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Conserved domains on  [gi|1207115676|ref|XP_021336623|]
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ankyrin repeat domain-containing protein 2-like [Danio rerio]

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
112-276 1.71e-39

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 140.09  E-value: 1.71e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115676 112 FLKAAAQGKMEVVERFLDDGGDPNTCDEFRKTALHRAALQNHTKIVEKLLDKGADINFKDRLGCRAVHWACRGGSLSALT 191
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115676 192 VLQDRGADINVRDKLLSSPLHVATRTGHSDVVQHLLDSGININAKDWEGDTVLHDAVRFNRYKIVKQLILAGADMQIKNA 271
Cdd:COG0666   171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250


                  ....*
gi 1207115676 272 EGITA 276
Cdd:COG0666   251 DGLTA 255
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
112-276 1.71e-39

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 140.09  E-value: 1.71e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115676 112 FLKAAAQGKMEVVERFLDDGGDPNTCDEFRKTALHRAALQNHTKIVEKLLDKGADINFKDRLGCRAVHWACRGGSLSALT 191
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115676 192 VLQDRGADINVRDKLLSSPLHVATRTGHSDVVQHLLDSGININAKDWEGDTVLHDAVRFNRYKIVKQLILAGADMQIKNA 271
Cdd:COG0666   171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250


                  ....*
gi 1207115676 272 EGITA 276
Cdd:COG0666   251 DGLTA 255
PHA03095 PHA03095
ankyrin-like protein; Provisional
 112-282 3.80e-25

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 104.34  E-value: 3.80e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115676 112 FLKAAAQGKMEVVERFLDDGGDPNTCDEFRKTALH---RAALQNHTKIVEKLLDKGADINFKDRLGCRAVH-WACRGGSL 187
Cdd:PHA03095   18 YLLNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHlylHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHlYLYNATTL 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115676 188 SALTVLQDRGADINVRDKLLSSPLHV--ATRTGHSDVVQHLLDSGININAKDWEGDTVLHDAVRFNR--YKIVKQLILAG 263
Cdd:PHA03095   98 DVIKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanVELLRLLIDAG 177

                         170
                  ....*....|....*....
gi 1207115676 264 ADMQIKNAEGITATEQVKQ 282
Cdd:PHA03095  178 ADVYAVDDRFRSLLHHHLQ 196
Ank_2 pfam12796
Ankyrin repeats (3 copies);
145-237 1.36e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 81.70  E-value: 1.36e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115676 145 LHRAALQNHTKIVEKLLDKGADINFKDRLGCRAVHWACRGGSLSALTVLQDRgADINVRDKLLsSPLHVATRTGHSDVVQ 224
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGR-TALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1207115676 225 HLLDSGININAKD 237
Cdd:pfam12796  79 LLLEKGADINVKD 91
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 113-275 3.28e-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: 54.63  E-value: 3.28e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115676 113 LKAAAQGKMEVVERFLDDggdpNTCDEFRK-----TALHRAALQNHTKIVEKLLDKGADINFKD-----RLGCRAVHWAC 182
Cdd:cd22192    22 LLAAKENDVQAIKKLLKC----PSCDLFQRgalgeTALHVAALYDNLEAAVVLMEAAPELVNEPmtsdlYQGETALHIAV 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115676 183 RGGSLSALTVLQDRGADINV-----------RDKLL---SSPLHVATRTGHSDVVQHLLDSGININAKDWEGDTVLHDAV 248
Cdd:cd22192    98 VNQNLNLVRELIARGADVVSpratgtffrpgPKNLIyygEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILV 177

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1207115676 249 RFNRYKIVKQ---LILA----GADM---QIKNAEGIT 275
Cdd:cd22192   178 LQPNKTFACQmydLILSydkeDDLQpldLVPNNQGLT 214
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 133-248 3.05e-05

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: 45.46  E-value: 3.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115676 133 DPNTCDEFR-KTALHRAALQNHTKIVEKLLDKGADINFkdRLGCRAVHWACRGGSLSaltvlqdrgadinvrdkLLSSPL 211
Cdd:TIGR00870 119 DQYTSEFTPgITALHLAAHRQNYEIVKLLLERGASVPA--RACGDFFVKSQGVDSFY-----------------HGESPL 179

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1207115676 212 HVATRTGHSDVVQHLLDSGININAKDWEGDTVLHDAV 248
Cdd:TIGR00870 180 NAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLV 216
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 209-235 9.63e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 38.72  E-value: 9.63e-05
                           10        20
                   ....*....|....*....|....*..
gi 1207115676  209 SPLHVATRTGHSDVVQHLLDSGININA 235
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
112-276 1.71e-39

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 140.09  E-value: 1.71e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115676 112 FLKAAAQGKMEVVERFLDDGGDPNTCDEFRKTALHRAALQNHTKIVEKLLDKGADINFKDRLGCRAVHWACRGGSLSALT 191
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115676 192 VLQDRGADINVRDKLLSSPLHVATRTGHSDVVQHLLDSGININAKDWEGDTVLHDAVRFNRYKIVKQLILAGADMQIKNA 271
Cdd:COG0666   171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250


                  ....*
gi 1207115676 272 EGITA 276
Cdd:COG0666   251 DGLTA 255
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
96-276 3.52e-39

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 139.32  E-value: 3.52e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115676  96 LSKDITNVSGAVEPEEFLKAAAQGKMEVVERFLDDGGDPNTCDEFRKTALHRAALQNHTKIVEKLLDKGADINFKDRLGC 175
Cdd:COG0666    42 LALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGE 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115676 176 RAVHWACRGGSLSALTVLQDRGADINVRDKLLSSPLHVATRTGHSDVVQHLLDSGININAKDWEGDTVLHDAVRFNRYKI 255
Cdd:COG0666   122 TPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEI 201

                         170       180
                  ....*....|....*....|.
gi 1207115676 256 VKQLILAGADMQIKNAEGITA 276
Cdd:COG0666   202 VKLLLEAGADVNAKDNDGKTA 222
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
115-276 6.28e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 120.06  E-value: 6.28e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115676 115 AAAQGKMEVVERFLDDGGDPNTCDEFRKTALHRAALQNHTKIVEKLLDKGADINFKDRLGCRAVHWACRGGSLSALTVLQ 194
Cdd:COG0666   127 AAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLL 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115676 195 DRGADINVRDKLLSSPLHVATRTGHSDVVQHLLDSGININAKDWEGDTVLHDAVRFNRYKIVKQLILAGADMQIKNAEGI 274
Cdd:COG0666   207 EAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLL 286


                  ..
gi 1207115676 275 TA 276
Cdd:COG0666   287 TL 288
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
112-276 6.34e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 114.67  E-value: 6.34e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115676 112 FLKAAAQGKMEVVERFLDDGGDPNTCDEFRKTALHRAALQNHTKIVEKLLDKGADINFKDRLGCRAVHWACRGGSLSALT 191
Cdd:COG0666    25 LLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVK 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115676 192 VLQDRGADINVRDKLLSSPLHVATRTGHSDVVQHLLDSGININAKDWEGDTVLHDAVRFNRYKIVKQLILAGADMQIKNA 271
Cdd:COG0666   105 LLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDN 184


                  ....*
gi 1207115676 272 EGITA 276
Cdd:COG0666   185 DGETP 189
PHA03095 PHA03095
ankyrin-like protein; Provisional
 112-282 3.80e-25

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 104.34  E-value: 3.80e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115676 112 FLKAAAQGKMEVVERFLDDGGDPNTCDEFRKTALH---RAALQNHTKIVEKLLDKGADINFKDRLGCRAVH-WACRGGSL 187
Cdd:PHA03095   18 YLLNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHlylHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHlYLYNATTL 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115676 188 SALTVLQDRGADINVRDKLLSSPLHV--ATRTGHSDVVQHLLDSGININAKDWEGDTVLHDAVRFNR--YKIVKQLILAG 263
Cdd:PHA03095   98 DVIKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanVELLRLLIDAG 177

                         170
                  ....*....|....*....
gi 1207115676 264 ADMQIKNAEGITATEQVKQ 282
Cdd:PHA03095  178 ADVYAVDDRFRSLLHHHLQ 196
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 119-271 7.80e-21

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 91.65  E-value: 7.80e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115676 119 GKMEVVERFLDDGGDPNTCDEFRKTALHRAALQNH--TKIVEKLLDKGADINFKDRLGCravhwacrggslsaltvLQDR 196
Cdd:PHA03100  119 NSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAKNRVNY-----------------LLSY 181

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207115676 197 GADINVRDKLLSSPLHVATRTGHSDVVQHLLDSGININAKDWEGDTVLHDAVRFNRYKIVKQLILAGADMQIKNA 271
Cdd:PHA03100  182 GVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 122-275 1.19e-20

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 91.18  E-value: 1.19e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115676 122 EVVERFLDDGGDPNTCDEFRKTALHRAALQNHTKIVEKLLDKGADINFKDRLGCRAVHWACRGGSLSALTVLQDRGADIN 201
Cdd:PHA02874  105 DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207115676 202 VRDKLLSSPLHVATRTGHSDVVQHLLDSGININAKDWEGDTVLHDAVRFNRYKIvkQLILAGADMQIKNAEGIT 275
Cdd:PHA02874  185 VKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAI--ELLINNASINDQDIDGST 256
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
115-244 1.94e-20

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 88.86  E-value: 1.94e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115676 115 AAAQGKMEVVERFLDDGGDPNTCDEFRKTALHRAALQNHTKIVEKLLDKGADINFKDRLGCRAVHWACRGGSLSALTVLQ 194
Cdd:COG0666   160 AAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1207115676 195 DRGADINVRDKLLSSPLHVATRTGHSDVVQHLLDSGININAKDWEGDTVL 244
Cdd:COG0666   240 EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 120-275 9.21e-20

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 88.57  E-value: 9.21e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115676 120 KMEVVERFLDDGGDPNTCDEFRKTALHRAALQNHT-----KIVEKLLDKGADINFKDRLGCRAVHWA--CRGGSLSALTV 192
Cdd:PHA03100   47 NIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAisKKSNSYSIVEY 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115676 193 LQDRGADINVRDKLLSSPLHVATRTGHSD--VVQHLLDSGININAK----------------DWEGDTVLHDAVRFNRYK 254
Cdd:PHA03100  127 LLDNGANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKGVDINAKnrvnyllsygvpinikDVYGFTPLHYAVYNNNPE 206

                         170       180
                  ....*....|....*....|.
gi 1207115676 255 IVKQLILAGADMQIKNAEGIT 275
Cdd:PHA03100  207 FVKYLLDLGANPNLVNKYGDT 227
Ank_2 pfam12796
Ankyrin repeats (3 copies);
145-237 1.36e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 81.70  E-value: 1.36e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115676 145 LHRAALQNHTKIVEKLLDKGADINFKDRLGCRAVHWACRGGSLSALTVLQDRgADINVRDKLLsSPLHVATRTGHSDVVQ 224
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGR-TALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1207115676 225 HLLDSGININAKD 237
Cdd:pfam12796  79 LLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
143-276 3.95e-19

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 85.39  E-value: 3.95e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115676 143 TALHRAALQNHTKIVEKLLDKGADINFKDRLGCRAVHWACRGGSLSALTVLQDRGADINVRDKLLSSPLHVATRTGHSDV 222
Cdd:COG0666    23 LLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEI 102

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1207115676 223 VQHLLDSGININAKDWEGDTVLHDAVRFNRYKIVKQLILAGADMQIKNAEGITA 276
Cdd:COG0666   103 VKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTP 156
Ank_2 pfam12796
Ankyrin repeats (3 copies);
179-270 1.05e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 76.31  E-value: 1.05e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115676 179 HWACRGGSLSALTVLQDRGADINVRDKLLSSPLHVATRTGHSDVVQHLLDSgININAKDwEGDTVLHDAVRFNRYKIVKQ 258
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKL 79

                          90
                  ....*....|..
gi 1207115676 259 LILAGADMQIKN 270
Cdd:pfam12796  80 LLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
115-204 2.25e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.54  E-value: 2.25e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115676 115 AAAQGKMEVVERFLDDGGDPNTCDEFRKTALHRAALQNHTKIVEKLLDKgADINFKDRlGCRAVHWACRGGSLSALTVLQ 194
Cdd:pfam12796   4 AAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLLL 81

                          90
                  ....*....|
gi 1207115676 195 DRGADINVRD 204
Cdd:pfam12796  82 EKGADINVKD 91
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 85-267 1.80e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 79.72  E-value: 1.80e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115676  85 TQKKKIKNKTTLSKDITNVsgavepeefLKAAAQGKMEVVERFLDDGGDPNTCDEFRKTALHRAA-LQNHTKIVEKLLDK 163
Cdd:PHA02876  226 TIKAIIDNRSNINKNDLSL---------LKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASqAPSLSRLVPKLLER 296

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115676 164 GADINFKDRLGCRAVHWACRGG-SLSALTVLQDRGADINVRDKLLSSPLHVA-TRTGHSDVVQHLLDSGININAKDWEGD 241
Cdd:PHA02876  297 GADVNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQAsTLDRNKDIVITLLELGANVNARDYCDK 376

                         170       180
                  ....*....|....*....|....*.
gi 1207115676 242 TVLHDAVRFNRYKIVKQLILAGADMQ 267
Cdd:PHA02876  377 TPIHYAAVRNNVVIINTLLDYGADIE 402
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 122-267 2.67e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 76.26  E-value: 2.67e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115676 122 EVVERFLDDGGDPNTCDEFRKTALHRAALQNHTKIVEKLLDKGADINFKDRLGCRAVHWA-CRGGSLSALTVLQDRGADI 200
Cdd:PHA02876  356 DIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANV 435

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207115676 201 NVRDKLLSSPLHVATRTG-HSDVVQHLLDSGININAKDWEGDTVLHDAVRFnrYKIVKQLILAGADMQ 267
Cdd:PHA02876  436 NSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIALEY--HGIVNILLHYGAELR 501
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 154-270 2.17e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 72.99  E-value: 2.17e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115676 154 TKIVEKLLDKGADINFKDR-LGCRAVHWACRGGSLSALTVLQDRGADINVRDKLLSSPLHVATRTGHSDVVQHLLDSGIN 232
Cdd:PHA02878  147 AEITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAS 226

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1207115676 233 INAKDWEGDTVLHDAV-RFNRYKIVKQLILAGADMQIKN 270
Cdd:PHA02878  227 TDARDKCGNTPLHISVgYCKDYDILKLLLEHGVDVNAKS 265
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 115-298 2.57e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 72.99  E-value: 2.57e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115676 115 AAAQGKMEVVERFLDDGGDPNTCDEFRKTALHRAALQNHTKIVEKLLDKGADINFKDRLGCRAVHWAC-RGGSLSALTVL 193
Cdd:PHA02878  175 ATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVgYCKDYDILKLL 254

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115676 194 QDRGADINVRDKLLS-SPLHVATRTghSDVVQHLLDSGININAKDWEGDTVLHDAVR-FNRYKIVKQLI-----LAGADM 266
Cdd:PHA02878  255 LEHGVDVNAKSYILGlTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSAVKqYLCINIGRILIsniclLKRIKP 332

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1207115676 267 QIKNAEG-------ITATEQVKQWQFDTKETLEKLEQMK 298
Cdd:PHA02878  333 DIKNSEGfidnmdcITSNKRLNQIKDKCEDELNRLASIK 371
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 122-283 4.27e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 72.22  E-value: 4.27e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115676 122 EVVERFLDDGGDPNTCDEFR-KTALHRAALQNHTKIVEKLLDKGADINFKDRLGCRAVHWACRGGSLSALTVLQDRGADI 200
Cdd:PHA02878  148 EITKLLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAST 227

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115676 201 NVRDKLLSSPLHVAT-RTGHSDVVQHLLDSGININAKDW-EGDTVLHDAVRFNRykIVKQLILAGADMQIKNAEGITA-T 277
Cdd:PHA02878  228 DARDKCGNTPLHISVgYCKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIKSER--KLKLLLEYGADINSLNSYKLTPlS 305


                  ....*.
gi 1207115676 278 EQVKQW 283
Cdd:PHA02878  306 SAVKQY 311
PHA03095 PHA03095
ankyrin-like protein; Provisional
 121-257 6.78e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 71.59  E-value: 6.78e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115676 121 MEVVERFLDDGGDPNTCDEFRKTALHRAALQNHT--KIVEKLLDKGADINFKDRLGCRAVHWACRGGSLSALTVLQ--DR 196
Cdd:PHA03095  167 VELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPraRIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVLPllIA 246

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207115676 197 GADINVRDKLLSSPLHVATRTGHSDVVQHLLDSGININAKDWEGDTVLHDAVRFNRYKIVK 257
Cdd:PHA03095  247 GISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVR 307
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 102-270 2.39e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 67.40  E-value: 2.39e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115676 102 NVSGavEPEEFLKAAAQGKMEVVERFLDDGGDPNTCDEFRKTALHRAA-LQNHTKIVEKLLDKGADINFKDRLGCRAVHW 180
Cdd:PHA02876  304 NIKG--ETPLYLMAKNGYDTENIRTLIMLGADVNAADRLYITPLHQAStLDRNKDIVITLLELGANVNARDYCDKTPIHY 381

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115676 181 ACRGGSLSALTVLQDRGADINVRDKLLSSPLHVA-TRTGHSDVVQHLLDSGININAKDWEGDTVLHDAVRFN-RYKIVKQ 258
Cdd:PHA02876  382 AAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEM 461

                         170
                  ....*....|..
gi 1207115676 259 LILAGADMQIKN 270
Cdd:PHA02876  462 LLDNGADVNAIN 473
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 115-273 6.86e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 65.37  E-value: 6.86e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115676 115 AAAQGKMEVVERFLDDGGDPNTCDEFRKTALHRAALQNHTKIVEKLLDKGADINFKDRLGCRAVHWACRGGSLSALTVLQ 194
Cdd:PHA02874  131 AIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLI 210

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115676 195 DRGADINVRDKLLSSPLHVATRtgHSDVVQHLLDSGININAKDWEGDTVLHDAVRFNRYK-IVKQLILAGADMQIKNAEG 273
Cdd:PHA02874  211 DHGNHIMNKCKNGFTPLHNAII--HNRSAIELLINNASINDQDIDGSTPLHHAINPPCDIdIIDILLYHKADISIKDNKG 288
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 111-268 2.03e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 63.86  E-value: 2.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115676 111 EFLKAAAQGKMEVVERFLDDGGDPNtcDEFRK---TALHRAALQNHTKIVEKLLDKGADINFKDRLGCRAVHWACRGGSL 187
Cdd:PHA02875   71 ELHDAVEEGDVKAVEELLDLGKFAD--DVFYKdgmTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDI 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115676 188 SALTVLQDRGADINVRDKLLSSPLHVATRTGHSDVVQHLLDSGININAKDWEGD-TVLHDAVRFNRYKIVKQLILAGADM 266
Cdd:PHA02875  149 KGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGADC 228


                  ..
gi 1207115676 267 QI 268
Cdd:PHA02875  229 NI 230
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 119-275 2.97e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 63.44  E-value: 2.97e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115676 119 GKMEVVERFLDDGGD-PNTCDEFRKTALHRAALQNHTKIVEKLLDKGADI------------------------------ 167
Cdd:PHA02874   12 GDIEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADInhintkiphplltaikigahdiikllidng 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115676 168 --------------------------NFKDRLGCRAVHWACRGGSLSALTVLQDRGADINVRDKLLSSPLHVATRTGHSD 221
Cdd:PHA02874   92 vdtsilpipciekdmiktildcgidvNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFD 171

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1207115676 222 VVQHLLDSGININAKDWEGDTVLHDAVRFNRYKIVKQLILAGADMQIKNAEGIT 275
Cdd:PHA02874  172 IIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFT 225
PHA03095 PHA03095
ankyrin-like protein; Provisional
 122-276 3.06e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 63.51  E-value: 3.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115676 122 EVVERFLDDGGDPNTCDEFRKTALHrAALQN---HTKIVEKLLDKGADINFKDRLGCRAVHWACRGGSLSALTV------ 192
Cdd:PHA03095   98 DVIKLLIKAGADVNAKDKVGRTPLH-VYLSGfniNPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVELLrllida 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115676 193 -------------------------------LQDRGADINVRDKLLSSPLHVA---TRTGHSDVVQhLLDSGININAKDW 238
Cdd:PHA03095  177 gadvyavddrfrsllhhhlqsfkprarivreLIRAGCDPAATDMLGNTPLHSMatgSSCKRSLVLP-LLIAGISINARNR 255

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1207115676 239 EGDTVLHDAVRFNRYKIVKQLILAGADMQIKNAEGITA 276
Cdd:PHA03095  256 YGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTP 293
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 118-288 4.48e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 63.54  E-value: 4.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115676 118 QGKMEVVERFLDDGGDPNTCDEFRKTALHRAALQNHTKIVEKLLDKGADINFKDRLGCRAVHWACRGGSLSALTVLQDRG 197
Cdd:PHA02876  155 QDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNR 234

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115676 198 ADINVRDkllsspLHVATRTGHSDVVQHLL--DSGININAKDWEGDTVLHDAVRF-NRYKIVKQLILAGADMQIKNAEGI 274
Cdd:PHA02876  235 SNINKND------LSLLKAIRNEDLETSLLlyDAGFSVNSIDDCKNTPLHHASQApSLSRLVPKLLERGADVNAKNIKGE 308

                         170
                  ....*....|....
gi 1207115676 275 TATEQVKQWQFDTK 288
Cdd:PHA02876  309 TPLYLMAKNGYDTE 322
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 155-294 5.49e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 59.68  E-value: 5.49e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115676 155 KIVEKLLDKGADINFKDRLGCRAVHWACRGGSLSALTVLQDRGADINVRDKLLSSPLHVATRTGHS-----DVVQHLLDS 229
Cdd:PHA03100   16 KNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEY 95

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207115676 230 GININAKDWEGDTVLHDAV--RFNRYKIVKQLILAGADMQIKNAEGITATEQVKQWQFDTKETLEKL 294
Cdd:PHA03100   96 GANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLKILKLL 162
Ank_4 pfam13637
Ankyrin repeats (many copies);
143-193 1.03e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.43  E-value: 1.03e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1207115676 143 TALHRAALQNHTKIVEKLLDKGADINFKDRLGCRAVHWACRGGSLSALTVL 193
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 113-278 1.59e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 58.73  E-value: 1.59e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115676 113 LKAAAQGKMEVVERFLDDGGDPNTCDEFRKTALHRAALQNHTKIVEKLLDKGADINFKDRLGCRAVHWACRGGSLSALTV 192
Cdd:PLN03192  530 LTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRI 609

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115676 193 LQD--RGADINVRDKLLSsplhVATRTGHSDVVQHLLDSGININAKDWEGDTVLHDAVRFNRYKIVKQLILAGADMQIKN 270
Cdd:PLN03192  610 LYHfaSISDPHAAGDLLC----TAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAN 685


                  ....*....
gi 1207115676 271 A-EGITATE 278
Cdd:PLN03192  686 TdDDFSPTE 694
Ank_2 pfam12796
Ankyrin repeats (3 copies);
211-260 1.29e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 51.27  E-value: 1.29e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1207115676 211 LHVATRTGHSDVVQHLLDSGININAKDWEGDTVLHDAVRFNRYKIVKQLI 260
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL 50
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 113-275 3.28e-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: 54.63  E-value: 3.28e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115676 113 LKAAAQGKMEVVERFLDDggdpNTCDEFRK-----TALHRAALQNHTKIVEKLLDKGADINFKD-----RLGCRAVHWAC 182
Cdd:cd22192    22 LLAAKENDVQAIKKLLKC----PSCDLFQRgalgeTALHVAALYDNLEAAVVLMEAAPELVNEPmtsdlYQGETALHIAV 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115676 183 RGGSLSALTVLQDRGADINV-----------RDKLL---SSPLHVATRTGHSDVVQHLLDSGININAKDWEGDTVLHDAV 248
Cdd:cd22192    98 VNQNLNLVRELIARGADVVSpratgtffrpgPKNLIyygEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILV 177

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1207115676 249 RFNRYKIVKQ---LILA----GADM---QIKNAEGIT 275
Cdd:cd22192   178 LQPNKTFACQmydLILSydkeDDLQpldLVPNNQGLT 214
Ank_4 pfam13637
Ankyrin repeats (many copies);
208-260 4.68e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.81  E-value: 4.68e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1207115676 208 SSPLHVATRTGHSDVVQHLLDSGININAKDWEGDTVLHDAVRFNRYKIVKQLI 260
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 135-281 5.14e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 52.51  E-value: 5.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115676 135 NTCDEFRKTALHRAALQNHT--KIVEKLLDKGADINFKDR-LGCRAVHWAC---RGGSLSALTVLQDRGADINVRDKLLS 208
Cdd:PHA02859   45 NDCNDLYETPIFSCLEKDKVnvEILKFLIENGADVNFKTRdNNLSALHHYLsfnKNVEPEILKILIDSGSSITEEDEDGK 124

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207115676 209 SPLHV--ATRTGHSDVVQHLLDSGININAKDWEGDTVLHDAVRF-NRYKIVKQLILAGADMQIKNAEGITATEQVK 281
Cdd:PHA02859  125 NLLHMymCNFNVRINVIKLLIDSGVSFLNKDFDNNNILYSYILFhSDKKIFDFLTSLGIDINETNKSGYNCYDLIK 200
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 160-227 7.35e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 53.36  E-value: 7.35e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207115676 160 LLDKGADINFKDRLGCRAVHWACRGGSLSALTVLQDRGADINVRDKLLSSPLHVATRTGHSDVVQHLL 227
Cdd:PTZ00322  101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 142-275 9.71e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 52.69  E-value: 9.71e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115676 142 KTALHRAALQNHTKIVEKLLDKGADINFKDRLGCRAVHWACRGGSLSALTVLQDRGADINVRDKLLSSPLHVATRTGHSD 221
Cdd:PHA02875    3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVK 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1207115676 222 VVQHLLDSGININAKDW-EGDTVLHDAVRFNRYKIVKQLILAGADMQIKNAEGIT 275
Cdd:PHA02875   83 AVEELLDLGKFADDVFYkDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFS 137
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 124-236 1.19e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 52.36  E-value: 1.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115676 124 VERFLDDGGDPNTCDEFRKTALHRAALQNHTKIVEKLLDKGADINFKDRLGCRAVHWACRGGSLSALTVLQDRGADINVR 203
Cdd:PHA03100  175 VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTI 254

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1207115676 204 DKLL----SSPLHVATRT---GHSDVVQHLLDSGININAK 236
Cdd:PHA03100  255 IETLlyfkDKDLNTITKIkmlKKSIMYMFLLDPGFYKNRK 294
Ank_4 pfam13637
Ankyrin repeats (many copies);
114-161 3.33e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.50  E-value: 3.33e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1207115676 114 KAAAQGKMEVVERFLDDGGDPNTCDEFRKTALHRAALQNHTKIVEKLL 161
Cdd:pfam13637   7 AAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
155-276 3.54e-07

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 50.72  E-value: 3.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115676 155 KIVEKLLDKGADINFKDRLGCRAVHWACRGGSLSALTVLQDRGADINVRDKLLSSPLHVATRTGHSDVVQHLLDSGININ 234
Cdd:COG0666     2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1207115676 235 AKDWEGDTVLHDAVRFNRYKIVKQLILAGADMQIKNAEGITA 276
Cdd:COG0666    82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETP 123
Ank_5 pfam13857
Ankyrin repeats (many copies);
193-245 5.77e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.80  E-value: 5.77e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1207115676 193 LQDRGADINVRDKLLSSPLHVATRTGHSDVVQHLLDSGININAKDWEGDTVLH 245
Cdd:pfam13857   2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 179-259 1.18e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.90  E-value: 1.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115676 179 HWACRGGSLSAlTVLQDRGADINVRDKLLSSPLHVATRTGHSDVVQHLLDSGININAKDWEGDTVLHDAVRFNRYKIVKQ 258
Cdd:PTZ00322   88 QLAASGDAVGA-RILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                  .
gi 1207115676 259 L 259
Cdd:PTZ00322  167 L 167
Ank_4 pfam13637
Ankyrin repeats (many copies);
176-227 3.47e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.42  E-value: 3.47e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1207115676 176 RAVHWACRGGSLSALTVLQDRGADINVRDKLLSSPLHVATRTGHSDVVQHLL 227
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 133-248 3.05e-05

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: 45.46  E-value: 3.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115676 133 DPNTCDEFR-KTALHRAALQNHTKIVEKLLDKGADINFkdRLGCRAVHWACRGGSLSaltvlqdrgadinvrdkLLSSPL 211
Cdd:TIGR00870 119 DQYTSEFTPgITALHLAAHRQNYEIVKLLLERGASVPA--RACGDFFVKSQGVDSFY-----------------HGESPL 179

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1207115676 212 HVATRTGHSDVVQHLLDSGININAKDWEGDTVLHDAV 248
Cdd:TIGR00870 180 NAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLV 216
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 143-172 5.75e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.58  E-value: 5.75e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1207115676 143 TALHRAALQ-NHTKIVEKLLDKGADINFKDR 172
Cdd:pfam00023   4 TPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
Ank_5 pfam13857
Ankyrin repeats (many copies);
133-181 8.88e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.64  E-value: 8.88e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1207115676 133 DPNTCDEFRKTALHRAALQNHTKIVEKLLDKGADINFKDRLGCRAVHWA 181
Cdd:pfam13857   8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 209-235 9.63e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 38.72  E-value: 9.63e-05
                           10        20
                   ....*....|....*....|....*..
gi 1207115676  209 SPLHVATRTGHSDVVQHLLDSGININA 235
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 142-168 1.18e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 38.72  E-value: 1.18e-04
                           10        20
                   ....*....|....*....|....*..
gi 1207115676  142 KTALHRAALQNHTKIVEKLLDKGADIN 168
Cdd:smart00248   3 RTPLHLAAENGNLEVVKLLLDKGADIN 29
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 143-168 1.37e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 38.39  E-value: 1.37e-04
                          10        20
                  ....*....|....*....|....*.
gi 1207115676 143 TALHRAALQNHTKIVEKLLDKGADIN 168
Cdd:pfam13606   4 TPLHLAARNGRLEIVKLLLENGADIN 29
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 209-237 1.63e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.42  E-value: 1.63e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1207115676 209 SPLHVA-TRTGHSDVVQHLLDSGININAKD 237
Cdd:pfam00023   4 TPLHLAaGRRGNLEIVKLLLSKGADVNARD 33
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 109-245 4.70e-04

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 41.79  E-value: 4.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115676 109 PEEFLKAAAQGKMEVVERFLDDGgdpntcdEFRKTALHRAALQNHTKIVEK---LLDKGADINFKDRL-----------G 174
Cdd:cd21882     1 LEELLGLLECLRWYLTDSAYQRG-------ATGKTCLHKAALNLNDGVNEAimlLLEAAPDSGNPKELvnapctdefyqG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115676 175 CRAVHWACRGGSLSALTVLQDRGADINVR---DKLLSS----------PLHVATRTGHSDVVQHLLDSGINI---NAKDW 238
Cdd:cd21882    74 QTALHIAIENRNLNLVRLLVENGADVSARatgRFFRKSpgnlfyfgelPLSLAACTNQEEIVRLLLENGAQPaalEAQDS 153


                  ....*..
gi 1207115676 239 EGDTVLH 245
Cdd:cd21882   154 LGNTVLH 160
Ank_5 pfam13857
Ankyrin repeats (many copies);
160-214 5.33e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.33  E-value: 5.33e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1207115676 160 LLDKG-ADINFKDRLGCRAVHWACRGGSLSALTVLQDRGADINVRDKLLSSPLHVA 214
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02946 PHA02946
ankyin-like protein; Provisional
 123-245 6.85e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 40.81  E-value: 6.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115676 123 VVERFLDDGGDPNTCDEFRKTALHRAAlQNHTKIVEK---LLDKGADINFK-DRLGCRAVhWACRGGSLSALTVLQDRGA 198
Cdd:PHA02946   87 IVAMLLTHGADPNACDKQHKTPLYYLS-GTDDEVIERinlLVQYGAKINNSvDEEGCGPL-LACTDPSERVFKKIMSIGF 164

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1207115676 199 DINVRDKLLSSPL--HVATRTGHSDVVQHLLDSGININAKDWEGDTVLH 245
Cdd:PHA02946  165 EARIVDKFGKNHIhrHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLH 213
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 111-275 1.19e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 40.36  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115676 111 EFLKAAAQGKMEVVERFLDDGGDPNTCDEFRKTALHRAALQNHTKIVEKLLDKGADINFKDRLGCRAVHWACRGGSLSAL 190
Cdd:PHA02875    5 ALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115676 191 TVLQDRGADIN-VRDKLLSSPLHVATRTGHSDVVQHLLDSGININAKDWEGDTVLHDAVRFNRYKIVKQLILAGADMQIK 269
Cdd:PHA02875   85 EELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIE 164


                  ....*.
gi 1207115676 270 NAEGIT 275
Cdd:PHA02875  165 DCCGCT 170
Ank_5 pfam13857
Ankyrin repeats (many copies);
226-276 1.54e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.17  E-value: 1.54e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1207115676 226 LLDSG-ININAKDWEGDTVLHDAVRFNRYKIVKQLILAGADMQIKNAEGITA 276
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTA 52
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 170-270 1.65e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 38.32  E-value: 1.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115676 170 KDRLGCRAVHWACRGGSLSALtvLQDRGADINVRDKLLSS-------PLHVATRTGHSDVVQH---LLDSGININAKDW- 238
Cdd:PHA02736   13 PDIEGENILHYLCRNGGVTDL--LAFKNAISDENRYLVLEynrhgkqCVHIVSNPDKADPQEKlklLMEWGADINGKERv 90

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1207115676 239 EGDTVLHDAVRFNRYKIVKQLI-LAGADMQIKN 270
Cdd:PHA02736   91 FGNTPLHIAVYTQNYELATWLCnQPGVNMEILN 123
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 209-235 1.70e-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: 1.70e-03
                          10        20
                  ....*....|....*....|....*..
gi 1207115676 209 SPLHVATRTGHSDVVQHLLDSGININA 235
Cdd:pfam13606   4 TPLHLAARNGRLEIVKLLLENGADINA 30
PHA02917 PHA02917
ankyrin-like protein; Provisional
 232-275 1.79e-03

ankyrin-like protein; Provisional


Pssm-ID: 165231 [Multi-domain]  Cd Length: 661  Bit Score: 39.98  E-value: 1.79e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1207115676 232 NINAKDWEGDTVLHDAVRFNRYKIVKQLILAGADMQIKNAEGIT 275
Cdd:PHA02917  444 DINMIDKRGETLLHKAVRYNKQSLVSLLLESGSDVNIRSNNGYT 487
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 110-248 2.49e-03

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 39.36  E-value: 2.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115676 110 EEFLKAAAQGKMEVVERFLDDGGDPN-----------TCDEFR-----KTALHRAAL---QNHTKIVEKLLDKGADINFK 170
Cdd:cd22194    47 KKRLKKVSEAAVEELGELLKELKDLSrrrrktdvpdfLMHKLTasdtgKTCLMKALLninENTKEIVRILLAFAEENGIL 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207115676 171 DRL-----------GCRAVHWACRGGSLSALTVLQDRGADINVRDK--------------LLSSPLHVATRTGHSDVVQH 225
Cdd:cd22194   127 DRFinaeyteeayeGQTALNIAIERRQGDIVKLLIAKGADVNAHAKgvffnpkykhegfyFGETPLALAACTNQPEIVQL 206

                         170       180
                  ....*....|....*....|....
gi 1207115676 226 LLDSG-ININAKDWEGDTVLHDAV 248
Cdd:cd22194   207 LMEKEsTDITSQDSRGNTVLHALV 230
Ank_2 pfam12796
Ankyrin repeats (3 copies);
244-276 4.51e-03

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 35.86  E-value: 4.51e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1207115676 244 LHDAVRFNRYKIVKQLILAGADMQIKNAEGITA 276
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTA 33
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 239-266 5.63e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 33.72  E-value: 5.63e-03
                           10        20
                   ....*....|....*....|....*...
gi 1207115676  239 EGDTVLHDAVRFNRYKIVKQLILAGADM 266
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 239-270 8.34e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 33.42  E-value: 8.34e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1207115676 239 EGDTVLHDAV-RFNRYKIVKQLILAGADMQIKN 270
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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