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Conserved domains on  [gi|2531541114|ref|XP_057770157|]
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uncharacterized protein LOC130989990 [Salvia miltiorrhiza]

Protein Classification

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

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
53-265 5.85e-34

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 128.53  E-value: 5.85e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531541114  53 LHHAAEIGHFQICKFLIHNLKVHIDARTFTRDTPLIAAAKGEHVKIVEYLINQGASVSSANSKGSTALHYAVLKDNRELM 132
Cdd:COG0666    57 LLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIV 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531541114 133 ELLVTKGALLEVDSMDG-TPLQIALSRVNVETVKFLLSHGAKPNICSLVLESPLVLAIKAHSFECFDLLLKARADPNMY- 210
Cdd:COG0666   137 KLLLEAGADVNAQDNDGnTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKd 216

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2531541114 211 IVGFSPLSYAAKVGDTKFLKSLLDAGADPNSSLIGHVKIIEDAALVRDREGVEIL 265
Cdd:COG0666   217 NDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLL 271
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
53-265 5.85e-34

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 128.53  E-value: 5.85e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531541114  53 LHHAAEIGHFQICKFLIHNLKVHIDARTFTRDTPLIAAAKGEHVKIVEYLINQGASVSSANSKGSTALHYAVLKDNRELM 132
Cdd:COG0666    57 LLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIV 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531541114 133 ELLVTKGALLEVDSMDG-TPLQIALSRVNVETVKFLLSHGAKPNICSLVLESPLVLAIKAHSFECFDLLLKARADPNMY- 210
Cdd:COG0666   137 KLLLEAGADVNAQDNDGnTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKd 216

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2531541114 211 IVGFSPLSYAAKVGDTKFLKSLLDAGADPNSSLIGHVKIIEDAALVRDREGVEIL 265
Cdd:COG0666   217 NDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLL 271
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 69-240 3.30e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 86.26  E-value: 3.30e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531541114  69 IHNLKVHIDARTFTRDTPLIAAAKGEHVKIVEYLINQGASVSSANSKGSTALHY-----AVLKDNRELMELLVTKGALLE 143
Cdd:PHA03100   21 IIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYlsnikYNLTDVKEIVKLLLEYGANVN 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531541114 144 VDSMDG-TPLQIALSRV--NVETVKFLLSHGAKPNICSLVLESPLVLAIKA--HSFECFDLLLKARADPNM--------- 209
Cdd:PHA03100  101 APDNNGiTPLLYAISKKsnSYSIVEYLLDNGANVNIKNSDGENLLHLYLESnkIDLKILKLLIDKGVDINAknrvnylls 180

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2531541114 210 YIV--------GFSPLSYAAKVGDTKFLKSLLDAGADPN 240
Cdd:PHA03100  181 YGVpinikdvyGFTPLHYAVYNNNPEFVKYLLDLGANPN 219
Ank_2 pfam12796
Ankyrin repeats (3 copies);
87-176 5.97e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.54  E-value: 5.97e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531541114  87 LIAAAKGEHVKIVEYLINQGASVSSANSKGSTALHYAVLKDNRELMELLVTKgALLEVDSMDGTPLQIALSRVNVETVKF 166
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGRTALHYAARSGHLEIVKL 79

                          90
                  ....*....|
gi 2531541114 167 LLSHGAKPNI 176
Cdd:pfam12796  80 LLEKGADINV 89
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 73-239 2.77e-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: 59.26  E-value: 2.77e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531541114  73 KVHIDARTFTRDTPLIAAAKGEHVKIVEYLI-NQGASVSSANSKGSTALHYAVLKDNRELMELLVTKGALLEVDSMDG-- 149
Cdd:cd22192     7 ELHLLQQKRISESPLLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEPMTSdl 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531541114 150 ----TPLQIALSRVNVETVKFLLSHGA---KPNICSLvlesplvlaikahsfeCFDLLLKaradpNMYIVGFSPLSYAAK 222
Cdd:cd22192    87 yqgeTALHIAVVNQNLNLVRELIARGAdvvSPRATGT----------------FFRPGPK-----NLIYYGEHPLSFAAC 145

                         170
                  ....*....|....*..
gi 2531541114 223 VGDTKFLKSLLDAGADP 239
Cdd:cd22192   146 VGNEEIVRLLIEHGADI 162
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 150-176 1.64e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.64  E-value: 1.64e-03
                           10        20
                   ....*....|....*....|....*..
gi 2531541114  150 TPLQIALSRVNVETVKFLLSHGAKPNI 176
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
53-265 5.85e-34

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 128.53  E-value: 5.85e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531541114  53 LHHAAEIGHFQICKFLIHNLKVHIDARTFTRDTPLIAAAKGEHVKIVEYLINQGASVSSANSKGSTALHYAVLKDNRELM 132
Cdd:COG0666    57 LLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIV 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531541114 133 ELLVTKGALLEVDSMDG-TPLQIALSRVNVETVKFLLSHGAKPNICSLVLESPLVLAIKAHSFECFDLLLKARADPNMY- 210
Cdd:COG0666   137 KLLLEAGADVNAQDNDGnTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKd 216

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2531541114 211 IVGFSPLSYAAKVGDTKFLKSLLDAGADPNSSLIGHVKIIEDAALVRDREGVEIL 265
Cdd:COG0666   217 NDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLL 271
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
19-240 3.49e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 123.91  E-value: 3.49e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531541114  19 DLKKLKEMRRKVGDDTELRRICDVYTDFSTGRCVLHHAAEIGHFQICKFLIHNlKVHIDARTFTRDTPLIAAAKGEHVKI 98
Cdd:COG0666    57 LLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEA-GADVNARDKDGETPLHLAAYNGNLEI 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531541114  99 VEYLINQGASVSSANSKGSTALHYAVLKDNRELMELLVTKGALLEV-DSMDGTPLQIALSRVNVETVKFLLSHGAKPNIC 177
Cdd:COG0666   136 VKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNArDNDGETPLHLAAENGHLEIVKLLLEAGADVNAK 215

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2531541114 178 SLVLESPLVLAIKAHSFECFDLLLKARADPNMYIV-GFSPLSYAAKVGDTKFLKSLLDAGADPN 240
Cdd:COG0666   216 DNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKdGLTALLLAAAAGAALIVKLLLLALLLLA 279
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
53-265 2.77e-29

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 115.82  E-value: 2.77e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531541114  53 LHHAAEIGHFQICKFLIHNLKVHIDARTFTRDTPLIAAAKGEHVKIVEYLINQGASVSSANSKGSTALHYAVLKDNRELM 132
Cdd:COG0666    24 LLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIV 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531541114 133 ELLVTKGALLEV-DSMDGTPLQIALSRVNVETVKFLLSHGAKPNICSLVLESPLVLAIKAHSFECFDLLLKARADPNMY- 210
Cdd:COG0666   104 KLLLEAGADVNArDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARd 183

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2531541114 211 IVGFSPLSYAAKVGDTKFLKSLLDAGADPNSSLIGHVKIIEDAALVRDREGVEIL 265
Cdd:COG0666   184 NDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLL 238
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
9-208 2.18e-26

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 107.73  E-value: 2.18e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531541114   9 ALIIEAGASGDLKKLKEMrrkvgddteLRRICDVYTDFSTGRCVLHHAAEIGHFQICKFLIHNlKVHIDARTFTRDTPLI 88
Cdd:COG0666    89 TLLHAAARNGDLEIVKLL---------LEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA-GADVNAQDNDGNTPLH 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531541114  89 AAAKGEHVKIVEYLINQGASVSSANSKGSTALHYAVLKDNRELMELLVTKGALLEV-DSMDGTPLQIALSRVNVETVKFL 167
Cdd:COG0666   159 LAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAkDNDGKTALDLAAENGNLEIVKLL 238

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2531541114 168 LSHGAKPNICSLVLESPLVLAIKAHSFECFDLLLKARADPN 208
Cdd:COG0666   239 LEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLA 279
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
67-240 1.60e-21

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 94.25  E-value: 1.60e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531541114  67 FLIHNLKVHIDARTFTRDTPLIAAAKGEHVKIVEYLINQGASVSSANSKGSTALHYAVLKDNRELMELLVTKGALLEVDS 146
Cdd:COG0666     5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531541114 147 MDG-TPLQIALSRVNVETVKFLLSHGAKPNICSLVLESPLVLAIKAHSFECFDLLLKARADPNM-YIVGFSPLSYAAKVG 224
Cdd:COG0666    85 DGGnTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAqDNDGNTPLHLAAANG 164

                         170
                  ....*....|....*.
gi 2531541114 225 DTKFLKSLLDAGADPN 240
Cdd:COG0666   165 NLEIVKLLLEAGADVN 180
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 69-240 3.30e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 86.26  E-value: 3.30e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531541114  69 IHNLKVHIDARTFTRDTPLIAAAKGEHVKIVEYLINQGASVSSANSKGSTALHY-----AVLKDNRELMELLVTKGALLE 143
Cdd:PHA03100   21 IIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYlsnikYNLTDVKEIVKLLLEYGANVN 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531541114 144 VDSMDG-TPLQIALSRV--NVETVKFLLSHGAKPNICSLVLESPLVLAIKA--HSFECFDLLLKARADPNM--------- 209
Cdd:PHA03100  101 APDNNGiTPLLYAISKKsnSYSIVEYLLDNGANVNIKNSDGENLLHLYLESnkIDLKILKLLIDKGVDINAknrvnylls 180

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2531541114 210 YIV--------GFSPLSYAAKVGDTKFLKSLLDAGADPN 240
Cdd:PHA03100  181 YGVpinikdvyGFTPLHYAVYNNNPEFVKYLLDLGANPN 219
Ank_2 pfam12796
Ankyrin repeats (3 copies);
87-176 5.97e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.54  E-value: 5.97e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531541114  87 LIAAAKGEHVKIVEYLINQGASVSSANSKGSTALHYAVLKDNRELMELLVTKgALLEVDSMDGTPLQIALSRVNVETVKF 166
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGRTALHYAARSGHLEIVKL 79

                          90
                  ....*....|
gi 2531541114 167 LLSHGAKPNI 176
Cdd:pfam12796  80 LLEKGADINV 89
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 85-211 1.77e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 80.86  E-value: 1.77e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531541114  85 TPLIAAA--KGEHVKIVEYLINQGASVSSANSKGSTALHYAV--LKDNRELMELLVTKGA-----------------LLE 143
Cdd:PHA03100  108 TPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLesNKIDLKILKLLIDKGVdinaknrvnyllsygvpINI 187

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2531541114 144 VDSMDGTPLQIALSRVNVETVKFLLSHGAKPNICSLVLESPLVLAIKAHSFECFDLLLKARADPNMYI 211
Cdd:PHA03100  188 KDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTII 255
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 97-241 3.31e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 77.23  E-value: 3.31e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531541114  97 KIVEYLINQGASVSSAN-SKGSTALHYAVLKDNRELMELLVTKGALLEV-DSMDGTPLQIALSRVNVETVKFLLSHGAKP 174
Cdd:PHA02878  148 EITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIpDKTNNSPLHHAVKHYNKPIVHILLENGAST 227

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531541114 175 NICSLVLESPLVLAI-KAHSFECFDLLLKARADPNM--YIVGFSPLSYAAKvgDTKFLKSLLDAGADPNS 241
Cdd:PHA02878  228 DARDKCGNTPLHISVgYCKDYDILKLLLEHGVDVNAksYILGLTALHSSIK--SERKLKLLLEYGADINS 295
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 82-222 2.95e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 74.53  E-value: 2.95e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531541114  82 TRDTPLIAAAKGEHVKIVEYLINQGASVSSANSKGSTALHYAVLKDNRELMELLVTKGALLEVDSMDG-TPLQIALSRV- 159
Cdd:PHA02878  167 KGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGnTPLHISVGYCk 246

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2531541114 160 NVETVKFLLSHGAKPNICSLVLE-SPLVLAIkaHSFECFDLLLKARADPNmyIVGF---SPLSYAAK 222
Cdd:PHA02878  247 DYDILKLLLEHGVDVNAKSYILGlTALHSSI--KSERKLKLLLEYGADIN--SLNSyklTPLSSAVK 309
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 85-240 1.57e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 71.95  E-value: 1.57e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531541114  85 TPLIAAAKGEHVKIVEYLINQGASVSSANSKGSTALHYAVLKDNRELMELLVTKGALL-EVDSMDG-TPLQIALSRVNVE 162
Cdd:PHA02875   37 SPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFAdDVFYKDGmTPLHLATILKKLD 116

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2531541114 163 TVKFLLSHGAKPNICSLVLESPLVLAIKAHSFECFDLLLKARADPNMY-IVGFSPLSYAAKVGDTKFLKSLLDAGADPN 240
Cdd:PHA02875  117 IMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEdCCGCTPLIIAMAKGDIAICKMLLDSGANID 195
Ank_2 pfam12796
Ankyrin repeats (3 copies);
152-241 2.07e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.52  E-value: 2.07e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531541114 152 LQIALSRVNVETVKFLLSHGAKPNICSLVLESPLVLAIKAHSFECFDLLLKaRADPNMYIVGFSPLSYAAKVGDTKFLKS 231
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDNGRTALHYAARSGHLEIVKL 79

                          90
                  ....*....|
gi 2531541114 232 LLDAGADPNS 241
Cdd:pfam12796  80 LLEKGADINV 89
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 85-236 1.07e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 69.61  E-value: 1.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531541114  85 TPLIAAAKGEHVKIVEYLINQGASVSSANSKGSTALHYAVLKDNRELMELLVTKG---ALLEV----------------- 144
Cdd:PHA02874   37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGvdtSILPIpciekdmiktildcgid 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531541114 145 ----DSMDGTPLQIALSRVNVETVKFLLSHGAKPNICSLVLESPLVLAIKAHSFECFDLLLK--ARADPNMYiVGFSPLS 218
Cdd:PHA02874  117 vnikDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEkgAYANVKDN-NGESPLH 195

                         170
                  ....*....|....*...
gi 2531541114 219 YAAKVGDTKFLKSLLDAG 236
Cdd:PHA02874  196 NAAEYGDYACIKLLIDHG 213
PHA03095 PHA03095
ankyrin-like protein; Provisional
 96-241 1.49e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 69.28  E-value: 1.49e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531541114  96 VKIVEYLINQGASVSSANSKGSTALHYAVLKDNRE-LMELLVTKGA-LLEVDSMDGTPLQIALS--RVNVETVKFLLSHG 171
Cdd:PHA03095   63 KDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAGAdVNAKDKVGRTPLHVYLSgfNINPKVIRLLLRKG 142

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2531541114 172 AKPNICSLVLESPLVLAIKAH--SFECFDLLLKARADP-NMYIVGFSPLSYAAKV--GDTKFLKSLLDAGADPNS 241
Cdd:PHA03095  143 ADVNALDLYGMTPLAVLLKSRnaNVELLRLLIDAGADVyAVDDRFRSLLHHHLQSfkPRARIVRELIRAGCDPAA 217
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 19-201 1.46e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 66.06  E-value: 1.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531541114  19 DLKKLKEMRRKVGDDTELRRICDVY------TDFSTGRCVLHHAAEIGHFQICKFLI-HNLKVHIDARTftRDTPLIAAA 91
Cdd:PHA02878  132 DLVYIDKKSKDDIIEAEITKLLLSYgadinmKDRHKGNTALHYATENKDQRLTELLLsYGANVNIPDKT--NNSPLHHAV 209

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531541114  92 KGEHVKIVEYLINQGASVSSANSKGSTALHYAVLK-DNRELMELLVTKGALLEVDS--MDGTPLQIALSRVNVetVKFLL 168
Cdd:PHA02878  210 KHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSyiLGLTALHSSIKSERK--LKLLL 287

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2531541114 169 SHGAKPNICSLVLESPLVLAIKAHS-FECFDLLL 201
Cdd:PHA02878  288 EYGADINSLNSYKLTPLSSAVKQYLcINIGRILI 321
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 3-249 9.76e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 63.93  E-value: 9.76e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531541114   3 STSEIGALIIEAGASGDLKKLK-----EMRRKVGDDTE-----LRRICDVYTDFSTGRCVLHHAAEIGHFQICKFLIHNL 72
Cdd:PHA02876  285 SLSRLVPKLLERGADVNAKNIKgetplYLMAKNGYDTEnirtlIMLGADVNAADRLYITPLHQASTLDRNKDIVITLLEL 364

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531541114  73 KVHIDARTFTRDTPLIAAAKGEHVKIVEYLINQGASVSSANSKGSTALHYAVLKDNREL-MELLVTKGALLEVDSMD-GT 150
Cdd:PHA02876  365 GANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMsVKTLIDRGANVNSKNKDlST 444

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531541114 151 PLQIALSR-VNVETVKFLLSHGAKPNICSLVLESPLVLAIKAHSFecFDLLLKaradpnmyivgfsplsYAAKVGDTKFL 229
Cdd:PHA02876  445 PLHYACKKnCKLDVIEMLLDNGADVNAINIQNQYPLLIALEYHGI--VNILLH----------------YGAELRDSRVL 506

                         250       260
                  ....*....|....*....|
gi 2531541114 230 KSLLDAGADPNSSLIGHVKI 249
Cdd:PHA02876  507 HKSLNDNMFSFRYIIAHICI 526
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
95-265 2.40e-10

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 61.12  E-value: 2.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531541114  95 HVKIVEYLINQGASVSSANSKGSTALHYAVLKDNRELMELLVTKGALLEVDSMDGTPLQIALSRVNVETVKFLLSHGAKP 174
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531541114 175 NICSLVLESPLVLAIKAHSFECFDLLLKARADPN-MYIVGFSPLSYAAKVGDTKFLKSLLDAGADPNSSLIGHVKIIEDA 253
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNaRDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                         170
                  ....*....|..
gi 2531541114 254 ALVRDREGVEIL 265
Cdd:COG0666   161 AANGNLEIVKLL 172
PHA03095 PHA03095
ankyrin-like protein; Provisional
 51-240 2.85e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 61.96  E-value: 2.85e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531541114  51 CVLHHAAEIGhfqICKFLIHNlKVHIDARTFTRDTPLIAAAKGE--HVKIVEYLINQGASVSSANSKGSTALHyAVLKDN 128
Cdd:PHA03095   89 LYLYNATTLD---VIKLLIKA-GADVNAKDKVGRTPLHVYLSGFniNPKVIRLLLRKGADVNALDLYGMTPLA-VLLKSR 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531541114 129 R---ELMELLVTKGA-LLEVDSMDGTPL-QIALS-RVNVETVKFLLSHGAKPNICSLVLESPLVLAIKAHSFECFDL--L 200
Cdd:PHA03095  164 NanvELLRLLIDAGAdVYAVDDRFRSLLhHHLQSfKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpL 243

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2531541114 201 LKARAD---PNMYivGFSPLSYAAKVGDTKFLKSLLDAGADPN 240
Cdd:PHA03095  244 LIAGISinaRNRY--GQTPLHYAAVFNNPRACRRLIALGADIN 284
Ank_2 pfam12796
Ankyrin repeats (3 copies);
11-113 8.99e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 55.12  E-value: 8.99e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531541114  11 IIEAGASGDLKKLKEMrrkvgddteLRRICDVYTDFSTGRCVLHHAAEIGHFQICKFLIhnlkVHIDARTFTRD-TPLIA 89
Cdd:pfam12796   1 LHLAAKNGNLELVKLL---------LENGADANLQDKNGRTALHLAAKNGHLEIVKLLL----EHADVNLKDNGrTALHY 67

                          90       100
                  ....*....|....*....|....
gi 2531541114  90 AAKGEHVKIVEYLINQGASVSSAN 113
Cdd:pfam12796  68 AARSGHLEIVKLLLEKGADINVKD 91
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 73-239 2.77e-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: 59.26  E-value: 2.77e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531541114  73 KVHIDARTFTRDTPLIAAAKGEHVKIVEYLI-NQGASVSSANSKGSTALHYAVLKDNRELMELLVTKGALLEVDSMDG-- 149
Cdd:cd22192     7 ELHLLQQKRISESPLLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEPMTSdl 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531541114 150 ----TPLQIALSRVNVETVKFLLSHGA---KPNICSLvlesplvlaikahsfeCFDLLLKaradpNMYIVGFSPLSYAAK 222
Cdd:cd22192    87 yqgeTALHIAVVNQNLNLVRELIARGAdvvSPRATGT----------------FFRPGPK-----NLIYYGEHPLSFAAC 145

                         170
                  ....*....|....*..
gi 2531541114 223 VGDTKFLKSLLDAGADP 239
Cdd:cd22192   146 VGNEEIVRLLIEHGADI 162
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 36-170 5.58e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 57.75  E-value: 5.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531541114  36 LRRICDVYTDFSTGRCVLHHAAEIGH--FQICKFLIHN---------------LKVHIDARTFTRDTPLIAAAKGEHVKI 98
Cdd:PHA03100  128 LDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKgvdinaknrvnyllsYGVPINIKDVYGFTPLHYAVYNNNPEF 207

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2531541114  99 VEYLINQGASVSSANSKGSTALHYAVLKDNRELMELLVTKGAllEVDSMDGTPLQIALSRVNVETVKFLLSH 170
Cdd:PHA03100  208 VKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGP--SIKTIIETLLYFKDKDLNTITKIKMLKK 277
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 119-265 1.59e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 56.54  E-value: 1.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531541114 119 ALHYAVLKDNRELMELLVTKGALLEVDSMDG-TPLQIALSRVNVETVKFLLSHGAKPNICSLVLESPLVLAIKAHSFECF 197
Cdd:PHA02875    5 ALCDAILFGELDIARRLLDIGINPNFEIYDGiSPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAV 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531541114 198 DLLLKAR--ADPNMYIVGFSPLSYAAKVGDTKFLKSLLDAGADPNSSLIGHVKIIEDAALVRDREGVEIL 265
Cdd:PHA02875   85 EELLDLGkfADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELL 154
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
49-152 6.35e-08

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 53.80  E-value: 6.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531541114  49 GRCVLHHAAEIGHFQICKFLIHNlKVHIDARTFTRDTPLIAAAKGEHVKIVEYLINQGASVSSANSKGSTALHYAVLKDN 128
Cdd:COG0666   186 GETPLHLAAENGHLEIVKLLLEA-GADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGA 264

                          90       100
                  ....*....|....*....|....
gi 2531541114 129 RELMELLVTKGALLEVDSMDGTPL 152
Cdd:COG0666   265 ALIVKLLLLALLLLAAALLDLLTL 288
Ank_4 pfam13637
Ankyrin repeats (many copies);
83-136 1.12e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.04  E-value: 1.12e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2531541114  83 RDTPLIAAAKGEHVKIVEYLINQGASVSSANSKGSTALHYAVLKDNRELMELLV 136
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 40-233 1.55e-07

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: 53.48  E-value: 1.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531541114  40 CDVYTDFSTGRCVLHHAAEIGHFQICKFLIHNlkvhidartftrdtpliaaakgehvkiVEYLINQgaSVSSANSKGSTA 119
Cdd:cd22192    42 CDLFQRGALGETALHVAALYDNLEAAVVLMEA---------------------------APELVNE--PMTSDLYQGETA 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531541114 120 LHYAVLKDNRELMELLVTKGALLEVDSMDGT---------------PLQIALSRVNVETVKFLLSHGAKP----NICSLV 180
Cdd:cd22192    93 LHIAVVNQNLNLVRELIARGADVVSPRATGTffrpgpknliyygehPLSFAACVGNEEIVRLLIEHGADIraqdSLGNTV 172

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2531541114 181 LESpLVL-AIKAHSFECFDLLLKARADPNMYIV-------GFSPLSYAAKVGDTKFLKSLL 233
Cdd:cd22192   173 LHI-LVLqPNKTFACQMYDLILSYDKEDDLQPLdlvpnnqGLTPFKLAAKEGNIVMFQHLV 232
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 74-220 2.06e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 53.04  E-value: 2.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531541114  74 VHIDARTFTRDTPLIAAAKGEHVKIVEYLINQGASVSSANSKGSTALHYAVLKDNRELMELLVTKGALLEVDSMDG-TPL 152
Cdd:PHA02874  115 IDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGeSPL 194

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2531541114 153 QIALSRVNVETVKFLLSHGAK-PNICSLVLeSPLVLAIkAHSFECFDLLLKARADPNMYIVGFSPLSYA 220
Cdd:PHA02874  195 HNAAEYGDYACIKLLIDHGNHiMNKCKNGF-TPLHNAI-IHNRSAIELLINNASINDQDIDGSTPLHHA 261
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 94-242 2.33e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 53.14  E-value: 2.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531541114  94 EHVKIVEYLINQGASVSSANSKGSTALHYAVLKDNRELMELLVTKGALLEVDSMDG-TPLQIALSRVNVETVKFLLSHGA 172
Cdd:PHA02876  156 DELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDlSVLECAVDSKNIDTIKAIIDNRS 235

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531541114 173 KPN---------ICSLVLESPLVLAIKAHSFECFDL---------------------LLKARADPNMY-IVGFSPLSYAA 221
Cdd:PHA02876  236 NINkndlsllkaIRNEDLETSLLLYDAGFSVNSIDDckntplhhasqapslsrlvpkLLERGADVNAKnIKGETPLYLMA 315

                         170       180
                  ....*....|....*....|..
gi 2531541114 222 KVG-DTKFLKSLLDAGADPNSS 242
Cdd:PHA02876  316 KNGyDTENIRTLIMLGADVNAA 337
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 150-242 4.35e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 51.97  E-value: 4.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531541114 150 TPLQIALSRVNVETVKFLLSHGAKPNICSLVLESPLVL-----AIKAHSFECFDLLLKARADPNMYIV-GFSPLSYAA-- 221
Cdd:PHA03100   37 LPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYlsnikYNLTDVKEIVKLLLEYGANVNAPDNnGITPLLYAIsk 116

                          90       100
                  ....*....|....*....|.
gi 2531541114 222 KVGDTKFLKSLLDAGADPNSS 242
Cdd:PHA03100  117 KSNSYSIVEYLLDNGANVNIK 137
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 66-233 1.95e-06

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: 50.14  E-value: 1.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531541114  66 KFLIHNLKVHIDART--------FTRDTP-----LIAAAKGEhvKIVEYLINqgASVSSANSKGSTALHYAVLKDNRELM 132
Cdd:cd22194    82 DFLMHKLTASDTGKTclmkallnINENTKeivriLLAFAEEN--GILDRFIN--AEYTEEAYEGQTALNIAIERRQGDIV 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531541114 133 ELLVTKGALLEV----------DSMDG-----TPLQIALSRVNVETVKFLLSHGAKP-----NICSLVLESPLVLA--IK 190
Cdd:cd22194   158 KLLIAKGADVNAhakgvffnpkYKHEGfyfgeTPLALAACTNQPEIVQLLMEKESTDitsqdSRGNTVLHALVTVAedSK 237

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2531541114 191 AHS---FECFDLLLKARADPNMYIV----GFSPLSYAAKVGDTKFLKSLL 233
Cdd:cd22194   238 TQNdfvKRMYDMILLKSENKNLETIrnneGLTPLQLAAKMGKAEILKYIL 287
Ank_4 pfam13637
Ankyrin repeats (many copies);
52-103 2.06e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.57  E-value: 2.06e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2531541114  52 VLHHAAEIGHFQICKFLIHNlKVHIDARTFTRDTPLIAAAKGEHVKIVEYLI 103
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEK-GADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 13-181 2.92e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 49.22  E-value: 2.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531541114  13 EAGASGDLKKLKE--MRRKVGDDTelrricdVYTDfstGRCVLHHAAEIGHFQICKFLIHNlKVHIDARTFTRDTPLIAA 90
Cdd:PHA02875   74 DAVEEGDVKAVEEllDLGKFADDV-------FYKD---GMTPLHLATILKKLDIMKLLIAR-GADPDIPNTDKFSPLHLA 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531541114  91 AKGEHVKIVEYLINQGASVSSANSKGSTALHYAVLKDNRELMELLVTKGALLEVDSMDG--TPLQIALSRVNVETVKFLL 168
Cdd:PHA02875  143 VMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcvAALCYAIENNKIDIVRLFI 222

                         170
                  ....*....|...
gi 2531541114 169 SHGAKPNICSLVL 181
Cdd:PHA02875  223 KRGADCNIMFMIE 235
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 86-265 2.67e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 46.41  E-value: 2.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531541114  86 PLIAAAKGEHVKIVEYLINQGASVSSANSKGSTALHYAVLKDNRELMELLVtkgALLEVDSMDGTPLQI--ALSRVNVET 163
Cdd:PHA02878   40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMI---RSINKCSVFYTLVAIkdAFNNRNVEI 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531541114 164 VKFLLSHGAKPNICSLVLESPLVLAIKAHSFECFDLLLKARADPNMYI--VGFSPLSYAAKVGDTKFLKSLLDAGADPNS 241
Cdd:PHA02878  117 FKIILTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDrhKGNTALHYATENKDQRLTELLLSYGANVNI 196

                         170       180
                  ....*....|....*....|....
gi 2531541114 242 SLIGHVKIIEDAALVRDREGVEIL 265
Cdd:PHA02878  197 PDKTNNSPLHHAVKHYNKPIVHIL 220
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 47-172 6.83e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 45.24  E-value: 6.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531541114  47 STGRCVLHHAAEIGHFQICKFLI-HNLKVHIdaRTFTRDTPLIAAAKGEHVKIVEYLiNQGASVSSANSKGSTaLHYAVL 125
Cdd:PLN03192  556 SKGRTPLHIAASKGYEDCVLVLLkHACNVHI--RDANGNTALWNAISAKHHKIFRIL-YHFASISDPHAAGDL-LCTAAK 631

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2531541114 126 KDNRELMELLVTKGalLEVDSMD---GTPLQIALSRVNVETVKFLLSHGA 172
Cdd:PLN03192  632 RNDLTAMKELLKQG--LNVDSEDhqgATALQVAMAEDHVDMVRLLIMNGA 679
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 67-241 1.27e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 44.47  E-value: 1.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531541114  67 FLIHNLKVH-IDARTFTRDTpliaaaKGEHVKIveyliNQGASVSSANSKGSTALhyavlkdnreLMELLVTKGALLEVD 145
Cdd:PLN03192  497 FLQHHKELHdLNVGDLLGDN------GGEHDDP-----NMASNLLTVASTGNAAL----------LEELLKAKLDPDIGD 555

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531541114 146 SMDGTPLQIALSRVNVETVKFLLSHGAKPNICSLVLESPLVLAIKAHSFECFDLLLKARADPNMYIVGfSPLSYAAKVGD 225
Cdd:PLN03192  556 SKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAG-DLLCTAAKRND 634

                         170
                  ....*....|....*.
gi 2531541114 226 TKFLKSLLDAGADPNS 241
Cdd:PLN03192  635 LTAMKELLKQGLNVDS 650
PHA02798 PHA02798
ankyrin-like protein; Provisional
 64-240 1.57e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 44.06  E-value: 1.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531541114  64 ICKFLIHNlKVHIDARTFTRDTPLIAAAKGEHV---KIVEYLINQGASVSSANSKGSTALHYAVLKDNR---ELMELLVT 137
Cdd:PHA02798   91 IVKILIEN-GADINKKNSDGETPLYCLLSNGYInnlEILLFMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLE 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531541114 138 KGALLEV-------DSMDgTPLQIALSRVNVETVKFLLSHG---------AKPNICSLVLEspLVLAIKAHSFECFDLLL 201
Cdd:PHA02798  170 KGVDINThnnkekyDTLH-CYFKYNIDRIDADILKLFVDNGfiinkenksHKKKFMEYLNS--LLYDNKRFKKNILDFIF 246

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2531541114 202 KaRADPNMY-IVGFSPLSYAAKVGDTKFLKSLLDAGADPN 240
Cdd:PHA02798  247 S-YIDINQVdELGFNPLYYSVSHNNRKIFEYLLQLGGDIN 285
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 41-233 3.04e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 42.94  E-value: 3.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531541114  41 DVYTDFSTGRCVLHHAAeighfqickflihnlkVHIDARTFTRDTPLIAAAKGEhvKIVEYLINqgASVSSANSKGSTAL 120
Cdd:cd21882    18 SAYQRGATGKTCLHKAA----------------LNLNDGVNEAIMLLLEAAPDS--GNPKELVN--APCTDEFYQGQTAL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531541114 121 HYAVLKDNRELMELLVTKGALLEVDSmDGT---------------PLQIALSRVNVETVKFLLSHGAKP-------NICS 178
Cdd:cd21882    78 HIAIENRNLNLVRLLVENGADVSARA-TGRffrkspgnlfyfgelPLSLAACTNQEEIVRLLLENGAQPaaleaqdSLGN 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2531541114 179 LVLESPLVLAIKA---HSFEC--FDLLLK--ARADPNMYI------VGFSPLSYAAKVGDTKFLKSLL 233
Cdd:cd21882   157 TVLHALVLQADNTpenSAFVCqmYNLLLSygAHLDPTQQLeeipnhQGLTPLKLAAVEGKIVMFQHIL 224
PHA03095 PHA03095
ankyrin-like protein; Provisional
 96-242 3.68e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 42.70  E-value: 3.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531541114  96 VKIVEYLINQGASVSSANSKGSTALHYAV---LKDNRELMELLVTKGALLEVDSMDG-TPLQIALSRVNVETV-KFLLSH 170
Cdd:PHA03095   27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLhysSEKVKDIVRLLLEAGADVNAPERCGfTPLHLYLYNATTLDViKLLIKA 106

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2531541114 171 GAKPNICSLVLESPLvlaikahsfecfdlllkaradpNMYIVGFSPlsyaakvgDTKFLKSLLDAGADPNSS 242
Cdd:PHA03095  107 GADVNAKDKVGRTPL----------------------HVYLSGFNI--------NPKVIRLLLRKGADVNAL 148
Ank_4 pfam13637
Ankyrin repeats (many copies);
116-168 4.58e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.02  E-value: 4.58e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2531541114 116 GSTALHYAVLKDNRELMELLVTKGA-LLEVDSMDGTPLQIALSRVNVETVKFLL 168
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGAdINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 36-176 9.44e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 41.55  E-value: 9.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531541114  36 LRRICDVYTDFSTGRCVLHHAAEIGH--FQICKFLIhNLKVHIDARTFTRDTPLIAAAKGEHVK--IVEYLINQGASVSS 111
Cdd:PHA03095  174 IDAGADVYAVDDRFRSLLHHHLQSFKprARIVRELI-RAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIAGISINA 252

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2531541114 112 ANSKGSTALHYAVLKDNRELMELLVTKGALLEVDSMDG-TPLQIALSRVNVETVKFLLShgAKPNI 176
Cdd:PHA03095  253 RNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGnTPLSLMVRNNNGRAVRAALA--KNPSA 316
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 150-176 1.64e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.64  E-value: 1.64e-03
                           10        20
                   ....*....|....*....|....*..
gi 2531541114  150 TPLQIALSRVNVETVKFLLSHGAKPNI 176
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 36-140 1.70e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 41.01  E-value: 1.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531541114  36 LRRICDVYTDFSTGRCVLHHAAEIGHFQICKFLIHNLKVhidARTFTRDTPLIAAAKGEHVKIVEYLINQGASVSSANSK 115
Cdd:PLN03192  578 LKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASI---SDPHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQ 654

                          90       100
                  ....*....|....*....|....*
gi 2531541114 116 GSTALHYAVLKDNRELMELLVTKGA 140
Cdd:PLN03192  655 GATALQVAMAEDHVDMVRLLIMNGA 679
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 114-241 2.29e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 40.25  E-value: 2.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531541114 114 SKGSTALHYAVLKDNRELMEllvTKGALLEVDSMDGTPLQIALSRVnveTVKFLLSHGAkpnicslvlespLVLAIKAHS 193
Cdd:cd21882    24 ATGKTCLHKAALNLNDGVNE---AIMLLLEAAPDSGNPKELVNAPC---TDEFYQGQTA------------LHIAIENRN 85

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2531541114 194 FECFDLLLKARAD--------------PNMYIVGFSPLSYAAKVGDTKFLKSLLDAGADPNS 241
Cdd:cd21882    86 LNLVRLLVENGADvsaratgrffrkspGNLFYFGELPLSLAACTNQEEIVRLLLENGAQPAA 147
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 43-169 2.30e-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: 40.16  E-value: 2.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531541114  43 YTD-FSTGRCVLHHAAEIGHFQICKFLIHN-LKVHIDART------------FTRDTPLIAAAKGEHVKIVEYLI---NQ 105
Cdd:cd22193    69 YTDeYYEGQTALHIAIERRQGDIVALLVENgADVHAHAKGrffqpkyqgegfYFGELPLSLAACTNQPDIVQYLLeneHQ 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531541114 106 GASVSSANSKGSTALHYAVL-----KDNRELM----ELLVTKGA-------LLEVDSMDG-TPLQIALSRVNVETVKFLL 168
Cdd:cd22193   149 PADIEAQDSRGNTVLHALVTvadntKENTKFVtrmyDMILIRGAklcptveLEEIRNNDGlTPLQLAAKMGKIEILKYIL 228


                  .
gi 2531541114 169 S 169
Cdd:cd22193   229 Q 229
Ank_4 pfam13637
Ankyrin repeats (many copies);
150-201 3.49e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 35.33  E-value: 3.49e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2531541114 150 TPLQIALSRVNVETVKFLLSHGAKPNICSLVLESPLVLAIKAHSFECFDLLL 201
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
68-123 3.81e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.40  E-value: 3.81e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2531541114  68 LIHNLKVHIDARTFTRDTPLIAAAKGEHVKIVEYLINQGASVSSANSKGSTALHYA 123
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 115-140 3.89e-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: 34.87  E-value: 3.89e-03
                           10        20
                   ....*....|....*....|....*.
gi 2531541114  115 KGSTALHYAVLKDNRELMELLVTKGA 140
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGA 26
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 53-164 4.38e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 39.18  E-value: 4.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531541114  53 LHHAAEIGHFQICKFLIHNLKvHIDARTFTRDTPLIAAAKgEHVKIVEYLINQgASVSSANSKGSTALHYAVLKD-NREL 131
Cdd:PHA02874  194 LHNAAEYGDYACIKLLIDHGN-HIMNKCKNGFTPLHNAII-HNRSAIELLINN-ASINDQDIDGSTPLHHAINPPcDIDI 270

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2531541114 132 MELLVTKGALLEVDSMDG-TPLQIALSRVNVETV 164
Cdd:PHA02874  271 IDILLYHKADISIKDNKGeNPIDTAFKYINKDPV 304
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 84-113 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. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 34.57  E-value: 5.56e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2531541114  84 DTPL-IAAAKGEHVKIVEYLINQGASVSSAN 113
Cdd:pfam00023   3 NTPLhLAAGRRGNLEIVKLLLSKGADVNARD 33
Ank_5 pfam13857
Ankyrin repeats (many copies);
102-155 5.82e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.01  E-value: 5.82e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2531541114 102 LINQG-ASVSSANSKGSTALHYAVLKDNRELMELLVTKGALLEVDSMDG-TPLQIA 155
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGlTALDLA 56
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 84-174 5.82e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 37.88  E-value: 5.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531541114  84 DTPLIAAAKGEHV--KIVEYLINQGASVS-SANSKGSTALHYAVLKD---NRELMELLVTKGALLEVDSMDG-TPLQIAL 156
Cdd:PHA02859   52 ETPIFSCLEKDKVnvEILKFLIENGADVNfKTRDNNLSALHHYLSFNknvEPEILKILIDSGSSITEEDEDGkNLLHMYM 131

                          90       100
                  ....*....|....*....|
gi 2531541114 157 SR--VNVETVKFLLSHGAKP 174
Cdd:PHA02859  132 CNfnVRINVIKLLIDSGVSF 151
PHA02741 PHA02741
hypothetical protein; Provisional
 88-167 8.27e-03

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 36.94  E-value: 8.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2531541114  88 IAAAKGEH---VKIVEYLINQGASVSSANS-KGSTALHYAVLKDNRELMELLVTK-GALLEVDSMDG-TPLQIALSRVNV 161
Cdd:PHA02741   66 IAAEKHEAqlaAEIIDHLIELGADINAQEMlEGDTALHLAAHRRDHDLAEWLCCQpGIDLHFCNADNkSPFELAIDNEDV 145


                  ....*.
gi 2531541114 162 ETVKFL 167
Cdd:PHA02741  146 AMMQIL 151
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 213-240 9.43e-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: 33.72  E-value: 9.43e-03
                           10        20
                   ....*....|....*....|....*...
gi 2531541114  213 GFSPLSYAAKVGDTKFLKSLLDAGADPN 240
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADIN 29
 
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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