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Conserved domains on  [gi|46519151|ref|NP_060448|]
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ankyrin repeat and KH domain-containing protein 1 isoform 2 [Homo sapiens]

Protein Classification

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

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

Gene Ontology:  GO:0005515
PubMed:  33435370|17176038

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
274-561 2.40e-46

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 165.13  E-value: 2.40e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151 274 LDIVKLLLLHDADVNSQSATGNTALTYACAGGFVDIVKVLLNEGANIEDHNENGHTPLMEAASAGHVEVARVLLDHGAGI 353
Cdd:COG0666   1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151 354 NThSNEFKESALTLACYKGHLDMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTL 433
Cdd:COG0666  81 NA-KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHL 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151 434 AACGGHVELAALLIERGANLEEVNDEGYTPLMEAAREGHEEMVALLLAQGANINAQTEEtQETALTLACCGGFSEVADFL 513
Cdd:COG0666 160 AAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDND-GKTALDLAAENGNLEIVKLL 238

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 46519151 514 IKAGADIELGC---STPLMEASQEGHLELVKYLLASGANVHATTATGDTAL 561
Cdd:COG0666 239 LEAGADLNAKDkdgLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
Ank_2 pfam12796
Ankyrin repeats (3 copies);
198-290 5.62e-16

Ankyrin repeats (3 copies);


:

Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 73.23  E-value: 5.62e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151   198 LAEACSDGDVNAVRKLLDEGRSVNEHTEEGESLLCLACSAGYYELAQVLLA-MHANVEDRGNkgdiTPLMAASSGGYLDI 276
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEhADVNLKDNGR----TALHYAARSGHLEI 76

                          90
                  ....*....|....
gi 46519151   277 VKLLLLHDADVNSQ 290
Cdd:pfam12796  77 VKLLLEKGADINVK 90
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 557-585 1.63e-04

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


:

Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.11  E-value: 1.63e-04
                           10        20
                   ....*....|....*....|....*....
gi 46519151    557 GDTALTYACENGHTDVADVLLQAGADLDK 585
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
274-561 2.40e-46

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 165.13  E-value: 2.40e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151 274 LDIVKLLLLHDADVNSQSATGNTALTYACAGGFVDIVKVLLNEGANIEDHNENGHTPLMEAASAGHVEVARVLLDHGAGI 353
Cdd:COG0666   1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151 354 NThSNEFKESALTLACYKGHLDMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTL 433
Cdd:COG0666  81 NA-KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHL 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151 434 AACGGHVELAALLIERGANLEEVNDEGYTPLMEAAREGHEEMVALLLAQGANINAQTEEtQETALTLACCGGFSEVADFL 513
Cdd:COG0666 160 AAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDND-GKTALDLAAENGNLEIVKLL 238

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 46519151 514 IKAGADIELGC---STPLMEASQEGHLELVKYLLASGANVHATTATGDTAL 561
Cdd:COG0666 239 LEAGADLNAKDkdgLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA03095 PHA03095
ankyrin-like protein; Provisional
 200-520 5.55e-25

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 108.57  E-value: 5.55e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  200 EACSDGDVNAVRKLLDEGRSVNEHTEEGESLLC--LACSAG-YYELAQVLLAMHANVEDRGNKGDiTPLMA-ASSGGYLD 275
Cdd:PHA03095  20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHlyLHYSSEkVKDIVRLLLEAGADVNAPERCGF-TPLHLyLYNATTLD 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  276 IVKLLLLHDADVNSQSATGNTALtYACAGGF---VDIVKVLLNEGANIEDHNENGHTPL---MEAASAgHVEVARVLLDH 349
Cdd:PHA03095  99 VIKLLIKAGADVNAKDKVGRTPL-HVYLSGFninPKVIRLLLRKGADVNALDLYGMTPLavlLKSRNA-NVELLRLLIDA 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  350 GAGI-----------NTHSNEFKESAltlacykghlDMVRFLLEAGADQEHKTDEMHTALMEACMDGHVE--VARLLLDS 416
Cdd:PHA03095 177 GADVyavddrfrsllHHHLQSFKPRA----------RIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIA 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  417 GAQVNMPADSFESPLTLAACGGHVELAALLIERGANLEEVNDEGYTPLMEAAREGHEEMVALLLAQGANINA-------- 488
Cdd:PHA03095 247 GISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETvaatlnta 326

                        330       340       350
                 ....*....|....*....|....*....|...
gi 46519151  489 -QTEETQETALTLACcggfseVADFLIKAGADI 520
Cdd:PHA03095 327 sVAGGDIPSDATRLC------VAKVVLRGAFSL 353
Ank_2 pfam12796
Ankyrin repeats (3 copies);
265-355 1.27e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.49  E-value: 1.27e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151   265 LMAASSGGYLDIVKLLLLHDADVNSQSATGNTALTYACAGGFVDIVKVLLNEGANieDHNENGHTPLMEAASAGHVEVAR 344
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|.
gi 46519151   345 VLLDHGAGINT 355
Cdd:pfam12796  79 LLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
198-290 5.62e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 73.23  E-value: 5.62e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151   198 LAEACSDGDVNAVRKLLDEGRSVNEHTEEGESLLCLACSAGYYELAQVLLA-MHANVEDRGNkgdiTPLMAASSGGYLDI 276
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEhADVNLKDNGR----TALHYAARSGHLEI 76

                          90
                  ....*....|....
gi 46519151   277 VKLLLLHDADVNSQ 290
Cdd:pfam12796  77 VKLLLEKGADINVK 90
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
198-331 1.31e-14

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 74.61  E-value: 1.31e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151 198 LAEACSDGDVNAVRKLLDEGRSVNEHTEEGESLLCLACSAGYYELAQVLLAMHANVEDRGNKGDiTPLMAASSGGYLDIV 277
Cdd:COG0666 157 LHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGK-TALDLAAENGNLEIV 235

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 46519151 278 KLLLLHDADVNSQSATGNTALTYACAGGFVDIVKVLLNEGANIEDHNENGHTPL 331
Cdd:COG0666 236 KLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 329-501 7.11e-12

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: 68.12  E-value: 7.11e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151 329 TPLMEAASAGHVEVARVLLdhgagINTHSNEFK-----ESALTLACYKGHLDMVRFLLEAGAD--QEHKTDEMH---TAL 398
Cdd:cd22192  19 SPLLLAAKENDVQAIKKLL-----KCPSCDLFQrgalgETALHVAALYDNLEAAVVLMEAAPElvNEPMTSDLYqgeTAL 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151 399 MEACMDGHVEVARLLLDSGAQVNMP--ADSF------------ESPLTLAACGGHVELAALLIERGANLEEVNDEGYTPL 464
Cdd:cd22192  94 HIAVVNQNLNLVRELIARGADVVSPraTGTFfrpgpknliyygEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 46519151 465 ----MEAAREGHEEMVALLLAQGANINAQTEETQE-----TALTLA 501
Cdd:cd22192 174 hilvLQPNKTFACQMYDLILSYDKEDDLQPLDLVPnnqglTPFKLA 219
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 205-326 1.70e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 63.53  E-value: 1.70e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  205 GDVNAVRKLLDEGRSVNEHTEEGESLLCLACSAGYYEL--AQVLL--AMHANVEDR--------------GNKGDiTPLM 266
Cdd:PHA03100 119 NSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLkiLKLLIdkGVDINAKNRvnyllsygvpinikDVYGF-TPLH 197

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  267 AASSGGYLDIVKLLLLHDADVNSQSATGNTALTYACAGGFVDIVKVLLNEGANIEDHNEN 326
Cdd:PHA03100 198 YAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 301-454 1.85e-06

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: 50.85  E-value: 1.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151   301 ACAGGFVDIVKVLLNEGA--NIEDHNENGHTPLMEAASAG-HVEVARVLLDHGAGINThsnefkESALTLACYKGHLDMV 377
Cdd:TIGR00870  24 AAERGDLASVYRDLEEPKklNINCPDRLGRSALFVAAIENeNLELTELLLNLSCRGAV------GDTLLHAISLEYVDAV 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151   378 ----RFLLEAGADQ-------EHKTDEM---HTALMEACMDGHVEVARLLLDSGAQVNMPA-----------DSF---ES 429
Cdd:TIGR00870  98 eailLHLLAAFRKSgplelanDQYTSEFtpgITALHLAAHRQNYEIVKLLLERGASVPARAcgdffvksqgvDSFyhgES 177

                         170       180
                  ....*....|....*....|....*
gi 46519151   430 PLTLAACGGHVELAALLIERGANLE 454
Cdd:TIGR00870 178 PLNAAACLGSPSIVALLSEDPADIL 202
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 459-488 2.68e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.42  E-value: 2.68e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 46519151    459 EGYTPLMEAAREGHEEMVALLLAQGANINA 488
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 557-585 1.63e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.11  E-value: 1.63e-04
                           10        20
                   ....*....|....*....|....*....
gi 46519151    557 GDTALTYACENGHTDVADVLLQAGADLDK 585
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 540-594 1.73e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.42  E-value: 1.73e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 46519151  540 VKYLLASGANVHATTATGDTALTYACENGHTDVADVLLQAGAD---LDKqeDMKTILE 594
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADptlLDK--DGKTPLE 153
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 557-585 2.49e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 35.70  E-value: 2.49e-03
                          10        20
                  ....*....|....*....|....*....
gi 46519151   557 GDTALTYACENGHTDVADVLLQAGADLDK 585
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
274-561 2.40e-46

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 165.13  E-value: 2.40e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151 274 LDIVKLLLLHDADVNSQSATGNTALTYACAGGFVDIVKVLLNEGANIEDHNENGHTPLMEAASAGHVEVARVLLDHGAGI 353
Cdd:COG0666   1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151 354 NThSNEFKESALTLACYKGHLDMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTL 433
Cdd:COG0666  81 NA-KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHL 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151 434 AACGGHVELAALLIERGANLEEVNDEGYTPLMEAAREGHEEMVALLLAQGANINAQTEEtQETALTLACCGGFSEVADFL 513
Cdd:COG0666 160 AAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDND-GKTALDLAAENGNLEIVKLL 238

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 46519151 514 IKAGADIELGC---STPLMEASQEGHLELVKYLLASGANVHATTATGDTAL 561
Cdd:COG0666 239 LEAGADLNAKDkdgLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
171-425 3.06e-45

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 162.43  E-value: 3.06e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151 171 ALDEAAAALTRMKAENSHNAGQVDTRSLAEACSDGDVNAVRKLLDEGRSVNEHTEEGESLLCLACSAGYYELAQVLLAMH 250
Cdd:COG0666  31 LLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAG 110

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151 251 ANVEDRGNKGDiTPLMAASSGGYLDIVKLLLLHDADVNSQSATGNTALTYACAGGFVDIVKVLLNEGANIEDHNENGHTP 330
Cdd:COG0666 111 ADVNARDKDGE-TPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETP 189

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151 331 LMEAASAGHVEVARVLLDHGAGINTHsNEFKESALTLACYKGHLDMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEVA 410
Cdd:COG0666 190 LHLAAENGHLEIVKLLLEAGADVNAK-DNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIV 268

                       250
                ....*....|....*
gi 46519151 411 RLLLDSGAQVNMPAD 425
Cdd:COG0666 269 KLLLLALLLLAAALL 283
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
346-606 3.75e-45

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 162.05  E-value: 3.75e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151 346 LLDHGAGINTHSNEFKESALTLACYKGHLDMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPAD 425
Cdd:COG0666   6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151 426 SFESPLTLAACGGHVELAALLIERGANLEEVNDEGYTPLMEAAREGHEEMVALLLAQGANINAQTEEtQETALTLACCGG 505
Cdd:COG0666  86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDND-GNTPLHLAAANG 164

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151 506 FSEVADFLIKAGADIELGCS---TPLMEASQEGHLELVKYLLASGANVHATTATGDTALTYACENGHTDVADVLLQAGAD 582
Cdd:COG0666 165 NLEIVKLLLEAGADVNARDNdgeTPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD 244

                       250       260
                ....*....|....*....|....
gi 46519151 583 LDKQEDMKTILEGIDPAKHQVRVA 606
Cdd:COG0666 245 LNAKDKDGLTALLLAAAAGAALIV 268
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
374-588 2.54e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 143.17  E-value: 2.54e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151 374 LDMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIERGANL 453
Cdd:COG0666   1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151 454 EEVNDEGYTPLMEAAREGHEEMVALLLAQGANINAQTEEtQETALTLACCGGFSEVADFLIKAGADIEL---GCSTPLME 530
Cdd:COG0666  81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKD-GETPLHLAAYNGNLEIVKLLLEAGADVNAqdnDGNTPLHL 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 46519151 531 ASQEGHLELVKYLLASGANVHATTATGDTALTYACENGHTDVADVLLQAGADLDKQED 588
Cdd:COG0666 160 AAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN 217
PHA03095 PHA03095
ankyrin-like protein; Provisional
 200-520 5.55e-25

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 108.57  E-value: 5.55e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  200 EACSDGDVNAVRKLLDEGRSVNEHTEEGESLLC--LACSAG-YYELAQVLLAMHANVEDRGNKGDiTPLMA-ASSGGYLD 275
Cdd:PHA03095  20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHlyLHYSSEkVKDIVRLLLEAGADVNAPERCGF-TPLHLyLYNATTLD 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  276 IVKLLLLHDADVNSQSATGNTALtYACAGGF---VDIVKVLLNEGANIEDHNENGHTPL---MEAASAgHVEVARVLLDH 349
Cdd:PHA03095  99 VIKLLIKAGADVNAKDKVGRTPL-HVYLSGFninPKVIRLLLRKGADVNALDLYGMTPLavlLKSRNA-NVELLRLLIDA 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  350 GAGI-----------NTHSNEFKESAltlacykghlDMVRFLLEAGADQEHKTDEMHTALMEACMDGHVE--VARLLLDS 416
Cdd:PHA03095 177 GADVyavddrfrsllHHHLQSFKPRA----------RIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIA 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  417 GAQVNMPADSFESPLTLAACGGHVELAALLIERGANLEEVNDEGYTPLMEAAREGHEEMVALLLAQGANINA-------- 488
Cdd:PHA03095 247 GISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETvaatlnta 326

                        330       340       350
                 ....*....|....*....|....*....|...
gi 46519151  489 -QTEETQETALTLACcggfseVADFLIKAGADI 520
Cdd:PHA03095 327 sVAGGDIPSDATRLC------VAKVVLRGAFSL 353
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 407-584 7.26e-25

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 107.44  E-value: 7.26e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  407 VEVARLLLDSGAQVNMPADSFESPLTLAACGGHV-----ELAALLIERGANLEEVNDEGYTPLMEAARE--GHEEMVALL 479
Cdd:PHA03100  48 IDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYL 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  480 LAQGANINAQTEeTQETALTLA--CCGGFSEVADFLIKAGADI----------ELGC---------STPLMEASQEGHLE 538
Cdd:PHA03100 128 LDNGANVNIKNS-DGENLLHLYleSNKIDLKILKLLIDKGVDInaknrvnyllSYGVpinikdvygFTPLHYAVYNNNPE 206

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 46519151  539 LVKYLLASGANVHATTATGDTALTYACENGHTDVADVLLQAGADLD 584
Cdd:PHA03100 207 FVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 186-583 7.51e-24

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 106.30  E-value: 7.51e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  186 NSHNAGQVDTRSLAEACSDGDV--NAVRKLLDEGRSVNEHTEEGESLLclacsagyyelAQVLLAMHANVedrgNKGDI- 262
Cdd:PHA02876 113 NKHKLDEACIHILKEAISGNDIhyDKINESIEYMKLIKERIQQDELLI-----------AEMLLEGGADV----NAKDIy 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  263 --TPLMAASSGGYLDIVKLLLLHDADVNSQSATGNTALTYACAGGFVDIVKVLLNEGANIedhNENGHTpLMEAASAGHV 340
Cdd:PHA02876 178 ciTPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNI---NKNDLS-LLKAIRNEDL 253

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  341 EVARVLLDHGAGINThSNEFKESALTLACYKGHLD-MVRFLLEAGADQEHKTDEMHTALMEACMDGH-VEVARLLLDSGA 418
Cdd:PHA02876 254 ETSLLLYDAGFSVNS-IDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGA 332

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  419 QVNMPADSFESPLTLAAC-GGHVELAALLIERGANLEEVNDEGYTPLMEAAREGHEEMVALLLAQGANINAQTEETQeTA 497
Cdd:PHA02876 333 DVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIG-TA 411

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  498 LTLACCGG--FSEVADfLIKAGADIELG---CSTPLMEASQEG-HLELVKYLLASGANVHATTATGDTALTYACenGHTD 571
Cdd:PHA02876 412 LHFALCGTnpYMSVKT-LIDRGANVNSKnkdLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIAL--EYHG 488

                        410
                 ....*....|..
gi 46519151  572 VADVLLQAGADL 583
Cdd:PHA02876 489 IVNILLHYGAEL 500
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 249-488 2.47e-23

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 102.82  E-value: 2.47e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  249 MHANVEDRGNKGDITPLMAASSGGYLDIVKLLLLHDADVNSQSATGNTALTYACAGGFV-----DIVKVLLNEGANIEDH 323
Cdd:PHA03100  23 MEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAP 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  324 NENGHTPLMEAASA--GHVEVARVLLDHGAGINTHSNEFKES-ALTLACYKGHLDMVRFLLEAGADQEHKTDemhtalme 400
Cdd:PHA03100 103 DNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLlHLYLESNKIDLKILKLLIDKGVDINAKNR-------- 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  401 acmdghVEvarLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIERGANLEEVNDEGYTPLMEAAREGHEEMVALLL 480
Cdd:PHA03100 175 ------VN---YLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLL 245


                 ....*...
gi 46519151  481 AQGANINA 488
Cdd:PHA03100 246 NNGPSIKT 253
Ank_2 pfam12796
Ankyrin repeats (3 copies);
265-355 1.27e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.49  E-value: 1.27e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151   265 LMAASSGGYLDIVKLLLLHDADVNSQSATGNTALTYACAGGFVDIVKVLLNEGANieDHNENGHTPLMEAASAGHVEVAR 344
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|.
gi 46519151   345 VLLDHGAGINT 355
Cdd:pfam12796  79 LLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
298-390 2.41e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.94  E-value: 2.41e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151   298 LTYACAGGFVDIVKVLLNEGANIEDHNENGHTPLMEAASAGHVEVARVLLDHgagINTHSNEFKESALTLACYKGHLDMV 377
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH---ADVNLKDNGRTALHYAARSGHLEIV 77

                          90
                  ....*....|...
gi 46519151   378 RFLLEAGADQEHK 390
Cdd:pfam12796  78 KLLLEKGADINVK 90
PHA03095 PHA03095
ankyrin-like protein; Provisional
 307-592 1.03e-19

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 92.40  E-value: 1.03e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  307 VDIVKVLLNEGANIEDHNENGHTPL---MEAASAGHVEVARVLLDHGAGINTHSNEFKESALTLACYKGHLDMVRFLLEA 383
Cdd:PHA03095  27 VEEVRRLLAAGADVNFRGEYGKTPLhlyLHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDVIKLLIKA 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  384 GADQEHKTDEMHTALmEACMDG---HVEVARLLLDSGAQVNmpaDSFESPLTLAAC-----GGHVELAALLIERGANLEE 455
Cdd:PHA03095 107 GADVNAKDKVGRTPL-HVYLSGfniNPKVIRLLLRKGADVN---ALDLYGMTPLAVllksrNANVELLRLLIDAGADVYA 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  456 VNDEGYTPL---MEAAREgHEEMVALLLAQGANINAqTEETQETALTLACCGGF---SEVADFLIkAGADIE----LGcS 525
Cdd:PHA03095 183 VDDRFRSLLhhhLQSFKP-RARIVRELIRAGCDPAA-TDMLGNTPLHSMATGSSckrSLVLPLLI-AGISINarnrYG-Q 258

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 46519151  526 TPLMEASQEGHLELVKYLLASGANVHATTATGDTALTYACENGHTDVADvllqagADLDKQEDMKTI 592
Cdd:PHA03095 259 TPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVR------AALAKNPSAETV 319
Ank_2 pfam12796
Ankyrin repeats (3 copies);
398-489 1.77e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 83.24  E-value: 1.77e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151   398 LMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIERGANleEVNDEGYTPLMEAAREGHEEMVA 477
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|..
gi 46519151   478 LLLAQGANINAQ 489
Cdd:pfam12796  79 LLLEKGADINVK 90
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 296-583 1.49e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 88.48  E-value: 1.49e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  296 TALTYACAGGFVDIVKVLLNEGANIEDHNENGHTPLMEAASAGHVEVARVLLDHGagINThsnefkeSALTLACYKGhlD 375
Cdd:PHA02874  37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNG--VDT-------SILPIPCIEK--D 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  376 MVRFLLEAGADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIERGANLEE 455
Cdd:PHA02874 106 MIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANV 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  456 VNDEGYTPLMEAAREGHEEMVALLLAQGANINAQteetqetaltlaCCGGFsevadflikagadielgcsTPLMEASQeg 535
Cdd:PHA02874 186 KDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNK------------CKNGF-------------------TPLHNAII-- 232

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 46519151  536 HLELVKYLLASGANVHATTATGDTALTYA----CEnghTDVADVLLQAGADL 583
Cdd:PHA02874 233 HNRSAIELLINNASINDQDIDGSTPLHHAinppCD---IDIIDILLYHKADI 281
Ank_2 pfam12796
Ankyrin repeats (3 copies);
331-421 1.71e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.55  E-value: 1.71e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151   331 LMEAASAGHVEVARVLLDHGAGINTHsNEFKESALTLACYKGHLDMVRFLLEaGADQEHKTDEMhTALMEACMDGHVEVA 410
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQ-DKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDNGR-TALHYAARSGHLEIV 77

                          90
                  ....*....|.
gi 46519151   411 RLLLDSGAQVN 421
Cdd:pfam12796  78 KLLLEKGADIN 88
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 326-582 2.39e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 87.74  E-value: 2.39e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  326 NGHTPLMEAASAGHVEVARVLLDHGAGIN-THSNEFkeSALTLACYKGHLDMVRFLLEAGADQEHKTDEMHTALMEACMD 404
Cdd:PHA02875   1 MDQVALCDAILFGELDIARRLLDIGINPNfEIYDGI--SPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  405 GHVEVARLLLDSGAQVNmpaDSF----ESPLTLAACGGHVELAALLIERGANLEEVNDEGYTPLMEAAREGHEEMVALLL 480
Cdd:PHA02875  79 GDVKAVEELLDLGKFAD---DVFykdgMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLI 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  481 AQganinaqteetqetaltlaccggfsevadfliKAGADIELGCS-TPLMEASQEGHLELVKYLLASGANVHATTATGD- 558
Cdd:PHA02875 156 DH--------------------------------KACLDIEDCCGcTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCv 203

                        250       260
                 ....*....|....*....|....
gi 46519151  559 TALTYACENGHTDVADVLLQAGAD 582
Cdd:PHA02875 204 AALCYAIENNKIDIVRLFIKRGAD 227
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 274-584 2.91e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 88.97  E-value: 2.91e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  274 LDIVKLLLLHDADVNSQSATGNTALTYACAGGFVDIVKVLLNEGANIEDHNENGHTPLMEAASAGHVEVARVLLDHGAGI 353
Cdd:PHA02876 158 LLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNI 237

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  354 NTHsnefkESALTLACYKGHLDMVRFLLEAGADQEHKTDEMHTALMEACMDGhvEVARL---LLDSGAQVNMPADSFESP 430
Cdd:PHA02876 238 NKN-----DLSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAP--SLSRLvpkLLERGADVNAKNIKGETP 310

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  431 LTLAACGGH-VELAALLIERGANLEEVNDEGYTPLMEAAR-EGHEEMVALLLAQGANINAQtEETQETALTLACCGGFSE 508
Cdd:PHA02876 311 LYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNAR-DYCDKTPIHYAAVRNNVV 389

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  509 VADFLIKAGADIE-----LGCSTPLMEASQEGHLElVKYLLASGANVHATTATGDTALTYACENG-HTDVADVLLQAGAD 582
Cdd:PHA02876 390 IINTLLDYGADIEalsqkIGTALHFALCGTNPYMS-VKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGAD 468


                 ..
gi 46519151  583 LD 584
Cdd:PHA02876 469 VN 470
Ank_2 pfam12796
Ankyrin repeats (3 copies);
464-553 4.43e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 76.69  E-value: 4.43e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151   464 LMEAAREGHEEMVALLLAQGANINAQTEETQeTALTLACCGGFSEVADFLI-KAGADIELGCSTPLMEASQEGHLELVKY 542
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGR-TALHLAAKNGHLEIVKLLLeHADVNLKDNGRTALHYAARSGHLEIVKL 79

                          90
                  ....*....|.
gi 46519151   543 LLASGANVHAT 553
Cdd:pfam12796  80 LLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
431-522 6.17e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 76.31  E-value: 6.17e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151   431 LTLAACGGHVELAALLIERGANLEEVNDEGYTPLMEAAREGHEEMVALLLAQgANINAQTEetQETALTLACCGGFSEVA 510
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN--GRTALHYAARSGHLEIV 77

                          90
                  ....*....|..
gi 46519151   511 DFLIKAGADIEL 522
Cdd:pfam12796  78 KLLLEKGADINV 89
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 206-355 1.01e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 82.79  E-value: 1.01e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  206 DVNAVRKLLDEGRSVNEHTEEGES-LLCLAC-SAGYYELAQVLLAMHANVEDRGNKGdITPLMAASSGGY--LDIVKLLL 281
Cdd:PHA03100  85 VKEIVKLLLEYGANVNAPDNNGITpLLYAISkKSNSYSIVEYLLDNGANVNIKNSDG-ENLLHLYLESNKidLKILKLLI 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  282 LHDADVN----------------SQSATGNTALTYACAGGFVDIVKVLLNEGANIEDHNENGHTPLMEAASAGHVEVARV 345
Cdd:PHA03100 164 DKGVDINaknrvnyllsygvpinIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKL 243

                        170
                 ....*....|
gi 46519151  346 LLDHGAGINT 355
Cdd:PHA03100 244 LLNNGPSIKT 253
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 272-522 1.57e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 81.96  E-value: 1.57e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  272 GYLDIVKLLLLHDADVNSQSATGNTALTYACAGGFVDIVKVLLNEGAnIEDHNENG-HTPLMEAASAGHVEVARVLLDHG 350
Cdd:PHA02875  13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGA-IPDVKYPDiESELHDAVEEGDVKAVEELLDLG 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  351 AGINTHSNEFKESALTLACYKGHLDMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESP 430
Cdd:PHA02875  92 KFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTP 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  431 LTLAACGGHVELAALLIERGANLEEVNDEGYTPLMEAAREGHE-EMVALLLAQGANINAQTEETQETALTLA-----CCG 504
Cdd:PHA02875 172 LIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKiDIVRLFIKRGADCNIMFMIEGEECTILDmicnmCTN 251

                        250
                 ....*....|....*...
gi 46519151  505 GFSEVADFLIkagADIEL 522
Cdd:PHA02875 252 LESEAIDALI---ADIAI 266
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 297-519 1.67e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 81.96  E-value: 1.67e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  297 ALTYACAGGFVDIVKVLLNEGANIEDHNENGHTPLMEAASAGHVEVARVLLDHGAGINTHSNEFkESALTLACYKGHLDM 376
Cdd:PHA02875   5 ALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDI-ESELHDAVEEGDVKA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  377 VRFLLEAG--ADQEHKTDEMhTALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIERGANLE 454
Cdd:PHA02875  84 VEELLDLGkfADDVFYKDGM-TPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLD 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46519151  455 EVNDEGYTPLMEAAREGHEEMVALLLAQGANINAQTEETQETALTLACCGGFSEVADFLIKAGAD 519
Cdd:PHA02875 163 IEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLFIKRGAD 227
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 206-402 3.46e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 81.19  E-value: 3.46e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  206 DVNAVRKLLDEGRSVNEHTEEGESLLCLACSAGYYELAQVLLAMHANVEDRGNKGDITPLMAASSGGYLDIVKLLLLHDA 285
Cdd:PHA02875  47 DSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGA 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  286 DVNSQSATGNTALTYACAGGFVDIVKVLLNEGANIEDHNENGHTPLMEAASAGHVEVARVLLDHGAGINTHSNEFKESAL 365
Cdd:PHA02875 127 DPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAAL 206

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 46519151  366 TLACYKGHLDMVRFLLEAGADQEHKT---DEMHTALMEAC 402
Cdd:PHA02875 207 CYAIENNKIDIVRLFIKRGADCNIMFmieGEECTILDMIC 246
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 252-433 5.32e-16

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 81.84  E-value: 5.32e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  252 NVEDRGNKGDITPLMAASSGGYLDIVKLLLLHDADVNSQSATGNTALTYACAGGFVDIVKVLLNEGANIEDHNENGHTPL 331
Cdd:PLN03192 516 NGGEHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTAL 595

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  332 MEAASAGHVEVARVLLDHGAGINTHSNefkESALTLACYKGHLDMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEVAR 411
Cdd:PLN03192 596 WNAISAKHHKIFRILYHFASISDPHAA---GDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVR 672

                        170       180
                 ....*....|....*....|...
gi 46519151  412 LLLDSGAQVNMPA-DSFESPLTL 433
Cdd:PLN03192 673 LLIMNGADVDKANtDDDFSPTEL 695
Ank_2 pfam12796
Ankyrin repeats (3 copies);
198-290 5.62e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 73.23  E-value: 5.62e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151   198 LAEACSDGDVNAVRKLLDEGRSVNEHTEEGESLLCLACSAGYYELAQVLLA-MHANVEDRGNkgdiTPLMAASSGGYLDI 276
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEhADVNLKDNGR----TALHYAARSGHLEI 76

                          90
                  ....*....|....
gi 46519151   277 VKLLLLHDADVNSQ 290
Cdd:pfam12796  77 VKLLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
498-586 4.26e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.92  E-value: 4.26e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151   498 LTLACCGGFSEVADFLIKAGADIELGCS---TPLMEASQEGHLELVKYLLaSGANVHATTAtGDTALTYACENGHTDVAD 574
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKngrTALHLAAKNGHLEIVKLLL-EHADVNLKDN-GRTALHYAARSGHLEIVK 78

                          90
                  ....*....|..
gi 46519151   575 VLLQAGADLDKQ 586
Cdd:pfam12796  79 LLLEKGADINVK 90
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
198-331 1.31e-14

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 74.61  E-value: 1.31e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151 198 LAEACSDGDVNAVRKLLDEGRSVNEHTEEGESLLCLACSAGYYELAQVLLAMHANVEDRGNKGDiTPLMAASSGGYLDIV 277
Cdd:COG0666 157 LHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGK-TALDLAAENGNLEIV 235

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 46519151 278 KLLLLHDADVNSQSATGNTALTYACAGGFVDIVKVLLNEGANIEDHNENGHTPL 331
Cdd:COG0666 236 KLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 264-520 2.62e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 72.61  E-value: 2.62e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  264 PLMAASSGGYLDIVKLLLLHDADVNSQSATGNTALTYACAGGFVDIVKVLLNEgaNIEDHNENGHTPLMEAASAGHVEVA 343
Cdd:PHA02878  40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRS--INKCSVFYTLVAIKDAFNNRNVEIF 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  344 RVLLdhgagINTHSNEfKESALTLACYKGHLD-----MVRFLLEAGADQEHKT-DEMHTALMEACMDGHVEVARLLLDSG 417
Cdd:PHA02878 118 KIIL-----TNRYKNI-QTIDLVYIDKKSKDDiieaeITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYG 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  418 AQVNMPADSFESPLTLAACGGHVELAALLIERGANLEEVNDEGYTPL-MEAAREGHEEMVALLLAQGANINAQTEETQET 496
Cdd:PHA02878 192 ANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLhISVGYCKDYDILKLLLEHGVDVNAKSYILGLT 271

                        250       260
                 ....*....|....*....|....
gi 46519151  497 ALTLACCGgfSEVADFLIKAGADI 520
Cdd:PHA02878 272 ALHSSIKS--ERKLKLLLEYGADI 293
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 307-584 3.79e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 71.83  E-value: 3.79e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  307 VDIVKVLLNEGANIEDHNENGHTPLMEAASAGHVEVARVLLdhgAGINTHSNEFKESALTLACYKGHLDMVRFLLEAGAD 386
Cdd:PHA02878  50 LDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMI---RSINKCSVFYTLVAIKDAFNNRNVEIFKIILTNRYK 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  387 QEHKTDEMHtaLMEACMDGHVE--VARLLLDSGAQVNM-PADSFESPLTLAACGGHVELAALLIERGANLEEVNDEGYTP 463
Cdd:PHA02878 127 NIQTIDLVY--IDKKSKDDIIEaeITKLLLSYGADINMkDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSP 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  464 LMEAAREGHEEMVALLLAQGANINAQTEetqetaltlacCGgfsevadflikagadielgcSTPL-MEASQEGHLELVKY 542
Cdd:PHA02878 205 LHHAVKHYNKPIVHILLENGASTDARDK-----------CG--------------------NTPLhISVGYCKDYDILKL 253

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 46519151  543 LLASGANVHA-TTATGDTALTYACENghTDVADVLLQAGADLD 584
Cdd:PHA02878 254 LLEHGVDVNAkSYILGLTALHSSIKS--ERKLKLLLEYGADIN 294
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 196-386 5.63e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 71.45  E-value: 5.63e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  196 RSLAEACSDGDVNAVRKLLdegrsVNEHTEEGESLLCLACSAGY-----YELAQVLLAMHANVEDRGNKGDITPLMAASS 270
Cdd:PHA02878 103 VAIKDAFNNRNVEIFKIIL-----TNRYKNIQTIDLVYIDKKSKddiieAEITKLLLSYGADINMKDRHKGNTALHYATE 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  271 GGYLDIVKLLLLHDADVNSQSATGNTALTYACAGGFVDIVKVLLNEGANIEDHNENGHTPL-MEAASAGHVEVARVLLDH 349
Cdd:PHA02878 178 NKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLhISVGYCKDYDILKLLLEH 257

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 46519151  350 GAGINTHSNEFKESALTLACYKGhlDMVRFLLEAGAD 386
Cdd:PHA02878 258 GVDVNAKSYILGLTALHSSIKSE--RKLKLLLEYGAD 292
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 407-585 6.34e-13

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 71.82  E-value: 6.34e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  407 VEVARLLLDSGAQVNMPADSFeSPLTLAACGGHVELAALLieRGANLEEVND-EGYTPLMEAAREGHEEMVALLLAQGAN 485
Cdd:PLN03192 507 LNVGDLLGDNGGEHDDPNMAS-NLLTVASTGNAALLEELL--KAKLDPDIGDsKGRTPLHIAASKGYEDCVLVLLKHACN 583

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  486 INAQtEETQETALTLACCGGFSEVADFLIK--------AGADIelgcstpLMEASQEGHLELVKYLLASGANVHATTATG 557
Cdd:PLN03192 584 VHIR-DANGNTALWNAISAKHHKIFRILYHfasisdphAAGDL-------LCTAAKRNDLTAMKELLKQGLNVDSEDHQG 655

                        170       180
                 ....*....|....*....|....*...
gi 46519151  558 DTALTYACENGHTDVADVLLQAGADLDK 585
Cdd:PLN03192 656 ATALQVAMAEDHVDMVRLLIMNGADVDK 683
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 397-584 7.45e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 70.79  E-value: 7.45e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  397 ALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIERGAnLEEVNDEGY-TPLMEAAREGHEEM 475
Cdd:PHA02875   5 ALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGA-IPDVKYPDIeSELHDAVEEGDVKA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  476 VALLLAQGANINAQTEETQETALTLACCGGFSEVADFLIKAGADIELGCS---TPLMEASQEGHLELVKYLLASGANVHA 552
Cdd:PHA02875  84 VEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTdkfSPLHLAVMMGDIKGIELLIDHKACLDI 163

                        170       180       190
                 ....*....|....*....|....*....|..
gi 46519151  553 TTATGDTALTYACENGHTDVADVLLQAGADLD 584
Cdd:PHA02875 164 EDCCGCTPLIIAMAKGDIAICKMLLDSGANID 195
Ank_2 pfam12796
Ankyrin repeats (3 copies);
528-593 2.49e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 63.21  E-value: 2.49e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46519151   528 LMEASQEGHLELVKYLLASGANVHATTATGDTALTYACENGHTDVADVLLQaGADLDKQEDMKTIL 593
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDNGRTAL 65
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 329-501 7.11e-12

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: 68.12  E-value: 7.11e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151 329 TPLMEAASAGHVEVARVLLdhgagINTHSNEFK-----ESALTLACYKGHLDMVRFLLEAGAD--QEHKTDEMH---TAL 398
Cdd:cd22192  19 SPLLLAAKENDVQAIKKLL-----KCPSCDLFQrgalgETALHVAALYDNLEAAVVLMEAAPElvNEPMTSDLYqgeTAL 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151 399 MEACMDGHVEVARLLLDSGAQVNMP--ADSF------------ESPLTLAACGGHVELAALLIERGANLEEVNDEGYTPL 464
Cdd:cd22192  94 HIAVVNQNLNLVRELIARGADVVSPraTGTFfrpgpknliyygEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 46519151 465 ----MEAAREGHEEMVALLLAQGANINAQTEETQE-----TALTLA 501
Cdd:cd22192 174 hilvLQPNKTFACQMYDLILSYDKEDDLQPLDLVPnnqglTPFKLA 219
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 198-434 9.52e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 67.60  E-value: 9.52e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  198 LAEACSDGDVNAVRKLLDEGRSVNEHTEEGESLLCLACSAG-----------------YYELAQVLLAMH---------- 250
Cdd:PHA02878  41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPnklgmkemirsinkcsvFYTLVAIKDAFNnrnveifkii 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  251 -ANVEDRGNKGDITPLMAASSGGYLD--IVKLLLLHDADVNSQSA-TGNTALTYACAGGFVDIVKVLLNEGANIEDHNEN 326
Cdd:PHA02878 121 lTNRYKNIQTIDLVYIDKKSKDDIIEaeITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDKT 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  327 GHTPLMEAASAGHVEVARVLLDHGAGINtHSNEFKESALTLAC-YKGHLDMVRFLLEAGADQEHKTDEMH-TALMEACMD 404
Cdd:PHA02878 201 NNSPLHHAVKHYNKPIVHILLENGASTD-ARDKCGNTPLHISVgYCKDYDILKLLLEHGVDVNAKSYILGlTALHSSIKS 279

                        250       260       270
                 ....*....|....*....|....*....|
gi 46519151  405 GhvEVARLLLDSGAQVNMPADSFESPLTLA 434
Cdd:PHA02878 280 E--RKLKLLLEYGADINSLNSYKLTPLSSA 307
PHA02798 PHA02798
ankyrin-like protein; Provisional
 274-491 4.94e-11

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 65.24  E-value: 4.94e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  274 LDIVKLLLLHDADVNSQSATGNTALTYACAGGFV---DIVKVLLNEGANIEDHNENGHTPLMEAASAGH---VEVARVLL 347
Cdd:PHA02798  89 LDIVKILIENGADINKKNSDGETPLYCLLSNGYInnlEILLFMIENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLL 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  348 DHGAGINTHSNEFKESalTLACY------KGHLDMVRFLLEAG-----ADQEHKTDemhtaLMEACMDghvevarLLLDS 416
Cdd:PHA02798 169 EKGVDINTHNNKEKYD--TLHCYfkynidRIDADILKLFVDNGfiinkENKSHKKK-----FMEYLNS-------LLYDN 234

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46519151  417 GaqvNMPADSFEspltlaacgghvelaalLIERGANLEEVNDEGYTPLMEAAREGHEEMVALLLAQGANINAQTE 491
Cdd:PHA02798 235 K---RFKKNILD-----------------FIFSYIDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITE 289
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 195-358 6.88e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 64.60  E-value: 6.88e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  195 TRSLAEACSDGDVNAVRKLLDEGRSVNEHTEEGESLLCLACSAGYYELAQVLL-------------------------AM 249
Cdd:PHA02874  36 TTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIdngvdtsilpipciekdmiktildcGI 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  250 HANVEDRGNKgdiTPLMAASSGGYLDIVKLLLLHDADVNSQSATGNTALTYACAGGFVDIVKVLLNEGANIEDHNENGHT 329
Cdd:PHA02874 116 DVNIKDAELK---TFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGES 192

                        170       180
                 ....*....|....*....|....*....
gi 46519151  330 PLMEAASAGHVEVARVLLDHGAGINTHSN 358
Cdd:PHA02874 193 PLHNAAEYGDYACIKLLIDHGNHIMNKCK 221
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 205-326 1.70e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 63.53  E-value: 1.70e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  205 GDVNAVRKLLDEGRSVNEHTEEGESLLCLACSAGYYEL--AQVLL--AMHANVEDR--------------GNKGDiTPLM 266
Cdd:PHA03100 119 NSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLkiLKLLIdkGVDINAKNRvnyllsygvpinikDVYGF-TPLH 197

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  267 AASSGGYLDIVKLLLLHDADVNSQSATGNTALTYACAGGFVDIVKVLLNEGANIEDHNEN 326
Cdd:PHA03100 198 YAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 392-583 2.74e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 62.67  E-value: 2.74e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  392 DEMHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIERGAnleevnDEGYTPLMEAareg 471
Cdd:PHA02874  33 DETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGV------DTSILPIPCI---- 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  472 HEEMVALLLAQGANINAQTEETQeTALTLACCGGFSEVADFLIKAGADIEL----GCsTPLMEASQEGHLELVKYLLASG 547
Cdd:PHA02874 103 EKDMIKTILDCGIDVNIKDAELK-TFLHYAIKKGDLESIKMLFEYGADVNIeddnGC-YPIHIAIKHNFFDIIKLLLEKG 180

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 46519151  548 ANVHATTATGDTALTYACENGHTDVADVLLQAGADL 583
Cdd:PHA02874 181 AYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHI 216
Ank_4 pfam13637
Ankyrin repeats (many copies);
524-577 2.93e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.74  E-value: 2.93e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 46519151   524 CSTPLMEASQEGHLELVKYLLASGANVHATTATGDTALTYACENGHTDVADVLL 577
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 193-334 8.51e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 61.13  E-value: 8.51e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  193 VDTRSLAEACSDGDVnaVRKLLDEGRSVNEHTEEGESLLCLACSAGYYELAQVLLAMHANVEDRGNKGDItPLMAASSGG 272
Cdd:PHA02874  92 VDTSILPIPCIEKDM--IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCY-PIHIAIKHN 168

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 46519151  273 YLDIVKLLLLHDADVNSQSATGNTALTYACAGGFVDIVKVLLNEGANIEDHNENGHTPLMEA 334
Cdd:PHA02874 169 FFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNA 230
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 273-578 4.40e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 58.98  E-value: 4.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  273 YLDIVKLLLLHDADVNSQSaTGNTALTYACAGGFV--DIVKVLLNEGANIedhNENGH--TPL------MEAASAGHVEV 342
Cdd:PHA02989  15 DKNALEFLLRTGFDVNEEY-RGNSILLLYLKRKDVkiKIVKLLIDNGADV---NYKGYieTPLcavlrnREITSNKIKKI 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  343 ARVLLDHGAGINTHSneFKESAlTLAC--YKGH---LDMVRFLLEAGADQEHKTDE-----MHTALmEACMDgHVEVARL 412
Cdd:PHA02989  91 VKLLLKFGADINLKT--FNGVS-PIVCfiYNSNinnCDMLRFLLSKGINVNDVKNSrgynlLHMYL-ESFSV-KKDVIKI 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  413 LLDSGAQVNMPADSFE-SPLTL----AACGGHVELAALLIERGANLEEvNDEGYTPLMEAAREGHEEMValllaqganin 487
Cdd:PHA02989 166 LLSFGVNLFEKTSLYGlTPMNIylrnDIDVISIKVIKYLIKKGVNIET-NNNGSESVLESFLDNNKILS----------- 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  488 aqteeTQETaltlaccggfsEVADFL---IKAGADIELGCsTPLMEASQEGHLELVKYLLASGANVHATTATGDTALTYA 564
Cdd:PHA02989 234 -----KKEF-----------KVLNFIlkyIKINKKDKKGF-NPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYA 296

                        330
                 ....*....|....
gi 46519151  565 CENGHTDVADVLLQ 578
Cdd:PHA02989 297 IKHGNIDMLNRILQ 310
Ank_4 pfam13637
Ankyrin repeats (many copies);
327-381 5.04e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.28  E-value: 5.04e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 46519151   327 GHTPLMEAASAGHVEVARVLLDHGAGINtHSNEFKESALTLACYKGHLDMVRFLL 381
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADIN-AVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
263-314 5.56e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.28  E-value: 5.56e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 46519151   263 TPLMAASSGGYLDIVKLLLLHDADVNSQSATGNTALTYACAGGFVDIVKVLL 314
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 438-588 1.51e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 57.28  E-value: 1.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  438 GHVELAALLIERGANLEEVN-DEGYTPLMEAAREGHEEMVALLLAQGANINAQTEETQETALTlACCGGFSEVADFLIKA 516
Cdd:PHA02874  12 GDIEAIEKIIKNKGNCINISvDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLT-AIKIGAHDIIKLLIDN 90

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 46519151  517 GADIELgCSTPLMEAsqeghlELVKYLLASGANVHATTATGDTALTYACENGHTDVADVLLQAGADLDKQED 588
Cdd:PHA02874  91 GVDTSI-LPIPCIEK------DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDD 155
Ank_4 pfam13637
Ankyrin repeats (many copies);
429-480 2.67e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.35  E-value: 2.67e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 46519151   429 SPLTLAACGGHVELAALLIERGANLEEVNDEGYTPLMEAAREGHEEMVALLL 480
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 182-367 5.94e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 56.03  E-value: 5.94e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  182 MKAENS--HNAGQVDTRSLAEAcSDGDVNAVRKLLDEGRSVNEHTEEGESLLCLACSAGYYELAQVLLAMHANVEDRGNK 259
Cdd:PLN03192 512 LLGDNGgeHDDPNMASNLLTVA-STGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDAN 590

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  260 GDiTPLMAASSGGYLDIVKlLLLHDADVNSQSATGNTaLTYACAGGFVDIVKVLLNEGANIEDHNENGHTPLMEAASAGH 339
Cdd:PLN03192 591 GN-TALWNAISAKHHKIFR-ILYHFASISDPHAAGDL-LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDH 667

                        170       180
                 ....*....|....*....|....*....
gi 46519151  340 VEVARVLLDHGAGInTHSNEFKE-SALTL 367
Cdd:PLN03192 668 VDMVRLLIMNGADV-DKANTDDDfSPTEL 695
Ank_4 pfam13637
Ankyrin repeats (many copies);
394-447 6.76e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.20  E-value: 6.76e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 46519151   394 MHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLI 447
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
294-347 1.25e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.42  E-value: 1.25e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 46519151   294 GNTALTYACAGGFVDIVKVLLNEGANIEDHNENGHTPLMEAASAGHVEVARVLL 347
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
363-414 3.87e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.27  E-value: 3.87e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 46519151   363 SALTLACYKGHLDMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEVARLLL 414
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
460-514 5.46e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.50  E-value: 5.46e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 46519151   460 GYTPLMEAAREGHEEMVALLLAQGANINAQTEEtQETALTLACCGGFSEVADFLI 514
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGN-GETALHFAASNGNVEVLKLLL 54
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 206-481 1.32e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 51.28  E-value: 1.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  206 DVNAVRKLLDEGRSVNEhTEEGESLLCLACSAGYY--ELAQVLLAMHANVEDRGNKGdiTPLMAA------SSGGYLDIV 277
Cdd:PHA02989  15 DKNALEFLLRTGFDVNE-EYRGNSILLLYLKRKDVkiKIVKLLIDNGADVNYKGYIE--TPLCAVlrnreiTSNKIKKIV 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  278 KLLLLHDADVNSQSATGNTALT---YACAGGFVDIVKVLLNEGANIED-HNENGHTPL---MEAASAgHVEVARVLLDHG 350
Cdd:PHA02989  92 KLLLKFGADINLKTFNGVSPIVcfiYNSNINNCDMLRFLLSKGINVNDvKNSRGYNLLhmyLESFSV-KKDVIKILLSFG 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  351 AGINTHSNEFKESALTLacYKGH------LDMVRFLLEAGADQEhKTDEMHTALMEACMDGH-------VEVARLLLdSG 417
Cdd:PHA02989 171 VNLFEKTSLYGLTPMNI--YLRNdidvisIKVIKYLIKKGVNIE-TNNNGSESVLESFLDNNkilskkeFKVLNFIL-KY 246

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 46519151  418 AQVNMPADSFESPLTLAACGGHVELAALLIERGANLEEVNDEGYTPLMEAAREGHEEMVALLLA 481
Cdd:PHA02989 247 IKINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHGNIDMLNRILQ 310
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 301-454 1.85e-06

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: 50.85  E-value: 1.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151   301 ACAGGFVDIVKVLLNEGA--NIEDHNENGHTPLMEAASAG-HVEVARVLLDHGAGINThsnefkESALTLACYKGHLDMV 377
Cdd:TIGR00870  24 AAERGDLASVYRDLEEPKklNINCPDRLGRSALFVAAIENeNLELTELLLNLSCRGAV------GDTLLHAISLEYVDAV 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151   378 ----RFLLEAGADQ-------EHKTDEM---HTALMEACMDGHVEVARLLLDSGAQVNMPA-----------DSF---ES 429
Cdd:TIGR00870  98 eailLHLLAAFRKSgplelanDQYTSEFtpgITALHLAAHRQNYEIVKLLLERGASVPARAcgdffvksqgvDSFyhgES 177

                         170       180
                  ....*....|....*....|....*
gi 46519151   430 PLTLAACGGHVELAALLIERGANLE 454
Cdd:TIGR00870 178 PLNAAACLGSPSIVALLSEDPADIL 202
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 211-449 2.32e-06

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: 50.85  E-value: 2.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151   211 RKLLDEGRSVNEHTEEGESLLCLACSAGYYELAQVLL----AMHANVEDRGNKGDItpLMAASSGGYLDIVKLLLLHDAD 286
Cdd:TIGR00870   1 RGPLDIVPAEESPLSDEEKAFLPAAERGDLASVYRDLeepkKLNINCPDRLGRSAL--FVAAIENENLELTELLLNLSCR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151   287 VnsqsATGNTALtYACAGGFVDIVKVLLN-------EGANIEDHNEN-------GHTPLMEAASAGHVEVARVLLDHGAG 352
Cdd:TIGR00870  79 G----AVGDTLL-HAISLEYVDAVEAILLhllaafrKSGPLELANDQytseftpGITALHLAAHRQNYEIVKLLLERGAS 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151   353 INT--HSNEFKESALT---------LACYK--GHLDMVRFLLEAGADQEhKTDEM-----HTALMEA------------C 402
Cdd:TIGR00870 154 VPAraCGDFFVKSQGVdsfyhgespLNAAAclGSPSIVALLSEDPADIL-TADSLgntllHLLVMENefkaeyeelscqM 232

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 46519151   403 MDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIER 449
Cdd:TIGR00870 233 YNFALSLLDKLRDSKELEVILNHQGLTPLKLAAKEGRIVLFRLKLAI 279
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 331-435 2.35e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.67  E-value: 2.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  331 LMEAASAGHVEVARVLLDHGAgiNTHSNEFKESA-LTLACYKGHLDMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEV 409
Cdd:PTZ00322  86 LCQLAASGDAVGARILLTGGA--DPNCRDYDGRTpLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREV 163

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 46519151  410 ARLLL-----DSGAQVNMPADSF--------ESPLTLAA 435
Cdd:PTZ00322 164 VQLLSrhsqcHFELGANAKPDSFtgkppsleDSPISSHH 202
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 277-360 2.84e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.28  E-value: 2.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  277 VKLLLLHDADVNSQSATGNTALTYACAGGFVDIVKVLLNEGANIEDHNENGHTPLMEAASAGHVEVARVLL-----DHGA 351
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSrhsqcHFEL 177


                 ....*....
gi 46519151  352 GINTHSNEF 360
Cdd:PTZ00322 178 GANAKPDSF 186
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 383-480 3.02e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.28  E-value: 3.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  383 AGADQEHKTDE------MHTALMEAC---MDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIERGANL 453
Cdd:PTZ00322  62 ATPDHNLTTEEvidpvvAHMLTVELCqlaASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADP 141

                         90       100
                 ....*....|....*....|....*..
gi 46519151  454 EEVNDEGYTPLMEAAREGHEEMVALLL 480
Cdd:PTZ00322 142 TLLDKDGKTPLELAEENGFREVVQLLS 168
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 377-446 5.95e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.51  E-value: 5.95e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  377 VRFLLEAGADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALL 446
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 198-353 6.63e-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: 49.24  E-value: 6.63e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151 198 LAEACSDGDVNAVRKLLdEGRSVNEHTE--EGESLLCLACSAGYYELAQVLLAmhaNVEDRGN--------KGDiTPLMA 267
Cdd:cd22192  21 LLLAAKENDVQAIKKLL-KCPSCDLFQRgaLGETALHVAALYDNLEAAVVLME---AAPELVNepmtsdlyQGE-TALHI 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151 268 ASSGGYLDIVKLLLLHDADVNSQSATGntalTYacaggFVDIVKVLLNEGanieDHnenghtPLMEAASAGHVEVARVLL 347
Cdd:cd22192  96 AVVNQNLNLVRELIARGADVVSPRATG----TF-----FRPGPKNLIYYG----EH------PLSFAACVGNEEIVRLLI 156


                ....*.
gi 46519151 348 DHGAGI 353
Cdd:cd22192 157 EHGADI 162
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 462-587 8.66e-06

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 48.86  E-value: 8.66e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151 462 TPLMEAAREGHEEMVALLLAQGANINAQTEETQETALTLACCGGFSEVADFLIKAG---------ADIELGcSTPLMEAS 532
Cdd:cd22192  19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAApelvnepmtSDLYQG-ETALHIAV 97

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 46519151 533 QEGHLELVKYLLASGANVHATTAT--------------GDTALTYACENGHTDVADVLLQAGADLDKQE 587
Cdd:cd22192  98 VNQNLNLVRELIARGADVVSPRATgtffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQD 166
Ank_5 pfam13857
Ankyrin repeats (many copies);
255-301 1.57e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.72  E-value: 1.57e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 46519151   255 DRGNKGDITPLMAASSGGYLDIVKLLLLHDADVNSQSATGNTALTYA 301
Cdd:pfam13857  10 NRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 459-491 1.71e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 41.89  E-value: 1.71e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 46519151   459 EGYTPLMEAA-REGHEEMVALLLAQGANINAQTE 491
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 459-488 2.68e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.42  E-value: 2.68e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 46519151    459 EGYTPLMEAAREGHEEMVALLLAQGANINA 488
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 326-354 2.90e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.03  E-value: 2.90e-05
                           10        20
                   ....*....|....*....|....*....
gi 46519151    326 NGHTPLMEAASAGHVEVARVLLDHGAGIN 354
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
PHA02798 PHA02798
ankyrin-like protein; Provisional
 307-567 2.92e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 46.75  E-value: 2.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  307 VDIVKVLLNEGANIEDHNENGHTPLMEAASaghvevarvlldhgaginthsnEFKEsaltlacYKGHLDMVRFLLEAGAD 386
Cdd:PHA02798  51 TDIVKLFINLGANVNGLDNEYSTPLCTILS----------------------NIKD-------YKHMLDIVKILIENGAD 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  387 QEHKTDEMHTALMEACMDGHV---EVARLLLDSGAQVNM-PADSFESPLTLAACGGHV--ELAALLIERGANLEEVND-E 459
Cdd:PHA02798 102 INKKNSDGETPLYCLLSNGYInnlEILLFMIENGADTTLlDKDGFTMLQVYLQSNHHIdiEIIKLLLEKGVDINTHNNkE 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  460 GYTPLMEAAREGHE----EMVALLLAQGANINAQTEETQETALT-----LACCGGF-SEVADFLIKAgADI----ELGCs 525
Cdd:PHA02798 182 KYDTLHCYFKYNIDridaDILKLFVDNGFIINKENKSHKKKFMEylnslLYDNKRFkKNILDFIFSY-IDInqvdELGF- 259

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 46519151  526 TPLMEASQEGHLELVKYLLASGANVHATTATGDTALTYACEN 567
Cdd:PHA02798 260 NPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFEN 301
Ank_5 pfam13857
Ankyrin repeats (many copies);
346-398 3.94e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.56  E-value: 3.94e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 46519151   346 LLDHGAGINTHSNEFKESALTLACYKGHLDMVRFLLEAGADQEHKTDEMHTAL 398
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 195-294 4.05e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.82  E-value: 4.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  195 TRSLAEACSDGDVNAVRKLLDEGRSVNEHTEEGESLLCLACSAGYYELAQVLLAMHANVE--DRGNKgdiTPLMAASSGG 272
Cdd:PTZ00322  83 TVELCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTllDKDGK---TPLELAEENG 159

                         90       100
                 ....*....|....*....|..
gi 46519151  273 YLDIVKLLLLHDADVNSQSATG 294
Cdd:PTZ00322 160 FREVVQLLSRHSQCHFELGANA 181
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 308-480 4.20e-05

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 46.68  E-value: 4.20e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151 308 DIVKVLLNegANIEDHNENGHTPLMEAASAGHVEVARVLLDHGAGIN----------THSNE---FKESALTLACYKGHL 374
Cdd:cd22194 124 GILDRFIN--AEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNahakgvffnpKYKHEgfyFGETPLALAACTNQP 201

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151 375 DMVRFLLEAGADQEHKTDEMHTALMEACmdghVEVARlllDSGAQVNMPADSFESPLTlaACGGHvelaalliergaNLE 454
Cdd:cd22194 202 EIVQLLMEKESTDITSQDSRGNTVLHAL----VTVAE---DSKTQNDFVKRMYDMILL--KSENK------------NLE 260

                       170       180
                ....*....|....*....|....*..
gi 46519151 455 EV-NDEGYTPLMEAAREGHEEMVALLL 480
Cdd:cd22194 261 TIrNNEGLTPLQLAAKMGKAEILKYIL 287
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 306-403 6.43e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 45.36  E-value: 6.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  306 FVDIVKVLLNEGANIE---DHNENGHT-PLMEAASAGHVEVARVLLDHGAGINTHSNEFKESALTLACYKGHLDMVRFLL 381
Cdd:PHA02884  45 YTDIIDAILKLGADPEapfPLSENSKTnPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKITPLYISVLHGCLKCLEILL 124

                         90       100
                 ....*....|....*....|..
gi 46519151  382 EAGADQEHKTDEMHTALMEACM 403
Cdd:PHA02884 125 SYGADINIQTNDMVTPIELALM 146
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 210-331 6.74e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 45.72  E-value: 6.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  210 VRKLLDEGRSVNEHTEEGESLLCLACSAGYYELAQVLLAMHANVEDRGNKGdITPLMAASSggYLDIVKLLLLHDADVNS 289
Cdd:PHA02874 173 IKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNG-FTPLHNAII--HNRSAIELLINNASIND 249

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 46519151  290 QSATGNTALTYA----CAggfVDIVKVLLNEGANIEDHNENGHTPL 331
Cdd:PHA02874 250 QDIDGSTPLHHAinppCD---IDIIDILLYHKADISIKDNKGENPI 292
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 509-587 8.98e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.44  E-value: 8.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  509 VADFLIKAGADI---ELGCSTPLMEASQEGHLELVKYLLASGANVHATTATGDTALTYACENGHTDVADVLLQAGADLDK 585
Cdd:PHA02876 160 IAEMLLEGGADVnakDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINK 239


                 ..
gi 46519151  586 QE 587
Cdd:PHA02876 240 ND 241
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 459-488 1.07e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 39.55  E-value: 1.07e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 46519151   459 EGYTPLMEAAREGHEEMVALLLAQGANINA 488
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 274-388 1.29e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 43.65  E-value: 1.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  274 LDIVKLLLLHDADVNSQSATGNTAL--TYACAGGFV--DIVKVLLNEGANIEDHNENGHTPL---MEAASAgHVEVARVL 346
Cdd:PHA02859  66 VEILKFLIENGADVNFKTRDNNLSAlhHYLSFNKNVepEILKILIDSGSSITEEDEDGKNLLhmyMCNFNV-RINVIKLL 144

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 46519151  347 LDHGAGINTHSNEFKESALTLACYKGHLDMVRFLLEAGADQE 388
Cdd:PHA02859 145 IDSGVSFLNKDFDNNNILYSYILFHSDKKIFDFLTSLGIDIN 186
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 195-288 1.60e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 44.60  E-value: 1.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  195 TRSLAEACSDGDVNAVRKLLDEGRSVNEHTEEGESLLCLACSAGYYELAQVLLAMHANVEDRGNKGDITPLMAASSGGYL 274
Cdd:PHA02875 136 FSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKI 215

                         90
                 ....*....|....
gi 46519151  275 DIVKLLLLHDADVN 288
Cdd:PHA02875 216 DIVRLFIKRGADCN 229
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 325-544 1.60e-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: 44.75  E-value: 1.60e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151 325 ENGHTPLMEAasaghvevarvLLDhgagINTHSNEFKESALTLACYKGHLDmvRFLleaGADQEHKTDEMHTALMEACMD 404
Cdd:cd22194  92 DTGKTCLMKA-----------LLN----INENTKEIVRILLAFAEENGILD--RFI---NAEYTEEAYEGQTALNIAIER 151

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151 405 GHVEVARLLLDSGAQVNMPA-----------DSF---ESPLTLAACGGHVELAALLIERGANLEEVNDE-GYTPLmeaar 469
Cdd:cd22194 152 RQGDIVKLLIAKGADVNAHAkgvffnpkykhEGFyfgETPLALAACTNQPEIVQLLMEKESTDITSQDSrGNTVL----- 226

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151 470 egHeemvALLLAqganinAQTEETQETALTlaccggfsEVADFLIKAGADIELGCS------TPLMEASQEGHLELVKYL 543
Cdd:cd22194 227 --H----ALVTV------AEDSKTQNDFVK--------RMYDMILLKSENKNLETIrnneglTPLQLAAKMGKAEILKYI 286


                .
gi 46519151 544 L 544
Cdd:cd22194 287 L 287
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 557-585 1.63e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.11  E-value: 1.63e-04
                           10        20
                   ....*....|....*....|....*....
gi 46519151    557 GDTALTYACENGHTDVADVLLQAGADLDK 585
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 294-322 2.19e-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: 2.19e-04
                           10        20
                   ....*....|....*....|....*....
gi 46519151    294 GNTALTYACAGGFVDIVKVLLNEGANIED 322
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 326-355 2.24e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 38.78  E-value: 2.24e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 46519151   326 NGHTPLMEAASAGHVEVARVLLDHGAGINT 355
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 326-354 3.49e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.04  E-value: 3.49e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 46519151   326 NGHTPLMEAA-SAGHVEVARVLLDHGAGIN 354
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVN 30
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 282-480 3.89e-04

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 43.33  E-value: 3.89e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151 282 LHDADVNSQSATGNTALTYACAGGFVDIVKVLLNEGANIEDHNenGHTPLMEAASAGHVEVARVLLDHGAGINTHSN--- 358
Cdd:cd21882  30 LHKAALNLNDGVNEAIMLLLEAAPDSGNPKELVNAPCTDEFYQ--GQTALHIAIENRNLNLVRLLVENGADVSARATgrf 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151 359 ---------EFKESALTLACYKGHLDMVRFLLEAGAD--QEHKTDEMHTALMEACmdghVEVARLLLDSGAQVnmpADSF 427
Cdd:cd21882 108 frkspgnlfYFGELPLSLAACTNQEEIVRLLLENGAQpaALEAQDSLGNTVLHAL----VLQADNTPENSAFV---CQMY 180

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 46519151 428 ESPLTLAACGGHVElaalliergaNLEEV-NDEGYTPLMEAAREGHEEMVALLL 480
Cdd:cd21882 181 NLLLSYGAHLDPTQ----------QLEEIpNHQGLTPLKLAAVEGKIVMFQHIL 224
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 396-586 4.13e-04

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 43.46  E-value: 4.13e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151 396 TALMEACMDGHVE-VARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIE---RGANLEEVND--EGYTPLMEAAR 469
Cdd:cd22192  19 SPLLLAAKENDVQaIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEaapELVNEPMTSDlyQGETALHIAVV 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151 470 EGHEEMVALLLAQGANInaqteetqetaLTLACCGGFsevadFLIKAGADIELGcSTPLMEASQEGHLELVKYLLASGAN 549
Cdd:cd22192  99 NQNLNLVRELIARGADV-----------VSPRATGTF-----FRPGPKNLIYYG-EHPLSFAACVGNEEIVRLLIEHGAD 161

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 46519151 550 VHATTATGDTAL---------TYACEnghtdVADVLLQAGADLDKQ 586
Cdd:cd22192 162 IRAQDSLGNTVLhilvlqpnkTFACQ-----MYDLILSYDKEDDLQ 202
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 467-577 4.15e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 43.35  E-value: 4.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  467 AAREGHEEMVAlllaqGANINAQTEETQETA----LTLACC----GGFSEVADFLIKAGAD---IELGCSTPLMEASQEG 535
Cdd:PTZ00322  52 EALEATENKDA-----TPDHNLTTEEVIDPVvahmLTVELCqlaaSGDAVGARILLTGGADpncRDYDGRTPLHIACANG 126

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 46519151  536 HLELVKYLLASGANVHATTATGDTALTYACENGHTDVADVLL 577
Cdd:PTZ00322 127 HVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
Ank_5 pfam13857
Ankyrin repeats (many copies);
279-331 5.04e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.48  E-value: 5.04e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 46519151   279 LLLLHDADVNSQSATGNTALTYACAGGFVDIVKVLLNEGANIEDHNENGHTPL 331
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
Ank_5 pfam13857
Ankyrin repeats (many copies);
446-501 5.40e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.48  E-value: 5.40e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 46519151   446 LIERG-ANLEEVNDEGYTPLMEAAREGHEEMVALLLAQGANINAQTEETqETALTLA 501
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEG-LTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
229-281 5.96e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.02  E-value: 5.96e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 46519151   229 SLLCLACSAGYYELAQVLLAMHANVEDRgNKGDITPLMAASSGGYLDIVKLLL 281
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAV-DGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
519-564 1.02e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.33  E-value: 1.02e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 46519151   519 DIELGCSTPLMEASQEGHLELVKYLLASGANVHATTATGDTALTYA 564
Cdd:pfam13857  11 RLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 526-552 1.06e-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: 36.80  E-value: 1.06e-03
                           10        20
                   ....*....|....*....|....*..
gi 46519151    526 TPLMEASQEGHLELVKYLLASGANVHA 552
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 525-583 1.28e-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: 41.92  E-value: 1.28e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151 525 STPLMEASQEGHLELVKYLLAS-GANVHATTATGDTALTYACENGHTDVADVLLQAGADL 583
Cdd:cd22192  18 ESPLLLAAKENDVQAIKKLLKCpSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPEL 77
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 395-422 1.34e-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: 36.41  E-value: 1.34e-03
                           10        20
                   ....*....|....*....|....*...
gi 46519151    395 HTALMEACMDGHVEVARLLLDSGAQVNM 422
Cdd:smart00248   3 RTPLHLAAENGNLEVVKLLLDKGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 433-539 1.39e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.81  E-value: 1.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  433 LAACGGHVElAALLIERGANLEEVNDEGYTPLMEAAREGHEEMVALLLAQGANINAqTEETQETALTLACCGGFSEVADF 512
Cdd:PTZ00322  89 LAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTL-LDKDGKTPLELAEENGFREVVQL 166

                         90       100
                 ....*....|....*....|....*....
gi 46519151  513 LIK-AGADIELG-CSTPLMEASQEGHLEL 539
Cdd:PTZ00322 167 LSRhSQCHFELGaNAKPDSFTGKPPSLED 195
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 231-324 1.40e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.81  E-value: 1.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  231 LCLACSAGYYELAQVLLAMHANVEDRGNKGDiTPLMAASSGGYLDIVKLLLLHDADVNSQSATGNTALTYACAGGFVDIV 310
Cdd:PTZ00322  86 LCQLAASGDAVGARILLTGGADPNCRDYDGR-TPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVV 164

                         90
                 ....*....|....
gi 46519151  311 KVLLneGANIEDHN 324
Cdd:PTZ00322 165 QLLS--RHSQCHFE 176
Ank_5 pfam13857
Ankyrin repeats (many copies);
313-368 1.42e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.94  E-value: 1.42e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 46519151   313 LLNEGANIEDHNENGHTPLMEAASAGHVEVARVLLDHGAGINThSNEFKESALTLA 368
Cdd:pfam13857   2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNL-KDEEGLTALDLA 56
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 358-487 1.71e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 40.19  E-value: 1.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  358 NEFKESALtLACY---KGHLDMVRFLLEAGADQEHKTDEMHTALMEACM----DGHVEVARLLLDSGAQVNMPADSFESP 430
Cdd:PHA02859  48 NDLYETPI-FSCLekdKVNVEILKFLIENGADVNFKTRDNNLSALHHYLsfnkNVEPEILKILIDSGSSITEEDEDGKNL 126

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 46519151  431 L--TLAACGGHVELAALLIERGANLEEVNDEG----YTPLMeaaREGHEEMVALLLAQGANIN 487
Cdd:PHA02859 127 LhmYMCNFNVRINVIKLLIDSGVSFLNKDFDNnnilYSYIL---FHSDKKIFDFLTSLGIDIN 186
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 540-594 1.73e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.42  E-value: 1.73e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 46519151  540 VKYLLASGANVHATTATGDTALTYACENGHTDVADVLLQAGAD---LDKqeDMKTILE 594
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADptlLDK--DGKTPLE 153
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 526-554 1.75e-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: 36.11  E-value: 1.75e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 46519151   526 TPLMEAS-QEGHLELVKYLLASGANVHATT 554
Cdd:pfam00023   4 TPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 263-290 1.97e-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: 36.11  E-value: 1.97e-03
                          10        20
                  ....*....|....*....|....*....
gi 46519151   263 TPLM-AASSGGYLDIVKLLLLHDADVNSQ 290
Cdd:pfam00023   4 TPLHlAAGRRGNLEIVKLLLSKGADVNAR 32
PHA02795 PHA02795
ankyrin-like protein; Provisional
 274-344 2.38e-03

ankyrin-like protein; Provisional


Pssm-ID: 165157 [Multi-domain]  Cd Length: 437  Bit Score: 40.75  E-value: 2.38e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 46519151  274 LDIVKLLLLHDADVNSQSATGNTALTYACAGGFVDIVKVLLNEGANIEDHNENGHTPLMEAASAGHVEVAR 344
Cdd:PHA02795 201 LEIYKLCIPYIEDINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDVAVDRGSVIARR 271
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 557-585 2.49e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 35.70  E-value: 2.49e-03
                          10        20
                  ....*....|....*....|....*....
gi 46519151   557 GDTALTYACENGHTDVADVLLQAGADLDK 585
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 330-584 2.93e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 40.63  E-value: 2.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  330 PLMEAASAGHVEVARVLLDHGAGINTHSNEFKeSALTLACYKGHLDMVRFLLEAgaDQEHKTDEMHTALMEACMDGHVEV 409
Cdd:PHA02878  40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDL-TPLHIICKEPNKLGMKEMIRS--INKCSVFYTLVAIKDAFNNRNVEI 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  410 ARLLLdsgaqvnmpADSFESpltlaacgghvelaalliERGANLEEVNDEGYTPLMEAaregheEMVALLLAQGANINAQ 489
Cdd:PHA02878 117 FKIIL---------TNRYKN------------------IQTIDLVYIDKKSKDDIIEA------EITKLLLSYGADINMK 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151  490 TEETQetaltlaccggfsevadflikagadielgcSTPLMEASQEGHLELVKYLLASGANVHATTATGDTALTYACENGH 569
Cdd:PHA02878 164 DRHKG------------------------------NTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYN 213

                        250
                 ....*....|....*
gi 46519151  570 TDVADVLLQAGADLD 584
Cdd:PHA02878 214 KPIVHILLENGASTD 228
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 363-386 4.75e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.87  E-value: 4.75e-03
                           10        20
                   ....*....|....*....|....
gi 46519151    363 SALTLACYKGHLDMVRFLLEAGAD 386
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGAD 27
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 263-288 4.89e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.87  E-value: 4.89e-03
                           10        20
                   ....*....|....*....|....*.
gi 46519151    263 TPLMAASSGGYLDIVKLLLLHDADVN 288
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADIN 29
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 263-347 5.01e-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: 39.78  E-value: 5.01e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46519151 263 TPLMAASSGGYLDIVKLLLLH---DADVNSQSATGNTAL--TYACAGGFVDIVKV-------LLNEGANI-------EDH 323
Cdd:cd22193 125 LPLSLAACTNQPDIVQYLLENehqPADIEAQDSRGNTVLhaLVTVADNTKENTKFvtrmydmILIRGAKLcptveleEIR 204

                        90       100
                ....*....|....*....|....
gi 46519151 324 NENGHTPLMEAASAGHVEVARVLL 347
Cdd:cd22193 205 NNDGLTPLQLAAKMGKIEILKYIL 228
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 557-586 7.15e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 34.57  E-value: 7.15e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 46519151   557 GDTALTYACE-NGHTDVADVLLQAGADLDKQ 586
Cdd:pfam00023   2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNAR 32
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 396-422 7.63e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 34.16  E-value: 7.63e-03
                          10        20
                  ....*....|....*....|....*..
gi 46519151   396 TALMEACMDGHVEVARLLLDSGAQVNM 422
Cdd:pfam13606   4 TPLHLAARNGRLEIVKLLLENGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 294-320 9.38e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 34.16  E-value: 9.38e-03
                          10        20
                  ....*....|....*....|....*..
gi 46519151   294 GNTALTYACAGGFVDIVKVLLNEGANI 320
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADI 28
 
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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