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Conserved domains on  [gi|2024376459|ref|XP_040552509|]
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serine/threonine-protein phosphatase 6 regulatory ankyrin repeat subunit A isoform X5 [Gallus gallus]

Protein Classification

ankyrin repeat domain-containing protein( domain architecture ID 13332612)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
37-306 3.16e-54

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 181.31  E-value: 3.16e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459  37 NVLPPLVQAIFNGDPDEVRALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCS 116
Cdd:COG0666    20 LLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGD 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 117 EDAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHVEMVSLLLSRGANI 196
Cdd:COG0666   100 LEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADV 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 197 NAFDKKDRRAIHWAAYMGHIEVVKLLVAHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVA 276
Cdd:COG0666   180 NARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLA 259
                         250       260       270
                  ....*....|....*....|....*....|
gi 2024376459 277 CYNGQDVVVNELIDSGANVNQMNEKGFTPL 306
Cdd:COG0666   260 AAAGAALIVKLLLLALLLLAAALLDLLTLL 289
Ank_2 pfam12796
Ankyrin repeats (3 copies);
273-366 1.47e-13

Ankyrin repeats (3 copies);


:

Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.91  E-value: 1.47e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 273 LHVACYNGQDVVVNELIDSGANVNQMNEKGFTPLHFAAASTHGALCLELLvcNGADVNMKSkDGKTPLHMTAIHGRFSRS 352
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL--EHADVNLKD-NGRTALHYAARSGHLEIV 77
                          90
                  ....*....|....
gi 2024376459 353 QTIIQNGAEIDCED 366
Cdd:pfam12796  78 KLLLEKGADINVKD 91
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
368-394 3.80e-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: 37.57  E-value: 3.80e-04
                           10        20
                   ....*....|....*....|....*..
gi 2024376459  368 NGNTPLHIAARYGHELLINTLITSGAD 394
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
37-306 3.16e-54

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 181.31  E-value: 3.16e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459  37 NVLPPLVQAIFNGDPDEVRALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCS 116
Cdd:COG0666    20 LLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGD 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 117 EDAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHVEMVSLLLSRGANI 196
Cdd:COG0666   100 LEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADV 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 197 NAFDKKDRRAIHWAAYMGHIEVVKLLVAHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVA 276
Cdd:COG0666   180 NARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLA 259
                         250       260       270
                  ....*....|....*....|....*....|
gi 2024376459 277 CYNGQDVVVNELIDSGANVNQMNEKGFTPL 306
Cdd:COG0666   260 AAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA03095 PHA03095
ankyrin-like protein; Provisional
52-340 5.32e-44

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 159.03  E-value: 5.32e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459  52 DEVRALIFKKEDVNFQDNEKRTPLHAaaYLG-----DAEIIELLILSGARVNAKDSKWLTPLHRAV-ASCSEDAVQVLLK 125
Cdd:PHA03095   28 EEVRRLLAAGADVNFRGEYGKTPLHL--YLHyssekVKDIVRLLLEAGADVNAPERCGFTPLHLYLyNATTLDVIKLLIK 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 126 HSADVNARDKNWQTPLHIAAANKAVkcaealvpllsnvnvsdragrtalhhaafsgHVEMVSLLLSRGANINAFDKKDRR 205
Cdd:PHA03095  106 AGADVNAKDKVGRTPLHVYLSGFNI-------------------------------NPKVIRLLLRKGADVNALDLYGMT 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 206 AIHwaAYMGH----IEVVKLLVAHGAEVTCKDKKSYTPLHAAASSGMIS--VVKYLLDLGVDMNEPNAYGNTPLHVACYN 279
Cdd:PHA03095  155 PLA--VLLKSrnanVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTPLHSMATG 232
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024376459 280 G--QDVVVNELIDSGANVNQMNEKGFTPLHFAAASTHGALCLELLVCnGADVNMKSKDGKTPL 340
Cdd:PHA03095  233 SscKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIAL-GADINAVSSDGNTPL 294
Ank_2 pfam12796
Ankyrin repeats (3 copies);
141-233 1.62e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.86  E-value: 1.62e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 141 LHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHVEMVSLLLSRgANINAFDkKDRRAIHWAAYMGHIEVVK 220
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 2024376459 221 LLVAHGAEVTCKD 233
Cdd:pfam12796  79 LLLEKGADINVKD 91
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
104-311 4.93e-15

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: 76.59  E-value: 4.93e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 104 WLTPLHRAVASCSEDAVQVLLK-HSADVNARDKNWQTPLHIAAANKAVKCAEAL---VPLLSNVNV-SD-RAGRTALHHA 177
Cdd:cd22192    17 SESPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLmeaAPELVNEPMtSDlYQGETALHIA 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 178 AFSGHVEMVSLLLSRGANIN-------AFDKKDRRAIHW-------AAYMGHIEVVKLLVAHGAEVTCKDkksytplhaa 243
Cdd:cd22192    97 VVNQNLNLVRELIARGADVVspratgtFFRPGPKNLIYYgehplsfAACVGNEEIVRLLIEHGADIRAQD---------- 166
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024376459 244 assgmisvvkylldlgvdmnepnAYGNTPLHVACYNGQDVVVNELID----SGANVNQM------NEKGFTPLHFAAA 311
Cdd:cd22192   167 -----------------------SLGNTVLHILVLQPNKTFACQMYDlilsYDKEDDLQpldlvpNNQGLTPFKLAAK 221
Ank_2 pfam12796
Ankyrin repeats (3 copies);
273-366 1.47e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.91  E-value: 1.47e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 273 LHVACYNGQDVVVNELIDSGANVNQMNEKGFTPLHFAAASTHGALCLELLvcNGADVNMKSkDGKTPLHMTAIHGRFSRS 352
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL--EHADVNLKD-NGRTALHYAARSGHLEIV 77
                          90
                  ....*....|....
gi 2024376459 353 QTIIQNGAEIDCED 366
Cdd:pfam12796  78 KLLLEKGADINVKD 91
PHA02878 PHA02878
ankyrin repeat protein; Provisional
239-395 6.22e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 66.83  E-value: 6.22e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 239 PLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDS------------------GANVN---- 296
Cdd:PHA02878   40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSinkcsvfytlvaikdafnNRNVEifki 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 297 -----QMNEKGFTPLHFAAASTHGAL---CLELLVCNGADVNMKSKD-GKTPLHMTAIHGRFSRSQTIIQNGAEIDCEDK 367
Cdd:PHA02878  120 iltnrYKNIQTIDLVYIDKKSKDDIIeaeITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDK 199
                         170       180
                  ....*....|....*....|....*...
gi 2024376459 368 NGNTPLHIAARYGHELLINTLITSGADT 395
Cdd:PHA02878  200 TNNSPLHHAVKHYNKPIVHILLENGAST 227
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
238-375 1.33e-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: 59.64  E-value: 1.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 238 TPLHAAASSGMISVVKYLLDL-GVDMNEPNAYGNTPLHVACYNGQDVVVNELIDSGAN-VNQ-MNE---KGFTPLHFAAA 311
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKCpSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNEpMTSdlyQGETALHIAVV 98
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024376459 312 STHGALcLELLVCNGADVN---------MKSKD-----GKTPLHMTAIHGRFSRSQTIIQNGAEIDCEDKNGNTPLHI 375
Cdd:cd22192    99 NQNLNL-VRELIARGADVVspratgtffRPGPKnliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHI 175
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
58-277 1.55e-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: 56.63  E-value: 1.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459  58 IFKKEDVNFQDNEKrtplhaaAYLGDAEIIELLILSGARVNAK-------DSKWLTPLHRAVA-SCSEDAVQVLLKHSAD 129
Cdd:TIGR00870   6 IVPAEESPLSDEEK-------AFLPAAERGDLASVYRDLEEPKklnincpDRLGRSALFVAAIeNENLELTELLLNLSCR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 130 VNARDknwqTPLHIAAANKAVKCAEALVPLLSN---------VNVSDR----AGRTALHHAAFSGHVEMVSLLLSRGANI 196
Cdd:TIGR00870  79 GAVGD----TLLHAISLEYVDAVEAILLHLLAAfrksgplelANDQYTseftPGITALHLAAHRQNYEIVKLLLERGASV 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 197 NA------FDKKDRRA--------IHWAAYMGHIEVVKLLVAHGAEVTCKDKKSYTPLHAAA------------SSGMIS 250
Cdd:TIGR00870 155 PAracgdfFVKSQGVDsfyhgespLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVmenefkaeyeelSCQMYN 234
                         250       260       270
                  ....*....|....*....|....*....|.
gi 2024376459 251 VVKYLLDLGVDMNE----PNAYGNTPLHVAC 277
Cdd:TIGR00870 235 FALSLLDKLRDSKEleviLNHQGLTPLKLAA 265
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
170-198 2.39e-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: 43.73  E-value: 2.39e-06
                           10        20
                   ....*....|....*....|....*....
gi 2024376459  170 GRTALHHAAFSGHVEMVSLLLSRGANINA 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 3.80e-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: 37.57  E-value: 3.80e-04
                           10        20
                   ....*....|....*....|....*..
gi 2024376459  368 NGNTPLHIAARYGHELLINTLITSGAD 394
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
368-394 2.19e-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: 2.19e-03
                          10        20
                  ....*....|....*....|....*...
gi 2024376459 368 NGNTPLHIAA-RYGHELLINTLITSGAD 394
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGAD 28
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
355-394 2.29e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 40.27  E-value: 2.29e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2024376459 355 IIQNGAEIDCEDKNGNTPLHIAARYGHELLINTLITSGAD 394
Cdd:PTZ00322  101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGAD 140
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
37-306 3.16e-54

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 181.31  E-value: 3.16e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459  37 NVLPPLVQAIFNGDPDEVRALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCS 116
Cdd:COG0666    20 LLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGD 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 117 EDAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHVEMVSLLLSRGANI 196
Cdd:COG0666   100 LEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADV 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 197 NAFDKKDRRAIHWAAYMGHIEVVKLLVAHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVA 276
Cdd:COG0666   180 NARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLA 259
                         250       260       270
                  ....*....|....*....|....*....|
gi 2024376459 277 CYNGQDVVVNELIDSGANVNQMNEKGFTPL 306
Cdd:COG0666   260 AAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
84-373 3.16e-54

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 181.31  E-value: 3.16e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459  84 AEIIELLILSGARVNAKDSKWLTPLHRAVASCSEDAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNV 163
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 164 NVSDRAGRTALHHAAFSGHVEMVSLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVAHGAEVTCKDKKSYTPLHAA 243
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 244 ASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDSGANVNQMNEKGFTPLHFAAASTHGALCLELLV 323
Cdd:COG0666   161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 2024376459 324 cNGADVNMKSKDGKTPLHMTAIHGRFSRSQTIIQNGAEIDCEDKNGNTPL 373
Cdd:COG0666   241 -AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
52-322 7.15e-53

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 177.84  E-value: 7.15e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459  52 DEVRALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEDAVQVLLKHSADVN 131
Cdd:COG0666     2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 132 ARDKNWQTPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHVEMVSLLLSRGANINAFDKKDRRAIHWAA 211
Cdd:COG0666    82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 212 YMGHIEVVKLLVAHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDS 291
Cdd:COG0666   162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241
                         250       260       270
                  ....*....|....*....|....*....|.
gi 2024376459 292 GANVNQMNEKGFTPLHFAAASTHGALCLELL 322
Cdd:COG0666   242 GADLNAKDKDGLTALLLAAAAGAALIVKLLL 272
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
123-397 2.62e-52

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 176.30  E-value: 2.62e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 123 LLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHVEMVSLLLSRGANINAFDKK 202
Cdd:COG0666     7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 203 DRRAIHWAAYMGHIEVVKLLVAHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQD 282
Cdd:COG0666    87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 283 VVVNELIDSGANVNQMNEKGFTPLHFAAASTHGALcLELLVCNGADVNMKSKDGKTPLHMTAIHGRFSRSQTIIQNGAEI 362
Cdd:COG0666   167 EIVKLLLEAGADVNARDNDGETPLHLAAENGHLEI-VKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADL 245
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 2024376459 363 DCEDKNGNTPLHIAARYGHELLINTLITSGADTAK 397
Cdd:COG0666   246 NAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAA 280
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
153-394 7.76e-46

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 159.35  E-value: 7.76e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 153 AEALVPLLSNVNVSDRAGRTALHHAAFSGHVEMVSLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVAHGAEVTCK 232
Cdd:COG0666     4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 233 DKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDSGANVNQMNEKGFTPLHFAAAS 312
Cdd:COG0666    84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 313 THGALcLELLVCNGADVNMKSKDGKTPLHMTAIHGRFSRSQTIIQNGAEIDCEDKNGNTPLHIAARYGHELLINTLITSG 392
Cdd:COG0666   164 GNLEI-VKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAG 242

                  ..
gi 2024376459 393 AD 394
Cdd:COG0666   243 AD 244
PHA03095 PHA03095
ankyrin-like protein; Provisional
52-340 5.32e-44

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 159.03  E-value: 5.32e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459  52 DEVRALIFKKEDVNFQDNEKRTPLHAaaYLG-----DAEIIELLILSGARVNAKDSKWLTPLHRAV-ASCSEDAVQVLLK 125
Cdd:PHA03095   28 EEVRRLLAAGADVNFRGEYGKTPLHL--YLHyssekVKDIVRLLLEAGADVNAPERCGFTPLHLYLyNATTLDVIKLLIK 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 126 HSADVNARDKNWQTPLHIAAANKAVkcaealvpllsnvnvsdragrtalhhaafsgHVEMVSLLLSRGANINAFDKKDRR 205
Cdd:PHA03095  106 AGADVNAKDKVGRTPLHVYLSGFNI-------------------------------NPKVIRLLLRKGADVNALDLYGMT 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 206 AIHwaAYMGH----IEVVKLLVAHGAEVTCKDKKSYTPLHAAASSGMIS--VVKYLLDLGVDMNEPNAYGNTPLHVACYN 279
Cdd:PHA03095  155 PLA--VLLKSrnanVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTPLHSMATG 232
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024376459 280 G--QDVVVNELIDSGANVNQMNEKGFTPLHFAAASTHGALCLELLVCnGADVNMKSKDGKTPL 340
Cdd:PHA03095  233 SscKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIAL-GADINAVSSDGNTPL 294
PHA03100 PHA03100
ankyrin repeat protein; Provisional
53-331 9.64e-40

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 146.35  E-value: 9.64e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459  53 EVRALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLH-----RAVASCSEDAVQVLLKHS 127
Cdd:PHA03100   17 NIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHylsniKYNLTDVKEIVKLLLEYG 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 128 ADVNARDKNWQTPLHIAAANKavkcaealvpllsnvnvsdragrtalhhaafSGHVEMVSLLLSRGANINAFDKKDRRAI 207
Cdd:PHA03100   97 ANVNAPDNNGITPLLYAISKK-------------------------------SNSYSIVEYLLDNGANVNIKNSDGENLL 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 208 HWAAYMGHI--EVVKLLVAHGAEVTCKDKksytplhaaassgmisvVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVV 285
Cdd:PHA03100  146 HLYLESNKIdlKILKLLIDKGVDINAKNR-----------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFV 208
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 2024376459 286 NELIDSGANVNQMNEKGFTPLHFAAASTHGALcLELLVCNGADVNM 331
Cdd:PHA03100  209 KYLLDLGANPNLVNKYGDTPLHIAILNNNKEI-FKLLLNNGPSIKT 253
PHA02876 PHA02876
ankyrin repeat protein; Provisional
52-394 2.37e-39

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 149.06  E-value: 2.37e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459  52 DEVR---ALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEDAVQVLLKHSA 128
Cdd:PHA02876  156 DELLiaeMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRS 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 129 DVNARDKNwqtpLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHV-EMVSLLLSRGANINAFDKKDRRAI 207
Cdd:PHA02876  236 NINKNDLS----LLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPL 311
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 208 HWAAYMGH-IEVVKLLVAHGAEVTCKDKKSYTPLHAAAS-SGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVV 285
Cdd:PHA02876  312 YLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVII 391
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 286 NELIDSGANVNQMNEKGFTPLHFAAASTHGALCLELLVCNGADVNMKSKDGKTPLHMTAIHG-RFSRSQTIIQNGAEIDC 364
Cdd:PHA02876  392 NTLLDYGADIEALSQKIGTALHFALCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNA 471
                         330       340       350
                  ....*....|....*....|....*....|
gi 2024376459 365 EDKNGNTPLHIAarYGHELLINTLITSGAD 394
Cdd:PHA02876  472 INIQNQYPLLIA--LEYHGIVNILLHYGAE 499
PHA02874 PHA02874
ankyrin repeat protein; Provisional
46-397 2.76e-36

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 137.40  E-value: 2.76e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459  46 IFNGDPDEVRALIFKKED-VNFQDNEKRTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEDAVQVLL 124
Cdd:PHA02874    9 IYSGDIEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLI 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 125 KHSADVNARDknwqtplhiaaankavkcaealVPLLSNvnvsdragrtalhhaafsghvEMVSLLLSRGANINAFDKKDR 204
Cdd:PHA02874   89 DNGVDTSILP----------------------IPCIEK---------------------DMIKTILDCGIDVNIKDAELK 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 205 RAIHWAAYMGHIEVVKLLVAHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVV 284
Cdd:PHA02874  126 TFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYAC 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 285 VNELIDSGANVNQMNEKGFTPLHfaAASTHGALCLELLVcNGADVNMKSKDGKTPLHMtAIHGRFSRS--QTIIQNGAEI 362
Cdd:PHA02874  206 IKLLIDHGNHIMNKCKNGFTPLH--NAIIHNRSAIELLI-NNASINDQDIDGSTPLHH-AINPPCDIDiiDILLYHKADI 281
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 2024376459 363 DCEDKNGNTPLHIAARYGH------ELLINTLITSGADTAK 397
Cdd:PHA02874  282 SIKDNKGENPIDTAFKYINkdpvikDIIANAVLIKEADKLK 322
PHA02878 PHA02878
ankyrin repeat protein; Provisional
105-383 1.25e-28

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 116.52  E-value: 1.25e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 105 LTPLHRAVASCSEDAVQVLLKHSADVNARDKNWQTPLHIA--AANKavkcaEALVPLLSNVNvSDRAGRT--ALHHAAFS 180
Cdd:PHA02878   38 FIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIIckEPNK-----LGMKEMIRSIN-KCSVFYTlvAIKDAFNN 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 181 GHVEMV-SLLLSRGANINAFDKKDRRAIHWAAYMgHIEVVKLLVAHGAEVTCKDK-KSYTPLHAAASSGMISVVKYLLDL 258
Cdd:PHA02878  112 RNVEIFkIILTNRYKNIQTIDLVYIDKKSKDDII-EAEITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSY 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 259 GVDMNEPNAYGNTPLHVACYNGQDVVVNELIDSGANVNQMNEKGFTPLHFAAASTHGALCLELLVCNGADVNMKSK-DGK 337
Cdd:PHA02878  191 GANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDYDILKLLLEHGVDVNAKSYiLGL 270
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 2024376459 338 TPLHMtAIHGRfSRSQTIIQNGAEIDCEDKNGNTPLHIAA--RYGHEL 383
Cdd:PHA02878  271 TALHS-SIKSE-RKLKLLLEYGADINSLNSYKLTPLSSAVkqYLCINI 316
PHA03100 PHA03100
ankyrin repeat protein; Provisional
53-300 2.42e-25

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 106.67  E-value: 2.42e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459  53 EVRALIFKKE-DVNFQDNEKRTPLHAAAY--LGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEDavqvllkhsad 129
Cdd:PHA03100   87 EIVKLLLEYGaNVNAPDNNGITPLLYAISkkSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKID----------- 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 130 vnardknwqtplhiaaankavkcaealvpllsnvnvsdragrtalhhaafsghVEMVSLLLSRGANINAfdkKDRraihw 209
Cdd:PHA03100  156 -----------------------------------------------------LKILKLLIDKGVDINA---KNR----- 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 210 aaymghievVKLLVAHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELI 289
Cdd:PHA03100  175 ---------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLL 245
                         250
                  ....*....|.
gi 2024376459 290 DSGANVNQMNE 300
Cdd:PHA03100  246 NNGPSIKTIIE 256
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
183-394 4.29e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 98.10  E-value: 4.29e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 183 VEMVSLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVAHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDM 262
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 263 NEPNAYGNTPLHVACYNGQDVVVNELIDSGANVNQMNEKGFTPLHFAAASTHGALcLELLVCNGADVNMKskdgktplhm 342
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEI-VKLLLEAGADVNAQ---------- 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2024376459 343 taihgrfsrsqtiiqngaeidceDKNGNTPLHIAARYGHELLINTLITSGAD 394
Cdd:COG0666   150 -----------------------DNDGNTPLHLAAANGNLEIVKLLLEAGAD 178
PHA03100 PHA03100
ankyrin repeat protein; Provisional
216-394 6.67e-23

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 99.35  E-value: 6.67e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 216 IEVVKLLVAHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLH---VACYNGQDVV--VNELID 290
Cdd:PHA03100   15 VKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHylsNIKYNLTDVKeiVKLLLE 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 291 SGANVNQMNEKGFTPLHFAAASTHGALCL-ELLVCNGADVNMKSKDGKTPLHMTA--IHGRFSRSQTIIQNGAEIDCE-- 365
Cdd:PHA03100   95 YGANVNAPDNNGITPLLYAISKKSNSYSIvEYLLDNGANVNIKNSDGENLLHLYLesNKIDLKILKLLIDKGVDINAKnr 174
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2024376459 366 --------------DKNGNTPLHIAARYGHELLINTLITSGAD 394
Cdd:PHA03100  175 vnyllsygvpinikDVYGFTPLHYAVYNNNPEFVKYLLDLGAN 217
PHA02878 PHA02878
ankyrin repeat protein; Provisional
60-347 9.57e-23

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 99.57  E-value: 9.57e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459  60 KKEDVNFQDNEKRT---------PLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEDAVQVLLK----- 125
Cdd:PHA02878   17 LKYIEYIDHTENYStsaslipfiPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRsinkc 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 126 -------------HSADVNA-------RDKNWQTP--LHIAAANKAVKCAEALVPLL----SNVNVSDR-AGRTALHHAA 178
Cdd:PHA02878   97 svfytlvaikdafNNRNVEIfkiiltnRYKNIQTIdlVYIDKKSKDDIIEAEITKLLlsygADINMKDRhKGNTALHYAT 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 179 FSGHVEMVSLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVAHGAEVTCKDKKSYTPLHAAASSGM-ISVVKYLLD 257
Cdd:PHA02878  177 ENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKdYDILKLLLE 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 258 LGVDMN-EPNAYGNTPLHVACYNGQdvVVNELIDSGANVNQMNEKGFTPLHFAAASTHGALCLELLVCNGADVNMKSKDG 336
Cdd:PHA02878  257 HGVDVNaKSYILGLTALHSSIKSER--KLKLLLEYGADINSLNSYKLTPLSSAVKQYLCINIGRILISNICLLKRIKPDI 334
                         330
                  ....*....|....*
gi 2024376459 337 KTPL----HMTAIHG 347
Cdd:PHA02878  335 KNSEgfidNMDCITS 349
Ank_2 pfam12796
Ankyrin repeats (3 copies);
141-233 1.62e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.86  E-value: 1.62e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 141 LHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHVEMVSLLLSRgANINAFDkKDRRAIHWAAYMGHIEVVK 220
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 2024376459 221 LLVAHGAEVTCKD 233
Cdd:pfam12796  79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
207-299 3.25e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.09  E-value: 3.25e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 207 IHWAAYMGHIEVVKLLVAHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDlGVDMNEPNaYGNTPLHVACYNGQDVVVN 286
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 2024376459 287 ELIDSGANVNQMN 299
Cdd:pfam12796  79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
174-266 3.32e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.09  E-value: 3.32e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 174 LHHAAFSGHVEMVSLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVAHgAEVTCKDKKsYTPLHAAASSGMISVVK 253
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNG-RTALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 2024376459 254 YLLDLGVDMNEPN 266
Cdd:pfam12796  79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
108-200 4.27e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 86.71  E-value: 4.27e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 108 LHRAVASCSEDAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLsNVNVSDRaGRTALHHAAFSGHVEMVS 187
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKDN-GRTALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 2024376459 188 LLLSRGANINAFD 200
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA02875 PHA02875
ankyrin repeat protein; Provisional
72-334 5.55e-20

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 90.82  E-value: 5.55e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459  72 RTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEDAVQVLLKHSADVNARDKNWQTPLHIAAANKAVK 151
Cdd:PHA02875    3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 152 CAEALvpLLSNVNVSD---RAGRTALHHAAFSGHVEMVSLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVAHGAE 228
Cdd:PHA02875   83 AVEEL--LDLGKFADDvfyKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKAC 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 229 VTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDmnePNAYGNTP-LHVACY---NGQDVVVNELIDSGANVNQMnekgft 304
Cdd:PHA02875  161 LDIEDCCGCTPLIIAMAKGDIAICKMLLDSGAN---IDYFGKNGcVAALCYaieNNKIDIVRLFIKRGADCNIM------ 231
                         250       260       270
                  ....*....|....*....|....*....|
gi 2024376459 305 plhfaaASTHGALCLELLVCNGADVNMKSK 334
Cdd:PHA02875  232 ------FMIEGEECTILDMICNMCTNLESE 255
Ank_2 pfam12796
Ankyrin repeats (3 copies);
42-134 5.86e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 83.63  E-value: 5.86e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459  42 LVQAIFNGDPDEVRALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLiLSGARVNAKDSKWlTPLHRAVASCSEDAVQ 121
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL-LEHADVNLKDNGR-TALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 2024376459 122 VLLKHSADVNARD 134
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
216-396 4.65e-19

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 88.54  E-value: 4.65e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 216 IEVVKLLVAHGAEVTCKDKKSYTPLHAAASSGM---ISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDV-VVNELIDS 291
Cdd:PHA03095   27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKA 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 292 GANVNQMNEKGFTPLH--FAAASTHgALCLELLVCNGADVNMKSKDGKTPLHMTAIHGRFSRS--QTIIQNGAEIDCEDK 367
Cdd:PHA03095  107 GADVNAKDKVGRTPLHvyLSGFNIN-PKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVEllRLLIDAGADVYAVDD 185
                         170       180       190
                  ....*....|....*....|....*....|.
gi 2024376459 368 NGNTPLHIAARYGH--ELLINTLITSGADTA 396
Cdd:PHA03095  186 RFRSLLHHHLQSFKprARIVRELIRAGCDPA 216
PHA02874 PHA02874
ankyrin repeat protein; Provisional
42-225 2.35e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 86.17  E-value: 2.35e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459  42 LVQAIFNGDPDEVRALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEDAVQ 121
Cdd:PHA02874  128 LHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIK 207
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 122 VLLKHSADVNARDKNWQTPLHIAAA-NKAVkcaealVPLLSN---VNVSDRAGRTALHHA-AFSGHVEMVSLLLSRGANI 196
Cdd:PHA02874  208 LLIDHGNHIMNKCKNGFTPLHNAIIhNRSA------IELLINnasINDQDIDGSTPLHHAiNPPCDIDIIDILLYHKADI 281
                         170       180       190
                  ....*....|....*....|....*....|
gi 2024376459 197 NAFDKKDRRAIHWA-AYMGHIEVVKLLVAH 225
Cdd:PHA02874  282 SIKDNKGENPIDTAfKYINKDPVIKDIIAN 311
PHA02875 PHA02875
ankyrin repeat protein; Provisional
63-228 6.08e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 81.96  E-value: 6.08e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459  63 DVNFQDneKRTPLHAAAYLGDAEIIELLILSGARVN-AKDSKWLTPLHRAVASCSEDAVQVLLKHSADVNARDKNWQTPL 141
Cdd:PHA02875   62 DVKYPD--IESELHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPL 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 142 HIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHVEMVSLLLSRGANINAFDKK-DRRAIHWAAYMGHIEVVK 220
Cdd:PHA02875  140 HLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNgCVAALCYAIENNKIDIVR 219

                  ....*...
gi 2024376459 221 LLVAHGAE 228
Cdd:PHA02875  220 LFIKRGAD 227
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
60-231 1.68e-16

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 81.45  E-value: 1.68e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459  60 KKEDVNFQDNEKRTPLHAAAYL------GDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEDAVQVLLKHSADVNAR 133
Cdd:PLN03192  508 NVGDLLGDNGGEHDDPNMASNLltvastGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIR 587
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 134 DKNWQTPLHIAAANKAVKCAEALVPLLSnvnVSD-RAGRTALHHAAFSGHVEMVSLLLSRGANINAFDKKDRRAIHWAAY 212
Cdd:PLN03192  588 DANGNTALWNAISAKHHKIFRILYHFAS---ISDpHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMA 664
                         170
                  ....*....|....*....
gi 2024376459 213 MGHIEVVKLLVAHGAEVTC 231
Cdd:PLN03192  665 EDHVDMVRLLIMNGADVDK 683
PHA02798 PHA02798
ankyrin-like protein; Provisional
85-348 2.40e-16

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 80.65  E-value: 2.40e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459  85 EIIELLILSGARVNAKDSKWLTPLHRAVASCSE-----DAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPL 159
Cdd:PHA02798   52 DIVKLFINLGANVNGLDNEYSTPLCTILSNIKDykhmlDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLFM 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 160 LSN---VNVSDRAGRTALHHAAFSGH---VEMVSLLLSRGANINAFDkkdrraiHWAAYmghievvkllvahgAEVTCKD 233
Cdd:PHA02798  132 IENgadTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDINTHN-------NKEKY--------------DTLHCYF 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 234 KKSYTPLHAaassgmiSVVKYLLDLGVDMNEPNAYGNTP----LHVACYNGQDVVVN--ELIDSGANVNQMNEKGFTPLH 307
Cdd:PHA02798  191 KYNIDRIDA-------DILKLFVDNGFIINKENKSHKKKfmeyLNSLLYDNKRFKKNilDFIFSYIDINQVDELGFNPLY 263
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 2024376459 308 FAAASTHGALClELLVCNGADVNMKSKDGKTPLhMTAIHGR 348
Cdd:PHA02798  264 YSVSHNNRKIF-EYLLQLGGDINIITELGNTCL-FTAFENE 302
PHA02876 PHA02876
ankyrin repeat protein; Provisional
41-250 2.60e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 80.88  E-value: 2.60e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459  41 PLVQAIFNG-DPDEVRALIFKKEDVNFQDNEKRTPLHAAAYLG-DAEIIELLILSGARVNAKDSKWLTPLHRAVASCSED 118
Cdd:PHA02876  310 PLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVV 389
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 119 AVQVLLKHSADVNARDKNWQTPLHIA-AANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSG-HVEMVSLLLSRGANI 196
Cdd:PHA02876  390 IINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADV 469
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2024376459 197 NAFDKKDRRAIHWAayMGHIEVVKLLVAHGAEVtcKDKKSytpLHAAASSGMIS 250
Cdd:PHA02876  470 NAINIQNQYPLLIA--LEYHGIVNILLHYGAEL--RDSRV---LHKSLNDNMFS 516
PHA02878 PHA02878
ankyrin repeat protein; Provisional
54-225 4.70e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 79.54  E-value: 4.70e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459  54 VRALIFKKEDVNFQDNEK-RTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEDAVQVLLKHSADVNA 132
Cdd:PHA02878  150 TKLLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDA 229
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 133 RDKNWQTPLHIAAAnkAVKCAEALVPLL---SNVNV-SDRAGRTALHHAAFSGHVemVSLLLSRGANINAFDKKDRRAIH 208
Cdd:PHA02878  230 RDKCGNTPLHISVG--YCKDYDILKLLLehgVDVNAkSYILGLTALHSSIKSERK--LKLLLEYGADINSLNSYKLTPLS 305
                         170
                  ....*....|....*....
gi 2024376459 209 WAA--YMGhIEVVKLLVAH 225
Cdd:PHA02878  306 SAVkqYLC-INIGRILISN 323
PHA02875 PHA02875
ankyrin repeat protein; Provisional
203-394 1.21e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 78.11  E-value: 1.21e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 203 DRRAIHWAAYMGHIEVVKLLVAHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGV--DMNEPNAygNTPLHVACYNG 280
Cdd:PHA02875    2 DQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAipDVKYPDI--ESELHDAVEEG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 281 QDVVVNELIDSGANVNQM-NEKGFTPLHFAAASTHGALcLELLVCNGADVNMKSKDGKTPLHMTAIHGRFSRSQTIIQNG 359
Cdd:PHA02875   80 DVKAVEELLDLGKFADDVfYKDGMTPLHLATILKKLDI-MKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHK 158
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2024376459 360 AEIDCEDKNGNTPLHIAARYGHELLINTLITSGAD 394
Cdd:PHA02875  159 ACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGAN 193
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
104-311 4.93e-15

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: 76.59  E-value: 4.93e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 104 WLTPLHRAVASCSEDAVQVLLK-HSADVNARDKNWQTPLHIAAANKAVKCAEAL---VPLLSNVNV-SD-RAGRTALHHA 177
Cdd:cd22192    17 SESPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLmeaAPELVNEPMtSDlYQGETALHIA 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 178 AFSGHVEMVSLLLSRGANIN-------AFDKKDRRAIHW-------AAYMGHIEVVKLLVAHGAEVTCKDkksytplhaa 243
Cdd:cd22192    97 VVNQNLNLVRELIARGADVVspratgtFFRPGPKNLIYYgehplsfAACVGNEEIVRLLIEHGADIRAQD---------- 166
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024376459 244 assgmisvvkylldlgvdmnepnAYGNTPLHVACYNGQDVVVNELID----SGANVNQM------NEKGFTPLHFAAA 311
Cdd:cd22192   167 -----------------------SLGNTVLHILVLQPNKTFACQMYDlilsYDKEDDLQpldlvpNNQGLTPFKLAAK 221
PHA03095 PHA03095
ankyrin-like protein; Provisional
47-198 5.09e-15

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 76.22  E-value: 5.09e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459  47 FNGDPDEVRALIFKKEDVNFQDNEKRTPLHaaAYLG----DAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEDA--V 120
Cdd:PHA03095  128 FNINPKVIRLLLRKGADVNALDLYGMTPLA--VLLKsrnaNVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRAriV 205
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 121 QVLLKHSADVNARDKNWQTPLHIAAANKAVKcAEALVPLLSN---VNVSDRAGRTALHHAAFSGHVEMVSLLLSRGANIN 197
Cdd:PHA03095  206 RELIRAGCDPAATDMLGNTPLHSMATGSSCK-RSLVLPLLIAgisINARNRYGQTPLHYAAVFNNPRACRRLIALGADIN 284

                  .
gi 2024376459 198 A 198
Cdd:PHA03095  285 A 285
PHA02875 PHA02875
ankyrin repeat protein; Provisional
171-395 8.38e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 75.41  E-value: 8.38e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 171 RTALHHAAFSGHVEMVSLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVAHGAEVTCKDKKSYTPLHAAASSGMIS 250
Cdd:PHA02875    3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 251 VVKYLLDLGVDMNEP-NAYGNTPLHVACYNGQDVVVNELIDSGANVNQMNEKGFTPLHFAAASTHGALcLELLVCNGADV 329
Cdd:PHA02875   83 AVEELLDLGKFADDVfYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKG-IELLIDHKACL 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024376459 330 NMKSKDGKTPLHMTAIHGRFSRSQTIIQNGAEIDCEDKNGNTPLHIAARYGHEL-LINTLITSGADT 395
Cdd:PHA02875  162 DIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIdIVRLFIKRGADC 228
PHA03095 PHA03095
ankyrin-like protein; Provisional
48-198 6.22e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 73.14  E-value: 6.22e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459  48 NGDPDEVRALIFKKEDVNFQDNEKRTPLH--AAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEDAVQV--L 123
Cdd:PHA03095  164 NANVELLRLLIDAGADVYAVDDRFRSLLHhhLQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpL 243
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024376459 124 LKHSADVNARDKNWQTPLHIAAA-NKAVKCAEaLVPLLSNVNVSDRAGRTALHHAAFSGHVEMVSLLLSRGANINA 198
Cdd:PHA03095  244 LIAGISINARNRYGQTPLHYAAVfNNPRACRR-LIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAET 318
Ank_2 pfam12796
Ankyrin repeats (3 copies);
273-366 1.47e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.91  E-value: 1.47e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 273 LHVACYNGQDVVVNELIDSGANVNQMNEKGFTPLHFAAASTHGALCLELLvcNGADVNMKSkDGKTPLHMTAIHGRFSRS 352
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL--EHADVNLKD-NGRTALHYAARSGHLEIV 77
                          90
                  ....*....|....
gi 2024376459 353 QTIIQNGAEIDCED 366
Cdd:pfam12796  78 KLLLEKGADINVKD 91
Ank_4 pfam13637
Ankyrin repeats (many copies);
170-223 4.18e-13

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 63.45  E-value: 4.18e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2024376459 170 GRTALHHAAFSGHVEMVSLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLV 223
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
306-394 6.52e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 63.98  E-value: 6.52e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 306 LHFAAASTHgALCLELLVCNGADVNMKSKDGKTPLHMTAIHGRFSRSQTIIQNgAEIDCEDkNGNTPLHIAARYGHELLI 385
Cdd:pfam12796   1 LHLAAKNGN-LELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIV 77

                  ....*....
gi 2024376459 386 NTLITSGAD 394
Cdd:pfam12796  78 KLLLEKGAD 86
PHA02878 PHA02878
ankyrin repeat protein; Provisional
239-395 6.22e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 66.83  E-value: 6.22e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 239 PLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDS------------------GANVN---- 296
Cdd:PHA02878   40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSinkcsvfytlvaikdafnNRNVEifki 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 297 -----QMNEKGFTPLHFAAASTHGAL---CLELLVCNGADVNMKSKD-GKTPLHMTAIHGRFSRSQTIIQNGAEIDCEDK 367
Cdd:PHA02878  120 iltnrYKNIQTIDLVYIDKKSKDDIIeaeITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDK 199
                         170       180
                  ....*....|....*....|....*...
gi 2024376459 368 NGNTPLHIAARYGHELLINTLITSGADT 395
Cdd:PHA02878  200 TNNSPLHHAVKHYNKPIVHILLENGAST 227
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
164-306 7.12e-12

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 67.20  E-value: 7.12e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 164 NVSDRAGRTALHHAAFSGHVEMVSLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLL--VAH------GAEVTCkdkk 235
Cdd:PLN03192  552 DIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILyhFASisdphaAGDLLC---- 627
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024376459 236 sytplhAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDSGANVNQMN-EKGFTPL 306
Cdd:PLN03192  628 ------TAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANtDDDFSPT 693
Ank_4 pfam13637
Ankyrin repeats (many copies);
204-256 7.13e-12

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 59.98  E-value: 7.13e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2024376459 204 RRAIHWAAYMGHIEVVKLLVAHGAEVTCKDKKSYTPLHAAASSGMISVVKYLL 256
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02946 PHA02946
ankyin-like protein; Provisional
79-306 9.00e-11

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 63.15  E-value: 9.00e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459  79 AYLG----DAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEDAVQVLLKHSADVNARDKNWQTPLH-IAAANKAVkca 153
Cdd:PHA02946   43 AYCGikglDERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYyLSGTDDEV--- 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 154 ealvpllsnvnvsdragrtalhhaafsghVEMVSLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVAHGAEVTCKD 233
Cdd:PHA02946  120 -----------------------------IERINLLVQYGAKINNSVDEEGCGPLLACTDPSERVFKKIMSIGFEARIVD 170
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024376459 234 K--KSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNG-QDVVVNELIDSGANVNQMNEKGFTPL 306
Cdd:PHA02946  171 KfgKNHIHRHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHIVCSKTvKNVDIINLLLPSTDVNKQNKFGDSPL 246
Ank_4 pfam13637
Ankyrin repeats (many copies);
237-281 9.58e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 56.90  E-value: 9.58e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2024376459 237 YTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQ 281
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGN 46
Ank_4 pfam13637
Ankyrin repeats (many copies);
104-157 1.64e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 56.13  E-value: 1.64e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2024376459 104 WLTPLHRAVASCSEDAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALV 157
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
41-144 1.64e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 62.59  E-value: 1.64e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459  41 PLVQAIFNGDPDEVRALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASC-SEDA 119
Cdd:PHA02878  171 ALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCkDYDI 250
                          90       100
                  ....*....|....*....|....*.
gi 2024376459 120 VQVLLKHSADVNARDKNWQ-TPLHIA 144
Cdd:PHA02878  251 LKLLLEHGVDVNAKSYILGlTALHSS 276
PHA02989 PHA02989
ankyrin repeat protein; Provisional
85-357 2.19e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 62.07  E-value: 2.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459  85 EIIELLILSGARVNAKdSKWLTPL-----HRAVASCS-EDAVQVLLKHSADVNARDKNWQTPlhiaaankavkcaeaLVP 158
Cdd:PHA02989   51 KIVKLLIDNGADVNYK-GYIETPLcavlrNREITSNKiKKIVKLLLKFGADINLKTFNGVSP---------------IVC 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 159 LLSNVNVSDragrtalhhaafsghVEMVSLLLSRGANINafDKKDRRA-----IHWAAYMGHIEVVKLLVAHGaeVTCKD 233
Cdd:PHA02989  115 FIYNSNINN---------------CDMLRFLLSKGINVN--DVKNSRGynllhMYLESFSVKKDVIKILLSFG--VNLFE 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 234 KKSY---TPLHAAASSGM----ISVVKYLLDLGVDMNEPNAYGNTPL------HVACYNGQDVVVNeLIDSGANVNQMNE 300
Cdd:PHA02989  176 KTSLyglTPMNIYLRNDIdvisIKVIKYLIKKGVNIETNNNGSESVLesfldnNKILSKKEFKVLN-FILKYIKINKKDK 254
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2024376459 301 KGFTPLHFAAASTHGALCLELLVCnGADVNMKSKDGKTPLHMTAIHGRFSRSQTIIQ 357
Cdd:PHA02989  255 KGFNPLLISAKVDNYEAFNYLLKL-GDDIYNVSKDGDTVLTYAIKHGNIDMLNRILQ 310
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
213-397 3.02e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 62.19  E-value: 3.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 213 MGHIEVVKLLVAHGAEVTckDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDSG 292
Cdd:PLN03192  504 LHDLNVGDLLGDNGGEHD--DPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHA 581
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 293 ANVNQMNEKGFTPLHFAAASTHGALCLELLVCNGADVNMKSKDgktPLHMTAIHGRFSRSQTIIQNGAEIDCEDKNGNTP 372
Cdd:PLN03192  582 CNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAGD---LLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATA 658
                         170       180
                  ....*....|....*....|....*
gi 2024376459 373 LHIAARYGHELLINTLITSGADTAK 397
Cdd:PLN03192  659 LQVAMAEDHVDMVRLLIMNGADVDK 683
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
63-306 5.14e-10

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 61.47  E-value: 5.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459  63 DVNFQDNEKRTP-LHAaaYLG----DAEIIELLILSGARVNAKDSKWLTPLHRAV--ASCSEDAVQVLLKHSADVNARDK 135
Cdd:PHA02716  168 NLNYVCKKTGYGiLHA--YLGnmyvDIDILEWLCNNGVNVNLQNNHLITPLHTYLitGNVCASVIKKIIELGGDMDMKCV 245
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 136 NWQTPLHIAAANkavkcAEALVPLLSNVNVSDRAGRTALHHAafsghvEMVSLLLSRGANINafdkkdrraihwaaymgh 215
Cdd:PHA02716  246 NGMSPIMTYIIN-----IDNINPEITNIYIESLDGNKVKNIP------MILHSYITLARNID------------------ 296
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 216 IEVVKLLVAHGAEVTCKDKKSYTPLHAAASSGMIS--VVKYLLDLGVDMNEPNAYGNTPLH--------VACYNGQ---D 282
Cdd:PHA02716  297 ISVVYSFLQPGVKLHYKDSAGRTCLHQYILRHNIStdIIKLLHEYGNDLNEPDNIGNTVLHtylsmlsvVNILDPEtdnD 376
                         250       260
                  ....*....|....*....|....*..
gi 2024376459 283 V---VVNELIDSGANVNQMNEKGFTPL 306
Cdd:PHA02716  377 IrldVIQCLISLGADITAVNCLGYTPL 403
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
177-335 9.01e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 60.65  E-value: 9.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 177 AAFSGHVEMVSLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVAHGAEVTCKDKKSYTPLHAAASSGMISVVKYLL 256
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILY 611
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024376459 257 DLGvDMNEPNAYGNTpLHVACYNGQDVVVNELIDSGANVNQMNEKGFTPLHFAAASTHGALcLELLVCNGADVNMKSKD 335
Cdd:PLN03192  612 HFA-SISDPHAAGDL-LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDM-VRLLIMNGADVDKANTD 687
Ank_4 pfam13637
Ankyrin repeats (many copies);
139-190 1.22e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.43  E-value: 1.22e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2024376459 139 TPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHVEMVSLLL 190
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
238-375 1.33e-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: 59.64  E-value: 1.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 238 TPLHAAASSGMISVVKYLLDL-GVDMNEPNAYGNTPLHVACYNGQDVVVNELIDSGAN-VNQ-MNE---KGFTPLHFAAA 311
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKCpSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNEpMTSdlyQGETALHIAVV 98
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024376459 312 STHGALcLELLVCNGADVN---------MKSKD-----GKTPLHMTAIHGRFSRSQTIIQNGAEIDCEDKNGNTPLHI 375
Cdd:cd22192    99 NQNLNL-VRELIARGADVVspratgtffRPGPKnliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHI 175
PHA02874 PHA02874
ankyrin repeat protein; Provisional
37-185 1.36e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 59.59  E-value: 1.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459  37 NVLPPLVQAIFNGDPDEVRALIFKKEDVNFQDNEKRTPLHAAAyLGDAEIIELLIlSGARVNAKDSKWLTPLHRAVA-SC 115
Cdd:PHA02874  189 NGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAI-IHNRSAIELLI-NNASINDQDIDGSTPLHHAINpPC 266
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 116 SEDAVQVLLKHSADVNARDKNWQTPLHIAAanKAVKCAEALVPLLSNVNVSDRAGRtaLHHAAFSGHVEM 185
Cdd:PHA02874  267 DIDIIDILLYHKADISIKDNKGENPIDTAF--KYINKDPVIKDIIANAVLIKEADK--LKDSDFLEHIEI 332
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
174-256 1.71e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 59.53  E-value: 1.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 174 LHHAAFSGHVEMVSLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVAHGAEVTCKDKKSYTPLHAAASSGMISVVK 253
Cdd:PTZ00322   86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165

                  ...
gi 2024376459 254 YLL 256
Cdd:PTZ00322  166 LLS 168
PHA02859 PHA02859
ankyrin repeat protein; Provisional
102-280 2.59e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 56.75  E-value: 2.59e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 102 SKWLTPLHRAVASCSEDAVQvllKHSADVNARDKNWQTPLHIAAANKAV--KCAEALVPLLSNVNVSDRA-GRTALHH-A 177
Cdd:PHA02859   19 YRYCNPLFYYVEKDDIEGVK---KWIKFVNDCNDLYETPIFSCLEKDKVnvEILKFLIENGADVNFKTRDnNLSALHHyL 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 178 AFSGHV--EMVSLLLSRGANINAFDKKDRRAIHwaAYMGH----IEVVKLLVAHGAEVTCKDKK------SYTPLHAAAS 245
Cdd:PHA02859   96 SFNKNVepEILKILIDSGSSITEEDEDGKNLLH--MYMCNfnvrINVIKLLIDSGVSFLNKDFDnnnilySYILFHSDKK 173
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2024376459 246 sgmisVVKYLLDLGVDMNEPNAYGNTPLHVACYNG 280
Cdd:PHA02859  174 -----IFDFLTSLGIDINETNKSGYNCYDLIKFRN 203
PHA03100 PHA03100
ankyrin repeat protein; Provisional
52-136 4.88e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 57.75  E-value: 4.88e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459  52 DEVRALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEDAVQVLLKHSADVN 131
Cdd:PHA03100  173 NRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252

                  ....*
gi 2024376459 132 ARDKN 136
Cdd:PHA03100  253 TIIET 257
Ank_4 pfam13637
Ankyrin repeats (many copies);
72-124 6.99e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.51  E-value: 6.99e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2024376459  72 RTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEDAVQVLL 124
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02859 PHA02859
ankyrin repeat protein; Provisional
236-394 8.89e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 55.21  E-value: 8.89e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 236 SYT-PLHAAASSGMISVVKYLLDLgvdMNEPNAYGNTPLHvACYNGQDVVVNE---LIDSGANVN-QMNEKGFTPLHFAA 310
Cdd:PHA02859   20 RYCnPLFYYVEKDDIEGVKKWIKF---VNDCNDLYETPIF-SCLEKDKVNVEIlkfLIENGADVNfKTRDNNLSALHHYL 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 311 ASTHGAL--CLELLVCNGADVNMKSKDGKTPLH--MTAIHGRFSRSQTIIQNGAEIDCEDKNGNTPLHIAARYGHELLI- 385
Cdd:PHA02859   96 SFNKNVEpeILKILIDSGSSITEEDEDGKNLLHmyMCNFNVRINVIKLLIDSGVSFLNKDFDNNNILYSYILFHSDKKIf 175

                  ....*....
gi 2024376459 386 NTLITSGAD 394
Cdd:PHA02859  176 DFLTSLGID 184
PHA02798 PHA02798
ankyrin-like protein; Provisional
284-394 9.55e-09

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 57.15  E-value: 9.55e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 284 VVNELIDSGANVNQMNEKGFTPLHFAAAS----THGALCLELLVCNGADVNMKSKDGKTPLHMTAIHGRFSRSQTI---I 356
Cdd:PHA02798   53 IVKLFINLGANVNGLDNEYSTPLCTILSNikdyKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILlfmI 132
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2024376459 357 QNGAEIDCEDKNGNTPLHIAARYGHEL---LINTLITSGAD 394
Cdd:PHA02798  133 ENGADTTLLDKDGFTMLQVYLQSNHHIdieIIKLLLEKGVD 173
PHA02875 PHA02875
ankyrin repeat protein; Provisional
41-197 1.45e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 56.15  E-value: 1.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459  41 PLVQAIFNGDPDEVRALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLIlsgarvnakdskwltplhravascsedav 120
Cdd:PHA02875  105 PLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLI----------------------------- 155
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024376459 121 qvllKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNVN-VSDRAGRTALHHAAFSGHVEMVSLLLSRGANIN 197
Cdd:PHA02875  156 ----DHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDyFGKNGCVAALCYAIENNKIDIVRLFIKRGADCN 229
PHA02946 PHA02946
ankyin-like protein; Provisional
164-342 1.51e-08

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 56.22  E-value: 1.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 164 NVSDRAGRTALHHAAFSGHVEMVSLLLSRGANINAFDKKDRRAIHWAAYMGH--IEVVKLLVAHGAEVTCK-DKKSYTPL 240
Cdd:PHA02946   66 NETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYGAKINNSvDEEGCGPL 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 241 HAAASSGMiSVVKYLLDLGVDMNEPNAYGNTPLH--VACYNGQDVVVNELIDSGANVNQMNEKGFTPLHFAAASTHGALC 318
Cdd:PHA02946  146 LACTDPSE-RVFKKIMSIGFEARIVDKFGKNHIHrhLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHIVCSKTVKNVD 224
                         170       180
                  ....*....|....*....|....
gi 2024376459 319 LELLVCNGADVNMKSKDGKTPLHM 342
Cdd:PHA02946  225 IINLLLPSTDVNKQNKFGDSPLTL 248
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
58-277 1.55e-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: 56.63  E-value: 1.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459  58 IFKKEDVNFQDNEKrtplhaaAYLGDAEIIELLILSGARVNAK-------DSKWLTPLHRAVA-SCSEDAVQVLLKHSAD 129
Cdd:TIGR00870   6 IVPAEESPLSDEEK-------AFLPAAERGDLASVYRDLEEPKklnincpDRLGRSALFVAAIeNENLELTELLLNLSCR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 130 VNARDknwqTPLHIAAANKAVKCAEALVPLLSN---------VNVSDR----AGRTALHHAAFSGHVEMVSLLLSRGANI 196
Cdd:TIGR00870  79 GAVGD----TLLHAISLEYVDAVEAILLHLLAAfrksgplelANDQYTseftPGITALHLAAHRQNYEIVKLLLERGASV 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 197 NA------FDKKDRRA--------IHWAAYMGHIEVVKLLVAHGAEVTCKDKKSYTPLHAAA------------SSGMIS 250
Cdd:TIGR00870 155 PAracgdfFVKSQGVDsfyhgespLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVmenefkaeyeelSCQMYN 234
                         250       260       270
                  ....*....|....*....|....*....|.
gi 2024376459 251 VVKYLLDLGVDMNE----PNAYGNTPLHVAC 277
Cdd:TIGR00870 235 FALSLLDKLRDSKEleviLNHQGLTPLKLAA 265
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
114-191 5.05e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.90  E-value: 5.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 114 SCSEDAV--QVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHVEMVSLLLS 191
Cdd:PTZ00322   90 AASGDAVgaRILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
219-288 5.46e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.90  E-value: 5.46e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 219 VKLLVAHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNEL 288
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
Ank_4 pfam13637
Ankyrin repeats (many copies);
338-389 6.78e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.81  E-value: 6.78e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2024376459 338 TPLHMTAIHGRFSRSQTIIQNGAEIDCEDKNGNTPLHIAARYGHELLINTLI 389
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
50-173 1.21e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 53.49  E-value: 1.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459  50 DPDEVRALIFKKEDVNFQDNEKRTPLHAAAYLGD--AEIIELLILSGARVNAKDSKWLTPLHRAVASCSEDAVQVLLKHS 127
Cdd:PHA03095  201 RARIVRELIRAGCDPAATDMLGNTPLHSMATGSSckRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALG 280
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2024376459 128 ADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTA 173
Cdd:PHA03095  281 ADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAATLNTA 326
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
304-397 1.40e-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: 53.48  E-value: 1.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 304 TPLhFAAASTHGALCLE-LLVCNGADVNMKSKDGKTPLHMTAIHGRFSRSQTIIQNGAE-----IDCEDKNGNTPLHIAA 377
Cdd:cd22192    19 SPL-LLAAKENDVQAIKkLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElvnepMTSDLYQGETALHIAV 97
                          90       100
                  ....*....|....*....|
gi 2024376459 378 RYGHELLINTLITSGADTAK 397
Cdd:cd22192    98 VNQNLNLVRELIARGADVVS 117
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
311-380 1.46e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 53.36  E-value: 1.46e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 311 ASTHGALCLELLVCNGADVNMKSKDGKTPLHMTAIHGRFSRSQTIIQNGAEIDCEDKNGNTPLHIAARYG 380
Cdd:PTZ00322   90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENG 159
Ank_4 pfam13637
Ankyrin repeats (many copies);
269-323 2.87e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.88  E-value: 2.87e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2024376459 269 GNTPLHVACYNGQDVVVNELIDSGANVNQMNEKGFTPLHFAAASTHGAlCLELLV 323
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVE-VLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
244-350 3.93e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.21  E-value: 3.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 244 ASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDSGANVNQMNEKGFTPLHFAAASTHGALCLELLV 323
Cdd:PTZ00322   90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2024376459 324 CNGADVNM------KSKDGKTPLH----MTAIHGRFS 350
Cdd:PTZ00322  170 HSQCHFELganakpDSFTGKPPSLedspISSHHPDFS 206
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
33-127 4.03e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.21  E-value: 4.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459  33 LPPGNVLPPLV---------QAIFNGDPDEVRALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLILSGARVNAKDSK 103
Cdd:PTZ00322   68 LTTEEVIDPVVahmltvelcQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKD 147
                          90       100
                  ....*....|....*....|....
gi 2024376459 104 WLTPLHRAVASCSEDAVQVLLKHS 127
Cdd:PTZ00322  148 GKTPLELAEENGFREVVQLLSRHS 171
Ank_5 pfam13857
Ankyrin repeats (many copies);
222-276 4.28e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.57  E-value: 4.28e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2024376459 222 LVAHG-AEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVA 276
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
39-91 9.96e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.34  E-value: 9.96e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2024376459  39 LPPLVQAIFNGDPDEVRALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLI 91
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
264-380 1.01e-06

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: 50.91  E-value: 1.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 264 EPNAYGNTPLHVACYNGQDVVVNELIDSGANVN----------QMNEKGF----TPLHFAAASTHGALcLELLVCNGAD- 328
Cdd:cd22194   136 EEAYEGQTALNIAIERRQGDIVKLLIAKGADVNahakgvffnpKYKHEGFyfgeTPLALAACTNQPEI-VQLLMEKESTd 214
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024376459 329 VNMKSKDGKTPLHMTAIHGRFSRSQT--IIQNGAEI--DCEDKN--------GNTPLHIAARYG 380
Cdd:cd22194   215 ITSQDSRGNTVLHALVTVAEDSKTQNdfVKRMYDMIllKSENKNletirnneGLTPLQLAAKMG 278
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
170-201 1.17e-06

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 44.59  E-value: 1.17e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2024376459 170 GRTALHHAAFS-GHVEMVSLLLSRGANINAFDK 201
Cdd:pfam00023   2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
138-289 1.60e-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: 50.26  E-value: 1.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 138 QTPLHIAAANKAVKCAEALVPLLSNVNVSDRA--------------GRTALHHAAFSGHVEMVSLLLSRGANINA----- 198
Cdd:cd21882    27 KTCLHKAALNLNDGVNEAIMLLLEAAPDSGNPkelvnapctdefyqGQTALHIAIENRNLNLVRLLVENGADVSAratgr 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 199 -FDKKDRRAIHW-------AAYMGHIEVVKLLVAHGAE---VTCKDKKSYTPLHA---------AASSGMISVVKYLLDL 258
Cdd:cd21882   107 fFRKSPGNLFYFgelplslAACTNQEEIVRLLLENGAQpaaLEAQDSLGNTVLHAlvlqadntpENSAFVCQMYNLLLSY 186
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2024376459 259 G------VDMNE-PNAYGNTPLHVACYNGQDVVVNELI 289
Cdd:cd21882   187 GahldptQQLEEiPNHQGLTPLKLAAVEGKIVMFQHIL 224
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
82-156 1.77e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.90  E-value: 1.77e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024376459  82 GDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEDAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEAL 156
Cdd:PTZ00322   93 GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
73-210 1.99e-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: 49.63  E-value: 1.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459  73 TPLHAAAYLGDAEIIELLILSGARVNA---------KDSKWLT-----PLHRAVASCSEDAVQVLLKHSADVNARDKNWQ 138
Cdd:cd22192    91 TALHIAVVNQNLNLVRELIARGADVVSpratgtffrPGPKNLIyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGN 170
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 139 TPLHIAA--ANKAVKCAE-----ALVPLLSNVNVS---DRAGRTALHHAAFSGHVEMVSLLLSRganinafdkkdRRAIH 208
Cdd:cd22192   171 TVLHILVlqPNKTFACQMydlilSYDKEDDLQPLDlvpNNQGLTPFKLAAKEGNIVMFQHLVQK-----------RRHIQ 239

                  ..
gi 2024376459 209 WA 210
Cdd:cd22192   240 WT 241
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
170-198 2.39e-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: 43.73  E-value: 2.39e-06
                           10        20
                   ....*....|....*....|....*....
gi 2024376459  170 GRTALHHAAFSGHVEMVSLLLSRGANINA 198
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
123-177 2.60e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.26  E-value: 2.60e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2024376459 123 LLKH-SADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHA 177
Cdd:pfam13857   1 LLEHgPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
304-356 1.01e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.65  E-value: 1.01e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2024376459 304 TPLHFAAASTHGAlCLELLVCNGADVNMKSKDGKTPLHMTAIHGRFSRSQTII 356
Cdd:pfam13637   3 TALHAAAASGHLE-LLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
170-198 1.06e-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.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 41.86  E-value: 1.06e-05
                          10        20
                  ....*....|....*....|....*....
gi 2024376459 170 GRTALHHAAFSGHVEMVSLLLSRGANINA 198
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
268-296 1.17e-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: 41.80  E-value: 1.17e-05
                           10        20
                   ....*....|....*....|....*....
gi 2024376459  268 YGNTPLHVACYNGQDVVVNELIDSGANVN 296
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
Ank_5 pfam13857
Ankyrin repeats (many copies);
293-342 2.17e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.56  E-value: 2.17e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2024376459 293 ANVNQMNEKGFTPLHFAAasTHGAL-CLELLVCNGADVNMKSKDGKTPLHM 342
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAA--KYGALeIVRVLLAYGVDLNLKDEEGLTALDL 55
PHA02946 PHA02946
ankyin-like protein; Provisional
219-375 2.38e-05

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 46.20  E-value: 2.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 219 VKLLVAHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVV--VNELIDSGANVN 296
Cdd:PHA02946   55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIerINLLVQYGAKIN 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 297 Q-MNEKGFTPLhfAAASTHGALCLELLVCNGADVNMKSKDGKTPLH--MTAIHGRFSRSQTIIQNGAEIDCEDKNGNTPL 373
Cdd:PHA02946  135 NsVDEEGCGPL--LACTDPSERVFKKIMSIGFEARIVDKFGKNHIHrhLMSDNPKASTISWMMKLGISPSKPDHDGNTPL 212

                  ..
gi 2024376459 374 HI 375
Cdd:PHA02946  213 HI 214
Ank_5 pfam13857
Ankyrin repeats (many copies);
189-243 3.03e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.18  E-value: 3.03e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2024376459 189 LLSRG-ANINAFDKKDRRAIHWAAYMGHIEVVKLLVAHGAEVTCKDKKSYTPLHAA 243
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
268-300 7.89e-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: 39.58  E-value: 7.89e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2024376459 268 YGNTPLHVACY-NGQDVVVNELIDSGANVNQMNE 300
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
Ank_5 pfam13857
Ankyrin repeats (many copies);
62-111 8.26e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.02  E-value: 8.26e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2024376459  62 EDVNFQDNEKRTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRA 111
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
95-144 1.04e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.64  E-value: 1.04e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2024376459  95 ARVNAKDSKWLTPLHRAVASCSEDAVQVLLKHSADVNARDKNWQTPLHIA 144
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
255-309 1.06e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.64  E-value: 1.06e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2024376459 255 LLDLG-VDMNEPNAYGNTPLHVACYNGQDVVVNELIDSGANVNQMNEKGFTPLHFA 309
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
237-264 1.25e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 38.72  E-value: 1.25e-04
                           10        20
                   ....*....|....*....|....*...
gi 2024376459  237 YTPLHAAASSGMISVVKYLLDLGVDMNE 264
Cdd:smart00248   3 RTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
61-279 1.74e-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: 43.64  E-value: 1.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459  61 KEDVN--FQDNEKR--TPLHAAAYLGDAEIIELLILSGARVNA------------KDSKWLTPLHRAVASCSE--DAVQV 122
Cdd:cd22196    80 KEFVNaaYTDSYYKgqTALHIAIERRNMHLVELLVQNGADVHArasgeffkkkkgGPGFYFGELPLSLAACTNqlDIVKF 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 123 LLKHS---ADVNARDKNWQTPLHiaaankavkcaeALVPLLSNvnvsdragrtALHHAAFSghVEMVSLLLSRGANINAF 199
Cdd:cd22196   160 LLENPhspADISARDSMGNTVLH------------ALVEVADN----------TPENTKFV--TKMYNEILILGAKIRPL 215
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 200 DKkdrraihwaaymghIEvvkllvahgaEVTckDKKSYTPLHAAASSGMISVVKYLldLGVDMNEPN-----------AY 268
Cdd:cd22196   216 LK--------------LE----------EIT--NKKGLTPLKLAAKTGKIGIFAYI--LGREIKEPEcrhlsrkftewAY 267
                         250
                  ....*....|.
gi 2024376459 269 GntPLHVACYN 279
Cdd:cd22196   268 G--PVHSSLYD 276
PHA02795 PHA02795
ankyrin-like protein; Provisional
157-198 1.83e-04

ankyrin-like protein; Provisional


Pssm-ID: 165157 [Multi-domain]  Cd Length: 437  Bit Score: 43.45  E-value: 1.83e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2024376459 157 VPLLSNVNVSDRAGRTALHHAAFSGHVEMVSLLLSRGANINA 198
Cdd:PHA02795  208 IPYIEDINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNA 249
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
170-310 2.21e-04

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: 43.21  E-value: 2.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 170 GRTALHHAAFSGHVEMVSLLLSRGANINA------FDKKDRraiHWAAYMGHievvkllvahgaevtckdkksyTPLHAA 243
Cdd:cd22194   141 GQTALNIAIERRQGDIVKLLIAKGADVNAhakgvfFNPKYK---HEGFYFGE----------------------TPLALA 195
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 244 ASSGMISVVKYLLDlgvdmNEPNAY------GNTPLH----VA-CYNGQDVVVNELID------SGANVNQM-NEKGFTP 305
Cdd:cd22194   196 ACTNQPEIVQLLME-----KESTDItsqdsrGNTVLHalvtVAeDSKTQNDFVKRMYDmillksENKNLETIrNNEGLTP 270

                  ....*
gi 2024376459 306 LHFAA 310
Cdd:cd22194   271 LQLAA 275
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
85-279 2.23e-04

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: 43.21  E-value: 2.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459  85 EIIELLI-----------LSGARVNAKDSKWLTPLHRAVASCSEDAVQVLLKHSADVNARDKN------WQ--------T 139
Cdd:cd22194   111 EIVRILLafaeengildrFINAEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGvffnpkYKhegfyfgeT 190
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 140 PLHIAAANKAVKCAEALVPLLS-NVNVSDRAGRTALH-----------HAAFSGHVEMVSLLLSRGANINAF-DKKDRRA 206
Cdd:cd22194   191 PLALAACTNQPEIVQLLMEKEStDITSQDSRGNTVLHalvtvaedsktQNDFVKRMYDMILLKSENKNLETIrNNEGLTP 270
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024376459 207 IHWAAYMGHIEVVKLLVahGAEVTCKDKKSYTPLHAAASSGMISVVKYllDL-GVDMNEPNAYgntpLHVACYN 279
Cdd:cd22194   271 LQLAAKMGKAEILKYIL--SREIKEKPNRSLSRKFTDWAYGPVSSSLY--DLtNVDTTTDNSV----LEIIVYN 336
PHA02884 PHA02884
ankyrin repeat protein; Provisional
85-225 2.37e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 42.66  E-value: 2.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459  85 EIIELLILSGARVNAK----DSKWLTPLHRAVASCSEDAVQVLLKHSADVNARDKNWQ-TPLHIAAANKAVKCAEALVPL 159
Cdd:PHA02884   47 DIIDAILKLGADPEAPfplsENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKiTPLYISVLHGCLKCLEILLSY 126
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024376459 160 LSNVNVSDRAGRTALHHAAFSGHVEMVSLLlsRGANINAFDKKDRRaihwaaYMGHIEVVKLLVAH 225
Cdd:PHA02884  127 GADINIQTNDMVTPIELALMICNNFLAFMI--CDNEISNFYKHPKK------ILINFDILKILVSH 184
PHA02884 PHA02884
ankyrin repeat protein; Provisional
251-343 2.68e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 42.66  E-value: 2.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 251 VVKYLLDLGVDMNEP-----NAYgNTPLHVACYNGQDVVVNELIDSGANVNQM-NEKGFTPLHFAAasTHGAL-CLELLV 323
Cdd:PHA02884   48 IIDAILKLGADPEAPfplseNSK-TNPLIYAIDCDNDDAAKLLIRYGADVNRYaEEAKITPLYISV--LHGCLkCLEILL 124
                          90       100
                  ....*....|....*....|
gi 2024376459 324 CNGADVNMKSKDGKTPLHMT 343
Cdd:PHA02884  125 SYGADINIQTNDMVTPIELA 144
Ank_5 pfam13857
Ankyrin repeats (many copies);
321-376 3.00e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.48  E-value: 3.00e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2024376459 321 LLVCNGADVNMKSKDGKTPLHMTAIHGRFSRSQTIIQNGAEIDCEDKNGNTPLHIA 376
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
301-334 3.03e-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: 3.03e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2024376459 301 KGFTPLHFAAASTHGALCLELLVCNGADVNMKSK 334
Cdd:pfam00023   1 DGNTPLHLAAGRRGNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
368-394 3.80e-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: 37.57  E-value: 3.80e-04
                           10        20
                   ....*....|....*....|....*..
gi 2024376459  368 NGNTPLHIAARYGHELLINTLITSGAD 394
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
PHA02736 PHA02736
Viral ankyrin protein; Provisional
167-293 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 2024376459 167 DRAGRTALHHAAFSGHVemVSLLLSRGANINA-------FDKKDRRAIHWAAYMGHI---EVVKLLVAHGAEVTCKDKK- 235
Cdd:PHA02736   14 DIEGENILHYLCRNGGV--TDLLAFKNAISDEnrylvleYNRHGKQCVHIVSNPDKAdpqEKLKLLMEWGADINGKERVf 91
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2024376459 236 SYTPLHAAASSGMISVVKYLLDL-GVDMNEPNAYGNTPLHVACYNGQDVVVNELIDSGA 293
Cdd:PHA02736   92 GNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYVACERHDAKMMNILRAKGA 150
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
72-101 5.10e-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: 5.10e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2024376459  72 RTPLHAAAY-LGDAEIIELLILSGARVNAKD 101
Cdd:pfam00023   3 NTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
202-312 6.48e-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: 41.72  E-value: 6.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 202 KDRRAIHWAAYMGHIEVVKLLVAHGAEVTC-------KDKKSYT-------PLHAAASSGMISVVKYLLD---LGVDMNE 264
Cdd:cd22196    93 KGQTALHIAIERRNMHLVELLVQNGADVHArasgeffKKKKGGPgfyfgelPLSLAACTNQLDIVKFLLEnphSPADISA 172
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024376459 265 PNAYGNTPLHVACYNGQDVVVN---------ELIDSGANVNQM-------NEKGFTPLHFAAAS 312
Cdd:cd22196   173 RDSMGNTVLHALVEVADNTPENtkfvtkmynEILILGAKIRPLlkleeitNKKGLTPLKLAAKT 236
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
106-135 9.12e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.50  E-value: 9.12e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2024376459 106 TPLHRAVASC-SEDAVQVLLKHSADVNARDK 135
Cdd:pfam00023   4 TPLHLAAGRRgNLEIVKLLLSKGADVNARDK 34
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
206-234 9.30e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.50  E-value: 9.30e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 2024376459 206 AIHWAAYM-GHIEVVKLLVAHGAEVTCKDK 234
Cdd:pfam00023   5 PLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
268-296 1.10e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 36.08  E-value: 1.10e-03
                          10        20
                  ....*....|....*....|....*....
gi 2024376459 268 YGNTPLHVACYNGQDVVVNELIDSGANVN 296
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
41-109 1.11e-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: 41.15  E-value: 1.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459  41 PLVQAIFNGDPDEVRALIFKKEDVN--------FQDNEKRT------PLHAAAYLGDAEIIELLILSGARVNAKDSKWLT 106
Cdd:cd22192    92 ALHIAVVNQNLNLVRELIARGADVVspratgtfFRPGPKNLiyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNT 171

                  ...
gi 2024376459 107 PLH 109
Cdd:cd22192   172 VLH 174
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
158-350 1.31e-03

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 40.83  E-value: 1.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 158 PLLSNVNVSDRAGRTALHHAAFSG-HVEMVSLLLSRGANINAFDKkdrrAIHwAAYMGHIEVVKLLVAHGAEVtckDKKS 236
Cdd:TIGR00870  40 PKKLNINCPDRLGRSALFVAAIENeNLELTELLLNLSCRGAVGDT----LLH-AISLEYVDAVEAILLHLLAA---FRKS 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 237 YTPLHAAASSGmisvvkylldlgvdmNEPNAyGNTPLHVACYNGQDVVVNELIDSGANVN-----------QMNEK---G 302
Cdd:TIGR00870 112 GPLELANDQYT---------------SEFTP-GITALHLAAHRQNYEIVKLLLERGASVParacgdffvksQGVDSfyhG 175
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2024376459 303 FTPLHFAAASTHGALcLELLVCNGADVNMKSKDGKTPLHMTAIHGRFS 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 ...
206-231 1.55e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.64  E-value: 1.55e-03
                           10        20
                   ....*....|....*....|....*.
gi 2024376459  206 AIHWAAYMGHIEVVKLLVAHGAEVTC 231
Cdd:smart00248   5 PLHLAAENGNLEVVKLLLDKGADINA 30
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
267-375 1.66e-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: 40.63  E-value: 1.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 267 AYGNTPLHVACYNGQDVVvNELI--------DSGANVNQMNE-------KGFTPLHFAAAStHGALCLELLVCNGADVNM 331
Cdd:cd21882    24 ATGKTCLHKAALNLNDGV-NEAImllleaapDSGNPKELVNApctdefyQGQTALHIAIEN-RNLNLVRLLVENGADVSA 101
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 332 KSKD-------------GKTPLHMTAIHGRFSRSQTIIQNGAEI---DCEDKNGNTPLHI 375
Cdd:cd21882   102 RATGrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQPaalEAQDSLGNTVLHA 161
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
368-394 2.19e-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: 2.19e-03
                          10        20
                  ....*....|....*....|....*...
gi 2024376459 368 NGNTPLHIAA-RYGHELLINTLITSGAD 394
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGAD 28
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
355-394 2.29e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 40.27  E-value: 2.29e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2024376459 355 IIQNGAEIDCEDKNGNTPLHIAARYGHELLINTLITSGAD 394
Cdd:PTZ00322  101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGAD 140
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
368-394 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.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 35.31  E-value: 2.34e-03
                          10        20
                  ....*....|....*....|....*..
gi 2024376459 368 NGNTPLHIAARYGHELLINTLITSGAD 394
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGAD 27
PHA02791 PHA02791
ankyrin-like protein; Provisional
70-197 2.49e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 39.25  E-value: 2.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459  70 EKRTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEDAVQVLLKHSADVNARDKN-WQTPL-HIAAAN 147
Cdd:PHA02791   60 ENEFPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDSGNMQTVKLFVKKNWRLMFYGKTgWKTSFyHAVMLN 139
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2024376459 148 KAVKCAEALVPLLSNVNVSDRAgrTALHHAAFSGHVEMVSLLLSRGANIN 197
Cdd:PHA02791  140 DVSIVSYFLSEIPSTFDLAILL--SCIHITIKNGHVDMMILLLDYMTSTN 187
PHA02989 PHA02989
ankyrin repeat protein; Provisional
249-340 2.49e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 39.72  E-value: 2.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 249 ISVVKYLLDLGVDMNEpnAYGNTPLHVACYNGQDV---VVNELIDSGANVNQmneKGF--TPL-----HFAAASTHGALC 318
Cdd:PHA02989   16 KNALEFLLRTGFDVNE--EYRGNSILLLYLKRKDVkikIVKLLIDNGADVNY---KGYieTPLcavlrNREITSNKIKKI 90
                          90       100
                  ....*....|....*....|..
gi 2024376459 319 LELLVCNGADVNMKSKDGKTPL 340
Cdd:PHA02989   91 VKLLLKFGADINLKTFNGVSPI 112
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
237-266 3.09e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 34.96  E-value: 3.09e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2024376459 237 YTPLHAAA-SSGMISVVKYLLDLGVDMNEPN 266
Cdd:pfam00023   3 NTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PHA03100 PHA03100
ankyrin repeat protein; Provisional
41-102 3.30e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 39.26  E-value: 3.30e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024376459  41 PLVQAIFNGDPDEVRALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLILSGARVNAKDS 102
Cdd:PHA03100  195 PLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
237-261 3.54e-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: 34.93  E-value: 3.54e-03
                          10        20
                  ....*....|....*....|....*
gi 2024376459 237 YTPLHAAASSGMISVVKYLLDLGVD 261
Cdd:pfam13606   3 NTPLHLAARNGRLEIVKLLLENGAD 27
Ank_5 pfam13857
Ankyrin repeats (many copies);
162-201 4.24e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.40  E-value: 4.24e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2024376459 162 NVNVSDRAGRTALHHAAFSGHVEMVSLLLSRGANINAFDK 201
Cdd:pfam13857   8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDE 47
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
106-132 4.85e-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: 4.85e-03
                          10        20
                  ....*....|....*....|....*..
gi 2024376459 106 TPLHRAVASCSEDAVQVLLKHSADVNA 132
Cdd:pfam13606   4 TPLHLAARNGRLEIVKLLLENGADINA 30
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
301-374 5.07e-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: 39.01  E-value: 5.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 301 KGFTPLHFAAASTHGAlCLELLVCNGADVNMKSKD--------------GKTPLHMTAIHGRFSRSQTIIQNG---AEID 363
Cdd:cd22193    75 EGQTALHIAIERRQGD-IVALLVENGADVHAHAKGrffqpkyqgegfyfGELPLSLAACTNQPDIVQYLLENEhqpADIE 153
                          90
                  ....*....|.
gi 2024376459 364 CEDKNGNTPLH 374
Cdd:cd22193   154 AQDSRGNTVLH 164
PHA02791 PHA02791
ankyrin-like protein; Provisional
127-305 5.08e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 38.48  E-value: 5.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 127 SADVNARDKNWQTPLHIAAANKAVKC------AEALVPLLSNvnvsdragRTALHHAAFSGHVEMVSLLLSRGANINAFD 200
Cdd:PHA02791   20 SKDAFKADVHGHSALYYAIADNNVRLvctllnAGALKNLLEN--------EFPLHQAATLEDTKIVKILLFSGMDDSQFD 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 201 KKDRRAIHWAAYMGHIEVVKLLVAHGAEVTCKDKKSY-TPLHAAASSGMISVVKYLL-------DLGVDMnepnaygnTP 272
Cdd:PHA02791   92 DKGNTALYYAVDSGNMQTVKLFVKKNWRLMFYGKTGWkTSFYHAVMLNDVSIVSYFLseipstfDLAILL--------SC 163
                         170       180       190
                  ....*....|....*....|....*....|...
gi 2024376459 273 LHVACYNGQDVVVNELIDSGANVNQMNEKGFTP 305
Cdd:PHA02791  164 IHITIKNGHVDMMILLLDYMTSTNTNNSLLFIP 196
PHA02989 PHA02989
ankyrin repeat protein; Provisional
216-307 5.46e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 38.95  E-value: 5.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 216 IEVVKLLVAHGAEVtckDKKSY--TPLHAA------ASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNE 287
Cdd:PHA02989   50 IKIVKLLIDNGADV---NYKGYieTPLCAVlrnreiTSNKIKKIVKLLLKFGADINLKTFNGVSPIVCFIYNSNINNCDM 126
                          90       100
                  ....*....|....*....|....
gi 2024376459 288 L---IDSGANVNQM-NEKGFTPLH 307
Cdd:PHA02989  127 LrflLSKGINVNDVkNSRGYNLLH 150
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
279-374 6.42e-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: 38.63  E-value: 6.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024376459 279 NGQDVVVNELIDSGANVNQMNE-----------KGFTPLHFAAASTHGALcLELLVCNGADVN----------MKSKD-- 335
Cdd:cd22196    60 NGQNDTISLLLDIAEKTGNLKEfvnaaytdsyyKGQTALHIAIERRNMHL-VELLVQNGADVHarasgeffkkKKGGPgf 138
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2024376459 336 --GKTPLHMTAIHGRFSRSQTIIQN---GAEIDCEDKNGNTPLH 374
Cdd:cd22196   139 yfGELPLSLAACTNQLDIVKFLLENphsPADISARDSMGNTVLH 182
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
70-99 7.77e-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: 33.72  E-value: 7.77e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 2024376459   70 EKRTPLHAAAYLGDAEIIELLILSGARVNA 99
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02917 PHA02917
ankyrin-like protein; Provisional
157-231 9.18e-03

ankyrin-like protein; Provisional


Pssm-ID: 165231 [Multi-domain]  Cd Length: 661  Bit Score: 38.06  E-value: 9.18e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024376459 157 VPLLSNVNVSDRAGRTALHHAAFSGHVEMVSLLLSRGANINAFDKKDRRAIHWAAYMG-HIEVVKLLVAHGAEVTC 231
Cdd:PHA02917  439 LPYLKDINMIDKRGETLLHKAVRYNKQSLVSLLLESGSDVNIRSNNGYTCIAIAINESrNIELLKMLLCHKPTLDC 514
 
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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