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Conserved domains on  [gi|1039780073|ref|XP_017167826|]
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ankyrin repeat domain-containing protein 42 isoform X4 [Mus musculus]

Protein Classification

ankyrin repeat domain-containing protein( domain architecture ID 11429852)

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

Gene Ontology:  GO:0005515
PubMed:  17176038
SCOP:  4000366

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
30-195 3.28e-33

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 120.06  E-value: 3.28e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780073  30 IHDAVRAGDVKQLSDIVERGANLNEVDAlHQFTPLHWAAHSGSLECLHWLLWSGADATQTTTRGWTAAHIAAIRGQDACL 109
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGADVNARDK-DGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIV 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780073 110 QALIINGANLATQDDRGCTPLHLAATHGHSFSLQIMLRSGVDPSVTDKREWKPVHYASFHGRLGCLQLLVKWGCGIEDVD 189
Cdd:COG0666   170 KLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKD 249


                  ....*.
gi 1039780073 190 YNGNLP 195
Cdd:COG0666   250 KDGLTA 255
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
30-195 3.28e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 120.06  E-value: 3.28e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780073  30 IHDAVRAGDVKQLSDIVERGANLNEVDAlHQFTPLHWAAHSGSLECLHWLLWSGADATQTTTRGWTAAHIAAIRGQDACL 109
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGADVNARDK-DGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIV 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780073 110 QALIINGANLATQDDRGCTPLHLAATHGHSFSLQIMLRSGVDPSVTDKREWKPVHYASFHGRLGCLQLLVKWGCGIEDVD 189
Cdd:COG0666   170 KLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKD 249


                  ....*.
gi 1039780073 190 YNGNLP 195
Cdd:COG0666   250 KDGLTA 255
Ank_2 pfam12796
Ankyrin repeats (3 copies);
64-156 4.61e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 82.86  E-value: 4.61e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780073  64 LHWAAHSGSLECLHWLLWSGADATQTTTRGWTAAHIAAIRGQDACLQALiINGANLATQDDrGCTPLHLAATHGHSFSLQ 143
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL-LEHADVNLKDN-GRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1039780073 144 IMLRSGVDPSVTD 156
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 28-158 1.70e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 70.79  E-value: 1.70e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780073  28 SSIHDAVRAGDVKQLSDIVERGANLNEVDALHQFTPLHWAAHSGSLECLHWLLWSGADATQTTTRGWTAAHIAAIRGQDA 107
Cdd:PHA02875   70 SELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIK 149

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1039780073 108 CLQALIINGANLATQDDRGCTPLHLAATHGHSFSLQIMLRSGVDPSVTDKR 158
Cdd:PHA02875  150 GIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKN 200
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 59-85 2.79e-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: 2.79e-04
                           10        20
                   ....*....|....*....|....*..
gi 1039780073   59 HQFTPLHWAAHSGSLECLHWLLWSGAD 85
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 62-132 4.61e-04

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 40.38  E-value: 4.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780073  62 TPLHWAAHSGSLECLHWLLWSGAD-----ATQTTTRG------WTAAHI---AAIRGQDACLQALIINGANLATQDDRGC 127
Cdd:cd22192    91 TALHIAVVNQNLNLVRELIARGADvvsprATGTFFRPgpknliYYGEHPlsfAACVGNEEIVRLLIEHGADIRAQDSLGN 170


                  ....*
gi 1039780073 128 TPLHL 132
Cdd:cd22192   171 TVLHI 175
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 62-134 6.12e-04

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 40.06  E-value: 6.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780073  62 TPLHWAAHSGSLECLHWLLWSGA--------DATQTTTRGWTAAH------IAAIRGQDACLQALIINGANLATQDDRGC 127
Cdd:TIGR00870 130 TALHLAAHRQNYEIVKLLLERGAsvparacgDFFVKSQGVDSFYHgesplnAAACLGSPSIVALLSEDPADILTADSLGN 209


                  ....*..
gi 1039780073 128 TPLHLAA 134
Cdd:TIGR00870 210 TLLHLLV 216
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
30-195 3.28e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 120.06  E-value: 3.28e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780073  30 IHDAVRAGDVKQLSDIVERGANLNEVDAlHQFTPLHWAAHSGSLECLHWLLWSGADATQTTTRGWTAAHIAAIRGQDACL 109
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGADVNARDK-DGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIV 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780073 110 QALIINGANLATQDDRGCTPLHLAATHGHSFSLQIMLRSGVDPSVTDKREWKPVHYASFHGRLGCLQLLVKWGCGIEDVD 189
Cdd:COG0666   170 KLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKD 249


                  ....*.
gi 1039780073 190 YNGNLP 195
Cdd:COG0666   250 KDGLTA 255
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
30-195 3.27e-31

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 115.05  E-value: 3.27e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780073  30 IHDAVRAGDVKQLSDIVERGANLNEVDAlHQFTPLHWAAHSGSLECLHWLLWSGADATQTTTRGWTAAHIAAIRGQDACL 109
Cdd:COG0666    58 LLAAALAGDLLVALLLLAAGADINAKDD-GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIV 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780073 110 QALIINGANLATQDDRGCTPLHLAATHGHSFSLQIMLRSGVDPSVTDKREWKPVHYASFHGRLGCLQLLVKWGCGIEDVD 189
Cdd:COG0666   137 KLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKD 216


                  ....*.
gi 1039780073 190 YNGNLP 195
Cdd:COG0666   217 NDGKTA 222
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
17-194 3.40e-26

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 101.57  E-value: 3.40e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780073  17 ADSSSRKKVHFSSIHDAVRAGDVKQLSDIVERGANLNEVDAlHQFTPLHWAAHSGSLECLHWLLWSGADATQTTTRGWTA 96
Cdd:COG0666   111 ADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDN-DGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETP 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780073  97 AHIAAIRGQDACLQALIINGANLATQDDRGCTPLHLAATHGHSFSLQIMLRSGVDPSVTDKREWKPVHYASFHGRLGCLQ 176
Cdd:COG0666   190 LHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVK 269

                         170
                  ....*....|....*...
gi 1039780073 177 LLVKWGCGIEDVDYNGNL 194
Cdd:COG0666   270 LLLLALLLLAAALLDLLT 287
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
49-195 3.52e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 91.17  E-value: 3.52e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780073  49 GANLNEVDALHQFTPLHWAAHSGSLECLHWLLWSGADATQTTTRGWTAAHIAAIRGQDACLQALIINGANLATQDDRGCT 128
Cdd:COG0666    43 ALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGET 122

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039780073 129 PLHLAATHGHSFSLQIMLRSGVDPSVTDKREWKPVHYASFHGRLGCLQLLVKWGCGIEDVDYNGNLP 195
Cdd:COG0666   123 PLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETP 189
Ank_2 pfam12796
Ankyrin repeats (3 copies);
64-156 4.61e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 82.86  E-value: 4.61e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780073  64 LHWAAHSGSLECLHWLLWSGADATQTTTRGWTAAHIAAIRGQDACLQALiINGANLATQDDrGCTPLHLAATHGHSFSLQ 143
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL-LEHADVNLKDN-GRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1039780073 144 IMLRSGVDPSVTD 156
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 28-158 1.70e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 70.79  E-value: 1.70e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780073  28 SSIHDAVRAGDVKQLSDIVERGANLNEVDALHQFTPLHWAAHSGSLECLHWLLWSGADATQTTTRGWTAAHIAAIRGQDA 107
Cdd:PHA02875   70 SELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIK 149

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1039780073 108 CLQALIINGANLATQDDRGCTPLHLAATHGHSFSLQIMLRSGVDPSVTDKR 158
Cdd:PHA02875  150 GIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKN 200
PHA03095 PHA03095
ankyrin-like protein; Provisional
 17-195 1.59e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 68.13  E-value: 1.59e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780073  17 ADSSSRKKVHFSSIH-----DAVRAGDVKQLsdiVERGANLNEVDaLHQFTPLHW--AAHSGSLECLHWLLWSGADATQT 89
Cdd:PHA03095  108 ADVNAKDKVGRTPLHvylsgFNINPKVIRLL---LRKGADVNALD-LYGMTPLAVllKSRNANVELLRLLIDAGADVYAV 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780073  90 TTRGWTAAHIAA--IRGQDACLQALIINGANLATQDDRGCTPLHLAATHGHSFSLQI--MLRSGVDPSVTDKREWKPVHY 165
Cdd:PHA03095  184 DDRFRSLLHHHLqsFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHY 263

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1039780073 166 AS-FHGRLGCLQLLvKWGCGIEDVDYNGNLP 195
Cdd:PHA03095  264 AAvFNNPRACRRLI-ALGADINAVSSDGNTP 293
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
42-195 1.26e-12

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 64.98  E-value: 1.26e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780073  42 LSDIVERGANLNEVDALHQFTPLHWAAHSGSLECLHWLLWSGADATQTTTRGWTAAHIAAIRGQDACLQALIINGANLAT 121
Cdd:COG0666     3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039780073 122 QDDRGCTPLHLAATHGHSFSLQIMLRSGVDPSVTDKREWKPVHYASFHGRLGCLQLLVKWGCGIEDVDYNGNLP 195
Cdd:COG0666    83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTP 156
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 30-166 3.48e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 64.21  E-value: 3.48e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780073  30 IHDAVRAGDVKQLSDIVERGANLNeVDALHQFTPLHWAAHSGSLECLHWLLWSGADATQTTTRGWTAAHIAAIRGQDACL 109
Cdd:PHA02874  128 LHYAIKKGDLESIKMLFEYGADVN-IEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACI 206

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039780073 110 QALIINGANLATQDDRGCTPLHLAATHGHS-FSLQIMLRSgvdPSVTDKREWKPVHYA 166
Cdd:PHA02874  207 KLLIDHGNHIMNKCKNGFTPLHNAIIHNRSaIELLINNAS---INDQDIDGSTPLHHA 261
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 45-195 6.21e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 63.44  E-value: 6.21e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780073  45 IVERGANLNEVDALHQfTPLHWAAHSGSLECLHWLLWSGADATQTTTRGWTAAHIAAIRGQDACLQALIINGANLATQDD 124
Cdd:PHA02874  110 ILDCGIDVNIKDAELK-TFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDN 188

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039780073 125 RGCTPLHLAATHGHSFSLQIMLRSGVDPSVTDKREWKPVHYASFHGRlGCLQLLVKwGCGIEDVDYNGNLP 195
Cdd:PHA02874  189 NGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLIN-NASINDQDIDGSTP 257
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 29-186 4.04e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 61.23  E-value: 4.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780073  29 SIHDAVRAGDVKQLSDIVERGANLNEVDaLHQFTPLHWAAHSGSLECL-HWLLWSGADATQTTTRGWTAAHIAAIRGQDA 107
Cdd:PHA02876  243 SLLKAIRNEDLETSLLLYDAGFSVNSID-DCKNTPLHHASQAPSLSRLvPKLLERGADVNAKNIKGETPLYLMAKNGYDT 321

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780073 108 -CLQALIINGANLATQDDRGCTPLHLAATHGHSFSLQI-MLRSGVDPSVTDKREWKPVHYASFHGRLGCLQLLVKWGCGI 185
Cdd:PHA02876  322 eNIRTLIMLGADVNAADRLYITPLHQASTLDRNKDIVItLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADI 401


                  .
gi 1039780073 186 E 186
Cdd:PHA02876  402 E 402
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 30-166 7.34e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 60.36  E-value: 7.34e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780073  30 IHDAVRAGDVKQLSDIVERGANLNeVDALHQFTPLHWAAHSGSLECLHWLLWSGADATQTTTRGWTAAHIAAIRGQDACl 109
Cdd:PHA02874  161 IHIAIKHNFFDIIKLLLEKGAYAN-VKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAI- 238

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039780073 110 qALIINGANLATQDDRGCTPLHLAATHGHSFS-LQIMLRSGVDPSVTDKREWKPVHYA 166
Cdd:PHA02874  239 -ELLINNASINDQDIDGSTPLHHAINPPCDIDiIDILLYHKADISIKDNKGENPIDTA 295
Ank_4 pfam13637
Ankyrin repeats (many copies);
62-113 3.58e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.43  E-value: 3.58e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039780073  62 TPLHWAAHSGSLECLHWLLWSGADATQTTTRGWTAAHIAAIRGQDACLQALI 113
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 32-195 2.05e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 56.13  E-value: 2.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780073  32 DAVRAGDVKQLSDIVERGANLNEVDAlHQFTPLHWAAHSGSLECLHWLLWSGADAT--------------------QTTT 91
Cdd:PHA02874   41 DAIRSGDAKIVELFIKHGADINHINT-KIPHPLLTAIKIGAHDIIKLLIDNGVDTSilpipciekdmiktildcgiDVNI 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780073  92 RGW---TAAHIAAIRGQDACLQALIINGANLATQDDRGCTPLHLAATHGHSFSLQIMLRSGVDPSVTDKREWKPVHYASF 168
Cdd:PHA02874  120 KDAelkTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAE 199

                         170       180
                  ....*....|....*....|....*..
gi 1039780073 169 HGRLGCLQLLVKWGCGIEDVDYNGNLP 195
Cdd:PHA02874  200 YGDYACIKLLIDHGNHIMNKCKNGFTP 226
Ank_4 pfam13637
Ankyrin repeats (many copies);
93-138 1.74e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.81  E-value: 1.74e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1039780073  93 GWTAAHIAAIRGQDACLQALIINGANLATQDDRGCTPLHLAATHGH 138
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGN 46
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 26-189 1.74e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 53.13  E-value: 1.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780073  26 HFSSIHDAVrAGDVKQLSDI-VERGANLNEVDAlHQFTPLHWAA--HSGSLECLHWLLWSGADATQTTTRGWTAAHIAAI 102
Cdd:PHA03100   73 HYLSNIKYN-LTDVKEIVKLlLEYGANVNAPDN-NGITPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLE 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780073 103 RGQ----------------DAC--LQALIINGANLATQDDRGCTPLHLAATHGHSFSLQIMLRSGVDPSVTDKREWKPVH 164
Cdd:PHA03100  151 SNKidlkilkllidkgvdiNAKnrVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLH 230

                         170       180
                  ....*....|....*....|....*..
gi 1039780073 165 YA--SFHGRLgcLQLLVKWGCGIEDVD 189
Cdd:PHA03100  231 IAilNNNKEI--FKLLLNNGPSIKTII 255
Ank_4 pfam13637
Ankyrin repeats (many copies);
128-179 5.30e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.65  E-value: 5.30e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039780073 128 TPLHLAATHGHSFSLQIMLRSGVDPSVTDKREWKPVHYASFHGRLGCLQLLV 179
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
130-180 9.32e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 48.19  E-value: 9.32e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1039780073 130 LHLAATHGHSFSLQIMLRSGVDPSVTDKREWKPVHYASFHGRLGCLQLLVK 180
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE 51
Ank_4 pfam13637
Ankyrin repeats (many copies);
28-80 1.12e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.88  E-value: 1.12e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1039780073  28 SSIHDAVRAGDVKQLSDIVERGANLNEVDALhQFTPLHWAAHSGSLECLHWLL 80
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGN-GETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 98-195 1.28e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.05  E-value: 1.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780073  98 HIAAiRGQDACLQALIINGANLATQDDRGCTPLHLAATHGHSFSLQIMLRSGVDPSVTDKREWKPVHYASFHGRLGCLQL 177
Cdd:PTZ00322   88 QLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166

                          90
                  ....*....|....*...
gi 1039780073 178 LVkwGCGIEDVDYNGNLP 195
Cdd:PTZ00322  167 LS--RHSQCHFELGANAK 182
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 17-187 1.29e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 50.83  E-value: 1.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780073  17 ADSSSRKKVHFSSIHdavRAGDVKQLSDIV----ERGANLNEVDALHQfTPLHWAAHSGSLECLHWLLWSGADATQTTTR 92
Cdd:PHA02876  332 ADVNAADRLYITPLH---QASTLDRNKDIVitllELGANVNARDYCDK-TPIHYAAVRNNVVIINTLLDYGADIEALSQK 407

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780073  93 GWTAAHIaAIRGQD--ACLQALIINGANLATQDDRGCTPLHLAATHGHSFS-LQIMLRSGVDPSVTDKREWKPVHYA-SF 168
Cdd:PHA02876  408 IGTALHF-ALCGTNpyMSVKTLIDRGANVNSKNKDLSTPLHYACKKNCKLDvIEMLLDNGADVNAINIQNQYPLLIAlEY 486

                         170
                  ....*....|....*....
gi 1039780073 169 HgrlGCLQLLVKWGCGIED 187
Cdd:PHA02876  487 H---GIVNILLHYGAELRD 502
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 45-195 1.55e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 50.65  E-value: 1.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780073  45 IVERGANLNEVDALHQFTPLHWAAHSGSLECLHWLLWSGADATQTTTRGWTAAHIAAIRGQDACLQALIINGANLATQDD 124
Cdd:PHA02878  153 LLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDK 232

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039780073 125 RGCTPLHLAATHGHSFS-LQIMLRSGVDPSVTDK-REWKPVHYASFHGRLgcLQLLVKWGCGIEDVDYNGNLP 195
Cdd:PHA02878  233 CGNTPLHISVGYCKDYDiLKLLLEHGVDVNAKSYiLGLTALHSSIKSERK--LKLLLEYGADINSLNSYKLTP 303
PHA03095 PHA03095
ankyrin-like protein; Provisional
 38-195 3.06e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 49.64  E-value: 3.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780073  38 DVKQLSDIVERGANLNEVDaLHQFTPLH-WAAHSGSLECLHWLLWSGADATQTTTRGWTAAHIAAiRGQ--DAC-LQALI 113
Cdd:PHA03095   62 VKDIVRLLLEAGADVNAPE-RCGFTPLHlYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVYL-SGFniNPKvIRLLL 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780073 114 INGANLATQDDRGCTPLH-LAATHGHSFS-LQIMLRSGVDPSVTDKREWKPVHY--ASFHGRLGCLQLLVKWGCGIEDVD 189
Cdd:PHA03095  140 RKGADVNALDLYGMTPLAvLLKSRNANVElLRLLIDAGADVYAVDDRFRSLLHHhlQSFKPRARIVRELIRAGCDPAATD 219


                  ....*.
gi 1039780073 190 YNGNLP 195
Cdd:PHA03095  220 MLGNTP 225
Ank_5 pfam13857
Ankyrin repeats (many copies);
45-100 3.22e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.42  E-value: 3.22e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039780073  45 IVERGANLNEVDALHQFTPLHWAAHSGSLECLHWLLWSGADATQTTTRGWTAAHIA 100
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA03095 PHA03095
ankyrin-like protein; Provisional
 14-156 2.01e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 47.33  E-value: 2.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780073  14 RETADSSSRKKVHFSSIHDAVRAG--DVKQLSDIVERGANLNEVDALHQfTPLHWAAHS--GSLECLHWLLWSGADATQT 89
Cdd:PHA03095  140 RKGADVNALDLYGMTPLAVLLKSRnaNVELLRLLIDAGADVYAVDDRFR-SLLHHHLQSfkPRARIVRELIRAGCDPAAT 218

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039780073  90 TTRGWTAAHIAAIRG--QDACLQALIINGANLATQDDRGCTPLHLAATHGHSFSLQIMLRSGVDPSVTD 156
Cdd:PHA03095  219 DMLGNTPLHSMATGSscKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVS 287
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 34-195 3.06e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 46.50  E-value: 3.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780073  34 VRAGDVKQLSDIVERGANLNEVDALHQFTPLHWAAHSGSLECLHWLLWSGADATQTTTRG----WTAAHIAA-------- 101
Cdd:PHA02874    9 IYSGDIEAIEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIphplLTAIKIGAhdiiklli 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780073 102 IRGQDA------CLQALIIN-----GANLATQDDRGCTPLHLAATHGHSFSLQIMLRSGVDPSVTDKREWKPVHYASFHG 170
Cdd:PHA02874   89 DNGVDTsilpipCIEKDMIKtildcGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHN 168

                         170       180
                  ....*....|....*....|....*
gi 1039780073 171 RLGCLQLLVKWGCGIEDVDYNGNLP 195
Cdd:PHA02874  169 FFDIIKLLLEKGAYANVKDNNGESP 193
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
31-130 4.79e-06

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 45.72  E-value: 4.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780073  31 HDAVRAGD---VKQLsdiVERGANLNEVDALHQfTPLHWAAHSGSLECLHWLLWSGADATQTTTRGWTAAHIAAIRGQDA 107
Cdd:COG0666   191 HLAAENGHleiVKLL---LEAGADVNAKDNDGK-TALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAAL 266

                          90       100
                  ....*....|....*....|...
gi 1039780073 108 CLQALIINGANLATQDDRGCTPL 130
Cdd:COG0666   267 IVKLLLLALLLLAAALLDLLTLL 289
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 133-193 5.00e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 46.40  E-value: 5.00e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039780073 133 AATHGHSFSLQIMLRSGVDPSVTDKREWKPVHYASFHGRLGCLQLLVKWGCGIEDVDYNGN 193
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGN 592
Ank_5 pfam13857
Ankyrin repeats (many copies);
117-166 6.40e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 6.40e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039780073 117 ANLATQDDRGCTPLHLAATHGHSFSLQIMLRSGVDPSVTDKREWKPVHYA 166
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 67-192 8.26e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 45.63  E-value: 8.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780073  67 AAHSGSLECLHWLLWSGADATQTTTRGWTAAHIAAIRGQDACLQALIINGANLATQDDRGCTPL--HLAATHGHSFSLQI 144
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALwnAISAKHHKIFRILY 611

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1039780073 145 MLRSGVDPSVTDKRewkpVHYASFHGRLGCLQLLVKWGCGIEDVDYNG 192
Cdd:PLN03192  612 HFASISDPHAAGDL----LCTAAKRNDLTAMKELLKQGLNVDSEDHQG 655
Ank_2 pfam12796
Ankyrin repeats (3 copies);
17-89 1.46e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 42.03  E-value: 1.46e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039780073  17 ADSSSRKKVHFSSIHDAVRAGDVkqlsDIVE---RGANLNEVDalHQFTPLHWAAHSGSLECLHWLLWSGADATQT 89
Cdd:pfam12796  21 ADANLQDKNGRTALHLAAKNGHL----EIVKlllEHADVNLKD--NGRTALHYAARSGHLEIVKLLLEKGADINVK 90
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 27-195 2.00e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 44.10  E-value: 2.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780073  27 FSSIHDAVRAGDVKQLSDIVERGANLNEVDalHQF-TPLHW-------------------------------AAHSGSLE 74
Cdd:PHA02878   38 FIPLHQAVEARNLDVVKSLLTRGHNVNQPD--HRDlTPLHIickepnklgmkemirsinkcsvfytlvaikdAFNNRNVE 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780073  75 CLHWLLWSGADATQTTTrgwtaahIAAIR--GQDACLQALIIN-----GANLATQD-DRGCTPLHLAATHGHSFSLQIML 146
Cdd:PHA02878  116 IFKIILTNRYKNIQTID-------LVYIDkkSKDDIIEAEITKlllsyGADINMKDrHKGNTALHYATENKDQRLTELLL 188

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1039780073 147 RSGVDPSVTDKREWKPVHYASFHGRLGCLQLLVKWGCGIEDVDYNGNLP 195
Cdd:PHA02878  189 SYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTP 237
Ank_5 pfam13857
Ankyrin repeats (many copies);
84-133 3.89e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.02  E-value: 3.89e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039780073  84 ADATQTTTRGWTAAHIAAIRGQDACLQALIINGANLATQDDRGCTPLHLA 133
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 28-133 2.19e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 41.02  E-value: 2.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780073  28 SSIHDAVRAGDVKQLSDIVERGANLNEVDaLHQFTPLHWAAHS-GSLECLHWLLWSGADAT-QTTTRGWTAAHIaAIRGQ 105
Cdd:PHA02878  203 SPLHHAVKHYNKPIVHILLENGASTDARD-KCGNTPLHISVGYcKDYDILKLLLEHGVDVNaKSYILGLTALHS-SIKSE 280

                          90       100
                  ....*....|....*....|....*...
gi 1039780073 106 DAcLQALIINGANLATQDDRGCTPLHLA 133
Cdd:PHA02878  281 RK-LKLLLEYGADINSLNSYKLTPLSSA 307
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 26-167 2.21e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 41.20  E-value: 2.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780073  26 HFSSIHDAVRAGDVKQLSDIVERGANLNEVDaLHQFTPLHWAAHSGSLECLHWLLWSGADATQTTTRGWTAAHIAAIRGQ 105
Cdd:PHA02876  145 YMKLIKERIQQDELLIAEMLLEGGADVNAKD-IYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKN 223

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039780073 106 DACLQALIINGANLATQDdrgCTPLHLAATHGHSFSLqIMLRSGVDPSVTDKREWKPVHYAS 167
Cdd:PHA02876  224 IDTIKAIIDNRSNINKND---LSLLKAIRNEDLETSL-LLYDAGFSVNSIDDCKNTPLHHAS 281
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 59-85 2.79e-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: 2.79e-04
                           10        20
                   ....*....|....*....|....*..
gi 1039780073   59 HQFTPLHWAAHSGSLECLHWLLWSGAD 85
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 62-132 4.61e-04

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 40.38  E-value: 4.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780073  62 TPLHWAAHSGSLECLHWLLWSGAD-----ATQTTTRG------WTAAHI---AAIRGQDACLQALIINGANLATQDDRGC 127
Cdd:cd22192    91 TALHIAVVNQNLNLVRELIARGADvvsprATGTFFRPgpknliYYGEHPlsfAACVGNEEIVRLLIEHGADIRAQDSLGN 170


                  ....*
gi 1039780073 128 TPLHL 132
Cdd:cd22192   171 TVLHI 175
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 62-155 5.49e-04

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 40.00  E-value: 5.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780073  62 TPLHWAAHSGSLECLHWLLWS-GADATQTTTRGWTAAHIAAIRGQDACLQALIING---ANLATQDD--RGCTPLHLAAT 135
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKCpSCDLFQRGALGETALHVAALYDNLEAAVVLMEAApelVNEPMTSDlyQGETALHIAVV 98

                          90       100
                  ....*....|....*....|...
gi 1039780073 136 HGHSFSLQIMLRSGVD---PSVT 155
Cdd:cd22192    99 NQNLNLVRELIARGADvvsPRAT 121
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 62-134 6.12e-04

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 40.06  E-value: 6.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780073  62 TPLHWAAHSGSLECLHWLLWSGA--------DATQTTTRGWTAAH------IAAIRGQDACLQALIINGANLATQDDRGC 127
Cdd:TIGR00870 130 TALHLAAHRQNYEIVKLLLERGAsvparacgDFFVKSQGVDSFYHgesplnAAACLGSPSIVALLSEDPADILTADSLGN 209


                  ....*..
gi 1039780073 128 TPLHLAA 134
Cdd:TIGR00870 210 TLLHLLV 216
PHA02946 PHA02946
ankyin-like protein; Provisional
 101-197 7.62e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 39.65  E-value: 7.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780073 101 AIRGQDA-CLQALIINGANLATQDDRGCTPLHLAATHGHSFSLQIMLRSGVDPSVTDKREWKPVHYASFHGR--LGCLQL 177
Cdd:PHA02946   46 GIKGLDErFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINL 125

                          90       100
                  ....*....|....*....|.
gi 1039780073 178 LVKWGCGIED-VDYNGNLPEL 197
Cdd:PHA02946  126 LVQYGAKINNsVDEEGCGPLL 146
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 59-85 1.05e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 35.31  E-value: 1.05e-03
                          10        20
                  ....*....|....*....|....*..
gi 1039780073  59 HQFTPLHWAAHSGSLECLHWLLWSGAD 85
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGAD 27
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 125-157 1.58e-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: 1.58e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1039780073 125 RGCTPLHLAATH-GHSFSLQIMLRSGVDPSVTDK 157
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 32-180 1.72e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 38.43  E-value: 1.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780073  32 DAVRAGDVKQLSDIVERGANLNeVDALHQFTPLHWAAHSGSLECLHWLLWSGADATQTTTRGWTAAHIAAIRGQDACLQA 111
Cdd:PHA02875    8 DAILFGELDIARRLLDIGINPN-FEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEE 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039780073 112 LIINGANLatqDD----RGCTPLHLAATHGHSFSLQIMLRSGVDPSVTDKREWKPVHYASFHGRLGCLQLLVK 180
Cdd:PHA02875   87 LLDLGKFA---DDvfykDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLID 156
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 125-154 1.96e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.49  E-value: 1.96e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1039780073  125 RGCTPLHLAATHGHSFSLQIMLRSGVDPSV 154
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA03095 PHA03095
ankyrin-like protein; Provisional
 111-195 2.38e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 38.08  E-value: 2.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780073 111 ALIINGANLATQDDRGCTPLHlaaTHGHSFS------LQIMLRSGVDPSVTDKREWKPVH-YASFHGRLGCLQLLVKWGC 183
Cdd:PHA03095   32 RLLAAGADVNFRGEYGKTPLH---LYLHYSSekvkdiVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGA 108

                          90
                  ....*....|..
gi 1039780073 184 GIEDVDYNGNLP 195
Cdd:PHA03095  109 DVNAKDKVGRTP 120
PHA03095 PHA03095
ankyrin-like protein; Provisional
 79-193 2.52e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 38.08  E-value: 2.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780073  79 LLWSGADATQTTTRGWTAAHIAAIRGQDAC---LQALIINGANLATQDDRGCTPLHLAATHG------------------ 137
Cdd:PHA03095   33 LLAAGADVNFRGEYGKTPLHLYLHYSSEKVkdiVRLLLEAGADVNAPERCGFTPLHLYLYNAttldvikllikagadvna 112

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039780073 138 ------------------HSFSLQIMLRSGVDPSVTDKREWKPVH-YASFHG-RLGCLQLLVKWGCGIEDVDYNGN 193
Cdd:PHA03095  113 kdkvgrtplhvylsgfniNPKVIRLLLRKGADVNALDLYGMTPLAvLLKSRNaNVELLRLLIDAGADVYAVDDRFR 188
PHA03095 PHA03095
ankyrin-like protein; Provisional
 25-138 2.92e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 37.70  E-value: 2.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780073  25 VHFSSIHDavRAGDVKQLsdiVERGANLNEVDALHQfTPLHWAAHSGSLECLHW--LLWSGADATQTTTRGWTAAHIAAI 102
Cdd:PHA03095  193 HHLQSFKP--RARIVREL---IRAGCDPAATDMLGN-TPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAV 266

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1039780073 103 RGQDACLQALIINGANLATQDDRGCTPLHLAATHGH 138
Cdd:PHA03095  267 FNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNN 302
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 12-103 3.93e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 37.28  E-value: 3.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039780073  12 SRRETADSSSRKKvhFSSIHDAVRAGDVKQLSDIVERGANLNEVDAlHQFTPLHWAAHSGSLECLHWLLWSGADATQTTT 91
Cdd:PHA02875  123 ARGADPDIPNTDK--FSPLHLAVMMGDIKGIELLIDHKACLDIEDC-CGCTPLIIAMAKGDIAICKMLLDSGANIDYFGK 199

                          90
                  ....*....|..
gi 1039780073  92 RGWTAAHIAAIR 103
Cdd:PHA02875  200 NGCVAALCYAIE 211
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 59-90 5.96e-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: 33.42  E-value: 5.96e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1039780073  59 HQFTPLHWAA-HSGSLECLHWLLWSGADATQTT 90
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
 
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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