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Conserved domains on  [gi|4506217|ref|NP_002805|]
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26S proteasome non-ATPase regulatory subunit 10 isoform 1 [Homo sapiens]

Protein Classification

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

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

Gene Ontology:  GO:0005515
PubMed:  33435370|17176038

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
12-222 1.67e-48

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 160.89  E-value: 1.67e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217   12 NLAYSGKLEELKESILADKSLATRTDQDSRTALHWACSAGHTEIVEFLLQLGVPVNDKDDAGWSPLHIAASAGRDEIVKA 91
Cdd:COG0666  59 LAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKL 138

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217   92 LLGKGAQVNAVNQNGCTPLHYAASKNRHEIAVMLLEGGANPDAKDHYEATAMHRAAAKGNLKMIHILLYYKASTNIQDTE 171
Cdd:COG0666 139 LLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDND 218

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 4506217  172 GNTPLHLACDEERVEEAKLLVSQGASIYIENKEEKTPLQVAKGGLGLILKR 222
Cdd:COG0666 219 GKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVK 269
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
12-222 1.67e-48

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 160.89  E-value: 1.67e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217   12 NLAYSGKLEELKESILADKSLATRTDQDSRTALHWACSAGHTEIVEFLLQLGVPVNDKDDAGWSPLHIAASAGRDEIVKA 91
Cdd:COG0666  59 LAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKL 138

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217   92 LLGKGAQVNAVNQNGCTPLHYAASKNRHEIAVMLLEGGANPDAKDHYEATAMHRAAAKGNLKMIHILLYYKASTNIQDTE 171
Cdd:COG0666 139 LLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDND 218

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 4506217  172 GNTPLHLACDEERVEEAKLLVSQGASIYIENKEEKTPLQVAKGGLGLILKR 222
Cdd:COG0666 219 GKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVK 269
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 20-212 9.46e-26

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 104.76  E-value: 9.46e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217    20 EELKESILA-DKSLATRTDQDSR-TALHWACSAGH-TEIVEFLLQLGVPVNDKDDAGWSPLHIAASAGRD-EIVKALLGK 95
Cdd:PHA02876 251 EDLETSLLLyDAGFSVNSIDDCKnTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYDtENIRTLIML 330

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217    96 GAQVNAVNQNGCTPLHYAASKNRH-EIAVMLLEGGANPDAKDHYEATAMHRAAAKGNLKMIHILLYYKASTNIQDTEGNT 174
Cdd:PHA02876 331 GADVNAADRLYITPLHQASTLDRNkDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGT 410

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 4506217   175 PLHLA-CDEERVEEAKLLVSQGASIYIENKEEKTPLQVA 212
Cdd:PHA02876 411 ALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYA 449
Ank_2 pfam12796
Ankyrin repeats (3 copies);
44-136 7.52e-25

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 93.64  E-value: 7.52e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217     44 LHWACSAGHTEIVEFLLQLGVPVNDKDDAGWSPLHIAASAGRDEIVKALLgKGAQVNAVNqNGCTPLHYAASKNRHEIAV 123
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 4506217    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 2.05e-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: 62.72  E-value: 2.05e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217   42 TALHWACSAGHTEIVEFLLQ-----LGVPVNDKDDAGWSPLHIAASAGRDEIVKALLGKGAQVNAVNQNGCT-------- 108
Cdd:cd22192  53 TALHVAALYDNLEAAVVLMEaapelVNEPMTSDLYQGETALHIAVVNQNLNLVRELIARGADVVSPRATGTFfrpgpknl 132

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217  109 ------PLHYAASKNRHEIAVMLLEGGANPDAKDHYEATAMHRAAAKGNLK----MIHILLYYKASTN------IQDTEG 172
Cdd:cd22192 133 iyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTfacqMYDLILSYDKEDDlqpldlVPNNQG 212

                       170
                ....*....|
gi 4506217  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 1.82e-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: 1.82e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 4506217     105 NGCTPLHYAASKNRHEIAVMLLEGGANPDA 134
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 42-194 2.20e-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: 41.61  E-value: 2.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217     42 TALHwACSAGHTEIVEFLLQLGVPVNDKDDAGW--------------SPLHIAASAGRDEIVKALLGKGAQVNA-VNQNG 106
Cdd:TIGR00870  84 TLLH-AISLEYVDAVEAILLHLLAAFRKSGPLElandqytseftpgiTALHLAAHRQNYEIVKLLLERGASVPArACGDF 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217    107 C--TPLHYAASKNRHEIAVmllegganpdakdhyeatamhrAAAKGNLKMIHILLYYKASTNIQDTEGNTPLHLACDE-E 183
Cdd:TIGR00870 163 FvkSQGVDSFYHGESPLNA----------------------AACLGSPSIVALLSEDPADILTADSLGNTLLHLLVMEnE 220

                         170
                  ....*....|.
gi 4506217    184 RVEEAKLLVSQ 194
Cdd:TIGR00870 221 FKAEYEELSCQ 231
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
12-222 1.67e-48

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 160.89  E-value: 1.67e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217   12 NLAYSGKLEELKESILADKSLATRTDQDSRTALHWACSAGHTEIVEFLLQLGVPVNDKDDAGWSPLHIAASAGRDEIVKA 91
Cdd:COG0666  59 LAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKL 138

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217   92 LLGKGAQVNAVNQNGCTPLHYAASKNRHEIAVMLLEGGANPDAKDHYEATAMHRAAAKGNLKMIHILLYYKASTNIQDTE 171
Cdd:COG0666 139 LLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDND 218

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 4506217  172 GNTPLHLACDEERVEEAKLLVSQGASIYIENKEEKTPLQVAKGGLGLILKR 222
Cdd:COG0666 219 GKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVK 269
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
13-213 3.32e-44

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 149.72  E-value: 3.32e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217   13 LAYSGKLEELKESILADKSLATRTDQDSRTALHWACSAGHTEIVEFLLQLGVPVNDKDDAGWSPLHIAASAGRDEIVKAL 92
Cdd:COG0666  27 AAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLL 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217   93 LGKGAQVNAVNQNGCTPLHYAASKNRHEIAVMLLEGGANPDAKDHYEATAMHRAAAKGNLKMIHILLYYKASTNIQDTEG 172
Cdd:COG0666 107 LEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDG 186

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 4506217  173 NTPLHLACDEERVEEAKLLVSQGASIYIENKEEKTPLQVAK 213
Cdd:COG0666 187 ETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAA 227
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
13-209 6.08e-42

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 143.94  E-value: 6.08e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217   13 LAYSGKLEELKESILADKSLATRTDQDSRTALHWACSAGHTEIVEFLLQLGVPVNDKDDAGWSPLHIAASAGRDEIVKAL 92
Cdd:COG0666  93 AAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLL 172

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217   93 LGKGAQVNAVNQNGCTPLHYAASKNRHEIAVMLLEGGANPDAKDHYEATAMHRAAAKGNLKMIHILLYYKASTNIQDTEG 172
Cdd:COG0666 173 LEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDG 252

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 4506217  173 NTPLHLACDEERVEEAKLLVSQGASIYIENKEEKTPL 209
Cdd:COG0666 253 LTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
20-212 2.03e-31

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 116.59  E-value: 2.03e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217   20 EELKESILADKSLATRTDQDSRTALHWACSAGHTEIVEFLLQLGVPVNDKDDAGWSPLHIAASAGRDEIVKALLGKGAQV 99
Cdd:COG0666   1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217  100 NAVNQNGCTPLHYAASKNRHEIAVMLLEGGANPDAKDHYEATAMHRAAAKGNLKMIHILLYYKASTNIQDTEGNTPLHLA 179
Cdd:COG0666  81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                       170       180       190
                ....*....|....*....|....*....|...
gi 4506217  180 CDEERVEEAKLLVSQGASIYIENKEEKTPLQVA 212
Cdd:COG0666 161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLA 193
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 20-212 9.46e-26

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 104.76  E-value: 9.46e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217    20 EELKESILA-DKSLATRTDQDSR-TALHWACSAGH-TEIVEFLLQLGVPVNDKDDAGWSPLHIAASAGRD-EIVKALLGK 95
Cdd:PHA02876 251 EDLETSLLLyDAGFSVNSIDDCKnTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYDtENIRTLIML 330

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217    96 GAQVNAVNQNGCTPLHYAASKNRH-EIAVMLLEGGANPDAKDHYEATAMHRAAAKGNLKMIHILLYYKASTNIQDTEGNT 174
Cdd:PHA02876 331 GADVNAADRLYITPLHQASTLDRNkDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGT 410

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 4506217   175 PLHLA-CDEERVEEAKLLVSQGASIYIENKEEKTPLQVA 212
Cdd:PHA02876 411 ALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYA 449
Ank_2 pfam12796
Ankyrin repeats (3 copies);
44-136 7.52e-25

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 93.64  E-value: 7.52e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217     44 LHWACSAGHTEIVEFLLQLGVPVNDKDDAGWSPLHIAASAGRDEIVKALLgKGAQVNAVNqNGCTPLHYAASKNRHEIAV 123
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 4506217    124 MLLEGGANPDAKD 136
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 37-212 7.70e-25

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 100.89  E-value: 7.70e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217    37 DQDSRTALHWACSAGHTEIVEFLLQLGVPVNDKDDAGWSPLHIA----ASAGRD-EIVKALLGKGAQVNAVNQNGCTPLH 111
Cdd:PHA03100  32 YKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLsnikYNLTDVkEIVKLLLEYGANVNAPDNNGITPLL 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217   112 YAASK--NRHEIAVMLLEGGANPDAKDHYEATAMHrAAAKGN---LKMIHILLYYKA----------------STNIQDT 170
Cdd:PHA03100 112 YAISKksNSYSIVEYLLDNGANVNIKNSDGENLLH-LYLESNkidLKILKLLIDKGVdinaknrvnyllsygvPINIKDV 190

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 4506217   171 EGNTPLHLACDEERVEEAKLLVSQGASIYIENKEEKTPLQVA 212
Cdd:PHA03100 191 YGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIA 232
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 37-212 1.40e-24

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 100.42  E-value: 1.40e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217    37 DQDSRTALHWACSAGHTEIVEFLLQLGVPVNDKDDAGWSPLHIAASAGRDEIVKALLGKGAQVNAVNQNGCTPLHYAASK 116
Cdd:PHA02874 121 DAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEY 200

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217   117 NRHEIAVMLLEGGANPDAKDHYEATAMHRAAAKgNLKMIHiLLYYKASTNIQDTEGNTPLHLA----CDEERVEeakLLV 192
Cdd:PHA02874 201 GDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIH-NRSAIE-LLINNASINDQDIDGSTPLHHAinppCDIDIID---ILL 275

                        170       180
                 ....*....|....*....|
gi 4506217   193 SQGASIYIENKEEKTPLQVA 212
Cdd:PHA02874 276 YHKADISIKDNKGENPIDTA 295
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 53-212 9.56e-24

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 98.41  E-value: 9.56e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217    53 TEIVEFLLQLGVPVNDKD-DAGWSPLHIAASAGRDEIVKALLGKGAQVNAVNQNGCTPLHYAASKNRHEIAVMLLEGGAN 131
Cdd:PHA02878 147 AEITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAS 226

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217   132 PDAKDHYEATAMHRAAAK-GNLKMIHILLYYKASTNIQDT-EGNTPLHLACDEERVeeAKLLVSQGASIYIENKEEKTPL 209
Cdd:PHA02878 227 TDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIKSERK--LKLLLEYGADINSLNSYKLTPL 304


                 ...
gi 4506217   210 QVA 212
Cdd:PHA02878 305 SSA 307
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 36-200 8.90e-23

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 95.12  E-value: 8.90e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217    36 TDQDSRTALHWACSAGHT-----EIVEFLLQLGVPVNDKDDAGWSPLHIAASA--GRDEIVKALLGKGAQVNAVNQNGCT 108
Cdd:PHA03100  64 STKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGEN 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217   109 PLHYAASKNRHEIAV------------------MLLEGGANPDAKDHYEATAMHRAAAKGNLKMIHILLYYKASTNIQDT 170
Cdd:PHA03100 144 LLHLYLESNKIDLKIlkllidkgvdinaknrvnYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNK 223

                        170       180       190
                 ....*....|....*....|....*....|
gi 4506217   171 EGNTPLHLACDEERVEEAKLLVSQGASIYI 200
Cdd:PHA03100 224 YGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
PHA03095 PHA03095
ankyrin-like protein; Provisional
 42-212 3.33e-19

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 85.46  E-value: 3.33e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217    42 TALH-WACSAGHTEIVEFLLQLGVPVNDKDDAGWSPLHIAAS--AGRDEIVKALLGKGAQVNAVNQNGCTPLHYAASKNR 118
Cdd:PHA03095  85 TPLHlYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVYLSgfNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRN 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217   119 HEIAV--MLLEGGANPDAKDHYEATAMHRAA--AKGNLKMIHILLYYKASTNIQDTEGNTPLHLACDEERVEEAKL--LV 192
Cdd:PHA03095 165 ANVELlrLLIDAGADVYAVDDRFRSLLHHHLqsFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLL 244

                        170       180
                 ....*....|....*....|
gi 4506217   193 SQGASIYIENKEEKTPLQVA 212
Cdd:PHA03095 245 IAGISINARNRYGQTPLHYA 264
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 44-202 5.83e-19

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 84.55  E-value: 5.83e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217    44 LHWACSAGHTEIVEFLLQLGVPVNDKDDAGWSPLHIAASA------------------------------GRD------- 86
Cdd:PHA02878  41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEpnklgmkemirsinkcsvfytlvaikdafnNRNveifkii 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217    87 ---------------------------EIVKALLGKGAQVNAVNQN-GCTPLHYAASKNRHEIAVMLLEGGANPDAKDHY 138
Cdd:PHA02878 121 ltnrykniqtidlvyidkkskddiieaEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKT 200

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4506217   139 EATAMHRAAAKGNLKMIHILLYYKASTNIQDTEGNTPLHLACDE-ERVEEAKLLVSQGASIYIEN 202
Cdd:PHA02878 201 NNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKS 265
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 28-179 7.42e-19

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 84.55  E-value: 7.42e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217    28 ADKSLATRtDQDSrTALHWACSAGHTEIVEFLLQLGVPVNDKDDAGWSPLHIAASAGRDEIVKALLGKGAQVNAVNQNGC 107
Cdd:PHA02878 158 ADINMKDR-HKGN-TALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGN 235

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4506217   108 TPLHYAASK-NRHEIAVMLLEGGANPDAKDHYEA-TAMHRAAAkgNLKMIHILLYYKASTNIQDTEGNTPLHLA 179
Cdd:PHA02878 236 TPLHISVGYcKDYDILKLLLEHGVDVNAKSYILGlTALHSSIK--SERKLKLLLEYGADINSLNSYKLTPLSSA 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 4506217    41 RTALHwACSAG---HTEIVEFLLQLGVPVNDKDDAGWSPLHIAASAGR--DEIVKALLGKGAQVNAVNQNGCTPLHYAA- 114
Cdd:PHA03095 118 RTPLH-VYLSGfniNPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanVELLRLLIDAGADVYAVDDRFRSLLHHHLq 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217   115 -SKNRHEIAVMLLEGGANPDAKDHYEATAMHRAAAKGNLKMIHI--LLYYKASTNIQDTEGNTPLHLA--------CDEe 183
Cdd:PHA03095 197 sFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAavfnnpraCRR- 275

                        170       180
                 ....*....|....*....|....*.
gi 4506217   184 rveeaklLVSQGASIYIENKEEKTPL 209
Cdd:PHA03095 276 -------LIALGADINAVSSDGNTPL 294
Ank_2 pfam12796
Ankyrin repeats (3 copies);
8-103 1.02e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.15  E-value: 1.02e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217      8 LMVCnlAYSGKLEELKEsILADKSLATRTDQDSRTALHWACSAGHTEIVEFLLQLGVPvnDKDDAGWSPLHIAASAGRDE 87
Cdd:pfam12796   1 LHLA--AKNGNLELVKL-LLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLE 75

                          90
                  ....*....|....*.
gi 4506217     88 IVKALLGKGAQVNAVN 103
Cdd:pfam12796  76 IVKLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 56-138 3.22e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 79.32  E-value: 3.22e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217    56 VEFLLQLGVPVNDKDDAGWSPLHIAASAGRDEIVKALLGKGAQVNAVNQNGCTPLHYAASKNRHEIAVMLLEGGANPDAK 135
Cdd:PHA03100 175 VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTI 254


                 ...
gi 4506217   136 DHY 138
Cdd:PHA03100 255 IET 257
Ank_2 pfam12796
Ankyrin repeats (3 copies);
110-202 7.76e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.84  E-value: 7.76e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217    110 LHYAASKNRHEIAVMLLEGGANPDAKDHYEATAMHRAAAKGNLKMIHILLYYKASTNiqDTEGNTPLHLACDEERVEEAK 189
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 4506217    190 LLVSQGASIYIEN 202
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 53-198 8.32e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 78.11  E-value: 8.32e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217    53 TEIVEFLLQLGVPVNDKDDAGWSPLHIAASAGRDEIVKALLGKGAQVNAV-NQNGCTPLHYAASKNRHEIAVMLLEGGAN 131
Cdd:PHA02875  48 SEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVfYKDGMTPLHLATILKKLDIMKLLIARGAD 127

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4506217   132 PDAKDHYEATAMHRAAAKGNLKMIHILLYYKASTNIQDTEGNTPLHLACDEERVEEAKLLVSQGASI 198
Cdd:PHA02875 128 PDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANI 194
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 15-212 1.19e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 75.00  E-value: 1.19e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217    15 YSGKLEELKESILADKSLATRTDQDSRTALHWACSAGHTEIVEFLLQLGVPVNDKDDAGWSPLHIAASAGRDEIVKAL-- 92
Cdd:PHA02874  10 YSGDIEAIEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLid 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217    93 ---------------------LGKGAQVNAVNQNGCTPLHYAASKNRHEIAVMLLEGGANPDAKDHYEATAMHRAAAKGN 151
Cdd:PHA02874  90 ngvdtsilpipciekdmiktiLDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNF 169

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4506217   152 LKMIHILLYYKASTNIQDTEGNTPLHLACDEERVEEAKLLVSQGASIYIENKEEKTPLQVA 212
Cdd:PHA02874 170 FDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNA 230
PHA03095 PHA03095
ankyrin-like protein; Provisional
 79-211 1.25e-15

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 75.06  E-value: 1.25e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217    79 IAASAGRDEIVKALLGKGAQVNAVNQNGCTPLHY---AASKNRHEIAVMLLEGGANPDAKDHYEATAMHRAAAKGN-LKM 154
Cdd:PHA03095  20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHLylhYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDV 99

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 4506217   155 IHILLYYKASTNIQDTEGNTPLHLACDEERVEE--AKLLVSQGASIYIENKEEKTPLQV 211
Cdd:PHA03095 100 IKLLIKAGADVNAKDKVGRTPLHVYLSGFNINPkvIRLLLRKGADVNALDLYGMTPLAV 158
PHA03095 PHA03095
ankyrin-like protein; Provisional
 54-199 1.65e-15

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 74.68  E-value: 1.65e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217    54 EIVEFLLQLGVPVNDKDDAGWSPLHI---AASAGRDEIVKALLGKGAQVNAVNQNGCTPLH-YAASKNRHEIAVMLLEGG 129
Cdd:PHA03095  28 EEVRRLLAAGADVNFRGEYGKTPLHLylhYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAG 107

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4506217   130 ANPDAKDHYEATAMHrAAAKG---NLKMIHILLYYKASTNIQDTEGNTPLHL-----ACDeerVEEAKLLVSQGASIY 199
Cdd:PHA03095 108 ADVNAKDKVGRTPLH-VYLSGfniNPKVIRLLLRKGADVNALDLYGMTPLAVllksrNAN---VELLRLLIDAGADVY 181
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 47-205 9.02e-14

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 69.90  E-value: 9.02e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217    47 ACSAGHTEIVEFLLQLGVPVNDKDDAGWSPLHIAASAGRDEIVKALLGKGAQVNAVNQNGCTPLHYAASKNRHEIAVMLL 126
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILY 611

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4506217   127 EGGANPDAkdHYEATAMHRAAAKGNLKMIHILLYYKASTNIQDTEGNTPLHLACDEERVEEAKLLVSQGASIYIENKEE 205
Cdd:PLN03192 612 HFASISDP--HAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDD 688
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 20-212 1.21e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 69.32  E-value: 1.21e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217    20 EELKESILADKSLATRTDQDsrtalhwacsagHTEIVEFLLQLGVPVNDKDDAGWSPLHIAASAGRDEIVKALLGKGAQV 99
Cdd:PHA02876 137 DKINESIEYMKLIKERIQQD------------ELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADV 204

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217   100 NAVNQNGCTPLHYAASKNR-----------------------------HEIAVMLLEGGANPDAKDHYEATAMHRAAAKG 150
Cdd:PHA02876 205 NIIALDDLSVLECAVDSKNidtikaiidnrsninkndlsllkairnedLETSLLLYDAGFSVNSIDDCKNTPLHHASQAP 284

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4506217   151 NL-KMIHILLYYKASTNIQDTEGNTPLHL-ACDEERVEEAKLLVSQGASIYIENKEEKTPLQVA 212
Cdd:PHA02876 285 SLsRLVPKLLERGADVNAKNIKGETPLYLmAKNGYDTENIRTLIMLGADVNAADRLYITPLHQA 348
Ank_4 pfam13637
Ankyrin repeats (many copies);
41-93 1.64e-13

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 62.68  E-value: 1.64e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 4506217     41 RTALHWACSAGHTEIVEFLLQLGVPVNDKDDAGWSPLHIAASAGRDEIVKALL 93
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 41-212 6.61e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 66.94  E-value: 6.61e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217    41 RTALHWACSAGHTEIVEFLLQLGVPVNDKDDAGWSPLHIAASAGRDEIVKALLGKGAQVNAVNQNGCTPLHYAASKNRHE 120
Cdd:PHA02875   3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217   121 IAVMLLEGGANPDAKDHYEA-TAMHRAAAKGNLKMIHILLYYKASTNIQDTEGNTPLHLACDEERVEEAKLLVSQGASIY 199
Cdd:PHA02875  83 AVEELLDLGKFADDVFYKDGmTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLD 162

                        170
                 ....*....|...
gi 4506217   200 IENKEEKTPLQVA 212
Cdd:PHA02875 163 IEDCCGCTPLIIA 175
Ank_4 pfam13637
Ankyrin repeats (many copies);
73-126 6.64e-13

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 61.14  E-value: 6.64e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 4506217     73 GWSPLHIAASAGRDEIVKALLGKGAQVNAVNQNGCTPLHYAASKNRHEIAVMLL 126
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 17-181 2.10e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 65.40  E-value: 2.10e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217    17 GKLEELKESILADKSLATRTDQDSRTALHWACSAGHTEIVEFLLQLG----VPVNDKddagWSPLHIAASAGRDEIVKAL 92
Cdd:PHA02875  79 GDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGadpdIPNTDK----FSPLHLAVMMGDIKGIELL 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217    93 LGKGAQVNAVNQNGCTPLHYAASKNRHEIAVMLLEGGANPD-AKDHYEATAMHRAAAKGNLKMIHILLYYKASTNIQDT- 170
Cdd:PHA02875 155 IDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDyFGKNGCVAALCYAIENNKIDIVRLFIKRGADCNIMFMi 234

                        170
                 ....*....|...
gi 4506217   171 --EGNTPLHLACD 181
Cdd:PHA02875 235 egEECTILDMICN 247
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 6-164 3.59e-12

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 65.27  E-value: 3.59e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217     6 SNLM-VCNLAYSGKLEELkesiLADKSLATRTDQDSRTALHWACSAGHTEIVEFLLQLGVPVNDKDDAGWSPLHIAASAG 84
Cdd:PLN03192 527 SNLLtVASTGNAALLEEL----LKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAK 602

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217    85 RDEIVKALLGKGAQVNAvnQNGCTPLHYAASKNRHEIAVMLLEGGANPDAKDHYEATAMHRAAAKGNLKMIHILLYYKAS 164
Cdd:PLN03192 603 HHKIFRILYHFASISDP--HAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGAD 680
PHA03095 PHA03095
ankyrin-like protein; Provisional
 26-155 9.12e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 63.51  E-value: 9.12e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217    26 ILADKSLATRtDQDSRTALHWACSAGHT--EIVEFLLQLGVPVNDKDDAGWSPLHIAA--SAGRDEIVKALLGKGAQVNA 101
Cdd:PHA03095 174 IDAGADVYAV-DDRFRSLLHHHLQSFKPraRIVRELIRAGCDPAATDMLGNTPLHSMAtgSSCKRSLVLPLLIAGISINA 252

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 4506217   102 VNQNGCTPLHYAASKNRHEIAVMLLEGGANPDAKDHYEATAMHRAAAKGNLKMI 155
Cdd:PHA03095 253 RNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAV 306
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 42-182 2.05e-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: 62.72  E-value: 2.05e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217   42 TALHWACSAGHTEIVEFLLQ-----LGVPVNDKDDAGWSPLHIAASAGRDEIVKALLGKGAQVNAVNQNGCT-------- 108
Cdd:cd22192  53 TALHVAALYDNLEAAVVLMEaapelVNEPMTSDLYQGETALHIAVVNQNLNLVRELIARGADVVSPRATGTFfrpgpknl 132

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217  109 ------PLHYAASKNRHEIAVMLLEGGANPDAKDHYEATAMHRAAAKGNLK----MIHILLYYKASTN------IQDTEG 172
Cdd:cd22192 133 iyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTfacqMYDLILSYDKEDDlqpldlVPNNQG 212

                       170
                ....*....|
gi 4506217  173 NTPLHLACDE 182
Cdd:cd22192 213 LTPFKLAAKE 222
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 76-216 3.87e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 61.82  E-value: 3.87e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217    76 PLHIAASAGRDEIVKALLGKGAQVNAVNQNGCTPLHYA-------------ASKNR------------------------ 118
Cdd:PHA02878  40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIIckepnklgmkemiRSINKcsvfytlvaikdafnnrnveifki 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217   119 ---------------------------HEIAVMLLEGGANPDAKD-HYEATAMHRAAAKGNLKMIHILLYYKASTNIQDT 170
Cdd:PHA02878 120 iltnrykniqtidlvyidkkskddiieAEITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDK 199

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 4506217   171 EGNTPLHLACDEERVEEAKLLVSQGASIYIENKEEKTPLQVAKGGL 216
Cdd:PHA02878 200 TNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYC 245
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 13-131 6.74e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 61.16  E-value: 6.74e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217    13 LAYSGKLEELKESILADKSLATRTDQDSRTALHWACSAGHTEIVEFLLQLGVPVNDKDDAGWSPLHIAASAGRDEIVKAL 92
Cdd:PHA02875 108 LATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKML 187

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 4506217    93 LGKGAQVNAVNQNGC-TPLHYAASKNRHEIAVMLLEGGAN 131
Cdd:PHA02875 188 LDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGAD 227
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 111-193 1.73e-10

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 59.91  E-value: 1.73e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217   111 HYAASKNRHEIAVmLLEGGANPDAKDHYEATAMHRAAAKGNLKMIHILLYYKASTNIQDTEGNTPLHLACDEERVEEAKL 190
Cdd:PTZ00322  88 QLAASGDAVGARI-LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                 ...
gi 4506217   191 LVS 193
Cdd:PTZ00322 167 LSR 169
Ank_4 pfam13637
Ankyrin repeats (many copies);
108-159 1.88e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.59  E-value: 1.88e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 4506217    108 TPLHYAASKNRHEIAVMLLEGGANPDAKDHYEATAMHRAAAKGNLKMIHILL 159
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 85-212 3.31e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 58.91  E-value: 3.31e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217    85 RDEIVKALLGKGAQVNAVNQNGCTPLHYAASKNRHEIAVMLLEGGANPDAKDHYEATAMH-----RAAAKGNLKMIHILL 159
Cdd:PHA03100  14 KVKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHylsniKYNLTDVKEIVKLLL 93

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 4506217   160 YYKASTNIQDTEGNTPLHLACDEER--VEEAKLLVSQGASIYIENKEEKTPLQVA 212
Cdd:PHA03100  94 EYGANVNAPDNNGITPLLYAISKKSnsYSIVEYLLDNGANVNIKNSDGENLLHLY 148
Ank_2 pfam12796
Ankyrin repeats (3 copies);
143-212 1.59e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 53.20  E-value: 1.59e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4506217    143 MHRAAAKGNLKMIHILLYYKASTNIQDTEGNTPLHLACDEERVEEAKLLVSQGAsiyIENKEE-KTPLQVA 212
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD---VNLKDNgRTALHYA 68
Ank_5 pfam13857
Ankyrin repeats (many copies);
35-80 3.24e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 51.19  E-value: 3.24e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 4506217     35 RTDQDSRTALHWACSAGHTEIVEFLLQLGVPVNDKDDAGWSPLHIA 80
Cdd:pfam13857  11 RLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 68-212 4.40e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 56.03  E-value: 4.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217    68 DKDDAGWSPLHIAASAGRDEIVKALLGKGAQVNAVNQNGCTPLHYAASKNRHEIAVMLLEGGANPDAKDHYEATAMHRAA 147
Cdd:PLN03192 520 HDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAI 599

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4506217   148 AKGNLKMIHILLYYKASTNIQdTEGNTpLHLACDEERVEEAKLLVSQGASIYIENKEEKTPLQVA 212
Cdd:PLN03192 600 SAKHHKIFRILYHFASISDPH-AAGDL-LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVA 662
PHA02946 PHA02946
ankyin-like protein; Provisional
 84-203 5.02e-09

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 55.45  E-value: 5.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217    84 GRDE-IVKALLGKGAQVNAVNQNGCTPLHYAASKNRHEIAVMLLEGGANPDAKDHYEATAMHRAAAKGN--LKMIHILLY 160
Cdd:PHA02946  49 GLDErFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQ 128

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 4506217   161 YKASTNIQ-DTEGNTPLhLACDEERVEEAKLLVSQGASIYIENK 203
Cdd:PHA02946 129 YGAKINNSvDEEGCGPL-LACTDPSERVFKKIMSIGFEARIVDK 171
PHA02946 PHA02946
ankyin-like protein; Provisional
 20-211 6.17e-09

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 55.45  E-value: 6.17e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217    20 EELKESILADKSLATRTDQDSRTALHWACSAGHTEIVEFLLQLGVPVNDKDDAGWSPLHIaASAGRDEIVKA---LLGKG 96
Cdd:PHA02946  52 ERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYY-LSGTDDEVIERinlLVQYG 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217    97 AQV-NAVNQNGCTPLhYAASKNRHEIAVMLLEGGANPDAKDHYEATAMHRAAAKGNLK--MIHILLYYKASTNIQDTEGN 173
Cdd:PHA02946 131 AKInNSVDEEGCGPL-LACTDPSERVFKKIMSIGFEARIVDKFGKNHIHRHLMSDNPKasTISWMMKLGISPSKPDHDGN 209

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 4506217   174 TPLHLACDE--ERVEEAKLLVSQgASIYIENKEEKTPLQV 211
Cdd:PHA02946 210 TPLHIVCSKtvKNVDIINLLLPS-TDVNKQNKFGDSPLTL 248
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 54-225 1.00e-08

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: 54.76  E-value: 1.00e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217   54 EIVEFLLQ-------LGVPVN----DKDDAGWSPLHIAASAGRDEIVKALLGKGAQVNA---------VNQNGC-----T 108
Cdd:cd22194 111 EIVRILLAfaeengiLDRFINaeytEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAhakgvffnpKYKHEGfyfgeT 190

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217  109 PLHYAASKNRHEIAVMLLEgganpdakdhyeatamhraaakgnlkmihillyyKASTNI--QDTEGNTPLH----LACDE 182
Cdd:cd22194 191 PLALAACTNQPEIVQLLME----------------------------------KESTDItsQDSRGNTVLHalvtVAEDS 236

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 4506217  183 E-------RVEEAKLLVSQGASI-YIENKEEKTPLQV-AKGGLGLILKRMVE 225
Cdd:cd22194 237 KtqndfvkRMYDMILLKSENKNLeTIRNNEGLTPLQLaAKMGKAEILKYILS 288
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 147-212 1.23e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.52  E-value: 1.23e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4506217   147 AAKGNLKMIHILLYYKASTNIQDTEGNTPLHLACDEERVEEAKLLVSQGASIYIENKEEKTPLQVA 212
Cdd:PTZ00322  90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELA 155
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 21-134 3.00e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 53.36  E-value: 3.00e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217    21 ELKESILA--DKSLATRTDQDSRTA-------LHWACSaGHTEIVEFLLQLGVPVNDKDDAGWSPLHIAASAGRDEIVKA 91
Cdd:PTZ00322  55 EATENKDAtpDHNLTTEEVIDPVVAhmltvelCQLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRV 133

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 4506217    92 LLGKGAQVNAVNQNGCTPLHYAASKNRHEIAVMLL-------EGGAN--PDA 134
Cdd:PTZ00322 134 LLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSrhsqchfELGANakPDS 185
Ank_5 pfam13857
Ankyrin repeats (many copies);
59-113 3.93e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.50  E-value: 3.93e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 4506217     59 LLQLG-VPVNDKDDAGWSPLHIAASAGRDEIVKALLGKGAQVNAVNQNGCTPLHYA 113
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 37-163 5.21e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 52.76  E-value: 5.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217    37 DQDSRTALHWACSAGHTEIVEFLLQLGVPVNDKDDAGWSPLHIAASAGRDEI-VKALLGKGAQVNAVNQNGCTPLHYAAS 115
Cdd:PHA02876 372 DYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMsVKTLIDRGANVNSKNKDLSTPLHYACK 451

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 4506217   116 KN-RHEIAVMLLEGGANPDA---KDHYEATamhraAAKGNLKMIHILLYYKA 163
Cdd:PHA02876 452 KNcKLDVIEMLLDNGADVNAiniQNQYPLL-----IALEYHGIVNILLHYGA 498
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 42-105 7.49e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 51.97  E-value: 7.49e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4506217    42 TALHWACSAGHTEIVEFLLQLGVPVNDKDDAGWSPLHIAASAGRDEIVKALLGKGAQVNAVNQN 105
Cdd:PHA03100 194 TPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
Ank_4 pfam13637
Ankyrin repeats (many copies);
139-192 1.08e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.27  E-value: 1.08e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 4506217    139 EATAMHRAAAKGNLKMIHILLYYKASTNIQDTEGNTPLHLACDEERVEEAKLLV 192
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 21-179 1.28e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 51.50  E-value: 1.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217    21 ELKESILADKSLATRTDQDSRTALHWACSAGHTEIVEFLLQLGVPVNDKDDAGWSPLHIAASAGRDEIvkALLGKGAQVN 100
Cdd:PHA02874 171 DIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAI--ELLINNASIN 248

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4506217   101 AVNQNGCTPLHYAASKnrheiavmllegganPDAKDhyeatamhraaakgnlkMIHILLYYKASTNIQDTEGNTPLHLA 179
Cdd:PHA02874 249 DQDIDGSTPLHHAINP---------------PCDID-----------------IIDILLYHKADISIKDNKGENPIDTA 295
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 54-213 2.95e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 49.43  E-value: 2.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217    54 EIVEFLLQLGVPVNDK-DDAGWSPLHIAASAGRD---EIVKALLGKGAQVNAVNQNGCTPLH-YAASKN-RHEIAVMLLE 127
Cdd:PHA02859  67 EILKFLIENGADVNFKtRDNNLSALHHYLSFNKNvepEILKILIDSGSSITEEDEDGKNLLHmYMCNFNvRINVIKLLID 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217   128 GGANPDAKDhyeatamhraaaKGNLKMIHILLYYKASTNIQDtegntplhlacdeerveeakLLVSQGASIYIENKEEKT 207
Cdd:PHA02859 147 SGVSFLNKD------------FDNNNILYSYILFHSDKKIFD--------------------FLTSLGIDINETNKSGYN 194


                 ....*.
gi 4506217   208 PLQVAK 213
Cdd:PHA02859 195 CYDLIK 200
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 87-179 1.00e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 48.44  E-value: 1.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217    87 EIVKALLGKGAQVNA---VNQNG-CTPLHYAASKNRHEIAVMLLEGGANPDAKDHY-EATAMHRAAAKGNLKMIHILLYY 161
Cdd:PHA02884  47 DIIDAILKLGADPEApfpLSENSkTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEaKITPLYISVLHGCLKCLEILLSY 126

                         90
                 ....*....|....*...
gi 4506217   162 KASTNIQDTEGNTPLHLA 179
Cdd:PHA02884 127 GADINIQTNDMVTPIELA 144
PHA03095 PHA03095
ankyrin-like protein; Provisional
 14-164 1.01e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 48.48  E-value: 1.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217    14 AYSGKLEELkesiLADKSLATRTDQDSRTALHWA---CSAGHTEIVEFLLQlGVPVNDKDDAGWSPLHIAASAGRDEIVK 90
Cdd:PHA03095 200 PRARIVREL----IRAGCDPAATDMLGNTPLHSMatgSSCKRSLVLPLLIA-GISINARNRYGQTPLHYAAVFNNPRACR 274

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217    91 ALLGKGAQVNAVNQNGCTPLHYAASKNRHEIAVMLLEggANPDAK------DHYEATAMHRAAAKGNLKMIHILLYYKAS 164
Cdd:PHA03095 275 RLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALA--KNPSAEtvaatlNTASVAGGDIPSDATRLCVAKVVLRGAFS 352
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 105-137 1.42e-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: 1.42e-06
                          10        20        30
                  ....*....|....*....|....*....|....
gi 4506217    105 NGCTPLHYAASKNRH-EIAVMLLEGGANPDAKDH 137
Cdd:pfam00023   1 DGNTPLHLAAGRRGNlEIVKLLLSKGADVNARDK 34
PHA02798 PHA02798
ankyrin-like protein; Provisional
 53-209 4.29e-06

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 46.75  E-value: 4.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217    53 TEIVEFLLQLGVPVNDKDDAGWSPLHIAASAGRD-----EIVKALLGKGAQVNAVNQNGCTPLHYAASK---NRHEIAVM 124
Cdd:PHA02798  51 TDIVKLFINLGANVNGLDNEYSTPLCTILSNIKDykhmlDIVKILIENGADINKKNSDGETPLYCLLSNgyiNNLEILLF 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217   125 LLEGGANPDAKDHYEATAMHRAAAKGN---LKMIHILLYYKASTN-IQDTEGNTPLHlaC------DEERVEEAKLLVSQ 194
Cdd:PHA02798 131 MIENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDINtHNNKEKYDTLH--CyfkyniDRIDADILKLFVDN 208

                        170
                 ....*....|....*
gi 4506217   195 GASIYIENKEEKTPL 209
Cdd:PHA02798 209 GFIINKENKSHKKKF 223
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 78-161 4.78e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.82  E-value: 4.78e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217    78 HIAASaGRDEIVKALLGKGAQVNAVNQNGCTPLHYAASKNRHEIAVMLLEGGANPDAKDHYEATAMHRAAAKGNLKMIHI 157
Cdd:PTZ00322  88 QLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                 ....
gi 4506217   158 LLYY 161
Cdd:PTZ00322 167 LSRH 170
Ank_5 pfam13857
Ankyrin repeats (many copies);
124-179 4.89e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.72  E-value: 4.89e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 4506217    124 MLLEGGANPDAKDHYEATAMHRAAAKGNLKMIHILLYYKASTNIQDTEGNTPLHLA 179
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
97-146 7.75e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 7.75e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 4506217     97 AQVNAVNQNGCTPLHYAASKNRHEIAVMLLEGGANPDAKDHYEATAMHRA 146
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 41-71 1.71e-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: 40.74  E-value: 1.71e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 4506217     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 1.82e-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: 1.82e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 4506217     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 2.16e-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: 40.32  E-value: 2.16e-05
                          10        20
                  ....*....|....*....|....*..
gi 4506217     41 RTALHWACSAGHTEIVEFLLQLGVPVN 67
Cdd:pfam13606   3 NTPLHLAARNGRLEIVKLLLENGADIN 29
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 73-103 2.69e-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: 2.69e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 4506217     73 GWSPLHIAA-SAGRDEIVKALLGKGAQVNAVN 103
Cdd:pfam00023   2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
Ank_4 pfam13637
Ankyrin repeats (many copies);
13-60 3.28e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 40.34  E-value: 3.28e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 4506217     13 LAYSGKLEELKeSILADKSLATRTDQDSRTALHWACSAGHTEIVEFLL 60
Cdd:pfam13637   8 AAASGHLELLR-LLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 73-101 3.65e-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: 39.55  E-value: 3.65e-05
                          10        20
                  ....*....|....*....|....*....
gi 4506217     73 GWSPLHIAASAGRDEIVKALLGKGAQVNA 101
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 77-158 4.36e-05

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 42.17  E-value: 4.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217    77 LHIAASAGR---DEIVKALLGKGAQVNAVNQ-NGCTPLHYAASKNRHEIAVMLL-EGGANPDAKDHYEATAMHRAAAKGN 151
Cdd:PHA02736  59 VHIVSNPDKadpQEKLKLLMEWGADINGKERvFGNTPLHIAVYTQNYELATWLCnQPGVNMEILNYAFKTPYYVACERHD 138


                 ....*..
gi 4506217   152 LKMIHIL 158
Cdd:PHA02736 139 AKMMNIL 145
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 39-68 5.94e-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: 39.11  E-value: 5.94e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 4506217      39 DSRTALHWACSAGHTEIVEFLLQLGVPVND 68
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 65-186 6.14e-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: 6.14e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217   65 PVNDKDDAGWSPLHIAASAGRDEIVKALLGKGAQVNA------VNQNGCT-------PLHYAASKNRHEIAVMLLEGGAN 131
Cdd:cd21882  65 PCTDEFYQGQTALHIAIENRNLNLVRLLVENGADVSAratgrfFRKSPGNlfyfgelPLSLAACTNQEEIVRLLLENGAQ 144

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4506217  132 P---DAKDHYEATAMHRAAAKGN---------LKMIHILLYYKASTN-------IQDTEGNTPLHLACDEERVE 186
Cdd:cd21882 145 PaalEAQDSLGNTVLHALVLQADntpensafvCQMYNLLLSYGAHLDptqqleeIPNHQGLTPLKLAAVEGKIV 218
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 42-154 8.19e-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: 43.08  E-value: 8.19e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217   42 TALHWACSAGHTEIVEFLLQLGVPVNdKDDA---------------GWSPLHIAASAGRDEIVKALLGKGAQVNAVNQNG 106
Cdd:cd22192  91 TALHIAVVNQNLNLVRELIARGADVV-SPRAtgtffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLG 169

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 4506217  107 CTPLHYAASKNRHEIA------VMLLEGGANPDAKDHYE----ATAMHRAAAKGNLKM 154
Cdd:cd22192 170 NTVLHILVLQPNKTFAcqmydlILSYDKEDDLQPLDLVPnnqgLTPFKLAAKEGNIVM 227
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 73-101 9.66e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 38.34  E-value: 9.66e-05
                           10        20
                   ....*....|....*....|....*....
gi 4506217      73 GWSPLHIAASAGRDEIVKALLGKGAQVNA 101
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 105-134 9.78e-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: 38.39  E-value: 9.78e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 4506217    105 NGCTPLHYAASKNRHEIAVMLLEGGANPDA 134
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02791 PHA02791
ankyrin-like protein; Provisional
 9-204 1.37e-04

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 41.95  E-value: 1.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217     9 MVCNLAYSGKLEELKESiladkslatrtdqdsRTALHWACSAGHTEIVEFLLQLGVPVNDKDDAGWSPLHIAASAGRDEI 88
Cdd:PHA02791  45 LVCTLLNAGALKNLLEN---------------EFPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDSGNMQT 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217    89 VKALLGKGAQVNAVNQNGC-TPLHYAASKNRHEIAVMLLEggANPDAKD-HYEATAMHRAAAKGNLKMIHILLYYKASTN 166
Cdd:PHA02791 110 VKLFVKKNWRLMFYGKTGWkTSFYHAVMLNDVSIVSYFLS--EIPSTFDlAILLSCIHITIKNGHVDMMILLLDYMTSTN 187

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 4506217   167 IQDTEGNTP-LHLACDEERVEEAKLLVSQGASIYIENKE 204
Cdd:PHA02791 188 TNNSLLFIPdIKLAIDNKDLEMLQALFKYDINIYSVNLE 226
Ank_5 pfam13857
Ankyrin repeats (many copies);
157-212 1.59e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.48  E-value: 1.59e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 4506217    157 ILLYYKASTNIQDTEGNTPLHLACDEERVEEAKLLVSQGASIYIENKEEKTPLQVA 212
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 54-225 1.67e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 42.04  E-value: 1.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217    54 EIVEFLLQLGVPVND-KDDAGWSPLHI--AASAGRDEIVKALLGKGaqVNAVNQN---GCTPLHYAAsknRHEIAVM--- 124
Cdd:PHA02989 125 DMLRFLLSKGINVNDvKNSRGYNLLHMylESFSVKKDVIKILLSFG--VNLFEKTslyGLTPMNIYL---RNDIDVIsik 199

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217   125 ----LLEGGANPDAKDHYEATAM------HRAAAKGNLKMIHILLYYkASTNIQDTEGNTPLHLACDEERVEEAKLLVSQ 194
Cdd:PHA02989 200 vikyLIKKGVNIETNNNGSESVLesfldnNKILSKKEFKVLNFILKY-IKINKKDKKGFNPLLISAKVDNYEAFNYLLKL 278

                        170       180       190
                 ....*....|....*....|....*....|..
gi 4506217   195 GASIYIENKEEKTPLQVA-KGGLGLILKRMVE 225
Cdd:PHA02989 279 GDDIYNVSKDGDTVLTYAiKHGNIDMLNRILQ 310
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 42-194 2.20e-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: 41.61  E-value: 2.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217     42 TALHwACSAGHTEIVEFLLQLGVPVNDKDDAGW--------------SPLHIAASAGRDEIVKALLGKGAQVNA-VNQNG 106
Cdd:TIGR00870  84 TLLH-AISLEYVDAVEAILLHLLAAFRKSGPLElandqytseftpgiTALHLAAHRQNYEIVKLLLERGASVPArACGDF 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217    107 C--TPLHYAASKNRHEIAVmllegganpdakdhyeatamhrAAAKGNLKMIHILLYYKASTNIQDTEGNTPLHLACDE-E 183
Cdd:TIGR00870 163 FvkSQGVDSFYHGESPLNA----------------------AACLGSPSIVALLSEDPADILTADSLGNTLLHLLVMEnE 220

                         170
                  ....*....|.
gi 4506217    184 RVEEAKLLVSQ 194
Cdd:TIGR00870 221 FKAEYEELSCQ 231
PHA02741 PHA02741
hypothetical protein; Provisional
 66-165 9.11e-04

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 38.87  E-value: 9.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217    66 VNDKDDAGWSPLHIAASAGRD----EIVKALLGKGAQVNAVNQ-NGCTPLHYAASKNRHEIAVMLLEGGA------NPDA 134
Cdd:PHA02741  53 LNATDDAGQMCIHIAAEKHEAqlaaEIIDHLIELGADINAQEMlEGDTALHLAAHRRDHDLAEWLCCQPGidlhfcNADN 132

                         90       100       110
                 ....*....|....*....|....*....|.
gi 4506217   135 KDHYEATAMHRaaakgNLKMIHILLYYKAST 165
Cdd:PHA02741 133 KSPFELAIDNE-----DVAMMQILREIVATS 158
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 171-203 1.13e-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: 35.34  E-value: 1.13e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 4506217    171 EGNTPLHLACDEERVEE-AKLLVSQGASIYIENK 203
Cdd:pfam00023   1 DGNTPLHLAAGRRGNLEiVKLLLSKGADVNARDK 34
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 42-116 1.30e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 39.48  E-value: 1.30e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4506217    42 TALHWACSA-GHTEIVEFLLQLGVPVNDKDDA-GWSPLHIAASAGRdeIVKALLGKGAQVNAVNQNGCTPLHYAASK 116
Cdd:PHA02878 236 TPLHISVGYcKDYDILKLLLEHGVDVNAKSYIlGLTALHSSIKSER--KLKLLLEYGADINSLNSYKLTPLSSAVKQ 310
PHA02791 PHA02791
ankyrin-like protein; Provisional
 105-194 1.45e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 38.87  E-value: 1.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217   105 NGCTPLHYAASKNRHEIAVMLLEGGANPDAKDHyeATAMHRAAAKGNLKMIHILLYYKASTNIQDTEGNTPLHLACDEER 184
Cdd:PHA02791  29 HGHSALYYAIADNNVRLVCTLLNAGALKNLLEN--EFPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDSGN 106

                         90
                 ....*....|
gi 4506217   185 VEEAKLLVSQ 194
Cdd:PHA02791 107 MQTVKLFVKK 116
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 98-198 3.43e-03

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 38.14  E-value: 3.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217     98 QVNAVNQNGCTPLHYAASKNRH-EIAVMLLEGGANPDAKDhyeaTAMHrAAAKG-----NLKMIHILLYYKASTNIQ--- 168
Cdd:TIGR00870  44 NINCPDRLGRSALFVAAIENENlELTELLLNLSCRGAVGD----TLLH-AISLEyvdavEAILLHLLAAFRKSGPLElan 118

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 4506217    169 ------DTEGNTPLHLACDEERVEEAKLLVSQGASI 198
Cdd:TIGR00870 119 dqytseFTPGITALHLAAHRQNYEIVKLLLERGASV 154
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 171-200 3.88e-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: 33.77  E-value: 3.88e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 4506217    171 EGNTPLHLACDEERVEEAKLLVSQGASIYI 200
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 171-200 5.53e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 33.33  E-value: 5.53e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 4506217     171 EGNTPLHLACDEERVEEAKLLVSQGASIYI 200
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 153-212 5.79e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 36.01  E-value: 5.79e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4506217   153 KMIHILLYYKASTNIQDT-EGNTPLHLACDEERVEEAKLLVSQ-GASIYIENKEEKTPLQVA 212
Cdd:PHA02736  72 EKLKLLMEWGADINGKERvFGNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYVA 133
PHA02741 PHA02741
hypothetical protein; Provisional
 54-212 8.09e-03

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 35.79  E-value: 8.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217    54 EIVEFLLQLGVPVNDKDDAGWSPLHIAASAGRDEIVKALL------GKGAQVNAVNQNGCTPLHYAASKNRHEIAVmlle 127
Cdd:PHA02741   2 ESPHFMTCLEEMIAEKNSEGENFFHEAARCGCFDIIARFTpfirgdCHAAALNATDDAGQMCIHIAAEKHEAQLAA---- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4506217   128 gganpdakdhyeatamhraaakgnlKMIHILLYYKASTNIQDT-EGNTPLHLACDEERVEEAKLLVSQ-GASIYIENKEE 205
Cdd:PHA02741  78 -------------------------EIIDHLIELGADINAQEMlEGDTALHLAAHRRDHDLAEWLCCQpGIDLHFCNADN 132


                 ....*..
gi 4506217   206 KTPLQVA 212
Cdd:PHA02741 133 KSPFELA 139
 
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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