NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1268743660|ref|NP_001344091|]
View 

KN motif and ankyrin repeat domain-containing protein 3 isoform 2 [Mus musculus]

Protein Classification

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

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

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
15-152 1.03e-27

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 104.65  E-value: 1.03e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743660  15 DVNHQNRAGYSALMLAAltsvgqEEEDMAVAQRLFSMG-DVNAKASQtGQTALMLAISHGHQDMVAALLECGADVNVQDA 93
Cdd:COG0666   112 DVNARDKDGETPLHLAA------YNGNLEIVKLLLEAGaDVNAQDND-GNTPLHLAAANGNLEIVKLLLEAGADVNARDN 184

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1268743660  94 DGATALMCASEYGRLDTVQLLLAQpGCDLTILDNEGTSALAIALEAEQDEVAALLHAHL 152
Cdd:COG0666   185 DGETPLHLAAENGHLEIVKLLLEA-GADVNAKDNDGKTALDLAAENGNLEIVKLLLEAG 242
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
15-152 1.03e-27

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 104.65  E-value: 1.03e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743660  15 DVNHQNRAGYSALMLAAltsvgqEEEDMAVAQRLFSMG-DVNAKASQtGQTALMLAISHGHQDMVAALLECGADVNVQDA 93
Cdd:COG0666   112 DVNARDKDGETPLHLAA------YNGNLEIVKLLLEAGaDVNAQDND-GNTPLHLAAANGNLEIVKLLLEAGADVNARDN 184

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1268743660  94 DGATALMCASEYGRLDTVQLLLAQpGCDLTILDNEGTSALAIALEAEQDEVAALLHAHL 152
Cdd:COG0666   185 DGETPLHLAAENGHLEIVKLLLEA-GADVNAKDNDGKTALDLAAENGNLEIVKLLLEAG 242
Ank_2 pfam12796
Ankyrin repeats (3 copies);
66-148 1.63e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.53  E-value: 1.63e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743660  66 LMLAISHGHQDMVAALLECGADVNVQDADGATALMCASEYGRLDTVQLLLAQPGCDltiLDNEGTSALAIALEAEQDEVA 145
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN---LKDNGRTALHYAARSGHLEIV 77


                  ...
gi 1268743660 146 ALL 148
Cdd:pfam12796  78 KLL 80
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 76-169 9.52e-11

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 59.53  E-value: 9.52e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743660  76 DMVAA--LLECGADVNVQDADGATALMCASEYGRLDTVQLLLaQPGCDLTILDNEGTSALAIALEAEQDEVAALLHAHLT 153
Cdd:PTZ00322   94 DAVGAriLLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLL-EFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQ 172

                          90       100
                  ....*....|....*....|..
gi 1268743660 154 SNHQG------QSSTGSPTAKE 169
Cdd:PTZ00322  173 CHFELganakpDSFTGKPPSLE 194
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 62-90 7.34e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 38.34  E-value: 7.34e-05
                           10        20
                   ....*....|....*....|....*....
gi 1268743660   62 GQTALMLAISHGHQDMVAALLECGADVNV 90
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 62-143 1.07e-04

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 41.67  E-value: 1.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743660  62 GQTALMLAISHGHQDMVAALLECGADVNVQDAD--------------GATALMCASEYGRLDTVQLLLAQPGCDLTILDN 127
Cdd:cd22194   141 GQTALNIAIERRQGDIVKLLIAKGADVNAHAKGvffnpkykhegfyfGETPLALAACTNQPEIVQLLMEKESTDITSQDS 220

                          90
                  ....*....|....*..
gi 1268743660 128 EGTSAL-AIALEAEQDE 143
Cdd:cd22194   221 RGNTVLhALVTVAEDSK 237
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 17-90 4.20e-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: 36.98  E-value: 4.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743660  17 NHQNRA--GYSALMLAALTSVGQEEEDMAVAQRLFSMGD----VNAKASQT---GQTALMLAISHGHQDMVAALLECGAD 87
Cdd:TIGR00870  74 NLSCRGavGDTLLHAISLEYVDAVEAILLHLLAAFRKSGplelANDQYTSEftpGITALHLAAHRQNYEIVKLLLERGAS 153


                  ...
gi 1268743660  88 VNV 90
Cdd:TIGR00870 154 VPA 156
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
15-152 1.03e-27

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 104.65  E-value: 1.03e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743660  15 DVNHQNRAGYSALMLAAltsvgqEEEDMAVAQRLFSMG-DVNAKASQtGQTALMLAISHGHQDMVAALLECGADVNVQDA 93
Cdd:COG0666   112 DVNARDKDGETPLHLAA------YNGNLEIVKLLLEAGaDVNAQDND-GNTPLHLAAANGNLEIVKLLLEAGADVNARDN 184

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1268743660  94 DGATALMCASEYGRLDTVQLLLAQpGCDLTILDNEGTSALAIALEAEQDEVAALLHAHL 152
Cdd:COG0666   185 DGETPLHLAAENGHLEIVKLLLEA-GADVNAKDNDGKTALDLAAENGNLEIVKLLLEAG 242
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
5-151 1.18e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 96.95  E-value: 1.18e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743660   5 VLNQNLPGVCDVNHQNRAGYSALMLAAltsvgqEEEDMAVAQRLFSMG-DVNAKASQtGQTALMLAISHGHQDMVAALLE 83
Cdd:COG0666    69 VALLLLAAGADINAKDDGGNTLLHAAA------RNGDLEIVKLLLEAGaDVNARDKD-GETPLHLAAYNGNLEIVKLLLE 141

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1268743660  84 CGADVNVQDADGATALMCASEYGRLDTVQLLLAQpGCDLTILDNEGTSALAIALEAEQDEVAALLHAH 151
Cdd:COG0666   142 AGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEA-GADVNARDNDGETPLHLAAENGHLEIVKLLLEA 208
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
15-148 1.85e-19

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 83.08  E-value: 1.85e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743660  15 DVNHQNRAGYSALMLAAltsvgqEEEDMAVAQRLFSMG-DVNAKaSQTGQTALMLAISHGHQDMVAALLECGADVNVQDA 93
Cdd:COG0666   145 DVNAQDNDGNTPLHLAA------ANGNLEIVKLLLEAGaDVNAR-DNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN 217

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1268743660  94 DGATALMCASEYGRLDTVQLLLAQpGCDLTILDNEGTSALAIALEAEQDEVAALL 148
Cdd:COG0666   218 DGKTALDLAAENGNLEIVKLLLEA-GADLNAKDKDGLTALLLAAAAGAALIVKLL 271
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
29-148 1.58e-18

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 80.38  E-value: 1.58e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743660  29 LAALTSVGQEEEDMAVAQRLFSMGDVNAKASQTGQTALMLAISHGHQDMVAALLECGADVNVQDADGATALMCASEYGRL 108
Cdd:COG0666    54 GALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNL 133

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1268743660 109 DTVQLLLAQpGCDLTILDNEGTSALAIALEAEQDEVAALL 148
Cdd:COG0666   134 EIVKLLLEA-GADVNAQDNDGNTPLHLAAANGNLEIVKLL 172
Ank_2 pfam12796
Ankyrin repeats (3 copies);
66-148 1.63e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.53  E-value: 1.63e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743660  66 LMLAISHGHQDMVAALLECGADVNVQDADGATALMCASEYGRLDTVQLLLAQPGCDltiLDNEGTSALAIALEAEQDEVA 145
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN---LKDNGRTALHYAARSGHLEIV 77


                  ...
gi 1268743660 146 ALL 148
Cdd:pfam12796  78 KLL 80
Ank_2 pfam12796
Ankyrin repeats (3 copies);
27-126 2.50e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 64.75  E-value: 2.50e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743660  27 LMLAAltsvgqEEEDMAVAQRLFSMGDVNAKASQTGQTALMLAISHGHQDMVAALLECgADVNVQDaDGATALMCASEYG 106
Cdd:pfam12796   1 LHLAA------KNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSG 72

                          90       100
                  ....*....|....*....|
gi 1268743660 107 RLDTVQLLLaQPGCDLTILD 126
Cdd:pfam12796  73 HLEIVKLLL-EKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
5-92 4.61e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 58.97  E-value: 4.61e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743660   5 VLNQNLPGVCDVNHQNRAGYSALMLAALTsvGQEEedmaVAQRLFSMGDVNAKASqtGQTALMLAISHGHQDMVAALLEC 84
Cdd:pfam12796  12 LVKLLLENGADANLQDKNGRTALHLAAKN--GHLE----IVKLLLEHADVNLKDN--GRTALHYAARSGHLEIVKLLLEK 83


                  ....*...
gi 1268743660  85 GADVNVQD 92
Cdd:pfam12796  84 GADINVKD 91
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 76-169 9.52e-11

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 59.53  E-value: 9.52e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743660  76 DMVAA--LLECGADVNVQDADGATALMCASEYGRLDTVQLLLaQPGCDLTILDNEGTSALAIALEAEQDEVAALLHAHLT 153
Cdd:PTZ00322   94 DAVGAriLLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLL-EFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQ 172

                          90       100
                  ....*....|....*....|..
gi 1268743660 154 SNHQG------QSSTGSPTAKE 169
Cdd:PTZ00322  173 CHFELganakpDSFTGKPPSLE 194
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
26-151 5.12e-10

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 56.89  E-value: 5.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743660  26 ALMLAALTSVGQEEEDMAVAQRLFSMGDVNAKASQTGQTALMLAISHGHQDMVAALLECGADVNVQDADGATALMCASEY 105
Cdd:COG0666    18 LLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARN 97

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1268743660 106 GRLDTVQLLLAQpGCDLTILDNEGTSALAIALEAEQDEVAALLHAH 151
Cdd:COG0666    98 GDLEIVKLLLEA-GADVNARDKDGETPLHLAAYNGNLEIVKLLLEA 142
Ank_4 pfam13637
Ankyrin repeats (many copies);
64-115 6.88e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.28  E-value: 6.88e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1268743660  64 TALMLAISHGHQDMVAALLECGADVNVQDADGATALMCASEYGRLDTVQLLL 115
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
15-130 2.97e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 54.57  E-value: 2.97e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743660  15 DVNHQNRAGYSALMLAAltsvgqEEEDMAVAQRLFSMG-DVNAKASQtGQTALMLAISHGHQDMVAALLECGADVNVQDA 93
Cdd:COG0666   178 DVNARDNDGETPLHLAA------ENGHLEIVKLLLEAGaDVNAKDND-GKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1268743660  94 DGATALMCASEYGRLDTVQLLLAQPGCDLTILDNEGT 130
Cdd:COG0666   251 DGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 62-121 3.60e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.82  E-value: 3.60e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743660  62 GQTALMLAISHGHQDMVAALLECGADVNVQDADGATALMCASEYGRLDTVQLLLAQPGCD 121
Cdd:PTZ00322  115 GRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCH 174
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 18-148 2.68e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 49.48  E-value: 2.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743660  18 HQNRAGYSALMLAALTSVGQEEEDMAVAQRLFSMGDvnakasQTGQTALMLAISHGHQDMVAALLECGADVNVQDADGAT 97
Cdd:PLN03192  520 HDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGD------SKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNT 593

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743660  98 AL------------------------------MC-ASEYGRLDTVQLLLAQpGCDLTILDNEGTSALAIALEAEQDEVAA 146
Cdd:PLN03192  594 ALwnaisakhhkifrilyhfasisdphaagdlLCtAAKRNDLTAMKELLKQ-GLNVDSEDHQGATALQVAMAEDHVDMVR 672


                  ..
gi 1268743660 147 LL 148
Cdd:PLN03192  673 LL 674
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 19-158 1.17e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 47.56  E-value: 1.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743660  19 QNRAGYSALMLAALTSVGQEEEDMAVAQRLFSMG----DVNAKASqtgqtaLMLAISHGHQDMVAALLECGADVNVQDAD 94
Cdd:PLN03192  484 QTRQEDNVVILKNFLQHHKELHDLNVGDLLGDNGgehdDPNMASN------LLTVASTGNAALLEELLKAKLDPDIGDSK 557

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1268743660  95 GATALMCASEYGRLDTVQLLLAQpGCDLTILDNEGTSALAIALEAEQDEVAALLH--AHLTSNHQG 158
Cdd:PLN03192  558 GRTPLHIAASKGYEDCVLVLLKH-ACNVHIRDANGNTALWNAISAKHHKIFRILYhfASISDPHAA 622
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 15-137 1.29e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 47.27  E-value: 1.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743660  15 DVNHQNRAGYSALMLAAltsvgqEEEDMAVAQRLFSMG-DVNAKaSQTGQTALMLAISHGHQDMVAALLECGADVNVQDA 93
Cdd:PHA02874  116 DVNIKDAELKTFLHYAI------KKGDLESIKMLFEYGaDVNIE-DDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDN 188

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1268743660  94 DGATALMCASEYGRLDTVQLLLAQpGCDLTILDNEGTSALAIAL 137
Cdd:PHA02874  189 NGESPLHNAAEYGDYACIKLLIDH-GNHIMNKCKNGFTPLHNAI 231
Ank_5 pfam13857
Ankyrin repeats (many copies);
81-136 1.48e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.49  E-value: 1.48e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1268743660  81 LLECG-ADVNVQDADGATALMCASEYGRLDTVQLLLAqPGCDLTILDNEGTSALAIA 136
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLA-YGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
62-99 1.55e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.49  E-value: 1.55e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1268743660  62 GQTALMLAISHGHQDMVAALLECGADVNVQDADGATAL 99
Cdd:pfam13857  16 GYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 38-115 2.68e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 46.21  E-value: 2.68e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1268743660  38 EEEDMAVAQRLFSMG-DVNAKASQTgQTALMLAISHGHQDMVAALLECGADVNVQDADGATALMCASEYGRLDTVQLLL 115
Cdd:PHA02876  154 QQDELLIAEMLLEGGaDVNAKDIYC-ITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAII 231
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 67-148 2.86e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 46.11  E-value: 2.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743660  67 MLAISHGHQDMVAALLECGADVNVQDADGATALMCASEYGRLDTVQLLLaQPGCDLTILDNEGTSALAIALEAEQDEVAA 146
Cdd:PHA02874   96 ILPIPCIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLF-EYGADVNIEDDNGCYPIHIAIKHNFFDIIK 174


                  ..
gi 1268743660 147 LL 148
Cdd:PHA02874  175 LL 176
PHA03095 PHA03095
ankyrin-like protein; Provisional
 15-106 5.34e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 45.40  E-value: 5.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743660  15 DVNHQNRAGYSALMLAALTSvgqeeEDMAVAqRLFSMG-DVNAkASQTGQTALMLAISHGHQDMVAALLECGADVNVQDA 93
Cdd:PHA03095  249 SINARNRYGQTPLHYAAVFN-----NPRACR-RLIALGaDINA-VSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAA 321

                          90
                  ....*....|...
gi 1268743660  94 dgatALMCASEYG 106
Cdd:PHA03095  322 ----TLNTASVAG 330
PHA03095 PHA03095
ankyrin-like protein; Provisional
 15-138 5.87e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 45.40  E-value: 5.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743660  15 DVNHQNRAGYSALMLAALTSvgqEEEDmaVAQRLFSMG-DVNAKaSQTGQTAL--MLAISHGHQDMVAALLECGADVNVQ 91
Cdd:PHA03095   75 DVNAPERCGFTPLHLYLYNA---TTLD--VIKLLIKAGaDVNAK-DKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNAL 148

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1268743660  92 DADGATALMCASEYGR--LDTVQLLLAQpGCDLTILDNEGTSALAIALE 138
Cdd:PHA03095  149 DLYGMTPLAVLLKSRNanVELLRLLIDA-GADVYAVDDRFRSLLHHHLQ 196
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 62-92 9.45e-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: 40.74  E-value: 9.45e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1268743660  62 GQTALMLAISH-GHQDMVAALLECGADVNVQD 92
Cdd:pfam00023   2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
Ank_2 pfam12796
Ankyrin repeats (3 copies);
99-162 1.38e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 41.64  E-value: 1.38e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1268743660  99 LMCASEYGRLDTVQLLLaQPGCDLTILDNEGTSALAIALEAEQDEVAALLHAHLTSNHQGQSST 162
Cdd:pfam12796   1 LHLAAKNGNLELVKLLL-ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGRT 63
PHA02798 PHA02798
ankyrin-like protein; Provisional
 76-139 4.28e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 42.90  E-value: 4.28e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1268743660  76 DMVAALLECGADVNVQDADGATALMCASEYGRLDTVQLLL--AQPGCDLTILDNEGTSALAIALEA 139
Cdd:PHA02798   90 DIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLfmIENGADTTLLDKDGFTMLQVYLQS 155
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 1-115 5.28e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 42.34  E-value: 5.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743660   1 MAKFVLNQNlpgvCDVNHQNRAGYSALMLAaltsVGQEEEDMAVAQRLFSMG-DVNAKAS---------------QTGQT 64
Cdd:PHA03100  123 IVEYLLDNG----ANVNIKNSDGENLLHLY----LESNKIDLKILKLLIDKGvDINAKNRvnyllsygvpinikdVYGFT 194

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1268743660  65 ALMLAISHGHQDMVAALLECGADVNVQDADGATALMCASEYGRLDTVQLLL 115
Cdd:PHA03100  195 PLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLL 245
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 62-90 7.34e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 38.34  E-value: 7.34e-05
                           10        20
                   ....*....|....*....|....*....
gi 1268743660   62 GQTALMLAISHGHQDMVAALLECGADVNV 90
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 41-154 1.01e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 41.79  E-value: 1.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743660  41 DMAVAQRLFSMG-DVNAKASQTGQTALMLAISHGHQDMVAALLECGADVNVQDADGATALMCASEYGRLDTVQLLLaQPG 119
Cdd:PHA02878  146 EAEITKLLLSYGaDINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILL-ENG 224

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1268743660 120 CDLTILDNEGTSALAIALEAEQD-EVAALLHAHLTS 154
Cdd:PHA02878  225 ASTDARDKCGNTPLHISVGYCKDyDILKLLLEHGVD 260
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 62-143 1.07e-04

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 41.67  E-value: 1.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743660  62 GQTALMLAISHGHQDMVAALLECGADVNVQDAD--------------GATALMCASEYGRLDTVQLLLAQPGCDLTILDN 127
Cdd:cd22194   141 GQTALNIAIERRQGDIVKLLIAKGADVNAHAKGvffnpkykhegfyfGETPLALAACTNQPEIVQLLMEKESTDITSQDS 220

                          90
                  ....*....|....*..
gi 1268743660 128 EGTSAL-AIALEAEQDE 143
Cdd:cd22194   221 RGNTVLhALVTVAEDSK 237
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 62-90 2.04e-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: 36.85  E-value: 2.04e-04
                          10        20
                  ....*....|....*....|....*....
gi 1268743660  62 GQTALMLAISHGHQDMVAALLECGADVNV 90
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 14-115 2.22e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 40.62  E-value: 2.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743660  14 CDVNHQNRAGYSALMLAAltsvgqeeedMAVAQRLFSMGDVNAKAS--QTGQTALMLAISHGHQDMVAALLECGADVNVQ 91
Cdd:PLN03192  582 CNVHIRDANGNTALWNAI----------SAKHHKIFRILYHFASISdpHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSE 651

                          90       100
                  ....*....|....*....|....
gi 1268743660  92 DADGATALMCASEYGRLDTVQLLL 115
Cdd:PLN03192  652 DHQGATALQVAMAEDHVDMVRLLI 675
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 62-163 3.87e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 39.97  E-value: 3.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743660  62 GQTALMLAISHGHQDMVAALLECGADVNVQDADGATALMC-ASEYGRLDTVQLLLAQpGCD---LTILDNEGTSALAI-- 135
Cdd:PHA02875  168 GCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCyAIENNKIDIVRLFIKR-GADcniMFMIEGEECTILDMic 246

                          90       100       110
                  ....*....|....*....|....*....|
gi 1268743660 136 --ALEAEQDEVAALLHAHLTSNHQGQSSTG 163
Cdd:PHA02875  247 nmCTNLESEAIDALIADIAIRIHKKTIRRD 276
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 81-148 4.25e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 40.05  E-value: 4.25e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1268743660  81 LLECGADVNVQDADGATALMCASEYGRLDTVQLLLAQpGCDLTILDNEGTSALAIALEAEQ-DEVAALL 148
Cdd:PHA02876  164 LLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSY-GADVNIIALDDLSVLECAVDSKNiDTIKAII 231
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 15-141 5.97e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 39.48  E-value: 5.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743660  15 DVNHQNR-AGYSALMLAAltsvgqEEEDMAVAQRLFSMG-DVNAkASQTGQTALMLAISHGHQDMVAALLECGADVNVQD 92
Cdd:PHA02878  159 DINMKDRhKGNTALHYAT------ENKDQRLTELLLSYGaNVNI-PDKTNNSPLHHAVKHYNKPIVHILLENGASTDARD 231

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1268743660  93 ADGATALMCASEYGRLDTVQLLLAQPGCDL----TILdneGTSALAIALEAEQ 141
Cdd:PHA02878  232 KCGNTPLHISVGYCKDYDILKLLLEHGVDVnaksYIL---GLTALHSSIKSER 281
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 38-148 8.66e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 38.82  E-value: 8.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743660  38 EEEDMAVAQRLFSMGD-VNAKASQTGQTALMLAISHGHQDMVAALLECGADVNVQDADGATALMCASEYGRLDTVQLLLA 116
Cdd:PHA02875   77 EEGDVKAVEELLDLGKfADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLID 156

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1268743660 117 QPGCdLTILDNEGTSALAIALEAEQDEVAALL 148
Cdd:PHA02875  157 HKAC-LDIEDCCGCTPLIIAMAKGDIAICKML 187
PHA03095 PHA03095
ankyrin-like protein; Provisional
 43-137 1.01e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 38.47  E-value: 1.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743660  43 AVAQRLFSMGDVNAKASQTGQTAL--MLAISHGHQDMVAALLECGADVNVQDADGATALMCASEYGRLDTVQLLLAQpGC 120
Cdd:PHA03095  203 RIVRELIRAGCDPAATDMLGNTPLhsMATGSSCKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIAL-GA 281

                          90
                  ....*....|....*..
gi 1268743660 121 DLTILDNEGTSALAIAL 137
Cdd:PHA03095  282 DINAVSSDGNTPLSLMV 298
PHA03095 PHA03095
ankyrin-like protein; Provisional
 17-137 1.26e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 38.47  E-value: 1.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743660  17 NHQNRAGYSALMLAALTSvgqEEEDMAVAQRLFSMG-DVNAKASqTGQTALMLAISHGHQ---DMVAALLECGADVNVQD 92
Cdd:PHA03095    5 ESVDIIMEAALYDYLLNA---SNVTVEEVRRLLAAGaDVNFRGE-YGKTPLHLYLHYSSEkvkDIVRLLLEAGADVNAPE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1268743660  93 ADGATALMCASEYG-RLDTVQLLLaQPGCDLTILDNEGTSALAIAL 137
Cdd:PHA03095   81 RCGFTPLHLYLYNAtTLDVIKLLI-KAGADVNAKDKVGRTPLHVYL 125
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 17-90 4.20e-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: 36.98  E-value: 4.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743660  17 NHQNRA--GYSALMLAALTSVGQEEEDMAVAQRLFSMGD----VNAKASQT---GQTALMLAISHGHQDMVAALLECGAD 87
Cdd:TIGR00870  74 NLSCRGavGDTLLHAISLEYVDAVEAILLHLLAAFRKSGplelANDQYTSEftpGITALHLAAHRQNYEIVKLLLERGAS 153


                  ...
gi 1268743660  88 VNV 90
Cdd:TIGR00870 154 VPA 156
PHA02917 PHA02917
ankyrin-like protein; Provisional
 51-124 4.31e-03

ankyrin-like protein; Provisional


Pssm-ID: 165231 [Multi-domain]  Cd Length: 661  Bit Score: 36.90  E-value: 4.31e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1268743660  51 MGDVNAkASQTGQTALMLAISHGHQDMVAALLECGADVNVQDADGATALMCA-SEYGRLDTVQLLLA-QPGCDLTI 124
Cdd:PHA02917  442 LKDINM-IDKRGETLLHKAVRYNKQSLVSLLLESGSDVNIRSNNGYTCIAIAiNESRNIELLKMLLChKPTLDCVI 516
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 62-138 6.29e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 36.48  E-value: 6.29e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1268743660  62 GQTALMLAISHGHQdmVAALLECGADVNVQDADGATALMCASEYG-RLDTVQLLLAQPGcDLTILDNEGTSALAIALE 138
Cdd:PHA02874  223 GFTPLHNAIIHNRS--AIELLINNASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKA-DISIKDNKGENPIDTAFK 297
PHA02795 PHA02795
ankyrin-like protein; Provisional
 62-118 6.64e-03

ankyrin-like protein; Provisional


Pssm-ID: 165157 [Multi-domain]  Cd Length: 437  Bit Score: 36.13  E-value: 6.64e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1268743660  62 GQTALMLAISHGHQDMVAALLECGADVNVQDADGATALMCASEYG--------RLDTVQLLLAQP 118
Cdd:PHA02795  221 GRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDVAVDRGsviarretHLKILEILLREP 285
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 62-133 7.09e-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: 36.31  E-value: 7.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743660  62 GQTALMLAISHGHQDMVAALLECGADVNVQDAD--------------GATALMCASEYGRLDTVQLLLAQPGCDLTIL-- 125
Cdd:cd22193    76 GQTALHIAIERRQGDIVALLVENGADVHAHAKGrffqpkyqgegfyfGELPLSLAACTNQPDIVQYLLENEHQPADIEaq 155


                  ....*...
gi 1268743660 126 DNEGTSAL 133
Cdd:cd22193   156 DSRGNTVL 163
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 78-138 7.97e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 35.80  E-value: 7.97e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1268743660  78 VAALLECGADVNVQDADGATALMCAS--EYGRLDTVQLLLAQpGCDLTILDNEGTSALAIALE 138
Cdd:PHA03100   89 VKLLLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDN-GANVNIKNSDGENLLHLYLE 150
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 16-102 9.70e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 35.63  E-value: 9.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743660  16 VNHQNRAGYSALMLaaltSVGQEEeDMAVAQRLFSMG-DVNAKASQTGQTALMLAISHghQDMVAALLECGADVNVQDAD 94
Cdd:PHA02878  227 TDARDKCGNTPLHI----SVGYCK-DYDILKLLLEHGvDVNAKSYILGLTALHSSIKS--ERKLKLLLEYGADINSLNSY 299


                  ....*...
gi 1268743660  95 GATALMCA 102
Cdd:PHA02878  300 KLTPLSSA 307
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH