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Conserved domains on  [gi|442629182|ref|NP_001261204|]
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Ada2a-containing complex component 3, isoform E [Drosophila melanogaster]

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];
58-251 1.97e-33

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 129.30  E-value: 1.97e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629182  58 LLQCARDSDVAGVKAALAHGA-PFASDWLGMSALHFAAMNNQLEICEILLQGGINMDGKTKVDRTPLHLACYYGHERIVS 136
Cdd:COG0666   91 LHAAARNGDLEIVKLLLEAGAdVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629182 137 LLLALKCSVNSRDMLRMTPLHWAVEKKHKGIVRLLLKCQADVTLVSKFGKTPIGLAVYTEQADVLAELEAArQAQASKKL 216
Cdd:COG0666  171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA-GADLNAKD 249
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 442629182 217 HEESEQQAHKTKKETNEAVSSIMDEPEVIKTVDDK 251
Cdd:COG0666  250 KDGLTALLLAAAAGAALIVKLLLLALLLLAAALLD 284
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
58-251 1.97e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 129.30  E-value: 1.97e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629182  58 LLQCARDSDVAGVKAALAHGA-PFASDWLGMSALHFAAMNNQLEICEILLQGGINMDGKTKVDRTPLHLACYYGHERIVS 136
Cdd:COG0666   91 LHAAARNGDLEIVKLLLEAGAdVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629182 137 LLLALKCSVNSRDMLRMTPLHWAVEKKHKGIVRLLLKCQADVTLVSKFGKTPIGLAVYTEQADVLAELEAArQAQASKKL 216
Cdd:COG0666  171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA-GADLNAKD 249
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 442629182 217 HEESEQQAHKTKKETNEAVSSIMDEPEVIKTVDDK 251
Cdd:COG0666  250 KDGLTALLLAAAAGAALIVKLLLLALLLLAAALLD 284
Ank_2 pfam12796
Ankyrin repeats (3 copies);
90-180 9.07e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.49  E-value: 9.07e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629182   90 LHFAAMNNQLEICEILLQGGINMDGKTKVDRTPLHLACYYGHERIVSLLLAlKCSVNSRDMlRMTPLHWAVEKKHKGIVR 169
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIVK 78
                          90
                  ....*....|.
gi 442629182  170 LLLKCQADVTL 180
Cdd:pfam12796  79 LLLEKGADINV 89
PHA03100 PHA03100
ankyrin repeat protein; Provisional
70-204 2.84e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 81.25  E-value: 2.84e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629182  70 VKAALAHGAPF-ASDWLGMSALHFAAMN--NQLEICEILLQGGINMDGKTKVDRTPLHLACYYGHERI------------ 134
Cdd:PHA03100  89 VKLLLEYGANVnAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLkilkllidkgvd 168
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442629182 135 ------VSLLLALKCSVNSRDMLRMTPLHWAVEKKHKGIVRLLLKCQADVTLVSKFGKTPIGLAVYTEQADVLAEL 204
Cdd:PHA03100 169 inaknrVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLL 244
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
58-189 3.02e-08

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: 56.56  E-value: 3.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629182  58 LLQCARDSDVAGVKAAL--AHGAPFASDWLGMSALHFAAMNNQLEICEILLQGG---IN--MDGKTKVDRTPLHLACYYG 130
Cdd:cd22192   21 LLLAAKENDVQAIKKLLkcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAApelVNepMTSDLYQGETALHIAVVNQ 100
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442629182 131 HERIVSLLLALKCSVNSRdmlRMT-----------------PLHWAVEKKHKGIVRLLLKCQADVTLVSKFGKTPI 189
Cdd:cd22192  101 NLNLVRELIARGADVVSP---RATgtffrpgpknliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
35-161 3.73e-05

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: 46.61  E-value: 3.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629182   35 EGDVQQKKGILVGPATCVDLGKQLLQCARDSDVAGVKAALAHGAPFASD----WL-----------GMSALHFAAMNNQL 99
Cdd:TIGR00870  62 ENENLELTELLLNLSCRGAVGDTLLHAISLEYVDAVEAILLHLLAAFRKsgplELandqytseftpGITALHLAAHRQNY 141
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442629182  100 EICEILLQGGINMDGKTKVD--------------RTPLHLACYYGHERIVSLLLALKCSVNSRDMLRMTPLHWAVE 161
Cdd:TIGR00870 142 EIVKLLLERGASVPARACGDffvksqgvdsfyhgESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVM 217
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
153-180 3.82e-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: 3.82e-04
                           10        20
                   ....*....|....*....|....*...
gi 442629182   153 MTPLHWAVEKKHKGIVRLLLKCQADVTL 180
Cdd:smart00248   3 RTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
58-251 1.97e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 129.30  E-value: 1.97e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629182  58 LLQCARDSDVAGVKAALAHGA-PFASDWLGMSALHFAAMNNQLEICEILLQGGINMDGKTKVDRTPLHLACYYGHERIVS 136
Cdd:COG0666   91 LHAAARNGDLEIVKLLLEAGAdVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629182 137 LLLALKCSVNSRDMLRMTPLHWAVEKKHKGIVRLLLKCQADVTLVSKFGKTPIGLAVYTEQADVLAELEAArQAQASKKL 216
Cdd:COG0666  171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA-GADLNAKD 249
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 442629182 217 HEESEQQAHKTKKETNEAVSSIMDEPEVIKTVDDK 251
Cdd:COG0666  250 KDGLTALLLAAAAGAALIVKLLLLALLLLAAALLD 284
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
58-207 1.57e-27

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 112.35  E-value: 1.57e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629182  58 LLQCARDSDVAGVKAALAHGAP-FASDWLGMSALHFAAMNNQLEICEILLQGGINMDGKTKVDRTPLHLACYYGHERIVS 136
Cdd:COG0666   58 LLAAALAGDLLVALLLLAAGADiNAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVK 137
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442629182 137 LLLALKCSVNSRDMLRMTPLHWAVEKKHKGIVRLLLKCQADVTLVSKFGKTPIGLAVYTEQADVLAELEAA 207
Cdd:COG0666  138 LLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA 208
Ank_2 pfam12796
Ankyrin repeats (3 copies);
90-180 9.07e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.49  E-value: 9.07e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629182   90 LHFAAMNNQLEICEILLQGGINMDGKTKVDRTPLHLACYYGHERIVSLLLAlKCSVNSRDMlRMTPLHWAVEKKHKGIVR 169
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIVK 78
                          90
                  ....*....|.
gi 442629182  170 LLLKCQADVTL 180
Cdd:pfam12796  79 LLLEKGADINV 89
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
58-204 3.09e-19

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 88.47  E-value: 3.09e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629182  58 LLQCARDSDVAGVKAALAHGAPFASDWLGMSALHFAAMNNQLEICEILLQGGINMDGKTKVDRTPLHLACYYGHERIVSL 137
Cdd:COG0666   26 LAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKL 105
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442629182 138 LLALKCSVNSRDMLRMTPLHWAVEKKHKGIVRLLLKCQADVTLVSKFGKTPIGLAVYTEQADVLAEL 204
Cdd:COG0666  106 LLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLL 172
PHA03100 PHA03100
ankyrin repeat protein; Provisional
70-204 2.84e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 81.25  E-value: 2.84e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629182  70 VKAALAHGAPF-ASDWLGMSALHFAAMN--NQLEICEILLQGGINMDGKTKVDRTPLHLACYYGHERI------------ 134
Cdd:PHA03100  89 VKLLLEYGANVnAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLkilkllidkgvd 168
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442629182 135 ------VSLLLALKCSVNSRDMLRMTPLHWAVEKKHKGIVRLLLKCQADVTLVSKFGKTPIGLAVYTEQADVLAEL 204
Cdd:PHA03100 169 inaknrVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLL 244
Ank_2 pfam12796
Ankyrin repeats (3 copies);
58-149 1.47e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.07  E-value: 1.47e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629182   58 LLQCARDSDVAGVKAALAHGA-PFASDWLGMSALHFAAMNNQLEICEILLQggiNMDGKTKVD-RTPLHLACYYGHERIV 135
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGAdANLQDKNGRTALHLAAKNGHLEIVKLLLE---HADVNLKDNgRTALHYAARSGHLEIV 77
                          90
                  ....*....|....
gi 442629182  136 SLLLALKCSVNSRD 149
Cdd:pfam12796  78 KLLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
71-207 7.56e-12

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 66.52  E-value: 7.56e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629182  71 KAALAHGAPFASDWLGMSALHFAAMNNQLEICEILLQGGINMDGKTKVDRTPLHLACYYGHERIVSLLLALKCSVNSRDM 150
Cdd:COG0666    6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 442629182 151 LRMTPLHWAVEKKHKGIVRLLLKCQADVTLVSKFGKTPIGLAVYTEQADVLAELEAA 207
Cdd:COG0666   86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA 142
PHA03095 PHA03095
ankyrin-like protein; Provisional
53-204 5.24e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 65.05  E-value: 5.24e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629182  53 DLGKQLLQCArDSDVAGVKAALAHGAPFA-SDWLGMSALHfAAMNNQL----EICEILLQGGINMDGKTKVDRTPLHLAC 127
Cdd:PHA03095  14 ALYDYLLNAS-NVTVEEVRRLLAAGADVNfRGEYGKTPLH-LYLHYSSekvkDIVRLLLEAGADVNAPERCGFTPLHLYL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629182 128 YYGH-ERIVSLLLALKCSVNSRDMLRMTPLH--WAVEKKHKGIVRLLLKCQADVTLVSKFGKTPigLAVYTEQADVLAEL 204
Cdd:PHA03095  92 YNATtLDVIKLLIKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTP--LAVLLKSRNANVEL 169
PHA02878 PHA02878
ankyrin repeat protein; Provisional
70-197 2.84e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 62.59  E-value: 2.84e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629182  70 VKAALAHGAP--FASDWLGMSALHFAAMNNQLEICEILLQGGINMDGKTKVDRTPLHLACYYGHERIVSLLLALKCSVNS 147
Cdd:PHA02878 150 TKLLLSYGADinMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDA 229
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 442629182 148 RDMLRMTPLHWAVEK-KHKGIVRLLLKCQADVTLVSKF-GKTPIGLAVYTEQ 197
Cdd:PHA02878 230 RDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYIlGLTALHSSIKSER 281
Ank_4 pfam13637
Ankyrin repeats (many copies);
86-139 3.53e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.74  E-value: 3.53e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 442629182   86 GMSALHFAAMNNQLEICEILLQGGINMDGKTKVDRTPLHLACYYGHERIVSLLL 139
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
32-188 5.79e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 61.58  E-value: 5.79e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629182  32 IRTEGDVQQKKGILVGPATcvdlgkQLLQCARDSDVAGVKAALAHGAPF-ASDWLGMSALHFAAMNNQ-LEICEILLQGG 109
Cdd:PHA03095  34 LAAGADVNFRGEYGKTPLH------LYLHYSSEKVKDIVRLLLEAGADVnAPERCGFTPLHLYLYNATtLDVIKLLIKAG 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629182 110 INMDGKTKVDRTPLHlACYYG---HERIVSLLLALKCSVNSRDMLRMTPLHWAVEKKHK--GIVRLLLKCQADVTLVSKF 184
Cdd:PHA03095 108 ADVNAKDKVGRTPLH-VYLSGfniNPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNAnvELLRLLIDAGADVYAVDDR 186

                 ....
gi 442629182 185 GKTP 188
Cdd:PHA03095 187 FRSL 190
PHA03095 PHA03095
ankyrin-like protein; Provisional
63-193 1.29e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 60.81  E-value: 1.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629182  63 RDSDVAGVKAALAHGA-PFASDWLGMSALHFAAMN--NQLEICEILLQGGINMDGKTKVDRTPLHLACYYGHER--IVSL 137
Cdd:PHA03095 163 RNANVELLRLLIDAGAdVYAVDDRFRSLLHHHLQSfkPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLP 242
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 442629182 138 LLALKCSVNSRDMLRMTPLHWAVEKKHKGIVRLLLKCQADVTLVSKFGKTPIGLAV 193
Cdd:PHA03095 243 LLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMV 298
PHA03100 PHA03100
ankyrin repeat protein; Provisional
82-193 1.67e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 60.06  E-value: 1.67e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629182  82 SDWLGMSALHFAAMNNQLEICEILLQGGINMDGKTKVDRTPLHLACYYGH-----ERIVSLLLALKCSVNSRDMLRMTPL 156
Cdd:PHA03100  31 SYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVNAPDNNGITPL 110
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 442629182 157 HWAVEKK--HKGIVRLLLKCQADVTLVSKFGKTPIGLAV 193
Cdd:PHA03100 111 LYAISKKsnSYSIVEYLLDNGANVNIKNSDGENLLHLYL 149
PHA02875 PHA02875
ankyrin repeat protein; Provisional
53-185 1.06e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 57.69  E-value: 1.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629182  53 DLGKQLLQCARDSDVAGVKAALAHGApFASDWL---GMSALHFAAMNNQLEICEILLQGGINMDGKTKVDRTPLHLACYY 129
Cdd:PHA02875  67 DIESELHDAVEEGDVKAVEELLDLGK-FADDVFykdGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMM 145
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 442629182 130 GHERIVSLLLALKCSVNSRDMLRMTPLHWAVEKKHKGIVRLLLKCQADVTLVSKFG 185
Cdd:PHA02875 146 GDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNG 201
Ank_4 pfam13637
Ankyrin repeats (many copies);
120-172 1.25e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.12  E-value: 1.25e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 442629182  120 RTPLHLACYYGHERIVSLLLALKCSVNSRDMLRMTPLHWAVEKKHKGIVRLLL 172
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
88-195 1.48e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 57.20  E-value: 1.48e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629182  88 SALHFAAMNNQLEICEILLQGGINMDGKTKVDRTPLHLACYYGHE-RIVSLLLALKCSVNSRDMLR-MTPLHWAVEKKHK 165
Cdd:PHA02878 203 SPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDyDILKLLLEHGVDVNAKSYILgLTALHSSIKSERK 282
                         90       100       110
                 ....*....|....*....|....*....|
gi 442629182 166 giVRLLLKCQADVTLVSKFGKTPIGLAVYT 195
Cdd:PHA02878 283 --LKLLLEYGADINSLNSYKLTPLSSAVKQ 310
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
58-189 3.02e-08

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: 56.56  E-value: 3.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629182  58 LLQCARDSDVAGVKAAL--AHGAPFASDWLGMSALHFAAMNNQLEICEILLQGG---IN--MDGKTKVDRTPLHLACYYG 130
Cdd:cd22192   21 LLLAAKENDVQAIKKLLkcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAApelVNepMTSDLYQGETALHIAVVNQ 100
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442629182 131 HERIVSLLLALKCSVNSRdmlRMT-----------------PLHWAVEKKHKGIVRLLLKCQADVTLVSKFGKTPI 189
Cdd:cd22192  101 NLNLVRELIARGADVVSP---RATgtffrpgpknliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
PHA02874 PHA02874
ankyrin repeat protein; Provisional
70-206 1.49e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 54.20  E-value: 1.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629182  70 VKAALAHGAPF-ASDWLGMSALHFAAMNNQLEICEILLQGGINMDGKTKVDRTPLHLACYygHERIVSLLLALKCSVNSR 148
Cdd:PHA02874 173 IKLLLEKGAYAnVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLINNASINDQ 250
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629182 149 DMLRMTPLHWAVEKK-HKGIVRLLLKCQADVTLVSKFGKTPIGLAV-YTEQADVLAELEA 206
Cdd:PHA02874 251 DIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTAFkYINKDPVIKDIIA 310
PHA02876 PHA02876
ankyrin repeat protein; Provisional
97-178 7.19e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 52.37  E-value: 7.19e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629182  97 NQLEICEILLQGGINMDGKTKVDRTPLHLACYYGHERIVSLLLALKCSVNSRDMLRMTPLHWAVEKKHKGIVRLLLKCQA 176
Cdd:PHA02876 156 DELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRS 235

                 ..
gi 442629182 177 DV 178
Cdd:PHA02876 236 NI 237
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
104-174 1.23e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.44  E-value: 1.23e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442629182 104 ILLQGGINMDGKTKVDRTPLHLACYYGHERIVSLLLALKCSVNSRDMLRMTPLHWAVEKKHKGIVRLLLKC 174
Cdd:PTZ00322 100 ILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
135-204 1.43e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.05  E-value: 1.43e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629182 135 VSLLLALKCSVNSRDMLRMTPLHWAVEKKHKGIVRLLLKCQADVTLVSKFGKTPIGLAVYTEQADVLAEL 204
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
Ank_5 pfam13857
Ankyrin repeats (many copies);
137-192 2.29e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.03  E-value: 2.29e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 442629182  137 LLLALKCSVNSRDMLRMTPLHWAVEKKHKGIVRLLLKCQADVTLVSKFGKTPIGLA 192
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
90-263 3.06e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 50.25  E-value: 3.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629182  90 LHFAAMNNQlEICEILLQGGINMDGKTKVDRTPLHLACYYGHERIVSLLLALKCSVNSRDMLRMTPLHWAVEKKHKGIVR 169
Cdd:PLN03192 530 LTVASTGNA-ALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFR 608
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629182 170 LLLKCQADVTlvSKFGKTPIGLAVYTEQADVLAELEAARQAQASKKLHEESEQQAHKTKKETNEAVSSIMDEPEVIKTVD 249
Cdd:PLN03192 609 ILYHFASISD--PHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANT 686
                        170
                 ....*....|....
gi 442629182 250 DKEMSVEERMDVLE 263
Cdd:PLN03192 687 DDDFSPTELRELLQ 700
PHA02875 PHA02875
ankyrin repeat protein; Provisional
66-193 6.09e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 48.83  E-value: 6.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629182  66 DVAGVKAALAHGAPFASDWLGM-SALHFAAMNNQLEICEILLQGGINMDGKT-KVDRTPLHLACYYGHERIVSLLLALKC 143
Cdd:PHA02875  47 DSEAIKLLMKHGAIPDVKYPDIeSELHDAVEEGDVKAVEELLDLGKFADDVFyKDGMTPLHLATILKKLDIMKLLIARGA 126
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 442629182 144 SVNSRDMLRMTPLHWAVEKKHKGIVRLLLKCQADVTLVSKFGKTPIGLAV 193
Cdd:PHA02875 127 DPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAM 176
PHA02876 PHA02876
ankyrin repeat protein; Provisional
81-208 6.35e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 49.29  E-value: 6.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629182  81 ASDWLGMSALHFAAMNNQLEICEILLQGGINMDGKTKVDRTPLHLACYYGHERI-VSLLLALKCSVNSRDMLRMTPLHWA 159
Cdd:PHA02876 370 ARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMsVKTLIDRGANVNSKNKDLSTPLHYA 449
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 442629182 160 VEKKHK-GIVRLLLKCQADVTLVSKFGKTPIGLAV-YTEQADVL----AELEAAR 208
Cdd:PHA02876 450 CKKNCKlDVIEMLLDNGADVNAINIQNQYPLLIALeYHGIVNILlhygAELRDSR 504
Ank_4 pfam13637
Ankyrin repeats (many copies);
152-204 1.09e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.03  E-value: 1.09e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 442629182  152 RMTPLHWAVEKKHKGIVRLLLKCQADVTLVSKFGKTPIGLAVYTEQADVLAEL 204
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PHA02874 PHA02874
ankyrin repeat protein; Provisional
90-193 1.34e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 47.65  E-value: 1.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629182  90 LHFAAMNNQLEICEILLQGGINMDGKTKVDRTPLHLACYYGHERIVSLLLALKCSVNSRDMLRMTPLHWAVEKKHKGIVR 169
Cdd:PHA02874 128 LHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIK 207
                         90       100
                 ....*....|....*....|....
gi 442629182 170 LLLKCQADVTLVSKFGKTPIGLAV 193
Cdd:PHA02874 208 LLIDHGNHIMNKCKNGFTPLHNAI 231
PHA02876 PHA02876
ankyrin repeat protein; Provisional
88-209 1.80e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 47.75  E-value: 1.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629182  88 SALHFAAMNNQL-EICEILLQGGINMDGKTKVDRTPLHLACYYGHE-RIVSLLLALKCSVNSRDMLRMTPLHWAVE-KKH 164
Cdd:PHA02876 275 TPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYLMAKNGYDtENIRTLIMLGADVNAADRLYITPLHQASTlDRN 354
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 442629182 165 KGIVRLLLKCQADVTLVSKFGKTPIGLAVYTEQA-------DVLAELEAARQ 209
Cdd:PHA02876 355 KDIVITLLELGANVNARDYCDKTPIHYAAVRNNVviintllDYGADIEALSQ 406
Ank_2 pfam12796
Ankyrin repeats (3 copies);
156-204 1.93e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 43.57  E-value: 1.93e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 442629182  156 LHWAVEKKHKGIVRLLLKCQADVTLVSKFGKTPIGLAVYTEQADVLAEL 204
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL 49
PHA03095 PHA03095
ankyrin-like protein; Provisional
70-181 2.50e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.94  E-value: 2.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629182  70 VKAALAHGA-PFASDWLGMSALHFAAMNNQLEICEI--LLQGGINMDGKTKVDRTPLHLACYYGHERIVSLLLALKCSVN 146
Cdd:PHA03095 205 VRELIRAGCdPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADIN 284
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 442629182 147 SRDMLRMTPLHWAVEKKHKGIVRLLLKCQADVTLV 181
Cdd:PHA03095 285 AVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETV 319
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
35-161 3.73e-05

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: 46.61  E-value: 3.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629182   35 EGDVQQKKGILVGPATCVDLGKQLLQCARDSDVAGVKAALAHGAPFASD----WL-----------GMSALHFAAMNNQL 99
Cdd:TIGR00870  62 ENENLELTELLLNLSCRGAVGDTLLHAISLEYVDAVEAILLHLLAAFRKsgplELandqytseftpGITALHLAAHRQNY 141
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442629182  100 EICEILLQGGINMDGKTKVD--------------RTPLHLACYYGHERIVSLLLALKCSVNSRDMLRMTPLHWAVE 161
Cdd:TIGR00870 142 EIVKLLLERGASVPARACGDffvksqgvdsfyhgESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVM 217
Ank_4 pfam13637
Ankyrin repeats (many copies);
58-106 5.75e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 40.72  E-value: 5.75e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 442629182   58 LLQCARDSDVAGVKAALAHGAPF-ASDWLGMSALHFAAMNNQLEICEILL 106
Cdd:pfam13637   5 LHAAAASGHLELLRLLLEKGADInAVDGNGETALHFAASNGNVEVLKLLL 54
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
120-149 6.65e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 40.35  E-value: 6.65e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 442629182  120 RTPLHLACY-YGHERIVSLLLALKCSVNSRD 149
Cdd:pfam00023   3 NTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
46-139 7.65e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 45.66  E-value: 7.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629182  46 VGPATCVDLGKQLLQCARDSDVAGVKAALAHGA-PFASDWLGMSALHFAAMNNQLEICEILLQGGINMDGKTKVDRTPLH 124
Cdd:PTZ00322  74 IDPVVAHMLTVELCQLAASGDAVGARILLTGGAdPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLE 153
                         90
                 ....*....|....*
gi 442629182 125 LACYYGHERIVSLLL 139
Cdd:PTZ00322 154 LAEENGFREVVQLLS 168
PHA03100 PHA03100
ankyrin repeat protein; Provisional
86-146 2.36e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 43.89  E-value: 2.36e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442629182  86 GMSALHFAAMNNQLEICEILLQGGINMDGKTKVDRTPLHLACYYGHERIVSLLLALKCSVN 146
Cdd:PHA03100 192 GFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
PHA02876 PHA02876
ankyrin repeat protein; Provisional
86-194 2.58e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 43.90  E-value: 2.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629182  86 GMSALHFAAMNN-QLEICEILLQGGINMDGKTKVDRTPLHLACYYGHER-IVSLLLALKCSVNSRDMLRMTPLHWAVEKK 163
Cdd:PHA02876 307 GETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKdIVITLLELGANVNARDYCDKTPIHYAAVRN 386
                         90       100       110
                 ....*....|....*....|....*....|.
gi 442629182 164 HKGIVRLLLKCQADVTLVSKFGKTPIGLAVY 194
Cdd:PHA02876 387 NVVIINTLLDYGADIEALSQKIGTALHFALC 417
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
153-180 3.82e-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: 3.82e-04
                           10        20
                   ....*....|....*....|....*...
gi 442629182   153 MTPLHWAVEKKHKGIVRLLLKCQADVTL 180
Cdd:smart00248   3 RTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
119-146 3.97e-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: 3.97e-04
                           10        20
                   ....*....|....*....|....*...
gi 442629182   119 DRTPLHLACYYGHERIVSLLLALKCSVN 146
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADIN 29
PHA02876 PHA02876
ankyrin repeat protein; Provisional
133-201 5.10e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 43.13  E-value: 5.10e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442629182 133 RIVSLLLALKCSVNSRDMLRMTPLHWAVEKKHKGIVRLLLKCQADVTLVSKFGKTPIGLAVYTEQADVL 201
Cdd:PHA02876 159 LIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTI 227
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
153-183 5.40e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 37.65  E-value: 5.40e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 442629182  153 MTPLHWAVEK-KHKGIVRLLLKCQADVTLVSK 183
Cdd:pfam00023   3 NTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
120-146 6.63e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.24  E-value: 6.63e-04
                          10        20
                  ....*....|....*....|....*..
gi 442629182  120 RTPLHLACYYGHERIVSLLLALKCSVN 146
Cdd:pfam13606   3 NTPLHLAARNGRLEIVKLLLENGADIN 29
PHA02875 PHA02875
ankyrin repeat protein; Provisional
86-193 7.47e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 42.29  E-value: 7.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629182  86 GMSALHFAAMNNQLEICEILLQGGINMDGKTKVDRTPLHLACYYGHERIVSLLLALKCSVNsrDMLR---MTPLHWAVEK 162
Cdd:PHA02875  35 GISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFAD--DVFYkdgMTPLHLATIL 112
                         90       100       110
                 ....*....|....*....|....*....|.
gi 442629182 163 KHKGIVRLLLKCQADVTLVSKFGKTPIGLAV 193
Cdd:PHA02875 113 KKLDIMKLLIARGADPDIPNTDKFSPLHLAV 143
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
86-113 1.36e-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: 36.41  E-value: 1.36e-03
                           10        20
                   ....*....|....*....|....*...
gi 442629182    86 GMSALHFAAMNNQLEICEILLQGGINMD 113
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADIN 29
PHA02878 PHA02878
ankyrin repeat protein; Provisional
58-162 1.77e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 41.02  E-value: 1.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629182  58 LLQCARDSDVAGVKAALAHGAPF-ASDWLGMSALHFAAMN-NQLEICEILLQGGINMDGKTKV-DRTPLHLACYygHERI 134
Cdd:PHA02878 205 LHHAVKHYNKPIVHILLENGASTdARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYIlGLTALHSSIK--SERK 282
                         90       100
                 ....*....|....*....|....*...
gi 442629182 135 VSLLLALKCSVNSRDMLRMTPLHWAVEK 162
Cdd:PHA02878 283 LKLLLEYGADINSLNSYKLTPLSSAVKQ 310
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
153-178 1.84e-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: 36.08  E-value: 1.84e-03
                          10        20
                  ....*....|....*....|....*.
gi 442629182  153 MTPLHWAVEKKHKGIVRLLLKCQADV 178
Cdd:pfam13606   3 NTPLHLAARNGRLEIVKLLLENGADI 28
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
86-111 2.31e-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: 35.70  E-value: 2.31e-03
                          10        20
                  ....*....|....*....|....*.
gi 442629182   86 GMSALHFAAMNNQLEICEILLQGGIN 111
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGAD 27
Ank_5 pfam13857
Ankyrin repeats (many copies);
121-159 3.38e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.17  E-value: 3.38e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 442629182  121 TPLHLACYYGHERIVSLLLALKCSVNSRDMLRMTPLHWA 159
Cdd:pfam13857  18 TPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
58-201 5.92e-03

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 39.74  E-value: 5.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629182  58 LLQCARDSDVAGVkaaLAHGAPFASDWLGMSALHFAAMNNQLEICEILLQGGINMDGKTKVD--------------RTPL 123
Cdd:cd22194  116 LLAFAEENGILDR---FINAEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGVffnpkykhegfyfgETPL 192
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629182 124 HLACYYGHERIVSLLLAlKCSVN--SRDMLRMTPLHWAVE-----KKHKGIV-----RLLLKCQADV--TLVSKFGKTPI 189
Cdd:cd22194  193 ALAACTNQPEIVQLLME-KESTDitSQDSRGNTVLHALVTvaedsKTQNDFVkrmydMILLKSENKNleTIRNNEGLTPL 271
                        170
                 ....*....|..
gi 442629182 190 GLAVYTEQADVL 201
Cdd:cd22194  272 QLAAKMGKAEIL 283
PHA02874 PHA02874
ankyrin repeat protein; Provisional
88-193 6.39e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 39.18  E-value: 6.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629182  88 SALHFAAMNNqlEICEILLQGGINMDGKTKVDRTPLHLACYYGHERIVSLLLALKCSVNSRDMLRMTPLHWAVEKKHKGI 167
Cdd:PHA02874  95 SILPIPCIEK--DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDI 172
                         90       100
                 ....*....|....*....|....*.
gi 442629182 168 VRLLLKCQADVTLVSKFGKTPIGLAV 193
Cdd:PHA02874 173 IKLLLEKGAYANVKDNNGESPLHNAA 198
Ank_5 pfam13857
Ankyrin repeats (many copies);
74-126 6.95e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.01  E-value: 6.95e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 442629182   74 LAHG--APFASDWLGMSALHFAAMNNQLEICEILLQGGINMDGKTKVDRTPLHLA 126
Cdd:pfam13857   2 LEHGpiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
53-202 8.82e-03

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 38.91  E-value: 8.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629182   53 DLGKQLLQCARDSDVAGVKAALAHGAPF---ASDWLGMSALHFAAM-NNQLEICEILLqggiNMDGKTKVDRTPLHLACY 128
Cdd:TIGR00870  16 DEEKAFLPAAERGDLASVYRDLEEPKKLninCPDRLGRSALFVAAIeNENLELTELLL----NLSCRGAVGDTLLHAISL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629182  129 YGHERIVSLLLALKCSVNSRDMLRM-------------TPLHWAVEKKHKGIVRLLL--------KCQADVTLVSK---- 183
Cdd:TIGR00870  92 EYVDAVEAILLHLLAAFRKSGPLELandqytseftpgiTALHLAAHRQNYEIVKLLLergasvpaRACGDFFVKSQgvds 171
                         170       180
                  ....*....|....*....|.
gi 442629182  184 --FGKTPIGLAVYTEQADVLA 202
Cdd:TIGR00870 172 fyHGESPLNAAACLGSPSIVA 192
 
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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