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Conserved domains on  [gi|315364424]
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Chain C, 26S proteasome non-ATPase regulatory subunit 10

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];
7-224 1.32e-46

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 155.88  E-value: 1.32e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424   7 NIMICNLAYSGKLDELKERILADKSLATRTDQDSRTALHWACSAGHTEIVEFLLQLGVPVNDKDDAGWSPLHIAASAG*D 86
Cdd:COG0666   54 GALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNL 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424  87 EIVKALLVKGAHVNAVNQNGCTPLHYAASKNRHEIAVMLLEGGANPDAKDHYDATAMHRAAAKGNLKMVHILLFYKASTN 166
Cdd:COG0666  134 EIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVN 213

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 315364424 167 IQDTEGNTPLHLACDEERVEEAKFLVTQGASIYIENKEEKTPLQVAKGGLGLILKRLA 224
Cdd:COG0666  214 AKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLL 271
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
7-224 1.32e-46

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 155.88  E-value: 1.32e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424   7 NIMICNLAYSGKLDELKERILADKSLATRTDQDSRTALHWACSAGHTEIVEFLLQLGVPVNDKDDAGWSPLHIAASAG*D 86
Cdd:COG0666   54 GALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNL 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424  87 EIVKALLVKGAHVNAVNQNGCTPLHYAASKNRHEIAVMLLEGGANPDAKDHYDATAMHRAAAKGNLKMVHILLFYKASTN 166
Cdd:COG0666  134 EIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVN 213

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 315364424 167 IQDTEGNTPLHLACDEERVEEAKFLVTQGASIYIENKEEKTPLQVAKGGLGLILKRLA 224
Cdd:COG0666  214 AKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLL 271
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 37-212 4.21e-25

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 101.96  E-value: 4.21e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424  37 DQDSRTALHWACSAGHTEIVEFLLQLGVPVNDKDDAGWSPLHIAASAG*DEIVKALLVKGAHVNAVNQNGCTPLHYAASK 116
Cdd:PHA02874 121 DAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEY 200

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424 117 NRHEIAVMLLEGGANPDAKDHYDATAMHRAAAKGnlKMVHILLFYKASTNIQDTEGNTPLHLA----CDEERVEeakFLV 192
Cdd:PHA02874 201 GDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHN--RSAIELLINNASINDQDIDGSTPLHHAinppCDIDIID---ILL 275

                        170       180
                 ....*....|....*....|
gi 315364424 193 TQGASIYIENKEEKTPLQVA 212
Cdd:PHA02874 276 YHKADISIKDNKGENPIDTA 295
Ank_2 pfam12796
Ankyrin repeats (3 copies);
44-136 1.55e-24

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.87  E-value: 1.55e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424   44 LHWACSAGHTEIVEFLLQLGVPVNDKDDAGWSPLHIAASAG*DEIVKaLLVKGAHVNAVNqNGCTPLHYAASKNRHEIAV 123
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVK-LLLEHADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 315364424  124 MLLEGGANPDAKD 136
Cdd:pfam12796  79 LLLEKGADINVKD 91
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 42-182 2.28e-10

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 59.64  E-value: 2.28e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424  42 TALHWACSAGHTEIVEFLLQ-----LGVPVNDKDDAGWSPLHIAASAG*DEIVKALLVKGAHVNAVNQNGCT-------- 108
Cdd:cd22192   53 TALHVAALYDNLEAAVVLMEaapelVNEPMTSDLYQGETALHIAVVNQNLNLVRELIARGADVVSPRATGTFfrpgpknl 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424 109 ------PLHYAASKNRHEIAVMLLEGGANPDAKDHYDATAMHRAAAKGNLK----MVHILLFYKASTN------IQDTEG 172
Cdd:cd22192  133 iyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTfacqMYDLILSYDKEDDlqpldlVPNNQG 212

                        170
                 ....*....|
gi 315364424 173 NTPLHLACDE 182
Cdd:cd22192  213 LTPFKLAAKE 222
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 105-134 2.35e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 40.26  E-value: 2.35e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 315364424   105 NGCTPLHYAASKNRHEIAVMLLEGGANPDA 134
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 42-194 3.61e-04

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: 41.22  E-value: 3.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424   42 TALHwACSAGHTEIVEFLLQLGVPVNDKDDAGW--------------SPLHIAASAG*DEIVKALLVKGAHVNA-VNQNG 106
Cdd:TIGR00870  84 TLLH-AISLEYVDAVEAILLHLLAAFRKSGPLElandqytseftpgiTALHLAAHRQNYEIVKLLLERGASVPArACGDF 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424  107 C--TPLHYAASKNRHEIAVmllegganpdakdhydatamhrAAAKGNLKMVHILLFYKASTNIQDTEGNTPLHLACDE-E 183
Cdd:TIGR00870 163 FvkSQGVDSFYHGESPLNA----------------------AACLGSPSIVALLSEDPADILTADSLGNTLLHLLVMEnE 220

                         170
                  ....*....|.
gi 315364424  184 RVEEAKFLVTQ 194
Cdd:TIGR00870 221 FKAEYEELSCQ 231
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
7-224 1.32e-46

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 155.88  E-value: 1.32e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424   7 NIMICNLAYSGKLDELKERILADKSLATRTDQDSRTALHWACSAGHTEIVEFLLQLGVPVNDKDDAGWSPLHIAASAG*D 86
Cdd:COG0666   54 GALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNL 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424  87 EIVKALLVKGAHVNAVNQNGCTPLHYAASKNRHEIAVMLLEGGANPDAKDHYDATAMHRAAAKGNLKMVHILLFYKASTN 166
Cdd:COG0666  134 EIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVN 213

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 315364424 167 IQDTEGNTPLHLACDEERVEEAKFLVTQGASIYIENKEEKTPLQVAKGGLGLILKRLA 224
Cdd:COG0666  214 AKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLL 271
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
6-229 6.21e-43

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 146.64  E-value: 6.21e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424   6 SNIMICNLAYSGKLDELKERILADKSLATRTDQDSRTALHWACSAGHTEIVEFLLQLGVPVNDKDDAGWSPLHIAASAG* 85
Cdd:COG0666   20 LLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGD 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424  86 DEIVKALLVKGAHVNAVNQNGCTPLHYAASKNRHEIAVMLLEGGANPDAKDHYDATAMHRAAAKGNLKMVHILLFYKAST 165
Cdd:COG0666  100 LEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADV 179

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 315364424 166 NIQDTEGNTPLHLACDEERVEEAKFLVTQGASIYIENKEEKTPLQVAKGGLGLILKRLAEGEEA 229
Cdd:COG0666  180 NARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
13-209 5.18e-40

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 138.93  E-value: 5.18e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424  13 LAYSGKLDELKERILADKSLATRTDQDSRTALHWACSAGHTEIVEFLLQLGVPVNDKDDAGWSPLHIAASAG*DEIVKAL 92
Cdd:COG0666   93 AAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLL 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424  93 LVKGAHVNAVNQNGCTPLHYAASKNRHEIAVMLLEGGANPDAKDHYDATAMHRAAAKGNLKMVHILLFYKASTNIQDTEG 172
Cdd:COG0666  173 LEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDG 252

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 315364424 173 NTPLHLACDEERVEEAKFLVTQGASIYIENKEEKTPL 209
Cdd:COG0666  253 LTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
20-212 1.21e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 114.67  E-value: 1.21e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424  20 DELKERILADKSLATRTDQDSRTALHWACSAGHTEIVEFLLQLGVPVNDKDDAGWSPLHIAASAG*DEIVKALLVKGAHV 99
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424 100 NAVNQNGCTPLHYAASKNRHEIAVMLLEGGANPDAKDHYDATAMHRAAAKGNLKMVHILLFYKASTNIQDTEGNTPLHLA 179
Cdd:COG0666   81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                        170       180       190
                 ....*....|....*....|....*....|...
gi 315364424 180 CDEERVEEAKFLVTQGASIYIENKEEKTPLQVA 212
Cdd:COG0666  161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLA 193
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 37-212 4.21e-25

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 101.96  E-value: 4.21e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424  37 DQDSRTALHWACSAGHTEIVEFLLQLGVPVNDKDDAGWSPLHIAASAG*DEIVKALLVKGAHVNAVNQNGCTPLHYAASK 116
Cdd:PHA02874 121 DAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEY 200

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424 117 NRHEIAVMLLEGGANPDAKDHYDATAMHRAAAKGnlKMVHILLFYKASTNIQDTEGNTPLHLA----CDEERVEeakFLV 192
Cdd:PHA02874 201 GDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHN--RSAIELLINNASINDQDIDGSTPLHHAinppCDIDIID---ILL 275

                        170       180
                 ....*....|....*....|
gi 315364424 193 TQGASIYIENKEEKTPLQVA 212
Cdd:PHA02874 276 YHKADISIKDNKGENPIDTA 295
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 37-212 6.23e-25

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 102.45  E-value: 6.23e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424  37 DQDSRTALHWACSAGH-TEIVEFLLQLGVPVNDKDDAGWSPLHIAASAG*D-EIVKALLVKGAHVNAVNQNGCTPLHYAA 114
Cdd:PHA02876 270 DDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYDtENIRTLIMLGADVNAADRLYITPLHQAS 349

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424 115 SKNRH-EIAVMLLEGGANPDAKDHYDATAMHRAAAKGNLKMVHILLFYKASTNIQDTEGNTPLHLA-CDEERVEEAKFLV 192
Cdd:PHA02876 350 TLDRNkDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLI 429

                        170       180
                 ....*....|....*....|
gi 315364424 193 TQGASIYIENKEEKTPLQVA 212
Cdd:PHA02876 430 DRGANVNSKNKDLSTPLHYA 449
Ank_2 pfam12796
Ankyrin repeats (3 copies);
44-136 1.55e-24

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.87  E-value: 1.55e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424   44 LHWACSAGHTEIVEFLLQLGVPVNDKDDAGWSPLHIAASAG*DEIVKaLLVKGAHVNAVNqNGCTPLHYAASKNRHEIAV 123
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVK-LLLEHADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 315364424  124 MLLEGGANPDAKD 136
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 5-212 1.90e-24

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 100.12  E-value: 1.90e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424   5 VSNImICNLAYSGKLDELKERILADKSLATRTDQDSRTALHWACSAGHTEIVEFLLQLGVPVNDKDDAGWSPLHIAASAG 84
Cdd:PHA03100   1 LYSY-IVLTKSRIIKVKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424  85 *D-----EIVKALLVKGAHVNAVNQNGCTPLHYAASK--NRHEIAVMLLEGGANPDAKDHYDATAMHrAAAKGN---LKM 154
Cdd:PHA03100  80 YNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLH-LYLESNkidLKI 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 315364424 155 ----------------VHILLFYKASTNIQDTEGNTPLHLACDEERVEEAKFLVTQGASIYIENKEEKTPLQVA 212
Cdd:PHA03100 159 lkllidkgvdinaknrVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIA 232
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 36-200 3.94e-23

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 96.27  E-value: 3.94e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424  36 TDQDSRTALHWACSAGHT-----EIVEFLLQLGVPVNDKDDAGWSPLHIAASA--G*DEIVKALLVKGAHVNAVNQNGCT 108
Cdd:PHA03100  64 STKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGEN 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424 109 PLHYAASKNRHEIAV------------------MLLEGGANPDAKDHYDATAMHRAAAKGNLKMVHILLFYKASTNIQDT 170
Cdd:PHA03100 144 LLHLYLESNKIDLKIlkllidkgvdinaknrvnYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNK 223

                        170       180       190
                 ....*....|....*....|....*....|
gi 315364424 171 EGNTPLHLACDEERVEEAKFLVTQGASIYI 200
Cdd:PHA03100 224 YGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
PHA03095 PHA03095
ankyrin-like protein; Provisional
 42-212 1.29e-18

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 83.92  E-value: 1.29e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424  42 TALH-WACSAGHTEIVEFLLQLGVPVNDKDDAGWSPLHIAAS--AG*DEIVKALLVKGAHVNAVNQNGCTPLHYAASKNR 118
Cdd:PHA03095  85 TPLHlYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVYLSgfNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRN 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424 119 HEIAV--MLLEGGANPDAKDHYDATAMHRAA--AKGNLKMVHILLFYKASTNIQDTEGNTPLHLACDEERVEEAK--FLV 192
Cdd:PHA03095 165 ANVELlrLLIDAGADVYAVDDRFRSLLHHHLqsFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLvlPLL 244

                        170       180
                 ....*....|....*....|
gi 315364424 193 TQGASIYIENKEEKTPLQVA 212
Cdd:PHA03095 245 IAGISINARNRYGQTPLHYA 264
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 10-179 1.72e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 83.39  E-value: 1.72e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424  10 ICNLAYSGKLDELKERIL----ADKSLATRtDQDSrTALHWACSAGHTEIVEFLLQLGVPVNDKDDAGWSPLHIAASAG* 85
Cdd:PHA02878 136 IDKKSKDDIIEAEITKLLlsygADINMKDR-HKGN-TALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYN 213

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424  86 DEIVKALLVKGAHVNAVNQNGCTPLHYAASK-NRHEIAVMLLEGGANPDAKDH-YDATAMHRAAAkgNLKMVHILLFYKA 163
Cdd:PHA02878 214 KPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIK--SERKLKLLLEYGA 291

                        170
                 ....*....|....*.
gi 315364424 164 STNIQDTEGNTPLHLA 179
Cdd:PHA02878 292 DINSLNSYKLTPLSSA 307
PHA03095 PHA03095
ankyrin-like protein; Provisional
 41-209 1.87e-18

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 83.15  E-value: 1.87e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424  41 RTALHwACSAG---HTEIVEFLLQLGVPVNDKDDAGWSPLHIA-ASAG*D-EIVKALLVKGAHVNAVNQNGCTPLHYAA- 114
Cdd:PHA03095 118 RTPLH-VYLSGfniNPKVIRLLLRKGADVNALDLYGMTPLAVLlKSRNANvELLRLLIDAGADVYAVDDRFRSLLHHHLq 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424 115 -SKNRHEIAVMLLEGGANPDAKDHYDATAMHRAAAKGNLKMVHILLFYKA--STNIQDTEGNTPLHLAcdeerveeAKF- 190
Cdd:PHA03095 197 sFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVLPLLIAgiSINARNRYGQTPLHYA--------AVFn 268

                        170       180
                 ....*....|....*....|....*.
gi 315364424 191 -------LVTQGASIYIENKEEKTPL 209
Cdd:PHA03095 269 npracrrLIALGADINAVSSDGNTPL 294
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 44-202 1.89e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 83.39  E-value: 1.89e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424  44 LHWACSAGHTEIVEFLLQLGVPVNDKDDAGWSPLHIAASAG--------------------------------------- 84
Cdd:PHA02878  41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPnklgmkemirsinkcsvfytlvaikdafnnrnveifkii 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424  85 -------------------------*DEIVKALLVKGAHVNAVNQN-GCTPLHYAASKNRHEIAVMLLEGGANPDAKDHY 138
Cdd:PHA02878 121 ltnrykniqtidlvyidkkskddiiEAEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKT 200

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 315364424 139 DATAMHRAAAKGNLKMVHILLFYKASTNIQDTEGNTPLHLACDE-ERVEEAKFLVTQGASIYIEN 202
Cdd:PHA02878 201 NNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKS 265
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 56-138 9.91e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 78.17  E-value: 9.91e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424  56 VEFLLQLGVPVNDKDDAGWSPLHIAASAG*DEIVKALLVKGAHVNAVNQNGCTPLHYAASKNRHEIAVMLLEGGANPDAK 135
Cdd:PHA03100 175 VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTI 254


                 ...
gi 315364424 136 DHY 138
Cdd:PHA03100 255 IET 257
Ank_2 pfam12796
Ankyrin repeats (3 copies);
8-103 1.48e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.07  E-value: 1.48e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424    8 IMICnlAYSGKLDELKErILADKSLATRTDQDSRTALHWACSAGHTEIVEFLLQLGVPvnDKDDAGWSPLHIAASAG*DE 87
Cdd:pfam12796   1 LHLA--AKNGNLELVKL-LLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLE 75

                          90
                  ....*....|....*.
gi 315364424   88 IVKALLVKGAHVNAVN 103
Cdd:pfam12796  76 IVKLLLEKGADINVKD 91
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 8-198 1.49e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 77.72  E-value: 1.49e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424   8 IMICNLAYSGKLDELKeRILADKSLATRTDQDSRTALHWACSAGHTEIVEFLLQLGVPVNDKDDAGWSPLHIAASAG*DE 87
Cdd:PHA02875   4 VALCDAILFGELDIAR-RLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424  88 IVKALLVKGAHVNAV-NQNGCTPLHYAASKNRHEIAVMLLEGGANPDAKDHYDATAMHRAAAKGNLKMVHILLFYKASTN 166
Cdd:PHA02875  83 AVEELLDLGKFADDVfYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLD 162

                        170       180       190
                 ....*....|....*....|....*....|..
gi 315364424 167 IQDTEGNTPLHLACDEERVEEAKFLVTQGASI 198
Cdd:PHA02875 163 IEDCCGCTPLIIAMAKGDIAICKMLLDSGANI 194
Ank_2 pfam12796
Ankyrin repeats (3 copies);
110-202 2.90e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 71.30  E-value: 2.90e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424  110 LHYAASKNRHEIAVMLLEGGANPDAKDHYDATAMHRAAAKGNLKMVHILLfYKASTNIQDtEGNTPLHLACDEERVEEAK 189
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 315364424  190 FLVTQGASIYIEN 202
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 54-199 1.64e-15

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 74.68  E-value: 1.64e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424  54 EIVEFLLQLGVPVNDKDDAGWSPLHIAASAG*D---EIVKALLVKGAHVNAVNQNGCTPLH-YAASKNRHEIAVMLLEGG 129
Cdd:PHA03095  28 EEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEkvkDIVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAG 107

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 315364424 130 ANPDAKDHYDATAMHrAAAKG---NLKMVHILLFYKASTNIQDTEGNTPLHL-----ACDeerVEEAKFLVTQGASIY 199
Cdd:PHA03095 108 ADVNAKDKVGRTPLH-VYLSGfniNPKVIRLLLRKGADVNALDLYGMTPLAVllksrNAN---VELLRLLIDAGADVY 181
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 15-212 2.75e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 74.23  E-value: 2.75e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424  15 YSGKLDELKERILADKSLATRTDQDSRTALHWACSAGHTEIVEFLLQLGVPVNDKDDAGWSPLHIAASAG*DEIVKALLV 94
Cdd:PHA02874  10 YSGDIEAIEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLID 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424  95 KGA-----------------------HVNAVNQNGCTPLHYAASKNRHEIAVMLLEGGANPDAKDHYDATAMHRAAAKGN 151
Cdd:PHA02874  90 NGVdtsilpipciekdmiktildcgiDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNF 169

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 315364424 152 LKMVHILLFYKASTNIQDTEGNTPLHLACDEERVEEAKFLVTQGASIYIENKEEKTPLQVA 212
Cdd:PHA02874 170 FDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNA 230
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 47-205 4.26e-14

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 71.05  E-value: 4.26e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424  47 ACSAGHTEIVEFLLQLGVPVNDKDDAGWSPLHIAASAG*DEIVKALLVKGAHVNAVNQNGCTPLHYAASKNRHEIAVMLL 126
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILY 611

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 315364424 127 EGGANPDAkdHYDATAMHRAAAKGNLKMVHILLFYKASTNIQDTEGNTPLHLACDEERVEEAKFLVTQGASIYIENKEE 205
Cdd:PLN03192 612 HFASISDP--HAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDD 688
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 17-181 7.42e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 66.94  E-value: 7.42e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424  17 GKLDELKERILADKSLATRTDQDSRTALHWACSAGHTEIVEFLLQLG----VPVNDKddagWSPLHIAASAG*DEIVKAL 92
Cdd:PHA02875  79 GDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGadpdIPNTDK----FSPLHLAVMMGDIKGIELL 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424  93 LVKGAHVNAVNQNGCTPLHYAASKNRHEIAVMLLEGGANPD-AKDHYDATAMHRAAAKGNLKMVHILLFYKASTNIQDT- 170
Cdd:PHA02875 155 IDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDyFGKNGCVAALCYAIENNKIDIVRLFIKRGADCNIMFMi 234

                        170
                 ....*....|...
gi 315364424 171 --EGNTPLHLACD 181
Cdd:PHA02875 235 egEECTILDMICN 247
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 41-212 1.12e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 66.55  E-value: 1.12e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424  41 RTALHWACSAGHTEIVEFLLQLGVPVNDKDDAGWSPLHIAASAG*DEIVKALLVKGAHVNAVNQNGCTPLHYAASKNRHE 120
Cdd:PHA02875   3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424 121 IAVMLLEGGANPDAKDHYDA-TAMHRAAAKGNLKMVHILLFYKASTNIQDTEGNTPLHLACDEERVEEAKFLVTQGASIY 199
Cdd:PHA02875  83 AVEELLDLGKFADDVFYKDGmTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLD 162

                        170
                 ....*....|...
gi 315364424 200 IENKEEKTPLQVA 212
Cdd:PHA02875 163 IEDCCGCTPLIIA 175
Ank_4 pfam13637
Ankyrin repeats (many copies);
41-93 1.50e-12

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 60.37  E-value: 1.50e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 315364424   41 RTALHWACSAGHTEIVEFLLQLGVPVNDKDDAGWSPLHIAASAG*DEIVKALL 93
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 20-212 1.94e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 65.86  E-value: 1.94e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424  20 DELKERILADKSLATRTDQDsrtalhwacsagHTEIVEFLLQLGVPVNDKDDAGWSPLHIAASAG*DEIVKALLVKGAHV 99
Cdd:PHA02876 137 DKINESIEYMKLIKERIQQD------------ELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADV 204

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424 100 NAVNQNGCTPLHYAASKNR-----------------------------HEIAVMLLEGGANPDAKDHYDATAMHRAAAKG 150
Cdd:PHA02876 205 NIIALDDLSVLECAVDSKNidtikaiidnrsninkndlsllkairnedLETSLLLYDAGFSVNSIDDCKNTPLHHASQAP 284

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 315364424 151 NL-KMVHILLFYKASTNIQDTEGNTPLHL-ACDEERVEEAKFLVTQGASIYIENKEEKTPLQVA 212
Cdd:PHA02876 285 SLsRLVPKLLERGADVNAKNIKGETPLYLmAKNGYDTENIRTLIMLGADVNAADRLYITPLHQA 348
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 16-164 3.62e-12

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 65.27  E-value: 3.62e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424  16 SGKLDELkeriLADKSLATRTDQDSRTALHWACSAGHTEIVEFLLQLGVPVNDKDDAGWSPLHIAASAG*DEIVKaLLVK 95
Cdd:PLN03192 538 AALLEEL----LKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFR-ILYH 612

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 315364424  96 GAHVNAVNQNG---CTplhyAASKNRHEIAVMLLEGGANPDAKDHYDATAMHRAAAKGNLKMVHILLFYKAS 164
Cdd:PLN03192 613 FASISDPHAAGdllCT----AAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGAD 680
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 76-225 1.11e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 63.75  E-value: 1.11e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424  76 PLHIAASAG*DEIVKALLVKGAHVNAVNQNGCTPLHYA-------------ASKNR------------------------ 118
Cdd:PHA02878  40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIIckepnklgmkemiRSINKcsvfytlvaikdafnnrnveifki 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424 119 ---------------------------HEIAVMLLEGGANPDAKD-HYDATAMHRAAAKGNLKMVHILLFYKASTNIQDT 170
Cdd:PHA02878 120 iltnrykniqtidlvyidkkskddiieAEITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDK 199

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 315364424 171 EGNTPLHLACDEERVEEAKFLVTQGASIYIENKEEKTPLQVAKGGLG--LILKRLAE 225
Cdd:PHA02878 200 TNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKdyDILKLLLE 256
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 18-198 3.38e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 62.39  E-value: 3.38e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424  18 KLDELKERILADKSLATRTDQDSRTALHWACSAghTEIVEFLLQLGVPVNDKDDAGWSPLhIAASAG*DEIVKALLVKGA 97
Cdd:PHA02876  53 QIDIVEEIIQQNPELIYITDHKCHSTLHTICII--PNVMDIVISLTLDCDIILDIKYASI-ILNKHKLDEACIHILKEAI 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424  98 HVNAVNQNGCT-PLHYAAS-KNRHE-----IAVMLLEGGANPDAKDHYDATAMHRAAAKGNLKMVHILLFYKASTNIQDT 170
Cdd:PHA02876 130 SGNDIHYDKINeSIEYMKLiKERIQqdellIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIAL 209

                        170       180
                 ....*....|....*....|....*...
gi 315364424 171 EGNTPLHLACDEERVEEAKFLVTQGASI 198
Cdd:PHA02876 210 DDLSVLECAVDSKNIDTIKAIIDNRSNI 237
Ank_4 pfam13637
Ankyrin repeats (many copies);
73-126 3.78e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 56.51  E-value: 3.78e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 315364424   73 GWSPLHIAASAG*DEIVKALLVKGAHVNAVNQNGCTPLHYAASKNRHEIAVMLL 126
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
108-159 7.61e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.74  E-value: 7.61e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 315364424  108 TPLHYAASKNRHEIAVMLLEGGANPDAKDHYDATAMHRAAAKGNLKMVHILL 159
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 26-155 7.96e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 60.81  E-value: 7.96e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424  26 ILADKSLATRtDQDSRTALHWACSAGHT--EIVEFLLQLGVPVNDKDDAGWSPLHIAA--SAG*DEIVKALLVKGAHVNA 101
Cdd:PHA03095 174 IDAGADVYAV-DDRFRSLLHHHLQSFKPraRIVRELIRAGCDPAATDMLGNTPLHSMAtgSSCKRSLVLPLLIAGISINA 252

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 315364424 102 VNQNGCTPLHYAASKNRHEIAVMLLEGGANPDAKDHYDATAMHRAAAKGNLKMV 155
Cdd:PHA03095 253 RNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAV 306
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 42-182 2.28e-10

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 59.64  E-value: 2.28e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424  42 TALHWACSAGHTEIVEFLLQ-----LGVPVNDKDDAGWSPLHIAASAG*DEIVKALLVKGAHVNAVNQNGCT-------- 108
Cdd:cd22192   53 TALHVAALYDNLEAAVVLMEaapelVNEPMTSDLYQGETALHIAVVNQNLNLVRELIARGADVVSPRATGTFfrpgpknl 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424 109 ------PLHYAASKNRHEIAVMLLEGGANPDAKDHYDATAMHRAAAKGNLK----MVHILLFYKASTN------IQDTEG 172
Cdd:cd22192  133 iyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTfacqMYDLILSYDKEDDlqpldlVPNNQG 212

                        170
                 ....*....|
gi 315364424 173 NTPLHLACDE 182
Cdd:cd22192  213 LTPFKLAAKE 222
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 13-131 2.31e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 59.62  E-value: 2.31e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424  13 LAYSGKLDELKERILADKSLATRTDQDSRTALHWACSAGHTEIVEFLLQLGVPVNDKDDAGWSPLHIAASAG*DEIVKAL 92
Cdd:PHA02875 108 LATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKML 187

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 315364424  93 LVKGAHVNAVNQNGC-TPLHYAASKNRHEIAVMLLEGGAN 131
Cdd:PHA02875 188 LDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGAD 227
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 111-191 2.08e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.83  E-value: 2.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424 111 HYAASKNRHEIAVmLLEGGANPDAKDHYDATAMHRAAAKGNLKMVHILLFYKASTNIQDTEGNTPLHLACDEERVEEAKF 190
Cdd:PTZ00322  88 QLAASGDAVGARI-LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                 .
gi 315364424 191 L 191
Cdd:PTZ00322 167 L 167
Ank_2 pfam12796
Ankyrin repeats (3 copies);
143-212 4.18e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 52.04  E-value: 4.18e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 315364424  143 MHRAAAKGNLKMVHILLFYKASTNIQDTEGNTPLHLACDEERVEEAKFLVTQGAsiyIENKEE-KTPLQVA 212
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD---VNLKDNgRTALHYA 68
Ank_5 pfam13857
Ankyrin repeats (many copies);
35-80 4.42e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 51.19  E-value: 4.42e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 315364424   35 RTDQDSRTALHWACSAGHTEIVEFLLQLGVPVNDKDDAGWSPLHIA 80
Cdd:pfam13857  11 RLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02946 PHA02946
ankyin-like protein; Provisional
 14-182 1.05e-08

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 54.67  E-value: 1.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424  14 AYSG--KLDE-LKERILADKSLATRTDQDSRTALHWACSAGHTEIVEFLLQLGVPVNDKDDAGWSPLHIaASAG*DEIVK 90
Cdd:PHA02946  43 AYCGikGLDErFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYY-LSGTDDEVIE 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424  91 A--LLVK-GAHV-NAVNQNGCTPLhYAASKNRHEIAVMLLEGGANPDAKDHYDATAMHRAAAKGNLKMVHILLFYK--AS 164
Cdd:PHA02946 122 RinLLVQyGAKInNSVDEEGCGPL-LACTDPSERVFKKIMSIGFEARIVDKFGKNHIHRHLMSDNPKASTISWMMKlgIS 200

                        170
                 ....*....|....*...
gi 315364424 165 TNIQDTEGNTPLHLACDE 182
Cdd:PHA02946 201 PSKPDHDGNTPLHIVCSK 218
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 10-93 2.29e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 53.75  E-value: 2.29e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424  10 ICNLAYSGklDELKERILADKSLATRT-DQDSRTALHWACSAGHTEIVEFLLQLGVPVNDKDDAGWSPLHIAASAG*DEI 88
Cdd:PTZ00322  86 LCQLAASG--DAVGARILLTGGADPNCrDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREV 163


                 ....*
gi 315364424  89 VKALL 93
Cdd:PTZ00322 164 VQLLS 168
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 68-212 2.60e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 53.72  E-value: 2.60e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424  68 DKDDAGWSPLHIAASAG*DEIVKALLVKGAHVNAVNQNGCTPLHYAASKNRHEIAVMLLEGGANPDAKDHYDATAMHRAA 147
Cdd:PLN03192 520 HDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAI 599

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 315364424 148 AKGNLKMVHILLFYKASTNIQdTEGNTpLHLACDEERVEEAKFLVTQGASIYIENKEEKTPLQVA 212
Cdd:PLN03192 600 SAKHHKIFRILYHFASISDPH-AAGDL-LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVA 662
PHA02946 PHA02946
ankyin-like protein; Provisional
 84-185 3.12e-08

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 53.13  E-value: 3.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424  84 G*DE-IVKALLVKGAHVNAVNQNGCTPLHYAASKNRHEIAVMLLEGGANPDAKDHYDATAMHRAAAKGN--LKMVHILLF 160
Cdd:PHA02946  49 GLDErFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQ 128

                         90       100
                 ....*....|....*....|....*...
gi 315364424 161 YKASTNIQ-DTEGNTPLhLACDE--ERV 185
Cdd:PHA02946 129 YGAKINNSvDEEGCGPL-LACTDpsERV 155
Ank_5 pfam13857
Ankyrin repeats (many copies);
59-113 5.05e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.11  E-value: 5.05e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 315364424   59 LLQLG-VPVNDKDDAGWSPLHIAASAG*DEIVKALLVKGAHVNAVNQNGCTPLHYA 113
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 147-212 6.22e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.59  E-value: 6.22e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 315364424 147 AAKGNLKMVHILLFYKASTNIQDTEGNTPLHLACDEERVEEAKFLVTQGASIYIENKEEKTPLQVA 212
Cdd:PTZ00322  90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELA 155
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 37-163 1.02e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 51.99  E-value: 1.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424  37 DQDSRTALHWACSAGHTEIVEFLLQLGVPVNDKDDAGWSPLHIAASAG*DEI-VKALLVKGAHVNAVNQNGCTPLHYAAS 115
Cdd:PHA02876 372 DYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMsVKTLIDRGANVNSKNKDLSTPLHYACK 451

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 315364424 116 KN-RHEIAVMLLEGGANPDAKDHYDATAMhrAAAKGNLKMVHILLFYKA 163
Cdd:PHA02876 452 KNcKLDVIEMLLDNGADVNAINIQNQYPL--LIALEYHGIVNILLHYGA 498
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 42-105 1.19e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 51.59  E-value: 1.19e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 315364424  42 TALHWACSAGHTEIVEFLLQLGVPVNDKDDAGWSPLHIAASAG*DEIVKALLVKGAHVNAVNQN 105
Cdd:PHA03100 194 TPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 54-227 1.34e-07

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 51.68  E-value: 1.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424  54 EIVEFLLQ-------LGVPVN----DKDDAGWSPLHIAASAG*DEIVKALLVKGAHVNA---------VNQNGC-----T 108
Cdd:cd22194  111 EIVRILLAfaeengiLDRFINaeytEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAhakgvffnpKYKHEGfyfgeT 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424 109 PLHYAASKNRHEIAVMLLEgganpdakdhydatamhraaakgnlkmvhillfyKASTNI--QDTEGNTPLH-LACDEERV 185
Cdd:cd22194  191 PLALAACTNQPEIVQLLME----------------------------------KESTDItsQDSRGNTVLHaLVTVAEDS 236

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 315364424 186 EEAKFLVTQgasIY--------------IENKEEKTPLQV-AKGGLGLILKRLAEGE 227
Cdd:cd22194  237 KTQNDFVKR---MYdmillksenknletIRNNEGLTPLQLaAKMGKAEILKYILSRE 290
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 54-213 2.84e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 49.43  E-value: 2.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424  54 EIVEFLLQLGVPVNDK-DDAGWSPLHIAASAG*D---EIVKALLVKGAHVNAVNQNGCTPLH-YAASKN-RHEIAVMLLE 127
Cdd:PHA02859  67 EILKFLIENGADVNFKtRDNNLSALHHYLSFNKNvepEILKILIDSGSSITEEDEDGKNLLHmYMCNFNvRINVIKLLID 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424 128 GGANPDAKDhydatamhraaaKGNLKMVHILLFYKASTNIQDtegntplhlacdeerveeakFLVTQGASIYIENKEEKT 207
Cdd:PHA02859 147 SGVSFLNKD------------FDNNNILYSYILFHSDKKIFD--------------------FLTSLGIDINETNKSGYN 194


                 ....*.
gi 315364424 208 PLQVAK 213
Cdd:PHA02859 195 CYDLIK 200
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 29-134 3.31e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.28  E-value: 3.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424  29 DKSLATRTDQDSRTA-------LHWACSaGHTEIVEFLLQLGVPVNDKDDAGWSPLHIAASAG*DEIVKALLVKGAHVNA 101
Cdd:PTZ00322  65 DHNLTTEEVIDPVVAhmltvelCQLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTL 143

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 315364424 102 VNQNGCTPLHYAASKNRHEIAVMLL-------EGGAN--PDA 134
Cdd:PTZ00322 144 LDKDGKTPLELAEENGFREVVQLLSrhsqchfELGANakPDS 185
Ank_4 pfam13637
Ankyrin repeats (many copies);
141-192 4.77e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.34  E-value: 4.77e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 315364424  141 TAMHRAAAKGNLKMVHILLFYKASTNIQDTEGNTPLHLACDEERVEEAKFLV 192
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 78-161 7.04e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.51  E-value: 7.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424  78 HIAASaG*DEIVKALLVKGAHVNAVNQNGCTPLHYAASKNRHEIAVMLLEGGANPDAKDHYDATAMHRAAAKGNLKMVHI 157
Cdd:PTZ00322  88 QLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                 ....
gi 315364424 158 LLFY 161
Cdd:PTZ00322 167 LSRH 170
Ank_5 pfam13857
Ankyrin repeats (many copies);
124-179 1.84e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.87  E-value: 1.84e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 315364424  124 MLLEGGANPDAKDHYDATAMHRAAAKGNLKMVHILLFYKASTNIQDTEGNTPLHLA 179
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 105-137 1.85e-06

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 43.43  E-value: 1.85e-06
                          10        20        30
                  ....*....|....*....|....*....|....
gi 315364424  105 NGCTPLHYAASKNRH-EIAVMLLEGGANPDAKDH 137
Cdd:pfam00023   1 DGNTPLHLAAGRRGNlEIVKLLLSKGADVNARDK 34
PHA03095 PHA03095
ankyrin-like protein; Provisional
 36-135 2.24e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 47.71  E-value: 2.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424  36 TDQDSRTALHWA---CSAGHTEIVEFLLQlGVPVNDKDDAGWSPLHIAASAG*DEIVKALLVKGAHVNAVNQNGCTPLHY 112
Cdd:PHA03095 218 TDMLGNTPLHSMatgSSCKRSLVLPLLIA-GISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSL 296

                         90       100
                 ....*....|....*....|...
gi 315364424 113 AASKNRHEIAVMLLEggANPDAK 135
Cdd:PHA03095 297 MVRNNNGRAVRAALA--KNPSAE 317
PHA03095 PHA03095
ankyrin-like protein; Provisional
 114-211 2.85e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 47.33  E-value: 2.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424 114 ASKNRHEIAVMLLEGGANPDAKDHYDATAMH---RAAAKGNLKMVHILLFYKASTNIQDTEGNTPLHL-ACDEERVEEAK 189
Cdd:PHA03095  22 ASNVTVEEVRRLLAAGADVNFRGEYGKTPLHlylHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLyLYNATTLDVIK 101

                         90       100
                 ....*....|....*....|..
gi 315364424 190 FLVTQGASIYIENKEEKTPLQV 211
Cdd:PHA03095 102 LLIKAGADVNAKDKVGRTPLHV 123
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 87-179 3.30e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 46.90  E-value: 3.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424  87 EIVKALLVKGAHVNA---VNQNG-CTPLHYAASKNRHEIAVMLLEGGANPDAKDHYDA-TAMHRAAAKGNLKMVHILLFY 161
Cdd:PHA02884  47 DIIDAILKLGADPEApfpLSENSkTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKiTPLYISVLHGCLKCLEILLSY 126

                         90
                 ....*....|....*...
gi 315364424 162 KASTNIQDTEGNTPLHLA 179
Cdd:PHA02884 127 GADINIQTNDMVTPIELA 144
PHA02798 PHA02798
ankyrin-like protein; Provisional
 53-209 8.48e-06

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 45.98  E-value: 8.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424  53 TEIVEFLLQLGVPVNDKDDAGWSPLHIAASAG*D-----EIVKALLVKGAHVNAVNQNGCTPLHYAASK---NRHEIAVM 124
Cdd:PHA02798  51 TDIVKLFINLGANVNGLDNEYSTPLCTILSNIKDykhmlDIVKILIENGADINKKNSDGETPLYCLLSNgyiNNLEILLF 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424 125 LLEGGANPDAKDHYDATAMHRAAAKGN---LKMVHILLFYKASTN-IQDTEGNTPLHlaC------DEERVEEAKFLVTQ 194
Cdd:PHA02798 131 MIENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDINtHNNKEKYDTLH--CyfkyniDRIDADILKLFVDN 208

                        170
                 ....*....|....*
gi 315364424 195 GASIYIENKEEKTPL 209
Cdd:PHA02798 209 GFIINKENKSHKKKF 223
Ank_5 pfam13857
Ankyrin repeats (many copies);
99-146 9.05e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 9.05e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 315364424   99 VNAVNQNGCTPLHYAASKNRHEIAVMLLEGGANPDAKDHYDATAMHRA 146
Cdd:pfam13857   9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
10-60 1.37e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.49  E-value: 1.37e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 315364424   10 ICNLAYSGKLDELKeRILADKSLATRTDQDSRTALHWACSAGHTEIVEFLL 60
Cdd:pfam13637   5 LHAAAASGHLELLR-LLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 42-154 1.85e-05

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 45.00  E-value: 1.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424  42 TALHWACSAGHTEIVEFLLQLGVPVNdKDDA---------------GWSPLHIAASAG*DEIVKALLVKGAHVNAVNQNG 106
Cdd:cd22192   91 TALHIAVVNQNLNLVRELIARGADVV-SPRAtgtffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLG 169

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 315364424 107 CTPLHYAASKNRHEIA------VMLLEGGANPDAKDH---YDA-TAMHRAAAKGNLKM 154
Cdd:cd22192  170 NTVLHILVLQPNKTFAcqmydlILSYDKEDDLQPLDLvpnNQGlTPFKLAAKEGNIVM 227
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 41-71 2.29e-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: 40.35  E-value: 2.29e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 315364424   41 RTALHWAC-SAGHTEIVEFLLQLGVPVNDKDD 71
Cdd:pfam00023   3 NTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 105-134 2.35e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 40.26  E-value: 2.35e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 315364424   105 NGCTPLHYAASKNRHEIAVMLLEGGANPDA 134
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 41-67 2.66e-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.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 39.93  E-value: 2.66e-05
                          10        20
                  ....*....|....*....|....*..
gi 315364424   41 RTALHWACSAGHTEIVEFLLQLGVPVN 67
Cdd:pfam13606   3 NTPLHLAARNGRLEIVKLLLENGADIN 29
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 73-103 4.51e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.58  E-value: 4.51e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 315364424   73 GWSPLHIAA-SAG*DEIVKALLVKGAHVNAVN 103
Cdd:pfam00023   2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
Ank_5 pfam13857
Ankyrin repeats (many copies);
163-212 7.26e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.64  E-value: 7.26e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 315364424  163 ASTNIQDTEGNTPLHLACDEERVEEAKFLVTQGASIYIENKEEKTPLQVA 212
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 65-186 7.28e-05

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: 43.33  E-value: 7.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424  65 PVNDKDDAGWSPLHIAASAG*DEIVKALLVKGAHVNA------VNQNGCT-------PLHYAASKNRHEIAVMLLEGGAN 131
Cdd:cd21882   65 PCTDEFYQGQTALHIAIENRNLNLVRLLVENGADVSAratgrfFRKSPGNlfyfgelPLSLAACTNQEEIVRLLLENGAQ 144

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 315364424 132 P---DAKDHYDATAMHRAAAKGN---------LKMVHILLFYKASTN-------IQDTEGNTPLHLACDEERVE 186
Cdd:cd21882  145 PaalEAQDSLGNTVLHALVLQADntpensafvCQMYNLLLSYGAHLDptqqleeIPNHQGLTPLKLAAVEGKIV 218
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 39-68 7.68e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 38.72  E-value: 7.68e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 315364424    39 DSRTALHWACSAGHTEIVEFLLQLGVPVND 68
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 105-134 1.21e-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: 38.01  E-value: 1.21e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 315364424  105 NGCTPLHYAASKNRHEIAVMLLEGGANPDA 134
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 77-158 2.08e-04

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 40.24  E-value: 2.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424  77 LHIAASAG*---DEIVKALLVKGAHVNAVNQ-NGCTPLHYAASKNRHEIAVMLL-EGGANPDAKDHYDATAMHRAAAKGN 151
Cdd:PHA02736  59 VHIVSNPDKadpQEKLKLLMEWGADINGKERvFGNTPLHIAVYTQNYELATWLCnQPGVNMEILNYAFKTPYYVACERHD 138


                 ....*..
gi 315364424 152 LKMVHIL 158
Cdd:PHA02736 139 AKMMNIL 145
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 73-229 2.87e-04

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: 41.32  E-value: 2.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424  73 GWSPLHIAASAG*DEIVKALLVKGAHVNA---------VNQNGC-----TPLHYAASKNRHEIAVMLLEGGANPdakdhy 138
Cdd:cd22193   76 GQTALHIAIERRQGDIVALLVENGADVHAhakgrffqpKYQGEGfyfgeLPLSLAACTNQPDIVQYLLENEHQP------ 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424 139 datamhraaakgnlkmvhillfykASTNIQDTEGNTPLH--LACDEERVEEAKF-------LVTQGASIY-------IEN 202
Cdd:cd22193  150 ------------------------ADIEAQDSRGNTVLHalVTVADNTKENTKFvtrmydmILIRGAKLCptveleeIRN 205

                        170       180       190
                 ....*....|....*....|....*....|..
gi 315364424 203 KEEKTPLQVA--KGGLGL---ILKRLAEGEEA 229
Cdd:cd22193  206 NDGLTPLQLAakMGKIEIlkyILQREIKEPEL 237
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 42-194 3.61e-04

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: 41.22  E-value: 3.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424   42 TALHwACSAGHTEIVEFLLQLGVPVNDKDDAGW--------------SPLHIAASAG*DEIVKALLVKGAHVNA-VNQNG 106
Cdd:TIGR00870  84 TLLH-AISLEYVDAVEAILLHLLAAFRKSGPLElandqytseftpgiTALHLAAHRQNYEIVKLLLERGASVPArACGDF 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424  107 C--TPLHYAASKNRHEIAVmllegganpdakdhydatamhrAAAKGNLKMVHILLFYKASTNIQDTEGNTPLHLACDE-E 183
Cdd:TIGR00870 163 FvkSQGVDSFYHGESPLNA----------------------AACLGSPSIVALLSEDPADILTADSLGNTLLHLLVMEnE 220

                         170
                  ....*....|.
gi 315364424  184 RVEEAKFLVTQ 194
Cdd:TIGR00870 221 FKAEYEELSCQ 231
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 73-101 5.10e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 36.47  E-value: 5.10e-04
                          10        20
                  ....*....|....*....|....*....
gi 315364424   73 GWSPLHIAASAG*DEIVKALLVKGAHVNA 101
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02791 PHA02791
ankyrin-like protein; Provisional
 105-194 1.10e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 39.25  E-value: 1.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424 105 NGCTPLHYAASKNRHEIAVMLLEGGANPDAKDhyDATAMHRAAAKGNLKMVHILLFYKASTNIQDTEGNTPLHLACDEER 184
Cdd:PHA02791  29 HGHSALYYAIADNNVRLVCTLLNAGALKNLLE--NEFPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDSGN 106

                         90
                 ....*....|
gi 315364424 185 VEEAKFLVTQ 194
Cdd:PHA02791 107 MQTVKLFVKK 116
PHA02791 PHA02791
ankyrin-like protein; Provisional
 9-204 1.31e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 38.87  E-value: 1.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424   9 MICNLAYSGKLDELKEriladkslatrtdqdSRTALHWACSAGHTEIVEFLLQLGVPVNDKDDAGWSPLHIAASAG*DEI 88
Cdd:PHA02791  45 LVCTLLNAGALKNLLE---------------NEFPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDSGNMQT 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424  89 VKALLVKGAHVNAVNQNGC-TPLHYAASKNRHEIAVMLLEgganpDAKDHYD----ATAMHRAAAKGNLKMVHILLFYKA 163
Cdd:PHA02791 110 VKLFVKKNWRLMFYGKTGWkTSFYHAVMLNDVSIVSYFLS-----EIPSTFDlailLSCIHITIKNGHVDMMILLLDYMT 184

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 315364424 164 STNIQDTEGNTP-LHLACDEERVEEAKFLVTQGASIYIENKE 204
Cdd:PHA02791 185 STNTNNSLLFIPdIKLAIDNKDLEMLQALFKYDINIYSVNLE 226
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 54-225 1.40e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 39.34  E-value: 1.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424  54 EIVEFLLQLGVPVND-KDDAGWSPLHI---AASAG*DeIVKALLVKGahVNAVNQN---GCTPLHYAAsknRHEIAVM-- 124
Cdd:PHA02989 125 DMLRFLLSKGINVNDvKNSRGYNLLHMyleSFSVKKD-VIKILLSFG--VNLFEKTslyGLTPMNIYL---RNDIDVIsi 198

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424 125 -----LLEGGANPDAKDHYDATAM------HRAAAKGNLKMVHILLFYkASTNIQDTEGNTPLHLACDEERVEEAKFLVT 193
Cdd:PHA02989 199 kvikyLIKKGVNIETNNNGSESVLesfldnNKILSKKEFKVLNFILKY-IKINKKDKKGFNPLLISAKVDNYEAFNYLLK 277

                        170       180       190
                 ....*....|....*....|....*....|...
gi 315364424 194 QGASIYIENKEEKTPLQVA-KGGLGLILKRLAE 225
Cdd:PHA02989 278 LGDDIYNVSKDGDTVLTYAiKHGNIDMLNRILQ 310
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 73-101 1.99e-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: 1.99e-03
                           10        20
                   ....*....|....*....|....*....
gi 315364424    73 GWSPLHIAASAG*DEIVKALLVKGAHVNA 101
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 42-116 2.17e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 38.71  E-value: 2.17e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 315364424  42 TALHWACSA-GHTEIVEFLLQLGVPVNDKDDA-GWSPLHIAASAg*DEIVKALLVKGAHVNAVNQNGCTPLHYAASK 116
Cdd:PHA02878 236 TPLHISVGYcKDYDILKLLLEHGVDVNAKSYIlGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSAVKQ 310
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 171-200 3.86e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 34.16  E-value: 3.86e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 315364424  171 EGNTPLHLACDEERVEEAKFLVTQGASIYI 200
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 171-203 4.20e-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: 33.80  E-value: 4.20e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 315364424  171 EGNTPLHLACDEERVEE-AKFLVTQGASIYIENK 203
Cdd:pfam00023   1 DGNTPLHLAAGRRGNLEiVKLLLSKGADVNARDK 34
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 157-212 5.10e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 36.39  E-value: 5.10e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 315364424 157 ILLFYKASTNIQDT-EGNTPLHLACDEERVEEAKFLVTQ-GASIYIENKEEKTPLQVA 212
Cdd:PHA02736  76 LLMEWGADINGKERvFGNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYVA 133
PHA02741 PHA02741
hypothetical protein; Provisional
 66-165 7.85e-03

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 36.17  E-value: 7.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315364424  66 VNDKDDAGWSPLHIAASAG*D----EIVKALLVKGAHVNAVNQ-NGCTPLHYAASKNRHEIAVMLL-EGGANPDAKDHYD 139
Cdd:PHA02741  53 LNATDDAGQMCIHIAAEKHEAqlaaEIIDHLIELGADINAQEMlEGDTALHLAAHRRDHDLAEWLCcQPGIDLHFCNADN 132

                         90       100
                 ....*....|....*....|....*.
gi 315364424 140 ATAMHRAAAKGNLKMVHILLFYKAST 165
Cdd:PHA02741 133 KSPFELAIDNEDVAMMQILREIVATS 158
 
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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