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Conserved domains on  [gi|894216230|ref|NP_001297701|]
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ankyrin repeat domain-containing protein 61 isoform 2 [Mus musculus]

Protein Classification

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

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

Gene Ontology:  GO:0005515
PubMed:  33435370|17176038

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
94-292 6.61e-31

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 119.29  E-value: 6.61e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216230  94 ILMDIQNNAVLCLCILCDHGAQVNARvdNSNKHSALHLAIIHGTYPVLSFLAQNGAQVNATNESSMTPLHMAADILNKNM 173
Cdd:COG0666   58 LLAAALAGDLLVALLLLAAGADINAK--DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEI 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216230 174 IETLIAFGANVNcAISSTGNTALKLAVCTASSKVgrllaagvgcIRLLLNNGAQVNAQDHEGQTALHEACFGGREAIISL 253
Cdd:COG0666  136 VKLLLEAGADVN-AQDNDGNTPLHLAAANGNLEI----------VKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKL 204

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 894216230 254 LLEFEANVNILTRNGESPIYMYLQRSSNIRDRSLLARLL 292
Cdd:COG0666  205 LLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243
PHA03095 super family cl33707
ankyrin-like protein; Provisional
 36-76 3.58e-03

ankyrin-like protein; Provisional


The actual alignment was detected with superfamily member PHA03095:

Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 39.24  E-value: 3.58e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 894216230  36 PIHLAAEYRKPQSLLCLLQHGADPEVRDAQGFTTLHLMLLN 76
Cdd:PHA03095 260 PLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRN 300
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
94-292 6.61e-31

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 119.29  E-value: 6.61e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216230  94 ILMDIQNNAVLCLCILCDHGAQVNARvdNSNKHSALHLAIIHGTYPVLSFLAQNGAQVNATNESSMTPLHMAADILNKNM 173
Cdd:COG0666   58 LLAAALAGDLLVALLLLAAGADINAK--DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEI 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216230 174 IETLIAFGANVNcAISSTGNTALKLAVCTASSKVgrllaagvgcIRLLLNNGAQVNAQDHEGQTALHEACFGGREAIISL 253
Cdd:COG0666  136 VKLLLEAGADVN-AQDNDGNTPLHLAAANGNLEI----------VKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKL 204

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 894216230 254 LLEFEANVNILTRNGESPIYMYLQRSSNIRDRSLLARLL 292
Cdd:COG0666  205 LLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 33-274 2.97e-20

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 91.65  E-value: 2.97e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216230  33 PIFPIHLAAEYRKPQSLLCLLQHGADPEVRDAQGFTTLHLMLLNwpassttwskpstqiqkilMDIQNNAVLCLCILCDH 112
Cdd:PHA03100  35 PVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNI-------------------KYNLTDVKEIVKLLLEY 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216230 113 GAQVNARVDNSNkhSALHLAIIH--GTYPVLSFLAQNGAQVNATNESSMTPLHMAAD--ILNKNMIETLIAFGANVNcAI 188
Cdd:PHA03100  96 GANVNAPDNNGI--TPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLEsnKIDLKILKLLIDKGVDIN-AK 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216230 189 SStgntalklavctasskvgrllaagvgcIRLLLNNGAQVNAQDHEGQTALHEACFGGREAIISLLLEFEANVNILTRNG 268
Cdd:PHA03100 173 NR---------------------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYG 225


                 ....*.
gi 894216230 269 ESPIYM 274
Cdd:PHA03100 226 DTPLHI 231
Ank_2 pfam12796
Ankyrin repeats (3 copies);
129-232 9.14e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 60.90  E-value: 9.14e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216230  129 LHLAIIHGTYPVLSFLAQNGAQVNATNESSMTPLHMAADILNKNMIETLIafgANVNCAISSTGNTALKLAVCTASSKvg 208
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL---EHADVNLKDNGRTALHYAARSGHLE-- 75

                          90       100
                  ....*....|....*....|....
gi 894216230  209 rllaagvgCIRLLLNNGAQVNAQD 232
Cdd:pfam12796  76 --------IVKLLLEKGADINVKD 91
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 127-240 6.54e-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: 54.25  E-value: 6.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216230 127 SALHLAIIHGTYPVLSFLAQNGAQ-VNATNESSM----TPLHMAADILNKNMIETLIAFGANVN-------------CAI 188
Cdd:cd22192   53 TALHVAALYDNLEAAVVLMEAAPElVNEPMTSDLyqgeTALHIAVVNQNLNLVRELIARGADVVspratgtffrpgpKNL 132

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 894216230 189 SSTGNTALKLAVCTASSKVgrllaagvgcIRLLLNNGAQVNAQDHEGQTALH 240
Cdd:cd22192  133 IYYGEHPLSFAACVGNEEI----------VRLLIEHGADIRAQDSLGNTVLH 174
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 126-258 4.40e-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: 4.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216230  126 HSALHLAIIHGTYPVLSFLAQNGAQVNAT------NESSMT--------PLHMAADILNKNMIETLIAFGANVNCAIsST 191
Cdd:TIGR00870 129 ITALHLAAHRQNYEIVKLLLERGASVPARacgdffVKSQGVdsfyhgesPLNAAACLGSPSIVALLSEDPADILTAD-SL 207

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 894216230  192 GNTALKLAVCTASSKVGRlLAAGVGCIRLLLNNGAQ----------VNaqdHEGQTALHEACFGGREAIISLLLEFE 258
Cdd:TIGR00870 208 GNTLLHLLVMENEFKAEY-EELSCQMYNFALSLLDKlrdskeleviLN---HQGLTPLKLAAKEGRIVLFRLKLAIK 280
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 159-186 1.78e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.64  E-value: 1.78e-03
                           10        20
                   ....*....|....*....|....*...
gi 894216230   159 MTPLHMAADILNKNMIETLIAFGANVNC 186
Cdd:smart00248   3 RTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA03095 PHA03095
ankyrin-like protein; Provisional
 36-76 3.58e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 39.24  E-value: 3.58e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 894216230  36 PIHLAAEYRKPQSLLCLLQHGADPEVRDAQGFTTLHLMLLN 76
Cdd:PHA03095 260 PLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRN 300
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
94-292 6.61e-31

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 119.29  E-value: 6.61e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216230  94 ILMDIQNNAVLCLCILCDHGAQVNARvdNSNKHSALHLAIIHGTYPVLSFLAQNGAQVNATNESSMTPLHMAADILNKNM 173
Cdd:COG0666   58 LLAAALAGDLLVALLLLAAGADINAK--DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEI 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216230 174 IETLIAFGANVNcAISSTGNTALKLAVCTASSKVgrllaagvgcIRLLLNNGAQVNAQDHEGQTALHEACFGGREAIISL 253
Cdd:COG0666  136 VKLLLEAGADVN-AQDNDGNTPLHLAAANGNLEI----------VKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKL 204

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 894216230 254 LLEFEANVNILTRNGESPIYMYLQRSSNIRDRSLLARLL 292
Cdd:COG0666  205 LLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
108-303 1.25e-29

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 115.82  E-value: 1.25e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216230 108 ILCDHGAQVNARvdNSNKHSALHLAIIHGTYPVLSFLAQNGAQVNATNESSMTPLHMAADILNKNMIETLIAFGANVNcA 187
Cdd:COG0666  105 LLLEAGADVNAR--DKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVN-A 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216230 188 ISSTGNTALKLAVCTASSKVgrllaagvgcIRLLLNNGAQVNAQDHEGQTALHEACFGGREAIISLLLEFEANVNILTRN 267
Cdd:COG0666  182 RDNDGETPLHLAAENGHLEI----------VKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKD 251

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 894216230 268 GESPIYMYLQRSSNIRDRSLLARLLYRTYPLRLSNK 303
Cdd:COG0666  252 GLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
36-269 7.78e-27

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 108.12  E-value: 7.78e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216230  36 PIHLAAEYRKPQSLLCLLQHGADPEVRDAQGFTTLHLMllnwpassttwskpstqiqkilmdIQNNAVLCLCILCDHGAQ 115
Cdd:COG0666   90 LLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLA------------------------AYNGNLEIVKLLLEAGAD 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216230 116 VNARvdNSNKHSALHLAIIHGTYPVLSFLAQNGAQVNATNESSMTPLHMAADILNKNMIETLIAFGANVNcAISSTGNTA 195
Cdd:COG0666  146 VNAQ--DNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVN-AKDNDGKTA 222

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 894216230 196 LKLAVCTASSKVgrllaagvgcIRLLLNNGAQVNAQDHEGQTALHEACFGGREAIISLLLEFEANVNILTRNGE 269
Cdd:COG0666  223 LDLAAENGNLEI----------VKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLL 286
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
95-274 2.19e-25

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 104.27  E-value: 2.19e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216230  95 LMDIQNNAVLCLCILCDHGAQVNARVDNSNKHSALHLAIIHGTYPVLSFLAQNGAQVNATNESSMTPLHMAADILNKNMI 174
Cdd:COG0666   24 LLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIV 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216230 175 ETLIAFGANVNcAISSTGNTALKLAVCTASSKVgrllaagvgcIRLLLNNGAQVNAQDHEGQTALHEACFGGREAIISLL 254
Cdd:COG0666  104 KLLLEAGADVN-ARDKDGETPLHLAAYNGNLEI----------VKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLL 172

                        170       180
                 ....*....|....*....|
gi 894216230 255 LEFEANVNILTRNGESPIYM 274
Cdd:COG0666  173 LEAGADVNARDNDGETPLHL 192
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 33-274 2.97e-20

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 91.65  E-value: 2.97e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216230  33 PIFPIHLAAEYRKPQSLLCLLQHGADPEVRDAQGFTTLHLMLLNwpassttwskpstqiqkilMDIQNNAVLCLCILCDH 112
Cdd:PHA03100  35 PVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNI-------------------KYNLTDVKEIVKLLLEY 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216230 113 GAQVNARVDNSNkhSALHLAIIH--GTYPVLSFLAQNGAQVNATNESSMTPLHMAAD--ILNKNMIETLIAFGANVNcAI 188
Cdd:PHA03100  96 GANVNAPDNNGI--TPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLEsnKIDLKILKLLIDKGVDIN-AK 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216230 189 SStgntalklavctasskvgrllaagvgcIRLLLNNGAQVNAQDHEGQTALHEACFGGREAIISLLLEFEANVNILTRNG 268
Cdd:PHA03100 173 NR---------------------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYG 225


                 ....*.
gi 894216230 269 ESPIYM 274
Cdd:PHA03100 226 DTPLHI 231
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
36-229 1.97e-18

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 84.62  E-value: 1.97e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216230  36 PIHLAAEYRKPQSLLCLLQHGADPEVRDAQGFTTLHLMllnwpassttwskpstqiqkilmdIQNNAVLCLCILCDHGAQ 115
Cdd:COG0666  123 PLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA------------------------AANGNLEIVKLLLEAGAD 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216230 116 VNARvdNSNKHSALHLAIIHGTYPVLSFLAQNGAQVNATNESSMTPLHMAADILNKNMIETLIAFGANVNcAISSTGNTA 195
Cdd:COG0666  179 VNAR--DNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN-AKDKDGLTA 255

                        170       180       190
                 ....*....|....*....|....*....|....
gi 894216230 196 LKLAVCTASSKVGRLLAAGVGCIRLLLNNGAQVN 229
Cdd:COG0666  256 LLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 108-282 5.52e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 85.32  E-value: 5.52e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216230 108 ILCDHGAQVNaRVDNSNKHSALHLAIIHGTYPVLSFLAQNGAQVNATNESSMTPLHMAADILNKNMIETLIAFGANVNcA 187
Cdd:PHA02878 152 LLLSYGADIN-MKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTD-A 229

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216230 188 ISSTGNTALKLAvctasskVGRLLAAGVgcIRLLLNNGAQVNAQDH-EGQTALHEACFGgrEAIISLLLEFEANVNILTR 266
Cdd:PHA02878 230 RDKCGNTPLHIS-------VGYCKDYDI--LKLLLEHGVDVNAKSYiLGLTALHSSIKS--ERKLKLLLEYGADINSLNS 298

                        170
                 ....*....|....*.
gi 894216230 267 NGESPIYMYLQRSSNI 282
Cdd:PHA02878 299 YKLTPLSSAVKQYLCI 314
PHA03095 PHA03095
ankyrin-like protein; Provisional
 36-272 3.22e-15

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 76.60  E-value: 3.22e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216230  36 PIHLAAEYRKPQS---LLCLLQHGADPEVRDAQGFTTLHLMLLNwpasSTTWSkpstqiqkiLMDIqnnavlclciLCDH 112
Cdd:PHA03095  50 PLHLYLHYSSEKVkdiVRLLLEAGADVNAPERCGFTPLHLYLYN----ATTLD---------VIKL----------LIKA 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216230 113 GAQVNARVDNSNkhSALHlaiIHGT-----YPVLSFLAQNGAQVNATNESSMTPLHmaADILNKN----MIETLIAFGAN 183
Cdd:PHA03095 107 GADVNAKDKVGR--TPLH---VYLSgfninPKVIRLLLRKGADVNALDLYGMTPLA--VLLKSRNanveLLRLLIDAGAD 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216230 184 VnCAISSTGNTAL---KLAVCTASSKVGRLLAAGVG--------------------CIRL----LLNNGAQVNAQDHEGQ 236
Cdd:PHA03095 180 V-YAVDDRFRSLLhhhLQSFKPRARIVRELIRAGCDpaatdmlgntplhsmatgssCKRSlvlpLLIAGISINARNRYGQ 258

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 894216230 237 TALHEA-CFGGREAiISLLLEFEANVNILTRNGESPI 272
Cdd:PHA03095 259 TPLHYAaVFNNPRA-CRRLIALGADINAVSSDGNTPL 294
PHA03095 PHA03095
ankyrin-like protein; Provisional
 52-274 6.31e-15

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 75.83  E-value: 6.31e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216230  52 LLQHGADPEVRDAQGFTTLHLMLLNwpassttWSKPSTQIQKILMdiqnnavlclcilcDHGAQVNARvdNSNKHSALHL 131
Cdd:PHA03095  33 LLAAGADVNFRGEYGKTPLHLYLHY-------SSEKVKDIVRLLL--------------EAGADVNAP--ERCGFTPLHL 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216230 132 AIIHG-TYPVLSFLAQNGAQVNATNESSMTPLH--MAADILNKNMIETLIAFGANVNcAISSTGNTAlkLAVCTASSK-- 206
Cdd:PHA03095  90 YLYNAtTLDVIKLLIKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVN-ALDLYGMTP--LAVLLKSRNan 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216230 207 ---VGRLLAAGV------------------------GCIRLLLNNGAQVNAQDHEGQTALHEACFGG--REAIISLLLEF 257
Cdd:PHA03095 167 velLRLLIDAGAdvyavddrfrsllhhhlqsfkpraRIVRELIRAGCDPAATDMLGNTPLHSMATGSscKRSLVLPLLIA 246

                        250
                 ....*....|....*..
gi 894216230 258 EANVNILTRNGESPIYM 274
Cdd:PHA03095 247 GISINARNRYGQTPLHY 263
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 98-322 1.70e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 74.23  E-value: 1.70e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216230  98 IQNNAVLCLCILCDHGAQVNARVDNSNkhSALHLAIIHGTYPVLSFLAQNGAQVNATNESSMTPLHMAADILNKNMIETL 177
Cdd:PHA02874 132 IKKGDLESIKMLFEYGADVNIEDDNGC--YPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLL 209

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216230 178 IAFGANVNCAISStGNTALKLAVCTASSkvgrllaagvgCIRLLLNNgAQVNAQDHEGQTALHEAC-FGGREAIISLLLE 256
Cdd:PHA02874 210 IDHGNHIMNKCKN-GFTPLHNAIIHNRS-----------AIELLINN-ASINDQDIDGSTPLHHAInPPCDIDIIDILLY 276

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 894216230 257 FEANVNILTRNGESPI---YMYLQRSSNIRDrsLLARLLyrtyplrLSNKQGILPAGIMLPEYQLLRET 322
Cdd:PHA02874 277 HKADISIKDNKGENPIdtaFKYINKDPVIKD--IIANAV-------LIKEADKLKDSDFLEHIEIKDNK 336
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 24-266 1.35e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 68.94  E-value: 1.35e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216230  24 ATMSCKQTQPIFPIHLAAEYRKPQSLLCLLQHGADPEVRDAQGFTTLHLMLLN-----WPASSTTWSKPSTQIQKILMDI 98
Cdd:PHA02876 169 ADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSknidtIKAIIDNRSNINKNDLSLLKAI 248

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216230  99 QNNAVLCLCILCDHGAQVNArVDNSnKHSALHLAIihgTYPVLSFLA----QNGAQVNATNESSMTPLH-MAADILNKNM 173
Cdd:PHA02876 249 RNEDLETSLLLYDAGFSVNS-IDDC-KNTPLHHAS---QAPSLSRLVpkllERGADVNAKNIKGETPLYlMAKNGYDTEN 323

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216230 174 IETLIAFGANVNcAISSTGNTALKLAVCTASSKvgrllaagvGCIRLLLNNGAQVNAQDHEGQTALHEACFGGREAIISL 253
Cdd:PHA02876 324 IRTLIMLGADVN-AADRLYITPLHQASTLDRNK---------DIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINT 393

                        250
                 ....*....|...
gi 894216230 254 LLEFEANVNILTR 266
Cdd:PHA02876 394 LLDYGADIEALSQ 406
Ank_2 pfam12796
Ankyrin repeats (3 copies);
129-232 9.14e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 60.90  E-value: 9.14e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216230  129 LHLAIIHGTYPVLSFLAQNGAQVNATNESSMTPLHMAADILNKNMIETLIafgANVNCAISSTGNTALKLAVCTASSKvg 208
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL---EHADVNLKDNGRTALHYAARSGHLE-- 75

                          90       100
                  ....*....|....*....|....
gi 894216230  209 rllaagvgCIRLLLNNGAQVNAQD 232
Cdd:pfam12796  76 --------IVKLLLEKGADINVKD 91
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 28-277 9.86e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 66.24  E-value: 9.86e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216230  28 CKQTqpifPIHLAAEYRKPQSLLC-LLQHGADPEVRDAQGFTTLHLMLLNwpassttwSKPSTQIQKILMdiqnnavlcl 106
Cdd:PHA02876 272 CKNT----PLHHASQAPSLSRLVPkLLERGADVNAKNIKGETPLYLMAKN--------GYDTENIRTLIM---------- 329

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216230 107 cilcdHGAQVNA--RVDNSNKHSALHLAIIHGTypVLSFLaQNGAQVNATNESSMTPLHMAADILNKNMIETLIAFGANV 184
Cdd:PHA02876 330 -----LGADVNAadRLYITPLHQASTLDRNKDI--VITLL-ELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADI 401

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216230 185 NcAISSTGNTALKLAVCTASSKVGrllaagvgcIRLLLNNGAQVNAQDHEGQTALHEACFGG-REAIISLLLEFEANVNI 263
Cdd:PHA02876 402 E-ALSQKIGTALHFALCGTNPYMS---------VKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNA 471

                        250
                 ....*....|....
gi 894216230 264 LTRNGESPIYMYLQ 277
Cdd:PHA02876 472 INIQNQYPLLIALE 485
PHA03095 PHA03095
ankyrin-like protein; Provisional
 52-200 1.21e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 65.82  E-value: 1.21e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216230  52 LLQHGADPEVRDAQGFTTLHLMLLNwpassttwSKPSTQIQKILMDiqnnavlclcilcdhgAQVNARVDNSNKHSALHL 131
Cdd:PHA03095 173 LIDAGADVYAVDDRFRSLLHHHLQS--------FKPRARIVRELIR----------------AGCDPAATDMLGNTPLHS 228

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 894216230 132 AIIHGT--YPVLSFLAQNGAQVNATNESSMTPLHMAADILNKNMIETLIAFGANVNCaISSTGNTALKLAV 200
Cdd:PHA03095 229 MATGSSckRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINA-VSSDGNTPLSLMV 298
PHA03095 PHA03095
ankyrin-like protein; Provisional
 144-292 1.21e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 62.73  E-value: 1.21e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216230 144 LAQNGAQVNATNESSMTPLHM---AADILNKNMIETLIAFGANVNcAISSTGNTALKLAVCTASSkvgrllaagVGCIRL 220
Cdd:PHA03095  33 LLAAGADVNFRGEYGKTPLHLylhYSSEKVKDIVRLLLEAGADVN-APERCGFTPLHLYLYNATT---------LDVIKL 102

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 894216230 221 LLNNGAQVNAQDHEGQTALHeACFGG---REAIISLLLEFEANVNILTRNGESPIYMYLqRSSNIrDRSLLARLL 292
Cdd:PHA03095 103 LIKAGADVNAKDKVGRTPLH-VYLSGfniNPKVIRLLLRKGADVNALDLYGMTPLAVLL-KSRNA-NVELLRLLI 174
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 210-294 1.48e-10

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 62.61  E-value: 1.48e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216230 210 LLAAG--VGcIRLLLNNGAQVNAQDHEGQTALHEACFGGREAIISLLLEFEANVNILTRNGESPiyMYLQRSSNIRDrsl 287
Cdd:PTZ00322  89 LAASGdaVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTP--LELAEENGFRE--- 162


                 ....*..
gi 894216230 288 LARLLYR 294
Cdd:PTZ00322 163 VVQLLSR 169
Ank_2 pfam12796
Ankyrin repeats (3 copies);
162-263 4.04e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 55.89  E-value: 4.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216230  162 LHMAADILNKNMIETLIAFGANVNCaISSTGNTALKLAVCTASSKvgrllaagvgCIRLLLNNgAQVNAQDHeGQTALHE 241
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANL-QDKNGRTALHLAAKNGHLE----------IVKLLLEH-ADVNLKDN-GRTALHY 67

                          90       100
                  ....*....|....*....|..
gi 894216230  242 ACFGGREAIISLLLEFEANVNI 263
Cdd:pfam12796  68 AARSGHLEIVKLLLEKGADINV 89
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 159-296 4.43e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 60.83  E-value: 4.43e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216230 159 MTPLHMAADILNKNMIETLIAFGANVNcaISSTGN-TALKLAVCTASSkvgrlLAAGVGCIRLLLNNGAQVNAQDHEGQT 237
Cdd:PHA03100  36 VLPLYLAKEARNIDVVKILLDNGADIN--SSTKNNsTPLHYLSNIKYN-----LTDVKEIVKLLLEYGANVNAPDNNGIT 108

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 894216230 238 ALHEA---CFGGREaIISLLLEFEANVNILTRNGESPIYMYLqrSSNIRDRSLLARLLYRTY 296
Cdd:PHA03100 109 PLLYAiskKSNSYS-IVEYLLDNGANVNIKNSDGENLLHLYL--ESNKIDLKILKLLIDKGV 167
Ank_4 pfam13637
Ankyrin repeats (many copies);
127-178 1.20e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.43  E-value: 1.20e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 894216230  127 SALHLAIIHGTYPVLSFLAQNGAQVNATNESSMTPLHMAADILNKNMIETLI 178
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 91-268 1.41e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 59.23  E-value: 1.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216230  91 IQKILMDIQNNAVLCLCILCDHGAQVNarVDNSNKHSALHLAIIHGTYPVLSFLAQNGAQVN-ATNESSMTPLHMAADIL 169
Cdd:PHA02875  36 ISPIKLAMKFRDSEAIKLLMKHGAIPD--VKYPDIESELHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILK 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216230 170 NKNMIETLIAFGANVNcaISSTGNTA-LKLAVctasskvgrlLAAGVGCIRLLLNNGAQVNAQDHEGQTALHEACFGGRE 248
Cdd:PHA02875 114 KLDIMKLLIARGADPD--IPNTDKFSpLHLAV----------MMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDI 181

                        170       180
                 ....*....|....*....|
gi 894216230 249 AIISLLLEFEANVNILTRNG 268
Cdd:PHA02875 182 AICKMLLDSGANIDYFGKNG 201
PHA03095 PHA03095
ankyrin-like protein; Provisional
 151-283 2.33e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 58.50  E-value: 2.33e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216230 151 VNATNESSMTPLHMAADILNKNMIETLIAFGANVNCAiSSTGNTALKLAVCTASSKVGRLlaagvgcIRLLLNNGAQVNA 230
Cdd:PHA03095   7 VDIIMEAALYDYLLNASNVTVEEVRRLLAAGADVNFR-GEYGKTPLHLYLHYSSEKVKDI-------VRLLLEAGADVNA 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 894216230 231 QDHEGQTALH-EACFGGREAIISLLLEFEANVNILTRNGESPIYMYLqRSSNIR 283
Cdd:PHA03095  79 PERCGFTPLHlYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVYL-SGFNIN 131
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 111-305 8.20e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 56.90  E-value: 8.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216230 111 DHGAQVNARvdNSNKHSALHLAIIHGTYPVLSFLAQNGAQVNATNESSMTPLHMAADILNKNMIETLIAFGANVNCAiSS 190
Cdd:PHA02874 112 DCGIDVNIK--DAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVK-DN 188

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216230 191 TGNTALKLAVCTASSKvgrllaagvgCIRLLLNNGAQVNAQDHEGQTALHEACFGGREAIisLLLEFEANVNILTRNGES 270
Cdd:PHA02874 189 NGESPLHNAAEYGDYA----------CIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAI--ELLINNASINDQDIDGST 256

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 894216230 271 PIYMYLQRSSnirDRSLLARLLYRTYPLRLSNKQG 305
Cdd:PHA02874 257 PLHHAINPPC---DIDIIDILLYHKADISIKDNKG 288
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 140-290 1.76e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 56.23  E-value: 1.76e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216230 140 VLSFLAQNGAQVNATNESSMTPLHMAADILNKNMIETLIAFGANVN-----------CAISSTGNTALKlAVCTASSKVG 208
Cdd:PHA02876 160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNiialddlsvleCAVDSKNIDTIK-AIIDNRSNIN 238

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216230 209 RLLAAGVGCIR--------LLLNNGAQVNAQDHEGQTALHEACFG-GREAIISLLLEFEANVNILTRNGESPIYMYLQRS 279
Cdd:PHA02876 239 KNDLSLLKAIRnedletslLLYDAGFSVNSIDDCKNTPLHHASQApSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNG 318

                        170
                 ....*....|..
gi 894216230 280 SNIRD-RSLLAR 290
Cdd:PHA02876 319 YDTENiRTLIML 330
Ank_2 pfam12796
Ankyrin repeats (3 copies);
98-185 4.76e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 50.11  E-value: 4.76e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216230   98 IQNNAVLCLCILCDHGAQVNarVDNSNKHSALHLAIIHGTYPVLSFLAQNgAQVNATNEsSMTPLHMAADILNKNMIETL 177
Cdd:pfam12796   5 AKNGNLELVKLLLENGADAN--LQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLL 80


                  ....*...
gi 894216230  178 IAFGANVN 185
Cdd:pfam12796  81 LEKGADIN 88
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 127-240 6.54e-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: 54.25  E-value: 6.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216230 127 SALHLAIIHGTYPVLSFLAQNGAQ-VNATNESSM----TPLHMAADILNKNMIETLIAFGANVN-------------CAI 188
Cdd:cd22192   53 TALHVAALYDNLEAAVVLMEAAPElVNEPMTSDLyqgeTALHIAVVNQNLNLVRELIARGADVVspratgtffrpgpKNL 132

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 894216230 189 SSTGNTALKLAVCTASSKVgrllaagvgcIRLLLNNGAQVNAQDHEGQTALH 240
Cdd:cd22192  133 IYYGEHPLSFAACVGNEEI----------VRLLIEHGADIRAQDSLGNTVLH 174
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 167-294 1.15e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 53.35  E-value: 1.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216230 167 DILNKNMIETLIAFGANVNCAISSTGNTALKLAvctASSKVGRLLaagvgciRLLLNNGAQVNAQDHEGQTALHEACFGG 246
Cdd:PHA02878 143 DIIEAEITKLLLSYGADINMKDRHKGNTALHYA---TENKDQRLT-------ELLLSYGANVNIPDKTNNSPLHHAVKHY 212

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 894216230 247 REAIISLLLEFEANVNILTRNGESPIYMylqRSSNIRDRSLLARLLYR 294
Cdd:PHA02878 213 NKPIVHILLENGASTDARDKCGNTPLHI---SVGYCKDYDILKLLLEH 257
Ank_4 pfam13637
Ankyrin repeats (many copies);
217-255 1.22e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.04  E-value: 1.22e-07
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 894216230  217 CIRLLLNNGAQVNAQDHEGQTALHEACFGGREAIISLLL 255
Cdd:pfam13637  16 LLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 34-185 1.57e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 52.75  E-value: 1.57e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216230  34 IFPIHLAAEYRKPQSLLC--LLQHGADPEVRDAQGFTTLHLMLLNwpassttwSKPSTQIQKILmdIQNNAVLCLC---- 107
Cdd:PHA03100 107 ITPLLYAISKKSNSYSIVeyLLDNGANVNIKNSDGENLLHLYLES--------NKIDLKILKLL--IDKGVDINAKnrvn 176

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 894216230 108 ILCDHGAQVNARVDNSNkhSALHLAIIHGTYPVLSFLAQNGAQVNATNESSMTPLHMAADILNKNMIETLIAFGANVN 185
Cdd:PHA03100 177 YLLSYGVPINIKDVYGF--TPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
Ank_2 pfam12796
Ankyrin repeats (3 copies);
211-273 2.08e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 48.57  E-value: 2.08e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 894216230  211 LAAGVG---CIRLLLNNGAQVNAQDHEGQTALHEACFGGREAIISLLLEFeANVNILTrNGESPIY 273
Cdd:pfam12796   3 LAAKNGnleLVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALH 66
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 151-280 2.36e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 52.27  E-value: 2.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216230 151 VNATNESSMTPLHMAADILNKNMIETLIAFGANVNCAISSTGNTALKLAVCTASSKVGRLLAAGVGC------------I 218
Cdd:PHA02874  28 INISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTsilpipciekdmI 107

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 894216230 219 RLLLNNGAQVNAQDHEGQTALHEACFGGREAIISLLLEFEANVNILTRNGESPIYMYLQRSS 280
Cdd:PHA02874 108 KTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNF 169
Ank_2 pfam12796
Ankyrin repeats (3 copies);
37-155 3.35e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 47.80  E-value: 3.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216230   37 IHLAAEYRKPQSLLCLLQHGADPEVRDAQGFTTLHLmllnwpAssttwskpstqiqkilmdIQNNAVLCLCILCDHgAQV 116
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHL------A------------------AKNGHLEIVKLLLEH-ADV 55

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 894216230  117 NarvDNSNKHSALHLAIIHGTYPVLSFLAQNGAQVNATN 155
Cdd:pfam12796  56 N---LKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 34-265 2.38e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 49.22  E-value: 2.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216230  34 IFPIHLAAEYRKPQSLLCLLQHGADPEVrdaqgfttlhlmllNWPAssttwskpstqIQKILMD-IQNNAVLCLCILCDH 112
Cdd:PHA02875  36 ISPIKLAMKFRDSEAIKLLMKHGAIPDV--------------KYPD-----------IESELHDaVEEGDVKAVEELLDL 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216230 113 GAQVNaRVDNSNKHSALHLAIIHGTYPVLSFLAQNGAQVNATNESSMTPLHMAADILNKNMIETLIAFGANVNCAiSSTG 192
Cdd:PHA02875  91 GKFAD-DVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIE-DCCG 168

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 894216230 193 NTALKLAVCTASSKVgrllaagvgCiRLLLNNGAQVNAQDHEGQ-TALHEACFGGREAIISLLLEFEANVNILT 265
Cdd:PHA02875 169 CTPLIIAMAKGDIAI---------C-KMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGADCNIMF 232
PHA02743 PHA02743
Viral ankyrin protein; Provisional
 100-192 4.84e-06

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 46.35  E-value: 4.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216230 100 NNAVLCLCILCDHGAQVNARVDNSNkHSALHLAIIHGTYPVLSFLAQN-GAQVNATNESSMTPLHMAADILNKNMIETLI 178
Cdd:PHA02743  70 ANAVMKIELLVNMGADINARELGTG-NTLLHIAASTKNYELAEWLCRQlGVNLGAINYQHETAYHIAYKMRDRRMMEILR 148

                         90
                 ....*....|....
gi 894216230 179 AFGANVNCAISSTG 192
Cdd:PHA02743 149 ANGAVCDDPLSIGL 162
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 151-276 1.73e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 45.20  E-value: 1.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216230 151 VNATNESSMTPLH--MAADILNKNMIETLIAFGANVNCAISSTGNTALKLAVcTASSKVGRLLaagvgcIRLLLNNGAQV 228
Cdd:PHA02859  44 VNDCNDLYETPIFscLEKDKVNVEILKFLIENGADVNFKTRDNNLSALHHYL-SFNKNVEPEI------LKILIDSGSSI 116

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 894216230 229 NAQDHEGQTALHEAC--FGGREAIISLLLEFEANVNILTRNGESPIYMYL 276
Cdd:PHA02859 117 TEEDEDGKNLLHMYMcnFNVRINVIKLLIDSGVSFLNKDFDNNNILYSYI 166
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 35-165 1.80e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 46.41  E-value: 1.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216230  35 FPIHLAAEYRKPQSLLCLLQHGADPEVRDAQGFTTLHLmllnwpassTTWSKPSTQIQKILMdiqnnavlclcilcDHGA 114
Cdd:PHA02878 203 SPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHI---------SVGYCKDYDILKLLL--------------EHGV 259

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 894216230 115 QVNARVDNSNkHSALHLAIihGTYPVLSFLAQNGAQVNATNESSMTPLHMA 165
Cdd:PHA02878 260 DVNAKSYILG-LTALHSSI--KSERKLKLLLEYGADINSLNSYKLTPLSSA 307
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 121-261 2.33e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 46.40  E-value: 2.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216230 121 DNSNKHSALHLAIIHGTYPVLSFLAQNGAQVNATNESSMTPLHMAADILNKNMIETLIAFGANVNCAiSSTGNTALKLAV 200
Cdd:PLN03192 521 DDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIR-DANGNTALWNAI 599

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216230 201 CTASSKVGRLL----------AAG-----------VGCIRLLLNNGAQVNAQDHEGQTALHEACFGGREAIISLLLEFEA 259
Cdd:PLN03192 600 SAKHHKIFRILyhfasisdphAAGdllctaakrndLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGA 679


                 ..
gi 894216230 260 NV 261
Cdd:PLN03192 680 DV 681
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 126-258 4.40e-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: 4.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216230  126 HSALHLAIIHGTYPVLSFLAQNGAQVNAT------NESSMT--------PLHMAADILNKNMIETLIAFGANVNCAIsST 191
Cdd:TIGR00870 129 ITALHLAAHRQNYEIVKLLLERGASVPARacgdffVKSQGVdsfyhgesPLNAAACLGSPSIVALLSEDPADILTAD-SL 207

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 894216230  192 GNTALKLAVCTASSKVGRlLAAGVGCIRLLLNNGAQ----------VNaqdHEGQTALHEACFGGREAIISLLLEFE 258
Cdd:TIGR00870 208 GNTLLHLLVMENEFKAEY-EELSCQMYNFALSLLDKlrdskeleviLN---HQGLTPLKLAAKEGRIVLFRLKLAIK 280
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 36-164 1.47e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 44.09  E-value: 1.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216230  36 PIHLAAEYRKPQSLLCLLQHGADPEVRDAQGFTTL-------HLMLLNWPASSTTWSKPSTQIQKILMDIQNNAVLCLCI 108
Cdd:PLN03192 561 PLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALwnaisakHHKIFRILYHFASISDPHAAGDLLCTAAKRNDLTAMKE 640

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 894216230 109 LCDHGAQVNArvDNSNKHSALHLAIIHGTYPVLSFLAQNGAQVNATN-ESSMTPLHM 164
Cdd:PLN03192 641 LLKQGLNVDS--EDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANtDDDFSPTEL 695
PHA02917 PHA02917
ankyrin-like protein; Provisional
 228-288 1.01e-03

ankyrin-like protein; Provisional


Pssm-ID: 165231 [Multi-domain]  Cd Length: 661  Bit Score: 41.14  E-value: 1.01e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 894216230 228 VNAQDHEGQTALHEACFGGREAIISLLLEFEANVNILTRNGESPIYMYLQRSSNIRDRSLL 288
Cdd:PHA02917 445 INMIDKRGETLLHKAVRYNKQSLVSLLLESGSDVNIRSNNGYTCIAIAINESRNIELLKML 505
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 234-266 1.68e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 35.73  E-value: 1.68e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 894216230  234 EGQTALHEAC-FGGREAIISLLLEFEANVNILTR 266
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 159-186 1.78e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.64  E-value: 1.78e-03
                           10        20
                   ....*....|....*....|....*...
gi 894216230   159 MTPLHMAADILNKNMIETLIAFGANVNC 186
Cdd:smart00248   3 RTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 1-379 2.24e-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: 40.13  E-value: 2.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216230   1 MDGWNTACVAGRRVPSSSQNTPTATMSCKQTQPifPIHLAAEYRKPQSLL-------------CLLQHGADPEVRDAQGF 67
Cdd:cd22194    2 MDSNIRQCPSGNCDDMDSPQSPQDDTPSNPNSP--SAELAKEEQRDKKKRlkkvseaaveelgELLKELKDLSRRRRKTD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216230  68 TTLHLMLlNWPASSTTwskpSTQIQKILMDIQNNAVLCLCILCDHGAQ-------VNARVDNSN--KHSALHLAIIHGTY 138
Cdd:cd22194   80 VPDFLMH-KLTASDTG----KTCLMKALLNINENTKEIVRILLAFAEEngildrfINAEYTEEAyeGQTALNIAIERRQG 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216230 139 PVLSFLAQNGAQVNAtnessmtplHMAADILNKNMIETLIAFganvncaisstGNTALKLAVCTASSKVgrllaagvgcI 218
Cdd:cd22194  155 DIVKLLIAKGADVNA---------HAKGVFFNPKYKHEGFYF-----------GETPLALAACTNQPEI----------V 204

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216230 219 RLLLNNGAQ-VNAQDHEGQTALHeacfggreAIISLLLEFEANVNILTRngespiyMYLQRSSNIRDRSLLArllyrtyp 297
Cdd:cd22194  205 QLLMEKESTdITSQDSRGNTVLH--------ALVTVAEDSKTQNDFVKR-------MYDMILLKSENKNLET-------- 261

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216230 298 lrLSNKQGILPAgimlpeyQLLRETlvklsKKPLTLEAICKRSIRnvygEKYKFHLEKllpaKLWNSIYG-----IYDLT 372
Cdd:cd22194  262 --IRNNEGLTPL-------QLAAKM-----GKAEILKYILSREIK----EKPNRSLSR----KFTDWAYGpvsssLYDLT 319


                 ....*..
gi 894216230 373 YLLKGEP 379
Cdd:cd22194  320 NVDTTTD 326
PHA02798 PHA02798
ankyrin-like protein; Provisional
 218-279 2.47e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 39.82  E-value: 2.47e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216230 218 IRLLLNNGAQVNAQDHEGQTALheaC--------FGGREAIISLLLEFEANVNILTRNGESPIYMYLQRS 279
Cdd:PHA02798  54 VKLFINLGANVNGLDNEYSTPL---CtilsnikdYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNG 120
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 160-240 2.49e-03

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 39.86  E-value: 2.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216230 160 TPLHMAADILNKNMIETLIAFGANVNCAISST------------GNTALKLAVCTASSKVgrllaagvgcIRLLLNNGAQ 227
Cdd:cd21882   75 TALHIAIENRNLNLVRLLVENGADVSARATGRffrkspgnlfyfGELPLSLAACTNQEEI----------VRLLLENGAQ 144

                         90
                 ....*....|....*.
gi 894216230 228 ---VNAQDHEGQTALH 240
Cdd:cd21882  145 paaLEAQDSLGNTVLH 160
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 234-263 2.52e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 34.93  E-value: 2.52e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 894216230  234 EGQTALHEACFGGREAIISLLLEFEANVNI 263
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02798 PHA02798
ankyrin-like protein; Provisional
 49-196 2.86e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 39.43  E-value: 2.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216230  49 LLCLLQHGADPEVRDAQGFTTLHLMLL------------------------NWPASSTTWSKPSTQIQKILMDIqnnavl 104
Cdd:PHA02798 128 LLFMIENGADTTLLDKDGFTMLQVYLQsnhhidieiiklllekgvdinthnNKEKYDTLHCYFKYNIDRIDADI------ 201

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216230 105 cLCILCDHGAQVNaRVDNSNKHSALHLaiihgtypVLSFLAQNGA-------------QVNATNESSMTPLHMAADILNK 171
Cdd:PHA02798 202 -LKLFVDNGFIIN-KENKSHKKKFMEY--------LNSLLYDNKRfkknildfifsyiDINQVDELGFNPLYYSVSHNNR 271

                        170       180
                 ....*....|....*....|....*
gi 894216230 172 NMIETLIAFGANVNCaISSTGNTAL 196
Cdd:PHA02798 272 KIFEYLLQLGGDINI-ITELGNTCL 295
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 89-319 2.87e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 39.78  E-value: 2.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216230  89 TQIQKILMDIQNNAVLCLCILCDHGAQ-------VNARVDNS--NKHSALHLAIIHGTYPVLSFLAQNGAQVNAtnessm 159
Cdd:cd22193   31 TCLMKALLNLNPGTNDTIRILLDIAEKtdnlkrfINAEYTDEyyEGQTALHIAIERRQGDIVALLVENGADVHA------ 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216230 160 tplHMAADILNKNMIETLIAFganvncaisstGNTALKLAVCTASSKVgrllaagvgcIRLLLNNG---AQVNAQDHEGQ 236
Cdd:cd22193  105 ---HAKGRFFQPKYQGEGFYF-----------GELPLSLAACTNQPDI----------VQYLLENEhqpADIEAQDSRGN 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216230 237 TALHeacfggreAIISLLLEFEANVNILTRngespIY-MYLQRSSNIRDRSLLARLLYRT--YPLRLSNKQG-------I 306
Cdd:cd22193  161 TVLH--------ALVTVADNTKENTKFVTR-----MYdMILIRGAKLCPTVELEEIRNNDglTPLQLAAKMGkieilkyI 227

                        250
                 ....*....|...
gi 894216230 307 LPAGIMLPEYQLL 319
Cdd:cd22193  228 LQREIKEPELRHL 240
PHA03095 PHA03095
ankyrin-like protein; Provisional
 36-76 3.58e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 39.24  E-value: 3.58e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 894216230  36 PIHLAAEYRKPQSLLCLLQHGADPEVRDAQGFTTLHLMLLN 76
Cdd:PHA03095 260 PLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRN 300
Ank_5 pfam13857
Ankyrin repeats (many copies);
220-272 4.16e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.01  E-value: 4.16e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 894216230  220 LLLNNGAQVNAQDHEGQTALHEACFGGREAIISLLLEFEANVNILTRNGESPI 272
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
Ank_5 pfam13857
Ankyrin repeats (many copies);
144-199 4.37e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.01  E-value: 4.37e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 894216230  144 LAQNG-AQVNATNESSMTPLHMAADILNKNMIETLIAFGANVNcAISSTGNTALKLA 199
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLN-LKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
237-274 4.56e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 34.94  E-value: 4.56e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 894216230  237 TALHEACFGGREAIISLLLEFEANVNILTRNGESPIYM 274
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHF 40
PHA02946 PHA02946
ankyin-like protein; Provisional
 109-280 5.94e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 38.50  E-value: 5.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216230 109 LCDHGAQVNARVDNSNkhSALHLAIIHGTYPVLSFLAQNGAQVNATNESSMTPLHMAADILNK--NMIETLIAFGANVNC 186
Cdd:PHA02946  58 LLHRGYSPNETDDDGN--YPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEviERINLLVQYGAKINN 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 894216230 187 AISSTGNTALkLAVCTASSKV-GRLLAAG------------------------VGCIRLLLNNGAQVNAQDHEGQTALHE 241
Cdd:PHA02946 136 SVDEEGCGPL-LACTDPSERVfKKIMSIGfearivdkfgknhihrhlmsdnpkASTISWMMKLGISPSKPDHDGNTPLHI 214

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 894216230 242 ACFGGREA--IISLLLEfEANVNILTRNGESPIYMYLQRSS 280
Cdd:PHA02946 215 VCSKTVKNvdIINLLLP-STDVNKQNKFGDSPLTLLIKTLS 254
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 234-263 7.73e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 33.72  E-value: 7.73e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 894216230   234 EGQTALHEACFGGREAIISLLLEFEANVNI 263
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
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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