NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|363583286|sp|E5RJM6|]
View 

RecName: Full=Ankyrin repeat domain-containing protein 65

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
44-359 2.50e-37

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 137.01  E-value: 2.50e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286  44 HLLQAVWRGPAGLVTQLLRQGASVEERDHAGRTPLHLAVLRGHAPLVRLLLQRGAPVGAVDRAGRTALHEAAWHGHSRVA 123
Cdd:COG0666   24 LLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIV 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286 124 ELLLQRGASAAARSGTGLTPLHWAAALGHTLLAARLLEApgpGpAAAEAEDARGWTAAHWAAAGGRLAVlellaaggagl 203
Cdd:COG0666  104 KLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA---G-ADVNAQDNDGNTPLHLAAANGNLEI----------- 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286 204 dgallvaaaagrgaalrfllargarvdardgagatalglaaalgrsqdIEVLLGHGADPGIRDRHGRSALHRAAARGHLL 283
Cdd:COG0666  169 ------------------------------------------------VKLLLEAGADVNARDNDGETPLHLAAENGHLE 200

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 363583286 284 AVQLLVTQGAEVDARDTLGLTPLHHASREGHVEVAGCLLDRGAQVDATGWLRKTPLHLAAERGHGPTVGLLLSRGA 359
Cdd:COG0666  201 IVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALL 276
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
44-359 2.50e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 137.01  E-value: 2.50e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286  44 HLLQAVWRGPAGLVTQLLRQGASVEERDHAGRTPLHLAVLRGHAPLVRLLLQRGAPVGAVDRAGRTALHEAAWHGHSRVA 123
Cdd:COG0666   24 LLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIV 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286 124 ELLLQRGASAAARSGTGLTPLHWAAALGHTLLAARLLEApgpGpAAAEAEDARGWTAAHWAAAGGRLAVlellaaggagl 203
Cdd:COG0666  104 KLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA---G-ADVNAQDNDGNTPLHLAAANGNLEI----------- 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286 204 dgallvaaaagrgaalrfllargarvdardgagatalglaaalgrsqdIEVLLGHGADPGIRDRHGRSALHRAAARGHLL 283
Cdd:COG0666  169 ------------------------------------------------VKLLLEAGADVNARDNDGETPLHLAAENGHLE 200

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 363583286 284 AVQLLVTQGAEVDARDTLGLTPLHHASREGHVEVAGCLLDRGAQVDATGWLRKTPLHLAAERGHGPTVGLLLSRGA 359
Cdd:COG0666  201 IVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALL 276
PHA03095 PHA03095
ankyrin-like protein; Provisional
 57-365 1.50e-19

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 90.08  E-value: 1.50e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286  57 VTQLLRQGASVEERDHAGRTPLHLAVLRGHAPL---VRLLLQRGAPVGAVDRAGRTALHEAAWHGHS-RVAELLLQRGAS 132
Cdd:PHA03095  30 VRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVkdiVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKAGAD 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286 133 AAARSGTGLTPLHwaaalghTLLAarlleapgpGPAAAEaedargwtaahwaaaggrlavlellaaggagldgallvaaa 212
Cdd:PHA03095 110 VNAKDKVGRTPLH-------VYLS---------GFNINP----------------------------------------- 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286 213 agrgAALRFLLARGARVDARDGAGATALGLAAalgRSQDIEV-----LLGHGADPGIRDRHGRSALH------RAAARgh 281
Cdd:PHA03095 133 ----KVIRLLLRKGADVNALDLYGMTPLAVLL---KSRNANVellrlLIDAGADVYAVDDRFRSLLHhhlqsfKPRAR-- 203

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286 282 llAVQLLVTQGAEVDARDTLGLTPLHHASREGHVE--VAGCLLDRGAQVDATGWLRKTPLHLAAERGHGPTVGLLLSRGA 359
Cdd:PHA03095 204 --IVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGA 281


                 ....*.
gi 363583286 360 SPTLRT 365
Cdd:PHA03095 282 DINAVS 287
Ank_2 pfam12796
Ankyrin repeats (3 copies);
273-364 2.76e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 82.09  E-value: 2.76e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286  273 LHRAAARGHLLAVQLLVTQGAEVDARDTLGLTPLHHASREGHVEVAGCLLDRgAQVDATGwLRKTPLHLAAERGHGPTVG 352
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|..
gi 363583286  353 LLLSRGASPTLR 364
Cdd:pfam12796  79 LLLEKGADINVK 90
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 72-145 1.34e-08

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 56.56  E-value: 1.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286  72 HAGRTPLHLAVLRGHAPLVRLLLQRGAPV------GAVDRAGRTAL-----HE---AAWHGHSRVAELLLQRGASAAARS 137
Cdd:cd22192   87 YQGETALHIAVVNQNLNLVRELIARGADVvspratGTFFRPGPKNLiyygeHPlsfAACVGNEEIVRLLIEHGADIRAQD 166


                 ....*...
gi 363583286 138 GTGLTPLH 145
Cdd:cd22192  167 SLGNTVLH 174
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 74-98 2.24e-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: 41.03  E-value: 2.24e-05
                           10        20
                   ....*....|....*....|....*
gi 363583286    74 GRTPLHLAVLRGHAPLVRLLLQRGA 98
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGA 26
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 266-360 6.71e-05

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 45.07  E-value: 6.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286  266 DRHGRSALHRAAARG-HLLAVQLLVTQGAEVDARDTLgltpLHHASREGHVEVAGCLLDRGAQVDATGWLR--------- 335
Cdd:TIGR00870  49 DRLGRSALFVAAIENeNLELTELLLNLSCRGAVGDTL----LHAISLEYVDAVEAILLHLLAAFRKSGPLElandqytse 124

                          90       100
                  ....*....|....*....|....*....
gi 363583286  336 ----KTPLHLAAERGHGPTVGLLLSRGAS 360
Cdd:TIGR00870 125 ftpgITALHLAAHRQNYEIVKLLLERGAS 153
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
44-359 2.50e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 137.01  E-value: 2.50e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286  44 HLLQAVWRGPAGLVTQLLRQGASVEERDHAGRTPLHLAVLRGHAPLVRLLLQRGAPVGAVDRAGRTALHEAAWHGHSRVA 123
Cdd:COG0666   24 LLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIV 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286 124 ELLLQRGASAAARSGTGLTPLHWAAALGHTLLAARLLEApgpGpAAAEAEDARGWTAAHWAAAGGRLAVlellaaggagl 203
Cdd:COG0666  104 KLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA---G-ADVNAQDNDGNTPLHLAAANGNLEI----------- 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286 204 dgallvaaaagrgaalrfllargarvdardgagatalglaaalgrsqdIEVLLGHGADPGIRDRHGRSALHRAAARGHLL 283
Cdd:COG0666  169 ------------------------------------------------VKLLLEAGADVNARDNDGETPLHLAAENGHLE 200

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 363583286 284 AVQLLVTQGAEVDARDTLGLTPLHHASREGHVEVAGCLLDRGAQVDATGWLRKTPLHLAAERGHGPTVGLLLSRGA 359
Cdd:COG0666  201 IVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALL 276
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
44-330 3.17e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 136.62  E-value: 3.17e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286  44 HLLQAVWRGPAGLVTQLLRQGASVEERDHAGRTPLHLAVLRGHAPLVRLLLQRGAPVGAVDRAGRTALHEAAWHGHSRVA 123
Cdd:COG0666   57 LLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIV 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286 124 ELLLQRGASAAARSGTGLTPLHWAAALGHTLLAARLLEApgpgPAAAEAEDARGWTAAHWAAAGGRLAVlellaaggagl 203
Cdd:COG0666  137 KLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEA----GADVNARDNDGETPLHLAAENGHLEI----------- 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286 204 dgallvaaaagrgaalrfllargarvdardgagatalglaaalgrsqdIEVLLGHGADPGIRDRHGRSALHRAAARGHLL 283
Cdd:COG0666  202 ------------------------------------------------VKLLLEAGADVNAKDNDGKTALDLAAENGNLE 233

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 363583286 284 AVQLLVTQGAEVDARDTLGLTPLHHASREGHVEVAGCLLDRGAQVDA 330
Cdd:COG0666  234 IVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAA 280
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
56-373 5.32e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 133.16  E-value: 5.32e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286  56 LVTQLLRQGASVEERDHAGRTPLHLAVLRGHAPLVRLLLQRGAPVGAVDRAGRTALHEAAWHGHSRVAELLLQRGASAAA 135
Cdd:COG0666    3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286 136 RSGTGLTPLHWAAALGHTLLAARLLEAPgpgpAAAEAEDARGWTAAHWAAAGGRLAVlellaaggagldgallvaaaagr 215
Cdd:COG0666   83 KDDGGNTLLHAAARNGDLEIVKLLLEAG----ADVNARDKDGETPLHLAAYNGNLEI----------------------- 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286 216 gaalrfllargarvdardgagatalglaaalgrsqdIEVLLGHGADPGIRDRHGRSALHRAAARGHLLAVQLLVTQGAEV 295
Cdd:COG0666  136 ------------------------------------VKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADV 179

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 363583286 296 DARDTLGLTPLHHASREGHVEVAGCLLDRGAQVDATGWLRKTPLHLAAERGHGPTVGLLLSRGASPTLRTQWAEVAQM 373
Cdd:COG0666  180 NARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALL 257
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
40-192 5.29e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 130.84  E-value: 5.29e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286  40 QGWGHLLQAVWRGPAGLVTQLLRQGASVEERDHAGRTPLHLAVLRGHAPLVRLLLQRGAPVGAVDRAGRTALHEAAWHGH 119
Cdd:COG0666   86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGN 165

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 363583286 120 SRVAELLLQRGASAAARSGTGLTPLHWAAALGHTLLAARLLEApgpgPAAAEAEDARGWTAAHWAAAGGRLAV 192
Cdd:COG0666  166 LEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA----GADVNAKDNDGKTALDLAAENGNLEI 234
PHA03095 PHA03095
ankyrin-like protein; Provisional
 57-365 1.50e-19

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 90.08  E-value: 1.50e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286  57 VTQLLRQGASVEERDHAGRTPLHLAVLRGHAPL---VRLLLQRGAPVGAVDRAGRTALHEAAWHGHS-RVAELLLQRGAS 132
Cdd:PHA03095  30 VRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVkdiVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKAGAD 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286 133 AAARSGTGLTPLHwaaalghTLLAarlleapgpGPAAAEaedargwtaahwaaaggrlavlellaaggagldgallvaaa 212
Cdd:PHA03095 110 VNAKDKVGRTPLH-------VYLS---------GFNINP----------------------------------------- 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286 213 agrgAALRFLLARGARVDARDGAGATALGLAAalgRSQDIEV-----LLGHGADPGIRDRHGRSALH------RAAARgh 281
Cdd:PHA03095 133 ----KVIRLLLRKGADVNALDLYGMTPLAVLL---KSRNANVellrlLIDAGADVYAVDDRFRSLLHhhlqsfKPRAR-- 203

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286 282 llAVQLLVTQGAEVDARDTLGLTPLHHASREGHVE--VAGCLLDRGAQVDATGWLRKTPLHLAAERGHGPTVGLLLSRGA 359
Cdd:PHA03095 204 --IVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGA 281


                 ....*.
gi 363583286 360 SPTLRT 365
Cdd:PHA03095 282 DINAVS 287
Ank_2 pfam12796
Ankyrin repeats (3 copies);
273-364 2.76e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 82.09  E-value: 2.76e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286  273 LHRAAARGHLLAVQLLVTQGAEVDARDTLGLTPLHHASREGHVEVAGCLLDRgAQVDATGwLRKTPLHLAAERGHGPTVG 352
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|..
gi 363583286  353 LLLSRGASPTLR 364
Cdd:pfam12796  79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
45-132 3.83e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 78.62  E-value: 3.83e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286   45 LLQAVWRGPAGLVTQLLRQGASVEERDHAGRTPLHLAVLRGHAPLVRLLLQRGApvGAVDRAGRTALHEAAWHGHSRVAE 124
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVK 78


                  ....*...
gi 363583286  125 LLLQRGAS 132
Cdd:pfam12796  79 LLLEKGAD 86
Ank_2 pfam12796
Ankyrin repeats (3 copies);
78-161 7.09e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.46  E-value: 7.09e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286   78 LHLAVLRGHAPLVRLLLQRGAPVGAVDRAGRTALHEAAWHGHSRVAELLLQRGasAAARSGTGLTPLHWAAALGHTLLAA 157
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA--DVNLKDNGRTALHYAARSGHLEIVK 78


                  ....
gi 363583286  158 RLLE 161
Cdd:pfam12796  79 LLLE 82
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 60-359 1.83e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 78.18  E-value: 1.83e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286  60 LLRQGASVEERDHAGRTPLHLAVLRGHAPLVRLLLQRGAPVGAVDRAGRTALH-----------EAAWHGHSRVAE---- 124
Cdd:PHA02876 164 LLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLEcavdsknidtiKAIIDNRSNINKndls 243

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286 125 --------------LLLQRGASAAARSGTGLTPLHWAA-ALGHTLLAARLLEAPgpgpAAAEAEDARGWTAAHWAAAGGr 189
Cdd:PHA02876 244 llkairnedletslLLYDAGFSVNSIDDCKNTPLHHASqAPSLSRLVPKLLERG----ADVNAKNIKGETPLYLMAKNG- 318

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286 190 lavlellaaggagldgallvaaaaGRGAALRFLLARGARVDARDGAGATALGLAAALGRSQDIEV-LLGHGADPGIRDRH 268
Cdd:PHA02876 319 ------------------------YDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKDIVItLLELGANVNARDYC 374

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286 269 GRSALHRAAARGHLLAVQLLVTQGAEVDARDTLGLTPLHHA--SREGHVEVAgCLLDRGAQVDATGWLRKTPLHLAAERG 346
Cdd:PHA02876 375 DKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlcGTNPYMSVK-TLIDRGANVNSKNKDLSTPLHYACKKN 453

                        330
                 ....*....|....
gi 363583286 347 HGPTV-GLLLSRGA 359
Cdd:PHA02876 454 CKLDViEMLLDNGA 467
Ank_2 pfam12796
Ankyrin repeats (3 copies);
252-331 2.62e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.83  E-value: 2.62e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286  252 IEVLLGHGADPGIRDRHGRSALHRAAARGHLLAVQLLVTQgAEVDARDTlGLTPLHHASREGHVEVAGCLLDRGAQVDAT 331
Cdd:pfam12796  13 VKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINVK 90
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 219-361 3.46e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 70.68  E-value: 3.46e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286 219 LRFLLARGARVDARDGAGATALGLAAALGRSQDI-EVLLGHGADPGIRDRHGRSALHRAAARGHLLAVQLLVTQGAEVDA 297
Cdd:PHA02878 150 TKLLLSYGADINMKDRHKGNTALHYATENKDQRLtELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDA 229

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 363583286 298 RDTLGLTPLHHA-SREGHVEVAGCLLDRGAQVDATGWLRK-TPLHLAAergHGPTV-GLLLSRGASP 361
Cdd:PHA02878 230 RDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSYILGlTALHSSI---KSERKlKLLLEYGADI 293
Ank_2 pfam12796
Ankyrin repeats (3 copies);
111-233 3.75e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 62.06  E-value: 3.75e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286  111 LHEAAWHGHSRVAELLLQRGASAAARSGTGLTPLHWAAALGHTLLAARLLEAPGPGpaaaeaEDARGWTAAHWAAAGGRL 190
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN------LKDNGRTALHYAARSGHL 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 363583286  191 AVlellaaggagldgallvaaaagrgaaLRFLLARGARVDARD 233
Cdd:pfam12796  75 EI--------------------------VKLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 45-186 4.11e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 67.36  E-value: 4.11e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286  45 LLQAVWRGP---AGLVTQLLRQGASVEERDHAGRTPLHLAVLRGHAP--LVRLLLQRGAPVGAVDRAGRTALHEAA--WH 117
Cdd:PHA03095 120 PLHVYLSGFninPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANveLLRLLIDAGADVYAVDDRFRSLLHHHLqsFK 199

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 363583286 118 GHSRVAELLLQRGASAAARSGTGLTPLHWAAALG--HTLLAARLLEApgpgPAAAEAEDARGWTAAHWAAA 186
Cdd:PHA03095 200 PRARIVRELIRAGCDPAATDMLGNTPLHSMATGSscKRSLVLPLLIA----GISINARNRYGQTPLHYAAV 266
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 54-147 8.24e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 66.44  E-value: 8.24e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286  54 AGLVTQLLRQGASVEERD-HAGRTPLHLAVLRGHAPLVRLLLQRGAPVGAVDRAGRTALHEAAWHGHSRVAELLLQRGAS 132
Cdd:PHA02878 147 AEITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAS 226

                         90
                 ....*....|....*
gi 363583286 133 AAARSGTGLTPLHWA 147
Cdd:PHA02878 227 TDARDKCGNTPLHIS 241
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 252-358 2.17e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 64.98  E-value: 2.17e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286 252 IEVLLGHGADPGIRDRHGRSALHRAAARGHLLAVQLLVTQGAEVDARDTLGLTPLHHASREGHVEVAGCLLDRGAQVDAT 331
Cdd:PHA02874 107 IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVK 186

                         90       100
                 ....*....|....*....|....*..
gi 363583286 332 GWLRKTPLHLAAERGHGPTVGLLLSRG 358
Cdd:PHA02874 187 DNNGESPLHNAAEYGDYACIKLLIDHG 213
Ank_4 pfam13637
Ankyrin repeats (many copies);
74-127 2.19e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.44  E-value: 2.19e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 363583286   74 GRTPLHLAVLRGHAPLVRLLLQRGAPVGAVDRAGRTALHEAAWHGHSRVAELLL 127
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 60-144 2.38e-11

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 65.30  E-value: 2.38e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286  60 LLRQGASVEERDHAGRTPLHLAVLRGHAPLVRLLLQRGAPVGAVDRAGRTALHEAAWHGHSRVAELLLQR-------GAS 132
Cdd:PTZ00322 101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHsqchfelGAN 180

                         90
                 ....*....|..
gi 363583286 133 AAARSGTGLTPL 144
Cdd:PTZ00322 181 AKPDSFTGKPPS 192
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 277-356 3.39e-11

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 64.92  E-value: 3.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286 277 AARGHLLAVQLLVTQGAEVDARDTLGLTPLHHASREGHVEVAGCLLDRGAQVDATGWLRKTPLHLAAERGHGPTVGLLLS 356
Cdd:PTZ00322  90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 249-363 1.84e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 62.32  E-value: 1.84e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286 249 SQDIEVLLGHGADPGIRDRHGRSALHRAAARGHLLAVQLLVTQGAEVDarDTL---GLTPLHHASREGHVEVAGCLLDRG 325
Cdd:PHA02875  48 SEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFAD--DVFykdGMTPLHLATILKKLDIMKLLIARG 125

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 363583286 326 AQVDATGWLRKTPLHLAAERGHGPTVGLLLSRGASPTL 363
Cdd:PHA02875 126 ADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDI 163
PHA03095 PHA03095
ankyrin-like protein; Provisional
 54-144 2.45e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 61.96  E-value: 2.45e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286  54 AGLVTQLLRQGASVEERDHAGRTPLHLAVLRG--HAPLVRLLLQRGAPVGAVDRAGRTALHEAAWHGHSRVAELLLQRGA 131
Cdd:PHA03095 202 ARIVRELIRAGCDPAATDMLGNTPLHSMATGSscKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGA 281

                         90
                 ....*....|...
gi 363583286 132 SAAARSGTGLTPL 144
Cdd:PHA03095 282 DINAVSSDGNTPL 294
Ank_4 pfam13637
Ankyrin repeats (many copies);
269-322 4.53e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.97  E-value: 4.53e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 363583286  269 GRSALHRAAARGHLLAVQLLVTQGAEVDARDTLGLTPLHHASREGHVEVAGCLL 322
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 23-188 9.71e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 60.65  E-value: 9.71e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286  23 LDSEEALGTRTEGPSVVQGWGHLLQAVWRGPAGLVTQLLRQGASVEERDHAGRTPLHLAVLRGHAPLVRLLLQRGAPVGA 102
Cdd:PLN03192 507 LNVGDLLGDNGGEHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHI 586

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286 103 VDRAGRTALHEAAWHGHSRVAELLLQRGASAAARSGTGLTPLhwaAALGHTLLAARLLEAPGpgpAAAEAEDARGWTAAH 182
Cdd:PLN03192 587 RDANGNTALWNAISAKHHKIFRILYHFASISDPHAAGDLLCT---AAKRNDLTAMKELLKQG---LNVDSEDHQGATALQ 660


                 ....*.
gi 363583286 183 WAAAGG 188
Cdd:PLN03192 661 VAMAED 666
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 252-338 1.54e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 59.53  E-value: 1.54e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286 252 IEVLLGHGADPGIRDRHGRSALHRAAARGHLLAVQLLVTQGAEVDARDTLGLTPLHHASREGHVEVAGcLLDRGAQVDAT 331
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ-LLSRHSQCHFE 176


                 ....*..
gi 363583286 332 GWLRKTP 338
Cdd:PTZ00322 177 LGANAKP 183
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 45-184 1.72e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 59.21  E-value: 1.72e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286  45 LLQAVWRGPAGLVTQLLRQGASVEERDHAGRTPLHLAVLRGHAPLVRLLLQRGAPVGAVDRAGRTALHEAAWHGHSRVAE 124
Cdd:PHA02874 128 LHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIK 207

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286 125 LLLQRGASAAARSGTGLTPLHwaAALGHTLLAARLLeapgPGPAAAEAEDARGWTAAHWA 184
Cdd:PHA02874 208 LLIDHGNHIMNKCKNGFTPLH--NAIIHNRSAIELL----INNASINDQDIDGSTPLHHA 261
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 60-330 2.03e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 58.91  E-value: 2.03e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286  60 LLRQGASVEERDHAGRTPLHLAVLRGHA-----PLVRLLLQRGAPVGAVDRAGRTALHEAAWH--GHSRVAELLLQRGAS 132
Cdd:PHA03100  54 LLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGAN 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286 133 AAARSGTGLTPLHWAAALGHTLLaarlleapgpgpaaaeaedargwtaahwaaaggrlavlellaaggagldgallvaaa 212
Cdd:PHA03100 134 VNIKNSDGENLLHLYLESNKIDL--------------------------------------------------------- 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286 213 agrgAALRFLLARGARVDARDGagatalglaaalgrsqdIEVLLGHGADPGIRDRHGRSALHRAAARGHLLAVQLLVTQG 292
Cdd:PHA03100 157 ----KILKLLIDKGVDINAKNR-----------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLG 215

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 363583286 293 AEVDARDTLGLTPLHHASREGHVEVAGCLLDRGAQVDA 330
Cdd:PHA03100 216 ANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
PHA03095 PHA03095
ankyrin-like protein; Provisional
 44-135 3.40e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 58.50  E-value: 3.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286  44 HLLQAVWRGPAGLVTQLLRQGASVEERDHAGRTPLHLAVLRGHAPLVRLLLQRGAPVGAVDRAGRTALHEAAWHGHSRVA 123
Cdd:PHA03095 227 HSMATGSSCKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAV 306

                         90
                 ....*....|..
gi 363583286 124 ELLLQRGASAAA 135
Cdd:PHA03095 307 RAALAKNPSAET 318
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 220-355 4.90e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 57.97  E-value: 4.90e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286 220 RFLLARGARVDARDGAGATALGLAAALGRSQDIEVLLGHGADPGIRDRHGRSALHRAAARGHLLAV-QLLVTQGAEVDAR 298
Cdd:PHA02878 185 ELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDYDIlKLLLEHGVDVNAK 264

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 363583286 299 DT-LGLTPLHHASREGhvEVAGCLLDRGAQVDATGWLRKTPLHLAAERGHGPTVGLLL 355
Cdd:PHA02878 265 SYiLGLTALHSSIKSE--RKLKLLLEYGADINSLNSYKLTPLSSAVKQYLCINIGRIL 320
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 248-359 7.25e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 57.31  E-value: 7.25e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286 248 RSQDIEV---LLGHGADPGIRDRHGRSALHRAAARGHLLAVQLLVTQGAEVDARDTLGLTPLHHASREGHVEVAGCLLDR 324
Cdd:PHA02875 111 ILKKLDImklLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDS 190

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 363583286 325 GAQVDATGwlRK---TPLHLAAERGHGPTVGLLLSRGA 359
Cdd:PHA02875 191 GANIDYFG--KNgcvAALCYAIENNKIDIVRLFIKRGA 226
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 72-145 1.34e-08

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 56.56  E-value: 1.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286  72 HAGRTPLHLAVLRGHAPLVRLLLQRGAPV------GAVDRAGRTAL-----HE---AAWHGHSRVAELLLQRGASAAARS 137
Cdd:cd22192   87 YQGETALHIAVVNQNLNLVRELIARGADVvspratGTFFRPGPKNLiyygeHPlsfAACVGNEEIVRLLIEHGADIRAQD 166


                 ....*...
gi 363583286 138 GTGLTPLH 145
Cdd:cd22192  167 SLGNTVLH 174
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 252-360 2.03e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 55.83  E-value: 2.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286 252 IEVLLGHGADPGIRDRhgrsalhraaarghllaVQLLVTQGAEVDARDTLGLTPLHHASREGHVEVAGCLLDRGAQVDAT 331
Cdd:PHA03100 159 LKLLIDKGVDINAKNR-----------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLV 221

                         90       100
                 ....*....|....*....|....*....
gi 363583286 332 GWLRKTPLHLAAERGHGPTVGLLLSRGAS 360
Cdd:PHA03100 222 NKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 252-360 2.61e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 56.03  E-value: 2.61e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286 252 IEVLLGHGADPGIRDRHGRSALHRAAARGHLLAVQLLVTQGAEVDARDTLGLTPL-------HH---------------- 308
Cdd:PLN03192 541 LEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALwnaisakHHkifrilyhfasisdph 620

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286 309 --------ASREGHVEVAGCLLDRGAQVDATGWLRKTPLHLAAERGHGPTVGLLLSRGAS 360
Cdd:PLN03192 621 aagdllctAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGAD 680
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 56-147 2.92e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 55.84  E-value: 2.92e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286  56 LVTQLLRQGASVEERDHAGRTPLHLAVLRGHAPLVRLLLQRGAPVGAVDRAGRTALHEAAWHGHSRVA-ELLLQRGASAA 134
Cdd:PHA02876 357 IVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMSvKTLIDRGANVN 436

                         90
                 ....*....|...
gi 363583286 135 ARSGTGLTPLHWA 147
Cdd:PHA02876 437 SKNKDLSTPLHYA 449
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 45-162 9.79e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 53.46  E-value: 9.79e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286  45 LLQAVWRGPAGLVTQLLRQGASVEERDHA-GRTPLHLAVLRGHAPLVRLLLQRGAP--VGAVDRAgrTALHEAAWHGHSR 121
Cdd:PHA02875  72 LHDAVEEGDVKAVEELLDLGKFADDVFYKdGMTPLHLATILKKLDIMKLLIARGADpdIPNTDKF--SPLHLAVMMGDIK 149

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 363583286 122 VAELLLQRGASAAARSGTGLTPLHWAAALGHTLLAARLLEA 162
Cdd:PHA02875 150 GIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDS 190
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 56-151 9.86e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 53.81  E-value: 9.86e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286  56 LVTQLLRQGASVEERDHAGRTPLHLAVLRGHAPLVRLLLQRGAPVGAVDRAGRTALHEAAWHGHSRVAELLLQRGASAAA 135
Cdd:PHA02874 106 MIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANV 185

                         90
                 ....*....|....*.
gi 363583286 136 RSGTGLTPLHWAAALG 151
Cdd:PHA02874 186 KDNNGESPLHNAAEYG 201
Ank_2 pfam12796
Ankyrin repeats (3 copies);
144-299 2.29e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 48.19  E-value: 2.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286  144 LHWAAALGHTLLAARLLEAPgpgpAAAEAEDARGWTAAHWAAAGGRLAVlellaaggagldgallvaaaagrgaaLRFLL 223
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENG----ADANLQDKNGRTALHLAAKNGHLEI--------------------------VKLLL 50

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 363583286  224 ARgARVDARDgagatalglaaalgrsqdievllghgadpgirdrHGRSALHRAAARGHLLAVQLLVTQGAEVDARD 299
Cdd:pfam12796  51 EH-ADVNLKD----------------------------------NGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 57-144 1.30e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 50.26  E-value: 1.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286  57 VTQLLRQGASVEERDHAGRTPLHLAVLR-GHAPLVRLLLQRGAPVGAVDRA-GRTALHEAAwhgHS-RVAELLLQRGASA 133
Cdd:PHA02878 217 VHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYIlGLTALHSSI---KSeRKLKLLLEYGADI 293

                         90
                 ....*....|.
gi 363583286 134 AARSGTGLTPL 144
Cdd:PHA02878 294 NSLNSYKLTPL 304
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 222-342 3.29e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 48.81  E-value: 3.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286 222 LLARGARVDARDGAGATALGLAAALGRSQDIEVLLGHGADPGIRDRHGRSALHRAAARGHLLAVQLLVTQGAEVDARDTL 301
Cdd:PHA02874 110 ILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNN 189

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 363583286 302 GLTPLHHASREGHVEVAGCLLDRGAQVDATGWLRKTPLHLA 342
Cdd:PHA02874 190 GESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNA 230
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 252-365 3.41e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 48.89  E-value: 3.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286 252 IEVLLGHGADPGIRDRHGRSALHRAAAR--GHLLAVQLLVTQGAEVDARDTLGLTPLHHASREGHV--EVAGCLLDRGAQ 327
Cdd:PHA03100  89 VKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVD 168

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 363583286 328 VDATG----WLRK------------TPLHLAAERGHGPTVGLLLSRGASPTLRT 365
Cdd:PHA03100 169 INAKNrvnyLLSYgvpinikdvygfTPLHYAVYNNNPEFVKYLLDLGANPNLVN 222
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 254-330 3.88e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 49.10  E-value: 3.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286 254 VLLGHGADPGIRDRHGRSAL--------HR-----------------------AAARGHLLAVQLLVTQGAEVDARDTLG 302
Cdd:PLN03192 576 VLLKHACNVHIRDANGNTALwnaisakhHKifrilyhfasisdphaagdllctAAKRNDLTAMKELLKQGLNVDSEDHQG 655

                         90       100
                 ....*....|....*....|....*...
gi 363583286 303 LTPLHHASREGHVEVAGCLLDRGAQVDA 330
Cdd:PLN03192 656 ATALQVAMAEDHVDMVRLLIMNGADVDK 683
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 250-367 5.03e-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: 48.47  E-value: 5.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286 250 QDIEVLLG-HGADPGIRDRHGRSALHRAAARGHLLAVQLLVTQGAE-VDARDT----LGLTPLHHASREGHVEVAGCLLD 323
Cdd:cd22192   31 QAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNEPMTsdlyQGETALHIAVVNQNLNLVRELIA 110

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 363583286 324 RGAQV---DATG-WLRKT----------PLHLAAERGHGPTVGLLLSRGASPTLRTQW 367
Cdd:cd22192  111 RGADVvspRATGtFFRPGpknliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSL 168
Ank_5 pfam13857
Ankyrin repeats (many copies);
74-114 6.84e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.10  E-value: 6.84e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 363583286   74 GRTPLHLAVLRGHAPLVRLLLQRGAPVGAVDRAGRTALHEA 114
Cdd:pfam13857  16 GYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
107-152 1.02e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.65  E-value: 1.02e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 363583286  107 GRTALHEAAWHGHSRVAELLLQRGASAAARSGTGLTPLHWAAALGH 152
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGN 46
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 74-105 1.04e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 41.89  E-value: 1.04e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 363583286   74 GRTPLHLAVLR-GHAPLVRLLLQRGAPVGAVDR 105
Cdd:pfam00023   2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 79-147 1.31e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.20  E-value: 1.31e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 363583286  79 HLAVlRGHAPLVRLLLQRGAPVGAVDRAGRTALHEAAWHGHSRVAELLLQRGASAAARSGTGLTPLHWA 147
Cdd:PTZ00322  88 QLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELA 155
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 45-104 1.34e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 47.17  E-value: 1.34e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286  45 LLQAVWRGPAGLVTQLLRQGASVEERDHAGRTPLHLAVLRGHAPLVRLLLQRGAPVGAVD 104
Cdd:PLN03192 626 LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAN 685
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 266-359 1.64e-05

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 44.48  E-value: 1.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286 266 DRHGRSALHRAAARGHL---LAVQLLVTQGAEVDARDTL-GLTPLHHASREGHVEVAGCLLDR-GAQVDATGWLRKTPLH 340
Cdd:PHA02736  52 NRHGKQCVHIVSNPDKAdpqEKLKLLMEWGADINGKERVfGNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYY 131

                         90
                 ....*....|....*....
gi 363583286 341 LAAERGHGPTVGLLLSRGA 359
Cdd:PHA02736 132 VACERHDAKMMNILRAKGA 150
PHA02743 PHA02743
Viral ankyrin protein; Provisional
 266-359 1.92e-05

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 44.81  E-value: 1.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286 266 DRHGRSALHRAA---ARGHLLAVQLLVTQGAEVDARDTL-GLTPLHHASREGHVEVAGCLL-DRGAQVDATGWLRKTPLH 340
Cdd:PHA02743  54 DHHGRQCTHMVAwydRANAVMKIELLVNMGADINARELGtGNTLLHIAASTKNYELAEWLCrQLGVNLGAINYQHETAYH 133

                         90
                 ....*....|....*....
gi 363583286 341 LAAERGHGPTVGLLLSRGA 359
Cdd:PHA02743 134 IAYKMRDRRMMEILRANGA 152
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 74-98 2.24e-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: 41.03  E-value: 2.24e-05
                           10        20
                   ....*....|....*....|....*
gi 363583286    74 GRTPLHLAVLRGHAPLVRLLLQRGA 98
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGA 26
Ank_5 pfam13857
Ankyrin repeats (many copies);
255-309 2.53e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.56  E-value: 2.53e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 363583286  255 LLGHG-ADPGIRDRHGRSALHRAAARGHLLAVQLLVTQGAEVDARDTLGLTPLHHA 309
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 252-342 2.72e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 46.11  E-value: 2.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286 252 IEVLLGHGADPGIRDRHGRSALHRAAARGHLLAVQLLVTQGAEVDARDTLGLTPLHHASRegHVEVAGCLLDRGAQVDAT 331
Cdd:PHA02874 173 IKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLINNASINDQ 250

                         90
                 ....*....|.
gi 363583286 332 GWLRKTPLHLA 342
Cdd:PHA02874 251 DIDGSTPLHHA 261
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 271-360 3.95e-05

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: 45.77  E-value: 3.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286 271 SALHRAAARGHLLAVQ-LLVTQGAEVDARDTLGLTPLHHASREGHVEVAGCLLD---RGAQVDATG--WLRKTPLHLAAE 344
Cdd:cd22192   19 SPLLLAAKENDVQAIKkLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEaapELVNEPMTSdlYQGETALHIAVV 98

                         90
                 ....*....|....*.
gi 363583286 345 RGHGPTVGLLLSRGAS 360
Cdd:cd22192   99 NQNLNLVRELIARGAD 114
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 45-182 4.09e-05

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: 45.77  E-value: 4.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286  45 LLQAVWRGPAGLVTQLLRQ-GASVEERDHAGRTPLHLAVLRGHAPLVRLLLqRGAPvGAVDRA-------GRTALHEAAW 116
Cdd:cd22192   21 LLLAAKENDVQAIKKLLKCpSCDLFQRGALGETALHVAALYDNLEAAVVLM-EAAP-ELVNEPmtsdlyqGETALHIAVV 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286 117 HGHSRVAELLLQRGASAAARSGTGLT--------------PLHWAAALGHTLLAARLLEApgpgPAAAEAEDARGWTAAH 182
Cdd:cd22192   99 NQNLNLVRELIARGADVVSPRATGTFfrpgpknliyygehPLSFAACVGNEEIVRLLIEH----GADIRAQDSLGNTVLH 174
Ank_2 pfam12796
Ankyrin repeats (3 copies);
41-104 5.27e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 41.64  E-value: 5.27e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 363583286   41 GWGHLLQAVWRGPAGLVTQLLRQgASVEERDHaGRTPLHLAVLRGHAPLVRLLLQRGAPVGAVD 104
Cdd:pfam12796  30 GRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
Ank_4 pfam13637
Ankyrin repeats (many copies);
302-355 5.29e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 40.34  E-value: 5.29e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 363583286  302 GLTPLHHASREGHVEVAGCLLDRGAQVDATGWLRKTPLHLAAERGHGPTVGLLL 355
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 56-149 5.98e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 45.04  E-value: 5.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286  56 LVTQLLRQGASVEERDHAGRTPLHLAVLRGHA--PLVRLLLQRGA----------------PVGAVDRAGRTALHEAAWH 117
Cdd:PHA03100 123 IVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVdinaknrvnyllsygvPINIKDVYGFTPLHYAVYN 202

                         90       100       110
                 ....*....|....*....|....*....|..
gi 363583286 118 GHSRVAELLLQRGASAAARSGTGLTPLHWAAA 149
Cdd:PHA03100 203 NNPEFVKYLLDLGANPNLVNKYGDTPLHIAIL 234
Ank_5 pfam13857
Ankyrin repeats (many copies);
93-147 6.18e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.41  E-value: 6.18e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 363583286   93 LLQRG-APVGAVDRAGRTALHEAAWHGHSRVAELLLQRGASAAARSGTGLTPLHWA 147
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 266-360 6.71e-05

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 45.07  E-value: 6.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286  266 DRHGRSALHRAAARG-HLLAVQLLVTQGAEVDARDTLgltpLHHASREGHVEVAGCLLDRGAQVDATGWLR--------- 335
Cdd:TIGR00870  49 DRLGRSALFVAAIENeNLELTELLLNLSCRGAVGDTL----LHAISLEYVDAVEAILLHLLAAFRKSGPLElandqytse 124

                          90       100
                  ....*....|....*....|....*....
gi 363583286  336 ----KTPLHLAAERGHGPTVGLLLSRGAS 360
Cdd:TIGR00870 125 ftpgITALHLAAHRQNYEIVKLLLERGAS 153
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 48-155 7.15e-05

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: 45.00  E-value: 7.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286  48 AVWRGPAGLVTQLLRQGASVEE-----------RD---HAGRTPLHLAVLRGHAPLVRLLLQRGAPVGAVDRAGRTALHE 113
Cdd:cd22192   96 AVVNQNLNLVRELIARGADVVSpratgtffrpgPKnliYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHI 175

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 363583286 114 AAWHGHSRVA----ELLLQRGASAAA------RSGTGLTPLHWAAALGHTLL 155
Cdd:cd22192  176 LVLQPNKTFAcqmyDLILSYDKEDDLqpldlvPNNQGLTPFKLAAKEGNIVM 227
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 302-330 1.05e-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: 1.05e-04
                           10        20
                   ....*....|....*....|....*....
gi 363583286   302 GLTPLHHASREGHVEVAGCLLDRGAQVDA 330
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 74-100 1.20e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 38.78  E-value: 1.20e-04
                          10        20
                  ....*....|....*....|....*..
gi 363583286   74 GRTPLHLAVLRGHAPLVRLLLQRGAPV 100
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADI 28
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 107-132 1.22e-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: 38.72  E-value: 1.22e-04
                           10        20
                   ....*....|....*....|....*.
gi 363583286   107 GRTALHEAAWHGHSRVAELLLQRGAS 132
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGAD 27
Ank_4 pfam13637
Ankyrin repeats (many copies);
252-289 1.58e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.18  E-value: 1.58e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 363583286  252 IEVLLGHGADPGIRDRHGRSALHRAAARGHLLAVQLLV 289
Cdd:pfam13637  17 LRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02743 PHA02743
Viral ankyrin protein; Provisional
 104-164 1.87e-04

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 41.73  E-value: 1.87e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 363583286 104 DRAGRTALHEAAWHGHSRVA---ELLLQRGASAAAR-SGTGLTPLHWAAALGHTLLAARLLEAPG 164
Cdd:PHA02743  54 DHHGRQCTHMVAWYDRANAVmkiELLVNMGADINAReLGTGNTLLHIAASTKNYELAEWLCRQLG 118
Ank_4 pfam13637
Ankyrin repeats (many copies);
140-192 2.36e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.79  E-value: 2.36e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 363583286  140 GLTPLHWAAALGHTLLAARLLEAPGPGPAAaeaeDARGWTAAHWAAAGGRLAV 192
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAV----DGNGETALHFAASNGNVEV 49
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 74-182 3.35e-04

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 42.76  E-value: 3.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286   74 GRTPLHLAVLRGHAPLVRLLLQRGAPVGAvdRAG-----RTALHEAAWHGHSrvaelllqrgasaaarsgtgltPLHWAA 148
Cdd:TIGR00870 128 GITALHLAAHRQNYEIVKLLLERGASVPA--RACgdffvKSQGVDSFYHGES----------------------PLNAAA 183

                          90       100       110
                  ....*....|....*....|....*....|....
gi 363583286  149 ALGHTLLAARLLEapgpGPAAAEAEDARGWTAAH 182
Cdd:TIGR00870 184 CLGSPSIVALLSE----DPADILTADSLGNTLLH 213
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 285-359 3.38e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 42.34  E-value: 3.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286 285 VQLLVTQGAEVDARDTLGLTPLHHASREGHV-----EVAGCLLDRGAQVDATGWLRKTPLHLAA--ERGHGPTVGLLLSR 357
Cdd:PHA03100  51 VKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDN 130


                 ..
gi 363583286 358 GA 359
Cdd:PHA03100 131 GA 132
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 62-182 4.13e-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: 42.56  E-value: 4.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286  62 RQGASVEERDHAGRTPLHLAVLRGH-------APLVRLLLQRGAPVGAVDRA-------GRTALHEAAWHGHSRVAELLL 127
Cdd:cd21882   14 YLTDSAYQRGATGKTCLHKAALNLNdgvneaiMLLLEAAPDSGNPKELVNAPctdefyqGQTALHIAIENRNLNLVRLLV 93

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 363583286 128 QRGASAAARS-GT------------GLTPLHWAAALGHTLLAARLLEAPGPgPAAAEAEDARGWTAAH 182
Cdd:cd21882   94 ENGADVSARAtGRffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQ-PAALEAQDSLGNTVLH 160
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 268-299 4.56e-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: 4.56e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 363583286  268 HGRSALHRAAAR-GHLLAVQLLVTQGAEVDARD 299
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 282-329 5.64e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 41.97  E-value: 5.64e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 363583286 282 LLAVQLLVTQGAEVDARDTLGLTPLHHASREGHVEVAGCLLDRGAQVD 329
Cdd:PHA02876 158 LLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVN 205
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 311-359 6.65e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 41.97  E-value: 6.65e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 363583286 311 REGHVEVAGCLLDRGAQVDATGWLRKTPLHLAAERGHGPTVGLLLSRGA 359
Cdd:PHA02876 154 QQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGA 202
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 107-136 7.53e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.88  E-value: 7.53e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 363583286  107 GRTALHEAAWH-GHSRVAELLLQRGASAAAR 136
Cdd:pfam00023   2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNAR 32
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 74-162 9.28e-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: 41.40  E-value: 9.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286  74 GRTPLHLAVLRGHAPLVRLLLQRGAPVGAvdRA---------------GRTALHEAAWHGHSRVAELLLQRGASAAARSG 138
Cdd:cd21882   73 GQTALHIAIENRNLNLVRLLVENGADVSA--RAtgrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQPAALEA 150

                         90       100
                 ....*....|....*....|....
gi 363583286 139 TGltplhwaaALGHTLLAARLLEA 162
Cdd:cd21882  151 QD--------SLGNTVLHALVLQA 166
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 40-179 1.01e-03

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: 41.40  E-value: 1.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286  40 QGWGHLLQAVWRGPAGLVTQLLRQGASVEERD-------------HAGRTPLHLAVLRGHAPLVRLLLQRGAPVGAV--- 103
Cdd:cd21882   72 QGQTALHIAIENRNLNLVRLLVENGADVSARAtgrffrkspgnlfYFGELPLSLAACTNQEEIVRLLLENGAQPAALeaq 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286 104 DRAGRTALHEAAWHGHSRVA---------ELLLQRGASA-------AARSGTGLTPLHWAAALGHTLLAARLLEAPGPGP 167
Cdd:cd21882  152 DSLGNTVLHALVLQADNTPEnsafvcqmyNLLLSYGAHLdptqqleEIPNHQGLTPLKLAAVEGKIVMFQHILQREFSGP 231

                        170
                 ....*....|..
gi 363583286 168 AAAEAEDARGWT 179
Cdd:cd21882  232 YQPLSRKFTEWT 243
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 302-331 1.62e-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: 35.73  E-value: 1.62e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 363583286  302 GLTPLHHAS-REGHVEVAGCLLDRGAQVDAT 331
Cdd:pfam00023   2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNAR 32
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 302-330 1.86e-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: 1.86e-03
                          10        20
                  ....*....|....*....|....*....
gi 363583286  302 GLTPLHHASREGHVEVAGCLLDRGAQVDA 330
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
41-94 3.18e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 35.33  E-value: 3.18e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 363583286   41 GWGHLLQAVWRGPAGLVTQLLRQGASVEERDHAGRTPLHLAVLRGHAPLVRLLL 94
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 56-112 3.78e-03

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 39.51  E-value: 3.78e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 363583286  56 LVTQLLRQGASVEERDHAGRTPLHLAVLRGH--APLVRLLLQRGAPVGAVDRAGRTALH 112
Cdd:PHA02716 299 VVYSFLQPGVKLHYKDSAGRTCLHQYILRHNisTDIIKLLHEYGNDLNEPDNIGNTVLH 357
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 154-359 4.12e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 39.28  E-value: 4.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286 154 LLAARLLEapgpGPAAAEAEDARGWTAAHWAAAGGR-------LAVLELLAAGGAGLDGALLVAAAAGRGAALRFLLARG 226
Cdd:PHA02876 159 LIAEMLLE----GGADVNAKDIYCITPIHYAAERGNakmvnllLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNR 234

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286 227 ARVDARDgagatalGLAAALGRSQDIEV-------------------------------------LLGHGADPGIRDRHG 269
Cdd:PHA02876 235 SNINKND-------LSLLKAIRNEDLETslllydagfsvnsiddckntplhhasqapslsrlvpkLLERGADVNAKNIKG 307

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286 270 RSALHRAAARGH-LLAVQLLVTQGAEVDARDTLGLTPLHHASR-EGHVEVAGCLLDRGAQVDATGWLRKTPLHLAAERGH 347
Cdd:PHA02876 308 ETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNN 387

                        250
                 ....*....|..
gi 363583286 348 GPTVGLLLSRGA 359
Cdd:PHA02876 388 VVIINTLLDYGA 399
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 337-365 4.51e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 34.57  E-value: 4.51e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 363583286  337 TPLHLAAER-GHGPTVGLLLSRGASPTLRT 365
Cdd:pfam00023   4 TPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
PHA02946 PHA02946
ankyin-like protein; Provisional
 44-112 4.98e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 38.88  E-value: 4.98e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 363583286  44 HLLQAvWRGPAGL----VTQLLRQGASVEERDHAGRTPLHLAVLRGHAPLVRLLLQRGAPVGAVDRAGRTALH 112
Cdd:PHA02946  39 HILHA-YCGIKGLderfVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLY 110
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 268-297 6.30e-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: 34.16  E-value: 6.30e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 363583286  268 HGRSALHRAAARGHLLAVQLLVTQGAEVDA 297
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 268-297 6.35e-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: 6.35e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 363583286   268 HGRSALHRAAARGHLLAVQLLVTQGAEVDA 297
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 44-131 7.20e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 38.43  E-value: 7.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286  44 HLlqAVWRGPAGLVTQLLRQGASVEERDHAGRTPLHLAVLRGHAPLVRLLLQRGAPVGAVDRAGR-TALHEAAWHGHSRV 122
Cdd:PHA02875 140 HL--AVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDI 217


                 ....*....
gi 363583286 123 AELLLQRGA 131
Cdd:PHA02875 218 VRLFIKRGA 226
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 269-341 8.79e-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: 38.07  E-value: 8.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 363583286 269 GRSALHRAAARGHLLAVQLLVTQGAEV-DARDT-------------LGLTPLHHASREGHVEVAGCLLDRGAQVDATGWL 334
Cdd:cd22192   89 GETALHIAVVNQNLNLVRELIARGADVvSPRATgtffrpgpknliyYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSL 168


                 ....*..
gi 363583286 335 RKTPLHL 341
Cdd:cd22192  169 GNTVLHI 175
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 60-132 8.80e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 38.05  E-value: 8.80e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 363583286  60 LLRQGASVEERDHAGRTPLHLAVLRGHAPLVRLLLQRGAPVGAVDRAGRTALHEAAWHGHSRVAELLLQRGAS 132
Cdd:PHA02875 121 LIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGAN 193
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH