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Conserved domains on  [gi|13385192|ref|NP_080008|]
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ankyrin repeat domain-containing protein 61 isoform 1 [Mus musculus]

Protein Classification

ankyrin repeat domain-containing protein( domain architecture ID 13270520)

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

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];
136-334 8.00e-29

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 114.28  E-value: 8.00e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385192 136 ILMDIQNNAVLCLCILCDHGAQVNARvdNSNKHSALHLAIIHGTYPVLSFLAQNGAQVNATNESSMTPLHMAADILNKNM 215
Cdd:COG0666  58 LLAAALAGDLLVALLLLAAGADINAK--DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEI 135

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385192 216 IETLIAFGANVNcAISSTGNTALKLAVCTASSKVgrllaagvgcIRLLLNNGAQVNAQDHEGQTALHEACFGGREAIISL 295
Cdd:COG0666 136 VKLLLEAGADVN-AQDNDGNTPLHLAAANGNLEI----------VKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKL 204

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 13385192 296 LLEFEANVNILTRNGESPIYMYLQRSSNIRDRSLLARLL 334
Cdd:COG0666 205 LLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243
PHA02875 super family cl31516
ankyrin repeat protein; Provisional
 28-227 2.70e-03

ankyrin repeat protein; Provisional


The actual alignment was detected with superfamily member PHA02875:

Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 39.97  E-value: 2.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385192   28 LHSKLYEAIIKEDCNTIKTLLRnhpvnqpLTILANSTRYRllsqqtQPIFPIHLAAEYRKPQSLLCLLQHGADPEVRDAQ 107
Cdd:PHA02875  68 IESELHDAVEEGDVKAVEELLD-------LGKFADDVFYK------DGMTPLHLATILKKLDIMKLLIARGADPDIPNTD 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385192  108 GFTTLHLMLLNWPASSTTwskpstqiqkilmdiqnnavlclcILCDHGAQVNarVDNSNKHSALHLAIIHGTYPVLSFLA 187
Cdd:PHA02875 135 KFSPLHLAVMMGDIKGIE------------------------LLIDHKACLD--IEDCCGCTPLIIAMAKGDIAICKMLL 188

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 13385192  188 QNGAQVNATNESSMTPLHMAADILNK-NMIETLIAFGANVN 227
Cdd:PHA02875 189 DSGANIDYFGKNGCVAALCYAIENNKiDIVRLFIKRGADCN 229
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
136-334 8.00e-29

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 114.28  E-value: 8.00e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385192 136 ILMDIQNNAVLCLCILCDHGAQVNARvdNSNKHSALHLAIIHGTYPVLSFLAQNGAQVNATNESSMTPLHMAADILNKNM 215
Cdd:COG0666  58 LLAAALAGDLLVALLLLAAGADINAK--DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEI 135

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385192 216 IETLIAFGANVNcAISSTGNTALKLAVCTASSKVgrllaagvgcIRLLLNNGAQVNAQDHEGQTALHEACFGGREAIISL 295
Cdd:COG0666 136 VKLLLEAGADVN-AQDNDGNTPLHLAAANGNLEI----------VKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKL 204

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 13385192 296 LLEFEANVNILTRNGESPIYMYLQRSSNIRDRSLLARLL 334
Cdd:COG0666 205 LLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 75-316 7.44e-19

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 87.80  E-value: 7.44e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385192   75 PIFPIHLAAEYRKPQSLLCLLQHGADPEVRDAQGFTTLHLMLLNwpassttwskpstqiqkilMDIQNNAVLCLCILCDH 154
Cdd:PHA03100  35 PVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNI-------------------KYNLTDVKEIVKLLLEY 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385192  155 GAQVNARVDNSNkhSALHLAIIH--GTYPVLSFLAQNGAQVNATNESSMTPLHMAAD--ILNKNMIETLIAFGANVNcAI 230
Cdd:PHA03100  96 GANVNAPDNNGI--TPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLEsnKIDLKILKLLIDKGVDIN-AK 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385192  231 SStgntalklavctasskvgrllaagvgcIRLLLNNGAQVNAQDHEGQTALHEACFGGREAIISLLLEFEANVNILTRNG 310
Cdd:PHA03100 173 NR---------------------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYG 225


                 ....*.
gi 13385192  311 ESPIYM 316
Cdd:PHA03100 226 DTPLHI 231
Ank_2 pfam12796
Ankyrin repeats (3 copies);
171-274 2.59e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 59.74  E-value: 2.59e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385192   171 LHLAIIHGTYPVLSFLAQNGAQVNATNESSMTPLHMAADILNKNMIETLIafgANVNCAISSTGNTALKLAVCTASSKvg 250
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL---EHADVNLKDNGRTALHYAARSGHLE-- 75

                          90       100
                  ....*....|....*....|....
gi 13385192   251 rllaagvgCIRLLLNNGAQVNAQD 274
Cdd:pfam12796  76 --------IVKLLLEKGADINVKD 91
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 169-282 1.07e-07

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 53.86  E-value: 1.07e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385192 169 SALHLAIIHGTYPVLSFLAQNGAQ-VNATNESSM----TPLHMAADILNKNMIETLIAFGANVN-------------CAI 230
Cdd:cd22192  53 TALHVAALYDNLEAAVVLMEAAPElVNEPMTSDLyqgeTALHIAVVNQNLNLVRELIARGADVVspratgtffrpgpKNL 132

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 13385192 231 SSTGNTALKLAVCTASSKVgrllaagvgcIRLLLNNGAQVNAQDHEGQTALH 282
Cdd:cd22192 133 IYYGEHPLSFAACVGNEEI----------VRLLIEHGADIRAQDSLGNTVLH 174
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 168-300 7.82e-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: 45.07  E-value: 7.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385192   168 HSALHLAIIHGTYPVLSFLAQNGAQVNAT------NESSMT--------PLHMAADILNKNMIETLIAFGANVNCAIsST 233
Cdd:TIGR00870 129 ITALHLAAHRQNYEIVKLLLERGASVPARacgdffVKSQGVdsfyhgesPLNAAACLGSPSIVALLSEDPADILTAD-SL 207

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13385192   234 GNTALKLAVCTASSKVgRLLAAGVGCIRLLLNNGAQ----------VNaqdHEGQTALHEACFGGREAIISLLLEFE 300
Cdd:TIGR00870 208 GNTLLHLLVMENEFKA-EYEELSCQMYNFALSLLDKlrdskeleviLN---HQGLTPLKLAAKEGRIVLFRLKLAIK 280
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 28-227 2.70e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 39.97  E-value: 2.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385192   28 LHSKLYEAIIKEDCNTIKTLLRnhpvnqpLTILANSTRYRllsqqtQPIFPIHLAAEYRKPQSLLCLLQHGADPEVRDAQ 107
Cdd:PHA02875  68 IESELHDAVEEGDVKAVEELLD-------LGKFADDVFYK------DGMTPLHLATILKKLDIMKLLIARGADPDIPNTD 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385192  108 GFTTLHLMLLNWPASSTTwskpstqiqkilmdiqnnavlclcILCDHGAQVNarVDNSNKHSALHLAIIHGTYPVLSFLA 187
Cdd:PHA02875 135 KFSPLHLAVMMGDIKGIE------------------------LLIDHKACLD--IEDCCGCTPLIIAMAKGDIAICKMLL 188

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 13385192  188 QNGAQVNATNESSMTPLHMAADILNK-NMIETLIAFGANVN 227
Cdd:PHA02875 189 DSGANIDYFGKNGCVAALCYAIENNKiDIVRLFIKRGADCN 229
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 201-228 3.11e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.87  E-value: 3.11e-03
                           10        20
                   ....*....|....*....|....*...
gi 13385192    201 MTPLHMAADILNKNMIETLIAFGANVNC 228
Cdd:smart00248   3 RTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
136-334 8.00e-29

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 114.28  E-value: 8.00e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385192 136 ILMDIQNNAVLCLCILCDHGAQVNARvdNSNKHSALHLAIIHGTYPVLSFLAQNGAQVNATNESSMTPLHMAADILNKNM 215
Cdd:COG0666  58 LLAAALAGDLLVALLLLAAGADINAK--DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEI 135

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385192 216 IETLIAFGANVNcAISSTGNTALKLAVCTASSKVgrllaagvgcIRLLLNNGAQVNAQDHEGQTALHEACFGGREAIISL 295
Cdd:COG0666 136 VKLLLEAGADVN-AQDNDGNTPLHLAAANGNLEI----------VKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKL 204

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 13385192 296 LLEFEANVNILTRNGESPIYMYLQRSSNIRDRSLLARLL 334
Cdd:COG0666 205 LLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
150-345 1.31e-27

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 110.81  E-value: 1.31e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385192 150 ILCDHGAQVNARvdNSNKHSALHLAIIHGTYPVLSFLAQNGAQVNATNESSMTPLHMAADILNKNMIETLIAFGANVNcA 229
Cdd:COG0666 105 LLLEAGADVNAR--DKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVN-A 181

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385192 230 ISSTGNTALKLAVCTASSKVgrllaagvgcIRLLLNNGAQVNAQDHEGQTALHEACFGGREAIISLLLEFEANVNILTRN 309
Cdd:COG0666 182 RDNDGETPLHLAAENGHLEI----------VKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKD 251

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 13385192 310 GESPIYMYLQRSSNIRDRSLLARLLYRTYPLRLSNK 345
Cdd:COG0666 252 GLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
78-311 8.61e-25

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 103.11  E-value: 8.61e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385192  78 PIHLAAEYRKPQSLLCLLQHGADPEVRDAQGFTTLHLMllnwpassttwskpstqiqkilmdIQNNAVLCLCILCDHGAQ 157
Cdd:COG0666  90 LLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLA------------------------AYNGNLEIVKLLLEAGAD 145

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385192 158 VNARvdNSNKHSALHLAIIHGTYPVLSFLAQNGAQVNATNESSMTPLHMAADILNKNMIETLIAFGANVNcAISSTGNTA 237
Cdd:COG0666 146 VNAQ--DNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVN-AKDNDGKTA 222

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13385192 238 LKLAVCTASSKVgrllaagvgcIRLLLNNGAQVNAQDHEGQTALHEACFGGREAIISLLLEFEANVNILTRNGE 311
Cdd:COG0666 223 LDLAAENGNLEI----------VKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLL 286
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
137-316 1.15e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 100.03  E-value: 1.15e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385192 137 LMDIQNNAVLCLCILCDHGAQVNARVDNSNKHSALHLAIIHGTYPVLSFLAQNGAQVNATNESSMTPLHMAADILNKNMI 216
Cdd:COG0666  24 LLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIV 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385192 217 ETLIAFGANVNcAISSTGNTALKLAVCTASSKVgrllaagvgcIRLLLNNGAQVNAQDHEGQTALHEACFGGREAIISLL 296
Cdd:COG0666 104 KLLLEAGADVN-ARDKDGETPLHLAAYNGNLEI----------VKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLL 172

                       170       180
                ....*....|....*....|
gi 13385192 297 LEFEANVNILTRNGESPIYM 316
Cdd:COG0666 173 LEAGADVNARDNDGETPLHL 192
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 75-316 7.44e-19

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 87.80  E-value: 7.44e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385192   75 PIFPIHLAAEYRKPQSLLCLLQHGADPEVRDAQGFTTLHLMLLNwpassttwskpstqiqkilMDIQNNAVLCLCILCDH 154
Cdd:PHA03100  35 PVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNI-------------------KYNLTDVKEIVKLLLEY 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385192  155 GAQVNARVDNSNkhSALHLAIIH--GTYPVLSFLAQNGAQVNATNESSMTPLHMAAD--ILNKNMIETLIAFGANVNcAI 230
Cdd:PHA03100  96 GANVNAPDNNGI--TPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLEsnKIDLKILKLLIDKGVDIN-AK 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385192  231 SStgntalklavctasskvgrllaagvgcIRLLLNNGAQVNAQDHEGQTALHEACFGGREAIISLLLEFEANVNILTRNG 310
Cdd:PHA03100 173 NR---------------------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYG 225


                 ....*.
gi 13385192  311 ESPIYM 316
Cdd:PHA03100 226 DTPLHI 231
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 150-324 3.92e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 83.01  E-value: 3.92e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385192  150 ILCDHGAQVNaRVDNSNKHSALHLAIIHGTYPVLSFLAQNGAQVNATNESSMTPLHMAADILNKNMIETLIAFGANVNcA 229
Cdd:PHA02878 152 LLLSYGADIN-MKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTD-A 229

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385192  230 ISSTGNTALKLAvctasskVGRLLAAGVgcIRLLLNNGAQVNAQDH-EGQTALHEACFGgrEAIISLLLEFEANVNILTR 308
Cdd:PHA02878 230 RDKCGNTPLHIS-------VGYCKDYDI--LKLLLEHGVDVNAKSYiLGLTALHSSIKS--ERKLKLLLEYGADINSLNS 298

                        170
                 ....*....|....*.
gi 13385192  309 NGESPIYMYLQRSSNI 324
Cdd:PHA02878 299 YKLTPLSSAVKQYLCI 314
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
78-271 5.49e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 80.77  E-value: 5.49e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385192  78 PIHLAAEYRKPQSLLCLLQHGADPEVRDAQGFTTLHLMllnwpassttwskpstqiqkilmdIQNNAVLCLCILCDHGAQ 157
Cdd:COG0666 123 PLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA------------------------AANGNLEIVKLLLEAGAD 178

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385192 158 VNARvdNSNKHSALHLAIIHGTYPVLSFLAQNGAQVNATNESSMTPLHMAADILNKNMIETLIAFGANVNcAISSTGNTA 237
Cdd:COG0666 179 VNAR--DNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN-AKDKDGLTA 255

                       170       180       190
                ....*....|....*....|....*....|....
gi 13385192 238 LKLAVCTASSKVGRLLAAGVGCIRLLLNNGAQVN 271
Cdd:COG0666 256 LLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA03095 PHA03095
ankyrin-like protein; Provisional
 78-314 1.84e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 75.06  E-value: 1.84e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385192   78 PIHLAAEYRKPQS---LLCLLQHGADPEVRDAQGFTTLHLMLLNwpasSTTWSkpstqiqkiLMDIqnnavlclciLCDH 154
Cdd:PHA03095  50 PLHLYLHYSSEKVkdiVRLLLEAGADVNAPERCGFTPLHLYLYN----ATTLD---------VIKL----------LIKA 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385192  155 GAQVNARVDNSNkhSALHlaiIHGT-----YPVLSFLAQNGAQVNATNESSMTPLHmaADILNKN----MIETLIAFGAN 225
Cdd:PHA03095 107 GADVNAKDKVGR--TPLH---VYLSgfninPKVIRLLLRKGADVNALDLYGMTPLA--VLLKSRNanveLLRLLIDAGAD 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385192  226 VnCAISSTGNTAL---KLAVCTASSKVGRLLAAGVG--------------------CIRL----LLNNGAQVNAQDHEGQ 278
Cdd:PHA03095 180 V-YAVDDRFRSLLhhhLQSFKPRARIVRELIRAGCDpaatdmlgntplhsmatgssCKRSlvlpLLIAGISINARNRYGQ 258

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 13385192  279 TALHEA-CFGGREAiISLLLEFEANVNILTRNGESPI 314
Cdd:PHA03095 259 TPLHYAaVFNNPRA-CRRLIALGADINAVSSDGNTPL 294
PHA03095 PHA03095
ankyrin-like protein; Provisional
 94-316 3.01e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 74.29  E-value: 3.01e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385192   94 LLQHGADPEVRDAQGFTTLHLMLLNwpassttWSKPSTQIQKILMdiqnnavlclcilcDHGAQVNARvdNSNKHSALHL 173
Cdd:PHA03095  33 LLAAGADVNFRGEYGKTPLHLYLHY-------SSEKVKDIVRLLL--------------EAGADVNAP--ERCGFTPLHL 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385192  174 AIIHG-TYPVLSFLAQNGAQVNATNESSMTPLH--MAADILNKNMIETLIAFGANVNcAISSTGNTAlkLAVCTASSK-- 248
Cdd:PHA03095  90 YLYNAtTLDVIKLLIKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVN-ALDLYGMTP--LAVLLKSRNan 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385192  249 ---VGRLLAAGV------------------------GCIRLLLNNGAQVNAQDHEGQTALHEACFGG--REAIISLLLEF 299
Cdd:PHA03095 167 velLRLLIDAGAdvyavddrfrsllhhhlqsfkpraRIVRELIRAGCDPAATDMLGNTPLHSMATGSscKRSLVLPLLIA 246

                        250
                 ....*....|....*..
gi 13385192  300 EANVNILTRNGESPIYM 316
Cdd:PHA03095 247 GISINARNRYGQTPLHY 263
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 140-364 7.90e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 72.69  E-value: 7.90e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385192  140 IQNNAVLCLCILCDHGAQVNARVDNSNkhSALHLAIIHGTYPVLSFLAQNGAQVNATNESSMTPLHMAADILNKNMIETL 219
Cdd:PHA02874 132 IKKGDLESIKMLFEYGADVNIEDDNGC--YPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLL 209

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385192  220 IAFGANVNCAISStGNTALKLAVCTASSkvgrllaagvgCIRLLLNNgAQVNAQDHEGQTALHEAC-FGGREAIISLLLE 298
Cdd:PHA02874 210 IDHGNHIMNKCKN-GFTPLHNAIIHNRS-----------AIELLINN-ASINDQDIDGSTPLHHAInPPCDIDIIDILLY 276

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13385192  299 FEANVNILTRNGESPI---YMYLQRSSNIRDrsLLARLLyrtyplrLSNKQGILPAGIMLPEYQLLRET 364
Cdd:PHA02874 277 HKADISIKDNKGENPIdtaFKYINKDPVIKD--IIANAV-------LIKEADKLKDSDFLEHIEIKDNK 336
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 76-308 1.15e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 66.63  E-value: 1.15e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385192   76 IFPIHLAAEYRKPQSLLCLLQHGADPEVRDAQGFTTLHLMLLN-----WPASSTTWSKPSTQIQKILMDIQNNAVLCLCI 150
Cdd:PHA02876 179 ITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSknidtIKAIIDNRSNINKNDLSLLKAIRNEDLETSLL 258

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385192  151 LCDHGAQVNArVDNSnKHSALHLAIihgTYPVLSFLA----QNGAQVNATNESSMTPLH-MAADILNKNMIETLIAFGAN 225
Cdd:PHA02876 259 LYDAGFSVNS-IDDC-KNTPLHHAS---QAPSLSRLVpkllERGADVNAKNIKGETPLYlMAKNGYDTENIRTLIMLGAD 333

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385192  226 VNcAISSTGNTALKLAVCTASSKvgrllaagvGCIRLLLNNGAQVNAQDHEGQTALHEACFGGREAIISLLLEFEANVNI 305
Cdd:PHA02876 334 VN-AADRLYITPLHQASTLDRNK---------DIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEA 403


                 ...
gi 13385192  306 LTR 308
Cdd:PHA02876 404 LSQ 406
Ank_2 pfam12796
Ankyrin repeats (3 copies);
171-274 2.59e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 59.74  E-value: 2.59e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385192   171 LHLAIIHGTYPVLSFLAQNGAQVNATNESSMTPLHMAADILNKNMIETLIafgANVNCAISSTGNTALKLAVCTASSKvg 250
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL---EHADVNLKDNGRTALHYAARSGHLE-- 75

                          90       100
                  ....*....|....*....|....
gi 13385192   251 rllaagvgCIRLLLNNGAQVNAQD 274
Cdd:pfam12796  76 --------IVKLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 94-242 3.26e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 64.66  E-value: 3.26e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385192   94 LLQHGADPEVRDAQGFTTLHLMLLNwpassttwSKPSTQIQKILMDiqnnavlclcilcdhgAQVNARVDNSNKHSALHL 173
Cdd:PHA03095 173 LIDAGADVYAVDDRFRSLLHHHLQS--------FKPRARIVRELIR----------------AGCDPAATDMLGNTPLHS 228

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13385192  174 AIIHGT--YPVLSFLAQNGAQVNATNESSMTPLHMAADILNKNMIETLIAFGANVNCaISSTGNTALKLAV 242
Cdd:PHA03095 229 MATGSSckRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINA-VSSDGNTPLSLMV 298
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 78-319 8.61e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 63.93  E-value: 8.61e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385192   78 PIHLAAEYRKPQSLLC-LLQHGADPEVRDAQGFTTLHLMLLNwpassttwSKPSTQIQKILMdiqnnavlclcilcdHGA 156
Cdd:PHA02876 276 PLHHASQAPSLSRLVPkLLERGADVNAKNIKGETPLYLMAKN--------GYDTENIRTLIM---------------LGA 332

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385192  157 QVNA--RVDNSNKHSALHLAIIHGTypVLSFLaQNGAQVNATNESSMTPLHMAADILNKNMIETLIAFGANVNcAISSTG 234
Cdd:PHA02876 333 DVNAadRLYITPLHQASTLDRNKDI--VITLL-ELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIE-ALSQKI 408

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385192  235 NTALKLAVCTASSKVGrllaagvgcIRLLLNNGAQVNAQDHEGQTALHEACFGG-REAIISLLLEFEANVNILTRNGESP 313
Cdd:PHA02876 409 GTALHFALCGTNPYMS---------VKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYP 479


                 ....*.
gi 13385192  314 IYMYLQ 319
Cdd:PHA02876 480 LLIALE 485
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 252-336 2.30e-10

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 62.61  E-value: 2.30e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385192  252 LLAAG--VGcIRLLLNNGAQVNAQDHEGQTALHEACFGGREAIISLLLEFEANVNILTRNGESPiyMYLQRSSNIRDrsl 329
Cdd:PTZ00322  89 LAASGdaVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTP--LELAEENGFRE--- 162


                 ....*..
gi 13385192  330 LARLLYR 336
Cdd:PTZ00322 163 VVQLLSR 169
PHA03095 PHA03095
ankyrin-like protein; Provisional
 186-324 3.49e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 61.58  E-value: 3.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385192  186 LAQNGAQVNATNESSMTPLHM---AADILNKNMIETLIAFGANVNcAISSTGNTALKLAVCTASSkvgrllaagVGCIRL 262
Cdd:PHA03095  33 LLAAGADVNFRGEYGKTPLHLylhYSSEKVKDIVRLLLEAGADVN-APERCGFTPLHLYLYNATT---------LDVIKL 102

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13385192  263 LLNNGAQVNAQDHEGQTALHeACFGG---REAIISLLLEFEANVNILTRNGESPIYMYLqRSSNI 324
Cdd:PHA03095 103 LIKAGADVNAKDKVGRTPLH-VYLSGfniNPKVIRLLLRKGADVNALDLYGMTPLAVLL-KSRNA 165
Ank_2 pfam12796
Ankyrin repeats (3 copies);
204-305 1.23e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 54.74  E-value: 1.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385192   204 LHMAADILNKNMIETLIAFGANVNCaISSTGNTALKLAVCTASSKvgrllaagvgCIRLLLNNgAQVNAQDHeGQTALHE 283
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANL-QDKNGRTALHLAAKNGHLE----------IVKLLLEH-ADVNLKDN-GRTALHY 67

                          90       100
                  ....*....|....*....|..
gi 13385192   284 ACFGGREAIISLLLEFEANVNI 305
Cdd:pfam12796  68 AARSGHLEIVKLLLEKGADINV 89
Ank_4 pfam13637
Ankyrin repeats (many copies);
169-220 2.14e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.05  E-value: 2.14e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 13385192   169 SALHLAIIHGTYPVLSFLAQNGAQVNATNESSMTPLHMAADILNKNMIETLI 220
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 201-338 3.24e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 58.52  E-value: 3.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385192  201 MTPLHMAADILNKNMIETLIAFGANVNcaISSTGN-TALKLAVCTASSkvgrlLAAGVGCIRLLLNNGAQVNAQDHEGQT 279
Cdd:PHA03100  36 VLPLYLAKEARNIDVVKILLDNGADIN--SSTKNNsTPLHYLSNIKYN-----LTDVKEIVKLLLEYGANVNAPDNNGIT 108

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13385192  280 ALHEACFGGREA--IISLLLEFEANVNILTRNGESPIYMYLqrSSNIRDRSLLARLLYRTY 338
Cdd:PHA03100 109 PLLYAISKKSNSysIVEYLLDNGANVNIKNSDGENLLHLYL--ESNKIDLKILKLLIDKGV 167
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 133-310 4.08e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 58.08  E-value: 4.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385192  133 IQKILMDIQNNAVLCLCILCDHGAQVNarVDNSNKHSALHLAIIHGTYPVLSFLAQNGAQVN-ATNESSMTPLHMAADIL 211
Cdd:PHA02875  36 ISPIKLAMKFRDSEAIKLLMKHGAIPD--VKYPDIESELHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILK 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385192  212 NKNMIETLIAFGANVNcaISSTGNTA-LKLAVctasskvgrlLAAGVGCIRLLLNNGAQVNAQDHEGQTALHEACFGGRE 290
Cdd:PHA02875 114 KLDIMKLLIARGADPD--IPNTDKFSpLHLAV----------MMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDI 181

                        170       180
                 ....*....|....*....|
gi 13385192  291 AIISLLLEFEANVNILTRNG 310
Cdd:PHA02875 182 AICKMLLDSGANIDYFGKNG 201
PHA03095 PHA03095
ankyrin-like protein; Provisional
 193-325 5.72e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 57.73  E-value: 5.72e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385192  193 VNATNESSMTPLHMAADILNKNMIETLIAFGANVNCAiSSTGNTALKLAVCTASSKVGRLlaagvgcIRLLLNNGAQVNA 272
Cdd:PHA03095   7 VDIIMEAALYDYLLNASNVTVEEVRRLLAAGADVNFR-GEYGKTPLHLYLHYSSEKVKDI-------VRLLLEAGADVNA 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 13385192  273 QDHEGQTALH-EACFGGREAIISLLLEFEANVNILTRNGESPIYMYLqRSSNIR 325
Cdd:PHA03095  79 PERCGFTPLHlYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVYL-SGFNIN 131
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 153-347 2.11e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 55.74  E-value: 2.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385192  153 DHGAQVNARvdNSNKHSALHLAIIHGTYPVLSFLAQNGAQVNATNESSMTPLHMAADILNKNMIETLIAFGANVNCAiSS 232
Cdd:PHA02874 112 DCGIDVNIK--DAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVK-DN 188

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385192  233 TGNTALKLAVCTASSKvgrllaagvgCIRLLLNNGAQVNAQDHEGQTALHEACFGGREAIisLLLEFEANVNILTRNGES 312
Cdd:PHA02874 189 NGESPLHNAAEYGDYA----------CIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAI--ELLINNASINDQDIDGST 256

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 13385192  313 PIYMYLQRSSnirDRSLLARLLYRTYPLRLSNKQG 347
Cdd:PHA02874 257 PLHHAINPPC---DIDIIDILLYHKADISIKDNKG 288
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 182-332 4.88e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 55.07  E-value: 4.88e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385192  182 VLSFLAQNGAQVNATNESSMTPLHMAADILNKNMIETLIAFGANVN-----------CAISSTGNTALKlAVCTASSKVG 250
Cdd:PHA02876 160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNiialddlsvleCAVDSKNIDTIK-AIIDNRSNIN 238

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385192  251 RLLAAGVGCIR--------LLLNNGAQVNAQDHEGQTALHEACFG-GREAIISLLLEFEANVNILTRNGESPIYMYLQRS 321
Cdd:PHA02876 239 KNDLSLLKAIRnedletslLLYDAGFSVNSIDDCKNTPLHHASQApSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNG 318

                        170
                 ....*....|..
gi 13385192  322 SNIRD-RSLLAR 332
Cdd:PHA02876 319 YDTENiRTLIML 330
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 169-282 1.07e-07

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 53.86  E-value: 1.07e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385192 169 SALHLAIIHGTYPVLSFLAQNGAQ-VNATNESSM----TPLHMAADILNKNMIETLIAFGANVN-------------CAI 230
Cdd:cd22192  53 TALHVAALYDNLEAAVVLMEAAPElVNEPMTSDLyqgeTALHIAVVNQNLNLVRELIARGADVVspratgtffrpgpKNL 132

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 13385192 231 SSTGNTALKLAVCTASSKVgrllaagvgcIRLLLNNGAQVNAQDHEGQTALH 282
Cdd:cd22192 133 IYYGEHPLSFAACVGNEEI----------VRLLIEHGADIRAQDSLGNTVLH 174
Ank_2 pfam12796
Ankyrin repeats (3 copies);
140-227 1.23e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 49.34  E-value: 1.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385192   140 IQNNAVLCLCILCDHGAQVNarVDNSNKHSALHLAIIHGTYPVLSFLAQNgAQVNATNEsSMTPLHMAADILNKNMIETL 219
Cdd:pfam12796   5 AKNGNLELVKLLLENGADAN--LQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLL 80


                  ....*...
gi 13385192   220 IAFGANVN 227
Cdd:pfam12796  81 LEKGADIN 88
Ank_4 pfam13637
Ankyrin repeats (many copies);
259-297 2.02e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.27  E-value: 2.02e-07
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 13385192   259 CIRLLLNNGAQVNAQDHEGQTALHEACFGGREAIISLLL 297
Cdd:pfam13637  16 LLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 209-336 3.48e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 52.19  E-value: 3.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385192  209 DILNKNMIETLIAFGANVNCAISSTGNTALKLAvctASSKVGRLLaagvgciRLLLNNGAQVNAQDHEGQTALHEACFGG 288
Cdd:PHA02878 143 DIIEAEITKLLLSYGADINMKDRHKGNTALHYA---TENKDQRLT-------ELLLSYGANVNIPDKTNNSPLHHAVKHY 212

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 13385192  289 REAIISLLLEFEANVNILTRNGESPIYMylqRSSNIRDRSLLARLLYR 336
Cdd:PHA02878 213 NKPIVHILLENGASTDARDKCGNTPLHI---SVGYCKDYDILKLLLEH 257
Ank_2 pfam12796
Ankyrin repeats (3 copies);
259-315 4.96e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 47.42  E-value: 4.96e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 13385192   259 CIRLLLNNGAQVNAQDHEGQTALHEACFGGREAIISLLLEFeANVNILTrNGESPIY 315
Cdd:pfam12796  12 LVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALH 66
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 193-322 5.12e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 51.50  E-value: 5.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385192  193 VNATNESSMTPLHMAADILNKNMIETLIAFGANVNCAISSTGNTALKLAVCTASSKVGRLLAAGVGC------------I 260
Cdd:PHA02874  28 INISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTsilpipciekdmI 107

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13385192  261 RLLLNNGAQVNAQDHEGQTALHEACFGGREAIISLLLEFEANVNILTRNGESPIYMYLQRSS 322
Cdd:PHA02874 108 KTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNF 169
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 76-227 8.53e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 50.82  E-value: 8.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385192   76 IFPIHLAAEYRKPQSLLC--LLQHGADPEVRDAQGFTTLHLMLLNwpassttwSKPSTQIQKILmdIQNNAVLCLC---- 149
Cdd:PHA03100 107 ITPLLYAISKKSNSYSIVeyLLDNGANVNIKNSDGENLLHLYLES--------NKIDLKILKLL--IDKGVDINAKnrvn 176

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13385192  150 ILCDHGAQVNARVDNSNkhSALHLAIIHGTYPVLSFLAQNGAQVNATNESSMTPLHMAADILNKNMIETLIAFGANVN 227
Cdd:PHA03100 177 YLLSYGVPINIKDVYGF--TPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
Ank_2 pfam12796
Ankyrin repeats (3 copies);
79-197 9.63e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 46.65  E-value: 9.63e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385192    79 IHLAAEYRKPQSLLCLLQHGADPEVRDAQGFTTLHLmllnwpAssttwskpstqiqkilmdIQNNAVLCLCILCDHgAQV 158
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHL------A------------------AKNGHLEIVKLLLEH-ADV 55

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 13385192   159 NarvDNSNKHSALHLAIIHGTYPVLSFLAQNGAQVNATN 197
Cdd:pfam12796  56 N---LKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA02743 PHA02743
Viral ankyrin protein; Provisional
 142-234 6.97e-06

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 45.96  E-value: 6.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385192  142 NNAVLCLCILCDHGAQVNARVDNSNkHSALHLAIIHGTYPVLSFLAQN-GAQVNATNESSMTPLHMAADILNKNMIETLI 220
Cdd:PHA02743  70 ANAVMKIELLVNMGADINARELGTG-NTLLHIAASTKNYELAEWLCRQlGVNLGAINYQHETAYHIAYKMRDRRMMEILR 148

                         90
                 ....*....|....
gi 13385192  221 AFGANVNCAISSTG 234
Cdd:PHA02743 149 ANGAVCDDPLSIGL 162
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 163-303 3.59e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 46.01  E-value: 3.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385192  163 DNSNKHSALHLAIIHGTYPVLSFLAQNGAQVNATNESSMTPLHMAADILNKNMIETLIAFGANVNCAiSSTGNTALKLAV 242
Cdd:PLN03192 521 DDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIR-DANGNTALWNAI 599

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385192  243 CTASSKVGRLL----------AAG-----------VGCIRLLLNNGAQVNAQDHEGQTALHEACFGGREAIISLLLEFEA 301
Cdd:PLN03192 600 SAKHHKIFRILyhfasisdphAAGdllctaakrndLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGA 679


                 ..
gi 13385192  302 NV 303
Cdd:PLN03192 680 DV 681
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 193-318 3.99e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 44.42  E-value: 3.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385192  193 VNATNESSMTPLH--MAADILNKNMIETLIAFGANVNCAISSTGNTALklavctaSSKVGRLLAAGVGCIRLLLNNGAQV 270
Cdd:PHA02859  44 VNDCNDLYETPIFscLEKDKVNVEILKFLIENGADVNFKTRDNNLSAL-------HHYLSFNKNVEPEILKILIDSGSSI 116

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 13385192  271 NAQDHEGQTALHEAC--FGGREAIISLLLEFEANVNILTRNGESPIYMYL 318
Cdd:PHA02859 117 TEEDEDGKNLLHMYMcnFNVRINVIKLLIDSGVSFLNKDFDNNNILYSYI 166
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 77-207 5.38e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 45.26  E-value: 5.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385192   77 FPIHLAAEYRKPQSLLCLLQHGADPEVRDAQGFTTLHLmllnwpassTTWSKPSTQIQKILMdiqnnavlclcilcDHGA 156
Cdd:PHA02878 203 SPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHI---------SVGYCKDYDILKLLL--------------EHGV 259

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 13385192  157 QVNARVDNSNkHSALHLAIihGTYPVLSFLAQNGAQVNATNESSMTPLHMA 207
Cdd:PHA02878 260 DVNAKSYILG-LTALHSSI--KSERKLKLLLEYGADINSLNSYKLTPLSSA 307
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 168-300 7.82e-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: 45.07  E-value: 7.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385192   168 HSALHLAIIHGTYPVLSFLAQNGAQVNAT------NESSMT--------PLHMAADILNKNMIETLIAFGANVNCAIsST 233
Cdd:TIGR00870 129 ITALHLAAHRQNYEIVKLLLERGASVPARacgdffVKSQGVdsfyhgesPLNAAACLGSPSIVALLSEDPADILTAD-SL 207

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13385192   234 GNTALKLAVCTASSKVgRLLAAGVGCIRLLLNNGAQ----------VNaqdHEGQTALHEACFGGREAIISLLLEFE 300
Cdd:TIGR00870 208 GNTLLHLLVMENEFKA-EYEELSCQMYNFALSLLDKlrdskeleviLN---HQGLTPLKLAAKEGRIVLFRLKLAIK 280
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 78-206 2.10e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 43.70  E-value: 2.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385192   78 PIHLAAEYRKPQSLLCLLQHGADPEVRDAQGFTTL-------HLMLLNWPASSTTWSKPSTQIQKILMDIQNNAVLCLCI 150
Cdd:PLN03192 561 PLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALwnaisakHHKIFRILYHFASISDPHAAGDLLCTAAKRNDLTAMKE 640

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 13385192  151 LCDHGAQVNArvDNSNKHSALHLAIIHGTYPVLSFLAQNGAQVNATN-ESSMTPLHM 206
Cdd:PLN03192 641 LLKQGLNVDS--EDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANtDDDFSPTEL 695
PHA02917 PHA02917
ankyrin-like protein; Provisional
 270-330 1.58e-03

ankyrin-like protein; Provisional


Pssm-ID: 165231 [Multi-domain]  Cd Length: 661  Bit Score: 40.75  E-value: 1.58e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13385192  270 VNAQDHEGQTALHEACFGGREAIISLLLEFEANVNILTRNGESPIYMYLQRSSNIRDRSLL 330
Cdd:PHA02917 445 INMIDKRGETLLHKAVRYNKQSLVSLLLESGSDVNIRSNNGYTCIAIAINESRNIELLKML 505
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 28-227 2.70e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 39.97  E-value: 2.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385192   28 LHSKLYEAIIKEDCNTIKTLLRnhpvnqpLTILANSTRYRllsqqtQPIFPIHLAAEYRKPQSLLCLLQHGADPEVRDAQ 107
Cdd:PHA02875  68 IESELHDAVEEGDVKAVEELLD-------LGKFADDVFYK------DGMTPLHLATILKKLDIMKLLIARGADPDIPNTD 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385192  108 GFTTLHLMLLNWPASSTTwskpstqiqkilmdiqnnavlclcILCDHGAQVNarVDNSNKHSALHLAIIHGTYPVLSFLA 187
Cdd:PHA02875 135 KFSPLHLAVMMGDIKGIE------------------------LLIDHKACLD--IEDCCGCTPLIIAMAKGDIAICKMLL 188

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 13385192  188 QNGAQVNATNESSMTPLHMAADILNK-NMIETLIAFGANVN 227
Cdd:PHA02875 189 DSGANIDYFGKNGCVAALCYAIENNKiDIVRLFIKRGADCN 229
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 276-308 2.77e-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: 35.34  E-value: 2.77e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 13385192   276 EGQTALHEAC-FGGREAIISLLLEFEANVNILTR 308
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 201-228 3.11e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.87  E-value: 3.11e-03
                           10        20
                   ....*....|....*....|....*...
gi 13385192    201 MTPLHMAADILNKNMIETLIAFGANVNC 228
Cdd:smart00248   3 RTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 202-282 3.84e-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: 39.48  E-value: 3.84e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385192 202 TPLHMAADILNKNMIETLIAFGANVNCAISST------------GNTALKLAVCTASSKVgrllaagvgcIRLLLNNGAQ 269
Cdd:cd21882  75 TALHIAIENRNLNLVRLLVENGADVSARATGRffrkspgnlfyfGELPLSLAACTNQEEI----------VRLLLENGAQ 144

                        90
                ....*....|....*.
gi 13385192 270 ---VNAQDHEGQTALH 282
Cdd:cd21882 145 paaLEAQDSLGNTVLH 160
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 276-305 4.27e-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: 34.54  E-value: 4.27e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 13385192   276 EGQTALHEACFGGREAIISLLLEFEANVNI 305
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA03095 PHA03095
ankyrin-like protein; Provisional
 78-118 5.37e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 38.85  E-value: 5.37e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 13385192   78 PIHLAAEYRKPQSLLCLLQHGADPEVRDAQGFTTLHLMLLN 118
Cdd:PHA03095 260 PLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRN 300
PHA02798 PHA02798
ankyrin-like protein; Provisional
 260-321 5.72e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 38.66  E-value: 5.72e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385192  260 IRLLLNNGAQVNAQDHEGQTALheaC--------FGGREAIISLLLEFEANVNILTRNGESPIYMYLQRS 321
Cdd:PHA02798  54 VKLFINLGANVNGLDNEYSTPL---CtilsnikdYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNG 120
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 131-361 5.79e-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: 39.01  E-value: 5.79e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385192 131 TQIQKILMDIQNNAVLCLCILCDHGAQ-------VNARVDNS--NKHSALHLAIIHGTYPVLSFLAQNGAQVNAtnessm 201
Cdd:cd22193  31 TCLMKALLNLNPGTNDTIRILLDIAEKtdnlkrfINAEYTDEyyEGQTALHIAIERRQGDIVALLVENGADVHA------ 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385192 202 tplHMAADILNKNMIETLIAFganvncaisstGNTALKLAVCTASSKVgrllaagvgcIRLLLNNG---AQVNAQDHEGQ 278
Cdd:cd22193 105 ---HAKGRFFQPKYQGEGFYF-----------GELPLSLAACTNQPDI----------VQYLLENEhqpADIEAQDSRGN 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13385192 279 TALHeacfggreAIISLLLEFEANVNILTRngespIY-MYLQRSSNIRDRSLLARLLYRT--YPLRLSNKQG-------I 348
Cdd:cd22193 161 TVLH--------ALVTVADNTKENTKFVTR-----MYdMILIRGAKLCPTVELEEIRNNDglTPLQLAAKMGkieilkyI 227

                       250
                ....*....|...
gi 13385192 349 LPAGIMLPEYQLL 361
Cdd:cd22193 228 LQREIKEPELRHL 240
Ank_4 pfam13637
Ankyrin repeats (many copies);
279-316 6.63e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 34.56  E-value: 6.63e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 13385192   279 TALHEACFGGREAIISLLLEFEANVNILTRNGESPIYM 316
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHF 40
Ank_5 pfam13857
Ankyrin repeats (many copies);
262-314 7.16e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 34.63  E-value: 7.16e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 13385192   262 LLLNNGAQVNAQDHEGQTALHEACFGGREAIISLLLEFEANVNILTRNGESPI 314
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
Ank_5 pfam13857
Ankyrin repeats (many copies);
186-241 8.22e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 34.63  E-value: 8.22e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 13385192   186 LAQNG-AQVNATNESSMTPLHMAADILNKNMIETLIAFGANVNcAISSTGNTALKLA 241
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLN-LKDEEGLTALDLA 56
 
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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