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Conserved domains on  [gi|1039795032|ref|XP_017169203|]
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ankyrin repeat and death domain-containing protein 1A isoform X3 [Mus musculus]

Protein Classification

ankyrin repeat domain-containing protein( domain architecture ID 12356329)

ankyrin repeat (ANK) domain-containing protein mediate specific protein-protein interactions without necessarily recognizing specific primary sequences which allows for one ankyrin repeat domain to recognize and bind to a variety of intracellular substrates and may be involved in a wide array of functions

CATH:  1.25.40.20
Gene Ontology:  GO:0005515
PubMed:  33435370|15152081|17176038
SCOP:  4000366

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
113-369 7.37e-41

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 148.56  E-value: 7.37e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 113 DGLTLLHCAAQKGHVPVLAFVMEDLEDVALDHADKLGRTAFHRAAEHGQLDALDFLVGSGCDHSVKDKGGNTALHLAASQ 192
Cdd:COG0666    18 LLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARN 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 193 GHVDVLQRLVDIGLDLEEQNTEGLTALHAAAEGIHADCVMLLLGAGSNVNALTQKRLSCLHYAALGGSEDLSRALIKAGG 272
Cdd:COG0666    98 GDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGA 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 273 CTNVADKQGTTPMHLAVKHNFPGLVQLLIDGHSDLDAVDIRRQTPLHLAAEHAWQDVADMLLIAGADLSLRDKQGKTALA 352
Cdd:COG0666   178 DVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALL 257

                         250
                  ....*....|....*..
gi 1039795032 353 VAARSNHVSLVDMIIKA 369
Cdd:COG0666   258 LAAAAGAALIVKLLLLA 274
Ank_2 pfam12796
Ankyrin repeats (3 copies);
19-108 4.77e-14

Ankyrin repeats (3 copies);


:

Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.45  E-value: 4.77e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032  19 LHEASRWNQVERMKELFEKRVNIRARNHVGRVALHWAAGAGHEQAVRLLLERGAAvdDVDSFGMNSLLLSAWFGHLQIVQ 98
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|
gi 1039795032  99 ILVNAGAKVH 108
Cdd:pfam12796  79 LLLEKGADIN 88
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
113-369 7.37e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 148.56  E-value: 7.37e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 113 DGLTLLHCAAQKGHVPVLAFVMEDLEDVALDHADKLGRTAFHRAAEHGQLDALDFLVGSGCDHSVKDKGGNTALHLAASQ 192
Cdd:COG0666    18 LLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARN 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 193 GHVDVLQRLVDIGLDLEEQNTEGLTALHAAAEGIHADCVMLLLGAGSNVNALTQKRLSCLHYAALGGSEDLSRALIKAGG 272
Cdd:COG0666    98 GDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGA 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 273 CTNVADKQGTTPMHLAVKHNFPGLVQLLIDGHSDLDAVDIRRQTPLHLAAEHAWQDVADMLLIAGADLSLRDKQGKTALA 352
Cdd:COG0666   178 DVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALL 257

                         250
                  ....*....|....*..
gi 1039795032 353 VAARSNHVSLVDMIIKA 369
Cdd:COG0666   258 LAAAAGAALIVKLLLLA 274
PHA03095 PHA03095
ankyrin-like protein; Provisional
 96-368 2.91e-29

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 120.13  E-value: 2.91e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032  96 IVQILVNAGAKVHCESKDGLTLLHCAAQKGHVPVLAFVMEDLEDVA-LDHADKLGRTAFHRAAEHGQ-LDALDFLVGSGC 173
Cdd:PHA03095   29 EVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIVRLLLEAGAdVNAPERCGFTPLHLYLYNATtLDVIKLLIKAGA 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 174 DHSVKDKGGNTALH--LAASQGHVDVLQRLVDIGLDLEEQNTEGLTALHAAAE--GIHADCVMLLLGAGSNVNALTQKRL 249
Cdd:PHA03095  109 DVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKsrNANVELLRLLIDAGADVYAVDDRFR 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 250 SCLHYAALG--GSEDLSRALIKAGGCTNVADKQGTTPMHLAVKHNF--PGLVQLLIDGHSDLDAVDIRRQTPLHLAAEHA 325
Cdd:PHA03095  189 SLLHHHLQSfkPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSckRSLVLPLLIAGISINARNRYGQTPLHYAAVFN 268

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1039795032 326 WQDVADMLLIAGADLSLRDKQGKTALAVAARSNHVSLVDMIIK 368
Cdd:PHA03095  269 NPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALA 311
Ank_2 pfam12796
Ankyrin repeats (3 copies);
153-243 2.04e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.08  E-value: 2.04e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 153 FHRAAEHGQLDALDFLVGSGCDHSVKDKGGNTALHLAASQGHVDVLQRLVDiGLDLEEQNtEGLTALHAAAEGIHADCVM 232
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|.
gi 1039795032 233 LLLGAGSNVNA 243
Cdd:pfam12796  79 LLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
19-108 4.77e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.45  E-value: 4.77e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032  19 LHEASRWNQVERMKELFEKRVNIRARNHVGRVALHWAAGAGHEQAVRLLLERGAAvdDVDSFGMNSLLLSAWFGHLQIVQ 98
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|
gi 1039795032  99 ILVNAGAKVH 108
Cdd:pfam12796  79 LLLEKGADIN 88
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 19-189 1.14e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 60.36  E-value: 1.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032  19 LHEASRWNQVERMKELFEKRVNIRARNHVGRVALHWAAGAGHEQAVRLLLERGAAVDDVDSFGMNSLLLSAWFGHLQIVQ 98
Cdd:PHA02874  128 LHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIK 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032  99 ILVNAGAKVHCESKDGLTLLHCAA--QKGHVPVLafvmedLEDVALDHADKLGRTAFHRAAEHG-QLDALDFLVGSGCDH 175
Cdd:PHA02874  208 LLIDHGNHIMNKCKNGFTPLHNAIihNRSAIELL------INNASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADI 281

                         170
                  ....*....|....
gi 1039795032 176 SVKDKGGNTALHLA 189
Cdd:PHA02874  282 SIKDNKGENPIDTA 295
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 183-382 2.16e-08

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 56.56  E-value: 2.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 183 NTALHLAASQGHVDVLQRLVDI-GLDLEEQNTEGLTALHAAAEGIHADCVMLLL-GAGSNVN-ALTQ---KRLSCLHYAA 256
Cdd:cd22192    18 ESPLLLAAKENDVQAIKKLLKCpSCDLFQRGALGETALHVAALYDNLEAAVVLMeAAPELVNePMTSdlyQGETALHIAV 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 257 LGGSEDLSRALIKAGGCTNVADKQGTT--------------PMHLAVKHNFPGLVQLLIDGHSDLDAVDIRRQTPLHLAA 322
Cdd:cd22192    98 VNQNLNLVRELIARGADVVSPRATGTFfrpgpknliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILV 177

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 323 EHAWQDVA----DMLLIAGADLS------LRDKQGKTALAVAARSNHVSLVDMIIKADRFYRWEKDHLSC 382
Cdd:cd22192   178 LQPNKTFAcqmyDLILSYDKEDDlqpldlVPNNQGLTPFKLAAKEGNIVMFQHLVQKRRHIQWTYGPLTS 247
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 121-289 1.98e-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: 50.46  E-value: 1.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 121 AAQKGHVPVLAFVMEDLEDVALDHADKLGRTA-FHRAAEHGQLDALDFLVGSGCDHSVkdkgGNTALHlAASQGHVDVLQ 199
Cdd:TIGR00870  24 AAERGDLASVYRDLEEPKKLNINCPDRLGRSAlFVAAIENENLELTELLLNLSCRGAV----GDTLLH-AISLEYVDAVE 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 200 RLVDI-------GLDLEEQN-------TEGLTALHAAAEGIHADCVMLLLGAGSNVNA-------LTQKRLSCLHY---- 254
Cdd:TIGR00870  99 AILLHllaafrkSGPLELANdqytsefTPGITALHLAAHRQNYEIVKLLLERGASVPAracgdffVKSQGVDSFYHgesp 178

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1039795032 255 ---AALGGSEDLSRALIKAGGCTNVADKQGTTPMHLAV 289
Cdd:TIGR00870 179 lnaAACLGSPSIVALLSEDPADILTADSLGNTLLHLLV 216
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 19-169 6.25e-05

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 45.39  E-value: 6.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032  19 LHEASRWNQVERMKELFE-KRVNIRARNHVGRVALHWAAGAGHEQA---------------------------------- 63
Cdd:cd22192    21 LLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAavvlmeaapelvnepmtsdlyqgetalhiavvnq 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032  64 ----VRLLLERGAavdDVDS-----------------FGMNSLLLSAWFGHLQIVQILVNAGAKVHCESKDGLTLLH-CA 121
Cdd:cd22192   101 nlnlVRELIARGA---DVVSpratgtffrpgpknliyYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHiLV 177

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039795032 122 AQKGHVPV-------LAFVMEDlEDVALDH-ADKLGRTAFHRAAEHGQLDALDFLV 169
Cdd:cd22192   178 LQPNKTFAcqmydliLSYDKED-DLQPLDLvPNNQGLTPFKLAAKEGNIVMFQHLV 232
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 182-210 8.04e-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: 36.80  E-value: 8.04e-04
                           10        20
                   ....*....|....*....|....*....
gi 1039795032  182 GNTALHLAASQGHVDVLQRLVDIGLDLEE 210
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
113-369 7.37e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 148.56  E-value: 7.37e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 113 DGLTLLHCAAQKGHVPVLAFVMEDLEDVALDHADKLGRTAFHRAAEHGQLDALDFLVGSGCDHSVKDKGGNTALHLAASQ 192
Cdd:COG0666    18 LLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARN 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 193 GHVDVLQRLVDIGLDLEEQNTEGLTALHAAAEGIHADCVMLLLGAGSNVNALTQKRLSCLHYAALGGSEDLSRALIKAGG 272
Cdd:COG0666    98 GDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGA 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 273 CTNVADKQGTTPMHLAVKHNFPGLVQLLIDGHSDLDAVDIRRQTPLHLAAEHAWQDVADMLLIAGADLSLRDKQGKTALA 352
Cdd:COG0666   178 DVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALL 257

                         250
                  ....*....|....*..
gi 1039795032 353 VAARSNHVSLVDMIIKA 369
Cdd:COG0666   258 LAAAAGAALIVKLLLLA 274
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
64-351 6.53e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 140.47  E-value: 6.53e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032  64 VRLLLERGAAVDDVDSFGMNSLLLSAWFGHLQIVQILVNAGAKVHCESKDGLTLLHCAAQKGHVPVLAFVMEDLEDVALD 143
Cdd:COG0666     4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 144 haDKLGRTAFHRAAEHGQLDALDFLVGSGCDHSVKDKGGNTALHLAASQGHVDVLQRLVDIGLDLEEQNTEGLTALHAAA 223
Cdd:COG0666    84 --DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 224 EGIHADCVMLLLGAGSNVNALTQKRLSCLHYAALGGSEDLSRALIKAGGCTNVADKQGTTPMHLAVKHNFPGLVQLLIDG 303
Cdd:COG0666   162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1039795032 304 HSDLDAVDIRRQTPLHLAAEHAWQDVADMLLIAGADLSLRDKQGKTAL 351
Cdd:COG0666   242 GADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
19-249 1.83e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 139.32  E-value: 1.83e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032  19 LHEASRWNQVERMKELFEKRVNIRARNHVGRVALHWAAGAGHEQAVRLLLERGAAVDDVDSFGMNSLLLSAWFGHLQIVQ 98
Cdd:COG0666    58 LLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVK 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032  99 ILVNAGAKVHCESKDGLTLLHCAAQKGHVPVLAFVMEDLEDValDHADKLGRTAFHRAAEHGQLDALDFLVGSGCDHSVK 178
Cdd:COG0666   138 LLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADV--NARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAK 215

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039795032 179 DKGGNTALHLAASQGHVDVLQRLVDIGLDLEEQNTEGLTALHAAAEGIHADCVMLLLGAGSNVNALTQKRL 249
Cdd:COG0666   216 DNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLL 286
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-285 4.82e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 138.16  E-value: 4.82e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032   1 MEEELAWETHGLLPLERQLHEASRWNQVERMKELFEKRVNIRARNHVGRVALHWAAGAGHEQAVRLLLERGAAVDDVDSF 80
Cdd:COG0666     7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032  81 GMNSLLLSAWFGHLQIVQILVNAGAKVHCESKDGLTLLHCAAQKGHVPVLAFVMEDLEDValDHADKLGRTAFHRAAEHG 160
Cdd:COG0666    87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADV--NAQDNDGNTPLHLAAANG 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 161 QLDALDFLVGSGCDHSVKDKGGNTALHLAASQGHVDVLQRLVDIGLDLEEQNTEGLTALHAAAEGIHADCVMLLLGAGSN 240
Cdd:COG0666   165 NLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD 244

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1039795032 241 VNALTQKRLSCLHYAALGGSEDLSRALIKAGGCTNVADKQGTTPM 285
Cdd:COG0666   245 LNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
33-318 1.76e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 136.62  E-value: 1.76e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032  33 ELFEKRVNIRARNHVGRVALHWAAGAGHEQAVRLLLERGAAVDDVDSFGMNSLLLSAWFGHLQIVQILVNAGAKVHCESK 112
Cdd:COG0666     6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 113 DGLTLLHCAAQKGHVPVLAFVMEDLEDValDHADKLGRTAFHRAAEHGQLDALDFLVGSGCDHSVKDKGGNTALHLAASQ 192
Cdd:COG0666    86 GGNTLLHAAARNGDLEIVKLLLEAGADV--NARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 193 GHVDVLQRLVDIGLDLEEQNTEGLTALHAAAEGIHADCVMLLLGAGSNVNALTQKRLSCLHYAALGGSEDLSRALIKAGG 272
Cdd:COG0666   164 GNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1039795032 273 CTNVADKQGTTPMHLAVKHNFPGLVQLLIDGHSDLDAVDIRRQTPL 318
Cdd:COG0666   244 DLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
135-369 2.46e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 136.24  E-value: 2.46e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 135 EDLEDVALDHADKLGRTAFHRAAEHGQLDALDFLVGSGCDHSVKDKGGNTALHLAASQGHVDVLQRLVDIGLDLEEQNTE 214
Cdd:COG0666     7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 215 GLTALHAAAEGIHADCVMLLLGAGSNVNALTQKRLSCLHYAALGGSEDLSRALIKAGGCTNVADKQGTTPMHLAVKHNFP 294
Cdd:COG0666    87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039795032 295 GLVQLLIDGHSDLDAVDIRRQTPLHLAAEHAWQDVADMLLIAGADLSLRDKQGKTALAVAARSNHVSLVDMIIKA 369
Cdd:COG0666   167 EIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241
PHA03095 PHA03095
ankyrin-like protein; Provisional
 96-368 2.91e-29

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 120.13  E-value: 2.91e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032  96 IVQILVNAGAKVHCESKDGLTLLHCAAQKGHVPVLAFVMEDLEDVA-LDHADKLGRTAFHRAAEHGQ-LDALDFLVGSGC 173
Cdd:PHA03095   29 EVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIVRLLLEAGAdVNAPERCGFTPLHLYLYNATtLDVIKLLIKAGA 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 174 DHSVKDKGGNTALH--LAASQGHVDVLQRLVDIGLDLEEQNTEGLTALHAAAE--GIHADCVMLLLGAGSNVNALTQKRL 249
Cdd:PHA03095  109 DVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKsrNANVELLRLLIDAGADVYAVDDRFR 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 250 SCLHYAALG--GSEDLSRALIKAGGCTNVADKQGTTPMHLAVKHNF--PGLVQLLIDGHSDLDAVDIRRQTPLHLAAEHA 325
Cdd:PHA03095  189 SLLHHHLQSfkPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSckRSLVLPLLIAGISINARNRYGQTPLHYAAVFN 268

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1039795032 326 WQDVADMLLIAGADLSLRDKQGKTALAVAARSNHVSLVDMIIK 368
Cdd:PHA03095  269 NPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALA 311
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 66-346 3.30e-23

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 103.22  E-value: 3.30e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032  66 LLLERGAAVDDVDSFGMNSLLLSAWFGHLQIVQILVNAGAKVHCESKDGLTLLHCAAQKGHVPVLAFVM----------- 134
Cdd:PHA02876  163 MLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIdnrsninkndl 242

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 135 --------EDLEDVAL--------DHADKLGRTAFHRAAEHGQLDAL-DFLVGSGCDHSVKDKGGNTALHLAASQGH-VD 196
Cdd:PHA02876  243 sllkairnEDLETSLLlydagfsvNSIDDCKNTPLHHASQAPSLSRLvPKLLERGADVNAKNIKGETPLYLMAKNGYdTE 322

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 197 VLQRLVDIGLDLEEQNTEGLTALHAAAE-GIHADCVMLLLGAGSNVNA-------------------------------- 243
Cdd:PHA02876  323 NIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNArdycdktpihyaavrnnvviintlldygadie 402

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 244 -LTQKRLSCLHYAALGGSEDLS-RALIKAGGCTNVADKQGTTPMHLAVKHNF-PGLVQLLIDGHSDLDAVDIRRQTPLHL 320
Cdd:PHA02876  403 aLSQKIGTALHFALCGTNPYMSvKTLIDRGANVNSKNKDLSTPLHYACKKNCkLDVIEMLLDNGADVNAINIQNQYPLLI 482

                         330       340
                  ....*....|....*....|....*.
gi 1039795032 321 AAEhaWQDVADMLLIAGADlsLRDKQ 346
Cdd:PHA02876  483 ALE--YHGIVNILLHYGAE--LRDSR 504
PHA03095 PHA03095
ankyrin-like protein; Provisional
 28-311 2.28e-21

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 96.63  E-value: 2.28e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032  28 VERMKELFEKRVNIRARNHVGRVALHWAAGAGHEQ---AVRLLLERGAAVDDVDSFGMNSLLLSAWFGH-LQIVQILVNA 103
Cdd:PHA03095   27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKvkdIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKA 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 104 GAKVHCESKDGLTLLH--CAAQKGHVPVLAFVME---DLEDValdhaDKLGRTAFH-----RAAEhgqLDALDFLVGSGC 173
Cdd:PHA03095  107 GADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRkgaDVNAL-----DLYGMTPLAvllksRNAN---VELLRLLIDAGA 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 174 DHSVKDKGGNTALH--LAASQGHVDVLQRLVDIGLDLEEQNTEGLTALHAAAegIHADC---VML-LLGAGSNVNALTQK 247
Cdd:PHA03095  179 DVYAVDDRFRSLLHhhLQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMA--TGSSCkrsLVLpLLIAGISINARNRY 256

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039795032 248 RLSCLHYAALGGSEDLSRALIKAGGCTNVADKQGTTPMHLAVKHNFPGLVQLLIDGHSDLDAVD 311
Cdd:PHA03095  257 GQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVA 320
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
195-369 6.10e-21

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 93.09  E-value: 6.10e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 195 VDVLQRLVDIGLDLEEQNTEGLTALHAAAEGIHADCVMLLLGAGSNVNALTQKRLSCLHYAALGGSEDLSRALIKAGGCT 274
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 275 NVADKQGTTPMHLAVKHNFPGLVQLLIDGHSDLDAVDIRRQTPLHLAAEHAWQDVADMLLIAGADLSLRDKQGKTALAVA 354
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                         170
                  ....*....|....*
gi 1039795032 355 ARSNHVSLVDMIIKA 369
Cdd:COG0666   161 AANGNLEIVKLLLEA 175
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 55-356 2.51e-20

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 93.10  E-value: 2.51e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032  55 AAGAGHEQAVRLLLERGAAVDDVDSFGMNSLLLSAWFGHLQIVQILVNAGAK-----VHCESKDGL-TLLHCAaqkghvp 128
Cdd:PHA02874   42 AIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDtsilpIPCIEKDMIkTILDCG------- 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 129 vlafvmedledVALDHADKLGRTAFHRAAEHGQLDALDFLVGSGCDHSVKDKGGNTALHLAASQGHVDVLQRLVDIGLDL 208
Cdd:PHA02874  115 -----------IDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYA 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 209 EEQNTEGLTALHAAAEGIHADCVMLLLGAGSNVNaltqkrlsclhyaalggsedlsralikaggctnVADKQGTTPMHLA 288
Cdd:PHA02874  184 NVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIM---------------------------------NKCKNGFTPLHNA 230

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039795032 289 VKHNfPGLVQLLIDGHSdLDAVDIRRQTPLHLAAEHAW-QDVADMLLIAGADLSLRDKQGKTALAVAAR 356
Cdd:PHA02874  231 IIHN-RSAIELLINNAS-INDQDIDGSTPLHHAINPPCdIDIIDILLYHKADISIKDNKGENPIDTAFK 297
Ank_2 pfam12796
Ankyrin repeats (3 copies);
153-243 2.04e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.08  E-value: 2.04e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 153 FHRAAEHGQLDALDFLVGSGCDHSVKDKGGNTALHLAASQGHVDVLQRLVDiGLDLEEQNtEGLTALHAAAEGIHADCVM 232
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|.
gi 1039795032 233 LLLGAGSNVNA 243
Cdd:pfam12796  79 LLLEKGADINV 89
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 138-368 2.23e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 84.33  E-value: 2.23e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 138 EDVALDHADKLGRTAFHRAAEHGQLDALDFLVGSGCDHSVKDKGGNTALHLAASQGHV-----DVLQRLVDIGLDLEEQN 212
Cdd:PHA03100   24 EDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPD 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 213 TEGLTALHAAAEGI--HADCVMLLLGAGSNVNALTQKRLSCLHYAALGGSEDLS--RALIKAGGCTNVADKqgttpmhla 288
Cdd:PHA03100  104 NNGITPLLYAISKKsnSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLKilKLLIDKGVDINAKNR--------- 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 289 vkhnfpglVQLLIDGHSDLDAVDIRRQTPLHLAAEHAWQDVADMLLIAGADLSLRDKQGKTALAVAARSNHVSLVDMIIK 368
Cdd:PHA03100  175 --------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLN 246
Ank_2 pfam12796
Ankyrin repeats (3 copies);
85-179 8.75e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.46  E-value: 8.75e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032  85 LLLSAWFGHLQIVQILVNAGAKVHCESKDGLTLLHCAAQKGHVPVLAFVmedLEDVALDHADKlGRTAFHRAAEHGQLDA 164
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL---LEHADVNLKDN-GRTALHYAARSGHLEI 76

                          90
                  ....*....|....*
gi 1039795032 165 LDFLVGSGCDHSVKD 179
Cdd:pfam12796  77 VKLLLEKGADINVKD 91
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 146-367 7.74e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 77.03  E-value: 7.74e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 146 DKLGRTAFHRAAEHGQLDALDFLVGSGCDHSVKDKGGNTALHLAASQGHVDVLQRLVDiglDLEEQNTEGLTALHAAAEg 225
Cdd:PHA02876  175 DIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIID---NRSNINKNDLSLLKAIRN- 250

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 226 IHADCVMLLLGAGSNVNALTQKRLSCLHYAALGGSedLSR---ALIKAGGCTNVADKQGTTPMHLAVKHNFPGL-VQLLI 301
Cdd:PHA02876  251 EDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPS--LSRlvpKLLERGADVNAKNIKGETPLYLMAKNGYDTEnIRTLI 328

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039795032 302 DGHSDLDAVDIRRQTPLHLAAE-HAWQDVADMLLIAGADLSLRDKQGKTALAVAARSNHVSLVDMII 367
Cdd:PHA02876  329 MLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLL 395
Ank_2 pfam12796
Ankyrin repeats (3 copies);
252-344 1.09e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 69.37  E-value: 1.09e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 252 LHYAALGGSEDLSRALIKAGGCTNVADKQGTTPMHLAVKHNFPGLVQLLIDgHSDLDAVDiRRQTPLHLAAEHAWQDVAD 331
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1039795032 332 MLLIAGADLSLRD 344
Cdd:pfam12796  79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
19-108 4.77e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.45  E-value: 4.77e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032  19 LHEASRWNQVERMKELFEKRVNIRARNHVGRVALHWAAGAGHEQAVRLLLERGAAvdDVDSFGMNSLLLSAWFGHLQIVQ 98
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|
gi 1039795032  99 ILVNAGAKVH 108
Cdd:pfam12796  79 LLLEKGADIN 88
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 184-367 5.41e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 70.76  E-value: 5.41e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 184 TALHLAASQGHVDVLQRLVDIGLDLEEQNTEG----LTALHAAAEGI-------------------HADCVMLLLGAGSN 240
Cdd:PHA02874   37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIphplLTAIKIGAHDIikllidngvdtsilpipciEKDMIKTILDCGID 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 241 VNALTQKRLSCLHYAALGGSEDLSRALIKAGGCTNVADKQGTTPMHLAVKHNFPGLVQLLIDGHSDLDAVDIRRQTPLHL 320
Cdd:PHA02874  117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHN 196

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1039795032 321 AAEHAWQDVADMLLIAGADLSLRDKQGKTALAVAARSNHvSLVDMII 367
Cdd:PHA02874  197 AAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLI 242
Ank_2 pfam12796
Ankyrin repeats (3 copies);
285-370 5.84e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 64.37  E-value: 5.84e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 285 MHLAVKHNFPGLVQLLIDGHSDLDAVDIRRQTPLHLAAEHAWQDVAdMLLIAGADLSLRDkQGKTALAVAARSNHVSLVD 364
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIV-KLLLEHADVNLKD-NGRTALHYAARSGHLEIVK 78


                  ....*.
gi 1039795032 365 MIIKAD 370
Cdd:pfam12796  79 LLLEKG 84
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 226-378 7.43e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 70.29  E-value: 7.43e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 226 IHADCVMLLLGAGSNVNALTQKRL-SCLHYAALGGSEDLSRALIKAGGCTNVADKQGTTPMHLAVKHNFPGLVQLLIDGH 304
Cdd:PHA02878  145 IEAEITKLLLSYGADINMKDRHKGnTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENG 224

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039795032 305 SDLDAVDIRRQTPLHLAAEHAWQ-DVADMLLIAGADLSLRDK-QGKTALAVAARSNHVSLVDMIIKAD-RFYRWEKD 378
Cdd:PHA02878  225 ASTDARDKCGNTPLHISVGYCKDyDILKLLLEHGVDVNAKSYiLGLTALHSSIKSERKLKLLLEYGADiNSLNSYKL 301
Ank_2 pfam12796
Ankyrin repeats (3 copies);
219-311 1.05e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 63.98  E-value: 1.05e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 219 LHAAAEGIHADCVMLLLGAGSNVNALTQKRLSCLHYAALGGSEDLSRALIKAGGCTNVADkqGTTPMHLAVKHNFPGLVQ 298
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN--GRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1039795032 299 LLIDGHSDLDAVD 311
Cdd:pfam12796  79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
118-212 2.07e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 62.83  E-value: 2.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 118 LHCAAQKGHVPVLAFVMEdlEDVALDHADKLGRTAFHRAAEHGQLDALDFLVgsgcDHSVKDK--GGNTALHLAASQGHV 195
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLE--NGADANLQDKNGRTALHLAAKNGHLEIVKLLL----EHADVNLkdNGRTALHYAARSGHL 74

                          90
                  ....*....|....*..
gi 1039795032 196 DVLQRLVDIGLDLEEQN 212
Cdd:pfam12796  75 EIVKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
52-140 3.79e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 62.06  E-value: 3.79e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032  52 LHWAAGAGHEQAVRLLLERGAAVDDVDSFGMNSLLLSAWFGHLQIVQILVNAGAKVHCEskDGLTLLHCAAQKGHVPVLA 131
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD--NGRTALHYAARSGHLEIVK 78


                  ....*....
gi 1039795032 132 FVMEDLEDV 140
Cdd:pfam12796  79 LLLEKGADI 87
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 150-368 7.41e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 66.94  E-value: 7.41e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 150 RTAFHRAAEHGQLDALDFLVGSGCDHSVKDKGGNTALHLAASQGHVDVLQRLVDIGLDLEEQNTEGLTALHAAAEGIHAD 229
Cdd:PHA02875    3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 230 CVMLLLGAGSNVNALTQKR-LSCLHYAALGGSEDLSRALIKAGGCTNVADKQGTTPMHLAVKHNFPGLVQLLIDGHSDLD 308
Cdd:PHA02875   83 AVEELLDLGKFADDVFYKDgMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLD 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039795032 309 AVDIRRQTPLHLAAEHAWQDVADMLLIAGADLSLRDKQGK-TALAVAARSNHVSLVDMIIK 368
Cdd:PHA02875  163 IEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIK 223
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 215-356 1.52e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 66.44  E-value: 1.52e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 215 GLTALHAAAEGIHADCVMLLLGAGSNVNALTQKRLSCLHYAALGGSEDLSRALIKAGGCTNVADKQGTTPMHLAVKH--N 292
Cdd:PHA02878  168 GNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYckD 247

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039795032 293 FPgLVQLLIDGHSDLDAVD-IRRQTPLHLAAEHawQDVADMLLIAGADLSLRDKQGKTALAVAAR 356
Cdd:PHA02878  248 YD-ILKLLLEHGVDVNAKSyILGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSAVK 309
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 19-244 1.65e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 65.84  E-value: 1.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032  19 LHEASRWNQVERMKELFEKRVNIRARNHVGRVALHWAAGAGHEQA-----VRLLLERGAAVDDVDSFGMNSLLLSAW--F 91
Cdd:PHA03100   39 LYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLTdvkeiVKLLLEYGANVNAPDNNGITPLLYAISkkS 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032  92 GHLQIVQILVNAGAKVHCESKDGLTLLHCAAQKGHVpvlafvmeDLEDVAL--DHADKLgrtafhraaehGQLDALDFLV 169
Cdd:PHA03100  119 NSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKI--------DLKILKLliDKGVDI-----------NAKNRVNYLL 179

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039795032 170 GSGCDHSVKDKGGNTALHLAASQGHVDVLQRLVDIGLDLEEQNTEGLTALHAAAEGIHADCVMLLLGAGSNVNAL 244
Cdd:PHA03100  180 SYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTI 254
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 96-280 5.63e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 64.30  E-value: 5.63e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032  96 IVQILVNAGAKVHCESKDGLTLLHCAAQKGHVpvLAFVMEdLEDVALDH------ADKLGRTAFHRAAEH--GQLDALDF 167
Cdd:PHA03100   50 VVKILLDNGADINSSTKNNSTPLHYLSNIKYN--LTDVKE-IVKLLLEYganvnaPDNNGITPLLYAISKksNSYSIVEY 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 168 LVGSGCDHSVKDKGGNTALHLAASQGHVDV------LQRLVDI------------GLDLEEQNTEGLTALHAAAEGIHAD 229
Cdd:PHA03100  127 LLDNGANVNIKNSDGENLLHLYLESNKIDLkilkllIDKGVDInaknrvnyllsyGVPINIKDVYGFTPLHYAVYNNNPE 206

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1039795032 230 CVMLLLGAGSNVNALTQKRLSCLHYAALGGSEDLSRALIKAGGCTNVADKQ 280
Cdd:PHA03100  207 FVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 154-367 1.33e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 63.73  E-value: 1.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 154 HRAAEHGqLDALDFLVGSGCDHSvkDKGGNTALHLAASQGHVDVLQRLVDIGLDLEEQNTEGLTALHAAAEGIHADCVML 233
Cdd:PLN03192  500 HHKELHD-LNVGDLLGDNGGEHD--DPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLV 576

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 234 LLGAGSNVnaltqkrlsclhyaalggsedlsralikaggctNVADKQGTTPM--HLAVKHN--FPGLVQL--LIDGHSDL 307
Cdd:PLN03192  577 LLKHACNV---------------------------------HIRDANGNTALwnAISAKHHkiFRILYHFasISDPHAAG 623

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 308 DAvdirrqtpLHLAAEHAWQDVADMLLIAGADLSLRDKQGKTALAVAARSNHVSLVDMII 367
Cdd:PLN03192  624 DL--------LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLI 675
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 131-243 3.20e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 62.58  E-value: 3.20e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 131 AFVMEDLEDVALDH--ADKLGRTAFHRAAEHGQLDALDFLVGSGCDHSVKDKGGNTAL-------H-------------- 187
Cdd:PLN03192  538 AALLEELLKAKLDPdiGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALwnaisakHhkifrilyhfasis 617

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039795032 188 ----------LAASQGHVDVLQRLVDIGLDLEEQNTEGLTALHAA-AEGiHADCVMLLLGAGSNVNA 243
Cdd:PLN03192  618 dphaagdllcTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAmAED-HVDMVRLLIMNGADVDK 683
Ank_4 pfam13637
Ankyrin repeats (many copies);
149-202 4.06e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.36  E-value: 4.06e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039795032 149 GRTAFHRAAEHGQLDALDFLVGSGCDHSVKDKGGNTALHLAASQGHVDVLQRLV 202
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 19-290 4.37e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 61.82  E-value: 4.37e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032  19 LHEASRWNQVERMKELFEKRVNIRARNHVGRVALHWAAGAGHEQAVRLLLergaAVDDVDSFGMNSLLLSAWFGH--LQI 96
Cdd:PHA02878   41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMI----RSINKCSVFYTLVAIKDAFNNrnVEI 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032  97 VQILVNAGAKVHCESKDGLTLLHCAAQKGHVPVLAFVMEDLEDVALDHADKlGRTAFHRAAEHGQLDALDFLVGSGCDHS 176
Cdd:PHA02878  117 FKIILTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDRHK-GNTALHYATENKDQRLTELLLSYGANVN 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 177 VKDKGGNTALHLAASQGHVDVLQRLVDIGLDLEEQNTEGLTALH-AAAEGIHADCVMLLLGAGSNVNALTQKR-LSCLHY 254
Cdd:PHA02878  196 IPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHiSVGYCKDYDILKLLLEHGVDVNAKSYILgLTALHS 275

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1039795032 255 AAlgGSEDLSRALIKAGGCTNVADKQGTTPMHLAVK 290
Cdd:PHA02878  276 SI--KSERKLKLLLEYGADINSLNSYKLTPLSSAVK 309
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 19-189 1.14e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 60.36  E-value: 1.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032  19 LHEASRWNQVERMKELFEKRVNIRARNHVGRVALHWAAGAGHEQAVRLLLERGAAVDDVDSFGMNSLLLSAWFGHLQIVQ 98
Cdd:PHA02874  128 LHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIK 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032  99 ILVNAGAKVHCESKDGLTLLHCAA--QKGHVPVLafvmedLEDVALDHADKLGRTAFHRAAEHG-QLDALDFLVGSGCDH 175
Cdd:PHA02874  208 LLIDHGNHIMNKCKNGFTPLHNAIihNRSAIELL------INNASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADI 281

                         170
                  ....*....|....
gi 1039795032 176 SVKDKGGNTALHLA 189
Cdd:PHA02874  282 SIKDNKGENPIDTA 295
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 192-355 3.11e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 59.31  E-value: 3.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 192 QGHVDVLQRLVDIGLDLEEQNTEGLTALHAAAEGIHADCVMLLLGAGSNVNALTQKRLSCLHYAALGGSEDLSRALI--- 268
Cdd:PHA02876  155 QDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIdnr 234

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 269 --------------------------KAGGCTNVADKQGTTPMHLAVKH-NFPGLVQLLIDGHSDLDAVDIRRQTPLHLA 321
Cdd:PHA02876  235 sninkndlsllkairnedletslllyDAGFSVNSIDDCKNTPLHHASQApSLSRLVPKLLERGADVNAKNIKGETPLYLM 314

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1039795032 322 AEHAWqDVADM--LLIAGADLSLRDKQGKTALAVAA 355
Cdd:PHA02876  315 AKNGY-DTENIrtLIMLGADVNAADRLYITPLHQAS 349
Ank_4 pfam13637
Ankyrin repeats (many copies);
51-101 1.69e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.74  E-value: 1.69e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1039795032  51 ALHWAAGAGHEQAVRLLLERGAAVDDVDSFGMNSLLLSAWFGHLQIVQILV 101
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 183-382 2.16e-08

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 56.56  E-value: 2.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 183 NTALHLAASQGHVDVLQRLVDI-GLDLEEQNTEGLTALHAAAEGIHADCVMLLL-GAGSNVN-ALTQ---KRLSCLHYAA 256
Cdd:cd22192    18 ESPLLLAAKENDVQAIKKLLKCpSCDLFQRGALGETALHVAALYDNLEAAVVLMeAAPELVNePMTSdlyQGETALHIAV 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 257 LGGSEDLSRALIKAGGCTNVADKQGTT--------------PMHLAVKHNFPGLVQLLIDGHSDLDAVDIRRQTPLHLAA 322
Cdd:cd22192    98 VNQNLNLVRELIARGADVVSPRATGTFfrpgpknliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILV 177

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 323 EHAWQDVA----DMLLIAGADLS------LRDKQGKTALAVAARSNHVSLVDMIIKADRFYRWEKDHLSC 382
Cdd:cd22192   178 LQPNKTFAcqmyDLILSYDKEDDlqpldlVPNNQGLTPFKLAAKEGNIVMFQHLVQKRRHIQWTYGPLTS 247
Ank_4 pfam13637
Ankyrin repeats (many copies);
182-235 4.68e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.58  E-value: 4.68e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039795032 182 GNTALHLAASQGHVDVLQRLVDIGLDLEEQNTEGLTALHAAAEGIHADCVMLLL 235
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 286-368 7.31e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.90  E-value: 7.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 286 HLAVKHNFPGlVQLLIDGHSDLDAVDIRRQTPLHLAAEHAWQDVADMLLIAGADLSLRDKQGKTALAVAARSNHVSLVDM 365
Cdd:PTZ00322   88 QLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                  ...
gi 1039795032 366 IIK 368
Cdd:PTZ00322  167 LSR 169
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 49-276 7.52e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 54.61  E-value: 7.52e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032  49 RVALHWAAGAGHEQAVRLLLERGAAVDDVDSFGMNSLLLSAWFGHLQIVQILVNAGAKVHCESKDGLTLLHCAAQKGHVP 128
Cdd:PHA02875    3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 129 VLAFVMeDLEDVALDHADKLGRTAFHRAAEHGQLDALDFLVGSGCDHSVKDKGGNTALHLAASQGHVDVLQRLVDIGLDL 208
Cdd:PHA02875   83 AVEELL-DLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACL 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 209 EEQNTEGLTAL-HAAAEGIHADCVMLLlGAGSNVNALTQKR-LSCLHYAALGGSEDLSRALIKAGGCTNV 276
Cdd:PHA02875  162 DIEDCCGCTPLiIAMAKGDIAICKMLL-DSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCNI 230
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 155-322 1.34e-07

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 54.25  E-value: 1.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 155 RAAEHGQLDALDFLVGS-GCDHSVKDKGGNTALHLAASQGHVDVLQRLVD-----IGLDLEEQNTEGLTALHAAAEGIHA 228
Cdd:cd22192    23 LAAKENDVQAIKKLLKCpSCDLFQRGALGETALHVAALYDNLEAAVVLMEaapelVNEPMTSDLYQGETALHIAVVNQNL 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 229 DCVMLLLGAGSNVN------ALTQKRLSCLHY--------AALGGSEDLSRALIKAGGCTNVADKQGTTPMHLAVKHNFP 294
Cdd:cd22192   103 NLVRELIARGADVVspratgTFFRPGPKNLIYygehplsfAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNK 182

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1039795032 295 GLVQLLID------GHSDLDAVDIRRQ----TPLHLAA 322
Cdd:cd22192   183 TFACQMYDlilsydKEDDLQPLDLVPNnqglTPFKLAA 220
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 48-213 2.37e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 53.33  E-value: 2.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032  48 GRVALHWAAGAGHEQAVRLLLERGAAVDDVDSFGMNSLLLSAWFGHLQIVQIlvnagakvhceskdgltLLHCAAqkghv 127
Cdd:PLN03192  558 GRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRI-----------------LYHFAS----- 615

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 128 pvlafvmedledVALDHAdklGRTAFHRAAEHGQLDALDFLVGSGCDHSVKDKGGNTALHLAASQGHVDVLQRLVDIGLD 207
Cdd:PLN03192  616 ------------ISDPHA---AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGAD 680


                  ....*.
gi 1039795032 208 LEEQNT 213
Cdd:PLN03192  681 VDKANT 686
Ank_4 pfam13637
Ankyrin repeats (many copies);
114-169 1.06e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.73  E-value: 1.06e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039795032 114 GLTLLHCAAQKGHVPVLAFVMEDLEDValDHADKLGRTAFHRAAEHGQLDALDFLV 169
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADI--NAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 196-356 1.52e-06

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 50.91  E-value: 1.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 196 DVLQRLVDIglDLEEQNTEGLTALHAAAEGIHADCVMLLLGAGSNVNALTQkrlsclhyaalggsedlsralikaGGCTN 275
Cdd:cd22194   124 GILDRFINA--EYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAK------------------------GVFFN 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 276 VADKQ-----GTTPMHLAVKHNFPGLVQLLID-GHSDLDAVDIRRQTPLH---LAAEHAWQDVA------DMLLIAGADL 340
Cdd:cd22194   178 PKYKHegfyfGETPLALAACTNQPEIVQLLMEkESTDITSQDSRGNTVLHalvTVAEDSKTQNDfvkrmyDMILLKSENK 257

                         170
                  ....*....|....*....
gi 1039795032 341 SL---RDKQGKTALAVAAR 356
Cdd:cd22194   258 NLetiRNNEGLTPLQLAAK 276
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 121-289 1.98e-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: 50.46  E-value: 1.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 121 AAQKGHVPVLAFVMEDLEDVALDHADKLGRTA-FHRAAEHGQLDALDFLVGSGCDHSVkdkgGNTALHlAASQGHVDVLQ 199
Cdd:TIGR00870  24 AAERGDLASVYRDLEEPKKLNINCPDRLGRSAlFVAAIENENLELTELLLNLSCRGAV----GDTLLH-AISLEYVDAVE 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 200 RLVDI-------GLDLEEQN-------TEGLTALHAAAEGIHADCVMLLLGAGSNVNA-------LTQKRLSCLHY---- 254
Cdd:TIGR00870  99 AILLHllaafrkSGPLELANdqytsefTPGITALHLAAHRQNYEIVKLLLERGASVPAracgdffVKSQGVDSFYHgesp 178

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1039795032 255 ---AALGGSEDLSRALIKAGGCTNVADKQGTTPMHLAV 289
Cdd:TIGR00870 179 lnaAACLGSPSIVALLSEDPADILTADSLGNTLLHLLV 216
Ank_5 pfam13857
Ankyrin repeats (many copies);
173-222 2.17e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.64  E-value: 2.17e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039795032 173 CDHSVKDKGGNTALHLAASQGHVDVLQRLVDIGLDLEEQNTEGLTALHAA 222
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 29-232 3.24e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 49.58  E-value: 3.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032  29 ERMKELFEKRVNIRARNHVGRVALHWAAGAGHEQAVRLLLERGAAVDDVDSFGMNSLLLSAWFGHLQIVQILVNAGAKVH 108
Cdd:PHA02874  105 DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 109 CESKDGLTLLHCAAQKGHVPVLAFVMEDLEDVALDHadKLGRTAFHRAAEHGQlDALDFLVGSGcDHSVKDKGGNTALHL 188
Cdd:PHA02874  185 VKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKC--KNGFTPLHNAIIHNR-SAIELLINNA-SINDQDIDGSTPLHH 260

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1039795032 189 AASQG-HVDVLQRLVDIGLDLEEQNTEGLTALHAAAEGIHADCVM 232
Cdd:PHA02874  261 AINPPcDIDIIDILLYHKADISIKDNKGENPIDTAFKYINKDPVI 305
Ank_4 pfam13637
Ankyrin repeats (many copies);
19-68 3.34e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.19  E-value: 3.34e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039795032  19 LHEASRWNQVERMKELFEKRVNIRARNHVGRVALHWAAGAGHEQAVRLLL 68
Cdd:pfam13637   5 LHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
19-78 3.98e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 45.11  E-value: 3.98e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032  19 LHEASRWNQVERMKELFEKrVNIRARNHvGRVALHWAAGAGHEQAVRLLLERGAAVDDVD 78
Cdd:pfam12796  34 LHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
Ank_4 pfam13637
Ankyrin repeats (many copies);
316-367 4.94e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.80  E-value: 4.94e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039795032 316 TPLHLAAEHAWQDVADMLLIAGADLSLRDKQGKTALAVAARSNHVSLVDMII 367
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 214-381 6.06e-06

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: 48.64  E-value: 6.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 214 EGLTALHAAAEGIHADCVMLLLGAGSNVNALTQKRLSCLHYaalggsedlsralikAGGCTNVadkqGTTPMHLAVKHNF 293
Cdd:cd22193    75 EGQTALHIAIERRQGDIVALLVENGADVHAHAKGRFFQPKY---------------QGEGFYF----GELPLSLAACTNQ 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 294 PGLVQLLIDGH---SDLDAVDIRRQTPLHLAAEHA---------WQDVADMLLIAGADL-------SLRDKQGKTALAVA 354
Cdd:cd22193   136 PDIVQYLLENEhqpADIEAQDSRGNTVLHALVTVAdntkentkfVTRMYDMILIRGAKLcptveleEIRNNDGLTPLQLA 215

                         170       180
                  ....*....|....*....|....*..
gi 1039795032 355 ARSNHVSLVDMIIKADrFYRWEKDHLS 381
Cdd:cd22193   216 AKMGKIEILKYILQRE-IKEPELRHLS 241
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 97-176 7.78e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.36  E-value: 7.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032  97 VQILVNAGAKVHCESKDGLTLLHCAAQKGHVPVLAFVMEDLEDVALdhADKLGRTAFHRAAEHGQLDALDFLVG-SGCDH 175
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTL--LDKDGKTPLELAEENGFREVVQLLSRhSQCHF 175


                  .
gi 1039795032 176 S 176
Cdd:PTZ00322  176 E 176
Ank_4 pfam13637
Ankyrin repeats (many copies);
248-301 7.92e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.03  E-value: 7.92e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039795032 248 RLSCLHYAALGGSEDLSRALIKAGGCTNVADKQGTTPMHLAVKHNFPGLVQLLI 301
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
299-354 1.64e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.33  E-value: 1.64e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039795032 299 LLIDGHSDLDAVDIRRQTPLHLAAEHAWQDVADMLLIAGADLSLRDKQGKTALAVA 354
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
267-321 2.45e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 2.45e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039795032 267 LIKAGGC-TNVADKQGTTPMHLAVKHNFPGLVQLLIDGHSDLDAVDIRRQTPLHLA 321
Cdd:pfam13857   1 LLEHGPIdLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 85-290 2.72e-05

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 46.54  E-value: 2.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032  85 LLLSAWFGHLQIVQ-ILVNAGAKVHCESKDGLTLLHCAAQKGHVPVLAFVME---DLEDVALDHADKLGRTAFHRAAEHG 160
Cdd:cd22192    21 LLLAAKENDVQAIKkLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEaapELVNEPMTSDLYQGETALHIAVVNQ 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 161 QLDALDFLVGSGCDHS---------VKDKG-----GNTALHLAASQGHVDVLQRLVDIGLDLEEQNTEGLTALHaaaegi 226
Cdd:cd22192   101 NLNLVRELIARGADVVspratgtffRPGPKnliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH------ 174

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 227 hadcvMLLLGAgsnvnaltQKRLSC------LHYAALGGSEDLSRalikaggctnVADKQGTTPMHLAVK 290
Cdd:cd22192   175 -----ILVLQP--------NKTFACqmydliLSYDKEDDLQPLDL----------VPNNQGLTPFKLAAK 221
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 19-93 2.89e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 46.78  E-value: 2.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032  19 LHEASRWNQVERMKELFEKRVNIRARNHVGRVALHWAAGAGHEQAVRLLLERGAAV------DDVDSFGMNSLLLSAWFG 92
Cdd:PLN03192  626 LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVdkantdDDFSPTELRELLQKRELG 705


                  .
gi 1039795032  93 H 93
Cdd:PLN03192  706 H 706
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 296-367 2.91e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 46.60  E-value: 2.91e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039795032 296 LVQLLIDGHSDLDAVDIRRQTPLHLAAEHAWQDVADMLLIAGADLSLRDKQGKTALAVAARSNHVSLVDMII 367
Cdd:PHA02876  160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAII 231
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 220-309 3.16e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.43  E-value: 3.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 220 HAAAEGiHADCVMLLLGAGSNVNALTQKRLSCLHYAALGGSEDLSRALIKAGGCTNVADKQGTTPMHLAVKHNFPGLVQL 299
Cdd:PTZ00322   88 QLAASG-DAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166

                          90
                  ....*....|...
gi 1039795032 300 LI---DGHSDLDA 309
Cdd:PTZ00322  167 LSrhsQCHFELGA 179
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 253-334 3.41e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.43  E-value: 3.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 253 HYAALGGSEDLsRALIKAGGCTNVADKQGTTPMHLAVKHNFPGLVQLLIDGHSDLDAVDIRRQTPLHLAAEHAWQDVADM 332
Cdd:PTZ00322   88 QLAASGDAVGA-RILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                  ..
gi 1039795032 333 LL 334
Cdd:PTZ00322  167 LS 168
Ank_5 pfam13857
Ankyrin repeats (many copies);
136-189 4.78e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.18  E-value: 4.78e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039795032 136 DLEDVALDHADKLGRTAFHRAAEHGQLDALDFLVGSGCDHSVKDKGGNTALHLA 189
Cdd:pfam13857   3 EHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 19-128 4.79e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 45.75  E-value: 4.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032  19 LHEASRWNQVERMKELFEKRVNIRARNHVGRVALHWAAGAGHEQAVRLLLERGAAVDDVDSFGMNSLLLSAWFGHLQIVQ 98
Cdd:PHA02875  106 LHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICK 185

                          90       100       110
                  ....*....|....*....|....*....|
gi 1039795032  99 ILVNAGAKVHCESKDGLTLLHCAAQKGHVP 128
Cdd:PHA02875  186 MLLDSGANIDYFGKNGCVAALCYAIENNKI 215
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 19-169 6.25e-05

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 45.39  E-value: 6.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032  19 LHEASRWNQVERMKELFE-KRVNIRARNHVGRVALHWAAGAGHEQA---------------------------------- 63
Cdd:cd22192    21 LLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAavvlmeaapelvnepmtsdlyqgetalhiavvnq 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032  64 ----VRLLLERGAavdDVDS-----------------FGMNSLLLSAWFGHLQIVQILVNAGAKVHCESKDGLTLLH-CA 121
Cdd:cd22192   101 nlnlVRELIARGA---DVVSpratgtffrpgpknliyYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHiLV 177

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039795032 122 AQKGHVPV-------LAFVMEDlEDVALDH-ADKLGRTAFHRAAEHGQLDALDFLV 169
Cdd:cd22192   178 LQPNKTFAcqmydliLSYDKED-DLQPLDLvPNNQGLTPFKLAAKEGNIVMFQHLV 232
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 168-236 7.88e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 45.27  E-value: 7.88e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039795032 168 LVGSGCDHSVKDKGGNTALHLAASQGHVDVLQRLVDIGLDLEEQNTEGLTALHAAAEGIHADCVMLLLG 236
Cdd:PTZ00322  101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 46-134 1.09e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.89  E-value: 1.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032  46 HVGRVALHWAAGAGHEQAVRLLLERGAAVDDVDSFGMNSLLLSAWFGHLQIVQILVNAGAKVHCESKDGLTLLHCAAQKG 125
Cdd:PTZ00322   80 HMLTVELCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENG 159


                  ....*....
gi 1039795032 126 HVPVLAFVM 134
Cdd:PTZ00322  160 FREVVQLLS 168
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 260-368 2.20e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 43.80  E-value: 2.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 260 SEDLS--RALIKA-GGCTNVADKQGTTPMHLAVKHNFPGLVQLLIDGHSDLDAVDIRRQTPLHLAAEHAWQDVADMLLIA 336
Cdd:PHA02874   11 SGDIEaiEKIIKNkGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDN 90

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1039795032 337 GADLSL-----------------------RDKQGKTALAVAARSNHVSLVDMIIK 368
Cdd:PHA02874   91 GVDTSIlpipciekdmiktildcgidvniKDAELKTFLHYAIKKGDLESIKMLFE 145
Ank_4 pfam13637
Ankyrin repeats (many copies);
91-132 3.62e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.41  E-value: 3.62e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1039795032  91 FGHLQIVQILVNAGAKVHCESKDGLTLLHCAAQKGHVPVLAF 132
Cdd:pfam13637  11 SGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKL 52
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 116-290 7.00e-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: 42.44  E-value: 7.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 116 TLLHCAAQKGhvpvlafVMEDLEDVALDHADKLGRTAFHRAAEHGQLDALDFLVGSGCDHSVKDKG-------------- 181
Cdd:cd22194   115 ILLAFAEENG-------ILDRFINAEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGvffnpkykhegfyf 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 182 GNTALHLAASQGHVDVLQRLVDIG-LDLEEQNTEGLTALHAaaegihadCVMLLLGAGSNVNALTQkrlscLHYAALGGS 260
Cdd:cd22194   188 GETPLALAACTNQPEIVQLLMEKEsTDITSQDSRGNTVLHA--------LVTVAEDSKTQNDFVKR-----MYDMILLKS 254

                         170       180       190
                  ....*....|....*....|....*....|
gi 1039795032 261 EDLSRALIKaggctnvaDKQGTTPMHLAVK 290
Cdd:cd22194   255 ENKNLETIR--------NNEGLTPLQLAAK 276
Ank_4 pfam13637
Ankyrin repeats (many copies);
215-268 7.22e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 37.64  E-value: 7.22e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039795032 215 GLTALHAAAEGIHADCVMLLLGAGSNVNALTQKRLSCLHYAALGGSEDLSRALI 268
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 182-210 8.04e-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: 36.80  E-value: 8.04e-04
                           10        20
                   ....*....|....*....|....*....
gi 1039795032  182 GNTALHLAASQGHVDVLQRLVDIGLDLEE 210
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02798 PHA02798
ankyrin-like protein; Provisional
 64-291 1.24e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 41.36  E-value: 1.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032  64 VRLLLERGAAVDDVDSFGMNSL--LLSAWFGH---LQIVQILVNAGAKVHCESKDGLTLLHCAAQKGHV---PVLAFVME 135
Cdd:PHA02798   54 VKLFINLGANVNGLDNEYSTPLctILSNIKDYkhmLDIVKILIENGADINKKNSDGETPLYCLLSNGYInnlEILLFMIE 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 136 DLEDVALdhADKLGRTAFH---RAAEHGQLDALDFLVGSGCD-HSVKDKGGNTALHL----AASQGHVDVLQRLVDIGLD 207
Cdd:PHA02798  134 NGADTTL--LDKDGFTMLQvylQSNHHIDIEIIKLLLEKGVDiNTHNNKEKYDTLHCyfkyNIDRIDADILKLFVDNGFI 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 208 LEEQNT-------EGLTALHAAAEGIHADCVMLLLgAGSNVNALTQKRLSCLHYAALGGSEDLSRALIKAGGCTNVADKQ 280
Cdd:PHA02798  212 INKENKshkkkfmEYLNSLLYDNKRFKKNILDFIF-SYIDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITEL 290

                         250
                  ....*....|.
gi 1039795032 281 GTTPMHLAVKH 291
Cdd:PHA02798  291 GNTCLFTAFEN 301
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 193-368 1.29e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 41.10  E-value: 1.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 193 GHVDVLQRLVD-----IGLDLEEQNTEGLTALHAAaegiHADCVMLLLGAGSNVNALTQKRLSCLHYAALGGSEDLSRAL 267
Cdd:PHA02874   12 GDIEAIEKIIKnkgncINISVDETTTPLIDAIRSG----DAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 268 IKAGGCTNVadkqgttpmhLAVKHNFPGLVQLLIDGHSDLDAVDIRRQTPLHLAAEHAWQDVADMLLIAGADLSLRDKQG 347
Cdd:PHA02874   88 IDNGVDTSI----------LPIPCIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNG 157

                         170       180
                  ....*....|....*....|.
gi 1039795032 348 KTALAVAARSNHVSLVDMIIK 368
Cdd:PHA02874  158 CYPIHIAIKHNFFDIIKLLLE 178
PHA02917 PHA02917
ankyrin-like protein; Provisional
 306-367 1.53e-03

ankyrin-like protein; Provisional


Pssm-ID: 165231 [Multi-domain]  Cd Length: 661  Bit Score: 41.14  E-value: 1.53e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039795032 306 DLDAVDIRRQTPLHLAAEHAWQDVADMLLIAGADLSLRDKQGKTALAVAA-RSNHVSLVDMII 367
Cdd:PHA02917  444 DINMIDKRGETLLHKAVRYNKQSLVSLLLESGSDVNIRSNNGYTCIAIAInESRNIELLKMLL 506
Ank_5 pfam13857
Ankyrin repeats (many copies);
240-288 1.79e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.56  E-value: 1.79e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1039795032 240 NVNALTQKRLSCLHYAALGGSEDLSRALIKAGGCTNVADKQGTTPMHLA 288
Cdd:pfam13857   8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 48-78 1.86e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 35.73  E-value: 1.86e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1039795032  48 GRVALHWAAG-AGHEQAVRLLLERGAAVDDVD 78
Cdd:pfam00023   2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 214-243 2.26e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.64  E-value: 2.26e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1039795032  214 EGLTALHAAAEGIHADCVMLLLGAGSNVNA 243
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02743 PHA02743
Viral ankyrin protein; Provisional
 146-224 3.30e-03

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 38.26  E-value: 3.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 146 DKLGRTAFHRAAEHGQLDA---LDFLVGSGCDHSVKDKG-GNTALHLAASQGHVDVLQRLV-DIGLDLEEQNTEGLTALH 220
Cdd:PHA02743   54 DHHGRQCTHMVAWYDRANAvmkIELLVNMGADINARELGtGNTLLHIAASTKNYELAEWLCrQLGVNLGAINYQHETAYH 133


                  ....
gi 1039795032 221 AAAE 224
Cdd:PHA02743  134 IAYK 137
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 182-212 3.89e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 34.96  E-value: 3.89e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1039795032 182 GNTALHLAASQ-GHVDVLQRLVDIGLDLEEQN 212
Cdd:pfam00023   2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
PHA02798 PHA02798
ankyrin-like protein; Provisional
 162-378 4.45e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 39.43  E-value: 4.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 162 LDALDFLVGSGCDHSVKDKGGNTALHLAASQGHVDVLQRL---VDIGLDLEEQNTEGLTALHA---AAEGIHADCVMLLL 235
Cdd:PHA02798   89 LDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILlfmIENGADTTLLDKDGFTMLQVylqSNHHIDIEIIKLLL 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 236 GAGSNVNALTQK----RLSC-LHYAALGGSEDLSRALIKAGGCTNVADKQGTTPMH------LAVKHNFPGLVQLLIDGH 304
Cdd:PHA02798  169 EKGVDINTHNNKekydTLHCyFKYNIDRIDADILKLFVDNGFIINKENKSHKKKFMeylnslLYDNKRFKKNILDFIFSY 248

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039795032 305 SDLDAVDIRRQTPLHLAAEHAWQDVADMLLIAGADLSLRDKQGKTALAVAARSNHVSLVDMIIKAD--------RFYRWE 376
Cdd:PHA02798  249 IDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILNKKpnkntisyTYYKLR 328


                  ..
gi 1039795032 377 KD 378
Cdd:PHA02798  329 KH 330
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 214-245 5.94e-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: 5.94e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1039795032 214 EGLTALHAAAEGI-HADCVMLLLGAGSNVNALT 245
Cdd:pfam00023   1 DGNTPLHLAAGRRgNLEIVKLLLSKGADVNARD 33
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 182-208 6.28e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 34.16  E-value: 6.28e-03
                          10        20
                  ....*....|....*....|....*..
gi 1039795032 182 GNTALHLAASQGHVDVLQRLVDIGLDL 208
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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