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Conserved domains on  [gi|226958669|ref|NP_034322|]
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protein fem-1 homolog A-A [Mus musculus]

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];
2-235 7.13e-42

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 153.57  E-value: 7.13e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958669   2 DLHTAVYNAAHDGKLPLLQKLLAGRGREELEEllgevAGGGTPLLIAARRGHLDVVEYLVDHcGASVEASGSvhfdgeti 81
Cdd:COG0666   53 LGALLLLAAALAGDLLVALLLLAAGADINAKD-----DGGNTLLHAAARNGDLEIVKLLLEA-GADVNARDK-------- 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958669  82 EGAPPLWAASAAGHLAVVRSLLRRGASVNRTTRTNSTPLRAACFDGHLDVVRYLVgEHKADLEVANRHGHTCLMISCYKG 161
Cdd:COG0666  119 DGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLL-EAGADVNARDNDGETPLHLAAENG 197

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 226958669 162 HREIARYLLERGAQVNRRSAKGNTALHDCAESGSLEILQLLLGCHARME-RDGYGMTPLLAASVTGHTNIVEYLI 235
Cdd:COG0666  198 HLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNaKDKDGLTALLLAAAAGAALIVKLLL 272
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
516-602 5.47e-16

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 78.84  E-value: 5.47e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958669 516 RGKNGFTPLHMAVDKEttnvgryrvgvfpSLQVVKVLLDCGADPDSRDFDNNTPLHIAAQNNCPAIMDALIEAGAHMDAT 595
Cdd:COG0666  116 RDKDGETPLHLAAYNG-------------NLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNAR 182


                 ....*..
gi 226958669 596 NAFKKTA 602
Cdd:COG0666  183 DNDGETP 189
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
2-235 7.13e-42

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 153.57  E-value: 7.13e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958669   2 DLHTAVYNAAHDGKLPLLQKLLAGRGREELEEllgevAGGGTPLLIAARRGHLDVVEYLVDHcGASVEASGSvhfdgeti 81
Cdd:COG0666   53 LGALLLLAAALAGDLLVALLLLAAGADINAKD-----DGGNTLLHAAARNGDLEIVKLLLEA-GADVNARDK-------- 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958669  82 EGAPPLWAASAAGHLAVVRSLLRRGASVNRTTRTNSTPLRAACFDGHLDVVRYLVgEHKADLEVANRHGHTCLMISCYKG 161
Cdd:COG0666  119 DGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLL-EAGADVNARDNDGETPLHLAAENG 197

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 226958669 162 HREIARYLLERGAQVNRRSAKGNTALHDCAESGSLEILQLLLGCHARME-RDGYGMTPLLAASVTGHTNIVEYLI 235
Cdd:COG0666  198 HLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNaKDKDGLTALLLAAAAGAALIVKLLL 272
Ank_2 pfam12796
Ankyrin repeats (3 copies);
87-179 1.38e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.93  E-value: 1.38e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958669   87 LWAASAAGHLAVVRSLLRRGASVNRTTRTNSTPLRAACFDGHLDVVRYLVGEHKADLEVanrHGHTCLMISCYKGHREIA 166
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD---NGRTALHYAARSGHLEIV 77

                          90
                  ....*....|...
gi 226958669  167 RYLLERGAQVNRR 179
Cdd:pfam12796  78 KLLLEKGADINVK 90
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
516-602 5.47e-16

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 78.84  E-value: 5.47e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958669 516 RGKNGFTPLHMAVDKEttnvgryrvgvfpSLQVVKVLLDCGADPDSRDFDNNTPLHIAAQNNCPAIMDALIEAGAHMDAT 595
Cdd:COG0666  116 RDKDGETPLHLAAYNG-------------NLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNAR 182


                 ....*..
gi 226958669 596 NAFKKTA 602
Cdd:COG0666  183 DNDGETP 189
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 41-207 1.22e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 67.00  E-value: 1.22e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958669  41 GGTPLLIAA--RRGHLDVVEYLVDHcGASVEASGSvhfDGETIegaPPLWAASAAGHLAVVRSLLRRGASVNRTTRtnst 118
Cdd:PHA03100 106 GITPLLYAIskKSNSYSIVEYLLDN-GANVNIKNS---DGENL---LHLYLESNKIDLKILKLLIDKGVDINAKNR---- 174

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958669 119 plraacfdghldvVRYLVgEHKADLEVANRHGHTCLMISCYKGHREIARYLLERGAQVNRRSAKGNTALHDCAESGSLEI 198
Cdd:PHA03100 175 -------------VNYLL-SYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEI 240


                 ....*....
gi 226958669 199 LQLLLGCHA 207
Cdd:PHA03100 241 FKLLLNNGP 249
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 518-595 2.12e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 60.06  E-value: 2.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958669 518 KNGFTPLHMAVDkettnvgryrvgvFPSLQVVKVLLDCGADPDSRDFDNNTPLHIAAQNNCPAIMDALIEAGA---HMDA 594
Cdd:PHA03100 190 VYGFTPLHYAVY-------------NNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPsikTIIE 256


                 .
gi 226958669 595 T 595
Cdd:PHA03100 257 T 257
Ank_2 pfam12796
Ankyrin repeats (3 copies);
504-596 5.67e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 50.88  E-value: 5.67e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958669  504 HQTVYRLLKCAP----RGKNGFTPLHMAVDKEttnvgryrvgvfpSLQVVKVLLDCgADPDSRDfDNNTPLHIAAQNNCP 579
Cdd:pfam12796  10 LELVKLLLENGAdanlQDKNGRTALHLAAKNG-------------HLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHL 74

                          90
                  ....*....|....*..
gi 226958669  580 AIMDALIEAGAHMDATN 596
Cdd:pfam12796  75 EIVKLLLEKGADINVKD 91
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 41-238 5.85e-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: 55.79  E-value: 5.85e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958669  41 GGTPLLIAARRGHLDVVEYLVDHCGASV-EASGSVHFDGETiegapPLWAASAAGHLAVVRSLLRRGASVN--RTTRTns 117
Cdd:cd22192   51 GETALHVAALYDNLEAAVVLMEAAPELVnEPMTSDLYQGET-----ALHIAVVNQNLNLVRELIARGADVVspRATGT-- 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958669 118 tplraaCFDGHLDVVRYLvGEHKadLEVAnrhghTCLmiscykGHREIARYLLERGAQVNRRSAKGNTALHDCA----ES 193
Cdd:cd22192  124 ------FFRPGPKNLIYY-GEHP--LSFA-----ACV------GNEEIVRLLIEHGADIRAQDSLGNTVLHILVlqpnKT 183

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 226958669 194 GSLEILQLLLGCHAR-------MERDGYGMTPLLAASVTGHTNIVEYLIQEQ 238
Cdd:cd22192  184 FACQMYDLILSYDKEddlqpldLVPNNQGLTPFKLAAKEGNIVMFQHLVQKR 235
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 149-177 1.55e-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: 39.11  E-value: 1.55e-04
                           10        20
                   ....*....|....*....|....*....
gi 226958669   149 HGHTCLMISCYKGHREIARYLLERGAQVN 177
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 41-219 2.81e-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: 40.83  E-value: 2.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958669   41 GGTPLLIAARRGHLDVVEYLVDHcGASVEASGSVHFDGETIE------GAPPLWAASAAGHLAVVRSLLRRGASVNRTTR 114
Cdd:TIGR00870 128 GITALHLAAHRQNYEIVKLLLER-GASVPARACGDFFVKSQGvdsfyhGESPLNAAACLGSPSIVALLSEDPADILTADS 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958669  115 TNSTPLRAA----------------CFDGHLDVvrylvGEHKADLE----VANRHGHTCLMISCYKGHREIARYLLERGA 174
Cdd:TIGR00870 207 LGNTLLHLLvmenefkaeyeelscqMYNFALSL-----LDKLRDSKelevILNHQGLTPLKLAAKEGRIVLFRLKLAIKY 281

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 226958669  175 QVNRRSAKGN----TALHDCAESGSLE----ILQLL----LGCHARMERDGYGMTPL 219
Cdd:TIGR00870 282 KQKKFVAWPNgqqlLSLYWLEELDGWRrkqsVLELIvvfvIGLKFPELSDMYLIAPL 338
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 505-590 3.54e-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: 40.38  E-value: 3.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958669 505 QTVYRLLKCA-----PRGKNGFTPLHMAVdkettnvgryrvgVFPSLQVVKVLLDCgaDPD-------SRDFDNNTPLHI 572
Cdd:cd22192   31 QAIKKLLKCPscdlfQRGALGETALHVAA-------------LYDNLEAAVVLMEA--APElvnepmtSDLYQGETALHI 95

                         90
                 ....*....|....*...
gi 226958669 573 AAQNNCPAIMDALIEAGA 590
Cdd:cd22192   96 AVVNQNLNLVRELIARGA 113
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 565-594 9.46e-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: 34.10  E-value: 9.46e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 226958669   565 DNNTPLHIAAQNNCPAIMDALIEAGAHMDA 594
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
2-235 7.13e-42

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 153.57  E-value: 7.13e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958669   2 DLHTAVYNAAHDGKLPLLQKLLAGRGREELEEllgevAGGGTPLLIAARRGHLDVVEYLVDHcGASVEASGSvhfdgeti 81
Cdd:COG0666   53 LGALLLLAAALAGDLLVALLLLAAGADINAKD-----DGGNTLLHAAARNGDLEIVKLLLEA-GADVNARDK-------- 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958669  82 EGAPPLWAASAAGHLAVVRSLLRRGASVNRTTRTNSTPLRAACFDGHLDVVRYLVgEHKADLEVANRHGHTCLMISCYKG 161
Cdd:COG0666  119 DGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLL-EAGADVNARDNDGETPLHLAAENG 197

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 226958669 162 HREIARYLLERGAQVNRRSAKGNTALHDCAESGSLEILQLLLGCHARME-RDGYGMTPLLAASVTGHTNIVEYLI 235
Cdd:COG0666  198 HLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNaKDKDGLTALLLAAAAGAALIVKLLL 272
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-238 5.74e-39

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 145.48  E-value: 5.74e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958669   1 MDLHTAVYNAAHDGKLPLLQKLLAGRGREELEELLGEVAGGGTPLLIAARRGHLDVVEYLVDHCGASVEAsgsvhfdgET 80
Cdd:COG0666   13 AALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA--------KD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958669  81 IEGAPPLWAASAAGHLAVVRSLLRRGASVNRTTRTNSTPLRAACFDGHLDVVRYLVgEHKADLEVANRHGHTCLMISCYK 160
Cdd:COG0666   85 DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLL-EAGADVNAQDNDGNTPLHLAAAN 163

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 226958669 161 GHREIARYLLERGAQVNRRSAKGNTALHDCAESGSLEILQLLLGCHARME-RDGYGMTPLLAASVTGHTNIVEYLIQEQ 238
Cdd:COG0666  164 GNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNaKDNDGKTALDLAAENGNLEIVKLLLEAG 242
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
4-187 1.84e-20

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 92.32  E-value: 1.84e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958669   4 HTAVYNAAHDGKLPLLQKLLAgrgreeleellgevAG---------GGTPLLIAARRGHLDVVEYLVDHcGASVEAsgsv 74
Cdd:COG0666  121 ETPLHLAAYNGNLEIVKLLLE--------------AGadvnaqdndGNTPLHLAAANGNLEIVKLLLEA-GADVNA---- 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958669  75 hfdgETIEGAPPLWAASAAGHLAVVRSLLRRGASVNRTTRTNSTPLRAACFDGHLDVVRYLVgEHKADLEVANRHGHTCL 154
Cdd:COG0666  182 ----RDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL-EAGADLNAKDKDGLTAL 256

                        170       180       190
                 ....*....|....*....|....*....|...
gi 226958669 155 MISCYKGHREIARYLLERGAQVNRRSAKGNTAL 187
Cdd:COG0666  257 LLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
Ank_2 pfam12796
Ankyrin repeats (3 copies);
87-179 1.38e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.93  E-value: 1.38e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958669   87 LWAASAAGHLAVVRSLLRRGASVNRTTRTNSTPLRAACFDGHLDVVRYLVGEHKADLEVanrHGHTCLMISCYKGHREIA 166
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD---NGRTALHYAARSGHLEIV 77

                          90
                  ....*....|...
gi 226958669  167 RYLLERGAQVNRR 179
Cdd:pfam12796  78 KLLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
154-236 4.79e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.39  E-value: 4.79e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958669  154 LMISCYKGHREIARYLLERGAQVNRRSAKGNTALHDCAESGSLEILQLLLGcHARMERDGYGMTPLLAASVTGHTNIVEY 233
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDNGRTALHYAARSGHLEIVKL 79


                  ...
gi 226958669  234 LIQ 236
Cdd:pfam12796  80 LLE 82
Ank_2 pfam12796
Ankyrin repeats (3 copies);
120-211 1.30e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.15  E-value: 1.30e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958669  120 LRAACFDGHLDVVRYLVgEHKADLEVANRHGHTCLMISCYKGHREIARYLLERGAQvnRRSAKGNTALHDCAESGSLEIL 199
Cdd:pfam12796   1 LHLAAKNGNLELVKLLL-ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIV 77

                          90
                  ....*....|..
gi 226958669  200 QLLLGCHARMER 211
Cdd:pfam12796  78 KLLLEKGADINV 89
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
516-602 5.47e-16

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 78.84  E-value: 5.47e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958669 516 RGKNGFTPLHMAVDKEttnvgryrvgvfpSLQVVKVLLDCGADPDSRDFDNNTPLHIAAQNNCPAIMDALIEAGAHMDAT 595
Cdd:COG0666  116 RDKDGETPLHLAAYNG-------------NLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNAR 182


                 ....*..
gi 226958669 596 NAFKKTA 602
Cdd:COG0666  183 DNDGETP 189
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
516-605 6.37e-15

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 75.76  E-value: 6.37e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958669 516 RGKNGFTPLHMAVDKEttnvgryrvgvfpSLQVVKVLLDCGADPDSRDFDNNTPLHIAAQNNCPAIMDALIEAGAHMDAT 595
Cdd:COG0666  149 QDNDGNTPLHLAAANG-------------NLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAK 215

                         90
                 ....*....|
gi 226958669 596 NAFKKTAYEL 605
Cdd:COG0666  216 DNDGKTALDL 225
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
516-602 3.72e-12

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 67.67  E-value: 3.72e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958669 516 RGKNGFTPLHMAVDKEttnvgryrvgvfpSLQVVKVLLDCGADPDSRDFDNNTPLHIAAQNNCPAIMDALIEAGAHMDAT 595
Cdd:COG0666   83 KDDGGNTLLHAAARNG-------------DLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQ 149


                 ....*..
gi 226958669 596 NAFKKTA 602
Cdd:COG0666  150 DNDGNTP 156
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 41-207 1.22e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 67.00  E-value: 1.22e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958669  41 GGTPLLIAA--RRGHLDVVEYLVDHcGASVEASGSvhfDGETIegaPPLWAASAAGHLAVVRSLLRRGASVNRTTRtnst 118
Cdd:PHA03100 106 GITPLLYAIskKSNSYSIVEYLLDN-GANVNIKNS---DGENL---LHLYLESNKIDLKILKLLIDKGVDINAKNR---- 174

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958669 119 plraacfdghldvVRYLVgEHKADLEVANRHGHTCLMISCYKGHREIARYLLERGAQVNRRSAKGNTALHDCAESGSLEI 198
Cdd:PHA03100 175 -------------VNYLL-SYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEI 240


                 ....*....
gi 226958669 199 LQLLLGCHA 207
Cdd:PHA03100 241 FKLLLNNGP 249
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 85-238 1.24e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 67.00  E-value: 1.24e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958669  85 PPLWAASAAGHLAVVRSLLRRGASVNRTTRTNSTPLRAACFDGH--LDVVR--YLVGEHKADLEVANRHGHTCLM--ISC 158
Cdd:PHA03100  37 LPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnlTDVKEivKLLLEYGANVNAPDNNGITPLLyaISK 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958669 159 YKGHREIARYLLERGAQVNRRSAKGNTALHDCAESGS--LEILQLLL------------------GCHARmERDGYGMTP 218
Cdd:PHA03100 117 KSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIdkgvdinaknrvnyllsyGVPIN-IKDVYGFTP 195

                        170       180
                 ....*....|....*....|
gi 226958669 219 LLAASVTGHTNIVEYLIQEQ 238
Cdd:PHA03100 196 LHYAVYNNNPEFVKYLLDLG 215
Ank_2 pfam12796
Ankyrin repeats (3 copies);
3-112 1.69e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 60.90  E-value: 1.69e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958669    3 LHTAVYNaahdGKLPLLQKLLAGRGREELEELLgevagGGTPLLIAARRGHLDVVEYLVDHCGASVEAsgsvhfDGETie 82
Cdd:pfam12796   1 LHLAAKN----GNLELVKLLLENGADANLQDKN-----GRTALHLAAKNGHLEIVKLLLEHADVNLKD------NGRT-- 63

                          90       100       110
                  ....*....|....*....|....*....|
gi 226958669   83 gapPLWAASAAGHLAVVRSLLRRGASVNRT 112
Cdd:pfam12796  64 ---ALHYAARSGHLEIVKLLLEKGADINVK 90
PHA03095 PHA03095
ankyrin-like protein; Provisional
 54-236 3.47e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 65.82  E-value: 3.47e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958669  54 LDVVEYLVDHcGASVEASGSVHFDgetiegapPL--WAASAAGHLAVVRSLLRRGASVNRTTRTNSTPLraACF----DG 127
Cdd:PHA03095  97 LDVIKLLIKA-GADVNAKDKVGRT--------PLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPL--AVLlksrNA 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958669 128 HLDVVRYLVgEHKADLEVANRHGHTCLMISC--YKGHREIARYLLERGAQVNRRSAKGNTALHDCAESGS---LEILQLL 202
Cdd:PHA03095 166 NVELLRLLI-DAGADVYAVDDRFRSLLHHHLqsFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSckrSLVLPLL 244

                        170       180       190
                 ....*....|....*....|....*....|....
gi 226958669 203 LGCHARMERDGYGMTPLLAASVTGHTNIVEYLIQ 236
Cdd:PHA03095 245 IAGISINARNRYGQTPLHYAAVFNNPRACRRLIA 278
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
516-613 1.69e-10

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 62.66  E-value: 1.69e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958669 516 RGKNGFTPLHMAVDKEttnvgryrvgvfpSLQVVKVLLDCGADPDSRDFDNNTPLHIAAQNNCPAIMDALIEAGAHMDAT 595
Cdd:COG0666  182 RDNDGETPLHLAAENG-------------HLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAK 248

                         90
                 ....*....|....*...
gi 226958669 596 NAFKKTAYELLDSKLLAK 613
Cdd:COG0666  249 DKDGLTALLLAAAAGAAL 266
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
102-236 2.16e-10

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 62.28  E-value: 2.16e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958669 102 LLRRGASVNRTTRTNSTPLRAACFDGHLDVVRYLVGEHKADLEVANRHGHTCLMISCYKGHREIARYLLERGAQVNRRSA 181
Cdd:COG0666    6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 226958669 182 KGNTALHDCAESGSLEILQLLLGCHARME-RDGYGMTPLLAASVTGHTNIVEYLIQ 236
Cdd:COG0666   86 GGNTLLHAAARNGDLEIVKLLLEAGADVNaRDKDGETPLHLAAYNGNLEIVKLLLE 141
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 43-203 2.46e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 63.09  E-value: 2.46e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958669  43 TPLLIAARRGHLDVVEYLVDhcgasveaSGSVHFDGETIEGAPPLWAASAAGHLAVVRSLLRRGASVNRTTRTNSTPLRA 122
Cdd:PHA02875  70 SELHDAVEEGDVKAVEELLD--------LGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHL 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958669 123 ACFDGHLDVVRYLVgEHKADLEVANRHGHTCLMISCYKGHREIARYLLERGAQVNRRSAKGN-TALHDCAESGSLEILQL 201
Cdd:PHA02875 142 AVMMGDIKGIELLI-DHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRL 220


                 ..
gi 226958669 202 LL 203
Cdd:PHA02875 221 FI 222
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 518-595 2.12e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 60.06  E-value: 2.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958669 518 KNGFTPLHMAVDkettnvgryrvgvFPSLQVVKVLLDCGADPDSRDFDNNTPLHIAAQNNCPAIMDALIEAGA---HMDA 594
Cdd:PHA03100 190 VYGFTPLHYAVY-------------NNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPsikTIIE 256


                 .
gi 226958669 595 T 595
Cdd:PHA03100 257 T 257
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 2-235 2.45e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 59.98  E-value: 2.45e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958669   2 DLHTAVYNaahdGKLPLLQKLLAGRGREELEELLGEVagggTPLLIAARRGHLDVVEYLVDHcGASVEasgsvHFDgeTI 81
Cdd:PHA02874   4 DLRMCIYS----GDIEAIEKIIKNKGNCINISVDETT----TPLIDAIRSGDAKIVELFIKH-GADIN-----HIN--TK 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958669  82 EGAPPLWAASAAGHLAV----------------------VRSLLRRGASVNRTTRTNSTPLRAACFDGHLDVVRYLVgEH 139
Cdd:PHA02874  68 IPHPLLTAIKIGAHDIIkllidngvdtsilpipciekdmIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLF-EY 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958669 140 KADLEVANRHGHTCLMISCYKGHREIARYLLERGAQVNRRSAKGNTALHDCAESGSLEILQLLL--GCHArMERDGYGMT 217
Cdd:PHA02874 147 GADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIdhGNHI-MNKCKNGFT 225

                        250
                 ....*....|....*...
gi 226958669 218 PLLAAsVTGHTNIVEYLI 235
Cdd:PHA02874 226 PLHNA-IIHNRSAIELLI 242
Ank_2 pfam12796
Ankyrin repeats (3 copies);
187-246 4.99e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 53.58  E-value: 4.99e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 226958669  187 LHDCAESGSLEILQLLLGCHARME-RDGYGMTPLLAASVTGHTNIVEYLIQEQPGHEQLSG 246
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANlQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNG 61
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 39-202 1.71e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 57.96  E-value: 1.71e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958669  39 AGGGTPLLIAARRGHLDVVEYLVDH-CgasveasgSVHFdgETIEGAPPLWAASAAGHLAVVRSLLRRGASVNrtTRTNS 117
Cdd:PLN03192 556 SKGRTPLHIAASKGYEDCVLVLLKHaC--------NVHI--RDANGNTALWNAISAKHHKIFRILYHFASISD--PHAAG 623

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958669 118 TPLRAACFDGHLDVVRYLVgEHKADLEVANRHGHTCLMISCYKGHREIARYLLERGAQVNRRSakgntaLHDcaESGSLE 197
Cdd:PLN03192 624 DLLCTAAKRNDLTAMKELL-KQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAN------TDD--DFSPTE 694


                 ....*
gi 226958669 198 ILQLL 202
Cdd:PLN03192 695 LRELL 699
PHA03095 PHA03095
ankyrin-like protein; Provisional
 96-235 2.18e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 56.96  E-value: 2.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958669  96 LAVVRSLLRRGASVNRTTRTNSTPL----RAACFDGhLDVVRYLVgEHKADLEVANRHGHT---CLMisCYKGHREIARY 168
Cdd:PHA03095  27 VEEVRRLLAAGADVNFRGEYGKTPLhlylHYSSEKV-KDIVRLLL-EAGADVNAPERCGFTplhLYL--YNATTLDVIKL 102

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 226958669 169 LLERGAQVNRRSAKGNTALHDCAESGSL--EILQLLLGCHARME-RDGYGMTPL--LAASVTGHTNIVEYLI 235
Cdd:PHA03095 103 LIKAGADVNAKDKVGRTPLHVYLSGFNInpKVIRLLLRKGADVNaLDLYGMTPLavLLKSRNANVELLRLLI 174
Ank_4 pfam13637
Ankyrin repeats (many copies);
116-170 4.58e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.97  E-value: 4.58e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 226958669  116 NSTPLRAACFDGHLDVVRYLVgEHKADLEVANRHGHTCLMISCYKGHREIARYLL 170
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLL-EKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
150-203 4.86e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.58  E-value: 4.86e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 226958669  150 GHTCLMISCYKGHREIARYLLERGAQVNRRSAKGNTALHDCAESGSLEILQLLL 203
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
504-596 5.67e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 50.88  E-value: 5.67e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958669  504 HQTVYRLLKCAP----RGKNGFTPLHMAVDKEttnvgryrvgvfpSLQVVKVLLDCgADPDSRDfDNNTPLHIAAQNNCP 579
Cdd:pfam12796  10 LELVKLLLENGAdanlQDKNGRTALHLAAKNG-------------HLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHL 74

                          90
                  ....*....|....*..
gi 226958669  580 AIMDALIEAGAHMDATN 596
Cdd:pfam12796  75 EIVKLLLEKGADINVKD 91
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 41-238 5.85e-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: 55.79  E-value: 5.85e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958669  41 GGTPLLIAARRGHLDVVEYLVDHCGASV-EASGSVHFDGETiegapPLWAASAAGHLAVVRSLLRRGASVN--RTTRTns 117
Cdd:cd22192   51 GETALHVAALYDNLEAAVVLMEAAPELVnEPMTSDLYQGET-----ALHIAVVNQNLNLVRELIARGADVVspRATGT-- 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958669 118 tplraaCFDGHLDVVRYLvGEHKadLEVAnrhghTCLmiscykGHREIARYLLERGAQVNRRSAKGNTALHDCA----ES 193
Cdd:cd22192  124 ------FFRPGPKNLIYY-GEHP--LSFA-----ACV------GNEEIVRLLIEHGADIRAQDSLGNTVLHILVlqpnKT 183

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 226958669 194 GSLEILQLLLGCHAR-------MERDGYGMTPLLAASVTGHTNIVEYLIQEQ 238
Cdd:cd22192  184 FACQMYDLILSYDKEddlqpldLVPNNQGLTPFKLAAKEGNIVMFQHLVQKR 235
Ank_4 pfam13637
Ankyrin repeats (many copies);
183-235 2.59e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.65  E-value: 2.59e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 226958669  183 GNTALHDCAESGSLEILQLLLGCHARM-ERDGYGMTPLLAASVTGHTNIVEYLI 235
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADInAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
85-136 4.36e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.88  E-value: 4.36e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 226958669   85 PPLWAASAAGHLAVVRSLLRRGASVNRTTRTNSTPLRAACFDGHLDVVRYLV 136
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 549-605 5.84e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.59  E-value: 5.84e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 226958669 549 VKVLLDCGADPDSRDFDNNTPLHIAAQNNCPAIMDALIEAGAHMDATNAFKKTAYEL 605
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLEL 154
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 52-235 6.10e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 52.30  E-value: 6.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958669  52 GHLDVVEYLVDhcgasveasGSVHFDGETIEGAPPLWAASAAGHLAVVRSLLRRGASVNRTTRTNSTPLRAACFDGHLDV 131
Cdd:PHA02875  13 GELDIARRLLD---------IGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958669 132 VRYLVGEHKADLEVANRHGHTCLMISCYKGHREIARYLLERGAQVNRRSAKGNTALHDCAESGSLEILQLLLGCHARME- 210
Cdd:PHA02875  84 VEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDi 163

                        170       180
                 ....*....|....*....|....*
gi 226958669 211 RDGYGMTPLLAASVTGHTNIVEYLI 235
Cdd:PHA02875 164 EDCCGCTPLIIAMAKGDIAICKMLL 188
Ank_2 pfam12796
Ankyrin repeats (3 copies);
545-587 8.14e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 47.42  E-value: 8.14e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 226958669  545 SLQVVKVLLDCGADPDSRDFDNNTPLHIAAQNNCPAIMDALIE 587
Cdd:pfam12796   9 NLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE 51
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 86-236 8.75e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 51.80  E-value: 8.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958669  86 PLWAASAAGHLAVVRSLLRRGASVNRTTRTNSTPLRAACFDGHLDVVRYLVGE-----------------HKADLEVANr 148
Cdd:PHA02878  40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSinkcsvfytlvaikdafNNRNVEIFK- 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958669 149 hghtCLMISCYKGHR------------------EIARYLLERGAQVNRRSA-KGNTALHDCAESGSLEILQLLLGCHARM 209
Cdd:PHA02878 119 ----IILTNRYKNIQtidlvyidkkskddiieaEITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANV 194

                        170       180
                 ....*....|....*....|....*...
gi 226958669 210 ER-DGYGMTPLLAASVTGHTNIVEYLIQ 236
Cdd:PHA02878 195 NIpDKTNNSPLHHAVKHYNKPIVHILLE 222
PHA03095 PHA03095
ankyrin-like protein; Provisional
 518-602 1.05e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 51.56  E-value: 1.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958669 518 KNGFTPLHMAVDKETTnvgryrvgvfpsLQVVKVLLDCGADPDSRDFDNNTPLHIAAQNNC--PAIMDALIEAGAHMDAT 595
Cdd:PHA03095  81 RCGFTPLHLYLYNATT------------LDVIKLLIKAGADVNAKDKVGRTPLHVYLSGFNinPKVIRLLLRKGADVNAL 148


                 ....*..
gi 226958669 596 NAFKKTA 602
Cdd:PHA03095 149 DLYGMTP 155
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 83-222 1.35e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 51.42  E-value: 1.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958669  83 GAPPLWAASAAGHLAVVRSLLRRGASVNRTTRTNSTPLRAACFDGHLDVVRYLVgEHKADLEVANRHGHTCLMISC-YKG 161
Cdd:PHA02878 168 GNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILL-ENGASTDARDKCGNTPLHISVgYCK 246

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 226958669 162 HREIARYLLERGAQVNRRSA-KGNTALHDCAESGslEILQLLLGCHARMER-DGYGMTPLLAA 222
Cdd:PHA02878 247 DYDILKLLLEHGVDVNAKSYiLGLTALHSSIKSE--RKLKLLLEYGADINSlNSYKLTPLSSA 307
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 141-205 3.37e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.28  E-value: 3.37e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 226958669 141 ADLEVANRHGHTCLMISCYKGHREIARYLLERGAQVNRRSAKGNTALHDCAESGSLEILQLLLGC 205
Cdd:PTZ00322 106 ADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PHA03095 PHA03095
ankyrin-like protein; Provisional
 516-602 4.93e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 49.64  E-value: 4.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958669 516 RGKNGFTPLHMAVDKETTNVGryrvgvfpslqVVKVLLDCGADPDSRDFDNNTPLHIAAQNN--CPAIMDALIEAGAHMD 593
Cdd:PHA03095 113 KDKVGRTPLHVYLSGFNINPK-----------VIRLLLRKGADVNALDLYGMTPLAVLLKSRnaNVELLRLLIDAGADVY 181


                 ....*....
gi 226958669 594 ATNAFKKTA 602
Cdd:PHA03095 182 AVDDRFRSL 190
Ank_5 pfam13857
Ankyrin repeats (many copies);
141-188 6.81e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.87  E-value: 6.81e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 226958669  141 ADLEVANRHGHTCLMISCYKGHREIARYLLERGAQVNRRSAKGNTALH 188
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 91-170 8.60e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.13  E-value: 8.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958669  91 SAAGHLAVVRSLLRRGASVNRTTRTNSTPLRAACFDGHLDVVRYLVgEHKADLEVANRHGHTCLMISCYKGHREIARYLL 170
Cdd:PTZ00322  90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLL-EFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
PHA03095 PHA03095
ankyrin-like protein; Provisional
 97-187 1.20e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 48.10  E-value: 1.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958669  97 AVVRSLLRRGASVNRTTRTNSTPLRAA---CFDGHLDVVRYLvgEHKADLEVANRHGHTCLMISCYKGHREIARYLLERG 173
Cdd:PHA03095 203 RIVRELIRAGCDPAATDMLGNTPLHSMatgSSCKRSLVLPLL--IAGISINARNRYGQTPLHYAAVFNNPRACRRLIALG 280

                         90
                 ....*....|....
gi 226958669 174 AQVNRRSAKGNTAL 187
Cdd:PHA03095 281 ADINAVSSDGNTPL 294
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 41-236 1.66e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 48.14  E-value: 1.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958669  41 GGTPLLIAARRGH-LDVVEYLVDHcGASVEASGSVHFDgetiegapPLWAASAAGHLA-VVRSLLRRGASVNRTTRTNST 118
Cdd:PHA02876 307 GETPLYLMAKNGYdTENIRTLIML-GADVNAADRLYIT--------PLHQASTLDRNKdIVITLLELGANVNARDYCDKT 377

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958669 119 PLRAACFDGHLDVVRYLVgEHKADLEVANRHGHTCLMISCYKGHREIA-RYLLERGAQVNRRSAKGNTALH-DCAESGSL 196
Cdd:PHA02876 378 PIHYAAVRNNVVIINTLL-DYGADIEALSQKIGTALHFALCGTNPYMSvKTLIDRGANVNSKNKDLSTPLHyACKKNCKL 456

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 226958669 197 EILQLLLGCHARME----RDGYgmtPLLAAsvTGHTNIVEYLIQ 236
Cdd:PHA02876 457 DVIEMLLDNGADVNainiQNQY---PLLIA--LEYHGIVNILLH 495
PHA03095 PHA03095
ankyrin-like protein; Provisional
 498-602 1.84e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 47.71  E-value: 1.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958669 498 SQEHLKHQTVYRLLKCAP----RGKNGFTPLHMAVdkettnvgryRVGVFPSLQVVKVLLDCGADPDSRDFDNNTPLHIA 573
Cdd:PHA03095  21 NASNVTVEEVRRLLAAGAdvnfRGEYGKTPLHLYL----------HYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLY 90

                         90       100       110
                 ....*....|....*....|....*....|
gi 226958669 574 AQNNC-PAIMDALIEAGAHMDATNAFKKTA 602
Cdd:PHA03095  91 LYNATtLDVIKLLIKAGADVNAKDKVGRTP 120
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 98-219 2.46e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 47.18  E-value: 2.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958669  98 VVRSLLRRGASVNRTTR-TNSTPLRAACFDGHLDVVRYLVgEHKADLEVANRHGHTCLMISCYKGHREIARYLLERGAQV 176
Cdd:PHA02878 149 ITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLL-SYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAST 227

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 226958669 177 NRRSAKGNTALHdcAESGSL---EILQLLL--GCHARMERDGYGMTPL 219
Cdd:PHA02878 228 DARDKCGNTPLH--ISVGYCkdyDILKLLLehGVDVNAKSYILGLTAL 273
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 43-176 2.62e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 47.37  E-value: 2.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958669  43 TPLLIAARRGHLDVVEYLVDHcGASVEA-----SGSVHFdgeTIEGAPPLWAasaaghlavVRSLLRRGASVNRTTRTNS 117
Cdd:PHA02876 377 TPIHYAAVRNNVVIINTLLDY-GADIEAlsqkiGTALHF---ALCGTNPYMS---------VKTLIDRGANVNSKNKDLS 443

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958669 118 TPLRAACFDG-HLDVVRYLVgEHKADLEVANRHGHTCLMISCykGHREIARYLLERGAQV 176
Cdd:PHA02876 444 TPLHYACKKNcKLDVIEMLL-DNGADVNAINIQNQYPLLIAL--EYHGIVNILLHYGAEL 500
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 87-249 2.64e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 47.56  E-value: 2.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958669  87 LWAASAAGHLAVVRSLLRRGASVNRTTRTNSTPLRAACFDGHLDVVRYLVgEHKADLEVANRHGHTCLMISCYKGHREIA 166
Cdd:PLN03192 529 LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLL-KHACNVHIRDANGNTALWNAISAKHHKIF 607

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958669 167 RYLLERGAQVNRRSakGNTALHDCAESGSLEILQLLL--GCHARMErDGYGMTPLLAASVTGHTNIVEYLIQEQPG---- 240
Cdd:PLN03192 608 RILYHFASISDPHA--AGDLLCTAAKRNDLTAMKELLkqGLNVDSE-DHQGATALQVAMAEDHVDMVRLLIMNGADvdka 684

                        170
                 ....*....|.
gi 226958669 241 --HEQLSGTEL 249
Cdd:PLN03192 685 ntDDDFSPTEL 695
Ank_5 pfam13857
Ankyrin repeats (many copies);
552-605 2.94e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 2.94e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 226958669  552 LLDCG-ADPDSRDFDNNTPLHIAAQNNCPAIMDALIEAGAHMDATNAFKKTAYEL 605
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 62-144 3.01e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.20  E-value: 3.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958669  62 DHCGASVEASGSVHFDGETIEGAPPLWAASAAGHLAVVRSLLRRGASVNRTTRTNSTPLRAACFDGHLDVVRYLVGEHKA 141
Cdd:PTZ00322  94 DAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQC 173


                 ...
gi 226958669 142 DLE 144
Cdd:PTZ00322 174 HFE 176
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
546-602 3.17e-05

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 46.49  E-value: 3.17e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 226958669 546 LQVVKVLLDCGADPDSRDFDNNTPLHIAAQNNCPAIMDALIEAGAHMDATNAFKKTA 602
Cdd:COG0666   67 LLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETP 123
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 82-237 4.42e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 46.50  E-value: 4.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958669  82 EGAPPLWAASAAGHLAVVRSLLRRGASVNRTTRTNSTPLRAACFDGHLDVVRYLVgEHKADLEVanrhghtcLMISCYKg 161
Cdd:PHA02874  34 ETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLI-DNGVDTSI--------LPIPCIE- 103

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 226958669 162 hREIARYLLERGAQVNRRSAKGNTALHDCAESGSLEILQLLLGCHARME-RDGYGMTPLLAASVTGHTNIVEYLIQE 237
Cdd:PHA02874 104 -KDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNiEDDNGCYPIHIAIKHNFFDIIKLLLEK 179
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 549-606 5.30e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 46.60  E-value: 5.30e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 226958669 549 VKVLLDCGADPDSRDFDNNTPLHIAAQNNC-PAIMDALIEAGAHMDATNAfkKTAYELL 606
Cdd:PHA02876 425 VKTLIDRGANVNSKNKDLSTPLHYACKKNCkLDVIEMLLDNGADVNAINI--QNQYPLL 481
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 513-585 6.25e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.04  E-value: 6.25e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 226958669 513 CAPRGKNGFTPLHMAvdketTNVGRyrvgvfpsLQVVKVLLDCGADPDSRDFDNNTPLHIAAQNNCPAIMDAL 585
Cdd:PTZ00322 108 PNCRDYDGRTPLHIA-----CANGH--------VQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 77-188 7.40e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.82  E-value: 7.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958669  77 DGETIEGAPPLWAASAAGH-LAVVRSLLRRGASVNRTTRTNSTPL-RAACFDGHLDVVRYLVgEHKADLEVANRHGHTCL 154
Cdd:PHA02876 301 NAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLhQASTLDRNKDIVITLL-ELGANVNARDYCDKTPI 379

                         90       100       110
                 ....*....|....*....|....*....|....
gi 226958669 155 MISCYKGHREIARYLLERGAQVNRRSAKGNTALH 188
Cdd:PHA02876 380 HYAAVRNNVVIINTLLDYGADIEALSQKIGTALH 413
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 546-601 1.28e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 44.95  E-value: 1.28e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 226958669 546 LQVVKVLLDCGADPDSRDFDNNTPLHIAAQNNCPAIMDALIEAGAHMDATNAFKKT 601
Cdd:PHA02874 137 LESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGES 192
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 149-177 1.55e-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: 39.11  E-value: 1.55e-04
                           10        20
                   ....*....|....*....|....*....
gi 226958669   149 HGHTCLMISCYKGHREIARYLLERGAQVN 177
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 522-594 1.81e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 44.67  E-value: 1.81e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 226958669 522 TPLHMAvdketTNVGRYRvgvfpslQVVKVLLDCGADPDSRDFDNNTPLHIAAQNNCPAIMDALIEAGAHMDA 594
Cdd:PHA02876 343 TPLHQA-----STLDRNK-------DIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEA 403
PHA03095 PHA03095
ankyrin-like protein; Provisional
 544-602 2.53e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 43.86  E-value: 2.53e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 226958669 544 PSLQVVKVLLDCGADPDSRDFDNNTPLHIAA-QNNCPAI-MDALIEAGAHMDATNAFKKTA 602
Cdd:PHA03095 200 PRARIVRELIRAGCDPAATDMLGNTPLHSMAtGSSCKRSlVLPLLIAGISINARNRYGQTP 260
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 522-635 2.54e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 44.10  E-value: 2.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958669 522 TPLHMAVDKETTNVGRYrvgvfpslqvvkvLLDCGADPDSRDFDNNTPLHIAAQNNCPAIMDALIEAGAHMDATNAFKKT 601
Cdd:PHA02878 170 TALHYATENKDQRLTEL-------------LLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNT 236

                         90       100       110
                 ....*....|....*....|....*....|....
gi 226958669 602 AYELLDSKLLakstvqpfNYVTLQCLAARALDRN 635
Cdd:PHA02878 237 PLHISVGYCK--------DYDILKLLLEHGVDVN 262
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 86-210 3.18e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 43.90  E-value: 3.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958669  86 PLWAASAAGHLA-VVRSLLRRGASVNRTTRTNSTPLRAACFDGH-LDVVRYLVgEHKADLEVANRHGHTCL-MISCYKGH 162
Cdd:PHA02876 276 PLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLI-MLGADVNAADRLYITPLhQASTLDRN 354

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 226958669 163 REIARYLLERGAQVNRRSAKGNTALHDCAESGSLEILQLLLGCHARME 210
Cdd:PHA02876 355 KDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIE 402
Ank_5 pfam13857
Ankyrin repeats (many copies);
518-573 3.91e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.87  E-value: 3.91e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 226958669  518 KNGFTPLHMAVDKettnvgryrvgvfPSLQVVKVLLDCGADPDSRDFDNNTPLHIA 573
Cdd:pfam13857  14 GEGYTPLHVAAKY-------------GALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 519-563 5.22e-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: 5.22e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 226958669  519 NGFTPLHMAVdkettnvgrYRVGvfpSLQVVKVLLDCGADPDSRD 563
Cdd:pfam00023   1 DGNTPLHLAA---------GRRG---NLEIVKLLLSKGADVNARD 33
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 112-236 5.99e-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: 43.08  E-value: 5.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958669 112 TTRTNSTPLRAACFDGHLDVVRYLVGEHKADLEVANRHGHTCLMISCYKGHREIARYLLERGAQ-VNRRSA----KGNTA 186
Cdd:cd22192   13 QKRISESPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNEPMTsdlyQGETA 92

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 226958669 187 LHDCAESGSLEILQLLL------------GCHARMERDG---YGMTPLLAASVTGHTNIVEYLIQ 236
Cdd:cd22192   93 LHIAVVNQNLNLVRELIargadvvspratGTFFRPGPKNliyYGEHPLSFAACVGNEEIVRLLIE 157
Ank_4 pfam13637
Ankyrin repeats (many copies);
41-103 6.09e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.02  E-value: 6.09e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 226958669   41 GGTPLLIAARRGHLDVVEYLVDHcGASVEASgsvhfdgeTIEGAPPLWAASAAGHLAVVRSLL 103
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEK-GADINAV--------DGNGETALHFAASNGNVEVLKLLL 54
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 149-179 6.80e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 37.27  E-value: 6.80e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 226958669  149 HGHTCLMISCYK-GHREIARYLLERGAQVNRR 179
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNAR 32
Ank_4 pfam13637
Ankyrin repeats (many copies);
522-586 6.92e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.02  E-value: 6.92e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 226958669  522 TPLHMAVdkettnvgryrvgVFPSLQVVKVLLDCGADPDSRDFDNNTPLHIAAQNNCPAIMDALI 586
Cdd:pfam13637   3 TALHAAA-------------ASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
5-61 8.34e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 37.64  E-value: 8.34e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 226958669    5 TAVYNAAHDGKLPLLQKLLAGRGREELEEllgevAGGGTPLLIAARRGHLDVVEYLV 61
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVD-----GNGETALHFAASNGNVEVLKLLL 54
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 565-596 8.45e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 37.27  E-value: 8.45e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 226958669  565 DNNTPLHIAA-QNNCPAIMDALIEAGAHMDATN 596
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 118-238 9.29e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 42.17  E-value: 9.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958669 118 TPLRAACFDGHLDVVRYLVgEHKADLEVA------NRHGHTC-------LMISCYKGHREIARYLLERGAQVNRRSAK-- 182
Cdd:cd21882   75 TALHIAIENRNLNLVRLLV-ENGADVSARatgrffRKSPGNLfyfgelpLSLAACTNQEEIVRLLLENGAQPAALEAQds 153

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 226958669 183 -GNTALHDCAESGSLEILQLLLGCHA-----RMERDGY------------GMTPLLAASVTGHTNIVEYLIQEQ 238
Cdd:cd21882  154 lGNTVLHALVLQADNTPENSAFVCQMynlllSYGAHLDptqqleeipnhqGLTPLKLAAVEGKIVMFQHILQRE 227
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 565-591 1.98e-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: 1.98e-03
                          10        20
                  ....*....|....*....|....*..
gi 226958669  565 DNNTPLHIAAQNNCPAIMDALIEAGAH 591
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGAD 27
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 43-70 2.63e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.64  E-value: 2.63e-03
                           10        20
                   ....*....|....*....|....*...
gi 226958669    43 TPLLIAARRGHLDVVEYLVDHcGASVEA 70
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDK-GADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 41-219 2.81e-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: 40.83  E-value: 2.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958669   41 GGTPLLIAARRGHLDVVEYLVDHcGASVEASGSVHFDGETIE------GAPPLWAASAAGHLAVVRSLLRRGASVNRTTR 114
Cdd:TIGR00870 128 GITALHLAAHRQNYEIVKLLLER-GASVPARACGDFFVKSQGvdsfyhGESPLNAAACLGSPSIVALLSEDPADILTADS 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958669  115 TNSTPLRAA----------------CFDGHLDVvrylvGEHKADLE----VANRHGHTCLMISCYKGHREIARYLLERGA 174
Cdd:TIGR00870 207 LGNTLLHLLvmenefkaeyeelscqMYNFALSL-----LDKLRDSKelevILNHQGLTPLKLAAKEGRIVLFRLKLAIKY 281

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 226958669  175 QVNRRSAKGN----TALHDCAESGSLE----ILQLL----LGCHARMERDGYGMTPL 219
Cdd:TIGR00870 282 KQKKFVAWPNgqqlLSLYWLEELDGWRrkqsVLELIvvfvIGLKFPELSDMYLIAPL 338
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 42-236 3.23e-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: 40.83  E-value: 3.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958669   42 GTPLLIAARRGHLDVVEYLVDHCGASVEASGSVHF-----DGETIEGAPPLWAASAAGHLAVVRSLLRRGASVnrttrtn 116
Cdd:TIGR00870  82 GDTLLHAISLEYVDAVEAILLHLLAAFRKSGPLELandqyTSEFTPGITALHLAAHRQNYEIVKLLLERGASV------- 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958669  117 stPLRAACFD----GHLDVVRYlvGEHKadlevanrhghtclmISCYK--GHREIARYLLERGAQVNRRSAKGNTALHDC 190
Cdd:TIGR00870 155 --PARACGDFfvksQGVDSFYH--GESP---------------LNAAAclGSPSIVALLSEDPADILTADSLGNTLLHLL 215

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 226958669  191 -------AESGSL------EILQLLLGCHARME----RDGYGMTPLLAASVTGHTNIVEYLIQ 236
Cdd:TIGR00870 216 vmenefkAEYEELscqmynFALSLLDKLRDSKEleviLNHQGLTPLKLAAKEGRIVLFRLKLA 278
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 149-177 3.44e-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: 3.44e-03
                          10        20
                  ....*....|....*....|....*....
gi 226958669  149 HGHTCLMISCYKGHREIARYLLERGAQVN 177
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 505-590 3.54e-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: 40.38  E-value: 3.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958669 505 QTVYRLLKCA-----PRGKNGFTPLHMAVdkettnvgryrvgVFPSLQVVKVLLDCgaDPD-------SRDFDNNTPLHI 572
Cdd:cd22192   31 QAIKKLLKCPscdlfQRGALGETALHVAA-------------LYDNLEAAVVLMEA--APElvnepmtSDLYQGETALHI 95

                         90
                 ....*....|....*...
gi 226958669 573 AAQNNCPAIMDALIEAGA 590
Cdd:cd22192   96 AVVNQNLNLVRELIARGA 113
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 522-642 4.23e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 40.03  E-value: 4.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958669 522 TPLHMAVDKETTNVgryrvgvfpslqvVKVLLDCGADPDSRDFDNNTPLHIAAQ-----NNCPAIMDALIEAGAHMDATN 596
Cdd:PHA03100  37 LPLYLAKEARNIDV-------------VKILLDNGADINSSTKNNSTPLHYLSNikynlTDVKEIVKLLLEYGANVNAPD 103

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 226958669 597 afKKTAYELLdskLLAKSTVQPFNYVTLqcLAARALDRNKVPYKGF 642
Cdd:PHA03100 104 --NNGITPLL---YAISKKSNSYSIVEY--LLDNGANVNIKNSDGE 142
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 549-601 5.63e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 39.65  E-value: 5.63e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 226958669 549 VKVLLDCGADPDSRDFDNNTPLHIAAQNNCPAIMDALIEAGAHMDATNAFKKT 601
Cdd:PHA03100 175 VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDT 227
PHA03095 PHA03095
ankyrin-like protein; Provisional
 544-606 7.55e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 39.24  E-value: 7.55e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 226958669 544 PSLQVVKVLLDCGADPDSRDFDNNTPLHIAAQNNCPA---IMDALIEAGAHMDATNAFKKTAYELL 606
Cdd:PHA03095  25 VTVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKvkdIVRLLLEAGADVNAPERCGFTPLHLY 90
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 43-222 8.50e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 39.18  E-value: 8.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958669  43 TPLLIAARRGHLDVVEYLVDHcGASVEAsgsvhfdgETIEGAPPLWAASAAGHLAVVRSLLRRGASVNRTTRTNSTPLRA 122
Cdd:PHA02874 126 TFLHYAIKKGDLESIKMLFEY-GADVNI--------EDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHN 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226958669 123 ACFDGHLDVVRYLVgEHKADLEVANRHGHTCLMISCYkgHREIARYLLERGAQVNRRSAKGNTALHDCAE-SGSLEILQL 201
Cdd:PHA02874 197 AAEYGDYACIKLLI-DHGNHIMNKCKNGFTPLHNAII--HNRSAIELLINNASINDQDIDGSTPLHHAINpPCDIDIIDI 273

                        170       180
                 ....*....|....*....|..
gi 226958669 202 LLGCHARME-RDGYGMTPLLAA 222
Cdd:PHA02874 274 LLYHKADISiKDNKGENPIDTA 295
PHA03095 PHA03095
ankyrin-like protein; Provisional
 516-587 9.05e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 38.85  E-value: 9.05e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 226958669 516 RGKNGFTPLHMAVdkettnvgryrvgVFPSLQVVKVLLDCGADPDSRDFDNNTPLHIAAQNNCPAIMDALIE 587
Cdd:PHA03095 253 RNRYGQTPLHYAA-------------VFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALA 311
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 565-594 9.46e-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: 34.10  E-value: 9.46e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 226958669   565 DNNTPLHIAAQNNCPAIMDALIEAGAHMDA 594
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 520-573 9.98e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 38.71  E-value: 9.98e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 226958669 520 GFTPLHMAVDKEttnvgryrvgvfpslQVVKVLLDCGADPDSRDFDNNTPLHIA 573
Cdd:PHA02878 269 GLTALHSSIKSE---------------RKLKLLLEYGADINSLNSYKLTPLSSA 307
 
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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