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Conserved domains on  [gi|50540222|ref|NP_001002578|]
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ankyrin repeat domain-containing protein 54 [Danio rerio]

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];
129-231 9.88e-31

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 117.36  E-value: 9.88e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540222 129 LREAANSNDIDTVRRLLEDDTDPCAADDKGRTALHFSSCNGNETIVQLLLSYGADPNQRDSLGNTPLHLAACTNHVPVIT 208
Cdd:COG0666  91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                        90       100
                ....*....|....*....|...
gi 50540222 209 TLLRGGARVDALDRAGRTPLHLA 231
Cdd:COG0666 171 LLLEAGADVNARDNDGETPLHLA 193
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
129-231 9.88e-31

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 117.36  E-value: 9.88e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540222 129 LREAANSNDIDTVRRLLEDDTDPCAADDKGRTALHFSSCNGNETIVQLLLSYGADPNQRDSLGNTPLHLAACTNHVPVIT 208
Cdd:COG0666  91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                        90       100
                ....*....|....*....|...
gi 50540222 209 TLLRGGARVDALDRAGRTPLHLA 231
Cdd:COG0666 171 LLLEAGADVNARDNDGETPLHLA 193
Ank_2 pfam12796
Ankyrin repeats (3 copies);
129-221 6.64e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 82.47  E-value: 6.64e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540222   129 LREAANSNDIDTVRRLLEDDTDPCAADDKGRTALHFSSCNGNETIVQLLLSYgADPNQRDSlGNTPLHLAACTNHVPVIT 208
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 50540222   209 TLLRGGARVDALD 221
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 126-235 7.17e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 80.69  E-value: 7.17e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540222  126 VKRLREAANSNDIDT--VRRLLEDDTDPCAAD-DKGRTALHFSSCNGNETIVQLLLSYGADPNQRDSLGNTPLHLAACTN 202
Cdd:PHA02878 133 LVYIDKKSKDDIIEAeiTKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHY 212

                         90       100       110
                 ....*....|....*....|....*....|...
gi 50540222  203 HVPVITTLLRGGARVDALDRAGRTPLHLARSKL 235
Cdd:PHA02878 213 NKPIVHILLENGASTDARDKCGNTPLHISVGYC 245
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 129-250 3.55e-11

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: 63.88  E-value: 3.55e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540222 129 LREAANSNDIDTVRRLLE-DDTDPCA--------------ADD------------------------KGRTALHFSSCNG 169
Cdd:cd22192  21 LLLAAKENDVQAIKKLLKcPSCDLFQrgalgetalhvaalYDNleaavvlmeaapelvnepmtsdlyQGETALHIAVVNQ 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540222 170 NETIVQLLLSYGAD------------PNQRDSL--GNTPLHLAACTNHVPVITTLLRGGARVDALDRAGRTPLH---LAR 232
Cdd:cd22192 101 NLNLVRELIARGADvvspratgtffrPGPKNLIyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHilvLQP 180

                       170       180
                ....*....|....*....|....*...
gi 50540222 233 SK----------LNILQEGDSRSLETLR 250
Cdd:cd22192 181 NKtfacqmydliLSYDKEDDLQPLDLVP 208
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 157-279 3.70e-06

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 48.54  E-value: 3.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540222   157 KGRTALHFSSCNGNETIVQLLLSYGADPNQR------------DSL--GNTPLHLAACTNHVPVITTLLRGGARVDALDR 222
Cdd:TIGR00870 127 PGITALHLAAHRQNYEIVKLLLERGASVPARacgdffvksqgvDSFyhGESPLNAAACLGSPSIVALLSEDPADILTADS 206

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 50540222   223 AGRTPLHLArsklnILQEGDSRSLETLRgevtqiIQMLREYLNIMGQSEEREKLEHI 279
Cdd:TIGR00870 207 LGNTLLHLL-----VMENEFKAEYEELS------CQMYNFALSLLDKLRDSKELEVI 252
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 157-185 9.87e-06

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.80  E-value: 9.87e-06
                           10        20
                   ....*....|....*....|....*....
gi 50540222    157 KGRTALHFSSCNGNETIVQLLLSYGADPN 185
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
129-231 9.88e-31

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 117.36  E-value: 9.88e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540222 129 LREAANSNDIDTVRRLLEDDTDPCAADDKGRTALHFSSCNGNETIVQLLLSYGADPNQRDSLGNTPLHLAACTNHVPVIT 208
Cdd:COG0666  91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                        90       100
                ....*....|....*....|...
gi 50540222 209 TLLRGGARVDALDRAGRTPLHLA 231
Cdd:COG0666 171 LLLEAGADVNARDNDGETPLHLA 193
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
129-236 2.04e-29

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 113.90  E-value: 2.04e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540222 129 LREAANSNDIDTVRRLLEDDTDPCAADDKGRTALHFSSCNGNETIVQLLLSYGADPNQRDSLGNTPLHLAACTNHVPVIT 208
Cdd:COG0666 124 LHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVK 203

                        90       100
                ....*....|....*....|....*...
gi 50540222 209 TLLRGGARVDALDRAGRTPLHLARSKLN 236
Cdd:COG0666 204 LLLEAGADVNAKDNDGKTALDLAAENGN 231
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
129-231 1.98e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 97.33  E-value: 1.98e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540222 129 LREAANSNDIDTVRRLLEDDTDPCAADDKGRTALHFSSCNGNETIVQLLLSYGADPNQRDSLGNTPLHLAACTNHVPVIT 208
Cdd:COG0666  58 LLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVK 137

                        90       100
                ....*....|....*....|...
gi 50540222 209 TLLRGGARVDALDRAGRTPLHLA 231
Cdd:COG0666 138 LLLEAGADVNAQDNDGNTPLHLA 160
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
129-238 2.91e-21

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 91.55  E-value: 2.91e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540222 129 LREAANSNDIDTVRRLLEDDTDPCAADDKGRTALHFSSCNGNETIVQLLLSYGADPNQRDSLGNTPLHLAACTNHVPVIT 208
Cdd:COG0666 157 LHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVK 236

                        90       100       110
                ....*....|....*....|....*....|
gi 50540222 209 TLLRGGARVDALDRAGRTPLHLARSKLNIL 238
Cdd:COG0666 237 LLLEAGADLNAKDKDGLTALLLAAAAGAAL 266
Ank_2 pfam12796
Ankyrin repeats (3 copies);
129-221 6.64e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 82.47  E-value: 6.64e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540222   129 LREAANSNDIDTVRRLLEDDTDPCAADDKGRTALHFSSCNGNETIVQLLLSYgADPNQRDSlGNTPLHLAACTNHVPVIT 208
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 50540222   209 TLLRGGARVDALD 221
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 126-235 7.17e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 80.69  E-value: 7.17e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540222  126 VKRLREAANSNDIDT--VRRLLEDDTDPCAAD-DKGRTALHFSSCNGNETIVQLLLSYGADPNQRDSLGNTPLHLAACTN 202
Cdd:PHA02878 133 LVYIDKKSKDDIIEAeiTKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHY 212

                         90       100       110
                 ....*....|....*....|....*....|...
gi 50540222  203 HVPVITTLLRGGARVDALDRAGRTPLHLARSKL 235
Cdd:PHA02878 213 NKPIVHILLENGASTDARDKCGNTPLHISVGYC 245
PHA03095 PHA03095
ankyrin-like protein; Provisional
 131-237 9.65e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 77.37  E-value: 9.65e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540222  131 EAANSNDIDTVRRLLEDDTDPCAADDKGRTALHF---SSCNGNETIVQLLLSYGADPNQRDSLGNTPLHLAACTNHV-PV 206
Cdd:PHA03095  20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHLylhYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDV 99

                         90       100       110
                 ....*....|....*....|....*....|.
gi 50540222  207 ITTLLRGGARVDALDRAGRTPLHLARSKLNI 237
Cdd:PHA03095 100 IKLLIKAGADVNAKDKVGRTPLHVYLSGFNI 130
Ank_2 pfam12796
Ankyrin repeats (3 copies);
162-231 2.73e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.14  E-value: 2.73e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540222   162 LHFSSCNGNETIVQLLLSYGADPNQRDSLGNTPLHLAACTNHVPVITTLLRgGARVDALDRaGRTPLHLA 231
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYA 68
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 133-222 1.12e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 70.85  E-value: 1.12e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540222  133 ANSNDIDTVRRLLEDDTDPCAADDKGRTALHFSSCNGNETIVQLLLSYGADPNQRDSLGNTPLHLAACTNHVPVITTLLR 212
Cdd:PHA03100 167 VDINAKNRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLN 246

                         90
                 ....*....|
gi 50540222  213 GGARVDALDR 222
Cdd:PHA03100 247 NGPSIKTIIE 256
PHA03095 PHA03095
ankyrin-like protein; Provisional
 120-231 1.40e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 70.82  E-value: 1.40e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540222  120 GKDLHAVK-RLREA----ANSNDIDT--VRRLLEDDTDPCAADDKGRTALH----FSSCNgnETIVQLLLSYGADPNQRD 188
Cdd:PHA03095 177 GADVYAVDdRFRSLlhhhLQSFKPRAriVRELIRAGCDPAATDMLGNTPLHsmatGSSCK--RSLVLPLLIAGISINARN 254

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 50540222  189 SLGNTPLHLAACTNHVPVITTLLRGGARVDALDRAGRTPLHLA 231
Cdd:PHA03095 255 RYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLM 297
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
122-231 3.96e-13

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 68.44  E-value: 3.96e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540222 122 DLHAVKRLREAANSNDIDTVRRLLEDDTDPCAADDKGRTALHFSSCNGNETIVQLLLSYGADPNQRDSLGNTPLHLAACT 201
Cdd:COG0666  18 LLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARN 97

                        90       100       110
                ....*....|....*....|....*....|
gi 50540222 202 NHVPVITTLLRGGARVDALDRAGRTPLHLA 231
Cdd:COG0666  98 GDLEIVKLLLEAGADVNARDKDGETPLHLA 127
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 146-231 5.87e-13

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 69.16  E-value: 5.87e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540222  146 EDDTDPCAADDKGRTALHFSScNGNETIVQLLLSYGADPNQRDSLGNTPLHLAACTNHVPVITTLLRGGARVDALDRAGR 225
Cdd:PTZ00322  71 EEVIDPVVAHMLTVELCQLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGK 149


                 ....*.
gi 50540222  226 TPLHLA 231
Cdd:PTZ00322 150 TPLELA 155
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 139-231 3.95e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 66.53  E-value: 3.95e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540222  139 DTVRRLLEDDTDPCAADDKGRTALHFSSCNGNETIVQLLLSYGADPNQRDSLGNTPLHLAACTNHVPVITTLLRGGARVD 218
Cdd:PHA02874 105 DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184

                         90
                 ....*....|...
gi 50540222  219 ALDRAGRTPLHLA 231
Cdd:PHA02874 185 VKDNNGESPLHNA 197
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 132-231 8.94e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 65.86  E-value: 8.94e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540222  132 AANSNDIDTVRRLLEDDTDPCAADDKGRTALH-FSSCNGNETIVQLLLSYGADPNQRDSLGNTPLHLAACTNHVPVITTL 210
Cdd:PHA02876 315 AKNGYDTENIRTLIMLGADVNAADRLYITPLHqASTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTL 394

                         90       100
                 ....*....|....*....|.
gi 50540222  211 LRGGARVDALDRAGRTPLHLA 231
Cdd:PHA02876 395 LDYGADIEALSQKIGTALHFA 415
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 123-239 1.69e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 64.30  E-value: 1.69e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540222  123 LHAVKRLREaansndIDTVRRLLEDDTDPCAADDKGRTALHFSSCNG-NET----IVQLLLSYGADPNQRDSLGNTPLHL 197
Cdd:PHA03100  39 LYLAKEARN------IDVVKILLDNGADINSSTKNNSTPLHYLSNIKyNLTdvkeIVKLLLEYGANVNAPDNNGITPLLY 112

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 50540222  198 AACT--NHVPVITTLLRGGARVDALDRAGRTPLHLA----RSKLNILQ 239
Cdd:PHA03100 113 AISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYlesnKIDLKILK 160
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 129-250 3.55e-11

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: 63.88  E-value: 3.55e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540222 129 LREAANSNDIDTVRRLLE-DDTDPCA--------------ADD------------------------KGRTALHFSSCNG 169
Cdd:cd22192  21 LLLAAKENDVQAIKKLLKcPSCDLFQrgalgetalhvaalYDNleaavvlmeaapelvnepmtsdlyQGETALHIAVVNQ 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540222 170 NETIVQLLLSYGAD------------PNQRDSL--GNTPLHLAACTNHVPVITTLLRGGARVDALDRAGRTPLH---LAR 232
Cdd:cd22192 101 NLNLVRELIARGADvvspratgtffrPGPKNLIyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHilvLQP 180

                       170       180
                ....*....|....*....|....*...
gi 50540222 233 SK----------LNILQEGDSRSLETLR 250
Cdd:cd22192 181 NKtfacqmydliLSYDKEDDLQPLDLVP 208
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 141-238 4.07e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 63.54  E-value: 4.07e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540222  141 VRRLLEDDTDPCAADDKGRTALHFSSCNGNETI-VQLLLSYGADPNQRDSLGNTPLHLAACTN-HVPVITTLLRGGARVD 218
Cdd:PHA02876 290 VPKLLERGADVNAKNIKGETPLYLMAKNGYDTEnIRTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGANVN 369

                         90       100
                 ....*....|....*....|
gi 50540222  219 ALDRAGRTPLHLARSKLNIL 238
Cdd:PHA02876 370 ARDYCDKTPIHYAAVRNNVV 389
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 129-212 6.73e-11

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 62.99  E-value: 6.73e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540222  129 LREAANSNDIDTVRRLLEDDTDPCAADDKGRTALHFSSCNGNETIVQLLLSYGADPNQRDSLGNTPLHLAACTNHVPVIT 208
Cdd:PTZ00322  86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165


                 ....
gi 50540222  209 TLLR 212
Cdd:PTZ00322 166 LLSR 169
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
129-228 1.32e-10

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 61.12  E-value: 1.32e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540222 129 LREAANSNDIDTVRRLLEDDTDPCAADDKGRTALHFSSCNGNETIVQLLLSYGADPNQRDSLGNTPLHLAACTNHVPVIT 208
Cdd:COG0666 190 LHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVK 269

                        90       100
                ....*....|....*....|
gi 50540222 209 TLLRGGARVDALDRAGRTPL 228
Cdd:COG0666 270 LLLLALLLLAAALLDLLTLL 289
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 135-231 6.30e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 59.68  E-value: 6.30e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540222  135 SNDIDTVRRLLEDDTDPCAADDKGRTALH-FSSCNGNET-IVQLLLSYGADPNQRDSL----------------GNTPLH 196
Cdd:PHA03100 118 SNSYSIVEYLLDNGANVNIKNSDGENLLHlYLESNKIDLkILKLLIDKGVDINAKNRVnyllsygvpinikdvyGFTPLH 197

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 50540222  197 LAACTNHVPVITTLLRGGARVDALDRAGRTPLHLA 231
Cdd:PHA03100 198 YAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIA 232
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 129-307 7.98e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 59.23  E-value: 7.98e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540222  129 LREAANSNDIDTVRRLLEDDTdpcAADD----KGRTALHFSSCNGNETIVQLLLSYGADPNQRDSLGNTPLHLAACTNHV 204
Cdd:PHA02875  72 LHDAVEEGDVKAVEELLDLGK---FADDvfykDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDI 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540222  205 PVITTLLRGGARVDALDRAGRTPLHLARSKLNI------LQEGDSRSLETLRGEVTQI--------IQMLREYL------ 264
Cdd:PHA02875 149 KGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIaickmlLDSGANIDYFGKNGCVAALcyaiennkIDIVRLFIkrgadc 228

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 50540222  265 NIMG--QSEEREKLEHISTQLQNTRTreqvdEVTDLLASFTSLSI 307
Cdd:PHA02875 229 NIMFmiEGEECTILDMICNMCTNLES-----EAIDALIADIAIRI 268
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 157-229 5.47e-09

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 57.12  E-value: 5.47e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540222 157 KGRTALHFSSCNGNETIVQLLLSYGADPNQRDS--------------LGNTPLHLAACTNHVPVITTLLRG---GARVDA 219
Cdd:cd22196  93 KGQTALHIAIERRNMHLVELLVQNGADVHARASgeffkkkkggpgfyFGELPLSLAACTNQLDIVKFLLENphsPADISA 172

                        90
                ....*....|
gi 50540222 220 LDRAGRTPLH 229
Cdd:cd22196 173 RDSMGNTVLH 182
PHA03095 PHA03095
ankyrin-like protein; Provisional
 134-229 6.79e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 56.57  E-value: 6.79e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540222  134 NSNDIDTVRRLLEDDTDPCAADDKGRTALH--FSSCNGNETIVQLLLSYGADPNQRDSLGNTPLHL----AACTnhVPVI 207
Cdd:PHA03095  93 NATTLDVIKLLIKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVllksRNAN--VELL 170

                         90       100
                 ....*....|....*....|..
gi 50540222  208 TTLLRGGARVDALDRAGRTPLH 229
Cdd:PHA03095 171 RLLIDAGADVYAVDDRFRSLLH 192
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 162-237 1.05e-08

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: 56.17  E-value: 1.05e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540222 162 LHFSSCNGNETIVQLLLSYGADPNQRDSLGNTPLH-LAACTNHVPV------ITTLLRGG--ARVDAL-DRAGRTPLHLA 231
Cdd:cd22192 140 LSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHiLVLQPNKTFAcqmydlILSYDKEDdlQPLDLVpNNQGLTPFKLA 219


                ....*.
gi 50540222 232 RSKLNI 237
Cdd:cd22192 220 AKEGNI 225
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 124-236 1.69e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 55.27  E-value: 1.69e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540222  124 HAVKRLREAANSNDIDTVRRLLEDDTDPCAADDKGRTALHFSSCNGNETIVQLLLSYGADPNQRD-SLGNTPLHLAACTN 202
Cdd:PHA02878 100 YTLVAIKDAFNNRNVEIFKIILTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDrHKGNTALHYATENK 179

                         90       100       110
                 ....*....|....*....|....*....|....
gi 50540222  203 HVPVITTLLRGGARVDALDRAGRTPLHLARSKLN 236
Cdd:PHA02878 180 DQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYN 213
Ank_4 pfam13637
Ankyrin repeats (many copies);
158-211 1.84e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.97  E-value: 1.84e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 50540222   158 GRTALHFSSCNGNETIVQLLLSYGADPNQRDSLGNTPLHLAACTNHVPVITTLL 211
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
129-178 3.00e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.20  E-value: 3.00e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 50540222   129 LREAANSNDIDTVRRLLEDDTDPCAADDKGRTALHFSSCNGNETIVQLLL 178
Cdd:pfam13637   5 LHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 129-238 4.81e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 53.81  E-value: 4.81e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540222  129 LREAANSNDIDTVRRLLEDDTDPCAADDKGRTALHFSSCNGNETIVQLLLSYGADPNQRDSLGNTPLHLAACTNHVPVIT 208
Cdd:PHA02874 128 LHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIK 207

                         90       100       110
                 ....*....|....*....|....*....|....
gi 50540222  209 TLLRGGARVDALDRAGRTPLHLA----RSKLNIL 238
Cdd:PHA02874 208 LLIDHGNHIMNKCKNGFTPLHNAiihnRSAIELL 241
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 144-231 4.87e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 54.10  E-value: 4.87e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540222  144 LLEDDTDPCAADDKGRTALHFSSCNGNETIVQLLLSYGADPNQRDSLGNTPL----------------HLAA-------- 199
Cdd:PLN03192 544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALwnaisakhhkifrilyHFASisdphaag 623

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 50540222  200 ---CT----NHVPVITTLLRGGARVDALDRAGRTPLHLA 231
Cdd:PLN03192 624 dllCTaakrNDLTAMKELLKQGLNVDSEDHQGATALQVA 662
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 157-280 8.97e-08

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: 53.35  E-value: 8.97e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540222 157 KGRTALHFSSCNGNETIVQLLLSYGADPNQRDS-------------LGNTPLHLAACTNHVPVITTLLRGGARVDAL--- 220
Cdd:cd21882  72 QGQTALHIAIENRNLNLVRLLVENGADVSARATgrffrkspgnlfyFGELPLSLAACTNQEEIVRLLLENGAQPAALeaq 151

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540222 221 DRAGRTPLHLArsklnILQEGDSRSLETLrgevtqIIQMLREYLNIMGQSEEREKLEHIS 280
Cdd:cd21882 152 DSLGNTVLHAL-----VLQADNTPENSAF------VCQMYNLLLSYGAHLDPTQQLEEIP 200
PHA02946 PHA02946
ankyin-like protein; Provisional
 141-228 1.01e-07

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 53.13  E-value: 1.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540222  141 VRRLLEDDTDPCAADDKGRTALHFSSCNGNETIVQLLLSYGADPNQRDSLGNTPLHLAACTNH--VPVITTLLRGGARV- 217
Cdd:PHA02946  55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYGAKIn 134

                         90
                 ....*....|.
gi 50540222  218 DALDRAGRTPL 228
Cdd:PHA02946 135 NSVDEEGCGPL 145
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 139-231 1.52e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 52.76  E-value: 1.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540222  139 DTVRRLLEDDTDPCAADDKGRTALHFSSCNGNETIVQLLLSYGADPNQRDSLGNTPLHLAAC-TNHVPVITTLLRGGARV 217
Cdd:PHA02876 356 DIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCgTNPYMSVKTLIDRGANV 435

                         90
                 ....*....|....
gi 50540222  218 DALDRAGRTPLHLA 231
Cdd:PHA02876 436 NSKNKDLSTPLHYA 449
PHA02946 PHA02946
ankyin-like protein; Provisional
 134-229 1.71e-07

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 52.36  E-value: 1.71e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540222  134 NSNDIDTVRRLLEddtdpcAADDKGRTALHFSSCN---GNETIVQLLLSYGADPNQRDSLGNTPLHLAACTNHVPVITTL 210
Cdd:PHA02946  18 NSKNLDVFRNMLQ------AIEPSGNYHILHAYCGikgLDERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAML 91

                         90
                 ....*....|....*....
gi 50540222  211 LRGGARVDALDRAGRTPLH 229
Cdd:PHA02946  92 LTHGADPNACDKQHKTPLY 110
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 132-238 1.72e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 52.37  E-value: 1.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540222  132 AANSNDIDTVRRLLEDDTDPCAADDKGRTALHFSSCNGNE-TIVQLLLSYGADPNQRDSLGNTPLHLAACTNHVP-VITT 209
Cdd:PHA02876 382 AAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPyMSVKTLIDRGANVNSKNKDLSTPLHYACKKNCKLdVIEM 461

                         90       100       110
                 ....*....|....*....|....*....|..
gi 50540222  210 LLRGGARVDALDRAGRTPLHLA---RSKLNIL 238
Cdd:PHA02876 462 LLDNGADVNAINIQNQYPLLIAleyHGIVNIL 493
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 133-228 2.15e-07

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 52.22  E-value: 2.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540222  133 ANSNDIDTVRRLLEDDTDPCAADDKGRTALH--FSSCNGNETIVQLLLSYGADPNQRDSLGNTPLH-----------LAA 199
Cdd:PHA02716 292 ARNIDISVVYSFLQPGVKLHYKDSAGRTCLHqyILRHNISTDIIKLLHEYGNDLNEPDNIGNTVLHtylsmlsvvniLDP 371

                         90       100       110
                 ....*....|....*....|....*....|..
gi 50540222  200 CTNH---VPVITTLLRGGARVDALDRAGRTPL 228
Cdd:PHA02716 372 ETDNdirLDVIQCLISLGADITAVNCLGYTPL 403
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 175-244 4.49e-07

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 48.72  E-value: 4.49e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 50540222  175 QLLLSYGADPNQRDSL-GNTPLHLAACTNHVPVITTLLRG-GARVDALDRAGRTPLHLARSK-----LNILQEGDSR 244
Cdd:PHA02736  75 KLLMEWGADINGKERVfGNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYVACERhdakmMNILRAKGAQ 151
Ank_5 pfam13857
Ankyrin repeats (many copies);
155-198 8.51e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.42  E-value: 8.51e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 50540222   155 DDKGRTALHFSSCNGNETIVQLLLSYGADPNQRDSLGNTPLHLA 198
Cdd:pfam13857  13 DGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 119-252 8.88e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 50.45  E-value: 8.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540222  119 IGKDLHAVKRLREAANSNDIDTVRRLLEDDTDPCAADDKGRTALHFSSCNGNETIVQLLLSYGADPN------------- 185
Cdd:PHA02876 139 INESIEYMKLIKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNiialddlsvleca 218

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540222  186 --------------QRDSLGNTPLHLAACTNHVPVITTLL--RGGARVDALDRAGRTPLH-------LARSKLNILQEGD 242
Cdd:PHA02876 219 vdsknidtikaiidNRSNINKNDLSLLKAIRNEDLETSLLlyDAGFSVNSIDDCKNTPLHhasqapsLSRLVPKLLERGA 298

                        170
                 ....*....|
gi 50540222  243 SRSLETLRGE 252
Cdd:PHA02876 299 DVNAKNIKGE 308
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 157-188 3.54e-06

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 43.05  E-value: 3.54e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 50540222   157 KGRTALHF-SSCNGNETIVQLLLSYGADPNQRD 188
Cdd:pfam00023   1 DGNTPLHLaAGRRGNLEIVKLLLSKGADVNARD 33
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 157-279 3.70e-06

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 48.54  E-value: 3.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540222   157 KGRTALHFSSCNGNETIVQLLLSYGADPNQR------------DSL--GNTPLHLAACTNHVPVITTLLRGGARVDALDR 222
Cdd:TIGR00870 127 PGITALHLAAHRQNYEIVKLLLERGASVPARacgdffvksqgvDSFyhGESPLNAAACLGSPSIVALLSEDPADILTADS 206

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 50540222   223 AGRTPLHLArsklnILQEGDSRSLETLRgevtqiIQMLREYLNIMGQSEEREKLEHI 279
Cdd:TIGR00870 207 LGNTLLHLL-----VMENEFKAEYEELS------CQMYNFALSLLDKLRDSKELEVI 252
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 129-233 4.63e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 48.14  E-value: 4.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540222  129 LREAANSNDIDTVRRLLEDDTDPCAADDKGRTALHFSSCNGN-ETIVQLLLSYGADPNQRDSLGNTPLHLAACTNH-VPV 206
Cdd:PHA02876 244 LLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTEN 323

                         90       100
                 ....*....|....*....|....*..
gi 50540222  207 ITTLLRGGARVDALDRAGRTPLHLARS 233
Cdd:PHA02876 324 IRTLIMLGADVNAADRLYITPLHQAST 350
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 121-231 6.83e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 47.27  E-value: 6.83e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540222  121 KDLHAVKRLREAANSNDIDTVRRLLEDDTDPCAADDKGRTALHFSSCNGNETIVQLLLSYGADPNQRDSLGNTPLHLAAC 200
Cdd:PHA02874 153 EDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII 232

                         90       100       110
                 ....*....|....*....|....*....|.
gi 50540222  201 TNHVPVitTLLRGGARVDALDRAGRTPLHLA 231
Cdd:PHA02874 233 HNRSAI--ELLINNASINDQDIDGSTPLHHA 261
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 157-229 6.89e-06

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: 47.48  E-value: 6.89e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540222 157 KGRTALHFSSCNGNETIVQLLLSYGADPNQRDS--------------LGNTPLHLAACTNHVPVITTLLRGG---ARVDA 219
Cdd:cd22193  75 EGQTALHIAIERRQGDIVALLVENGADVHAHAKgrffqpkyqgegfyFGELPLSLAACTNQPDIVQYLLENEhqpADIEA 154

                        90
                ....*....|
gi 50540222 220 LDRAGRTPLH 229
Cdd:cd22193 155 QDSRGNTVLH 164
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 157-185 9.87e-06

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.80  E-value: 9.87e-06
                           10        20
                   ....*....|....*....|....*....
gi 50540222    157 KGRTALHFSSCNGNETIVQLLLSYGADPN 185
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
PHA03095 PHA03095
ankyrin-like protein; Provisional
 141-223 1.51e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.17  E-value: 1.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540222  141 VRRLLEDDTDPCAADDKGRTALHFSSCNGNETIVQLLLSYGADPNQRDSLGNTPLHLAACTNHVPVITTLLRGGARVDAL 220
Cdd:PHA03095 240 VLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETV 319


                 ...
gi 50540222  221 DRA 223
Cdd:PHA03095 320 AAT 322
Ank_5 pfam13857
Ankyrin repeats (many copies);
177-231 1.72e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.56  E-value: 1.72e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 50540222   177 LLSYG-ADPNQRDSLGNTPLHLAACTNHVPVITTLLRGGARVDALDRAGRTPLHLA 231
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
191-249 3.61e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 40.72  E-value: 3.61e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 50540222   191 GNTPLHLAACTNHVPVITTLLRGGARVDALDRAGRTPLHLArsklniLQEGDSRSLETL 249
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFA------ASNGNVEVLKLL 53
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 126-229 4.12e-05

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 45.13  E-value: 4.12e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540222 126 VKRLREAANSNDIdtVRRLLedDTDPCAADDKGRTALHFSSCNGNETIVQLLLSYGAD-----------PNQRDS---LG 191
Cdd:cd22194 113 VRILLAFAEENGI--LDRFI--NAEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADvnahakgvffnPKYKHEgfyFG 188

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 50540222 192 NTPLHLAACTNHVPVITTLL-RGGARVDALDRAGRTPLH 229
Cdd:cd22194 189 ETPLALAACTNQPEIVQLLMeKESTDITSQDSRGNTVLH 227
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 131-231 4.24e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 44.60  E-value: 4.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540222  131 EAANSNDIDTVRRLLEDDTDPCAADDKGRTALHFSSCNGNETIVQLLLSYGADPNQRDSLGNTPLHLAACTNHVPVITTL 210
Cdd:PHA02875   8 DAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEEL 87

                         90       100
                 ....*....|....*....|..
gi 50540222  211 LRGGARV-DALDRAGRTPLHLA 231
Cdd:PHA02875  88 LDLGKFAdDVFYKDGMTPLHLA 109
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 191-222 4.54e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.97  E-value: 4.54e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 50540222   191 GNTPLHLAAC-TNHVPVITTLLRGGARVDALDR 222
Cdd:pfam00023   2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 157-229 4.85e-05

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


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 44.85  E-value: 4.85e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540222 157 KGRTALHFSSCNGNETIVQLLLSYGADPNQRDS-------------LGNTPLHLAACTNHVPVITTLLRGG---ARVDAL 220
Cdd:cd22197  93 RGHSALHIAIEKRSLQCVKLLVENGADVHARACgrffqkkqgtcfyFGELPLSLAACTKQWDVVNYLLENPhqpASLQAQ 172


                ....*....
gi 50540222 221 DRAGRTPLH 229
Cdd:cd22197 173 DSLGNTVLH 181
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 157-185 3.19e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.24  E-value: 3.19e-04
                          10        20
                  ....*....|....*....|....*....
gi 50540222   157 KGRTALHFSSCNGNETIVQLLLSYGADPN 185
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 191-219 5.47e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.80  E-value: 5.47e-04
                           10        20
                   ....*....|....*....|....*....
gi 50540222    191 GNTPLHLAACTNHVPVITTLLRGGARVDA 219
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 137-198 1.02e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 40.63  E-value: 1.02e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50540222  137 DIDTVRRLLEDDTDPCAADD-KGRTALHFSScnGNETIVQLLLSYGADPNQRDSLGNTPLHLA 198
Cdd:PHA02878 247 DYDILKLLLEHGVDVNAKSYiLGLTALHSSI--KSERKLKLLLEYGADINSLNSYKLTPLSSA 307
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 170-231 1.64e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 39.95  E-value: 1.64e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 50540222  170 NETIVQLLLSYGADPNQRDSLGNTPLHLAACTNHVPVITTLLRGGARVDALDRAGRTPLHLA 231
Cdd:PHA02874 103 EKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIA 164
PHA02741 PHA02741
hypothetical protein; Provisional
 131-199 2.67e-03

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 38.10  E-value: 2.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540222  131 EAANSNDIDTVRRLLEDDTDPC------AADDKGRTALHFSSCNGNE----TIVQLLLSYGADPNQRDSL-GNTPLHLAA 199
Cdd:PHA02741  27 EAARCGCFDIIARFTPFIRGDChaaalnATDDAGQMCIHIAAEKHEAqlaaEIIDHLIELGADINAQEMLeGDTALHLAA 106
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 129-236 3.03e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 39.18  E-value: 3.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50540222  129 LREAANSNDIDTVRRLLEDDTDPCAADDKGRTALHfSSCNGNETIVQLLLSyGADPNQRDSLGNTPLHLA---ACTnhVP 205
Cdd:PHA02874 194 LHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLH-NAIIHNRSAIELLIN-NASINDQDIDGSTPLHHAinpPCD--ID 269

                         90       100       110
                 ....*....|....*....|....*....|.
gi 50540222  206 VITTLLRGGARVDALDRAGRTPLHLARSKLN 236
Cdd:PHA02874 270 IIDILLYHKADISIKDNKGENPIDTAFKYIN 300
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 191-219 8.02e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 33.38  E-value: 8.02e-03
                          10        20
                  ....*....|....*....|....*....
gi 50540222   191 GNTPLHLAACTNHVPVITTLLRGGARVDA 219
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
 
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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