKQVSINSRFTLFDL 244
Cdd:PHA02878 302 TPLSSAVkQYLCINIGRILISNICLLKRIKPDIKNSEGFIDNMDCITSNKRLNQIKDKCEDELNRLASIKITNTYSFDDF 381

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9634701   245 FVNNNVDLLLRCINKDNRFIVNFDKKLTVFNILYTDfIDTFMSRHVLLNKASKVLEDLFLDNDSntSSWNNLPNEIKDHI 324
Cdd:PHA02878 382 LKCDNSTLLCKLVNNSIIDDILIDSFNIYGNIIKKN-IYRARKRLLLIEGAIYSLDNIFFEKQN--YMWNRLPLEIKHYI 458

                        330
                 ....*....|..
gi 9634701   325 FTYINNDELKIM 336
Cdd:PHA02878 459 MELLDDASLCNM 470
Ank_2 pfam12796
Ankyrin repeats (3 copies);
28-123 4.44e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.15  E-value: 4.44e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9634701     28 LLVATKRNYIDVVRYLVKKGVDINFQETirDNLTPLMIASRFNSHQLVELLLNNgaiINQRSLTCGNTALHLAVKNDNRI 107
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDK--NGRTALHLAAKNGHLEIVKLLLEH---ADVNLKDNGRTALHYAARSGHLE 75

                          90
                  ....*....|....*.
gi 9634701    108 TVDILLFHGANTNITN 123
Cdd:pfam12796  76 IVKLLLEKGADINVKD 91
PRANC pfam09372
PRANC domain; This presumed domain is found at the C-terminus of a variety of Pox virus ...
 237-336 9.20e-14

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: 66.12  E-value: 9.20e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9634701    237 SRFTLFDLFVN-NNVDLLLRCINKDNRFIVnfdKKLTVFNILYTDFIDTFMSRHVLLNKASKVLEDLFldndSNTSSWNN 315
Cdd:pfam09372   1 DNVSLYDILFNkNNINILVRYVNNDSLIKL---KSFPIYGDIIKKIIKSSKERYKLINKAIDVLNNIC----SNNSLWNL 73

                          90       100
                  ....*....|....*....|.
gi 9634701    316 LPNEIKDHIFTYINNDELKIM 336
Cdd:pfam09372  74 LPIEIKYNILEYLNDDDLKNL 94
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 50-186 3.90e-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: 57.72  E-value: 3.90e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9634701   50 INFQETIRDNLTPLMIASRFNSHQLVE-LLLNNGAIINQRSlTCGNTALHLAVKNDNRITVDILLfHGA----NTNITNN 124
Cdd:cd22192   8 LHLLQQKRISESPLLLAAKENDVQAIKkLLKCPSCDLFQRG-ALGETALHVAALYDNLEAAVVLM-EAApelvNEPMTSD 85

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9634701  125 --DGFTPLHKAVIyNASIDIIKKLLRYKADVNirdnEEENTGLT--------------PLDIAMSCNNYEIISLLVSH 186
Cdd:cd22192  86 lyQGETALHIAVV-NQNLNLVRELIARGADVV----SPRATGTFfrpgpknliyygehPLSFAACVGNEEIVRLLIEH 158
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 23-130 5.05e-06

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 48.15  E-value: 5.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9634701     23 DRNSLLLVATKRNYiDVVRYLVKKGVDIN-------FQETIRDNL-----TPLMIASRFNSHQLVELLLNNGAIIN-QRS 89
Cdd:TIGR00870 128 GITALHLAAHRQNY-EIVKLLLERGASVParacgdfFVKSQGVDSfyhgeSPLNAAACLGSPSIVALLSEDPADILtADS 206

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 9634701     90 LtcGNTALHLAV-----KNDNRITV----DILLFHGANTN-------ITNNDGFTPL 130
Cdd:TIGR00870 207 L--GNTLLHLLVmenefKAEYEELScqmyNFALSLLDKLRdskelevILNHQGLTPL 261
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 125-155 4.84e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.10  E-value: 4.84e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 9634701     125 DGFTPLHKAVIYNaSIDIIKKLLRYKADVNI 155
Cdd:smart00248   1 DGRTPLHLAAENG-NLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
23-222 9.40e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 123.14  E-value: 9.40e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9634701   23 DRNSLLLVATKRNYIDVVRYLVKKGVDINFQEtiRDNLTPLMIASRFNSHQLVELLLNNGAIINQRSlTCGNTALHLAVK 102
Cdd:COG0666  86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARD--KDGETPLHLAAYNGNLEIVKLLLEAGADVNAQD-NDGNTPLHLAAA 162

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9634701  103 NDNRITVDILLFHGANTNITNNDGFTPLHKAVIYNaSIDIIKKLLRYKADVNIRDNEeentGLTPLDIAMSCNNYEIISL 182
Cdd:COG0666 163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENG-HLEIVKLLLEAGADVNAKDND----GKTALDLAAENGNLEIVKL 237

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 9634701  183 LVSHVIRLDYSTCMSNKTKGFDHNKKLVKDNKRLQRIAIH 222
Cdd:COG0666 238 LLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLL 277
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 38-336 2.95e-30

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 119.98  E-value: 2.95e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9634701    38 DVVRYLVKKGVDINFQETIRDNlTPLMIASRFNSHQLVELLLNNGAIINQRSLtCGNTALHLAVKNDNRITVDILLFHGA 117
Cdd:PHA02878 148 EITKLLLSYGADINMKDRHKGN-TALHYATENKDQRLTELLLSYGANVNIPDK-TNNSPLHHAVKHYNKPIVHILLENGA 225

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9634701   118 NTNITNNDGFTPLHKAVIYNASIDIIKK--------------------------------LLRYKADVNIRDNEEEntgl 165
Cdd:PHA02878 226 STDARDKCGNTPLHISVGYCKDYDILKLllehgvdvnaksyilgltalhssikserklklLLEYGADINSLNSYKL---- 301

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9634701   166 TPLDIAM-SCNNYEIISLLVSHVIRLDYSTCMSNKTKGFDHNKKLVKDNKRLQRIAIHCLKDIEKMKQVSINSRFTLFDL 244
Cdd:PHA02878 302 TPLSSAVkQYLCINIGRILISNICLLKRIKPDIKNSEGFIDNMDCITSNKRLNQIKDKCEDELNRLASIKITNTYSFDDF 381

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9634701   245 FVNNNVDLLLRCINKDNRFIVNFDKKLTVFNILYTDfIDTFMSRHVLLNKASKVLEDLFLDNDSntSSWNNLPNEIKDHI 324
Cdd:PHA02878 382 LKCDNSTLLCKLVNNSIIDDILIDSFNIYGNIIKKN-IYRARKRLLLIEGAIYSLDNIFFEKQN--YMWNRLPLEIKHYI 458

                        330
                 ....*....|..
gi 9634701   325 FTYINNDELKIM 336
Cdd:PHA02878 459 MELLDDASLCNM 470
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 27-335 1.30e-29

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 117.46  E-value: 1.30e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9634701    27 LLLVATKRNYIDVVRYLVKKGVDINFQETIRDNLTPLMIASRFNSHQLVELLLNNGAIINqrsltcgntalhlaVKNdnr 106
Cdd:PHA03100 111 LYAISKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLKILKLLIDKGVDIN--------------AKN--- 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9634701   107 iTVDILLFHGANTNITNNDGFTPLHKAVIYNaSIDIIKKLLRYKADVNIRDneeeNTGLTPLDIAMSCNNYEIISLLVSH 186
Cdd:PHA03100 174 -RVNYLLSYGVPINIKDVYGFTPLHYAVYNN-NPEFVKYLLDLGANPNLVN----KYGDTPLHIAILNNNKEIFKLLLNN 247

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9634701   187 ---------VIRLDYSTCMSNKTK----------------GFDHNKKLVKDNKRLQRIAIHCLKDIEKMKQVSINSrFTL 241
Cdd:PHA03100 248 gpsiktiieTLLYFKDKDLNTITKikmlkksimymflldpGFYKNRKLIENSKSLKDVINECEKEIERMKEIKLNK-VTV 326

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9634701   242 FDLFVNNNVDLLLRCINkdNRFIVNFDkKLTVFNILYTDFIDTFMSRHVLLNKASKVLEDLfldndSNTSSWNNLPNEIK 321
Cdd:PHA03100 327 YDIIFNKNINFLSRYVN--NKSVTKYT-TSKIYGKYIKKVINKAIERKKLIKKIIKKLNNL-----CKNTYWNILPIEIK 398

                        330
                 ....*....|....
gi 9634701   322 DHIFTYINNDELKI 335
Cdd:PHA03100 399 YKILEYLSNRDLKS 412
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 23-337 5.28e-23

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 98.91  E-value: 5.28e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9634701    23 DRNSLLLVATKRNYIDVVRYLVKKGVDINFQETirDNLTPLMIASRFNSHQLVELLLNNGAIINQRSlTCGNTALHLAVK 102
Cdd:PHA02875 101 DGMTPLHLATILKKLDIMKLLIARGADPDIPNT--DKFSPLHLAVMMGDIKGIELLIDHKACLDIED-CCGCTPLIIAMA 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9634701   103 NDNRITVDILLFHGANTNITNNDGFTPLHKAVIYNASIDIIKKLLRYKADVNIR---DNEEENTgltpldIAMSCN---- 175
Cdd:PHA02875 178 KGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLFIKRGADCNIMfmiEGEECTI------LDMICNmctn 251

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9634701   176 -NYEIISLLVSHVIRLDYSTCMSnKTKGFDHNKKLVKDNKRLQRIAIHCLKDIEKMKQVSINsRFTLFDLFV--NNNVDL 252
Cdd:PHA02875 252 lESEAIDALIADIAIRIHKKTIR-RDEGFKNNMSTIEDKEEFKDVFEKCIIELRRIKSEKIG-KKNILDLCIleKNSHNL 329

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9634701   253 LLRCINKDNRFIVNFDKKLTVFNILYTDFIDTFMSRHVLLNKASKVLEDLFLDNDSNtssWNNLPNEIKDHIFTYINNDE 332
Cdd:PHA02875 330 DENILARHSKKILGLNDEAHFYKYLLKEAADIALKRAEAIESAIRVIDDEITGDESK---WNILPHEIKYLILEKIGNKD 406


                 ....*
gi 9634701   333 LKIMT 337
Cdd:PHA02875 407 IDIAI 411
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 26-247 6.84e-22

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 95.80  E-value: 6.84e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9634701    26 SLLLVATKRNYIDVVRYLVKKGVDINFQETirDNLTPLMIASRFNSHQLVELLLNNGAIINQRSLTcGNTALHLAVKNDN 105
Cdd:PHA02874 126 TFLHYAIKKGDLESIKMLFEYGADVNIEDD--NGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNN-GESPLHNAAEYGD 202

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9634701   106 RITVDILLFHGANTNITNNDGFTPLHKAVIYNAS-------------------------------IDIIKKLLRYKADVN 154
Cdd:PHA02874 203 YACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSaiellinnasindqdidgstplhhainppcdIDIIDILLYHKADIS 282

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9634701   155 IRDNEEENtgltPLDIAMSCNNYEII-------SLLVSHVIRLDYSTCMsnktkgfdhNKKLVKDNKRLQRIAIHCLKDI 227
Cdd:PHA02874 283 IKDNKGEN----PIDTAFKYINKDPVikdiianAVLIKEADKLKDSDFL---------EHIEIKDNKEFSDFIKECNEEI 349

                        250       260
                 ....*....|....*....|
gi 9634701   228 EKMKQVSINSRFTLFDLFVN 247
Cdd:PHA02874 350 EDMKKTKCGCDKNIFDLCLI 369
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
23-162 4.22e-19

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 86.16  E-value: 4.22e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9634701   23 DRNSLLLVATKRNYIDVVRYLVKKGVDINFQEtiRDNLTPLMIASRFNSHQLVELLLNNGAIINQRSLTcGNTALHLAVK 102
Cdd:COG0666 152 DGNTPLHLAAANGNLEIVKLLLEAGADVNARD--NDGETPLHLAAENGHLEIVKLLLEAGADVNAKDND-GKTALDLAAE 228

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 9634701  103 NDNRITVDILLFHGANTNITNNDGFTPLHKAVIYNASIDIIKKLLRYKADVNIRDNEEEN 162
Cdd:COG0666 229 NGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
PHA03095 PHA03095
ankyrin-like protein; Provisional
 19-186 6.87e-19

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 87.00  E-value: 6.87e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9634701    19 KYRLDRNSLL--LVATKRNYIDVVRYLVKKGVDINFQETIrdNLTPLMIASRFNSHQL---VELLLNNGAIINQRSlTCG 93
Cdd:PHA03095   7 VDIIMEAALYdyLLNASNVTVEEVRRLLAAGADVNFRGEY--GKTPLHLYLHYSSEKVkdiVRLLLEAGADVNAPE-RCG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9634701    94 NTALHLAVKNDNRITV-DILLFHGANTNITNNDGFTPLHkavIY----NASIDIIKKLLRYKADVNIRDneeeNTGLTPL 168
Cdd:PHA03095  84 FTPLHLYLYNATTLDViKLLIKAGADVNAKDKVGRTPLH---VYlsgfNINPKVIRLLLRKGADVNALD----LYGMTPL 156

                        170       180
                 ....*....|....*....|
gi 9634701   169 DIAMSCNN--YEIISLLVSH 186
Cdd:PHA03095 157 AVLLKSRNanVELLRLLIDA 176
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
19-186 1.19e-18

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 84.62  E-value: 1.19e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9634701   19 KYRLDRNSLLLVATKRNYIDVVRYLVKKGVDINFQETIRDNLTPLMIASRFNSHQLVELLLNNGAIINQRSLTcGNTALH 98
Cdd:COG0666  14 ALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG-GNTLLH 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9634701   99 LAVKNDNRITVDILLFHGANTNITNNDGFTPLHKAVIYNaSIDIIKKLLRYKADVNIRDNEeentGLTPLDIAMSCNNYE 178
Cdd:COG0666  93 AAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNG-NLEIVKLLLEAGADVNAQDND----GNTPLHLAAANGNLE 167


                ....*...
gi 9634701  179 IISLLVSH 186
Cdd:COG0666 168 IVKLLLEA 175
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 3-275 4.19e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 80.41  E-value: 4.19e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9634701     3 FLIELLRITGIVTLCPKYRLDRNSLLLVATKRNYIDVVRYLVKKGVDINFQETIRDN--LTPLMIASRFNSHQLVELLLN 80
Cdd:PHA02884  12 LLCRIFYIIFYIAIKKKNKICIANILYSSIKFHYTDIIDAILKLGADPEAPFPLSENskTNPLIYAIDCDNDDAAKLLIR 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9634701    81 NGAIINQRSLTCGNTALHLAVKNDNRITVDILLFHGANTNITNNDGFTPlhkaviynasIDIIKKLLRYKADVNIRDNEE 160
Cdd:PHA02884  92 YGADVNRYAEEAKITPLYISVLHGCLKCLEILLSYGADINIQTNDMVTP----------IELALMICNNFLAFMICDNEI 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9634701   161 ENTGLTPLDIAMscnNYEIISLLVSHVIRLDYSTCMSNK-----TKGFDHNKKLVKDNKRLQRIAIHCLKDIEKMKQVSI 235
Cdd:PHA02884 162 SNFYKHPKKILI---NFDILKILVSHFILQASNDRLNEKhnknfNAGYNKNKHLIIQSIILKQFKDLCIDDIDIMKNIKL 238

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 9634701   236 ----NSRFTLFDLFVNNNVDLLLRciNKDNRFIVNFDKKLTVFN 275
Cdd:PHA02884 239 gddsNDMLSFFDILVENDLIKLLN--NIDNIDILDIPKKLKVYN 280
Ank_2 pfam12796
Ankyrin repeats (3 copies);
28-123 4.44e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.15  E-value: 4.44e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9634701     28 LLVATKRNYIDVVRYLVKKGVDINFQETirDNLTPLMIASRFNSHQLVELLLNNgaiINQRSLTCGNTALHLAVKNDNRI 107
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDK--NGRTALHLAAKNGHLEIVKLLLEH---ADVNLKDNGRTALHYAARSGHLE 75

                          90
                  ....*....|....*.
gi 9634701    108 TVDILLFHGANTNITN 123
Cdd:pfam12796  76 IVKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
63-157 1.36e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 74.00  E-value: 1.36e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9634701     63 LMIASRFNSHQLVELLLNNGAIINQRSlTCGNTALHLAVKNDNRITVDILLFHgANTNITNNdGFTPLHKAVIYNaSIDI 142
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQD-KNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSG-HLEI 76

                          90
                  ....*....|....*
gi 9634701    143 IKKLLRYKADVNIRD 157
Cdd:pfam12796  77 VKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
97-191 8.17e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 68.99  E-value: 8.17e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9634701     97 LHLAVKNDNRITVDILLFHGANTNITNNDGFTPLHKAVIYNaSIDIIKKLLRYkADVNIRDNeeentGLTPLDIAMSCNN 176
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNG-HLEIVKLLLEH-ADVNLKDN-----GRTALHYAARSGH 73

                          90
                  ....*....|....*
gi 9634701    177 YEIISLLVSHVIRLD 191
Cdd:pfam12796  74 LEIVKLLLEKGADIN 88
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 31-334 8.26e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 75.49  E-value: 8.26e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9634701    31 ATKRNYIDVVRYLVKKGVDINFQETIRDnlTPLMIASRFNSHQLVELLLNNGAIINQRSLTCGnTALHLAVKNDN-RITV 109
Cdd:PHA02876 349 STLDRNKDIVITLLELGANVNARDYCDK--TPIHYAAVRNNVVIINTLLDYGADIEALSQKIG-TALHFALCGTNpYMSV 425

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9634701   110 DILLFHGANTNITNNDGFTPLHKAVIYNASIDIIKKLLRYKADVNIRDNEEENTGLTPLDIAMSCN-------------- 175
Cdd:PHA02876 426 KTLIDRGANVNSKNKDLSTPLHYACKKNCKLDVIEMLLDNGADVNAINIQNQYPLLIALEYHGIVNillhygaelrdsrv 505

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9634701   176 -------NYEIISLLVSHVIRLDYST------------CMSNKTKGFDHNKKLVKDNKRLQRIAIHCLKDIEKMKQVSIN 236
Cdd:PHA02876 506 lhkslndNMFSFRYIIAHICIQDFIRhdirnevnplkrVPTRFTSLRESFKEIIQSDDTFKRIWLRCKEELKDISKIRIN 585

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9634701   237 SRFTLFDLFVNNNVDLLLRCINK------DNRFIVNFDKKLTVFNILYTDfidtfmsRHVLLNKASKVLEDLFldndsNT 310
Cdd:PHA02876 586 MFYSLDIFIISKNMNLLHHLVNNpiikeiNTWHFCNYGDRLKTSISLASD-------RHEILEKSRSKLDEIL-----DS 653

                        330       340
                 ....*....|....*....|....
gi 9634701   311 SSWNNLPNEIKDHIFTYINNDELK 334
Cdd:PHA02876 654 SDWSKLPPDIKLSILEFIDNNELR 677
PRANC pfam09372
PRANC domain; This presumed domain is found at the C-terminus of a variety of Pox virus ...
 237-336 9.20e-14

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: 66.12  E-value: 9.20e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9634701    237 SRFTLFDLFVN-NNVDLLLRCINKDNRFIVnfdKKLTVFNILYTDFIDTFMSRHVLLNKASKVLEDLFldndSNTSSWNN 315
Cdd:pfam09372   1 DNVSLYDILFNkNNINILVRYVNNDSLIKL---KSFPIYGDIIKKIIKSSKERYKLINKAIDVLNNIC----SNNSLWNL 73

                          90       100
                  ....*....|....*....|.
gi 9634701    316 LPNEIKDHIFTYINNDELKIM 336
Cdd:pfam09372  74 LPIEIKYNILEYLNDDDLKNL 94
PHA03095 PHA03095
ankyrin-like protein; Provisional
 35-170 7.88e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 65.82  E-value: 7.88e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9634701    35 NYIDVVRYLVKKGVDINFQEtiRDNLTPLMIASRFNSH-QLVELLLNNGAIINQRSlTCGNTALH--LAVKNDNRITVDI 111
Cdd:PHA03095  61 KVKDIVRLLLEAGADVNAPE--RCGFTPLHLYLYNATTlDVIKLLIKAGADVNAKD-KVGRTPLHvyLSGFNINPKVIRL 137

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 9634701   112 LLFHGANTNITNNDGFTPLHKAVIY-NASIDIIKKLLRYKADVNIRDNEeentGLTPLDI 170
Cdd:PHA03095 138 LLRKGADVNALDLYGMTPLAVLLKSrNANVELLRLLIDAGADVYAVDDR----FRSLLHH 193
PHA03095 PHA03095
ankyrin-like protein; Provisional
 34-334 1.46e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 61.96  E-value: 1.46e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9634701    34 RNYIDVVRYLVKKGVDINfqETIRDNLTPLMIASRFNS--HQLVELLLNNGAIINQRSLTcGNTALHLAVKNDNRITVDI 111
Cdd:PHA03095 199 KPRARIVRELIRAGCDPA--ATDMLGNTPLHSMATGSSckRSLVLPLLIAGISINARNRY-GQTPLHYAAVFNNPRACRR 275

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9634701   112 LLFHGANTNITNNDGFTPLHKAVIyNASIDIIKKLLRYKADVNIRDNE----EENTGLTPLDIAMSCNNYEIISL---LV 184
Cdd:PHA03095 276 LIALGADINAVSSDGNTPLSLMVR-NNNGRAVRAALAKNPSAETVAATlntaSVAGGDIPSDATRLCVAKVVLRGafsLL 354

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9634701   185 SHVIRLDYstcmsnktkgfdhnKKLVKDnkrlqriaihCLKDIEKMKQVSINSRFTLFDLFVNNNVDLLL---RCINKDN 261
Cdd:PHA03095 355 PEPIRAYH--------------ADFIRE----------CEAEIAVMRTTRIGTGVSLLDILFARNPDILLvsnASLRKKA 410

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9634701   262 RFIVnfdkkltvfnilYTDFIDTFMSRHV----LLNKASKVLEdlfldndsntssWNNLPNEIKDHIFTYINNDELK 334
Cdd:PHA03095 411 RLTV------------YGKALRARIEEMRkrskLVERIIKLIC------------PCALPPEIVMRILDFLPDDDLR 463
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 28-331 1.23e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 59.21  E-value: 1.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9634701    28 LLVATKRNYIDVVRYLVKKGVDINFQETIRDNltPLMIASRFNSHQLVELLLNNGAiinqrsltcgNTALhLAVKNDNRI 107
Cdd:PHA02874  39 LIDAIRSGDAKIVELFIKHGADINHINTKIPH--PLLTAIKIGAHDIIKLLIDNGV----------DTSI-LPIPCIEKD 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9634701   108 TVDILLFHGANTNITNNDGFTPLHKAvIYNASIDIIKKLLRYKADVNIRDNeeenTGLTPLDIAMSCNNYEIISLLVS-- 185
Cdd:PHA02874 106 MIKTILDCGIDVNIKDAELKTFLHYA-IKKGDLESIKMLFEYGADVNIEDD----NGCYPIHIAIKHNFFDIIKLLLEkg 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9634701   186 ---HVIRLDYSTCMSNKTKGFDHNK-KLVKDNKrlQRIAIHCLKDIEKMKQVSINSRfTLFDLFVNNnvdlllRCINKDN 261
Cdd:PHA02874 181 ayaNVKDNNGESPLHNAAEYGDYACiKLLIDHG--NHIMNKCKNGFTPLHNAIIHNR-SAIELLINN------ASINDQD 251

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9634701   262 rfivnfdkkltvfnilytdfIDTFMSRHVLLN-KASKVLEDLFLDNDSNTSSWNNLPNEIKDHIFTYINND 331
Cdd:PHA02874 252 --------------------IDGSTPLHHAINpPCDIDIIDILLYHKADISIKDNKGENPIDTAFKYINKD 302
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 50-186 3.90e-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: 57.72  E-value: 3.90e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9634701   50 INFQETIRDNLTPLMIASRFNSHQLVE-LLLNNGAIINQRSlTCGNTALHLAVKNDNRITVDILLfHGA----NTNITNN 124
Cdd:cd22192   8 LHLLQQKRISESPLLLAAKENDVQAIKkLLKCPSCDLFQRG-ALGETALHVAALYDNLEAAVVLM-EAApelvNEPMTSD 85

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9634701  125 --DGFTPLHKAVIyNASIDIIKKLLRYKADVNirdnEEENTGLT--------------PLDIAMSCNNYEIISLLVSH 186
Cdd:cd22192  86 lyQGETALHIAVV-NQNLNLVRELIARGADVV----SPRATGTFfrpgpknliyygehPLSFAACVGNEEIVRLLIEH 158
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 98-188 4.45e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.52  E-value: 4.45e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9634701    98 HLAVKNDNrITVDILLFHGANTNITNNDGFTPLHKAVIyNASIDIIKKLLRYKADVNIRDNEeentGLTPLDIAMSCNNY 177
Cdd:PTZ00322  88 QLAASGDA-VGARILLTGGADPNCRDYDGRTPLHIACA-NGHVQVVRVLLEFGADPTLLDKD----GKTPLELAEENGFR 161

                         90
                 ....*....|.
gi 9634701   178 EIISLLVSHVI 188
Cdd:PTZ00322 162 EVVQLLSRHSQ 172
Ank_5 pfam13857
Ankyrin repeats (many copies);
111-171 5.22e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.88  E-value: 5.22e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9634701    111 ILLFHGANTNITNNDGFTPLHKAVIYNASiDIIKKLLRYKADVNIRDNEeentGLTPLDIA 171
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGAL-EIVRVLLAYGVDLNLKDEE----GLTALDLA 56
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 37-184 5.49e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 54.20  E-value: 5.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9634701    37 IDVVRYLVK-KGVDINFqeTIRDNLTPLMIASRFNSHQLVELLLNNGAIINQRSLTCGNTALH----------------- 98
Cdd:PHA02874  14 IEAIEKIIKnKGNCINI--SVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTaikigahdiikllidng 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9634701    99 -----LAVKNDNRITVDILLFHGANTNITNNDGFTPLHKAvIYNASIDIIKKLLRYKADVNIRDneeeNTGLTPLDIAMS 173
Cdd:PHA02874  92 vdtsiLPIPCIEKDMIKTILDCGIDVNIKDAELKTFLHYA-IKKGDLESIKMLFEYGADVNIED----DNGCYPIHIAIK 166

                        170
                 ....*....|.
gi 9634701   174 CNNYEIISLLV 184
Cdd:PHA02874 167 HNFFDIIKLLL 177
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 28-147 1.17e-07

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: 53.22  E-value: 1.17e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9634701   28 LLVATKRNYIDVVRYLVKKGVDIN-------FQETIRDN-----LTPLMIASRFNSHQLVELLLNNGAIINQRSLTCGNT 95
Cdd:cd22194 145 LNIAIERRQGDIVKLLIAKGADVNahakgvfFNPKYKHEgfyfgETPLALAACTNQPEIVQLLMEKESTDITSQDSRGNT 224

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9634701   96 ALHLAV------KNDN----RITVDILLFHGaNTN---ITNNDGFTPLHKAVIYnASIDIIKKLL 147
Cdd:cd22194 225 VLHALVtvaedsKTQNdfvkRMYDMILLKSE-NKNletIRNNEGLTPLQLAAKM-GKAEILKYIL 287
Ank_2 pfam12796
Ankyrin repeats (3 copies);
23-88 4.18e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 47.42  E-value: 4.18e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9634701     23 DRNSLLLVATKRNYIDVVRYLVKKgVDINFQEtirDNLTPLMIASRFNSHQLVELLLNNGAIINQR 88
Cdd:pfam12796  29 NGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD---NGRTALHYAARSGHLEIVKLLLEKGADINVK 90
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 22-186 8.74e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 50.45  E-value: 8.74e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9634701    22 LDRNSLLLVATKRNY-IDVVRYLVKKGVDINFQETIRDnlTPLMIASRFNS-HQLVELLLNNGAIINQRSLTcGNTALHL 99
Cdd:PHA02876 237 INKNDLSLLKAIRNEdLETSLLLYDAGFSVNSIDDCKN--TPLHHASQAPSlSRLVPKLLERGADVNAKNIK-GETPLYL 313

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9634701   100 AVKND-NRITVDILLFHGANTNITNNDGFTPLHKAVIYNASIDIIKKLLRYKADVNIRDNEEEntglTPLDIAMSCNNYE 178
Cdd:PHA02876 314 MAKNGyDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKDIVITLLELGANVNARDYCDK----TPIHYAAVRNNVV 389


                 ....*...
gi 9634701   179 IISLLVSH 186
Cdd:PHA02876 390 IINTLLDY 397
Ank_4 pfam13637
Ankyrin repeats (many copies);
24-79 1.14e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.96  E-value: 1.14e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 9634701     24 RNSLLLVATKRNYIDVVRYLVKKGVDINfqETIRDNLTPLMIASRFNSHQLVELLL 79
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADIN--AVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
78-133 2.45e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.26  E-value: 2.45e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 9634701     78 LLNNGAIINQRSLTCGNTALHLAVKNDNRITVDILLFHGANTNITNNDGFTPLHKA 133
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 125-158 2.67e-06

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: 43.43  E-value: 2.67e-06
                          10        20        30
                  ....*....|....*....|....*....|....
gi 9634701    125 DGFTPLHKAVIYNASIDIIKKLLRYKADVNIRDN 158
Cdd:pfam00023   1 DGNTPLHLAAGRRGNLEIVKLLLSKGADVNARDK 34
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 23-130 5.05e-06

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 48.15  E-value: 5.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9634701     23 DRNSLLLVATKRNYiDVVRYLVKKGVDIN-------FQETIRDNL-----TPLMIASRFNSHQLVELLLNNGAIIN-QRS 89
Cdd:TIGR00870 128 GITALHLAAHRQNY-EIVKLLLERGASVParacgdfFVKSQGVDSfyhgeSPLNAAACLGSPSIVALLSEDPADILtADS 206

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 9634701     90 LtcGNTALHLAV-----KNDNRITV----DILLFHGANTN-------ITNNDGFTPL 130
Cdd:TIGR00870 207 L--GNTLLHLLVmenefKAEYEELScqmyNFALSLLDKLRdskelevILNHQGLTPL 261
Ank_4 pfam13637
Ankyrin repeats (many copies);
93-147 7.52e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.65  E-value: 7.52e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 9634701     93 GNTALHLAVKNDNRITVDILLFHGANTNITNNDGFTPLHKAViYNASIDIIKKLL 147
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAA-SNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 74-179 1.25e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 46.98  E-value: 1.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9634701    74 LVELLLNNGAIINQRSLTCgNTALHLAVKNDNRITVDILLFHGANTNITNNDGFTPLHKAVIYNaSIDIIKKLLRYKADV 153
Cdd:PHA02876 160 IAEMLLEGGADVNAKDIYC-ITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSK-NIDTIKAIIDNRSNI 237

                         90       100       110
                 ....*....|....*....|....*....|....
gi 9634701   154 NIRD--------NEEENTGLTPLDIAMSCNNYEI 179
Cdd:PHA02876 238 NKNDlsllkairNEDLETSLLLYDAGFSVNSIDD 271
Ank_4 pfam13637
Ankyrin repeats (many copies);
59-113 1.64e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.88  E-value: 1.64e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 9634701     59 NLTPLMIASRFNSHQLVELLLNNGAIINQRSLtCGNTALHLAVKNDNRITVDILL 113
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDG-NGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 28-134 4.70e-05

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: 45.00  E-value: 4.70e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9634701   28 LLVATKRNYIDVVRYLVKKGVDIN-------FQETIRDNLT-----PLMIASRFNSHQLVELLLNNGA-IINQRSLtcGN 94
Cdd:cd22192  93 LHIAVVNQNLNLVRELIARGADVVspratgtFFRPGPKNLIyygehPLSFAACVGNEEIVRLLIEHGAdIRAQDSL--GN 170

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 9634701   95 TALHLAVKNDNRITV----DILLFHGANTN------ITNNDGFTPLHKAV 134
Cdd:cd22192 171 TVLHILVLQPNKTFAcqmyDLILSYDKEDDlqpldlVPNNQGLTPFKLAA 220
Ank_4 pfam13637
Ankyrin repeats (many copies);
128-184 4.77e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 40.34  E-value: 4.77e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 9634701    128 TPLHKAVIYNaSIDIIKKLLRYKADVNIRDNEeentGLTPLDIAMSCNNYEIISLLV 184
Cdd:pfam13637   3 TALHAAAASG-HLELLRLLLEKGADINAVDGN----GETALHFAASNGNVEVLKLLL 54
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 23-191 6.56e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 44.35  E-value: 6.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9634701    23 DRNSLLLVATKRNYI--DVVRYLVKKGVDINFQETIRDNLTPLMIASRFNSH---QLVELLLNNGAIINQRSLTcGNTAL 97
Cdd:PHA02989  34 RGNSILLLYLKRKDVkiKIVKLLIDNGADVNYKGYIETPLCAVLRNREITSNkikKIVKLLLKFGADINLKTFN-GVSPI 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9634701    98 HLAVKNDNRITVDILLF---HGANTN-ITNNDGFTPLHkavIY----NASIDIIKKLLRYkaDVNIRDNEEEnTGLTPLD 169
Cdd:PHA02989 113 VCFIYNSNINNCDMLRFllsKGINVNdVKNSRGYNLLH---MYlesfSVKKDVIKILLSF--GVNLFEKTSL-YGLTPMN 186

                        170       180
                 ....*....|....*....|....*.
gi 9634701   170 I----AMSCNNYEIISLLVSHVIRLD 191
Cdd:PHA02989 187 IylrnDIDVISIKVIKYLIKKGVNIE 212
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 21-194 7.84e-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: 44.30  E-value: 7.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9634701     21 RLDRNSLLLVATKRNYIDVVRYLVKKGVDINFQETirdnltpLMIASRFNSHQLVELLLN----------NGAIINQRSL 90
Cdd:TIGR00870  50 RLGRSALFVAAIENENLELTELLLNLSCRGAVGDT-------LLHAISLEYVDAVEAILLhllaafrksgPLELANDQYT 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9634701     91 ---TCGNTALHLAVKNDNRITVDILLFHGANTNITNNDGF--TPLHKAVIYN-----------ASIDIIKKLLRYKADVN 154
Cdd:TIGR00870 123 sefTPGITALHLAAHRQNYEIVKLLLERGASVPARACGDFfvKSQGVDSFYHgesplnaaaclGSPSIVALLSEDPADIL 202

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 9634701    155 IRD---NE-----EENTGLTPLDIAMSCNNYeiiSLLVSHVIRLDYST 194
Cdd:TIGR00870 203 TADslgNTllhllVMENEFKAEYEELSCQMY---NFALSLLDKLRDSK 247
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 93-124 3.24e-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: 37.65  E-value: 3.24e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 9634701     93 GNTALHLAV-KNDNRITVDILLFHGANTNITNN 124
Cdd:pfam00023   2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 75-149 3.69e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 42.19  E-value: 3.69e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9634701    75 VELLLNNGAIINQRSLTcGNTALHLAVKNDNRITVDILLFHGANTNITNNDGFTPLHKAViYNASIDIIKKLLRY 149
Cdd:PTZ00322  98 ARILLTGGADPNCRDYD-GRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAE-ENGFREVVQLLSRH 170
PHA02743 PHA02743
Viral ankyrin protein; Provisional
 68-133 7.35e-04

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 39.80  E-value: 7.35e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9634701    68 RFNSHQLVELLLNNGAIINQRSLTCGNTALHLAVKNDNRITVDILLFH-GANTNITNNDGFTPLHKA 133
Cdd:PHA02743  69 RANAVMKIELLVNMGADINARELGTGNTLLHIAASTKNYELAEWLCRQlGVNLGAINYQHETAYHIA 135
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 39-178 1.06e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 40.82  E-value: 1.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9634701    39 VVRYLVKKGVDINFQETIrdNLTPLMIASRFNSHQLVELLLNNGAIINQRSLTcGNTALHLAVKNDNRITVDILLFHGAN 118
Cdd:PHA02876 160 IAEMLLEGGADVNAKDIY--CITPIHYAAERGNAKMVNLLLSYGADVNIIALD-DLSVLECAVDSKNIDTIKAIIDNRSN 236

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9634701   119 TN---------ITNND----------GF----------TPLHKAVIYNASIDIIKKLLRYKADVNIRDNEEEntglTPLD 169
Cdd:PHA02876 237 INkndlsllkaIRNEDletslllydaGFsvnsiddcknTPLHHASQAPSLSRLVPKLLERGADVNAKNIKGE----TPLY 312


                 ....*....
gi 9634701   170 IaMSCNNYE 178
Cdd:PHA02876 313 L-MAKNGYD 320
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 32-154 2.03e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 39.72  E-value: 2.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9634701    32 TKRNYIDVVRYLVKKGVDINfqETIRDNLTPLMIASR-FNSHQLVELLLNNGAIINQRSLTcgNTALHLAVKN----DNR 106
Cdd:PHA02989  11 SDTVDKNALEFLLRTGFDVN--EEYRGNSILLLYLKRkDVKIKIVKLLIDNGADVNYKGYI--ETPLCAVLRNreitSNK 86

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 9634701   107 IT--VDILLFHGANTNITNNDGFTPLhKAVIYNASI---DIIKKLLRYKADVN 154
Cdd:PHA02989  87 IKkiVKLLLKFGADINLKTFNGVSPI-VCFIYNSNInncDMLRFLLSKGINVN 138
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 125-155 4.84e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.10  E-value: 4.84e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 9634701     125 DGFTPLHKAVIYNaSIDIIKKLLRYKADVNI 155
Cdd:smart00248   1 DGRTPLHLAAENG-NLEVVKLLLDKGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 24-180 5.17e-03

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: 38.46  E-value: 5.17e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9634701   24 RNSLLLVATKRNYIDVVRYLVKKGvDINFQETIRDNLTPLMIASRFNSHQLVELLLNNG-AIINQ---RSLTCGNTALHL 99
Cdd:cd22192  17 SESPLLLAAKENDVQAIKKLLKCP-SCDLFQRGALGETALHVAALYDNLEAAVVLMEAApELVNEpmtSDLYQGETALHI 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9634701  100 AVKNDNRITVDILLFHGANTNITNNDG--FTPLHKAVIY-----------NASIDIIKKLLRYKADVNIRDneeeNTGLT 166
Cdd:cd22192  96 AVVNQNLNLVRELIARGADVVSPRATGtfFRPGPKNLIYygehplsfaacVGNEEIVRLLIEHGADIRAQD----SLGNT 171

                       170       180
                ....*....|....*....|.
gi 9634701  167 PLDI-------AMSCNNYEII 180
Cdd:cd22192 172 VLHIlvlqpnkTFACQMYDLI 192
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 125-155 5.56e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 34.16  E-value: 5.56e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 9634701    125 DGFTPLHKAVIYNaSIDIIKKLLRYKADVNI 155
Cdd:pfam13606   1 DGNTPLHLAARNG-RLEIVKLLLENGADINA 30
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 26-148 6.03e-03

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


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 38.24  E-value: 6.03e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9634701   26 SLLLVATKRNYIDVVRYLVKKGVDIN-------FQETIRDNL-----TPLMIASRFNSHQLVELLLNN----GAIINQRS 89
Cdd:cd22193  78 TALHIAIERRQGDIVALLVENGADVHahakgrfFQPKYQGEGfyfgeLPLSLAACTNQPDIVQYLLENehqpADIEAQDS 157

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9634701   90 LtcGNTALH-LAVKNDNRIT--------VDILLFHGAN-------TNITNNDGFTPLHKAViYNASIDIIKKLLR 148
Cdd:cd22193 158 R--GNTVLHaLVTVADNTKEntkfvtrmYDMILIRGAKlcptvelEEIRNNDGLTPLQLAA-KMGKIEILKYILQ 229
PHA02798 PHA02798
ankyrin-like protein; Provisional
 37-336 7.40e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 37.89  E-value: 7.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9634701    37 IDVVRYLVKKGVDIN-----FQETIRDNLTPLMIASRFNSHQLVELLLNNGAIINQRSLtcGNTALHLAVKNDNRITVDI 111
Cdd:PHA02798 199 ADILKLFVDNGFIINkenksHKKKFMEYLNSLLYDNKRFKKNILDFIFSYIDINQVDEL--GFNPLYYSVSHNNRKIFEY 276

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9634701   112 LLFHGANTNITNNDGFTPLHKAvIYNASIDIIKKLLRYKADVNIRDNEEENTGLTPLDIAMSCNN---YEIISLLVSHVI 188
Cdd:PHA02798 277 LLQLGGDINIITELGNTCLFTA-FENESKFIFNSILNKKPNKNTISYTYYKLRKHILNVEGDFINqleFDIIKKFIAYVI 355

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9634701   189 RLDYSTCMSNKTKGF--DHNKKLVKdnkrlqriaiHCLKDIEKMKQVSINSRfTLFDLFVNNNVdLLLRCINkdNRFIVN 266
Cdd:PHA02798 356 LYVKNFSIRNLTYPFifTYFDDFIE----------KCTKSINEIHNTYVNNE-TIFQICFNKKY-IPIKYIN--NKKLKK 421

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9634701   267 FDKKLTVFNILYTdfidTFMSRHVLLNKASKVLEDLFLDNDSNTSSWNNLPNEIKDHIFTYINNDELKIM 336
Cdd:PHA02798 422 YTKLFYYGNIIKK----IIEKSKKRYENIYKVSCYITKICSNELSYWNYIPNEIKFKIINNLSNNDILET 487
 
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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