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Conserved domains on  [gi|568954244|ref|XP_006509255|]
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POTE ankyrin domain family member A isoform X2 [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];
52-282 1.46e-46

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 169.36  E-value: 1.46e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954244   52 HRVAAEGDAARMEILLTLGQCNVYHRDRKDRTALHFACVYGRLPVVTILVKNNCEIDALDKNHTTPLMKSVQCWKQKCAT 131
Cdd:COG0666    58 LLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVK 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954244  132 VLLEHGADPNIRDSSGNSALHYAVYNGHQEMASLLLQYNADIEQKTKDGFTPLLLALREKRVEVAEFLVRMGADIHVVDE 211
Cdd:COG0666   138 LLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN 217

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568954244  212 LQRNTLIYAIRCGSKDLSVLLLEKGIDFFYKDVFGWTALRYAIEGHCTFRQTLLDFEESLHSNKKDKEPEL 282
Cdd:COG0666   218 DGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
52-282 1.46e-46

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 169.36  E-value: 1.46e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954244   52 HRVAAEGDAARMEILLTLGQCNVYHRDRKDRTALHFACVYGRLPVVTILVKNNCEIDALDKNHTTPLMKSVQCWKQKCAT 131
Cdd:COG0666    58 LLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVK 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954244  132 VLLEHGADPNIRDSSGNSALHYAVYNGHQEMASLLLQYNADIEQKTKDGFTPLLLALREKRVEVAEFLVRMGADIHVVDE 211
Cdd:COG0666   138 LLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN 217

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568954244  212 LQRNTLIYAIRCGSKDLSVLLLEKGIDFFYKDVFGWTALRYAIEGHCTFRQTLLDFEESLHSNKKDKEPEL 282
Cdd:COG0666   218 DGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
Ank_2 pfam12796
Ankyrin repeats (3 copies);
85-176 1.23e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.48  E-value: 1.23e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954244    85 LHFACVYGRLPVVTILVKNNCEIDALDKNHTTPLMKSVQCWKQKCATVLLEHgADPNIRDsSGNSALHYAVYNGHQEMAS 164
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|..
gi 568954244   165 LLLQYNADIEQK 176
Cdd:pfam12796   79 LLLEKGADINVK 90
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 66-254 9.16e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 87.41  E-value: 9.16e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954244   66 LLTLGQCNVYhRDRKDRTALHFACVYGRLPVVTILVKNNCEIDALDKNHTTPLMK-SVQCWKQKC----ATVLLEHGADP 140
Cdd:PHA03100   21 IIMEDDLNDY-SYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYlSNIKYNLTDvkeiVKLLLEYGANV 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954244  141 NIRDSSGNSALHYAVYN--GHQEMASLLLQYNADIEQKTKDGFTPLLLALREKRV--EVAEFLVRMGADIHVVDELQR-- 214
Cdd:PHA03100  100 NAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINAKNRVNYll 179

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568954244  215 -------------NT-LIYAIRCGSKDLSVLLLEKGIDFFYKDVFGWTALRYAI 254
Cdd:PHA03100  180 sygvpinikdvygFTpLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAI 233
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 55-201 5.33e-06

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: 50.78  E-value: 5.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954244   55 AAEGDAARMEILLTLGQCNVYHRDRKDRTALHFACVYGRLPVVTILVKNNCE------------------IDALDKNhtt 116
Cdd:cd22192    25 AKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElvnepmtsdlyqgetalhIAVVNQN--- 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954244  117 plMKSVQCWKQKCATV---------------------------------------LLEHGADPNIRDSSGNSALHYAVYN 157
Cdd:cd22192   102 --LNLVRELIARGADVvspratgtffrpgpknliyygehplsfaacvgneeivrlLIEHGADIRAQDSLGNTVLHILVLQ 179

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568954244  158 GHQ----EMASLLLQYNADIEQKT------KDGFTPLLLALREKRVEVAEFLVR 201
Cdd:cd22192   180 PNKtfacQMYDLILSYDKEDDLQPldlvpnNQGLTPFKLAAKEGNIVMFQHLVQ 233
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 147-174 1.95e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.57  E-value: 1.95e-05
                            10        20
                    ....*....|....*....|....*...
gi 568954244    147 GNSALHYAVYNGHQEMASLLLQYNADIE 174
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADIN 29
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 132-255 1.61e-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: 42.76  E-value: 1.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954244   132 VLLEHGADPnirdSSGNSALHYA---VYNGHQEMASLLLQYNAD-------IEQKTKD---GFTPLLLALREKRVEVAEF 198
Cdd:TIGR00870   71 LLLNLSCRG----AVGDTLLHAIsleYVDAVEAILLHLLAAFRKsgplelaNDQYTSEftpGITALHLAAHRQNYEIVKL 146

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568954244   199 LVRMGADIHVV---DEL---QRNTLIY-------AIRC-GSKDLSVLLLEKGIDFFYKDVFGWTALRYAIE 255
Cdd:TIGR00870  147 LLERGASVPARacgDFFvksQGVDSFYhgesplnAAAClGSPSIVALLSEDPADILTADSLGNTLLHLLVM 217
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
52-282 1.46e-46

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 169.36  E-value: 1.46e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954244   52 HRVAAEGDAARMEILLTLGQCNVYHRDRKDRTALHFACVYGRLPVVTILVKNNCEIDALDKNHTTPLMKSVQCWKQKCAT 131
Cdd:COG0666    58 LLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVK 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954244  132 VLLEHGADPNIRDSSGNSALHYAVYNGHQEMASLLLQYNADIEQKTKDGFTPLLLALREKRVEVAEFLVRMGADIHVVDE 211
Cdd:COG0666   138 LLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN 217

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568954244  212 LQRNTLIYAIRCGSKDLSVLLLEKGIDFFYKDVFGWTALRYAIEGHCTFRQTLLDFEESLHSNKKDKEPEL 282
Cdd:COG0666   218 DGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
51-250 1.00e-42

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 158.19  E-value: 1.00e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954244   51 IHRVAAEGDAARMEILLTLGqCNVYHRDRKDRTALHFACVYGRLPVVTILVKNNCEIDALDKNHTTPLMKSVQCWKQKCA 130
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAG-ADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIV 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954244  131 TVLLEHGADPNIRDSSGNSALHYAVYNGHQEMASLLLQYNADIEQKTKDGFTPLLLALREKRVEVAEFLVRMGADIHVVD 210
Cdd:COG0666   170 KLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKD 249

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 568954244  211 ELQRNTLIYAIRCGSKDLSVLLLEKGIDFFYKDVFGWTAL 250
Cdd:COG0666   250 KDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
50-255 4.68e-42

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 156.27  E-value: 4.68e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954244   50 HIHRVAAEGDAARMEILLTLGQCNVYHRDRKDRTALHFACVYGRLPVVTILVKNNCEIDALDKNHTTPLMKSVQCWKQKC 129
Cdd:COG0666    23 LLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEI 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954244  130 ATVLLEHGADPNIRDSSGNSALHYAVYNGHQEMASLLLQYNADIEQKTKDGFTPLLLALREKRVEVAEFLVRMGADIHVV 209
Cdd:COG0666   103 VKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNAR 182

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 568954244  210 DELQRNTLIYAIRCGSKDLSVLLLEKGIDFFYKDVFGWTALRYAIE 255
Cdd:COG0666   183 DNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAE 228
Ank_2 pfam12796
Ankyrin repeats (3 copies);
85-176 1.23e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.48  E-value: 1.23e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954244    85 LHFACVYGRLPVVTILVKNNCEIDALDKNHTTPLMKSVQCWKQKCATVLLEHgADPNIRDsSGNSALHYAVYNGHQEMAS 164
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|..
gi 568954244   165 LLLQYNADIEQK 176
Cdd:pfam12796   79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
118-210 3.15e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.93  E-value: 3.15e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954244   118 LMKSVQCWKQKCATVLLEHGADPNIRDSSGNSALHYAVYNGHQEMASLLLQYnADIEQKTkDGFTPLLLALREKRVEVAE 197
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 568954244   198 FLVRMGADIHVVD 210
Cdd:pfam12796   79 LLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 66-254 9.16e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 87.41  E-value: 9.16e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954244   66 LLTLGQCNVYhRDRKDRTALHFACVYGRLPVVTILVKNNCEIDALDKNHTTPLMK-SVQCWKQKC----ATVLLEHGADP 140
Cdd:PHA03100   21 IIMEDDLNDY-SYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYlSNIKYNLTDvkeiVKLLLEYGANV 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954244  141 NIRDSSGNSALHYAVYN--GHQEMASLLLQYNADIEQKTKDGFTPLLLALREKRV--EVAEFLVRMGADIHVVDELQR-- 214
Cdd:PHA03100  100 NAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINAKNRVNYll 179

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568954244  215 -------------NT-LIYAIRCGSKDLSVLLLEKGIDFFYKDVFGWTALRYAI 254
Cdd:PHA03100  180 sygvpinikdvygFTpLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAI 233
PHA03095 PHA03095
ankyrin-like protein; Provisional
 111-263 2.26e-17

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 86.62  E-value: 2.26e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954244  111 DKNHT-----TPLMKSVQCWKQKCATV---LLEHGADPNIRDSSGNSALHYAVYNGHQE-MASLLLQYNADIEQKTKDGF 181
Cdd:PHA03095   39 DVNFRgeygkTPLHLYLHYSSEKVKDIvrlLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAGADVNAKDKVGR 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954244  182 TPLLLALREKRV--EVAEFLVRMGADIHVVDELQRNTLiyAIRCGSKDLSV----LLLEKGIDFFYKDVFGWTALRYaie 255
Cdd:PHA03095  119 TPLHVYLSGFNInpKVIRLLLRKGADVNALDLYGMTPL--AVLLKSRNANVellrLLIDAGADVYAVDDRFRSLLHH--- 193


                  ....*...
gi 568954244  256 gHCTFRQT 263
Cdd:PHA03095  194 -HLQSFKP 200
Ank_2 pfam12796
Ankyrin repeats (3 copies);
151-243 1.40e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 73.23  E-value: 1.40e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954244   151 LHYAVYNGHQEMASLLLQYNADIEQKTKDGFTPLLLALREKRVEVAEFLVRmGADIHVVDElQRNTLIYAIRCGSKDLSV 230
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 568954244   231 LLLEKGIDFFYKD 243
Cdd:pfam12796   79 LLLEKGADINVKD 91
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 33-254 5.45e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 79.15  E-value: 5.45e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954244   33 GENPNYPKYHTTYrPLghiHRVAAEGDAARM-EILLTLGQCNVYHRDRKDRTALHFACVYGRLPVVTILVKNNCEID--A 109
Cdd:PHA02878   60 GHNVNQPDHRDLT-PL---HIICKEPNKLGMkEMIRSINKCSVFYTLVAIKDAFNNRNVEIFKIILTNRYKNIQTIDlvY 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954244  110 LDKNHTTPLMKSvqcwkqKCATVLLEHGADPNIRD-SSGNSALHYAVYNGHQEMASLLLQYNADIEQKTKDGFTPLLLAL 188
Cdd:PHA02878  136 IDKKSKDDIIEA------EITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAV 209

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568954244  189 REKRVEVAEFLVRMGADIHVVDELQRNTLIYAI-RCGSKDLSVLLLEKGIDFFYKD-VFGWTALRYAI 254
Cdd:PHA02878  210 KHYNKPIVHILLENGASTDARDKCGNTPLHISVgYCKDYDILKLLLEHGVDVNAKSyILGLTALHSSI 277
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 64-252 5.62e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 75.77  E-value: 5.62e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954244   64 EILLTLGQC--NVYHRDRKDRTALHFACVYGRLPVVTILVKNNCEIDALDKNHTTPLMKSVQCWKQKCATVLLEHGADPN 141
Cdd:PHA02874  105 DMIKTILDCgiDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954244  142 IRDSSGNSALHYAVYNGHQEMASLLLQYNADIEQKTKDGFTPLLLALREKRvEVAEFLVRmGADIHVVDELQRNTLIYAI 221
Cdd:PHA02874  185 VKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLIN-NASINDQDIDGSTPLHHAI 262

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 568954244  222 R--CgSKDLSVLLLEKGIDFFYKDVFGW----TALRY 252
Cdd:PHA02874  263 NppC-DIDIIDILLYHKADISIKDNKGEnpidTAFKY 298
Ank_2 pfam12796
Ankyrin repeats (3 copies);
51-144 7.22e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 68.22  E-value: 7.22e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954244    51 IHRVAAEGDAARMEILLTLGqCNVYHRDRKDRTALHFACVYGRLPVVTILVkNNCEIDALDKNHTtPLMKSVQCWKQKCA 130
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENG-ADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKDNGRT-ALHYAARSGHLEIV 77

                           90
                   ....*....|....
gi 568954244   131 TVLLEHGADPNIRD 144
Cdd:pfam12796   78 KLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 66-243 8.65e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 75.09  E-value: 8.65e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954244   66 LLTLGQCNVYHRDRKDRTALHFA--CVYGRLPVVTILVKNNCEIDALDKnhttplmksVQCwkqkcatvLLEHGADPNIR 143
Cdd:PHA03100  126 YLLDNGANVNIKNSDGENLLHLYleSNKIDLKILKLLIDKGVDINAKNR---------VNY--------LLSYGVPINIK 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954244  144 DSSGNSALHYAVYNGHQEMASLLLQYNADIEQKTKDGFTPLLLALREKRVEVAEFLVRMGADIHVVDElqrnTLIY-AIR 222
Cdd:PHA03100  189 DVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE----TLLYfKDK 264

                         170       180
                  ....*....|....*....|....*...
gi 568954244  223 CGSKDLSVLLLEKGIDF-------FYKD 243
Cdd:PHA03100  265 DLNTITKIKMLKKSIMYmflldpgFYKN 292
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 20-238 2.39e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 73.87  E-value: 2.39e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954244   20 CDA---PQMTVSEFFF--GENPNYPKYHTtYRPLGHIHRVAaegDAARMEILLTLGQC-NVYHRDRkdRTALHFACVYGR 93
Cdd:PHA02875    7 CDAilfGELDIARRLLdiGINPNFEIYDG-ISPIKLAMKFR---DSEAIKLLMKHGAIpDVKYPDI--ESELHDAVEEGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954244   94 LPVVTILVKNNCEI-DALDKNHTTPLMKSVQCWKQKCATVLLEHGADPNIRDSSGNSALHYAVYNGHQEMASLLLQYNAD 172
Cdd:PHA02875   81 VKAVEELLDLGKFAdDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKAC 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568954244  173 IEQKTKDGFTPLLLALREKRVEVAEFLVRMGADIHVVDELQRNTLI-YAIRCGSKDLSVLLLEKGID 238
Cdd:PHA02875  161 LDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALcYAIENNKIDIVRLFIKRGAD 227
PHA03095 PHA03095
ankyrin-like protein; Provisional
 133-309 2.72e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 73.91  E-value: 2.72e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954244  133 LLEHGADPNIRDSSGNSALHYAVYNGHQ---EMASLLLQYNADIEQKTKDGFTPLLLALREK-RVEVAEFLVRMGADIHV 208
Cdd:PHA03095   33 LLAAGADVNFRGEYGKTPLHLYLHYSSEkvkDIVRLLLEAGADVNAPERCGFTPLHLYLYNAtTLDVIKLLIKAGADVNA 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954244  209 VDELQRNTL-IYAirCG-SKDLSV--LLLEKGIDFFYKDVFGWTAL--------------RYAIEGHCT------FRQTL 264
Cdd:PHA03095  113 KDKVGRTPLhVYL--SGfNINPKVirLLLRKGADVNALDLYGMTPLavllksrnanvellRLLIDAGADvyavddRFRSL 190

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 568954244  265 LD-FEESLHSNKKdKEPELQVepsTSCILAKQIDAGND---SLARISSC 309
Cdd:PHA03095  191 LHhHLQSFKPRAR-IVRELIR---AGCDPAATDMLGNTplhSMATGSSC 235
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 30-190 2.88e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 73.76  E-value: 2.88e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954244   30 FFFGENPNYPKYHTTYRPLghiHRVAAEGDAARMEILLTLGqCNVYHRDRKDRTALHFACVYGRLPVVTILVKNNCEIDA 109
Cdd:PHA02878  154 LSYGADINMKDRHKGNTAL---HYATENKDQRLTELLLSYG-ANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDA 229

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954244  110 LDKNHTTPLMKSV-QCWKQKCATVLLEHGADPNIRDS-SGNSALHYAVYNghQEMASLLLQYNADIEQKTKDGFTPLLLA 187
Cdd:PHA02878  230 RDKCGNTPLHISVgYCKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSA 307


                  ...
gi 568954244  188 LRE 190
Cdd:PHA02878  308 VKQ 310
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 92-254 1.56e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 68.07  E-value: 1.56e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954244   92 GRLPVVTILVKNNCEIDALDKNHTTPLMKSVQ-----------------------CWKQKCATVLLEHGADPNIRDSSGN 148
Cdd:PHA02874   46 GDAKIVELFIKHGADINHINTKIPHPLLTAIKigahdiikllidngvdtsilpipCIEKDMIKTILDCGIDVNIKDAELK 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954244  149 SALHYAVYNGHQEMASLLLQYNADIEQKTKDGFTPLLLALREKRVEVAEFLVRMGADIHVVDELQRNTLIYAIRCGSKDL 228
Cdd:PHA02874  126 TFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYAC 205

                         170       180
                  ....*....|....*....|....*.
gi 568954244  229 SVLLLEKGIDFFYKDVFGWTALRYAI 254
Cdd:PHA02874  206 IKLLIDHGNHIMNKCKNGFTPLHNAI 231
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 130-201 3.80e-11

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 67.62  E-value: 3.80e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568954244  130 ATVLLEHGADPNIRDSSGNSALHYAVYNGHQEMASLLLQYNADIEQKTKDGFTPLLLALREKRVEVAEFLVR 201
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
PHA03095 PHA03095
ankyrin-like protein; Provisional
 19-253 8.44e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 65.82  E-value: 8.44e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954244   19 FCDAPQMTVSEFF----FGENPNYPK-YHTTyrPLGHIHRVAAEGDAARMEILLTLGqCNVYHRDRKDRTALH----FAC 89
Cdd:PHA03095   19 LLNASNVTVEEVRrllaAGADVNFRGeYGKT--PLHLYLHYSSEKVKDIVRLLLEAG-ADVNAPERCGFTPLHlylyNAT 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954244   90 VygrLPVVTILVKNNCEIDALDKNHTTPLMK--SVQCWKQKCATVLLEHGADPNIRDSSGNSALHYAVYNGHQEMASLLL 167
Cdd:PHA03095   96 T---LDVIKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVELLRL 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954244  168 QYNADIEQKTKD--GFTPL---LLALReKRVEVAEFLVRMGADIHVVDELQRNTLIYAIRCGSKDLSVL--LLEKGIDFF 240
Cdd:PHA03095  173 LIDAGADVYAVDdrFRSLLhhhLQSFK-PRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISIN 251

                         250
                  ....*....|...
gi 568954244  241 YKDVFGWTALRYA 253
Cdd:PHA03095  252 ARNRYGQTPLHYA 264
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 54-206 1.88e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 65.66  E-value: 1.88e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954244   54 VAAEGDAARMEILLTLGQcNVYHRDRKDRTALHFACVYGRLPVVTILVKNNCEIDALDKNHTTPLMKSVQCWKQKCATVL 133
Cdd:PLN03192  532 VASTGNAALLEELLKAKL-DPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL 610

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568954244  134 --LEHGADPNIrdssGNSALHYAVYNGHQEMASLLLQYNADIEQKTKDGFTPLLLALREKRVEVAEFLVRMGADI 206
Cdd:PLN03192  611 yhFASISDPHA----AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
PHA03095 PHA03095
ankyrin-like protein; Provisional
 66-189 4.80e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 63.51  E-value: 4.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954244   66 LLTLGQCNVYHRDRKDRTALHFACVY--GRLPVVTILVKNNCEIDALDKNHTTPLMKSVQCWKQKCATV--LLEHGADPN 141
Cdd:PHA03095  172 LLIDAGADVYAVDDRFRSLLHHHLQSfkPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISIN 251

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 568954244  142 IRDSSGNSALHYAVYNGHQEMASLLLQYNADIEQKTKDGFTPLLLALR 189
Cdd:PHA03095  252 ARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVR 299
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 24-281 1.96e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 62.00  E-value: 1.96e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954244   24 QMTVSEFFFGENPNYpKYHTTYRPLGHIHRVAAEGDAARMEILLTLgQCNV-----YHRDRKDRTALHFACVYgrlpVVT 98
Cdd:PHA02876   53 QIDIVEEIIQQNPEL-IYITDHKCHSTLHTICIIPNVMDIVISLTL-DCDIildikYASIILNKHKLDEACIH----ILK 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954244   99 ILVKNNcEIDALDKNHTTPLMKSVQCWKQK----CATVLLEHGADPNIRDSSGNSALHYAVYNGHQEMASLLLQYNADIE 174
Cdd:PHA02876  127 EAISGN-DIHYDKINESIEYMKLIKERIQQdellIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVN 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954244  175 QKTKDGFTPLLLALREKRVEVAEFLVRMGADIHVVDElqrnTLIYAIRCGSKDLSVLLLEKGIDFFYKDVFGWTALRYAI 254
Cdd:PHA02876  206 IIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKNDL----SLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHAS 281

                         250       260
                  ....*....|....*....|....*..
gi 568954244  255 EGHCTFRQTLLDFEESLHSNKKDKEPE 281
Cdd:PHA02876  282 QAPSLSRLVPKLLERGADVNAKNIKGE 308
Ank_5 pfam13857
Ankyrin repeats (many copies);
133-187 2.06e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 54.66  E-value: 2.06e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 568954244   133 LLEHG-ADPNIRDSSGNSALHYAVYNGHQEMASLLLQYNADIEQKTKDGFTPLLLA 187
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
82-167 2.38e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.20  E-value: 2.38e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954244    82 RTALHFACVYGRLPVVTilvknnceidaldknhttplmksvqcwkqkcatVLLEHGADPNIRDSSGNSALHYAVYNGHQE 161
Cdd:pfam13637    2 LTALHAAAASGHLELLR---------------------------------LLLEKGADINAVDGNGETALHFAASNGNVE 48


                   ....*.
gi 568954244   162 MASLLL 167
Cdd:pfam13637   49 VLKLLL 54
PHA02798 PHA02798
ankyrin-like protein; Provisional
 94-261 3.26e-09

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 61.00  E-value: 3.26e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954244   94 LPVVTILVKNNCEIDALDKNHTTPLmksvqcwkqkcATVLlehgadPNIRDssgnsalhyavYNGHQEMASLLLQYNADI 173
Cdd:PHA02798   51 TDIVKLFINLGANVNGLDNEYSTPL-----------CTIL------SNIKD-----------YKHMLDIVKILIENGADI 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954244  174 EQKTKDGFTPLLLALREKRV---EVAEFLVRMGADIHVVDELQRNTL-IYAIRCGSKDLSV--LLLEKGIDF-FYKDVFG 246
Cdd:PHA02798  103 NKKNSDGETPLYCLLSNGYInnlEILLFMIENGADTTLLDKDGFTMLqVYLQSNHHIDIEIikLLLEKGVDInTHNNKEK 182

                         170
                  ....*....|....*
gi 568954244  247 WTALryaiegHCTFR 261
Cdd:PHA02798  183 YDTL------HCYFK 191
Ank_4 pfam13637
Ankyrin repeats (many copies);
147-200 3.81e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.82  E-value: 3.81e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 568954244   147 GNSALHYAVYNGHQEMASLLLQYNADIEQKTKDGFTPLLLALREKRVEVAEFLV 200
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 96-243 3.88e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 60.66  E-value: 3.88e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954244   96 VVTILVKNNCEIDALDKNH-TTPLMKSVQCWKQKCATVLLEHGADPNIRDSSGNSALHYAVYNGHQEMASLLLQYNADIE 174
Cdd:PHA02878  149 ITKLLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTD 228

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568954244  175 QKTKDGFTPLLLAL-REKRVEVAEFLVRMGADIHVVDELQRNTLIY-AIRcgSKDLSVLLLEKGIDF----FYKD 243
Cdd:PHA02878  229 ARDKCGNTPLHISVgYCKDYDILKLLLEHGVDVNAKSYILGLTALHsSIK--SERKLKLLLEYGADInslnSYKL 301
PHA03095 PHA03095
ankyrin-like protein; Provisional
 45-206 6.34e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 60.04  E-value: 6.34e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954244   45 YRPLGHIHRVAAEGDAARMEILLTLGqCNVYHRDRKDRTALHFACVYG--RLPVVTILVKNNCEIDALDKNHTTPLMKSV 122
Cdd:PHA03095  187 FRSLLHHHLQSFKPRARIVRELIRAG-CDPAATDMLGNTPLHSMATGSscKRSLVLPLLIAGISINARNRYGQTPLHYAA 265

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954244  123 qCWKQKCATV-LLEHGADPNIRDSSGNSALHYAVYNGHQEMASLLLQYNADIE--QKTKDGFTPLLLA--LREKRVEVAE 197
Cdd:PHA03095  266 -VFNNPRACRrLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAEtvAATLNTASVAGGDipSDATRLCVAK 344


                  ....*....
gi 568954244  198 FLVRMGADI 206
Cdd:PHA03095  345 VVLRGAFSL 353
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 54-169 2.15e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 58.76  E-value: 2.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954244   54 VAAEGDAARMEILLTLG-QCNVyhRDRKDRTALHFACVYGRLPVVtilvknnceidaldknhttplmksvqcwkqkcaTV 132
Cdd:PTZ00322   89 LAASGDAVGARILLTGGaDPNC--RDYDGRTPLHIACANGHVQVV---------------------------------RV 133

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 568954244  133 LLEHGADPNIRDSSGNSALHYAVYNGHQEMASLLLQY 169
Cdd:PTZ00322  134 LLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 97-255 1.09e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 55.77  E-value: 1.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954244   97 VTILVKNNCEIDALDKNHTTPLMKSVQCWKQKCATVLLEHGADPN-IRDSSGNSALHYAVYNGHQEMASLLLQYNADIEQ 175
Cdd:PHA02875   51 IKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDI 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954244  176 KTKDGFTPLLLALREKRVEVAEFLVRMGADIHVVDELQRNTLIYAIRCGSKDLSVLLLEKG--IDFFYK--DVfgwTALR 251
Cdd:PHA02875  131 PNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGanIDYFGKngCV---AALC 207


                  ....
gi 568954244  252 YAIE 255
Cdd:PHA02875  208 YAIE 211
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 100-259 1.23e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 55.83  E-value: 1.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954244  100 LVKNNCEIDALDKNHTTPLMKSVQCWKQKCATVLLEHGADPNIRDSSGNSALHYAVYNGH-----QEMASLLLQYNADIE 174
Cdd:PHA03100   21 IIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVN 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954244  175 QKTKDGFTPLLLALREKRvevaeflvrmgadihvvdelqrntliyaircGSKDLSVLLLEKGIDFFYKDVFGWTALRYAI 254
Cdd:PHA03100  101 APDNNGITPLLYAISKKS-------------------------------NSYSIVEYLLDNGANVNIKNSDGENLLHLYL 149


                  ....*
gi 568954244  255 EGHCT 259
Cdd:PHA03100  150 ESNKI 154
PHA03095 PHA03095
ankyrin-like protein; Provisional
 63-211 1.86e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 55.42  E-value: 1.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954244   63 MEILLTLGqCNVYHRDRKDRTALHfACVYG---RLPVVTILVKNNCEIDALDKNHTTPL---MKSVQC------------ 124
Cdd:PHA03095  100 IKLLIKAG-ADVNAKDKVGRTPLH-VYLSGfniNPKVIRLLLRKGADVNALDLYGMTPLavlLKSRNAnvellrllidag 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954244  125 ----------------------WKQKCATVLLEHGADPNIRDSSGNSALHYAVyNGHQEMASLLLQY---NADIEQKTKD 179
Cdd:PHA03095  178 advyavddrfrsllhhhlqsfkPRARIVRELIRAGCDPAATDMLGNTPLHSMA-TGSSCKRSLVLPLliaGISINARNRY 256

                         170       180       190
                  ....*....|....*....|....*....|..
gi 568954244  180 GFTPLLLALREKRVEVAEFLVRMGADIHVVDE 211
Cdd:PHA03095  257 GQTPLHYAAVFNNPRACRRLIALGADINAVSS 288
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 133-257 3.31e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 54.87  E-value: 3.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954244  133 LLEHGADPNIRDSSGNSALHYAVYNGHQEMASLLLQYNADIEQKTKDGFTPLLLALREKRVEVAEFLVRMGA--DIHVVD 210
Cdd:PLN03192  544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASisDPHAAG 623

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 568954244  211 ELqrntLIYAIRCGskDLSVL--LLEKGIDFFYKDVFGWTALRYAI-EGH 257
Cdd:PLN03192  624 DL----LCTAAKRN--DLTAMkeLLKQGLNVDSEDHQGATALQVAMaEDH 667
Ank_5 pfam13857
Ankyrin repeats (many copies);
66-118 6.17e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 47.73  E-value: 6.17e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 568954244    66 LLTLGQCNVYHRDRKDRTALHFACVYGRLPVVTILVKNNCEIDALDKNHTTPL 118
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 55-201 5.33e-06

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: 50.78  E-value: 5.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954244   55 AAEGDAARMEILLTLGQCNVYHRDRKDRTALHFACVYGRLPVVTILVKNNCE------------------IDALDKNhtt 116
Cdd:cd22192    25 AKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElvnepmtsdlyqgetalhIAVVNQN--- 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954244  117 plMKSVQCWKQKCATV---------------------------------------LLEHGADPNIRDSSGNSALHYAVYN 157
Cdd:cd22192   102 --LNLVRELIARGADVvspratgtffrpgpknliyygehplsfaacvgneeivrlLIEHGADIRAQDSLGNTVLHILVLQ 179

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568954244  158 GHQ----EMASLLLQYNADIEQKT------KDGFTPLLLALREKRVEVAEFLVR 201
Cdd:cd22192   180 PNKtfacQMYDLILSYDKEDDLQPldlvpnNQGLTPFKLAAKEGNIVMFQHLVQ 233
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 66-206 5.74e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 50.83  E-value: 5.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954244   66 LLTLGqCNVYHRDRKDRTALHFACVYGRLPVVTILVKNNCEIDALDKNHTTPLMKSVqCWKQKCATV--LLEHGADPNIR 143
Cdd:PHA02876  361 LLELG-ANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAL-CGTNPYMSVktLIDRGANVNSK 438

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568954244  144 DSSGNSALHYAVYNGHQ-EMASLLLQYNADIEQKTKDGFTPLLLALREKrvEVAEFLVRMGADI 206
Cdd:PHA02876  439 NKDLSTPLHYACKKNCKlDVIEMLLDNGADVNAINIQNQYPLLIALEYH--GIVNILLHYGAEL 500
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 147-178 7.78e-06

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: 43.82  E-value: 7.78e-06
                           10        20        30
                   ....*....|....*....|....*....|...
gi 568954244   147 GNSALHYAVY-NGHQEMASLLLQYNADIEQKTK 178
Cdd:pfam00023    2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 133-248 1.02e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 47.89  E-value: 1.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954244  133 LLEHGADPNIRDSSGN-SALH-YAVYNGH--QEMASLLLQYNADIEQKTKDGFTPLLLALR--EKRVEVAEFLVRMGADI 206
Cdd:PHA02859   72 LIENGADVNFKTRDNNlSALHhYLSFNKNvePEILKILIDSGSSITEEDEDGKNLLHMYMCnfNVRINVIKLLIDSGVSF 151

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 568954244  207 HVVDELQRNTL-IYAIRCGSKDLSVLLLEKGIDFFYKDVFGWT 248
Cdd:PHA02859  152 LNKDFDNNNILySYILFHSDKKIFDFLTSLGIDINETNKSGYN 194
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 147-174 1.95e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.57  E-value: 1.95e-05
                            10        20
                    ....*....|....*....|....*...
gi 568954244    147 GNSALHYAVYNGHQEMASLLLQYNADIE 174
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADIN 29
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 97-257 2.40e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 48.91  E-value: 2.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954244   97 VTILVKNNCEIDALDKNHTTPLMKSVQCWKQKCATV-LLEHGADPNIRDSSGNSALHYAVYNGHQEMASLLLQYNADIEQ 175
Cdd:PHA02876  324 IRTLIMLGADVNAADRLYITPLHQASTLDRNKDIVItLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEA 403

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954244  176 KTKDGFTPLLLALREKRVEVA-EFLVRMGADIHVVDELQRNTLIYAIRCGSK-DLSVLLLEKGIDFFYKDVFGWTALRYA 253
Cdd:PHA02876  404 LSQKIGTALHFALCGTNPYMSvKTLIDRGANVNSKNKDLSTPLHYACKKNCKlDVIEMLLDNGADVNAINIQNQYPLLIA 483


                  ....
gi 568954244  254 IEGH 257
Cdd:PHA02876  484 LEYH 487
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 80-201 1.16e-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: 46.41  E-value: 1.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954244   80 KDRTALHFACVYGRLPVVTILVKNNCEIDALD-----KNHTTPL-------MKSVQCWKQ-KCATVLLEHGADP---NIR 143
Cdd:cd21882    72 QGQTALHIAIENRNLNLVRLLVENGADVSARAtgrffRKSPGNLfyfgelpLSLAACTNQeEIVRLLLENGAQPaalEAQ 151

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568954244  144 DSSGNSALHYAVYNGHQ---------EMASLLLQYNADI-------EQKTKDGFTPLLLALREKRVEVAEFLVR 201
Cdd:cd21882   152 DSLGNTVLHALVLQADNtpensafvcQMYNLLLSYGAHLdptqqleEIPNHQGLTPLKLAAVEGKIVMFQHILQ 225
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 169-238 1.89e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 45.72  E-value: 1.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954244  169 YNADIEQ-----KTKDGF---------TPLLLALREKRVEVAEFLVRMGADIHVVDELQRNTLIYAIRCGSKDLSVLLLE 234
Cdd:PHA02874   10 YSGDIEAiekiiKNKGNCinisvdettTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLID 89


                  ....
gi 568954244  235 KGID 238
Cdd:PHA02874   90 NGVD 93
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 107-301 2.90e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.05  E-value: 2.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954244  107 IDALDKNHTTPLMKSVQCWK-QKCATVLLEHGADPNIRDSSGNSALHYAVYNGHQ-EMASLLLQYNADIEQKTKDGFTPL 184
Cdd:PHA02876  266 VNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYDtENIRTLIMLGADVNAADRLYITPL 345

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954244  185 LLA-LREKRVEVAEFLVRMGADIHVVDELQRNTLIYAIRCGSKDLSVLLLEKGIDFFYKDVFGWTALRYAIEGHCTFR-- 261
Cdd:PHA02876  346 HQAsTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMsv 425

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 568954244  262 QTLLDFEESLHSNKKDKEPELQVEPSTSC---ILAKQIDAGND 301
Cdd:PHA02876  426 KTLIDRGANVNSKNKDLSTPLHYACKKNCkldVIEMLLDNGAD 468
Ank_5 pfam13857
Ankyrin repeats (many copies);
204-253 3.00e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.02  E-value: 3.00e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 568954244   204 ADIHVVDELQRNTLIYAIRCGSKDLSVLLLEKGIDFFYKDVFGWTALRYA 253
Cdd:pfam13857    7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 121-250 5.97e-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: 44.23  E-value: 5.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954244  121 SVQCWKqkcaTVLLEHGADPNIRDSSGNSALHYAVYNGHQEMASLLLQYNADI--EQKTKD---GFTPLLLALREKRVEV 195
Cdd:cd22192    29 DVQAIK----KLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELvnEPMTSDlyqGETALHIAVVNQNLNL 104

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568954244  196 AEFLVRMGADIH------VVDELQRNTLIY--------AIRCGSKDLSVLLLEKGIDFFYKDVFGWTAL 250
Cdd:cd22192   105 VRELIARGADVVspratgTFFRPGPKNLIYygehplsfAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 57-183 1.28e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 41.73  E-value: 1.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954244   57 EGDAARMEIL--LTLGQCNVYHRDRKDR-TALHFACVYGR---LPVVTILVKNNCEIDALDKNHTTPLMKSVQCWKQKCA 130
Cdd:PHA02859   60 EKDKVNVEILkfLIENGADVNFKTRDNNlSALHHYLSFNKnvePEILKILIDSGSSITEEDEDGKNLLHMYMCNFNVRIN 139

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568954244  131 TV--LLEHGADPNIRDSSGNSALH-YAVYNGHQEMASLLLQYNADIEQKTKDGFTP 183
Cdd:PHA02859  140 VIklLIDSGVSFLNKDFDNNNILYsYILFHSDKKIFDFLTSLGIDINETNKSGYNC 195
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 179-208 1.42e-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: 37.18  E-value: 1.42e-03
                            10        20        30
                    ....*....|....*....|....*....|
gi 568954244    179 DGFTPLLLALREKRVEVAEFLVRMGADIHV 208
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 132-255 1.61e-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: 42.76  E-value: 1.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954244   132 VLLEHGADPnirdSSGNSALHYA---VYNGHQEMASLLLQYNAD-------IEQKTKD---GFTPLLLALREKRVEVAEF 198
Cdd:TIGR00870   71 LLLNLSCRG----AVGDTLLHAIsleYVDAVEAILLHLLAAFRKsgplelaNDQYTSEftpGITALHLAAHRQNYEIVKL 146

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568954244   199 LVRMGADIHVV---DEL---QRNTLIY-------AIRC-GSKDLSVLLLEKGIDFFYKDVFGWTALRYAIE 255
Cdd:TIGR00870  147 LLERGASVPARacgDFFvksQGVDSFYhgesplnAAAClGSPSIVALLSEDPADILTADSLGNTLLHLLVM 217
PHA02917 PHA02917
ankyrin-like protein; Provisional
 111-200 1.61e-03

ankyrin-like protein; Provisional


Pssm-ID: 165231 [Multi-domain]  Cd Length: 661  Bit Score: 42.68  E-value: 1.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954244  111 DKNHTTPLMKSVQcwkqkcatVLLEHGADPNIRDSSGNSALHYAVYNGHQEMASLLLQYNADIEQKTKDGFTPLLLALRE 190
Cdd:PHA02917  424 DMSYACPILSTIN--------ICLPYLKDINMIDKRGETLLHKAVRYNKQSLVSLLLESGSDVNIRSNNGYTCIAIAINE 495

                          90
                  ....*....|.
gi 568954244  191 KR-VEVAEFLV 200
Cdd:PHA02917  496 SRnIELLKMLL 506
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 179-208 1.65e-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: 37.24  E-value: 1.65e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 568954244   179 DGFTPLLLALREKRVEVAEFLVRMGADIHV 208
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02946 PHA02946
ankyin-like protein; Provisional
 111-215 1.71e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 42.35  E-value: 1.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954244  111 DKNHTTPLMKSVQCWKQKCATVLLEHGADPNIRDSSGNSALHYAVYNGHQ--EMASLLLQYNADIEQKTKDGFTPLLLAL 188
Cdd:PHA02946   69 DDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEviERINLLVQYGAKINNSVDEEGCGPLLAC 148

                          90       100
                  ....*....|....*....|....*..
gi 568954244  189 REKRVEVAEFLVRMGADIHVVDELQRN 215
Cdd:PHA02946  149 TDPSERVFKKIMSIGFEARIVDKFGKN 175
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 114-189 2.18e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 41.89  E-value: 2.18e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568954244  114 HTTPLMKSVQCWKQKCATVLLEHGADPNIRDSSGN-SALHYAVYNGHQEMASLLLQYNADIEQKTKDGFTPLLLALR 189
Cdd:PHA02884   70 KTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKiTPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPIELALM 146
Ank_4 pfam13637
Ankyrin repeats (many copies);
182-233 2.80e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 37.25  E-value: 2.80e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 568954244   182 TPLLLALREKRVEVAEFLVRMGADIHVVDELQRNTLIYAIRCGSKDLSVLLL 233
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
213-254 4.23e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.48  E-value: 4.23e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 568954244   213 QRNTLIYAIRCGSKDLSVLLLEKGIDFFYKDVFGWTALRYAI 254
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAA 42
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 82-109 5.02e-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: 5.02e-03
                           10        20
                   ....*....|....*....|....*...
gi 568954244    82 RTALHFACVYGRLPVVTILVKNNCEIDA 109
Cdd:pfam13606    3 NTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 147-173 5.07e-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: 5.07e-03
                           10        20
                   ....*....|....*....|....*..
gi 568954244   147 GNSALHYAVYNGHQEMASLLLQYNADI 173
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADI 28
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 144-236 6.63e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 38.70  E-value: 6.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568954244  144 DSSGNSALHYAVYNGH---QEMASLLLQYNADIE-QKTKDGFTPLLLALREKRVEVAEFLVRM-GADIHVVDELQRNTLI 218
Cdd:PHA02736   52 NRHGKQCVHIVSNPDKadpQEKLKLLMEWGADINgKERVFGNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYY 131

                          90
                  ....*....|....*...
gi 568954244  219 YAIRCGSKDLSVLLLEKG 236
Cdd:PHA02736  132 VACERHDAKMMNILRAKG 149
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 82-112 7.95e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 35.34  E-value: 7.95e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 568954244    82 RTALHFACV-YGRLPVVTILVKNNCEIDALDK 112
Cdd:pfam00023    3 NTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
 
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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