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Conserved domains on  [gi|1907098180|ref|XP_036014259|]
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serine/threonine-protein phosphatase 6 regulatory ankyrin repeat subunit A isoform X4 [Mus musculus]

Protein Classification

ankyrin repeat domain-containing protein( domain architecture ID 13333862)

ankyrin repeat (ANK) domain-containing protein is involved in mediating protein-protein interactions

Gene Ontology:  GO:0005515
PubMed:  33435370|17176038

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
84-373 4.90e-56

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 185.93  E-value: 4.90e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180  84 AEIIELLILSGARVNAKDSKWLTPLHRAVASCSEEAVQILLKHSADVNARDKNWQTPLHIAAANKAVKCAESLVPLLSNV 163
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 164 NVSDRAGRTALHHAAFSGHGEMVKLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVSHGAEVTCKDKKSYTPLHAA 243
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 244 ASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDCGANVNQKNEKGFTPLHFAAASTHGALcLELLV 323
Cdd:COG0666   161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEI-VKLLL 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907098180 324 GNGADVNMKSKDGKTPLHMTALHGRFSRSQTIIQSGAVIDCEDKNGNTPL 373
Cdd:COG0666   240 EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
Ank_4 pfam13637
Ankyrin repeats (many copies);
39-91 2.23e-06

Ankyrin repeats (many copies);


:

Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.57  E-value: 2.23e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907098180  39 LPSLVQAIFNGDPDEVRALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLI 91
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
368-394 2.83e-04

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


:

Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.95  E-value: 2.83e-04
                           10        20
                   ....*....|....*....|....*..
gi 1907098180  368 NGNTPLHIAARYGHELLINTLITSGAD 394
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
84-373 4.90e-56

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 185.93  E-value: 4.90e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180  84 AEIIELLILSGARVNAKDSKWLTPLHRAVASCSEEAVQILLKHSADVNARDKNWQTPLHIAAANKAVKCAESLVPLLSNV 163
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 164 NVSDRAGRTALHHAAFSGHGEMVKLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVSHGAEVTCKDKKSYTPLHAA 243
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 244 ASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDCGANVNQKNEKGFTPLHFAAASTHGALcLELLV 323
Cdd:COG0666   161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEI-VKLLL 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907098180 324 GNGADVNMKSKDGKTPLHMTALHGRFSRSQTIIQSGAVIDCEDKNGNTPL 373
Cdd:COG0666   240 EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA03095 PHA03095
ankyrin-like protein; Provisional
52-340 2.00e-43

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 157.49  E-value: 2.00e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180  52 DEVRALIFKKEDVNFQDNEKRTPLHAaaYLG-----DAEIIELLILSGARVNAKDSKWLTPLHRAV-ASCSEEAVQILLK 125
Cdd:PHA03095   28 EEVRRLLAAGADVNFRGEYGKTPLHL--YLHyssekVKDIVRLLLEAGADVNAPERCGFTPLHLYLyNATTLDVIKLLIK 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 126 HSADVNARDKNWQTPLHIAAANKAVkcaeslvpllsnvnvsdragrtalhhaafsgHGEMVKLLLSRGANINAFDKKDRR 205
Cdd:PHA03095  106 AGADVNAKDKVGRTPLHVYLSGFNI-------------------------------NPKVIRLLLRKGADVNALDLYGMT 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 206 AIHwaAYMGH----IEVVKLLVSHGAEVTCKDKKSYTPLHAAASSGMIS--VVKYLLDLGVDMNEPNAYGNTPLHVACYN 279
Cdd:PHA03095  155 PLA--VLLKSrnanVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTPLHSMATG 232
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907098180 280 G--QDVVVNELIDCGANVNQKNEKGFTPLHFAAASTHGALCLELLVGnGADVNMKSKDGKTPL 340
Cdd:PHA03095  233 SscKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIAL-GADINAVSSDGNTPL 294
Ank_2 pfam12796
Ankyrin repeats (3 copies);
174-266 3.54e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 89.79  E-value: 3.54e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 174 LHHAAFSGHGEMVKLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVSHgAEVTCKDKKsYTPLHAAASSGMISVVK 253
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNG-RTALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 1907098180 254 YLLDLGVDMNEPN 266
Cdd:pfam12796  79 LLLEKGADINVKD 91
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
104-289 1.27e-14

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: 75.43  E-value: 1.27e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 104 WLTPLHRAVASCSEEAVQILLK-HSADVNARDKNWQTPLHIAAANKAVKCAESL---VPLLSNVNV-SD-RAGRTALHHA 177
Cdd:cd22192    17 SESPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLmeaAPELVNEPMtSDlYQGETALHIA 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 178 AFSGHGEMVKLLLSRGANIN-------AFDKKDRRAIHW-------AAYMGHIEVVKLLVSHGAEVTCKDKKSYTPLHAA 243
Cdd:cd22192    97 VVNQNLNLVRELIARGADVVspratgtFFRPGPKNLIYYgehplsfAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHIL 176
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907098180 244 ASSGMISVVKYLLDLGVDMNE----------PNAYGNTPLHVACYNGQDVVVNELI 289
Cdd:cd22192   177 VLQPNKTFACQMYDLILSYDKeddlqpldlvPNNQGLTPFKLAAKEGNIVMFQHLV 232
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
58-277 3.49e-08

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: 55.47  E-value: 3.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180  58 IFKKEDVNFQDNEKrtplhaaAYLGDAEIIELLILSGARVNAK-------DSKWLTPLHRAVA-SCSEEAVQILLKHSAD 129
Cdd:TIGR00870   6 IVPAEESPLSDEEK-------AFLPAAERGDLASVYRDLEEPKklnincpDRLGRSALFVAAIeNENLELTELLLNLSCR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 130 VNARDknwqTPLHIAAANKAVKCAESLVPLLSN---------VNVSDR----AGRTALHHAAFSGHGEMVKLLLSRGANI 196
Cdd:TIGR00870  79 GAVGD----TLLHAISLEYVDAVEAILLHLLAAfrksgplelANDQYTseftPGITALHLAAHRQNYEIVKLLLERGASV 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 197 NA------FDKKDRRA--------IHWAAYMGHIEVVKLLVSHGAEVTCKDKKSYTPLHAAA------------SSGMIS 250
Cdd:TIGR00870 155 PAracgdfFVKSQGVDsfyhgespLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVmenefkaeyeelSCQMYN 234
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1907098180 251 VVKYLLDLGVDMNE----PNAYGNTPLHVAC 277
Cdd:TIGR00870 235 FALSLLDKLRDSKEleviLNHQGLTPLKLAA 265
Ank_4 pfam13637
Ankyrin repeats (many copies);
39-91 2.23e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.57  E-value: 2.23e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907098180  39 LPSLVQAIFNGDPDEVRALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLI 91
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
170-198 4.38e-06

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.96  E-value: 4.38e-06
                           10        20
                   ....*....|....*....|....*....
gi 1907098180  170 GRTALHHAAFSGHGEMVKLLLSRGANINA 198
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
368-394 2.83e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.95  E-value: 2.83e-04
                           10        20
                   ....*....|....*....|....*..
gi 1907098180  368 NGNTPLHIAARYGHELLINTLITSGAD 394
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
45-109 1.37e-03

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 40.77  E-value: 1.37e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907098180  45 AIFNGDPDEVRALIFKKEDVN--------FQDNEKRT------PLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLH 109
Cdd:cd22192    96 AVVNQNLNLVRELIARGADVVspratgtfFRPGPKNLiyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
368-394 1.66e-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: 1.66e-03
                          10        20
                  ....*....|....*....|....*...
gi 1907098180 368 NGNTPLHIAA-RYGHELLINTLITSGAD 394
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGAD 28
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
355-394 4.06e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 39.50  E-value: 4.06e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1907098180 355 IIQSGAVIDCEDKNGNTPLHIAARYGHELLINTLITSGAD 394
Cdd:PTZ00322  101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGAD 140
PHA02875 PHA02875
ankyrin repeat protein; Provisional
34-131 8.08e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 38.05  E-value: 8.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180  34 PSGNVLPSLVQAIFNGDPDEVRALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLILSGARVN-AKDSKWLTPLHRAV 112
Cdd:PHA02875  131 PNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDyFGKNGCVAALCYAI 210
                          90
                  ....*....|....*....
gi 1907098180 113 ASCSEEAVQILLKHSADVN 131
Cdd:PHA02875  211 ENNKIDIVRLFIKRGADCN 229
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
84-373 4.90e-56

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 185.93  E-value: 4.90e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180  84 AEIIELLILSGARVNAKDSKWLTPLHRAVASCSEEAVQILLKHSADVNARDKNWQTPLHIAAANKAVKCAESLVPLLSNV 163
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 164 NVSDRAGRTALHHAAFSGHGEMVKLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVSHGAEVTCKDKKSYTPLHAA 243
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 244 ASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDCGANVNQKNEKGFTPLHFAAASTHGALcLELLV 323
Cdd:COG0666   161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEI-VKLLL 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907098180 324 GNGADVNMKSKDGKTPLHMTALHGRFSRSQTIIQSGAVIDCEDKNGNTPL 373
Cdd:COG0666   240 EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
42-306 1.98e-54

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 181.69  E-value: 1.98e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180  42 LVQAIFNGDPDEVRALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEEAVQ 121
Cdd:COG0666    25 LLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVK 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 122 ILLKHSADVNARDKNWQTPLHIAAANKAVKCAESLVPLLSNVNVSDRAGRTALHHAAFSGHGEMVKLLLSRGANINAFDK 201
Cdd:COG0666   105 LLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDN 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 202 KDRRAIHWAAYMGHIEVVKLLVSHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQ 281
Cdd:COG0666   185 DGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGA 264
                         250       260
                  ....*....|....*....|....*
gi 1907098180 282 DVVVNELIDCGANVNQKNEKGFTPL 306
Cdd:COG0666   265 ALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
52-340 4.22e-54

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 180.92  E-value: 4.22e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180  52 DEVRALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEEAVQILLKHSADVN 131
Cdd:COG0666     2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 132 ARDKNWQTPLHIAAANKAVKCAESLVPLLSNVNVSDRAGRTALHHAAFSGHGEMVKLLLSRGANINAFDKKDRRAIHWAA 211
Cdd:COG0666    82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 212 YMGHIEVVKLLVSHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDC 291
Cdd:COG0666   162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1907098180 292 GANVNQKNEKGFTPLHFAAASTHgALCLELLVGNGADVNMKSKDGKTPL 340
Cdd:COG0666   242 GADLNAKDKDGLTALLLAAAAGA-ALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
122-397 9.68e-54

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 180.15  E-value: 9.68e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 122 ILLKHSADVNARDKNWQTPLHIAAANKAVKCAESLVPLLSNVNVSDRAGRTALHHAAFSGHGEMVKLLLSRGANINAFDK 201
Cdd:COG0666     6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 202 KDRRAIHWAAYMGHIEVVKLLVSHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQ 281
Cdd:COG0666    86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGN 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 282 DVVVNELIDCGANVNQKNEKGFTPLHFAAASTHGALcLELLVGNGADVNMKSKDGKTPLHMTALHGRFSRSQTIIQSGAV 361
Cdd:COG0666   166 LEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEI-VKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD 244
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1907098180 362 IDCEDKNGNTPLHIAARYGHELLINTLITSGADTAK 397
Cdd:COG0666   245 LNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAA 280
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
153-394 2.88e-47

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 163.20  E-value: 2.88e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 153 AESLVPLLSNVNVSDRAGRTALHHAAFSGHGEMVKLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVSHGAEVTCK 232
Cdd:COG0666     4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 233 DKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDCGANVNQKNEKGFTPLHFAAAS 312
Cdd:COG0666    84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 313 THGALcLELLVGNGADVNMKSKDGKTPLHMTALHGRFSRSQTIIQSGAVIDCEDKNGNTPLHIAARYGHELLINTLITSG 392
Cdd:COG0666   164 GNLEI-VKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAG 242

                  ..
gi 1907098180 393 AD 394
Cdd:COG0666   243 AD 244
PHA03095 PHA03095
ankyrin-like protein; Provisional
52-340 2.00e-43

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 157.49  E-value: 2.00e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180  52 DEVRALIFKKEDVNFQDNEKRTPLHAaaYLG-----DAEIIELLILSGARVNAKDSKWLTPLHRAV-ASCSEEAVQILLK 125
Cdd:PHA03095   28 EEVRRLLAAGADVNFRGEYGKTPLHL--YLHyssekVKDIVRLLLEAGADVNAPERCGFTPLHLYLyNATTLDVIKLLIK 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 126 HSADVNARDKNWQTPLHIAAANKAVkcaeslvpllsnvnvsdragrtalhhaafsgHGEMVKLLLSRGANINAFDKKDRR 205
Cdd:PHA03095  106 AGADVNAKDKVGRTPLHVYLSGFNI-------------------------------NPKVIRLLLRKGADVNALDLYGMT 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 206 AIHwaAYMGH----IEVVKLLVSHGAEVTCKDKKSYTPLHAAASSGMIS--VVKYLLDLGVDMNEPNAYGNTPLHVACYN 279
Cdd:PHA03095  155 PLA--VLLKSrnanVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTPLHSMATG 232
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907098180 280 G--QDVVVNELIDCGANVNQKNEKGFTPLHFAAASTHGALCLELLVGnGADVNMKSKDGKTPL 340
Cdd:PHA03095  233 SscKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIAL-GADINAVSSDGNTPL 294
PHA03100 PHA03100
ankyrin repeat protein; Provisional
53-331 5.63e-42

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 152.51  E-value: 5.63e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180  53 EVRALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLH-----RAVASCSEEAVQILLKHS 127
Cdd:PHA03100   17 NIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHylsniKYNLTDVKEIVKLLLEYG 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 128 ADVNARDKNWQTPLHIAAANKavkcaeslvpllsnvnvsdragrtalhhaafSGHGEMVKLLLSRGANINAFDKKDRRAI 207
Cdd:PHA03100   97 ANVNAPDNNGITPLLYAISKK-------------------------------SNSYSIVEYLLDNGANVNIKNSDGENLL 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 208 HWAAYMGHI--EVVKLLVSHGAEVTCKDKksytplhaaassgmisvVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVV 285
Cdd:PHA03100  146 HLYLESNKIdlKILKLLIDKGVDINAKNR-----------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFV 208
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1907098180 286 NELIDCGANVNQKNEKGFTPLHFAAASTHGALcLELLVGNGADVNM 331
Cdd:PHA03100  209 KYLLDLGANPNLVNKYGDTPLHIAILNNNKEI-FKLLLNNGPSIKT 253
PHA02876 PHA02876
ankyrin repeat protein; Provisional
52-394 7.10e-37

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 142.12  E-value: 7.10e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180  52 DEVR---ALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEEAVQILLKHSA 128
Cdd:PHA02876  156 DELLiaeMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRS 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 129 DVNARDKNwqtpLHIAAANKAVKCAESLVPLLSNVNVSDRAGRTALHHAAFSGH-GEMVKLLLSRGANINAFDKKDRRAI 207
Cdd:PHA02876  236 NINKNDLS----LLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPL 311
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 208 HWAAYMGH-IEVVKLLVSHGAEVTCKDKKSYTPLHAAAS-SGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVV 285
Cdd:PHA02876  312 YLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVII 391
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 286 NELIDCGANVNQKNEKGFTPLHFAAASTHGALCLELLVGNGADVNMKSKDGKTPLHMTALHG-RFSRSQTIIQSGAVIDC 364
Cdd:PHA02876  392 NTLLDYGADIEALSQKIGTALHFALCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNA 471
                         330       340       350
                  ....*....|....*....|....*....|
gi 1907098180 365 EDKNGNTPLHIAarYGHELLINTLITSGAD 394
Cdd:PHA02876  472 INIQNQYPLLIA--LEYHGIVNILLHYGAE 499
PHA02874 PHA02874
ankyrin repeat protein; Provisional
46-397 5.61e-36

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 136.63  E-value: 5.61e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180  46 IFNGDPDEVRALIFKKED-VNFQDNEKRTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEEAVQILL 124
Cdd:PHA02874    9 IYSGDIEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLI 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 125 KHSADVNARDknwqtplhiaaankavkcaeslVPLLSNvnvsdragrtalhhaafsghgEMVKLLLSRGANINAFDKKDR 204
Cdd:PHA02874   89 DNGVDTSILP----------------------IPCIEK---------------------DMIKTILDCGIDVNIKDAELK 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 205 RAIHWAAYMGHIEVVKLLVSHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVV 284
Cdd:PHA02874  126 TFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYAC 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 285 VNELIDCGANVNQKNEKGFTPLHfaAASTHGALCLELLVgNGADVNMKSKDGKTPLHMtALHGRFSRS--QTIIQSGAVI 362
Cdd:PHA02874  206 IKLLIDHGNHIMNKCKNGFTPLH--NAIIHNRSAIELLI-NNASINDQDIDGSTPLHH-AINPPCDIDiiDILLYHKADI 281
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1907098180 363 DCEDKNGNTPLHIAARYGH------ELLINTLITSGADTAK 397
Cdd:PHA02874  282 SIKDNKGENPIDTAFKYINkdpvikDIIANAVLIKEADKLK 322
PHA02878 PHA02878
ankyrin repeat protein; Provisional
105-383 1.00e-26

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 111.13  E-value: 1.00e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 105 LTPLHRAVASCSEEAVQILLKHSADVNARDKNWQTPLHIAAANKAVKCAESLVPLLSNVNVSD--RAGRTALHHAAFsgh 182
Cdd:PHA02878   38 FIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVFYtlVAIKDAFNNRNV--- 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 183 gEMVK-LLLSRGANINAFDKKDRRAIHWAAYMgHIEVVKLLVSHGAEVTCKDK-KSYTPLHAAASSGMISVVKYLLDLGV 260
Cdd:PHA02878  115 -EIFKiILTNRYKNIQTIDLVYIDKKSKDDII-EAEITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGA 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 261 DMNEPNAYGNTPLHVACYNGQDVVVNELIDCGANVNQKNEKGFTPLHFAAASTHGALCLELLVGNGADVNMKSK-DGKTP 339
Cdd:PHA02878  193 NVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDYDILKLLLEHGVDVNAKSYiLGLTA 272
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1907098180 340 LHMtALHGRfSRSQTIIQSGAVIDCEDKNGNTPLHIAA--RYGHEL 383
Cdd:PHA02878  273 LHS-SIKSE-RKLKLLLEYGADINSLNSYKLTPLSSAVkqYLCINI 316
PHA03100 PHA03100
ankyrin repeat protein; Provisional
39-300 4.82e-26

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 108.60  E-value: 4.82e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180  39 LPSLVQAIFN-GDPDEVRALIFKKE-DVNFQDNEKRTPLHAAAY--LGDAEIIELLILSGARVNAKDSKWLTPLHRAVAS 114
Cdd:PHA03100   72 LHYLSNIKYNlTDVKEIVKLLLEYGaNVNAPDNNGITPLLYAISkkSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLES 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 115 CSEEAvqillkhsadvnardknwqtplhiaaankavkcaeslvpllsnvnvsdragrtalhhaafsghgEMVKLLLSRGA 194
Cdd:PHA03100  152 NKIDL----------------------------------------------------------------KILKLLIDKGV 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 195 NINAfdkKDRraihwaaymghievVKLLVSHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLH 274
Cdd:PHA03100  168 DINA---KNR--------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLH 230
                         250       260
                  ....*....|....*....|....*.
gi 1907098180 275 VACYNGQDVVVNELIDCGANVNQKNE 300
Cdd:PHA03100  231 IAILNNNKEIFKLLLNNGPSIKTIIE 256
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
184-394 1.86e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 101.95  E-value: 1.86e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 184 EMVKLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVSHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMN 263
Cdd:COG0666     2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 264 EPNAYGNTPLHVACYNGQDVVVNELIDCGANVNQKNEKGFTPLHFAAASTHGALcLELLVGNGADVNMKskdgktplhmt 343
Cdd:COG0666    82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEI-VKLLLEAGADVNAQ----------- 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907098180 344 alhgrfsrsqtiiqsgavidceDKNGNTPLHIAARYGHELLINTLITSGAD 394
Cdd:COG0666   150 ----------------------DNDGNTPLHLAAANGNLEIVKLLLEAGAD 178
Ank_2 pfam12796
Ankyrin repeats (3 copies);
174-266 3.54e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 89.79  E-value: 3.54e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 174 LHHAAFSGHGEMVKLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVSHgAEVTCKDKKsYTPLHAAASSGMISVVK 253
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNG-RTALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 1907098180 254 YLLDLGVDMNEPN 266
Cdd:pfam12796  79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
207-299 5.26e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 89.40  E-value: 5.26e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 207 IHWAAYMGHIEVVKLLVSHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDlGVDMNEPNaYGNTPLHVACYNGQDVVVN 286
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 1907098180 287 ELIDCGANVNQKN 299
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA02878 PHA02878
ankyrin repeat protein; Provisional
60-347 5.35e-22

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 97.26  E-value: 5.35e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180  60 KKEDVNFQDNEKRT---------PLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEEAVQILLK----- 125
Cdd:PHA02878   17 LKYIEYIDHTENYStsaslipfiPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRsinkc 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 126 -------------HSADVNA-------RDKNWQTP--LHIAAANKAVKCAESLVPLL----SNVNVSDR-AGRTALHHAA 178
Cdd:PHA02878   97 svfytlvaikdafNNRNVEIfkiiltnRYKNIQTIdlVYIDKKSKDDIIEAEITKLLlsygADINMKDRhKGNTALHYAT 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 179 FSGHGEMVKLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVSHGAEVTCKDKKSYTPLHAAASSGM-ISVVKYLLD 257
Cdd:PHA02878  177 ENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKdYDILKLLLE 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 258 LGVDMN-EPNAYGNTPLHVACYNGQdvVVNELIDCGANVNQKNEKGFTPLHFAAASTHGALCLELLVGNGADVNMKSKDG 336
Cdd:PHA02878  257 HGVDVNaKSYILGLTALHSSIKSER--KLKLLLEYGADINSLNSYKLTPLSSAVKQYLCINIGRILISNICLLKRIKPDI 334
                         330
                  ....*....|....*
gi 1907098180 337 KTPL----HMTALHG 347
Cdd:PHA02878  335 KNSEgfidNMDCITS 349
Ank_2 pfam12796
Ankyrin repeats (3 copies);
141-233 5.94e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 89.40  E-value: 5.94e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 141 LHIAAANKAVKCAESLVPLLSNVNVSDRAGRTALHHAAFSGHGEMVKLLLSRgANINAFDkKDRRAIHWAAYMGHIEVVK 220
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 1907098180 221 LLVSHGAEVTCKD 233
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
216-394 6.27e-22

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 96.66  E-value: 6.27e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 216 IEVVKLLVSHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLH---VACYNGQDVV--VNELID 290
Cdd:PHA03100   15 VKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHylsNIKYNLTDVKeiVKLLLE 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 291 CGANVNQKNEKGFTPLHFAAASTHGALCL-ELLVGNGADVNMKSKDGKTPLHMTA--LHGRFSRSQTIIQSGA------- 360
Cdd:PHA03100   95 YGANVNAPDNNGITPLLYAISKKSNSYSIvEYLLDNGANVNIKNSDGENLLHLYLesNKIDLKILKLLIDKGVdinaknr 174
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1907098180 361 ---------VIDCEDKNGNTPLHIAARYGHELLINTLITSGAD 394
Cdd:PHA03100  175 vnyllsygvPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGAN 217
PHA03095 PHA03095
ankyrin-like protein; Provisional
216-394 2.25e-21

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 95.48  E-value: 2.25e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 216 IEVVKLLVSHGAEVTCKDKKSYTPLHAAASSGM---ISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDV-VVNELIDC 291
Cdd:PHA03095   27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKA 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 292 GANVNQKNEKGFTPLH--FAAASTHgALCLELLVGNGADVNMKSKDGKTPLH---------------------------- 341
Cdd:PHA03095  107 GADVNAKDKVGRTPLHvyLSGFNIN-PKVIRLLLRKGADVNALDLYGMTPLAvllksrnanvellrllidagadvyavdd 185
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907098180 342 --MTALH-------GRFSRSQTIIQSGAVIDCEDKNGNTPLHIAARYG--HELLINTLITSGAD 394
Cdd:PHA03095  186 rfRSLLHhhlqsfkPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSscKRSLVLPLLIAGIS 249
Ank_2 pfam12796
Ankyrin repeats (3 copies);
42-134 1.63e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.17  E-value: 1.63e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180  42 LVQAIFNGDPDEVRALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLiLSGARVNAKDSKWlTPLHRAVASCSEEAVQ 121
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL-LEHADVNLKDNGR-TALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 1907098180 122 ILLKHSADVNARD 134
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA02875 PHA02875
ankyrin repeat protein; Provisional
72-296 5.98e-20

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 90.82  E-value: 5.98e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180  72 RTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEEAVQILLKHSADVNARDKNWQTPLHIAAANKAVK 151
Cdd:PHA02875    3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 152 CAESLvpLLSNVNVSD---RAGRTALHHAAFSGHGEMVKLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVSHGAE 228
Cdd:PHA02875   83 AVEEL--LDLGKFADDvfyKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKAC 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907098180 229 VTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDmnePNAYGNTP-LHVACY---NGQDVVVNELIDCGANVN 296
Cdd:PHA02875  161 LDIEDCCGCTPLIIAMAKGDIAICKMLLDSGAN---IDYFGKNGcVAALCYaieNNKIDIVRLFIKRGADCN 229
Ank_2 pfam12796
Ankyrin repeats (3 copies);
240-332 3.23e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 81.70  E-value: 3.23e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 240 LHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDCgANVNQKNEkGFTPLHFAAASTHGAlCL 319
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLE-IV 77
                          90
                  ....*....|...
gi 1907098180 320 ELLVGNGADVNMK 332
Cdd:pfam12796  78 KLLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
75-200 3.33e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 81.70  E-value: 3.33e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180  75 LHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEEAVQILLKHsADVNARDKnwqtplhiaaankavkcae 154
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN------------------- 60
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1907098180 155 slvpllsnvnvsdraGRTALHHAAFSGHGEMVKLLLSRGANINAFD 200
Cdd:pfam12796  61 ---------------GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
42-225 3.77e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 85.79  E-value: 3.77e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180  42 LVQAIFNGDPDEVRALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEEAVQ 121
Cdd:PHA02874  128 LHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIK 207
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 122 ILLKHSADVNARDKNWQTPLHiaaanKAVKCAESLVPLLSN---VNVSDRAGRTALHHA-AFSGHGEMVKLLLSRGANIN 197
Cdd:PHA02874  208 LLIDHGNHIMNKCKNGFTPLH-----NAIIHNRSAIELLINnasINDQDIDGSTPLHHAiNPPCDIDIIDILLYHKADIS 282
                         170       180
                  ....*....|....*....|....*....
gi 1907098180 198 AFDKKDRRAIHWA-AYMGHIEVVKLLVSH 225
Cdd:PHA02874  283 IKDNKGENPIDTAfKYINKDPVIKDIIAN 311
PHA02878 PHA02878
ankyrin repeat protein; Provisional
54-225 9.91e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 81.46  E-value: 9.91e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180  54 VRALIFKKEDVNFQDNEK-RTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEEAVQILLKHSADVNA 132
Cdd:PHA02878  150 TKLLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDA 229
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 133 RDKNWQTPLHIAAAnkAVKCAESLVPLL---SNVNV-SDRAGRTALHHAAFSghGEMVKLLLSRGANINAFDKKDRRAIH 208
Cdd:PHA02878  230 RDKCGNTPLHISVG--YCKDYDILKLLLehgVDVNAkSYILGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLS 305
                         170
                  ....*....|....*....
gi 1907098180 209 WAA--YMGhIEVVKLLVSH 225
Cdd:PHA02878  306 SAVkqYLC-INIGRILISN 323
PHA02876 PHA02876
ankyrin repeat protein; Provisional
48-250 1.27e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 81.65  E-value: 1.27e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180  48 NG-DPDEVRALIFKKEDVNFQDNEKRTPLHAAAYLG-DAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEEAVQILLK 125
Cdd:PHA02876  317 NGyDTENIRTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLD 396
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 126 HSADVNARDKNWQTPLHIA-AANKAVKCAESLVPLLSNVNVSDRAGRTALHHAAFSG-HGEMVKLLLSRGANINAFDKKD 203
Cdd:PHA02876  397 YGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQN 476
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1907098180 204 RRAIHWAayMGHIEVVKLLVSHGAEVtcKDKKSytpLHAAASSGMIS 250
Cdd:PHA02876  477 QYPLLIA--LEYHGIVNILLHYGAEL--RDSRV---LHKSLNDNMFS 516
PHA02798 PHA02798
ankyrin-like protein; Provisional
35-340 1.95e-16

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 80.65  E-value: 1.95e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180  35 SGNVLPSLVQAIFNG-DPDEVralifKKEDVNFQDNEKRTPLhaaaylgDAEIIELLILSGARVNAKDSKWLTPLHRAVA 113
Cdd:PHA02798   13 SDNVKLSTVKLLIKScNPNEI-----VNEYSIFQKYLQRDSP-------STDIVKLFINLGANVNGLDNEYSTPLCTILS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 114 SCSE-----EAVQILLKHSADVNARDKNWQTPLHIAAANKAVKCAESLVPLLSN---VNVSDRAGRTALHHAAFSGHG-- 183
Cdd:PHA02798   81 NIKDykhmlDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLFMIENgadTTLLDKDGFTMLQVYLQSNHHid 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 184 -EMVKLLLSRGANINAFDkkdrraiHWAAYmghievvkllvshgAEVTCKDKKSYTPLHAaassgmiSVVKYLLDLGVDM 262
Cdd:PHA02798  161 iEIIKLLLEKGVDINTHN-------NKEKY--------------DTLHCYFKYNIDRIDA-------DILKLFVDNGFII 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 263 NEPNAYGNTP----LHVACYNGQDVVVN--ELIDCGANVNQKNEKGFTPLHFAAASTHGALClELLVGNGADVNMKSKDG 336
Cdd:PHA02798  213 NKENKSHKKKfmeyLNSLLYDNKRFKKNilDFIFSYIDINQVDELGFNPLYYSVSHNNRKIF-EYLLQLGGDINIITELG 291

                  ....
gi 1907098180 337 KTPL 340
Cdd:PHA02798  292 NTCL 295
PHA03095 PHA03095
ankyrin-like protein; Provisional
47-198 6.43e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 78.91  E-value: 6.43e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180  47 FNGDPDEVRALIFKKEDVNFQDNEKRTPLHaaAYLG----DAEIIELLILSGARVNAKDSKWLTPLH------RAVASCS 116
Cdd:PHA03095  128 FNINPKVIRLLLRKGADVNALDLYGMTPLA--VLLKsrnaNVELLRLLIDAGADVYAVDDRFRSLLHhhlqsfKPRARIV 205
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 117 EEavqiLLKHSADVNARDKNWQTPLHIAAANKAvkCAESLV-PLLSN---VNVSDRAGRTALHHAAFSGHGEMVKLLLSR 192
Cdd:PHA03095  206 RE----LIRAGCDPAATDMLGNTPLHSMATGSS--CKRSLVlPLLIAgisINARNRYGQTPLHYAAVFNNPRACRRLIAL 279

                  ....*.
gi 1907098180 193 GANINA 198
Cdd:PHA03095  280 GADINA 285
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
60-231 1.72e-15

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 78.37  E-value: 1.72e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180  60 KKEDVNFQDNEKRTPLHAAAYL------GDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEEAVQILLKHSADVNAR 133
Cdd:PLN03192  508 NVGDLLGDNGGEHDDPNMASNLltvastGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIR 587
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 134 DKNWQTPLHIAAANKAVKCAESLVPLLSnvnVSD-RAGRTALHHAAFSGHGEMVKLLLSRGANINAFDKKDRRAIHWAAY 212
Cdd:PLN03192  588 DANGNTALWNAISAKHHKIFRILYHFAS---ISDpHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMA 664
                         170
                  ....*....|....*....
gi 1907098180 213 MGHIEVVKLLVSHGAEVTC 231
Cdd:PLN03192  665 EDHVDMVRLLIMNGADVDK 683
PHA02875 PHA02875
ankyrin repeat protein; Provisional
203-394 2.63e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 76.95  E-value: 2.63e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 203 DRRAIHWAAYMGHIEVVKLLVSHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGV--DMNEPNAygNTPLHVACYNG 280
Cdd:PHA02875    2 DQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAipDVKYPDI--ESELHDAVEEG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 281 QDVVVNELIDCGANVNQK-NEKGFTPLHFAAASTHGALcLELLVGNGADVNMKSKDGKTPLHMTALHGRFSRSQTIIQSG 359
Cdd:PHA02875   80 DVKAVEELLDLGKFADDVfYKDGMTPLHLATILKKLDI-MKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHK 158
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1907098180 360 AVIDCEDKNGNTPLHIAARYGHELLINTLITSGAD 394
Cdd:PHA02875  159 ACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGAN 193
PHA02875 PHA02875
ankyrin repeat protein; Provisional
171-395 5.98e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 75.80  E-value: 5.98e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 171 RTALHHAAFSGHGEMVKLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVSHGAEVTCKDKKSYTPLHAAASSGMIS 250
Cdd:PHA02875    3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 251 VVKYLLDLGVDMNEP-NAYGNTPLHVACYNGQDVVVNELIDCGANVNQKNEKGFTPLHFAAASTHGALcLELLVGNGADV 329
Cdd:PHA02875   83 AVEELLDLGKFADDVfYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKG-IELLIDHKACL 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907098180 330 NMKSKDGKTPLHMTALHGRFSRSQTIIQSGAVIDCEDKNGNTPLHIAARYGHEL-LINTLITSGADT 395
Cdd:PHA02875  162 DIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIdIVRLFIKRGADC 228
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
104-289 1.27e-14

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: 75.43  E-value: 1.27e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 104 WLTPLHRAVASCSEEAVQILLK-HSADVNARDKNWQTPLHIAAANKAVKCAESL---VPLLSNVNV-SD-RAGRTALHHA 177
Cdd:cd22192    17 SESPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLmeaAPELVNEPMtSDlYQGETALHIA 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 178 AFSGHGEMVKLLLSRGANIN-------AFDKKDRRAIHW-------AAYMGHIEVVKLLVSHGAEVTCKDKKSYTPLHAA 243
Cdd:cd22192    97 VVNQNLNLVRELIARGADVVspratgtFFRPGPKNLIYYgehplsfAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHIL 176
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907098180 244 ASSGMISVVKYLLDLGVDMNE----------PNAYGNTPLHVACYNGQDVVVNELI 289
Cdd:cd22192   177 VLQPNKTFACQMYDLILSYDKeddlqpldlvPNNQGLTPFKLAAKEGNIVMFQHLV 232
PHA03095 PHA03095
ankyrin-like protein; Provisional
48-198 2.07e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 74.29  E-value: 2.07e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180  48 NGDPDEVRALIFKKEDVNFQDNEKRTPLH--AAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEEAVQI--L 123
Cdd:PHA03095  164 NANVELLRLLIDAGADVYAVDDRFRSLLHhhLQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpL 243
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907098180 124 LKHSADVNARDKNWQTPLHIAAA-NKAVKCAEsLVPLLSNVNVSDRAGRTALHHAAFSGHGEMVKLLLSRGANINA 198
Cdd:PHA03095  244 LIAGISINARNRYGQTPLHYAAVfNNPRACRR-LIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAET 318
Ank_2 pfam12796
Ankyrin repeats (3 copies);
273-366 8.17e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 63.60  E-value: 8.17e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 273 LHVACYNGQDVVVNELIDCGANVNQKNEKGFTPLHFAAASTHGALCLELLvgNGADVNMKSkDGKTPLHMTALHGRFSRS 352
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL--EHADVNLKD-NGRTALHYAARSGHLEIV 77
                          90
                  ....*....|....
gi 1907098180 353 QTIIQSGAVIDCED 366
Cdd:pfam12796  78 KLLLEKGADINVKD 91
Ank_4 pfam13637
Ankyrin repeats (many copies);
170-223 1.11e-12

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 62.29  E-value: 1.11e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907098180 170 GRTALHHAAFSGHGEMVKLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLV 223
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
306-394 1.67e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 62.83  E-value: 1.67e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 306 LHFAAASTHgALCLELLVGNGADVNMKSKDGKTPLHMTALHGRFSRSQTIIQSgAVIDCEDkNGNTPLHIAARYGHELLI 385
Cdd:pfam12796   1 LHLAAKNGN-LELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIV 77

                  ....*....
gi 1907098180 386 NTLITSGAD 394
Cdd:pfam12796  78 KLLLEKGAD 86
Ank_4 pfam13637
Ankyrin repeats (many copies);
204-256 5.47e-12

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 60.37  E-value: 5.47e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907098180 204 RRAIHWAAYMGHIEVVKLLVSHGAEVTCKDKKSYTPLHAAASSGMISVVKYLL 256
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
239-395 8.58e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 66.44  E-value: 8.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 239 PLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYN----GQDVVVNELIDCGA--------------NVN---- 296
Cdd:PHA02878   40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEpnklGMKEMIRSINKCSVfytlvaikdafnnrNVEifki 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 297 -----QKNEKGFTPLHFAAASTHGAL---CLELLVGNGADVNMKSKD-GKTPLHMTALHGRFSRSQTIIQSGAVIDCEDK 367
Cdd:PHA02878  120 iltnrYKNIQTIDLVYIDKKSKDDIIeaeITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDK 199
                         170       180
                  ....*....|....*....|....*...
gi 1907098180 368 NGNTPLHIAARYGHELLINTLITSGADT 395
Cdd:PHA02878  200 TNNSPLHHAVKHYNKPIVHILLENGAST 227
PHA02989 PHA02989
ankyrin repeat protein; Provisional
85-357 9.50e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 66.30  E-value: 9.50e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180  85 EIIELLILSGARVNAKdSKWLTPL-----HRAVASCS-EEAVQILLKHSADVNARDKNWQTPLhiaaankavkcaeslVP 158
Cdd:PHA02989   51 KIVKLLIDNGADVNYK-GYIETPLcavlrNREITSNKiKKIVKLLLKFGADINLKTFNGVSPI---------------VC 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 159 LLSNVNVSDRagrtalhhaafsghgEMVKLLLSRGANINafDKKDRRA-----IHWAAYMGHIEVVKLLVSHGaeVTCKD 233
Cdd:PHA02989  115 FIYNSNINNC---------------DMLRFLLSKGINVN--DVKNSRGynllhMYLESFSVKKDVIKILLSFG--VNLFE 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 234 KKSY---TPLHAAASSGM----ISVVKYLLDLGVDMNEPNAYGNTPL------HVACYNGQDVVVNeLIDCGANVNQKNE 300
Cdd:PHA02989  176 KTSLyglTPMNIYLRNDIdvisIKVIKYLIKKGVNIETNNNGSESVLesfldnNKILSKKEFKVLN-FILKYIKINKKDK 254
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907098180 301 KGFTPLHFAA-ASTHGALCLELLVGNgaDVNMKSKDGKTPLHMTALHGRFSRSQTIIQ 357
Cdd:PHA02989  255 KGFNPLLISAkVDNYEAFNYLLKLGD--DIYNVSKDGDTVLTYAIKHGNIDMLNRILQ 310
Ank_4 pfam13637
Ankyrin repeats (many copies);
237-281 6.28e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 57.28  E-value: 6.28e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1907098180 237 YTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQ 281
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGN 46
PHA02946 PHA02946
ankyin-like protein; Provisional
79-306 7.94e-11

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 63.53  E-value: 7.94e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180  79 AYLG----DAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEEAVQILLKHSADVNARDKNWQTPLHIAAAnkavkcae 154
Cdd:PHA02946   43 AYCGikglDERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSG-------- 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 155 slvpllSNVNVSDRagrtalhhaafsghgemVKLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVSHGAEVTCKDK 234
Cdd:PHA02946  115 ------TDDEVIER-----------------INLLVQYGAKINNSVDEEGCGPLLACTDPSERVFKKIMSIGFEARIVDK 171
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907098180 235 --KSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNG-QDVVVNELIDCGANVNQKNEKGFTPL 306
Cdd:PHA02946  172 fgKNHIHRHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHIVCSKTvKNVDIINLLLPSTDVNKQNKFGDSPL 246
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
177-335 1.66e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 62.96  E-value: 1.66e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 177 AAFSGHGEMVKLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVSHGAEVTCKDKKSYTPLHAAASSGMISVVKYLL 256
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILY 611
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907098180 257 DLGvDMNEPNAYGNTpLHVACYNGQDVVVNELIDCGANVNQKNEKGFTPLHFAAASTHGALcLELLVGNGADVNMKSKD 335
Cdd:PLN03192  612 HFA-SISDPHAAGDL-LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDM-VRLLIMNGADVDKANTD 687
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
174-256 5.24e-10

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 61.07  E-value: 5.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 174 LHHAAFSGHGEMVKLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVSHGAEVTCKDKKSYTPLHAAASSGMISVVK 253
Cdd:PTZ00322   86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165

                  ...
gi 1907098180 254 YLL 256
Cdd:PTZ00322  166 LLS 168
Ank_4 pfam13637
Ankyrin repeats (many copies);
104-157 6.34e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.59  E-value: 6.34e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907098180 104 WLTPLHRAVASCSEEAVQILLKHSADVNARDKNWQTPLHIAAANKAVKCAESLV 157
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02859 PHA02859
ankyrin repeat protein; Provisional
102-280 7.82e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 58.29  E-value: 7.82e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 102 SKWLTPLHRAVASCSEEAVQillKHSADVNARDKNWQTPLHIAAANKAV--KCAESLVPLLSNVNVSDRA-GRTALHHAA 178
Cdd:PHA02859   19 YRYCNPLFYYVEKDDIEGVK---KWIKFVNDCNDLYETPIFSCLEKDKVnvEILKFLIENGADVNFKTRDnNLSALHHYL 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 179 FSGHG---EMVKLLLSRGANINAFDKKDRRAIHwaAYMGH----IEVVKLLVSHGAEVTCKDKK------SYTPLHAAAS 245
Cdd:PHA02859   96 SFNKNvepEILKILIDSGSSITEEDEDGKNLLH--MYMCNfnvrINVIKLLIDSGVSFLNKDFDnnnilySYILFHSDKK 173
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1907098180 246 sgmisVVKYLLDLGVDMNEPNAYGNTPLHVACYNG 280
Cdd:PHA02859  174 -----IFDFLTSLGIDINETNKSGYNCYDLIKFRN 203
Ank_4 pfam13637
Ankyrin repeats (many copies);
139-190 9.11e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.82  E-value: 9.11e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907098180 139 TPLHIAAANKAVKCAESLVPLLSNVNVSDRAGRTALHHAAFSGHGEMVKLLL 190
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
238-375 1.03e-09

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: 60.03  E-value: 1.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 238 TPLHAAASSGMISVVKYLLDL-GVDMNEPNAYGNTPLHVACYNGQDVVVNELIDCGAN-VNQKNE----KGFTPLHFAAA 311
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKCpSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNEPMTsdlyQGETALHIAVV 98
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907098180 312 STHGALcLELLVGNGADVN---------MKSKD-----GKTPLHMTALHGRFSRSQTIIQSGAVIDCEDKNGNTPLHI 375
Cdd:cd22192    99 NQNLNL-VRELIARGADVVspratgtffRPGPKnliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHI 175
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
213-397 1.29e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 59.88  E-value: 1.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 213 MGHIEVVKLLVSHGAEVTckDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDCG 292
Cdd:PLN03192  504 LHDLNVGDLLGDNGGEHD--DPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHA 581
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 293 ANVNQKNEKGFTPLHFAAASTHGALcLELLVGNGADVNMKSkdGKTPLHMTALHGRFSRSQTIIQSGAVIDCEDKNGNTP 372
Cdd:PLN03192  582 CNVHIRDANGNTALWNAISAKHHKI-FRILYHFASISDPHA--AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATA 658
                         170       180
                  ....*....|....*....|....*
gi 1907098180 373 LHIAARYGHELLINTLITSGADTAK 397
Cdd:PLN03192  659 LQVAMAEDHVDMVRLLIMNGADVDK 683
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
63-306 2.53e-09

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 59.16  E-value: 2.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180  63 DVNFQDNEKRTP-LHAaaYLG----DAEIIELLILSGARVNAKDSKWLTPLHRAV--ASCSEEAVQILLKHSADVNARDK 135
Cdd:PHA02716  168 NLNYVCKKTGYGiLHA--YLGnmyvDIDILEWLCNNGVNVNLQNNHLITPLHTYLitGNVCASVIKKIIELGGDMDMKCV 245
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 136 NWQTPLHIAAANkavkcAESLVPLLSNVNVSDRAGRTalhhaaFSGHGEMVKLLLSRGANINafdkkdrraihwaaymgh 215
Cdd:PHA02716  246 NGMSPIMTYIIN-----IDNINPEITNIYIESLDGNK------VKNIPMILHSYITLARNID------------------ 296
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 216 IEVVKLLVSHGAEVTCKDKKSYTPLHAAASSGMIS--VVKYLLDLGVDMNEPNAYGNTPLH--------VACYNGQ---D 282
Cdd:PHA02716  297 ISVVYSFLQPGVKLHYKDSAGRTCLHQYILRHNIStdIIKLLHEYGNDLNEPDNIGNTVLHtylsmlsvVNILDPEtdnD 376
                         250       260
                  ....*....|....*....|....*..
gi 1907098180 283 V---VVNELIDCGANVNQKNEKGFTPL 306
Cdd:PHA02716  377 IrldVIQCLISLGADITAVNCLGYTPL 403
PHA03100 PHA03100
ankyrin repeat protein; Provisional
52-136 3.74e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 58.14  E-value: 3.74e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180  52 DEVRALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEEAVQILLKHSADVN 131
Cdd:PHA03100  173 NRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252

                  ....*
gi 1907098180 132 ARDKN 136
Cdd:PHA03100  253 TIIET 257
Ank_4 pfam13637
Ankyrin repeats (many copies);
72-124 4.54e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.89  E-value: 4.54e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907098180  72 RTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEEAVQILL 124
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
219-291 7.84e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 57.60  E-value: 7.84e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907098180 219 VKLLVSHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDC 291
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
113-191 8.71e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 57.22  E-value: 8.71e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907098180 113 ASCSEEAVQILLKHSADVNARDKNWQTPLHIAAANKAVKCAESLVPLLSNVNVSDRAGRTALHHAAFSGHGEMVKLLLS 191
Cdd:PTZ00322   91 ASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
PHA02859 PHA02859
ankyrin repeat protein; Provisional
236-394 1.19e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 54.83  E-value: 1.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 236 SYT-PLHAAASSGMISVVKYLLDLgvdMNEPNAYGNTPLHvACYNGQDVVVNE---LIDCGANVNQK-NEKGFTPLHFAA 310
Cdd:PHA02859   20 RYCnPLFYYVEKDDIEGVKKWIKF---VNDCNDLYETPIF-SCLEKDKVNVEIlkfLIENGADVNFKtRDNNLSALHHYL 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 311 ASTHGAL--CLELLVGNGADVNMKSKDGKTPLH--MTALHGRFSRSQTIIQSGAVIDCEDKNGNTPLHIAARYGHELLI- 385
Cdd:PHA02859   96 SFNKNVEpeILKILIDSGSSITEEDEDGKNLLHmyMCNFNVRINVIKLLIDSGVSFLNKDFDNNNILYSYILFHSDKKIf 175

                  ....*....
gi 1907098180 386 NTLITSGAD 394
Cdd:PHA02859  176 DFLTSLGID 184
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
58-277 3.49e-08

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: 55.47  E-value: 3.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180  58 IFKKEDVNFQDNEKrtplhaaAYLGDAEIIELLILSGARVNAK-------DSKWLTPLHRAVA-SCSEEAVQILLKHSAD 129
Cdd:TIGR00870   6 IVPAEESPLSDEEK-------AFLPAAERGDLASVYRDLEEPKklnincpDRLGRSALFVAAIeNENLELTELLLNLSCR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 130 VNARDknwqTPLHIAAANKAVKCAESLVPLLSN---------VNVSDR----AGRTALHHAAFSGHGEMVKLLLSRGANI 196
Cdd:TIGR00870  79 GAVGD----TLLHAISLEYVDAVEAILLHLLAAfrksgplelANDQYTseftPGITALHLAAHRQNYEIVKLLLERGASV 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 197 NA------FDKKDRRA--------IHWAAYMGHIEVVKLLVSHGAEVTCKDKKSYTPLHAAA------------SSGMIS 250
Cdd:TIGR00870 155 PAracgdfFVKSQGVDsfyhgespLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVmenefkaeyeelSCQMYN 234
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1907098180 251 VVKYLLDLGVDMNE----PNAYGNTPLHVAC 277
Cdd:TIGR00870 235 FALSLLDKLRDSKEleviLNHQGLTPLKLAA 265
PHA02875 PHA02875
ankyrin repeat protein; Provisional
52-197 1.36e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 53.07  E-value: 1.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180  52 DEVRALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEEAVQILLKHSADVN 131
Cdd:PHA02875  116 DIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANID 195
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907098180 132 ArdknwqtplhiaaankavkcaeslvpllsnvnVSDRAGRTALHHAAFSGHGEMVKLLLSRGANIN 197
Cdd:PHA02875  196 Y--------------------------------FGKNGCVAALCYAIENNKIDIVRLFIKRGADCN 229
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
311-380 2.34e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.98  E-value: 2.34e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 311 ASTHGALCLELLVGNGADVNMKSKDGKTPLHMTALHGRFSRSQTIIQSGAVIDCEDKNGNTPLHIAARYG 380
Cdd:PTZ00322   90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENG 159
Ank_5 pfam13857
Ankyrin repeats (many copies);
288-342 2.35e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 47.34  E-value: 2.35e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907098180 288 LIDCG-ANVNQKNEKGFTPLHFAAasTHGAL-CLELLVGNGADVNMKSKDGKTPLHM 342
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAA--KYGALeIVRVLLAYGVDLNLKDEEGLTALDL 55
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
220-345 3.00e-07

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: 52.32  E-value: 3.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 220 KLLVSHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDM-NEP---NAY-GNTPLHVACYNGQDVVVNELIDCGAN 294
Cdd:cd22192    35 KLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELvNEPmtsDLYqGETALHIAVVNQNLNLVRELIARGAD 114
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907098180 295 VN---------QKNEK-----GFTPLHFAAASTHGALcLELLVGNGADVNMKSKDGKTPLHMTAL 345
Cdd:cd22192   115 VVspratgtffRPGPKnliyyGEHPLSFAACVGNEEI-VRLLIEHGADIRAQDSLGNTVLHILVL 178
Ank_5 pfam13857
Ankyrin repeats (many copies);
222-276 4.03e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.57  E-value: 4.03e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907098180 222 LVSHG-AEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVA 276
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
42-127 4.76e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.82  E-value: 4.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180  42 LVQAIFNGDPDEVRALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEEAVQ 121
Cdd:PTZ00322   86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165

                  ....*.
gi 1907098180 122 ILLKHS 127
Cdd:PTZ00322  166 LLSRHS 171
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
170-201 8.41e-07

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: 44.97  E-value: 8.41e-07
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1907098180 170 GRTALHHAAFS-GHGEMVKLLLSRGANINAFDK 201
Cdd:pfam00023   2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
Ank_4 pfam13637
Ankyrin repeats (many copies);
269-323 1.18e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.34  E-value: 1.18e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907098180 269 GNTPLHVACYNGQDVVVNELIDCGANVNQKNEKGFTPLHFAAASTHGAlCLELLV 323
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVE-VLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
338-389 1.25e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.96  E-value: 1.25e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907098180 338 TPLHMTALHGRFSRSQTIIQSGAVIDCEDKNGNTPLHIAARYGHELLINTLI 389
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
244-350 1.34e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.28  E-value: 1.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 244 ASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDCGANVNQKNEKGFTPLHFAAASTHGALcLELLV 323
Cdd:PTZ00322   90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREV-VQLLS 168
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1907098180 324 GN-------GADVNMKSKDGKTPLH----MTALHGRFS 350
Cdd:PTZ00322  169 RHsqchfelGANAKPDSFTGKPPSLedspISSHHPDFS 206
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
73-210 1.81e-06

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 50.01  E-value: 1.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180  73 TPLHAAAYLGDAEIIELLILSGARVNA---------KDSKWLT-----PLHRAVASCSEEAVQILLKHSADVNARDKNWQ 138
Cdd:cd22192    91 TALHIAVVNQNLNLVRELIARGADVVSpratgtffrPGPKNLIyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGN 170
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 139 TPLHIAA--ANKAVKCAE-----SLVPLLSNVNVS---DRAGRTALHHAAFSGHGEMVKLLLSRganinafdkkdRRAIH 208
Cdd:cd22192   171 TVLHILVlqPNKTFACQMydlilSYDKEDDLQPLDlvpNNQGLTPFKLAAKEGNIVMFQHLVQK-----------RRHIQ 239

                  ..
gi 1907098180 209 WA 210
Cdd:cd22192   240 WT 241
Ank_5 pfam13857
Ankyrin repeats (many copies);
123-177 2.04e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.64  E-value: 2.04e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907098180 123 LLKH-SADVNARDKNWQTPLHIAAANKAVKCAESLVPLLSNVNVSDRAGRTALHHA 177
Cdd:pfam13857   1 LLEHgPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
39-91 2.23e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.57  E-value: 2.23e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907098180  39 LPSLVQAIFNGDPDEVRALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLI 91
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
138-289 3.40e-06

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: 49.11  E-value: 3.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 138 QTPLHIAAANKAVKCAESLVPLLSNVNVSDRA--------------GRTALHHAAFSGHGEMVKLLLSRGANINA----- 198
Cdd:cd21882    27 KTCLHKAALNLNDGVNEAIMLLLEAAPDSGNPkelvnapctdefyqGQTALHIAIENRNLNLVRLLVENGADVSAratgr 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 199 -FDKKDRRAIHW-------AAYMGHIEVVKLLVSHGAE---VTCKDKKSYTPLHA---------AASSGMISVVKYLLDL 258
Cdd:cd21882   107 fFRKSPGNLFYFgelplslAACTNQEEIVRLLLENGAQpaaLEAQDSLGNTVLHAlvlqadntpENSAFVCQMYNLLLSY 186
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1907098180 259 G------VDMNE-PNAYGNTPLHVACYNGQDVVVNELI 289
Cdd:cd21882   187 GahldptQQLEEiPNHQGLTPLKLAAVEGKIVMFQHIL 224
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
170-198 4.38e-06

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.96  E-value: 4.38e-06
                           10        20
                   ....*....|....*....|....*....
gi 1907098180  170 GRTALHHAAFSGHGEMVKLLLSRGANINA 198
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
255-309 5.02e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.49  E-value: 5.02e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907098180 255 LLDLG-VDMNEPNAYGNTPLHVACYNGQDVVVNELIDCGANVNQKNEKGFTPLHFA 309
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
82-147 6.66e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.36  E-value: 6.66e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907098180  82 GDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEEAVQILLKHSADVNARDKNWQTPLHIAAAN 147
Cdd:PTZ00322   93 GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEEN 158
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
142-228 7.15e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.97  E-value: 7.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 142 HIAAANKAVKcAESLVPLLSNVNVSDRAGRTALHHAAFSGHGEMVKLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKL 221
Cdd:PTZ00322   88 QLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166

                  ....*..
gi 1907098180 222 LVSHGAE 228
Cdd:PTZ00322  167 LSRHSQC 173
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
304-397 7.20e-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: 48.09  E-value: 7.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 304 TPLhFAAASTHGALCLE-LLVGNGADVNMKSKDGKTPLHMTALHGRFSRSQTIIQSGA-----VIDCEDKNGNTPLHIAA 377
Cdd:cd22192    19 SPL-LLAAKENDVQAIKkLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPelvnePMTSDLYQGETALHIAV 97
                          90       100
                  ....*....|....*....|
gi 1907098180 378 RYGHELLINTLITSGADTAK 397
Cdd:cd22192    98 VNQNLNLVRELIARGADVVS 117
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
170-198 8.46e-06

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 42.24  E-value: 8.46e-06
                          10        20
                  ....*....|....*....|....*....
gi 1907098180 170 GRTALHHAAFSGHGEMVKLLLSRGANINA 198
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
304-356 9.25e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.65  E-value: 9.25e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907098180 304 TPLHFAAASTHGAlCLELLVGNGADVNMKSKDGKTPLHMTALHGRFSRSQTII 356
Cdd:pfam13637   3 TALHAAAASGHLE-LLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
268-300 1.25e-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: 1.25e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1907098180 268 YGNTPLHVACY-NGQDVVVNELIDCGANVNQKNE 300
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
PHA02798 PHA02798
ankyrin-like protein; Provisional
251-365 1.30e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 47.14  E-value: 1.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 251 VVKYLLDLGVDMNEPNAYGNTPL-----HVACYNGQDVVVNELIDCGANVNQKNEKGFTPLhFAAASTHGALCLELL--- 322
Cdd:PHA02798   53 IVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPL-YCLLSNGYINNLEILlfm 131
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1907098180 323 VGNGADVNMKSKDGKTPLhmtalhgrfsrsQTIIQSGAVIDCE 365
Cdd:PHA02798  132 IENGADTTLLDKDGFTML------------QVYLQSNHHIDIE 162
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
268-296 1.54e-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: 41.42  E-value: 1.54e-05
                           10        20
                   ....*....|....*....|....*....
gi 1907098180  268 YGNTPLHVACYNGQDVVVNELIDCGANVN 296
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
264-380 1.57e-05

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 47.06  E-value: 1.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 264 EPNAYGNTPLHVACYNGQDVVVNELIDCGANVNQK----------NEKGF----TPLHFAAASTHGALcLELLVGNGAD- 328
Cdd:cd22194   136 EEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHakgvffnpkyKHEGFyfgeTPLALAACTNQPEI-VQLLMEKESTd 214
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907098180 329 VNMKSKDGKTPLHMTALHGRFSRSQT--IIQSGAVI--DCEDKN--------GNTPLHIAARYG 380
Cdd:cd22194   215 ITSQDSRGNTVLHALVTVAEDSKTQNdfVKRMYDMIllKSENKNletirnneGLTPLQLAAKMG 278
PHA02946 PHA02946
ankyin-like protein; Provisional
219-375 2.78e-05

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 45.82  E-value: 2.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 219 VKLLVSHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVV--VNELIDCGANVN 296
Cdd:PHA02946   55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIerINLLVQYGAKIN 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 297 QK-NEKGFTPLhfAAASTHGALCLELLVGNGADVNMKSKDGKTPLH--MTALHGRFSRSQTIIQSGAVIDCEDKNGNTPL 373
Cdd:PHA02946  135 NSvDEEGCGPL--LACTDPSERVFKKIMSIGFEARIVDKFGKNHIHrhLMSDNPKASTISWMMKLGISPSKPDHDGNTPL 212

                  ..
gi 1907098180 374 HI 375
Cdd:PHA02946  213 HI 214
Ank_5 pfam13857
Ankyrin repeats (many copies);
62-111 5.15e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.79  E-value: 5.15e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907098180  62 EDVNFQDNEKRTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRA 111
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
189-243 6.40e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.41  E-value: 6.40e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907098180 189 LLSRG-ANINAFDKKDRRAIHWAAYMGHIEVVKLLVSHGAEVTCKDKKSYTPLHAA 243
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
95-144 6.59e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.41  E-value: 6.59e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907098180  95 ARVNAKDSKWLTPLHRAVASCSEEAVQILLKHSADVNARDKNWQTPLHIA 144
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
170-310 7.14e-05

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 44.75  E-value: 7.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 170 GRTALHHAAFSGHGEMVKLLLSRGANINA------FDKKDRraiHWAAYMGHievvkllvshgaevtckdkksyTPLHAA 243
Cdd:cd22194   141 GQTALNIAIERRQGDIVKLLIAKGADVNAhakgvfFNPKYK---HEGFYFGE----------------------TPLALA 195
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 244 ASSGMISVVKYLLDlgvdmNEPNAY------GNTPLH----VA-CYNGQDVVVNELIDC------GANVNQ-KNEKGFTP 305
Cdd:cd22194   196 ACTNQPEIVQLLME-----KESTDItsqdsrGNTVLHalvtVAeDSKTQNDFVKRMYDMillkseNKNLETiRNNEGLTP 270

                  ....*
gi 1907098180 306 LHFAA 310
Cdd:cd22194   271 LQLAA 275
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
237-264 9.34e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.11  E-value: 9.34e-05
                           10        20
                   ....*....|....*....|....*...
gi 1907098180  237 YTPLHAAASSGMISVVKYLLDLGVDMNE 264
Cdd:smart00248   3 RTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02989 PHA02989
ankyrin repeat protein; Provisional
83-394 9.99e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 44.35  E-value: 9.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180  83 DAEIIELLILSGARVNA--KDSKWLTpLHRAVASCSEEAVQILLKHSADVNARDKnWQTPLhiaaankavkCAeslvpLL 160
Cdd:PHA02989   15 DKNALEFLLRTGFDVNEeyRGNSILL-LYLKRKDVKIKIVKLLIDNGADVNYKGY-IETPL----------CA-----VL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 161 SNVNVSDRAGRtalhhaafsghgEMVKLLLSRGANINAFDKKDRRAIHWAAYMGHI---EVVKLLVSHGAEV-TCKDKKS 236
Cdd:PHA02989   78 RNREITSNKIK------------KIVKLLLKFGADINLKTFNGVSPIVCFIYNSNInncDMLRFLLSKGINVnDVKNSRG 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 237 YTPLHAAASSGMIS--VVKYLLDLGVDMNEP-NAYGNTPLHVACYNGQDV----VVNELIDCGANVNQKNEkgftplhfa 309
Cdd:PHA02989  146 YNLLHMYLESFSVKkdVIKILLSFGVNLFEKtSLYGLTPMNIYLRNDIDVisikVIKYLIKKGVNIETNNN--------- 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 310 aasTHGALCLELLVGNGAdvnMKSKDgktplhMTALHgrfsrsqtIIQSGAVIDCEDKNGNTPLHIAARYGHELLINTLI 389
Cdd:PHA02989  217 ---GSESVLESFLDNNKI---LSKKE------FKVLN--------FILKYIKINKKDKKGFNPLLISAKVDNYEAFNYLL 276

                  ....*
gi 1907098180 390 TSGAD 394
Cdd:PHA02989  277 KLGDD 281
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
301-334 1.73e-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: 38.42  E-value: 1.73e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1907098180 301 KGFTPLHFAAASTHGALCLELLVGNGADVNMKSK 334
Cdd:pfam00023   1 DGNTPLHLAAGRRGNLEIVKLLLSKGADVNARDK 34
PHA02884 PHA02884
ankyrin repeat protein; Provisional
251-345 2.03e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 43.05  E-value: 2.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 251 VVKYLLDLGVDMNEP-----NAYgNTPLHVACYNGQDVVVNELIDCGANVNQ-KNEKGFTPLHFAAasTHGAL-CLELLV 323
Cdd:PHA02884   48 IIDAILKLGADPEAPfplseNSK-TNPLIYAIDCDNDDAAKLLIRYGADVNRyAEEAKITPLYISV--LHGCLkCLEILL 124
                          90       100
                  ....*....|....*....|..
gi 1907098180 324 GNGADVNMKSKDGKTPLHMTAL 345
Cdd:PHA02884  125 SYGADINIQTNDMVTPIELALM 146
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
268-296 2.13e-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: 38.01  E-value: 2.13e-04
                          10        20
                  ....*....|....*....|....*....
gi 1907098180 268 YGNTPLHVACYNGQDVVVNELIDCGANVN 296
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
PHA02884 PHA02884
ankyrin repeat protein; Provisional
85-225 2.43e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 42.66  E-value: 2.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180  85 EIIELLILSGARVNAK----DSKWLTPLHRAVASCSEEAVQILLKHSADVNARDKNWQ-TPLHIAAANKAVKCAESLVPL 159
Cdd:PHA02884   47 DIIDAILKLGADPEAPfplsENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKiTPLYISVLHGCLKCLEILLSY 126
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907098180 160 LSNVNVSDRAGRTALHHAAFSGHGEMVKLLlsRGANINAFDKKDRRaihwaaYMGHIEVVKLLVSH 225
Cdd:PHA02884  127 GADINIQTNDMVTPIELALMICNNFLAFMI--CDNEISNFYKHPKK------ILINFDILKILVSH 184
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
368-394 2.83e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.95  E-value: 2.83e-04
                           10        20
                   ....*....|....*....|....*..
gi 1907098180  368 NGNTPLHIAARYGHELLINTLITSGAD 394
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
202-312 3.35e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. 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.


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 42.87  E-value: 3.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 202 KDRRAIHWAAYMGHIEVVKLLVSHGAEVTC-------KDKKSYT-------PLHAAASSGMISVVKYLLD---LGVDMNE 264
Cdd:cd22196    93 KGQTALHIAIERRNMHLVELLVQNGADVHArasgeffKKKKGGPgfyfgelPLSLAACTNQLDIVKFLLEnphSPADISA 172
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907098180 265 PNAYGNTPLHVACYNGQDVVVN---------ELIDCGANVNQK-------NEKGFTPLHFAAAS 312
Cdd:cd22196   173 RDSMGNTVLHALVEVADNTPENtkfvtkmynEILILGAKIRPLlkleeitNKKGLTPLKLAAKT 236
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
72-101 3.84e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 37.65  E-value: 3.84e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1907098180  72 RTPLHAAAY-LGDAEIIELLILSGARVNAKD 101
Cdd:pfam00023   3 NTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
PHA02736 PHA02736
Viral ankyrin protein; Provisional
167-277 4.02e-04

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 40.63  E-value: 4.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 167 DRAGRTALHHaaFSGHGEMVKLLLSRGANINA-------FDKKDRRAIHWAAYMGHI---EVVKLLVSHGAEVTCKDKK- 235
Cdd:PHA02736   14 DIEGENILHY--LCRNGGVTDLLAFKNAISDEnrylvleYNRHGKQCVHIVSNPDKAdpqEKLKLLMEWGADINGKERVf 91
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1907098180 236 SYTPLHAAASSGMISVVKYLLDL-GVDMNEPNAYGNTPLHVAC 277
Cdd:PHA02736   92 GNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYVAC 134
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
206-234 4.19e-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: 4.19e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1907098180 206 AIHWAAYM-GHIEVVKLLVSHGAEVTCKDK 234
Cdd:pfam00023   5 PLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
206-231 4.81e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.18  E-value: 4.81e-04
                           10        20
                   ....*....|....*....|....*.
gi 1907098180  206 AIHWAAYMGHIEVVKLLVSHGAEVTC 231
Cdd:smart00248   5 PLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
106-135 4.86e-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: 4.86e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1907098180 106 TPLHRAVASC-SEEAVQILLKHSADVNARDK 135
Cdd:pfam00023   4 TPLHLAAGRRgNLEIVKLLLSKGADVNARDK 34
Ank_5 pfam13857
Ankyrin repeats (many copies);
162-201 5.41e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.71  E-value: 5.41e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1907098180 162 NVNVSDRAGRTALHHAAFSGHGEMVKLLLSRGANINAFDK 201
Cdd:pfam13857   8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDE 47
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
170-312 1.33e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 40.93  E-value: 1.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 170 GRTALHHAAFSGHGEMVKLLLSRGANINA------FDKKDRRAihwAAYMGHievvkllvshgaevtckdkksyTPLHAA 243
Cdd:cd22193    76 GQTALHIAIERRQGDIVALLVENGADVHAhakgrfFQPKYQGE---GFYFGE----------------------LPLSLA 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 244 ASSGMISVVKYLLD---LGVDMNEPNAYGNTPLHVACYNGQDVVVN---------ELIDCGANVNQ-------KNEKGFT 304
Cdd:cd22193   131 ACTNQPDIVQYLLEnehQPADIEAQDSRGNTVLHALVTVADNTKENtkfvtrmydMILIRGAKLCPtveleeiRNNDGLT 210

                  ....*...
gi 1907098180 305 PLHFAAAS 312
Cdd:cd22193   211 PLQLAAKM 218
PHA02791 PHA02791
ankyrin-like protein; Provisional
127-305 1.37e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 40.41  E-value: 1.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 127 SADVNARDKNWQTPLHIAAANKAVKCAESLVPLLSNVNVSDRagRTALHHAAFSGHGEMVKLLLSRGANINAFDKKDRRA 206
Cdd:PHA02791   20 SKDAFKADVHGHSALYYAIADNNVRLVCTLLNAGALKNLLEN--EFPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTA 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 207 IHWAAYMGHIEVVKLLVSHGAEVTCKDKKSY-TPLHAAASSGMISVVKYLL-------DLGVDMnepnaygnTPLHVACY 278
Cdd:PHA02791   98 LYYAVDSGNMQTVKLFVKKNWRLMFYGKTGWkTSFYHAVMLNDVSIVSYFLseipstfDLAILL--------SCIHITIK 169
                         170       180
                  ....*....|....*....|....*..
gi 1907098180 279 NGQDVVVNELIDCGANVNQKNEKGFTP 305
Cdd:PHA02791  170 NGHVDMMILLLDYMTSTNTNNSLLFIP 196
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
45-109 1.37e-03

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 40.77  E-value: 1.37e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907098180  45 AIFNGDPDEVRALIFKKEDVN--------FQDNEKRT------PLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLH 109
Cdd:cd22192    96 AVVNQNLNLVRELIARGADVVspratgtfFRPGPKNLiyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
368-394 1.66e-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: 1.66e-03
                          10        20
                  ....*....|....*....|....*...
gi 1907098180 368 NGNTPLHIAA-RYGHELLINTLITSGAD 394
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGAD 28
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
368-394 1.73e-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: 1.73e-03
                          10        20
                  ....*....|....*....|....*..
gi 1907098180 368 NGNTPLHIAARYGHELLINTLITSGAD 394
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGAD 27
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
61-279 2.06e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. 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.


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 40.17  E-value: 2.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180  61 KEDVN--FQDNEKR--TPLHAAAYLGDAEIIELLILSGARVNA------------KDSKWLTPLHRAVASCSEEA--VQI 122
Cdd:cd22196    80 KEFVNaaYTDSYYKgqTALHIAIERRNMHLVELLVQNGADVHArasgeffkkkkgGPGFYFGELPLSLAACTNQLdiVKF 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 123 LLKHS---ADVNARDKNWQTPLHiaaankavkcaeSLVPLLSNvnvsdragrtALHHAAFSghGEMVKLLLSRGANINAF 199
Cdd:cd22196   160 LLENPhspADISARDSMGNTVLH------------ALVEVADN----------TPENTKFV--TKMYNEILILGAKIRPL 215
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 200 DKkdrraihwaaymghIEvvkllvshgaEVTckDKKSYTPLHAAASSGMISVVKYLldLGVDMNEPN-----------AY 268
Cdd:cd22196   216 LK--------------LE----------EIT--NKKGLTPLKLAAKTGKIGIFAYI--LGREIKEPEcrhlsrkftewAY 267
                         250
                  ....*....|.
gi 1907098180 269 GntPLHVACYN 279
Cdd:cd22196   268 G--PVHSSLYD 276
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
237-266 2.34e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 35.34  E-value: 2.34e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1907098180 237 YTPLHAAA-SSGMISVVKYLLDLGVDMNEPN 266
Cdd:pfam00023   3 NTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
237-261 2.59e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 35.31  E-value: 2.59e-03
                          10        20
                  ....*....|....*....|....*
gi 1907098180 237 YTPLHAAASSGMISVVKYLLDLGVD 261
Cdd:pfam13606   3 NTPLHLAARNGRLEIVKLLLENGAD 27
PHA02795 PHA02795
ankyrin-like protein; Provisional
157-198 3.05e-03

ankyrin-like protein; Provisional


Pssm-ID: 165157 [Multi-domain]  Cd Length: 437  Bit Score: 39.59  E-value: 3.05e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1907098180 157 VPLLSNVNVSDRAGRTALHHAAFSGHGEMVKLLLSRGANINA 198
Cdd:PHA02795  208 IPYIEDINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNA 249
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
355-394 4.06e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 39.50  E-value: 4.06e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1907098180 355 IIQSGAVIDCEDKNGNTPLHIAARYGHELLINTLITSGAD 394
Cdd:PTZ00322  101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGAD 140
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
70-210 4.15e-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: 39.09  E-value: 4.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180  70 EKRTPLHAAAYLGDAEIIELLILSGARVNAKDSKWL-------------TPLHRAVASCSEEAVQILLKHSAD---VNAR 133
Cdd:cd21882    72 QGQTALHIAIENRNLNLVRLLVENGADVSARATGRFfrkspgnlfyfgeLPLSLAACTNQEEIVRLLLENGAQpaaLEAQ 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 134 DKNWQTPLH--IAAANKAVKCA--------------ESLVPLLSNVNVSDRAGRTALHHAAFSGHGEMVKLLLSRGANiN 197
Cdd:cd21882   152 DSLGNTVLHalVLQADNTPENSafvcqmynlllsygAHLDPTQQLEEIPNHQGLTPLKLAAVEGKIVMFQHILQREFS-G 230
                         170
                  ....*....|...
gi 1907098180 198 AFDKKDRRAIHWA 210
Cdd:cd21882   231 PYQPLSRKFTEWT 243
PHA02736 PHA02736
Viral ankyrin protein; Provisional
264-393 4.17e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 37.55  E-value: 4.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 264 EPNAYGNTPLHVACYNGqDVV-----VNELIDcgAN---VNQKNEKGFTPLHFAAAS--THGALCLELLVGNGADVNMK- 332
Cdd:PHA02736   12 EPDIEGENILHYLCRNG-GVTdllafKNAISD--ENrylVLEYNRHGKQCVHIVSNPdkADPQEKLKLLMEWGADINGKe 88
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907098180 333 SKDGKTPLHMTALHGRFSRSQTII-QSGAVIDCEDKNGNTPLHIAARYGHELLINTLITSGA 393
Cdd:PHA02736   89 RVFGNTPLHIAVYTQNYELATWLCnQPGVNMEILNYAFKTPYYVACERHDAKMMNILRAKGA 150
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
106-132 4.53e-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: 34.54  E-value: 4.53e-03
                          10        20
                  ....*....|....*....|....*..
gi 1907098180 106 TPLHRAVASCSEEAVQILLKHSADVNA 132
Cdd:pfam13606   4 TPLHLAARNGRLEIVKLLLENGADINA 30
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
29-307 4.87e-03

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 38.97  E-value: 4.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180  29 CLQPPPSGNVLPSLVQAIFNGDPDEVRAlifkkEDVNFQDNEKRTPLHAAAYLGDAEIIELL----ILSGARVNAKDSKW 104
Cdd:cd22194     9 CPSGNCDDMDSPQSPQDDTPSNPNSPSA-----ELAKEEQRDKKKRLKKVSEAAVEELGELLkelkDLSRRRRKTDVPDF 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 105 L-----------TPLHRA---VASCSEEAVQILLKHSAD-------VNAR--DKNW--QTPLHIAAANKAVKCAESLVPL 159
Cdd:cd22194    84 LmhkltasdtgkTCLMKAllnINENTKEIVRILLAFAEEngildrfINAEytEEAYegQTALNIAIERRQGDIVKLLIAK 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 160 LSNVNVSDRA--------------GRTALHHAAFSGHGEMVKLLLSRGANINAF-DKKDRRAIHwAAYM------GHIEV 218
Cdd:cd22194   164 GADVNAHAKGvffnpkykhegfyfGETPLALAACTNQPEIVQLLMEKESTDITSqDSRGNTVLH-ALVTvaedskTQNDF 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 219 VK------LLVSHGAEV-TCKDKKSYTPLHAAASSGMISVVKYLLDLGVDmNEPN----------AYGntPLHVACYN-- 279
Cdd:cd22194   243 VKrmydmiLLKSENKNLeTIRNNEGLTPLQLAAKMGKAEILKYILSREIK-EKPNrslsrkftdwAYG--PVSSSLYDlt 319
                         330       340       350
                  ....*....|....*....|....*....|...
gi 1907098180 280 ----GQDVVVNELIDCGANVNQKNEK-GFTPLH 307
Cdd:cd22194   320 nvdtTTDNSVLEIIVYNTNIDNRHEMlTLEPLH 352
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
158-350 5.06e-03

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 38.91  E-value: 5.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 158 PLLSNVNVSDRAGRTALHHAAFSG-HGEMVKLLLSRGANINAFDKkdrrAIHwAAYMGHIEVVKLLVSHGAEVtckDKKS 236
Cdd:TIGR00870  40 PKKLNINCPDRLGRSALFVAAIENeNLELTELLLNLSCRGAVGDT----LLH-AISLEYVDAVEAILLHLLAA---FRKS 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180 237 YTPLHAAASSGmisvvkylldlgvdmNEPNAyGNTPLHVACYNGQDVVVNELIDCGANVNQKNEKGF------------- 303
Cdd:TIGR00870 112 GPLELANDQYT---------------SEFTP-GITALHLAAHRQNYEIVKLLLERGASVPARACGDFfvksqgvdsfyhg 175
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1907098180 304 -TPLHFAAASTHGALcLELLVGNGADVNMKSKDGKTPLHMTALHGRFS 350
Cdd:TIGR00870 176 eSPLNAAACLGSPSI-VALLSEDPADILTADSLGNTLLHLLVMENEFK 222
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
70-99 6.14e-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: 6.14e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1907098180   70 EKRTPLHAAAYLGDAEIIELLILSGARVNA 99
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
321-376 7.74e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 34.63  E-value: 7.74e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907098180 321 LLVGNGADVNMKSKDGKTPLHMTALHGRFSRSQTIIQSGAVIDCEDKNGNTPLHIA 376
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02875 PHA02875
ankyrin repeat protein; Provisional
34-131 8.08e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 38.05  E-value: 8.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180  34 PSGNVLPSLVQAIFNGDPDEVRALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLILSGARVN-AKDSKWLTPLHRAV 112
Cdd:PHA02875  131 PNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDyFGKNGCVAALCYAI 210
                          90
                  ....*....|....*....
gi 1907098180 113 ASCSEEAVQILLKHSADVN 131
Cdd:PHA02875  211 ENNKIDIVRLFIKRGADCN 229
PHA02791 PHA02791
ankyrin-like protein; Provisional
70-197 9.64e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 37.71  E-value: 9.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907098180  70 EKRTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEEAVQILLKHSADVNARDKN-WQTPL-HIAAAN 147
Cdd:PHA02791   60 ENEFPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDSGNMQTVKLFVKKNWRLMFYGKTgWKTSFyHAVMLN 139
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907098180 148 KAVKCAESLVPLLSNVNVSDRAgrTALHHAAFSGHGEMVKLLLSRGANIN 197
Cdd:PHA02791  140 DVSIVSYFLSEIPSTFDLAILL--SCIHITIKNGHVDMMILLLDYMTSTN 187
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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