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Conserved domains on  [gi|557878701|ref|NP_001273650|]
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ankyrin repeat domain-containing protein 10 isoform 2 [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];
25-152 2.90e-28

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 107.73  E-value: 2.90e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878701  25 PLHRACRDGDLATLCSLLQQtpHAHLASEDSfYGWTPVHWAAHFGKLECLVQLVRAGATLNVsTTRYAQTPAHIAAFGGH 104
Cdd:COG0666   90 LLHAAARNGDLEIVKLLLEA--GADVNARDK-DGETPLHLAAYNGNLEIVKLLLEAGADVNA-QDNDGNTPLHLAAANGN 165

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 557878701 105 PQCLVWLIQAGANINKPDCEGETPIHKAARSGSLECISALVANGAHVE 152
Cdd:COG0666  166 LEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVN 213
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
25-152 2.90e-28

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 107.73  E-value: 2.90e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878701  25 PLHRACRDGDLATLCSLLQQtpHAHLASEDSfYGWTPVHWAAHFGKLECLVQLVRAGATLNVsTTRYAQTPAHIAAFGGH 104
Cdd:COG0666   90 LLHAAARNGDLEIVKLLLEA--GADVNARDK-DGETPLHLAAYNGNLEIVKLLLEAGADVNA-QDNDGNTPLHLAAANGN 165

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 557878701 105 PQCLVWLIQAGANINKPDCEGETPIHKAARSGSLECISALVANGAHVE 152
Cdd:COG0666  166 LEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVN 213
Ank_2 pfam12796
Ankyrin repeats (3 copies);
63-151 7.89e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.46  E-value: 7.89e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878701   63 HWAAHFGKLECLVQLVRAGATLNVsTTRYAQTPAHIAAFGGHPQCLVWLIQaGANINKpDCEGETPIHKAARSGSLECIS 142
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENGADANL-QDKNGRTALHLAAKNGHLEIVKLLLE-HADVNL-KDNGRTALHYAARSGHLEIVK 78


                  ....*....
gi 557878701  143 ALVANGAHV 151
Cdd:pfam12796  79 LLLEKGADI 87
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 22-156 4.28e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 58.46  E-value: 4.28e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878701  22 LRFPLHRACRDGDLATLCSLLQQTPHAhlasEDSFY--GWTPVHWAAHFGKLECLVQLVRAGATLNVSTTRYAqTPAHIA 99
Cdd:PHA02875  68 IESELHDAVEEGDVKAVEELLDLGKFA----DDVFYkdGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKF-SPLHLA 142

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 557878701 100 AFGGHPQCLVWLIQAGANINKPDCEGETPIHKAARSGSLECISALVANGAHVEFISQ 156
Cdd:PHA02875 143 VMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGK 199
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 57-86 3.92e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.49  E-value: 3.92e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 557878701    57 YGWTPVHWAAHFGKLECLVQLVRAGATLNV 86
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 25-149 1.19e-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: 1.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878701  25 PLHRACRDGDLATLCSLLQQtPHAHLASEDSFyGWTPVHWAAHFGKLECLVQLVRAGATL-NVSTTR--YA-QTPAHIAA 100
Cdd:cd22192   20 PLLLAAKENDVQAIKKLLKC-PSCDLFQRGAL-GETALHVAALYDNLEAAVVLMEAAPELvNEPMTSdlYQgETALHIAV 97

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 557878701 101 FGGHPQCLVWLIQAGANINKP-----------DCE---GETPIHKAARSGSLECISALVANGA 149
Cdd:cd22192   98 VNQNLNLVRELIARGADVVSPratgtffrpgpKNLiyyGEHPLSFAACVGNEEIVRLLIEHGA 160
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 54-130 9.78e-03

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 36.60  E-value: 9.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878701   54 DSFY-GWTPVHWAAHFGKLECLVQLVRAGATLNVSTT-------------RYAQTPAHIAAFGGHPQCLVWLIQAGANIN 119
Cdd:TIGR00870 123 SEFTpGITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfYHGESPLNAAACLGSPSIVALLSEDPADIL 202

                          90
                  ....*....|.
gi 557878701  120 KPDCEGETPIH 130
Cdd:TIGR00870 203 TADSLGNTLLH 213
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
25-152 2.90e-28

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 107.73  E-value: 2.90e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878701  25 PLHRACRDGDLATLCSLLQQtpHAHLASEDSfYGWTPVHWAAHFGKLECLVQLVRAGATLNVsTTRYAQTPAHIAAFGGH 104
Cdd:COG0666   90 LLHAAARNGDLEIVKLLLEA--GADVNARDK-DGETPLHLAAYNGNLEIVKLLLEAGADVNA-QDNDGNTPLHLAAANGN 165

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 557878701 105 PQCLVWLIQAGANINKPDCEGETPIHKAARSGSLECISALVANGAHVE 152
Cdd:COG0666  166 LEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVN 213
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
25-151 7.74e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 96.18  E-value: 7.74e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878701  25 PLHRACRDGDLATLCSLLQQTPHAHLASEDsfyGWTPVHWAAHFGKLECLVQLVRAGATLNVsTTRYAQTPAHIAAFGGH 104
Cdd:COG0666   57 LLLAAALAGDLLVALLLLAAGADINAKDDG---GNTLLHAAARNGDLEIVKLLLEAGADVNA-RDKDGETPLHLAAYNGN 132

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 557878701 105 PQCLVWLIQAGANINKPDCEGETPIHKAARSGSLECISALVANGAHV 151
Cdd:COG0666  133 LEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADV 179
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
25-149 1.19e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 93.09  E-value: 1.19e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878701  25 PLHRACRDGDLATLCSLLQQtpHAHLASEDSfYGWTPVHWAAHFGKLECLVQLVRAGATLNVsTTRYAQTPAHIAAFGGH 104
Cdd:COG0666  123 PLHLAAYNGNLEIVKLLLEA--GADVNAQDN-DGNTPLHLAAANGNLEIVKLLLEAGADVNA-RDNDGETPLHLAAENGH 198

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 557878701 105 PQCLVWLIQAGANINKPDCEGETPIHKAARSGSLECISALVANGA 149
Cdd:COG0666  199 LEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243
Ank_2 pfam12796
Ankyrin repeats (3 copies);
63-151 7.89e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.46  E-value: 7.89e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878701   63 HWAAHFGKLECLVQLVRAGATLNVsTTRYAQTPAHIAAFGGHPQCLVWLIQaGANINKpDCEGETPIHKAARSGSLECIS 142
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENGADANL-QDKNGRTALHLAAKNGHLEIVKLLLE-HADVNL-KDNGRTALHYAARSGHLEIVK 78


                  ....*....
gi 557878701  143 ALVANGAHV 151
Cdd:pfam12796  79 LLLEKGADI 87
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
25-154 3.13e-16

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 75.38  E-value: 3.13e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878701  25 PLHRACRDGDLATLCSLLQQtpHAHLASEDSfYGWTPVHWAAHFGKLECLVQLVRAGATLNVsTTRYAQTPAHIAAFGGH 104
Cdd:COG0666  156 PLHLAAANGNLEIVKLLLEA--GADVNARDN-DGETPLHLAAENGHLEIVKLLLEAGADVNA-KDNDGKTALDLAAENGN 231

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 557878701 105 PQCLVWLIQAGANINKPDCEGETPIHKAARSGSLECISALVANGAHVEFI 154
Cdd:COG0666  232 LEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAA 281
Ank_2 pfam12796
Ankyrin repeats (3 copies);
26-122 3.43e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 68.22  E-value: 3.43e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878701   26 LHRACRDGDLATLCSLLQQTPHAHLASEDsfyGWTPVHWAAHFGKLECLVQLVragATLNVSTTRYAQTPAHIAAFGGHP 105
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKN---GRTALHLAAKNGHLEIVKLLL---EHADVNLKDNGRTALHYAARSGHL 74

                          90
                  ....*....|....*..
gi 557878701  106 QCLVWLIQAGANINKPD 122
Cdd:pfam12796  75 EIVKLLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
19-152 8.34e-15

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 71.52  E-value: 8.34e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878701  19 LLSLRFPLHRACRDGDLATLCSLLQQTPHAHLASEDSfygwTPVHWAAHFGKLECLVQLVRAGATLNVSTTRYAQTPAHI 98
Cdd:COG0666   18 LLLLALLLLAAALLLLLLLLLLLLLALLALALADALG----ALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHA 93

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 557878701  99 AAFGGHPQCLVWLIQAGANINKPDCEGETPIHKAARSGSLECISALVANGAHVE 152
Cdd:COG0666   94 AARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVN 147
Ank_4 pfam13637
Ankyrin repeats (many copies);
94-145 3.87e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 56.51  E-value: 3.87e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 557878701   94 TPAHIAAFGGHPQCLVWLIQAGANINKPDCEGETPIHKAARSGSLECISALV 145
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 22-156 4.28e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 58.46  E-value: 4.28e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878701  22 LRFPLHRACRDGDLATLCSLLQQTPHAhlasEDSFY--GWTPVHWAAHFGKLECLVQLVRAGATLNVSTTRYAqTPAHIA 99
Cdd:PHA02875  68 IESELHDAVEEGDVKAVEELLDLGKFA----DDVFYkdGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKF-SPLHLA 142

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 557878701 100 AFGGHPQCLVWLIQAGANINKPDCEGETPIHKAARSGSLECISALVANGAHVEFISQ 156
Cdd:PHA02875 143 VMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGK 199
Ank_4 pfam13637
Ankyrin repeats (many copies);
58-112 5.64e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.04  E-value: 5.64e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 557878701   58 GWTPVHWAAHFGKLECLVQLVRAGATLNVsTTRYAQTPAHIAAFGGHPQCLVWLI 112
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINA-VDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 25-165 9.56e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 51.99  E-value: 9.56e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878701  25 PLHRACRDGDLATLC-SLLQQTPHAhlaSEDSFYGWTPVHWAAHFG-KLECLVQLVRAGATLNVSTTRYaQTPAHIAA-F 101
Cdd:PHA02876 276 PLHHASQAPSLSRLVpKLLERGADV---NAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLY-ITPLHQAStL 351

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 557878701 102 GGHPQCLVWLIQAGANINKPDCEGETPIHKAARSGSLECISALVANGAHVEFISQ---SSVHSCLPG 165
Cdd:PHA02876 352 DRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQkigTALHFALCG 418
PHA03095 PHA03095
ankyrin-like protein; Provisional
 57-176 2.96e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 50.02  E-value: 2.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878701  57 YGWTPVHWAAHFGKLECLVQ-LVRAGATLNVSTtRYAQTPAHI--AAFGGHPQCLVWLIQAGANINKPDCEGETPIHKAA 133
Cdd:PHA03095  82 CGFTPLHLYLYNATTLDVIKlLIKAGADVNAKD-KVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLL 160

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 557878701 134 RSG--SLECISALVANGAH---VEFISQSSVHsclpgelQHGVTFDPS 176
Cdd:PHA03095 161 KSRnaNVELLRLLIDAGADvyaVDDRFRSLLH-------HHLQSFKPR 201
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 60-151 3.00e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 49.96  E-value: 3.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878701  60 TPVHWAAHFGKLECLVQLVRAGATLNVSTTRyAQTPAHIAAFGGHPQCLVWLIQAGANINKPDCEGETPIHKAARSGSLE 139
Cdd:PHA02874 126 TFLHYAIKKGDLESIKMLFEYGADVNIEDDN-GCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYA 204

                         90
                 ....*....|..
gi 557878701 140 CISALVANGAHV 151
Cdd:PHA02874 205 CIKLLIDHGNHI 216
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 26-132 3.61e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 49.96  E-value: 3.61e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878701  26 LHRACRDGDLATLCSLLQQTPHAHLASEDSFYgwtPVHWAAHFGKLECLVQLVRAGATLNVSTTrYAQTPAHIAAFGGHP 105
Cdd:PHA02874 128 LHYAIKKGDLESIKMLFEYGADVNIEDDNGCY---PIHIAIKHNFFDIIKLLLEKGAYANVKDN-NGESPLHNAAEYGDY 203

                         90       100
                 ....*....|....*....|....*..
gi 557878701 106 QCLVWLIQAGANINKPDCEGETPIHKA 132
Cdd:PHA02874 204 ACIKLLIDHGNHIMNKCKNGFTPLHNA 230
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 25-171 4.18e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 50.06  E-value: 4.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878701  25 PLHRACR-DGDLATLCSLLQQTphAHLASEDsFYGWTPVHWAAHFGKLECLVQLVRAGATLNVSTTRYAqTPAHIAAFGG 103
Cdd:PHA02876 344 PLHQASTlDRNKDIVITLLELG--ANVNARD-YCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIG-TALHFALCGT 419

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878701 104 HPQCLV-WLIQAGANINKPDCEGETPIHKAARSG-SLECISALVANGAHVEFISQSSVHSCLPGELQHGV 171
Cdd:PHA02876 420 NPYMSVkTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIALEYHGI 489
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 24-151 7.86e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 48.81  E-value: 7.86e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878701  24 FPLHRACRDGDLATLCSLLQQTPHAHLaseDSFYGWTPVHWAAHFGKLECLVQLVRAGATLNVSTTRyAQTPAHIAAFgg 103
Cdd:PHA02874 159 YPIHIAIKHNFFDIIKLLLEKGAYANV---KDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKN-GFTPLHNAII-- 232

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 557878701 104 HPQCLVWLIQAGANINKPDCEGETPIHKAAR-SGSLECISALVANGAHV 151
Cdd:PHA02874 233 HNRSAIELLINNASINDQDIDGSTPLHHAINpPCDIDIIDILLYHKADI 281
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 26-149 2.24e-06

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 46.02  E-value: 2.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878701  26 LHRACRDGDLATLCSLLQQTPHA--HLASEDSFYGWTPVHWAAHFGKL---ECLVQLVRAGATLNVSTTRYAQTPAHIAA 100
Cdd:PHA02736  21 LHYLCRNGGVTDLLAFKNAISDEnrYLVLEYNRHGKQCVHIVSNPDKAdpqEKLKLLMEWGADINGKERVFGNTPLHIAV 100

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 557878701 101 FGGHPQCLVWLI-QAGANINKPDCEGETPIHKAARSGSLECISALVANGA 149
Cdd:PHA02736 101 YTQNYELATWLCnQPGVNMEILNYAFKTPYYVACERHDAKMMNILRAKGA 150
Ank_5 pfam13857
Ankyrin repeats (many copies);
77-132 8.27e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 8.27e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 557878701   77 LVRAGATLNVSTTRYAQTPAHIAAFGGHPQCLVWLIQAGANINKPDCEGETPIHKA 132
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA03095 PHA03095
ankyrin-like protein; Provisional
 58-129 1.23e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 45.40  E-value: 1.23e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 557878701  58 GWTPVHWAAHFGKLECLV--QLVRAGATLNvSTTRYAQTPAHIAAFGGHPQCLVWLIQAGANINKPDCEGETPI 129
Cdd:PHA03095 222 GNTPLHSMATGSSCKRSLvlPLLIAGISIN-ARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPL 294
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 23-154 1.28e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 45.26  E-value: 1.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878701  23 RFPLHRACRDGDLATLCSLLQQTphahlASED--SFYGWTPVHWAAHFGK-LECLVQLVRAGATLNVSTTRYAQTPAHIA 99
Cdd:PHA02878 202 NSPLHHAVKHYNKPIVHILLENG-----ASTDarDKCGNTPLHISVGYCKdYDILKLLLEHGVDVNAKSYILGLTALHSS 276

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 557878701 100 AFGghPQCLVWLIQAGANINKPDCEGETPIHKAARSGS-LECISALVANGAHVEFI 154
Cdd:PHA02878 277 IKS--ERKLKLLLEYGADINSLNSYKLTPLSSAVKQYLcINIGRILISNICLLKRI 330
PHA03095 PHA03095
ankyrin-like protein; Provisional
 57-152 1.73e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 45.02  E-value: 1.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878701  57 YGWTPVHWAAHFGKLECL--VQ-LVRAGATLNVsTTRYAQTPAHI-AAFGGHPQCLVWLIQAGANINKPDCEGETPIHKA 132
Cdd:PHA03095  46 YGKTPLHLYLHYSSEKVKdiVRlLLEAGADVNA-PERCGFTPLHLyLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVY 124

                         90       100
                 ....*....|....*....|..
gi 557878701 133 ARSGSL--ECISALVANGAHVE 152
Cdd:PHA03095 125 LSGFNInpKVIRLLLRKGADVN 146
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 57-86 3.92e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.49  E-value: 3.92e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 557878701    57 YGWTPVHWAAHFGKLECLVQLVRAGATLNV 86
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 77-184 5.79e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 43.33  E-value: 5.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878701  77 LVRAGATLNVSTTRYAQTPAHIAAFGGHPQCLVWLIQAGANINKPDCEGETPIHKAARSGSLECISALVANGAHVEFISQ 156
Cdd:PHA02878 153 LLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDK 232

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 557878701 157 S-------SVHSCLPGE-----LQHGVTFDPSVLIQCLKP 184
Cdd:PHA02878 233 CgntplhiSVGYCKDYDilkllLEHGVDVNAKSYILGLTA 272
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
25-129 6.54e-05

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 43.02  E-value: 6.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878701  25 PLHRACRDGDLATLCSLLQQTPHAHLASEDsfyGWTPVHWAAHFGKLECLVQLVRAGATLNVStTRYAQTPAHIAAFGGH 104
Cdd:COG0666  189 PLHLAAENGHLEIVKLLLEAGADVNAKDND---GKTALDLAAENGNLEIVKLLLEAGADLNAK-DKDGLTALLLAAAAGA 264

                         90       100
                 ....*....|....*....|....*
gi 557878701 105 PQCLVWLIQAGANINKPDCEGETPI 129
Cdd:COG0666  265 ALIVKLLLLALLLLAAALLDLLTLL 289
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 91-154 7.52e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 42.73  E-value: 7.52e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 557878701  91 YAQTPAHIAAFGGHPQCLVWLIQAGANINKPDCEGETPIHKAARSGSLECISALVANGAHVEFI 154
Cdd:PHA03100 191 YGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTI 254
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 25-149 1.19e-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: 1.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878701  25 PLHRACRDGDLATLCSLLQQtPHAHLASEDSFyGWTPVHWAAHFGKLECLVQLVRAGATL-NVSTTR--YA-QTPAHIAA 100
Cdd:cd22192   20 PLLLAAKENDVQAIKKLLKC-PSCDLFQRGAL-GETALHVAALYDNLEAAVVLMEAAPELvNEPMTSdlYQgETALHIAV 97

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 557878701 101 FGGHPQCLVWLIQAGANINKP-----------DCE---GETPIHKAARSGSLECISALVANGA 149
Cdd:cd22192   98 VNQNLNLVRELIARGADVVSPratgtffrpgpKNLiyyGEHPLSFAACVGNEEIVRLLIEHGA 160
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 65-136 1.57e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 42.16  E-value: 1.57e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 557878701  65 AAHFGKLECLVQLVRAGATLNVSTTRyAQTPAHIAAFGGHPQCLVWLIQAGANINKPDCEGETPIHKAARSG 136
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPDIGDSK-GRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAK 602
Ank_4 pfam13637
Ankyrin repeats (many copies);
25-74 1.88e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.02  E-value: 1.88e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 557878701   25 PLHRACRDGDLATLCSLLQQTPHAHLASEDsfyGWTPVHWAAHFGKLECL 74
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKGADINAVDGN---GETALHFAASNGNVEVL 50
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 94-120 4.95e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.41  E-value: 4.95e-04
                           10        20
                   ....*....|....*....|....*..
gi 557878701    94 TPAHIAAFGGHPQCLVWLIQAGANINK 120
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 77-144 6.52e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 40.27  E-value: 6.52e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 557878701  77 LVRAGATLNvSTTRYAQTPAHIAAFGGHPQCLVWLIQAGANINKPDCEGETPIHKAARSGSLECISAL 144
Cdd:PTZ00322 101 LLTGGADPN-CRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 57-119 7.15e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 40.03  E-value: 7.15e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 557878701  57 YGWTPVHWAAHFGKLECLVQLVRAGATLNVsTTRYAQTPAHIAAFGGHPQCLVWLIQAGANIN 119
Cdd:PHA03100 191 YGFTPLHYAVYNNNPEFVKYLLDLGANPNL-VNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 93-122 7.17e-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: 36.11  E-value: 7.17e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 557878701   93 QTPAHIAA-FGGHPQCLVWLIQAGANINKPD 122
Cdd:pfam00023   3 NTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 77-151 1.04e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 39.56  E-value: 1.04e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 557878701  77 LVRAGATLNVSTtRYAQTPAHIAAFGGHPQCLVWLIQAGANINKPDCEGETPIHKAARSGSLECISALVANGAHV 151
Cdd:PHA02874 110 ILDCGIDVNIKD-AELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYA 183
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 124-151 1.28e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 35.31  E-value: 1.28e-03
                          10        20
                  ....*....|....*....|....*...
gi 557878701  124 EGETPIHKAARSGSLECISALVANGAHV 151
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADI 28
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 77-151 1.95e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 38.49  E-value: 1.95e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 557878701  77 LVRAGATLNVsTTRYAQTPAHIAAFG--GHPQCLVWLIQAGANINKPDCEGETPIHKAARSGS--LECISALVANGAHV 151
Cdd:PHA03100  92 LLEYGANVNA-PDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDI 169
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 124-149 2.16e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.49  E-value: 2.16e-03
                           10        20
                   ....*....|....*....|....*.
gi 557878701   124 EGETPIHKAARSGSLECISALVANGA 149
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGA 26
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 57-88 2.36e-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: 2.36e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 557878701   57 YGWTPVHWAA-HFGKLECLVQLVRAGATLNVST 88
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 49-134 2.82e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 38.04  E-value: 2.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878701  49 HLASEDSFYgwTPVHWAAHFGKLECLVQLVRAGATLNVSTTRYAQTPAHIAAFGGHPQCLVWLIQAGANINKPDCEGETP 128
Cdd:PHA02884  63 FPLSENSKT--NPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKITPLYISVLHGCLKCLEILLSYGADINIQTNDMVTP 140


                 ....*.
gi 557878701 129 IHKAAR 134
Cdd:PHA02884 141 IELALM 146
Ank_5 pfam13857
Ankyrin repeats (many copies);
111-151 4.04e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 34.63  E-value: 4.04e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 557878701  111 LIQAG-ANINKPDCEGETPIHKAARSGSLECISALVANGAHV 151
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDL 42
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 111-155 5.07e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 37.35  E-value: 5.07e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 557878701 111 LIQAGANINKPDCEGETPIHKAARSGSLECISALVANGAHVEFIS 155
Cdd:PHA02876 164 LLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIA 208
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 57-86 6.37e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 33.38  E-value: 6.37e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 557878701   57 YGWTPVHWAAHFGKLECLVQLVRAGATLNV 86
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 60-151 8.33e-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: 36.91  E-value: 8.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878701  60 TPVHWAAHFGKLECLVQLVRAGATLNVSTTRYAQTPAHIAAFGGHPQCLVWLIQAGAN-INKPDC----EGETPIHKAAR 134
Cdd:cd22192   19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNEPMTsdlyQGETALHIAVV 98

                         90
                 ....*....|....*..
gi 557878701 135 SGSLECISALVANGAHV 151
Cdd:cd22192   99 NQNLNLVRELIARGADV 115
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 54-130 9.78e-03

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 36.60  E-value: 9.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557878701   54 DSFY-GWTPVHWAAHFGKLECLVQLVRAGATLNVSTT-------------RYAQTPAHIAAFGGHPQCLVWLIQAGANIN 119
Cdd:TIGR00870 123 SEFTpGITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfYHGESPLNAAACLGSPSIVALLSEDPADIL 202

                          90
                  ....*....|.
gi 557878701  120 KPDCEGETPIH 130
Cdd:TIGR00870 203 TADSLGNTLLH 213
 
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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