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Conserved domains on  [gi|269784664|ref|NP_598732|]
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ankyrin repeat domain-containing protein 10 isoform 1 [Mus musculus]

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];
24-177 3.63e-32

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 123.53  E-value: 3.63e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784664  24 PLHRACRDGDLVALCSLLPHtpRAHLAAEDSfYGWTPVHWAAHFGKLECLMQLVRAGASLNVsTTRYAQTPAHIAAFGGH 103
Cdd:COG0666   90 LLHAAARNGDLEIVKLLLEA--GADVNARDK-DGETPLHLAAYNGNLEIVKLLLEAGADVNA-QDNDGNTPLHLAAANGN 165

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 269784664 104 PQCLVWLIQAGANINKPDCEGETPIHKAARSGSLECITALVGSGAHTDLRNASGLTAADIAQTQGFQECTQFLL 177
Cdd:COG0666  166 LEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
24-177 3.63e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 123.53  E-value: 3.63e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784664  24 PLHRACRDGDLVALCSLLPHtpRAHLAAEDSfYGWTPVHWAAHFGKLECLMQLVRAGASLNVsTTRYAQTPAHIAAFGGH 103
Cdd:COG0666   90 LLHAAARNGDLEIVKLLLEA--GADVNARDK-DGETPLHLAAYNGNLEIVKLLLEAGADVNA-QDNDGNTPLHLAAANGN 165

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 269784664 104 PQCLVWLIQAGANINKPDCEGETPIHKAARSGSLECITALVGSGAHTDLRNASGLTAADIAQTQGFQECTQFLL 177
Cdd:COG0666  166 LEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239
Ank_2 pfam12796
Ankyrin repeats (3 copies);
62-154 6.08e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.84  E-value: 6.08e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784664   62 HWAAHFGKLECLMQLVRAGASLNVsTTRYAQTPAHIAAFGGHPQCLVWLIQaGANINKpDCEGETPIHKAARSGSLECIT 141
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENGADANL-QDKNGRTALHLAAKNGHLEIVKLLLE-HADVNL-KDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 269784664  142 ALVGSGAHTDLRN 154
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 21-161 5.35e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 60.78  E-value: 5.35e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784664  21 LRFPLHRACRDGDLVALCSLLphtpRAHLAAEDSFY--GWTPVHWAAHFGKLECLMQLVRAGASLNVSTTRYAqTPAHIA 98
Cdd:PHA02875  68 IESELHDAVEEGDVKAVEELL----DLGKFADDVFYkdGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKF-SPLHLA 142

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 269784664  99 AFGGHPQCLVWLIQAGANINKPDCEGETPIHKAARSGSLECITALVGSGAHTDLRNASGLTAA 161
Cdd:PHA02875 143 VMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAA 205
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 53-184 1.05e-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: 44.69  E-value: 1.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784664   53 DSFY-GWTPVHWAAHFGKLECLMQLVRAGASLNVSTT-------------RYAQTPAHIAAFGGHPQCLVWLIQAGANIN 118
Cdd:TIGR00870 123 SEFTpGITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfYHGESPLNAAACLGSPSIVALLSEDPADIL 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784664  119 KPDCEGETPIHKAA---------RSGSLECITALVGSGAHTD-------LRNASGLTAADIAQTQGFQECTQFLLSLQNH 182
Cdd:TIGR00870 203 TADSLGNTLLHLLVmenefkaeyEELSCQMYNFALSLLDKLRdskelevILNHQGLTPLKLAAKEGRIVLFRLKLAIKYK 282


                  ..
gi 269784664  183 QM 184
Cdd:TIGR00870 283 QK 284
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 56-85 2.82e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.95  E-value: 2.82e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 269784664    56 YGWTPVHWAAHFGKLECLMQLVRAGASLNV 85
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 25-182 5.13e-03

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: 39.23  E-value: 5.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784664  25 LHRACRDGDLVALCSLLPHTPR-AHLAAEDSFY-GWTPVHWAAHFGKLECLMQLVRAGASlnVSTTR------------- 89
Cdd:cd22192   55 LHVAALYDNLEAAVVLMEAAPElVNEPMTSDLYqGETALHIAVVNQNLNLVRELIARGAD--VVSPRatgtffrpgpknl 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784664  90 --YAQTPAHIAAFGGHPQCLVWLIQAGANINKPDCEGETPIH----KAARSGSLECITALVGSGAHTD------LRNASG 157
Cdd:cd22192  133 iyYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHilvlQPNKTFACQMYDLILSYDKEDDlqpldlVPNNQG 212

                        170       180
                 ....*....|....*....|....*
gi 269784664 158 LTAADIAQTQGFQECTQFLLSLQNH 182
Cdd:cd22192  213 LTPFKLAAKEGNIVMFQHLVQKRRH 237
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
24-177 3.63e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 123.53  E-value: 3.63e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784664  24 PLHRACRDGDLVALCSLLPHtpRAHLAAEDSfYGWTPVHWAAHFGKLECLMQLVRAGASLNVsTTRYAQTPAHIAAFGGH 103
Cdd:COG0666   90 LLHAAARNGDLEIVKLLLEA--GADVNARDK-DGETPLHLAAYNGNLEIVKLLLEAGADVNA-QDNDGNTPLHLAAANGN 165

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 269784664 104 PQCLVWLIQAGANINKPDCEGETPIHKAARSGSLECITALVGSGAHTDLRNASGLTAADIAQTQGFQECTQFLL 177
Cdd:COG0666  166 LEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
24-178 1.13e-27

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 111.20  E-value: 1.13e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784664  24 PLHRACRDGDLVALCSLLPHtprAHLAAEDSFYGWTPVHWAAHFGKLECLMQLVRAGASLNVsTTRYAQTPAHIAAFGGH 103
Cdd:COG0666   57 LLLAAALAGDLLVALLLLAA---GADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNA-RDKDGETPLHLAAYNGN 132

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 269784664 104 PQCLVWLIQAGANINKPDCEGETPIHKAARSGSLECITALVGSGAHTDLRNASGLTAADIAQTQGFQECTQFLLS 178
Cdd:COG0666  133 LEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLE 207
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
24-177 1.49e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 96.95  E-value: 1.49e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784664  24 PLHRACRDGDLVALCSLLPHtpRAHLAAEDSfYGWTPVHWAAHFGKLECLMQLVRAGASLNVsTTRYAQTPAHIAAFGGH 103
Cdd:COG0666  123 PLHLAAYNGNLEIVKLLLEA--GADVNAQDN-DGNTPLHLAAANGNLEIVKLLLEAGADVNA-RDNDGETPLHLAAENGH 198

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 269784664 104 PQCLVWLIQAGANINKPDCEGETPIHKAARSGSLECITALVGSGAHTDLRNASGLTAADIAQTQGFQECTQFLL 177
Cdd:COG0666  199 LEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLL 272
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
47-178 5.75e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 80.77  E-value: 5.75e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784664  47 AHLAAEDSFYGWTPVHWAAHFGKLECLMQLVRAGASLNVSTTRYAQTPAHIAAFGGHPQCLVWLIQAGANINKPDCEGET 126
Cdd:COG0666   43 ALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGET 122

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 269784664 127 PIHKAARSGSLECITALVGSGAHTDLRNASGLTAADIAQTQGFQECTQFLLS 178
Cdd:COG0666  123 PLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLE 174
Ank_2 pfam12796
Ankyrin repeats (3 copies);
62-154 6.08e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.84  E-value: 6.08e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784664   62 HWAAHFGKLECLMQLVRAGASLNVsTTRYAQTPAHIAAFGGHPQCLVWLIQaGANINKpDCEGETPIHKAARSGSLECIT 141
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENGADANL-QDKNGRTALHLAAKNGHLEIVKLLLE-HADVNL-KDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 269784664  142 ALVGSGAHTDLRN 154
Cdd:pfam12796  79 LLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
24-161 1.31e-15

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 76.92  E-value: 1.31e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784664  24 PLHRACRDGDLVALCSLLPHtpRAHLAAEDSfYGWTPVHWAAHFGKLECLMQLVRAGASLNVsTTRYAQTPAHIAAFGGH 103
Cdd:COG0666  156 PLHLAAANGNLEIVKLLLEA--GADVNARDN-DGETPLHLAAENGHLEIVKLLLEAGADVNA-KDNDGKTALDLAAENGN 231

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 269784664 104 PQCLVWLIQAGANINKPDCEGETPIHKAARSGSLECITALVGSGAHTDLRNASGLTAA 161
Cdd:COG0666  232 LEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
Ank_2 pfam12796
Ankyrin repeats (3 copies);
96-178 2.51e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.92  E-value: 2.51e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784664   96 HIAAFGGHPQCLVWLIQAGANINKPDCEGETPIHKAARSGSLECITALVgsgAHTDLRNA-SGLTAADIAQTQGFQECTQ 174
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL---EHADVNLKdNGRTALHYAARSGHLEIVK 78


                  ....
gi 269784664  175 FLLS 178
Cdd:pfam12796  79 LLLE 82
Ank_2 pfam12796
Ankyrin repeats (3 copies);
25-121 6.60e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.06  E-value: 6.60e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784664   25 LHRACRDGDLVALCSLLPHTPRAHLAAEDsfyGWTPVHWAAHFGKLECLMQLVragASLNVSTTRYAQTPAHIAAFGGHP 104
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKN---GRTALHLAAKNGHLEIVKLLL---EHADVNLKDNGRTALHYAARSGHL 74

                          90
                  ....*....|....*..
gi 269784664  105 QCLVWLIQAGANINKPD 121
Cdd:pfam12796  75 EIVKLLLEKGADINVKD 91
Ank_4 pfam13637
Ankyrin repeats (many copies);
93-144 2.35e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.74  E-value: 2.35e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 269784664   93 TPAHIAAFGGHPQCLVWLIQAGANINKPDCEGETPIHKAARSGSLECITALV 144
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 21-161 5.35e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 60.78  E-value: 5.35e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784664  21 LRFPLHRACRDGDLVALCSLLphtpRAHLAAEDSFY--GWTPVHWAAHFGKLECLMQLVRAGASLNVSTTRYAqTPAHIA 98
Cdd:PHA02875  68 IESELHDAVEEGDVKAVEELL----DLGKFADDVFYkdGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKF-SPLHLA 142

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 269784664  99 AFGGHPQCLVWLIQAGANINKPDCEGETPIHKAARSGSLECITALVGSGAHTDLRNASGLTAA 161
Cdd:PHA02875 143 VMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAA 205
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
64-178 8.64e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 56.50  E-value: 8.64e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784664  64 AAHFGKLECLMQLVRAGASLNVSTTRYAQTPAHIAAFGGHPQCLVWLIQAGANINKPDCEGETPIHKAARSGSLECITAL 143
Cdd:COG0666   27 AAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLL 106

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 269784664 144 VGSGAHTDLRNASGLTAADIAQTQGFQECTQFLLS 178
Cdd:COG0666  107 LEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLE 141
Ank_4 pfam13637
Ankyrin repeats (many copies);
57-111 1.62e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.35  E-value: 1.62e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 269784664   57 GWTPVHWAAHFGKLECLMQLVRAGASLNVsTTRYAQTPAHIAAFGGHPQCLVWLI 111
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINA-VDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 71-211 2.36e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 52.66  E-value: 2.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784664  71 ECLMQLVRAGASLNVSTtRYAQTPAHIAAFGGHPQCLVWLIQAGANINKPDCEGETPIHKAARSGSLECITALVGSGAHT 150
Cdd:PHA02874 105 DMIKTILDCGIDVNIKD-AELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYA 183

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 269784664 151 DLRNASGLTAADIAQTQGFQECTQFLLSLQNHQMSRfCHNGtlsgghesILPTHVSLGTNR 211
Cdd:PHA02874 184 NVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNK-CKNG--------FTPLHNAIIHNR 235
Ank_5 pfam13857
Ankyrin repeats (many copies);
110-164 5.89e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.19  E-value: 5.89e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 269784664  110 LIQAG-ANINKPDCEGETPIHKAARSGSLECITALVGSGAHTDLRNASGLTAADIA 164
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 25-131 1.26e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 50.35  E-value: 1.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784664  25 LHRACRDGDLVALCSLLPHtpRAHLAAEDSfYGWTPVHWAAHFGKLECLMQLVRAGASLNVSTTrYAQTPAHIAAFGGHP 104
Cdd:PHA02874 128 LHYAIKKGDLESIKMLFEY--GADVNIEDD-NGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDN-NGESPLHNAAEYGDY 203

                         90       100
                 ....*....|....*....|....*..
gi 269784664 105 QCLVWLIQAGANINKPDCEGETPIHKA 131
Cdd:PHA02874 204 ACIKLLIDHGNHIMNKCKNGFTPLHNA 230
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 59-159 2.37e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 49.58  E-value: 2.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784664  59 TPVHWAAHFGKLECLMQLVRAGASLNVSTTRyAQTPAHIAAFGGHPQCLVWLIQAGANINKPDCEGETPIHKAARSGSLE 138
Cdd:PHA02874 126 TFLHYAIKKGDLESIKMLFEYGADVNIEDDN-GCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYA 204

                         90       100
                 ....*....|....*....|.
gi 269784664 139 CITALVGSGAHTDLRNASGLT 159
Cdd:PHA02874 205 CIKLLIDHGNHIMNKCKNGFT 225
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 76-164 3.44e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 49.11  E-value: 3.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784664  76 LVRAGASLNVSTTRYAQTPAHIAAFGGHPQCLVWLIQAGANINKPDCEGETPIHKAARSGSLECITALVGSGAHTDLRNA 155
Cdd:PHA02878 153 LLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDK 232


                 ....*....
gi 269784664 156 SGLTAADIA 164
Cdd:PHA02878 233 CGNTPLHIS 241
Ank_4 pfam13637
Ankyrin repeats (many copies);
126-177 4.87e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.42  E-value: 4.87e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 269784664  126 TPIHKAARSGSLECITALVGSGAHTDLRNASGLTAADIAQTQGFQECTQFLL 177
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 23-164 5.10e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 48.42  E-value: 5.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784664  23 FPLHRACRDGDLVALCSLLPHTprAHLAAEDsFYGWTPVHWAAHFGKLECLMQLVRAGASLNVSTTRyAQTPAHIAAFgg 102
Cdd:PHA02874 159 YPIHIAIKHNFFDIIKLLLEKG--AYANVKD-NNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKN-GFTPLHNAII-- 232

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 269784664 103 HPQCLVWLIQAGANINKPDCEGETPIHKAAR-SGSLECITALVGSGAHTDLRNASGLTAADIA 164
Cdd:PHA02874 233 HNRSAIELLINNASINDQDIDGSTPLHHAINpPCDIDIIDILLYHKADISIKDNKGENPIDTA 295
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 25-151 6.59e-06

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 46.02  E-value: 6.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784664  25 LHRACRDGDLVALCSLLPHTPRA--HLAAEDSFYGWTPVHWAAHFGKL---ECLMQLVRAGASLNVSTTRYAQTPAHIAA 99
Cdd:PHA02736  21 LHYLCRNGGVTDLLAFKNAISDEnrYLVLEYNRHGKQCVHIVSNPDKAdpqEKLKLLMEWGADINGKERVFGNTPLHIAV 100

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 269784664 100 FGGHPQCLVWLI-QAGANINKPDCEGETPIHKAARSGSLECITALVGSGAHTD 151
Cdd:PHA02736 101 YTQNYELATWLCnQPGVNMEILNYAFKTPYYVACERHDAKMMNILRAKGAQCK 153
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 57-177 1.51e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 47.17  E-value: 1.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784664  57 GWTPVHWAAHFGKLECLMQLVRAGASLNVSTTRyAQTPAHIAAFGGHpQCLVWLIQAGANINKPDCEGETpIHKAARSGS 136
Cdd:PLN03192 558 GRTPLHIAASKGYEDCVLVLLKHACNVHIRDAN-GNTALWNAISAKH-HKIFRILYHFASISDPHAAGDL-LCTAAKRND 634

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 269784664 137 LECITALVGSGAHTDLRNASGLTAADIAQTQGFQECTQFLL 177
Cdd:PLN03192 635 LTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLI 675
PHA03095 PHA03095
ankyrin-like protein; Provisional
 56-163 1.60e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.94  E-value: 1.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784664  56 YGWTPVHWAAHFGK---LECLMQLVRAGASLNVsTTRYAQTPAHI-AAFGGHPQCLVWLIQAGANINKPDCEGETPIHKA 131
Cdd:PHA03095  46 YGKTPLHLYLHYSSekvKDIVRLLLEAGADVNA-PERCGFTPLHLyLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVY 124

                         90       100       110
                 ....*....|....*....|....*....|....
gi 269784664 132 ARSGSL--ECITALVGSGAHTDLRNASGLTAADI 163
Cdd:PHA03095 125 LSGFNInpKVIRLLLRKGADVNALDLYGMTPLAV 158
Ank_2 pfam12796
Ankyrin repeats (3 copies);
128-191 1.88e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 42.80  E-value: 1.88e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 269784664  128 IHKAARSGSLECITALVGSGAHTDLRNASGLTAADIAQTQGFQECTQFLLslqNHQMSRFCHNG 191
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL---EHADVNLKDNG 61
PHA03095 PHA03095
ankyrin-like protein; Provisional
 50-128 2.12e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.56  E-value: 2.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784664  50 AAEDSFyGWTPVHWAAHFG--KLECLMQLVRAGASLNvSTTRYAQTPAHIAAFGGHPQCLVWLIQAGANINKPDCEGETP 127
Cdd:PHA03095 216 AATDML-GNTPLHSMATGSscKRSLVLPLLIAGISIN-ARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTP 293


                 .
gi 269784664 128 I 128
Cdd:PHA03095 294 L 294
Ank_5 pfam13857
Ankyrin repeats (many copies);
76-131 2.63e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.56  E-value: 2.63e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 269784664   76 LVRAGASLNVSTTRYAQTPAHIAAFGGHPQCLVWLIQAGANINKPDCEGETPIHKA 131
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_2 pfam12796
Ankyrin repeats (3 copies);
22-85 3.65e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 42.03  E-value: 3.65e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 269784664   22 RFPLHRACRDGDLVALCSLLPHtprahLAAEDSFYGWTPVHWAAHFGKLECLMQLVRAGASLNV 85
Cdd:pfam12796  31 RTALHLAAKNGHLEIVKLLLEH-----ADVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINV 89
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 24-154 4.85e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.44  E-value: 4.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784664  24 PLHRAC---RDGDLValCSLLPHTprAHLAAEDsFYGWTPVHWAAHFGKLECLMQLVRAGASLNVSTTRYAqTPAHIAAF 100
Cdd:PHA02876 344 PLHQAStldRNKDIV--ITLLELG--ANVNARD-YCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIG-TALHFALC 417

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 269784664 101 GGHPQCLV-WLIQAGANINKPDCEGETPIHKAARSG-SLECITALVGSGAHTDLRN 154
Cdd:PHA02876 418 GTNPYMSVkTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAIN 473
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 24-148 6.51e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.05  E-value: 6.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784664  24 PLHRACRDGDLVALCSLLphTPRAHLAAEDSFYGWTPVHWAAHFG-KLECLMQLVRAGASLNVSTTRYaQTPAHIAA-FG 101
Cdd:PHA02876 276 PLHHASQAPSLSRLVPKL--LERGADVNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLY-ITPLHQAStLD 352

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 269784664 102 GHPQCLVWLIQAGANINKPDCEGETPIHKAARSGSLECITALVGSGA 148
Cdd:PHA02876 353 RNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGA 399
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 24-177 7.39e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 44.60  E-value: 7.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784664  24 PLHRACRDGDLVALCSLLPHTPRAHLAAEDSfygWTPVHWAAHFGKLECLMQLVRAGASLNVSTTRYAQTPAHIAAFGGH 103
Cdd:PHA02875  38 PIKLAMKFRDSEAIKLLMKHGAIPDVKYPDI---ESELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKK 114

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 269784664 104 PQCLVWLIQAGANINKPDCEGETPIHKAARSGSLECITALVGSGAHTDLRNASGLTAADIAQTQGFQECTQFLL 177
Cdd:PHA02875 115 LDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLL 188
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 53-184 1.05e-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: 44.69  E-value: 1.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784664   53 DSFY-GWTPVHWAAHFGKLECLMQLVRAGASLNVSTT-------------RYAQTPAHIAAFGGHPQCLVWLIQAGANIN 118
Cdd:TIGR00870 123 SEFTpGITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfYHGESPLNAAACLGSPSIVALLSEDPADIL 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784664  119 KPDCEGETPIHKAA---------RSGSLECITALVGSGAHTD-------LRNASGLTAADIAQTQGFQECTQFLLSLQNH 182
Cdd:TIGR00870 203 TADSLGNTLLHLLVmenefkaeyEELSCQMYNFALSLLDKLRdskelevILNHQGLTPLKLAAKEGRIVLFRLKLAIKYK 282


                  ..
gi 269784664  183 QM 184
Cdd:TIGR00870 283 QK 284
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 56-118 1.42e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 43.89  E-value: 1.42e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 269784664  56 YGWTPVHWAAHFGKLECLMQLVRAGASLNVsTTRYAQTPAHIAAFGGHPQCLVWLIQAGANIN 118
Cdd:PHA03100 191 YGFTPLHYAVYNNNPEFVKYLLDLGANPNL-VNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 110-178 1.44e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.12  E-value: 1.44e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 269784664 110 LIQAGANINKPDCEGETPIHKAARSGSLECITALVGSGAHTDLRNASGLTAADIAQTQGFQECTQFLLS 178
Cdd:PTZ00322 101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 56-85 2.82e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.95  E-value: 2.82e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 269784664    56 YGWTPVHWAAHFGKLECLMQLVRAGASLNV 85
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 22-133 3.63e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 42.56  E-value: 3.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784664  22 RFPLHRACRDGDLVALCSLLPHTprAHLAAEDSfYGWTPVHWAAHFGK-LECLMQLVRAGASLNVSTTRYAQTPAHIAAF 100
Cdd:PHA02878 202 NSPLHHAVKHYNKPIVHILLENG--ASTDARDK-CGNTPLHISVGYCKdYDILKLLLEHGVDVNAKSYILGLTALHSSIK 278

                         90       100       110
                 ....*....|....*....|....*....|...
gi 269784664 101 GghPQCLVWLIQAGANINKPDCEGETPIHKAAR 133
Cdd:PHA02878 279 S--ERKLKLLLEYGADINSLNSYKLTPLSSAVK 309
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 110-164 6.03e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 41.96  E-value: 6.03e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 269784664 110 LIQAGANINKPDCEGETPIHKAARSGSLECITALVGSGAHTDLRNASGLTAADIA 164
Cdd:PHA03100 178 LLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIA 232
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 76-145 1.72e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 40.65  E-value: 1.72e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784664  76 LVRAGASLNvSTTRYAQTPAHIAAFGGHPQCLVWLIQAGANINKPDCEGETPIHKAARSGSLECITALVG 145
Cdd:PTZ00322 101 LLTGGADPN-CRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 93-119 2.22e-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: 35.26  E-value: 2.22e-03
                           10        20
                   ....*....|....*....|....*..
gi 269784664    93 TPAHIAAFGGHPQCLVWLIQAGANINK 119
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 56-87 3.39e-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: 34.96  E-value: 3.39e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 269784664   56 YGWTPVHWAA-HFGKLECLMQLVRAGASLNVST 87
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 92-121 4.09e-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: 4.09e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 269784664   92 QTPAHIAA-FGGHPQCLVWLIQAGANINKPD 121
Cdd:pfam00023   3 NTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 59-133 4.98e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 38.81  E-value: 4.98e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 269784664  59 TPVHWAAHFGKLECLMQLVRAGASLNVSTTRYAQTPAHIAAFGGHPQCLVWLIQAGANINKPDCEGETPIHKAAR 133
Cdd:PHA02884  72 NPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKITPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPIELALM 146
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 25-182 5.13e-03

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: 39.23  E-value: 5.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784664  25 LHRACRDGDLVALCSLLPHTPR-AHLAAEDSFY-GWTPVHWAAHFGKLECLMQLVRAGASlnVSTTR------------- 89
Cdd:cd22192   55 LHVAALYDNLEAAVVLMEAAPElVNEPMTSDLYqGETALHIAVVNQNLNLVRELIARGAD--VVSPRatgtffrpgpknl 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269784664  90 --YAQTPAHIAAFGGHPQCLVWLIQAGANINKPDCEGETPIH----KAARSGSLECITALVGSGAHTD------LRNASG 157
Cdd:cd22192  133 iyYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHilvlQPNKTFACQMYDLILSYDKEDDlqpldlVPNNQG 212

                        170       180
                 ....*....|....*....|....*
gi 269784664 158 LTAADIAQTQGFQECTQFLLSLQNH 182
Cdd:cd22192  213 LTPFKLAAKEGNIVMFQHLVQKRRH 237
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 90-148 7.37e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 38.49  E-value: 7.37e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 269784664  90 YAQTPAHIAAFGGHPQCLVWLIQAGANINKPDCEGETPIHKAARSGSLECITALVGSGA 148
Cdd:PHA03100 191 YGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249
 
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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