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Conserved domains on  [gi|665821229|ref|NP_001287905|]
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ankyrin repeat domain-containing protein 42 isoform 5 [Homo sapiens]

Protein Classification

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

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
30-219 6.44e-38

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 133.54  E-value: 6.44e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821229  30 IHDAVRAGDVKQLSEIVVRGASINELDvLHKFTPLHWAAHSGSLECLHWLLWHGADITHVTTRGWTASHIAAIRGQDACV 109
Cdd:COG0666   91 LHAAARNGDLEIVKLLLEAGADVNARD-KDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIV 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821229 110 QALIMNGANLTAQDDRGCTPLHLAATHGHSFTLQIMLRSGVDPSVTDKREWRPVHYAAFHGRLGCLQLLVKWGCSIEDVD 189
Cdd:COG0666  170 KLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKD 249

                        170       180       190
                 ....*....|....*....|....*....|
gi 665821229 190 YNGNLPGGSHLLLSIMATLRPLVKPRIIKK 219
Cdd:COG0666  250 KDGLTALLLAAAAGAALIVKLLLLALLLLA 279
Ribosomal_L32_L32e super family cl00748
Ribosomal_L32_L32e: L32 is a protein from the large subunit that contains a surface-exposed ...
 210-230 8.23e-05

Ribosomal_L32_L32e: L32 is a protein from the large subunit that contains a surface-exposed globular domain and a finger-like projection that extends into the RNA core to stabilize the tertiary structure. L32 does not appear to play a role in forming the A (aminacyl), P (peptidyl) or E (exit) sites of the ribosome, but does interact with 23S rRNA, which has a "kink-turn" secondary structure motif. L32 is overexpressed in human prostate cancer and has been identified as a stably expressed housekeeping gene in macrophages of human chronic obstructive pulmonary disease (COPD) patients. In Schizosaccharomyces pombe, L32 has also been suggested to play a role as a transcriptional regulator in the nucleus. Found in archaea and eukaryotes, this protein is known as L32 in eukaryotes and L32e in archaea.


The actual alignment was detected with superfamily member PTZ00159:

Pssm-ID: 469901  Cd Length: 133  Bit Score: 41.14  E-value: 8.23e-05
                         10        20
                 ....*....|....*....|.
gi 665821229 210 PLVKPRIIKKRTKKFFRHQTD 230
Cdd:PTZ00159   4 PKVKKKIVKKRTKKFTRFQSE 24
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
30-219 6.44e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 133.54  E-value: 6.44e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821229  30 IHDAVRAGDVKQLSEIVVRGASINELDvLHKFTPLHWAAHSGSLECLHWLLWHGADITHVTTRGWTASHIAAIRGQDACV 109
Cdd:COG0666   91 LHAAARNGDLEIVKLLLEAGADVNARD-KDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIV 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821229 110 QALIMNGANLTAQDDRGCTPLHLAATHGHSFTLQIMLRSGVDPSVTDKREWRPVHYAAFHGRLGCLQLLVKWGCSIEDVD 189
Cdd:COG0666  170 KLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKD 249

                        170       180       190
                 ....*....|....*....|....*....|
gi 665821229 190 YNGNLPGGSHLLLSIMATLRPLVKPRIIKK 219
Cdd:COG0666  250 KDGLTALLLAAAAGAALIVKLLLLALLLLA 279
Ank_2 pfam12796
Ankyrin repeats (3 copies);
64-156 2.53e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 84.40  E-value: 2.53e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821229   64 LHWAAHSGSLECLHWLLWHGADITHVTTRGWTASHIAAIRGQDACVQALImNGANLTAQDDrGCTPLHLAATHGHSFTLQ 143
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKDN-GRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 665821229  144 IMLRSGVDPSVTD 156
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 30-185 6.58e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 72.72  E-value: 6.58e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821229  30 IHDAVRAGDVKQLSEIVVRGASINelDVLHK--FTPLHWAAHSGSLECLHWLLWHGADITHVTTRGWTASHIAAIRGQDA 107
Cdd:PHA02875  72 LHDAVEEGDVKAVEELLDLGKFAD--DVFYKdgMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIK 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821229 108 CVQALIMNGANLTAQDDRGCTPLHLAATHGHSFTLQIMLRSGVDPSVTDKR-EWRPVHYAAFHGRLGCLQLLVKWG--CS 184
Cdd:PHA02875 150 GIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNgCVAALCYAIENNKIDIVRLFIKRGadCN 229


                 .
gi 665821229 185 I 185
Cdd:PHA02875 230 I 230
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 59-87 1.56e-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: 40.65  E-value: 1.56e-05
                           10        20
                   ....*....|....*....|....*....
gi 665821229    59 HKFTPLHWAAHSGSLECLHWLLWHGADIT 87
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 62-132 2.17e-05

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 45.00  E-value: 2.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821229  62 TPLHWAAHSGSLECLHWLLWHGADIthVTTRG-------------WTASHI---AAIRGQDACVQALIMNGANLTAQDDR 125
Cdd:cd22192   91 TALHIAVVNQNLNLVRELIARGADV--VSPRAtgtffrpgpknliYYGEHPlsfAACVGNEEIVRLLIEHGADIRAQDSL 168


                 ....*..
gi 665821229 126 GCTPLHL 132
Cdd:cd22192  169 GNTVLHI 175
PTZ00159 PTZ00159
60S ribosomal protein L32; Provisional
 210-230 8.23e-05

60S ribosomal protein L32; Provisional


Pssm-ID: 240297  Cd Length: 133  Bit Score: 41.14  E-value: 8.23e-05
                         10        20
                 ....*....|....*....|.
gi 665821229 210 PLVKPRIIKKRTKKFFRHQTD 230
Cdd:PTZ00159   4 PKVKKKIVKKRTKKFTRFQSE 24
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 62-134 1.79e-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: 41.99  E-value: 1.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821229   62 TPLHWAAHSGSLECLHWLLWHGADITH-------VTTRGWT-ASH------IAAIRGQDACVQALIMNGANLTAQDDRGC 127
Cdd:TIGR00870 130 TALHLAAHRQNYEIVKLLLERGASVPAracgdffVKSQGVDsFYHgesplnAAACLGSPSIVALLSEDPADILTADSLGN 209


                  ....*..
gi 665821229  128 TPLHLAA 134
Cdd:TIGR00870 210 TLLHLLV 216
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
30-219 6.44e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 133.54  E-value: 6.44e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821229  30 IHDAVRAGDVKQLSEIVVRGASINELDvLHKFTPLHWAAHSGSLECLHWLLWHGADITHVTTRGWTASHIAAIRGQDACV 109
Cdd:COG0666   91 LHAAARNGDLEIVKLLLEAGADVNARD-KDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIV 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821229 110 QALIMNGANLTAQDDRGCTPLHLAATHGHSFTLQIMLRSGVDPSVTDKREWRPVHYAAFHGRLGCLQLLVKWGCSIEDVD 189
Cdd:COG0666  170 KLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKD 249

                        170       180       190
                 ....*....|....*....|....*....|
gi 665821229 190 YNGNLPGGSHLLLSIMATLRPLVKPRIIKK 219
Cdd:COG0666  250 KDGLTALLLAAAAGAALIVKLLLLALLLLA 279
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
30-195 2.29e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 132.00  E-value: 2.29e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821229  30 IHDAVRAGDVKQLSEIVVRGASINELDvLHKFTPLHWAAHSGSLECLHWLLWHGADITHVTTRGWTASHIAAIRGQDACV 109
Cdd:COG0666   58 LLAAALAGDLLVALLLLAAGADINAKD-DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIV 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821229 110 QALIMNGANLTAQDDRGCTPLHLAATHGHSFTLQIMLRSGVDPSVTDKREWRPVHYAAFHGRLGCLQLLVKWGCSIEDVD 189
Cdd:COG0666  137 KLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKD 216


                 ....*.
gi 665821229 190 YNGNLP 195
Cdd:COG0666  217 NDGKTA 222
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
17-194 1.09e-28

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 109.27  E-value: 1.09e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821229  17 ANPCSRKKVHFGSIHDAVRAGDVKQLSEIVVRGASINELDvLHKFTPLHWAAHSGSLECLHWLLWHGADITHVTTRGWTA 96
Cdd:COG0666  111 ADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQD-NDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETP 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821229  97 SHIAAIRGQDACVQALIMNGANLTAQDDRGCTPLHLAATHGHSFTLQIMLRSGVDPSVTDKREWRPVHYAAFHGRLGCLQ 176
Cdd:COG0666  190 LHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVK 269

                        170
                 ....*....|....*...
gi 665821229 177 LLVKWGCSIEDVDYNGNL 194
Cdd:COG0666  270 LLLLALLLLAAALLDLLT 287
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
49-195 2.19e-25

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 100.41  E-value: 2.19e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821229  49 GASINELDVLHKFTPLHWAAHSGSLECLHWLLWHGADITHVTTRGWTASHIAAIRGQDACVQALIMNGANLTAQDDRGCT 128
Cdd:COG0666   43 ALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGET 122

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665821229 129 PLHLAATHGHSFTLQIMLRSGVDPSVTDKREWRPVHYAAFHGRLGCLQLLVKWGCSIEDVDYNGNLP 195
Cdd:COG0666  123 PLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETP 189
Ank_2 pfam12796
Ankyrin repeats (3 copies);
64-156 2.53e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 84.40  E-value: 2.53e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821229   64 LHWAAHSGSLECLHWLLWHGADITHVTTRGWTASHIAAIRGQDACVQALImNGANLTAQDDrGCTPLHLAATHGHSFTLQ 143
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKDN-GRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 665821229  144 IMLRSGVDPSVTD 156
Cdd:pfam12796  79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
98-189 2.50e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 74.00  E-value: 2.50e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821229   98 HIAAIRGQDACVQALIMNGANLTAQDDRGCTPLHLAATHGHSFTLQIMLrSGVDPSVTDKReWRPVHYAAFHGRLGCLQL 177
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKDNG-RTALHYAARSGHLEIVKL 79

                          90
                  ....*....|..
gi 665821229  178 LVKWGCSIEDVD 189
Cdd:pfam12796  80 LLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
30-123 1.32e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 69.37  E-value: 1.32e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821229   30 IHDAVRAGDVKQLSEIVVRGASINELDVLHKfTPLHWAAHSGSLECLHWLLWHGAdiTHVTTRGWTASHIAAIRGQDACV 109
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGR-TALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIV 77

                          90
                  ....*....|....
gi 665821229  110 QALIMNGANLTAQD 123
Cdd:pfam12796  78 KLLLEKGADINVKD 91
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 30-185 6.58e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 72.72  E-value: 6.58e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821229  30 IHDAVRAGDVKQLSEIVVRGASINelDVLHK--FTPLHWAAHSGSLECLHWLLWHGADITHVTTRGWTASHIAAIRGQDA 107
Cdd:PHA02875  72 LHDAVEEGDVKAVEELLDLGKFAD--DVFYKdgMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIK 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821229 108 CVQALIMNGANLTAQDDRGCTPLHLAATHGHSFTLQIMLRSGVDPSVTDKR-EWRPVHYAAFHGRLGCLQLLVKWG--CS 184
Cdd:PHA02875 150 GIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNgCVAALCYAIENNKIDIVRLFIKRGadCN 229


                 .
gi 665821229 185 I 185
Cdd:PHA02875 230 I 230
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
42-195 1.22e-14

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 71.14  E-value: 1.22e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821229  42 LSEIVVRGASINELDVLHKFTPLHWAAHSGSLECLHWLLWHGADITHVTTRGWTASHIAAIRGQDACVQALIMNGANLTA 121
Cdd:COG0666    3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665821229 122 QDDRGCTPLHLAATHGHSFTLQIMLRSGVDPSVTDKREWRPVHYAAFHGRLGCLQLLVKWGCSIEDVDYNGNLP 195
Cdd:COG0666   83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTP 156
PHA03095 PHA03095
ankyrin-like protein; Provisional
 48-196 1.87e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 71.59  E-value: 1.87e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821229  48 RGASINELDvLHKFTPLHW--AAHSGSLECLHWLLWHGADITHVTTRGWTASHIAA--IRGQDACVQALIMNGANLTAQD 123
Cdd:PHA03095 141 KGADVNALD-LYGMTPLAVllKSRNANVELLRLLIDAGADVYAVDDRFRSLLHHHLqsFKPRARIVRELIRAGCDPAATD 219

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665821229 124 DRGCTPLHLAATHGHSFTLQI--MLRSGVDPSVTDKREWRPVHYAA-FHGRLGCLQLLvKWGCSIEDVDYNGNLPG 196
Cdd:PHA03095 220 MLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAvFNNPRACRRLI-ALGADINAVSSDGNTPL 294
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 29-186 4.88e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 70.48  E-value: 4.88e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821229  29 SIHDAVRAGDVKQLSEIVVRGASINELDVlHKFTPLHWAAHSGSLECL-HWLLWHGADITHVTTRGWTASHIAAIRGQDA 107
Cdd:PHA02876 243 SLLKAIRNEDLETSLLLYDAGFSVNSIDD-CKNTPLHHASQAPSLSRLvPKLLERGADVNAKNIKGETPLYLMAKNGYDT 321

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821229 108 -CVQALIMNGANLTAQDDRGCTPLHLAAT-HGHSFTLQIMLRSGVDPSVTDKREWRPVHYAAFHGRLGCLQLLVKWGCSI 185
Cdd:PHA02876 322 eNIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADI 401


                 .
gi 665821229 186 E 186
Cdd:PHA02876 402 E 402
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 45-195 6.49e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 67.30  E-value: 6.49e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821229  45 IVVRGASINELDVLHKfTPLHWAAHSGSLECLHWLLWHGADITHVTTRGWTASHIAAIRGQDACVQALIMNGANLTAQDD 124
Cdd:PHA02874 110 ILDCGIDVNIKDAELK-TFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDN 188

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665821229 125 RGCTPLHLAATHGHSFTLQIMLRSGVDPSVTDKREWRPVHYAAFHGRlGCLQLLVKwGCSIEDVDYNGNLP 195
Cdd:PHA02874 189 NGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLIN-NASINDQDIDGSTP 257
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 26-189 7.40e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 63.92  E-value: 7.40e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821229  26 HFGSIHDAVRAGDVKQLSEIVVRGASINELDVLHkFTPLHWAA--HSGSLECLHWLLWHGADITHVTTRGWTASHIAAIR 103
Cdd:PHA03100  73 HYLSNIKYNLTDVKEIVKLLLEYGANVNAPDNNG-ITPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLES 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821229 104 GQ----------------DAC--VQALIMNGANLTAQDDRGCTPLHLAATHGHSFTLQIMLRSGVDPSVTDKREWRPVHY 165
Cdd:PHA03100 152 NKidlkilkllidkgvdiNAKnrVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHI 231

                        170       180
                 ....*....|....*....|....
gi 665821229 166 AAFHGRLGCLQLLVKWGCSIEDVD 189
Cdd:PHA03100 232 AILNNNKEIFKLLLNNGPSIKTII 255
PHA03095 PHA03095
ankyrin-like protein; Provisional
 49-218 7.19e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 61.19  E-value: 7.19e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821229  49 GASINELDvLHKFTPLH-WAAHSGSLECLHWLLWHGADITHVTTRGWTASHIAAiRGQ--DACV-QALIMNGANLTAQDD 124
Cdd:PHA03095  73 GADVNAPE-RCGFTPLHlYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVYL-SGFniNPKViRLLLRKGADVNALDL 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821229 125 RGCTPLH-LAATHGHSF-TLQIMLRSGVDPSVTDKREWRPVHYAA--FHGRLGCLQLLVKWGCSIEDVDYNGNLPggSHL 200
Cdd:PHA03095 151 YGMTPLAvLLKSRNANVeLLRLLIDAGADVYAVDDRFRSLLHHHLqsFKPRARIVRELIRAGCDPAATDMLGNTP--LHS 228

                        170
                 ....*....|....*...
gi 665821229 201 LLSIMATLRPLVKPRIIK 218
Cdd:PHA03095 229 MATGSSCKRSLVLPLLIA 246
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 32-195 1.18e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 60.36  E-value: 1.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821229  32 DAVRAGDVKQLSEIVVRGASINELD--VLHkftPLHWAAHSGSLECLHWLLWHGADIT--------------------HV 89
Cdd:PHA02874  41 DAIRSGDAKIVELFIKHGADINHINtkIPH---PLLTAIKIGAHDIIKLLIDNGVDTSilpipciekdmiktildcgiDV 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821229  90 TTRGW---TASHIAAIRGQDACVQALIMNGANLTAQDDRGCTPLHLAATHGHSFTLQIMLRSGVDPSVTDKREWRPVHYA 166
Cdd:PHA02874 118 NIKDAelkTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNA 197

                        170       180
                 ....*....|....*....|....*....
gi 665821229 167 AFHGRLGCLQLLVKWGCSIEDVDYNGNLP 195
Cdd:PHA02874 198 AEYGDYACIKLLIDHGNHIMNKCKNGFTP 226
Ank_4 pfam13637
Ankyrin repeats (many copies);
62-113 1.64e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.97  E-value: 1.64e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 665821229   62 TPLHWAAHSGSLECLHWLLWHGADITHVTTRGWTASHIAAIRGQDACVQALI 113
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 30-166 9.23e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 57.67  E-value: 9.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821229  30 IHDAVRAGDVKQLSEIVVRGASINELDVlHKFTPLHWAAHSGSLECLHWLLWHGADITHVTTRGWTASHIAAIRGQDACv 109
Cdd:PHA02874 161 IHIAIKHNFFDIIKLLLEKGAYANVKDN-NGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAI- 238

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 665821229 110 qALIMNGANLTAQDDRGCTPLHLAATHGHSF-TLQIMLRSGVDPSVTDKREWRPVHYA 166
Cdd:PHA02874 239 -ELLINNASINDQDIDGSTPLHHAINPPCDIdIIDILLYHKADISIKDNKGENPIDTA 295
Ank_4 pfam13637
Ankyrin repeats (many copies);
128-179 8.59e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.35  E-value: 8.59e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 665821229  128 TPLHLAATHGHSFTLQIMLRSGVDPSVTDKREWRPVHYAAFHGRLGCLQLLV 179
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
130-213 9.51e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 51.27  E-value: 9.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821229  130 LHLAATHGHSFTLQIMLRSGVDPSVTDKREWRPVHYAAFHGRLGCLQLLvkwgcsIEDVDYNGNLPGGSHLLLSIMATLR 209
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL------LEHADVNLKDNGRTALHYAARSGHL 74


                  ....
gi 665821229  210 PLVK 213
Cdd:pfam12796  75 EIVK 78
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 98-195 1.50e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.52  E-value: 1.50e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821229  98 HIAAiRGQDACVQALIMNGANLTAQDDRGCTPLHLAATHGHSFTLQIMLRSGVDPSVTDKREWRPVHYAAFHGRLGCLQL 177
Cdd:PTZ00322  88 QLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166

                         90
                 ....*....|....*...
gi 665821229 178 LVkwGCSIEDVDYNGNLP 195
Cdd:PTZ00322 167 LS--RHSQCHFELGANAK 182
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 49-187 2.32e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 53.91  E-value: 2.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821229  49 GASINELDVLHKfTPLHWAAHSGSLECLHWLLWHGADITHVTTRGWTASHIaAIRGQD--ACVQALIMNGANLTAQDDRG 126
Cdd:PHA02876 365 GANVNARDYCDK-TPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHF-ALCGTNpyMSVKTLIDRGANVNSKNKDL 442

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665821229 127 CTPLHLAATHGHSF-TLQIMLRSGVDPSVTDKREWRPVHYA-AFHgrlGCLQLLVKWGCSIED 187
Cdd:PHA02876 443 STPLHYACKKNCKLdVIEMLLDNGADVNAINIQNQYPLLIAlEYH---GIVNILLHYGAELRD 502
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 34-195 3.61e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 53.04  E-value: 3.61e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821229  34 VRAGDVKQLSEIV-VRGASINeLDVLHKFTPLHWAAHSGSLECLHWLLWHGADITHVTTRgwtASH--IAAIR-GQDACV 109
Cdd:PHA02874   9 IYSGDIEAIEKIIkNKGNCIN-ISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTK---IPHplLTAIKiGAHDII 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821229 110 QALIMNGANLTAqddrgctplhLAATHGHSFTLQIMLRSGVDPSVTDKREWRPVHYAAFHGRLGCLQLLVKWGCSIEDVD 189
Cdd:PHA02874  85 KLLIDNGVDTSI----------LPIPCIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIED 154


                 ....*.
gi 665821229 190 YNGNLP 195
Cdd:PHA02874 155 DNGCYP 160
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 49-195 7.15e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 52.19  E-value: 7.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821229  49 GASINELDVLHKFTPLHWAAHSGSLECLHWLLWHGADITHVTTRGWTASHIAAIRGQDACVQALIMNGANLTAQDDRGCT 128
Cdd:PHA02878 157 GADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNT 236

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665821229 129 PLHLAATHGHSFT-LQIMLRSGVDPSVTDK-REWRPVHYAAFHGRLgcLQLLVKWGCSIEDVDYNGNLP 195
Cdd:PHA02878 237 PLHISVGYCKDYDiLKLLLEHGVDVNAKSYiLGLTALHSSIKSERK--LKLLLEYGADINSLNSYKLTP 303
Ank_4 pfam13637
Ankyrin repeats (many copies);
93-138 1.06e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.27  E-value: 1.06e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 665821229   93 GWTASHIAAIRGQDACVQALIMNGANLTAQDDRGCTPLHLAATHGH 138
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGN 46
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 133-193 1.34e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 48.71  E-value: 1.34e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665821229 133 AATHGHSFTLQIMLRSGVDPSVTDKREWRPVHYAAFHGRLGCLQLLVKWGCSIEDVDYNGN 193
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGN 592
Ank_5 pfam13857
Ankyrin repeats (many copies);
84-133 1.64e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.87  E-value: 1.64e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 665821229   84 ADITHVTTRGWTASHIAAIRGQDACVQALIMNGANLTAQDDRGCTPLHLA 133
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 29-166 1.09e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 45.64  E-value: 1.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821229  29 SIHDAVRAGDVKQLSEIVVRGASINELDVLHKfTPLHWAAHSGSLECLHWLLWHGADITHVTTRGWTASHIAAIRGQD-A 107
Cdd:PHA02878 171 ALHYATENKDQRLTELLLSYGANVNIPDKTNN-SPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDyD 249

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665821229 108 CVQALIMNGANLTAQDD-RGCTPLHLAAthgHS-FTLQIMLRSGVDPSVTDKREWRPVHYA 166
Cdd:PHA02878 250 ILKLLLEHGVDVNAKSYiLGLTALHSSI---KSeRKLKLLLEYGADINSLNSYKLTPLSSA 307
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 59-87 1.56e-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: 40.65  E-value: 1.56e-05
                           10        20
                   ....*....|....*....|....*....
gi 665821229    59 HKFTPLHWAAHSGSLECLHWLLWHGADIT 87
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
Ank_5 pfam13857
Ankyrin repeats (many copies);
58-100 1.96e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.18  E-value: 1.96e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 665821229   58 LHKFTPLHWAAHSGSLECLHWLLWHGADITHVTTRGWTASHIA 100
Cdd:pfam13857  14 GEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 109-195 2.05e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 44.87  E-value: 2.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821229 109 VQALIMNGANLTAQD-DRGCTPLHLAATHGHSFTLQIMLRSGVDPSVTDKREWRPVHYAAFHGRLGCLQLLVKWGCSIED 187
Cdd:PHA02878 150 TKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDA 229


                 ....*...
gi 665821229 188 VDYNGNLP 195
Cdd:PHA02878 230 RDKCGNTP 237
Ank_5 pfam13857
Ankyrin repeats (many copies);
117-166 2.16e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.79  E-value: 2.16e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 665821229  117 ANLTAQDDRGCTPLHLAATHGHSFTLQIMLRSGVDPSVTDKREWRPVHYA 166
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 62-132 2.17e-05

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 45.00  E-value: 2.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821229  62 TPLHWAAHSGSLECLHWLLWHGADIthVTTRG-------------WTASHI---AAIRGQDACVQALIMNGANLTAQDDR 125
Cdd:cd22192   91 TALHIAVVNQNLNLVRELIARGADV--VSPRAtgtffrpgpknliYYGEHPlsfAACVGNEEIVRLLIEHGADIRAQDSL 168


                 ....*..
gi 665821229 126 GCTPLHL 132
Cdd:cd22192  169 GNTVLHI 175
Ank_4 pfam13637
Ankyrin repeats (many copies);
30-80 2.22e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 40.72  E-value: 2.22e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 665821229   30 IHDAVRAGDVKQLSEIVVRGASINELDVLHkFTPLHWAAHSGSLECLHWLL 80
Cdd:pfam13637   5 LHAAAASGHLELLRLLLEKGADINAVDGNG-ETALHFAASNGNVEVLKLLL 54
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
31-130 2.72e-05

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 44.17  E-value: 2.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821229  31 HDAVRAGDVKQLSEIVVRGASINELDVLHKfTPLHWAAHSGSLECLHWLLWHGADITHVTTRGWTASHIAAIRGQDACVQ 110
Cdd:COG0666  191 HLAAENGHLEIVKLLLEAGADVNAKDNDGK-TALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVK 269

                         90       100
                 ....*....|....*....|
gi 665821229 111 ALIMNGANLTAQDDRGCTPL 130
Cdd:COG0666  270 LLLLALLLLAAALLDLLTLL 289
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 30-166 3.27e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 44.28  E-value: 3.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821229  30 IHDAVRAGDVKQL-SEIVVRGASINELDVLHKfTPLHWAAHSG-SLECLHWLLWHGADITHVTTRGWTASHIAAI--RGQ 105
Cdd:PHA02876 277 LHHASQAPSLSRLvPKLLERGADVNAKNIKGE-TPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQASTldRNK 355

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665821229 106 DACVQALIMnGANLTAQDDRGCTPLHLAATHGHSFTLQIMLRSGVDPSVTDKREWRPVHYA 166
Cdd:PHA02876 356 DIVITLLEL-GANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFA 415
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 67-192 3.32e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 44.47  E-value: 3.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821229  67 AAHSGSLECLHWLLWHGADITHVTTRGWTASHIAAIRGQDACVQALIMNGANLTAQDDRGCTPLHLAATHGHSFTLQIM- 145
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILy 611

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 665821229 146 -LRSGVDPSVTDKRewrpVHYAAFHGRLGCLQLLVKWGCSIEDVDYNG 192
Cdd:PLN03192 612 hFASISDPHAAGDL----LCTAAKRNDLTAMKELLKQGLNVDSEDHQG 655
PHA03095 PHA03095
ankyrin-like protein; Provisional
 42-138 3.50e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 44.25  E-value: 3.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821229  42 LSEIVVRGASINELDVLHKfTPLHWAAHSGSLECLHW--LLWHGADITHVTTRGWTASHIAAIRGQDACVQALIMNGANL 119
Cdd:PHA03095 205 VRELIRAGCDPAATDMLGN-TPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADI 283

                         90
                 ....*....|....*....
gi 665821229 120 TAQDDRGCTPLHLAATHGH 138
Cdd:PHA03095 284 NAVSSDGNTPLSLMVRNNN 302
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 59-88 3.82e-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: 3.82e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 665821229   59 HKFTPLHWAAHSGSLECLHWLLWHGADITH 88
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 79-185 4.10e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 44.10  E-value: 4.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821229  79 LLWHGADITHVT-TRGWTASHIAAIRGQDACVQALIMNGANLTAQDDRGCTPLHLAATHGHSFTLQIMLRSGVDPSVTDK 157
Cdd:PHA02878 153 LLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDK 232

                         90       100       110
                 ....*....|....*....|....*....|.
gi 665821229 158 REWRPVHYAAfhGRL---GCLQLLVKWGCSI 185
Cdd:PHA02878 233 CGNTPLHISV--GYCkdyDILKLLLEHGVDV 261
PHA03095 PHA03095
ankyrin-like protein; Provisional
 79-219 4.36e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 43.86  E-value: 4.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821229  79 LLWHGADITHVTTRGWTASHIAAIRGQDAC---VQALIMNGANLTAQDDRGCTPLHLAATHG------------------ 137
Cdd:PHA03095  33 LLAAGADVNFRGEYGKTPLHLYLHYSSEKVkdiVRLLLEAGADVNAPERCGFTPLHLYLYNAttldvikllikagadvna 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821229 138 ------------------HSFTLQIMLRSGVDPSVTDKREWRPVH-YAAFHG-RLGCLQLLVKWGCSIEDVDYNGNlpgg 197
Cdd:PHA03095 113 kdkvgrtplhvylsgfniNPKVIRLLLRKGADVNALDLYGMTPLAvLLKSRNaNVELLRLLIDAGADVYAVDDRFR---- 188

                        170       180
                 ....*....|....*....|..
gi 665821229 198 sHLLLSIMATLRPlvKPRIIKK 219
Cdd:PHA03095 189 -SLLHHHLQSFKP--RARIVRE 207
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 29-167 4.83e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 43.90  E-value: 4.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821229  29 SIHDAVRAGDVKQLSEIVVRGASINELDVlHKFTPLHWAAHSGSLECLHWLLWHGADITHVTTRGWTASHIAAIRGQDAC 108
Cdd:PHA02876 148 LIKERIQQDELLIAEMLLEGGADVNAKDI-YCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDT 226

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 665821229 109 VQALIMNGANLTAQDdrgcTPLHLAATHGHSFTLQIMLRSGVDPSVTDKREWRPVHYAA 167
Cdd:PHA02876 227 IKAIIDNRSNINKND----LSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHAS 281
PTZ00159 PTZ00159
60S ribosomal protein L32; Provisional
 210-230 8.23e-05

60S ribosomal protein L32; Provisional


Pssm-ID: 240297  Cd Length: 133  Bit Score: 41.14  E-value: 8.23e-05
                         10        20
                 ....*....|....*....|.
gi 665821229 210 PLVKPRIIKKRTKKFFRHQTD 230
Cdd:PTZ00159   4 PKVKKKIVKKRTKKFTRFQSE 24
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 62-195 1.50e-04

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: 42.31  E-value: 1.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821229  62 TPLHWAAHSGSLECLHWLL-WHGADITHVTTRGWTASHIAAIRGQDACVQALIMNGANL-----TAQDDRGCTPLHLAAT 135
Cdd:cd22192   19 SPLLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELvnepmTSDLYQGETALHIAVV 98

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665821229 136 HGHSFTLQIMLRSGVD---PSVTDK--REWR---------PVHYAAFHGRLGCLQLLVKWGCSIEDVDYNGNLP 195
Cdd:cd22192   99 NQNLNLVRELIARGADvvsPRATGTffRPGPknliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTV 172
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 62-134 1.79e-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: 41.99  E-value: 1.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821229   62 TPLHWAAHSGSLECLHWLLWHGADITH-------VTTRGWT-ASH------IAAIRGQDACVQALIMNGANLTAQDDRGC 127
Cdd:TIGR00870 130 TALHLAAHRQNYEIVKLLLERGASVPAracgdffVKSQGVDsFYHgesplnAAACLGSPSIVALLSEDPADILTADSLGN 209


                  ....*..
gi 665821229  128 TPLHLAA 134
Cdd:TIGR00870 210 TLLHLLV 216
PHA02946 PHA02946
ankyin-like protein; Provisional
 101-195 2.41e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 41.58  E-value: 2.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821229 101 AIRGQDA-CVQALIMNGANLTAQDDRGCTPLHLAATHGHSFTLQIMLRSGVDPSVTDKREWRPVHYAAFHGR--LGCLQL 177
Cdd:PHA02946  46 GIKGLDErFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINL 125

                         90
                 ....*....|....*....
gi 665821229 178 LVKWGCSIED-VDYNGNLP 195
Cdd:PHA02946 126 LVQYGAKINNsVDEEGCGP 144
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 59-90 3.19e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. 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: 37.27  E-value: 3.19e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 665821229   59 HKFTPLHWAA-HSGSLECLHWLLWHGADITHVT 90
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PHA02946 PHA02946
ankyin-like protein; Provisional
 33-195 3.51e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 41.19  E-value: 3.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821229  33 AVRAGDVKQLSEIVVRGASINELDVLHKFtPLHWAAHSGSLECLHWLLWHGADITHVTTRGWTAshIAAIRGQDACV--- 109
Cdd:PHA02946  46 GIKGLDERFVEELLHRGYSPNETDDDGNY-PLHIASKINNNRIVAMLLTHGADPNACDKQHKTP--LYYLSGTDDEVier 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821229 110 -QALIMNGANL-TAQDDRGCTPLhLAATHGHSFTLQIMLRSGVDPSVTDKREWRPV--HYAAFHGRLGCLQLLVKWGCSI 185
Cdd:PHA02946 123 iNLLVQYGAKInNSVDEEGCGPL-LACTDPSERVFKKIMSIGFEARIVDKFGKNHIhrHLMSDNPKASTISWMMKLGISP 201

                        170
                 ....*....|
gi 665821229 186 EDVDYNGNLP 195
Cdd:PHA02946 202 SKPDHDGNTP 211
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 57-147 5.57e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 40.65  E-value: 5.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821229  57 VLHKFT-PLHWAAHSGSLECLHWLLWHGADITHVTTRGWTASHIAAIRGQDACVQALIMNGANLTAQDDRGCTPLHLAAT 135
Cdd:PTZ00322  78 VAHMLTvELCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEE 157

                         90
                 ....*....|..
gi 665821229 136 HGHSFTLQIMLR 147
Cdd:PTZ00322 158 NGFREVVQLLSR 169
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 125-157 8.85e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. 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: 35.73  E-value: 8.85e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 665821229  125 RGCTPLHLAATH-GHSFTLQIMLRSGVDPSVTDK 157
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 125-154 1.07e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.64  E-value: 1.07e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 665821229   125 RGCTPLHLAATHGHSFTLQIMLRSGVDPSV 154
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 92-124 2.29e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 34.57  E-value: 2.29e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 665821229   92 RGWTASHIAAIR-GQDACVQALIMNGANLTAQDD 124
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
PHA03095 PHA03095
ankyrin-like protein; Provisional
 109-195 3.29e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 38.08  E-value: 3.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821229 109 VQALIMNGANLTAQDDRGCTPLHlaaTHGHSFT------LQIMLRSGVDPSVTDKREWRPVH-YAAFHGRLGCLQLLVKW 181
Cdd:PHA03095  30 VRRLLAAGADVNFRGEYGKTPLH---LYLHYSSekvkdiVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKA 106

                         90
                 ....*....|....
gi 665821229 182 GCSIEDVDYNGNLP 195
Cdd:PHA03095 107 GADVNAKDKVGRTP 120
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 26-132 5.16e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 37.54  E-value: 5.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665821229  26 HFGSIHDAVRAGDVkqlseivvrgasineldvlhkftpLHWAAHSGSLECLHWLLWHGADITHVTTRGWTASHIAAIRGQ 105
Cdd:PLN03192 612 HFASISDPHAAGDL------------------------LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDH 667

                         90       100
                 ....*....|....*....|....*...
gi 665821229 106 DACVQALIMNGANLT-AQDDRGCTPLHL 132
Cdd:PLN03192 668 VDMVRLLIMNGADVDkANTDDDFSPTEL 695
Ank_4 pfam13637
Ankyrin repeats (many copies);
159-195 5.81e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 34.17  E-value: 5.81e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 665821229  159 EWRPVHYAAFHGRLGCLQLLVKWGCSIEDVDYNGNLP 195
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETA 37
 
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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