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Conserved domains on  [gi|1958678629|ref|XP_038948778|]
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ankyrin repeat domain 36 isoform X4 [Rattus norvegicus]

Protein Classification

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

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
38-240 1.02e-49

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 178.22  E-value: 1.02e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958678629   38 HKAASMGDIPQVQKLLEFGNIDVNITDRKKRTALHYACAHGQSEMVSLLLWYDCNIEARDREESTALIKATQRQHEICVK 117
Cdd:COG0666     58 LLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVK 137

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958678629  118 ILLENGADPNAVDAYHITALHYAVYNNDTAIAAKLLSFNANTEIKTKNGYTPLILAVLENKQEMVELLLRAAANINALDN 197
Cdd:COG0666    138 LLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN 217

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1958678629  198 CKRSALIHAVRIQSKNMISLLLQQGADPSLVDIYGATAQSYAV 240
Cdd:COG0666    218 DGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAA 260
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
38-240 1.02e-49

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 178.22  E-value: 1.02e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958678629   38 HKAASMGDIPQVQKLLEFGNIDVNITDRKKRTALHYACAHGQSEMVSLLLWYDCNIEARDREESTALIKATQRQHEICVK 117
Cdd:COG0666     58 LLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVK 137

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958678629  118 ILLENGADPNAVDAYHITALHYAVYNNDTAIAAKLLSFNANTEIKTKNGYTPLILAVLENKQEMVELLLRAAANINALDN 197
Cdd:COG0666    138 LLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN 217

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1958678629  198 CKRSALIHAVRIQSKNMISLLLQQGADPSLVDIYGATAQSYAV 240
Cdd:COG0666    218 DGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAA 260
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 57-240 9.02e-23

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 102.44  E-value: 9.02e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958678629   57 NIDVNITDRKKRTALHYACAHGQSEMVSLLLWYDCNIEARDREESTALIKATQRQH------EIcVKILLENGADPNAVD 130
Cdd:PHA03100    25 DDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvkEI-VKLLLEYGANVNAPD 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958678629  131 AYHITALHYAVYN--NDTAIAAKLLSFNANTEIKTKNGYTPLILAV--LENKQEMVELLLRAAANINALDNCKR------ 200
Cdd:PHA03100   104 NNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLesNKIDLKILKLLIDKGVDINAKNRVNYllsygv 183

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958678629  201 ----------SALIHAVRIQSKNMISLLLQQGADPSLVDIYGATAQSYAV 240
Cdd:PHA03100   184 pinikdvygfTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAI 233
Ank_2 pfam12796
Ankyrin repeats (3 copies);
37-130 1.64e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 84.40  E-value: 1.64e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958678629   37 IHKAASMGDIPQVQKLLEFGNiDVNITDRKKRTALHYACAHGQSEMVSLLLWYdCNIEARDREEsTALIKATQRQHEICV 116
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGA-DANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGR-TALHYAARSGHLEIV 77

                           90
                   ....*....|....
gi 1958678629  117 KILLENGADPNAVD 130
Cdd:pfam12796   78 KLLLEKGADINVKD 91
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 35-243 7.59e-08

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: 56.63  E-value: 7.59e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958678629   35 KRIHKAASMGDIPQVQK-LLEFGNIDVNITDRKKRTALHYACAHGQS-EMVSLLLWYDCNIEARDreesTALIKATQRQH 112
Cdd:TIGR00870   19 KAFLPAAERGDLASVYRdLEEPKKLNINCPDRLGRSALFVAAIENENlELTELLLNLSCRGAVGD----TLLHAISLEYV 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958678629  113 EICVKILLengadpnavdayHITALHYAVYNNDTAIAAKLLSFNAnteiktknGYTPLILAVLENKQEMVELLLRAAANI 192
Cdd:TIGR00870   95 DAVEAILL------------HLLAAFRKSGPLELANDQYTSEFTP--------GITALHLAAHRQNYEIVKLLLERGASV 154

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958678629  193 NALDNCK--------------RSALIHAVRIQSKNMISLLLQQGADPSLVDIYGATAQSYAVFET 243
Cdd:TIGR00870  155 PARACGDffvksqgvdsfyhgESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVMEN 219
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 69-187 1.47e-04

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 46.16  E-value: 1.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958678629   69 TALHYACAHGQSEMVSLLLWYDCN-IEARD-----REESTALIK--------ATQRQHEICVKILLENGADPNAVDAYHI 134
Cdd:cd22192     91 TALHIAVVNQNLNLVRELIARGADvVSPRAtgtffRPGPKNLIYygehplsfAACVGNEEIVRLLIEHGADIRAQDSLGN 170

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958678629  135 TALHYAVYNNDTAIAAK----LLSFNANTE------IKTKNGYTPLILAVLENKQEMVELLLR 187
Cdd:cd22192    171 TVLHILVLQPNKTFACQmydlILSYDKEDDlqpldlVPNNQGLTPFKLAAKEGNIVMFQHLVQ 233
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 165-194 3.41e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.11  E-value: 3.41e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 1958678629   165 NGYTPLILAVLENKQEMVELLLRAAANINA 194
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
38-240 1.02e-49

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 178.22  E-value: 1.02e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958678629   38 HKAASMGDIPQVQKLLEFGNIDVNITDRKKRTALHYACAHGQSEMVSLLLWYDCNIEARDREESTALIKATQRQHEICVK 117
Cdd:COG0666     58 LLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVK 137

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958678629  118 ILLENGADPNAVDAYHITALHYAVYNNDTAIAAKLLSFNANTEIKTKNGYTPLILAVLENKQEMVELLLRAAANINALDN 197
Cdd:COG0666    138 LLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN 217

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1958678629  198 CKRSALIHAVRIQSKNMISLLLQQGADPSLVDIYGATAQSYAV 240
Cdd:COG0666    218 DGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAA 260
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
37-240 2.91e-46

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 168.21  E-value: 2.91e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958678629   37 IHKAASMGDIPQVQKLLEFGNIDVNITDRKKRTALHYACAHGQSEMVSLLLWYDCNIEARDREESTALIKATQRQHEICV 116
Cdd:COG0666     24 LLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIV 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958678629  117 KILLENGADPNAVDAYHITALHYAVYNNDTAIAAKLLSFNANTEIKTKNGYTPLILAVLENKQEMVELLLRAAANINALD 196
Cdd:COG0666    104 KLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARD 183

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1958678629  197 NCKRSALIHAVRIQSKNMISLLLQQGADPSLVDIYGATAQSYAV 240
Cdd:COG0666    184 NDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAA 227
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
37-235 1.91e-45

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 165.90  E-value: 1.91e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958678629   37 IHKAASMGDIPQVQKLLEFGnIDVNITDRKKRTALHYACAHGQSEMVSLLLWYDCNIEARDREESTALIKATQRQHEICV 116
Cdd:COG0666     91 LHAAARNGDLEIVKLLLEAG-ADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIV 169

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958678629  117 KILLENGADPNAVDAYHITALHYAVYNNDTAIAAKLLSFNANTEIKTKNGYTPLILAVLENKQEMVELLLRAAANINALD 196
Cdd:COG0666    170 KLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKD 249

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1958678629  197 NCKRSALIHAVRIQSKNMISLLLQQGADPSLVDIYGATA 235
Cdd:COG0666    250 KDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
30-203 4.21e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 141.63  E-value: 4.21e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958678629   30 GYTPvkrIHKAASMGDIPQVQKLLEFGnIDVNITDRKKRTALHYACAHGQSEMVSLLLWYDCNIEARDREESTALIKATQ 109
Cdd:COG0666    120 GETP---LHLAAYNGNLEIVKLLLEAG-ADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAE 195

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958678629  110 RQHEICVKILLENGADPNAVDAYHITALHYAVYNNDTAIAAKLLSFNANTEIKTKNGYTPLILAVLENKQEMVELLLRAA 189
Cdd:COG0666    196 NGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLAL 275

                          170
                   ....*....|....
gi 1958678629  190 ANINALDNCKRSAL 203
Cdd:COG0666    276 LLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
52-240 2.46e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 130.84  E-value: 2.46e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958678629   52 LLEFGNIDVNITDRKKRTALHYACAHGQSEMVSLLLWYDCNIEARDREESTALIKATQRQHEICVKILLENGADPNAVDA 131
Cdd:COG0666      6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958678629  132 YHITALHYAVYNNDTAIAAKLLSFNANTEIKTKNGYTPLILAVLENKQEMVELLLRAAANINALDNCKRSALIHAVRIQS 211
Cdd:COG0666     86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGN 165

                          170       180
                   ....*....|....*....|....*....
gi 1958678629  212 KNMISLLLQQGADPSLVDIYGATAQSYAV 240
Cdd:COG0666    166 LEIVKLLLEAGADVNARDNDGETPLHLAA 194
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
81-241 6.45e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 100.41  E-value: 6.45e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958678629   81 EMVSLLLWYDCNIEARDREESTALIKATQRQHEICVKILLENGADPNAVDAYHITALHYAVYNNDTAIAAKLLSFNANTE 160
Cdd:COG0666      2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958678629  161 IKTKNGYTPLILAVLENKQEMVELLLRAAANINALDNCKRSALIHAVRIQSKNMISLLLQQGADPSLVDIYGATAQSYAV 240
Cdd:COG0666     82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161


                   .
gi 1958678629  241 F 241
Cdd:COG0666    162 A 162
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 57-240 9.02e-23

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 102.44  E-value: 9.02e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958678629   57 NIDVNITDRKKRTALHYACAHGQSEMVSLLLWYDCNIEARDREESTALIKATQRQH------EIcVKILLENGADPNAVD 130
Cdd:PHA03100    25 DDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvkEI-VKLLLEYGANVNAPD 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958678629  131 AYHITALHYAVYN--NDTAIAAKLLSFNANTEIKTKNGYTPLILAV--LENKQEMVELLLRAAANINALDNCKR------ 200
Cdd:PHA03100   104 NNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLesNKIDLKILKLLIDKGVDINAKNRVNYllsygv 183

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958678629  201 ----------SALIHAVRIQSKNMISLLLQQGADPSLVDIYGATAQSYAV 240
Cdd:PHA03100   184 pinikdvygfTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAI 233
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 49-232 1.88e-20

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 95.80  E-value: 1.88e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958678629   49 VQKLLEFGnIDVNITDRKKRTALHYACAHGQSEMVSLLLWYDCNIEARDREESTALIKATQRQHEICVKILLENGADPNA 128
Cdd:PHA02874   107 IKTILDCG-IDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANV 185

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958678629  129 VDAYHITALHYAVYNNDTAIAAKLLSFNANTEIKTKNGYTPLILAVLENKQeMVELLLRAAAnINALDNCKRSALIHAVR 208
Cdd:PHA02874   186 KDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRS-AIELLINNAS-INDQDIDGSTPLHHAIN 263

                          170       180
                   ....*....|....*....|....*
gi 1958678629  209 IQ-SKNMISLLLQQGADPSLVDIYG 232
Cdd:PHA02874   264 PPcDIDIIDILLYHKADISIKDNKG 288
Ank_2 pfam12796
Ankyrin repeats (3 copies);
37-130 1.64e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 84.40  E-value: 1.64e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958678629   37 IHKAASMGDIPQVQKLLEFGNiDVNITDRKKRTALHYACAHGQSEMVSLLLWYdCNIEARDREEsTALIKATQRQHEICV 116
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGA-DANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGR-TALHYAARSGHLEIV 77

                           90
                   ....*....|....
gi 1958678629  117 KILLENGADPNAVD 130
Cdd:pfam12796   78 KLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 30-198 5.58e-19

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 90.88  E-value: 5.58e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958678629   30 GYTPvkrIHKAAS--MGDIPQVQKLLEFGnIDVNITDRKKRTALHYA--CAHGQSEMVSLLLWYDCNIEARDReestali 105
Cdd:PHA03100   106 GITP---LLYAISkkSNSYSIVEYLLDNG-ANVNIKNSDGENLLHLYleSNKIDLKILKLLIDKGVDINAKNR------- 174

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958678629  106 katqrqheicVKILLENGADPNAVDAYHITALHYAVYNNDTAIAAKLLSFNANTEIKTKNGYTPLILAVLENKQEMVELL 185
Cdd:PHA03100   175 ----------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLL 244

                          170
                   ....*....|...
gi 1958678629  186 LRAAANINALDNC 198
Cdd:PHA03100   245 LNNGPSIKTIIET 257
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 49-224 4.36e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 88.18  E-value: 4.36e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958678629   49 VQKLLEFGnIDVNITDRKKRTALHYACAHGQS-----EMVSLLLWYDCNIEARDREESTAL---IKATQRQHEIcVKILL 120
Cdd:PHA03100    51 VKILLDNG-ADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLlyaISKKSNSYSI-VEYLL 128

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958678629  121 ENGADPNAVDAYHITALHYAVYNN--DTAIAAKLLSFNANTEIKTK----------------NGYTPLILAVLENKQEMV 182
Cdd:PHA03100   129 DNGANVNIKNSDGENLLHLYLESNkiDLKILKLLIDKGVDINAKNRvnyllsygvpinikdvYGFTPLHYAVYNNNPEFV 208

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1958678629  183 ELLLRAAANINALDNCKRSALIHAVRIQSKNMISLLLQQGAD 224
Cdd:PHA03100   209 KYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
Ank_2 pfam12796
Ankyrin repeats (3 copies);
71-162 1.86e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 78.62  E-value: 1.86e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958678629   71 LHYACAHGQSEMVSLLLWYDCNIEARDREESTALIKATQRQHEICVKILLENgADPNAVDaYHITALHYAVYNNDTAIAA 150
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|..
gi 1958678629  151 KLLSFNANTEIK 162
Cdd:pfam12796   79 LLLEKGADINVK 90
PHA03095 PHA03095
ankyrin-like protein; Provisional
 34-235 2.87e-17

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 86.23  E-value: 2.87e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958678629   34 VKRIHKAASMG--------DIPQVQKLLEFGNiDVNITDRKKRTALHYacahgqsemvslLLWYDCNIEArdreestali 105
Cdd:PHA03095     7 VDIIMEAALYDyllnasnvTVEEVRRLLAAGA-DVNFRGEYGKTPLHL------------YLHYSSEKVK---------- 63

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958678629  106 katqrqhEIcVKILLENGADPNAVDAYHITALHYAVYNNDTAIAAKLL-SFNANTEIKTKNGYTPL--ILAVLENKQEMV 182
Cdd:PHA03095    64 -------DI-VRLLLEAGADVNAPERCGFTPLHLYLYNATTLDVIKLLiKAGADVNAKDKVGRTPLhvYLSGFNINPKVI 135

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958678629  183 ELLLRAAANINALDNCKRSALihAVRIQSKN----MISLLLQQGADPSLVDIYGATA 235
Cdd:PHA03095   136 RLLLRKGADVNALDLYGMTPL--AVLLKSRNanveLLRLLIDAGADVYAVDDRFRSL 190
Ank_2 pfam12796
Ankyrin repeats (3 copies);
137-229 3.67e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.46  E-value: 3.67e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958678629  137 LHYAVYNNDTAIAAKLLSFNANTEIKTKNGYTPLILAVLENKQEMVELLLrAAANINALDNcKRSALIHAVRIQSKNMIS 216
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKDN-GRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 1958678629  217 LLLQQGADPSLVD 229
Cdd:pfam12796   79 LLLEKGADINVKD 91
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 30-228 6.57e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 84.66  E-value: 6.57e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958678629   30 GYTPVKRihkAASMGDIPQVQKLLEFGNI-DVNITDrkKRTALHYACAHGQSEMVSLLLwyDCNIEARD---REESTALI 105
Cdd:PHA02875    35 GISPIKL---AMKFRDSEAIKLLMKHGAIpDVKYPD--IESELHDAVEEGDVKAVEELL--DLGKFADDvfyKDGMTPLH 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958678629  106 KATQRQHEICVKILLENGADPNAVDAYHITALHYAVYNNDTAIAAKLLSFNANTEIKTKNGYTPLILAVLENKQEMVELL 185
Cdd:PHA02875   108 LATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKML 187

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1958678629  186 LRAAANINALD-NCKRSALIHAVRIQSKNMISLLLQQGADPSLV 228
Cdd:PHA02875   188 LDSGANIDYFGkNGCVAALCYAIENNKIDIVRLFIKRGADCNIM 231
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 15-240 2.21e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 83.39  E-value: 2.21e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958678629   15 SFRHAENqepprYLTGYT--PVKRIHKAASMGDIPQVQKLLEFGnIDVNITDRKKRTALHYACAH----GQSEMVS---- 84
Cdd:PHA02878    22 YIDHTEN-----YSTSASliPFIPLHQAVEARNLDVVKSLLTRG-HNVNQPDHRDLTPLHIICKEpnklGMKEMIRsink 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958678629   85 ------------------------LLLWYDCNIEARDREESTALIKATQRQHEIcVKILLENGADPNAVDAYHI-TALHY 139
Cdd:PHA02878    96 csvfytlvaikdafnnrnveifkiILTNRYKNIQTIDLVYIDKKSKDDIIEAEI-TKLLLSYGADINMKDRHKGnTALHY 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958678629  140 AVYNNDTAIAAKLLSFNANTEIKTKNGYTPLILAVLENKQEMVELLLRAAANINALDNCKRSALIHAV------------ 207
Cdd:PHA02878   175 ATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVgyckdydilkll 254

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1958678629  208 ---------------------RIQSKNMISLLLQQGADPSLVDIYGATAQSYAV 240
Cdd:PHA02878   255 lehgvdvnaksyilgltalhsSIKSERKLKLLLEYGADINSLNSYKLTPLSSAV 308
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 49-208 2.95e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 79.92  E-value: 2.95e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958678629   49 VQKLLEFGnIDVNITDRKK-RTALHYACAHGQSEMVSLLLWYDCNIEARDREESTALIKATQRQHEICVKILLENGADPN 127
Cdd:PHA02878   150 TKLLLSYG-ADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTD 228

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958678629  128 AVDAYHITALHYAV-YNNDTAIAAKLLSFNANTEIK-TKNGYTPLILAVleNKQEMVELLLRAAANINALDNCKRSALIH 205
Cdd:PHA02878   229 ARDKCGNTPLHISVgYCKDYDILKLLLEHGVDVNAKsYILGLTALHSSI--KSERKLKLLLEYGADINSLNSYKLTPLSS 306


                   ...
gi 1958678629  206 AVR 208
Cdd:PHA02878   307 AVK 309
PHA03095 PHA03095
ankyrin-like protein; Provisional
 49-239 2.58e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 76.99  E-value: 2.58e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958678629   49 VQKLLEFGnIDVNITDRKKRTALH-YACAHGQSEMVSLLLWYDCNIEARDREESTALIK--ATQRQHEICVKILLENGAD 125
Cdd:PHA03095    66 VRLLLEAG-ADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGAD 144

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958678629  126 PNAVDAYHITALHyavynndtaiaAKLLSFNANTEIktkngytplilavlenkqemVELLLRAAANINALDNCKRSAL-I 204
Cdd:PHA03095   145 VNALDLYGMTPLA-----------VLLKSRNANVEL--------------------LRLLIDAGADVYAVDDRFRSLLhH 193

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1958678629  205 HAVRIQSKN-MISLLLQQGADPSLVDIYGATAQSYA 239
Cdd:PHA03095   194 HLQSFKPRArIVRELIRAGCDPAATDMLGNTPLHSM 229
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 28-224 6.24e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 76.64  E-value: 6.24e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958678629   28 LTGYTPVKRIHKAASmgDIPQVQKLLEFGnIDVNITDRKKRTALHYACAHGQ-SEMVSLLLWYDCNIEARDREESTALIK 106
Cdd:PHA02876   305 IKGETPLYLMAKNGY--DTENIRTLIMLG-ADVNAADRLYITPLHQASTLDRnKDIVITLLELGANVNARDYCDKTPIHY 381

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958678629  107 ATQRQHEICVKILLENGADPNAVDAYHITALHYAVYNNDTAIAAK-LLSFNANTEIKTKNGYTPLILAVLEN-KQEMVEL 184
Cdd:PHA02876   382 AAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMSVKtLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEM 461

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1958678629  185 LLRAAANINALDNCKRSALIHAVRIQSknMISLLLQQGAD 224
Cdd:PHA02876   462 LLDNGADVNAINIQNQYPLLIALEYHG--IVNILLHYGAE 499
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 33-234 2.99e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 74.33  E-value: 2.99e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958678629   33 PVKRIHKAASMGDIPQVQKLLEFGNIDVNITDRKKRTALHYACAHGQSEMVSLLLWYDCNI------------------- 93
Cdd:PHA02876    41 PFTAIHQALQLRQIDIVEEIIQQNPELIYITDHKCHSTLHTICIIPNVMDIVISLTLDCDIildikyasiilnkhkldea 120

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958678629   94 -----------------EARDREESTALIKATQRQHEICV-KILLENGADPNAVDAYHITALHYAVYNNDTAIAAKLLSF 155
Cdd:PHA02876   121 cihilkeaisgndihydKINESIEYMKLIKERIQQDELLIaEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSY 200

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958678629  156 NANTEIKTKNGYTPL-----------ILAVLENKQ------------------EMVELLLRAAANINALDNCKRSALIHA 206
Cdd:PHA02876   201 GADVNIIALDDLSVLecavdsknidtIKAIIDNRSninkndlsllkairnedlETSLLLYDAGFSVNSIDDCKNTPLHHA 280

                          250       260
                   ....*....|....*....|....*....
gi 1958678629  207 VRIQS-KNMISLLLQQGADPSLVDIYGAT 234
Cdd:PHA02876   281 SQAPSlSRLVPKLLERGADVNAKNIKGET 309
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 49-239 5.89e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 70.09  E-value: 5.89e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958678629   49 VQKLLEFGNIDVNITDRKKRTALHYACAHGQSEMVSLLLWY--DCNIEARD---------------------------RE 99
Cdd:PHA02876   160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYgaDVNIIALDdlsvlecavdsknidtikaiidnrsniNK 239

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958678629  100 ESTALIKATQRQHEICVKILLENGADPNAVDAYHITALHYAVYNND-TAIAAKLLSFNANTEIKTKNGYTPLILAVLEN- 177
Cdd:PHA02876   240 NDLSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYLMAKNGy 319

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958678629  178 KQEMVELLLRAAANINALDNCKRSALIHAVRI-QSKNMISLLLQQGADPSLVDIYGATAQSYA 239
Cdd:PHA02876   320 DTENIRTLIMLGADVNAADRLYITPLHQASTLdRNKDIVITLLELGANVNARDYCDKTPIHYA 382
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 40-194 1.23e-11

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 69.13  E-value: 1.23e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958678629   40 AASMGDIPQVQKLLEFGnIDVNITDRKKRTALHYACAHGQSEMVSLLLWYDCNIEARDREESTALIKATQRQHEICVKIL 119
Cdd:PLN03192   532 VASTGNAALLEELLKAK-LDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL 610

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958678629  120 --LENGADPNAVDayhiTALHYAVYNNDTAIAAKLLSFNANTEIKTKNGYTPLILAVLENKQEMVELLLRAAANINA 194
Cdd:PLN03192   611 yhFASISDPHAAG----DLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDK 683
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
116-242 1.27e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 66.90  E-value: 1.27e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958678629  116 VKILLENGADPNAVDAYHITALHYAVYNNDTAIAAKLLSFNANTEIKTKNGYTPLILAVLENKQEMVELLLRAAANINAL 195
Cdd:COG0666      4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1958678629  196 DNCKRSALIHAVRIQSKNMISLLLQQGADPSLVDIYGATAQSYAVFE 242
Cdd:COG0666     84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYN 130
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 44-222 1.89e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 67.68  E-value: 1.89e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958678629   44 GDIPQVQKLLEFGNIDVNITDRKKRTALHYACAHGQSEMVSLLLWYDCNIEARDREESTALIKATQ-RQHEIcVKILLEN 122
Cdd:PHA02874    12 GDIEAIEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKiGAHDI-IKLLIDN 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958678629  123 GADP-----------------------NAVDAYHITALHYAVYNNDTAIAAKLLSFNANTEIKTKNGYTPLILAVLENKQ 179
Cdd:PHA02874    91 GVDTsilpipciekdmiktildcgidvNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFF 170

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1958678629  180 EMVELLLRAAANINALDNCKRSALIHAVRIQSKNMISLLLQQG 222
Cdd:PHA02874   171 DIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHG 213
PHA03095 PHA03095
ankyrin-like protein; Provisional
 52-229 2.36e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 67.74  E-value: 2.36e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958678629   52 LLEFGnIDVNITDRKKRTALH-YACAHGQS-EMVSLLLWYDCNIEARDREESTAL--IKATQRQHEICVKILLENGADPN 127
Cdd:PHA03095   138 LLRKG-ADVNALDLYGMTPLAvLLKSRNANvELLRLLIDAGADVYAVDDRFRSLLhhHLQSFKPRARIVRELIRAGCDPA 216

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958678629  128 AVDAYHITALHY-AVYNNDTAI-AAKLLSFNANTEIKTKNGYTPLILAVLENKQEMVELLLRAAANINALDNCKRSALIH 205
Cdd:PHA03095   217 ATDMLGNTPLHSmATGSSCKRSlVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSL 296

                          170       180
                   ....*....|....*....|....
gi 1958678629  206 AVRIQSKNMISLLLQQGADPSLVD 229
Cdd:PHA03095   297 MVRNNNGRAVRAALAKNPSAETVA 320
PHA03095 PHA03095
ankyrin-like protein; Provisional
 52-197 4.78e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 66.59  E-value: 4.78e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958678629   52 LLEFGNIDVNI-------------TDRKKRTALHYAC--AHGQSEMVSLLLWYDCNIEARDREESTALIKATQrqHEICV 116
Cdd:PHA03095   159 LLKSRNANVELlrllidagadvyaVDDRFRSLLHHHLqsFKPRARIVRELIRAGCDPAATDMLGNTPLHSMAT--GSSCK 236

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958678629  117 KI----LLENGADPNAVDAYHITALHYA-VYNNDTAiAAKLLSFNANTEIKTKNGYTPLILAVLENKQEMVELLLRAAAN 191
Cdd:PHA03095   237 RSlvlpLLIAGISINARNRYGQTPLHYAaVFNNPRA-CRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPS 315


                   ....*.
gi 1958678629  192 INALDN 197
Cdd:PHA03095   316 AETVAA 321
Ank_4 pfam13637
Ankyrin repeats (many copies);
37-87 1.31e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 57.67  E-value: 1.31e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1958678629   37 IHKAASMGDIPQVQKLLEFGnIDVNITDRKKRTALHYACAHGQSEMVSLLL 87
Cdd:pfam13637    5 LHAAAASGHLELLRLLLEKG-ADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
52-107 1.36e-10

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 57.74  E-value: 1.36e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958678629   52 LLEFGNIDVNITDRKKRTALHYACAHGQSEMVSLLLWYDCNIEARDREESTALIKA 107
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 40-240 2.43e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 60.78  E-value: 2.43e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958678629   40 AASMGDIPQVQKLLEFGnIDVNITDRKKRTALHYACAHGQSEMVSLLLWYDCNIEARDREESTALIKATQRQHEICVKIL 119
Cdd:PHA02875     9 AILFGELDIARRLLDIG-INPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEEL 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958678629  120 LENGADPNAVdAYH--ITALHYAVYNNDTAIAAKLLSFNANTEIKTKNGYTPLILAVLENKQEMVELLLRAAANINALDN 197
Cdd:PHA02875    88 LDLGKFADDV-FYKdgMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDC 166

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1958678629  198 CKRSALIHAVRIQSKNMISLLLQQGADPSLVDIYG-ATAQSYAV 240
Cdd:PHA02875   167 CGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAI 210
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 116-198 3.45e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 61.07  E-value: 3.45e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958678629  116 VKILLENGADPNAVDAYHITALHYAVYNNDTAIAAKLLSFNANTEIKTKNGYTPLILAVLENKQEMVELLLRAAANINAL 195
Cdd:PTZ00322    98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFEL 177


                   ...
gi 1958678629  196 DNC 198
Cdd:PTZ00322   178 GAN 180
Ank_4 pfam13637
Ankyrin repeats (many copies);
100-153 9.89e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.28  E-value: 9.89e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1958678629  100 ESTALIKATQRQHEICVKILLENGADPNAVDAYHITALHYAVYNNDTAIAAKLL 153
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 35-243 7.59e-08

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: 56.63  E-value: 7.59e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958678629   35 KRIHKAASMGDIPQVQK-LLEFGNIDVNITDRKKRTALHYACAHGQS-EMVSLLLWYDCNIEARDreesTALIKATQRQH 112
Cdd:TIGR00870   19 KAFLPAAERGDLASVYRdLEEPKKLNINCPDRLGRSALFVAAIENENlELTELLLNLSCRGAVGD----TLLHAISLEYV 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958678629  113 EICVKILLengadpnavdayHITALHYAVYNNDTAIAAKLLSFNAnteiktknGYTPLILAVLENKQEMVELLLRAAANI 192
Cdd:TIGR00870   95 DAVEAILL------------HLLAAFRKSGPLELANDQYTSEFTP--------GITALHLAAHRQNYEIVKLLLERGASV 154

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958678629  193 NALDNCK--------------RSALIHAVRIQSKNMISLLLQQGADPSLVDIYGATAQSYAVFET 243
Cdd:TIGR00870  155 PARACGDffvksqgvdsfyhgESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVMEN 219
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 27-186 3.70e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 53.84  E-value: 3.70e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958678629   27 YLTGYTPvkrIHKAASMGDIPQVQKLLEFGnIDVNITDRKKRTALHYACAHGQSEMVSLLLWYDCNIEARDREESTALIK 106
Cdd:PHA02875    99 YKDGMTP---LHLATILKKLDIMKLLIARG-ADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLII 174

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958678629  107 ATQRQH-EICvKILLENGADPNAVDAY-HITALHYAVYNNDTAIAAKLLSFNANTEIKTK-NGYTPLILAVLEN-----K 178
Cdd:PHA02875   175 AMAKGDiAIC-KMLLDSGANIDYFGKNgCVAALCYAIENNKIDIVRLFIKRGADCNIMFMiEGEECTILDMICNmctnlE 253


                   ....*...
gi 1958678629  179 QEMVELLL 186
Cdd:PHA02875   254 SEAIDALI 261
Ank_5 pfam13857
Ankyrin repeats (many copies);
119-173 9.72e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.96  E-value: 9.72e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958678629  119 LLENG-ADPNAVDAYHITALHYAVYNNDTAIAAKLLSFNANTEIKTKNGYTPLILA 173
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
166-219 1.29e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.50  E-value: 1.29e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1958678629  166 GYTPLILAVLENKQEMVELLLRAAANINALDNCKRSALIHAVRIQSKNMISLLL 219
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 165-197 1.59e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 42.66  E-value: 1.59e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1958678629  165 NGYTPLILAVLE-NKQEMVELLLRAAANINALDN 197
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
Ank_5 pfam13857
Ankyrin repeats (many copies);
155-206 6.89e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.56  E-value: 6.89e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1958678629  155 FNANTEIKTKNGYTPLILAVLENKQEMVELLLRAAANINALDNCKRSALIHA 206
Cdd:pfam13857    5 GPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 141-230 7.61e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 46.50  E-value: 7.61e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958678629  141 VYNNDTAIAAKLLSFNAN-TEIKTKNGYTPLILAVLENKQEMVELLLRAAANINALDNCKRSALIHAVRIQSKNMISLLL 219
Cdd:PHA02874     9 IYSGDIEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLI 88

                           90
                   ....*....|.
gi 1958678629  220 QQGADPSLVDI 230
Cdd:PHA02874    89 DNGVDTSILPI 99
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 69-187 1.47e-04

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 46.16  E-value: 1.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958678629   69 TALHYACAHGQSEMVSLLLWYDCN-IEARD-----REESTALIK--------ATQRQHEICVKILLENGADPNAVDAYHI 134
Cdd:cd22192     91 TALHIAVVNQNLNLVRELIARGADvVSPRAtgtffRPGPKNLIYygehplsfAACVGNEEIVRLLIEHGADIRAQDSLGN 170

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958678629  135 TALHYAVYNNDTAIAAK----LLSFNANTE------IKTKNGYTPLILAVLENKQEMVELLLR 187
Cdd:cd22192    171 TVLHILVLQPNKTFACQmydlILSYDKEDDlqpldlVPNNQGLTPFKLAAKEGNIVMFQHLVQ 233
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 92-234 1.54e-04

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 45.77  E-value: 1.54e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958678629   92 NIEARDREESTALIKATQRQHEICVKILLE-NGADPNAVDAYHITALHYAV-YNNDTAiaAKLLSFNA----NTEIKTK- 164
Cdd:cd22192      9 HLLQQKRISESPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAAlYDNLEA--AVVLMEAApelvNEPMTSDl 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958678629  165 -NGYTPLILAVLENKQEMVELLLRAAANINALDNC------KRSALIH--------AVRIQSKNMISLLLQQGADPSLVD 229
Cdd:cd22192     87 yQGETALHIAVVNQNLNLVRELIARGADVVSPRATgtffrpGPKNLIYygehplsfAACVGNEEIVRLLIEHGADIRAQD 166


                   ....*
gi 1958678629  230 IYGAT 234
Cdd:cd22192    167 SLGNT 171
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 68-98 1.79e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.97  E-value: 1.79e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1958678629   68 RTALHYACAH-GQSEMVSLLLWYDCNIEARDR 98
Cdd:pfam00023    3 NTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
Ank_4 pfam13637
Ankyrin repeats (many copies);
133-186 2.45e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.95  E-value: 2.45e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1958678629  133 HITALHYAVYNNDTAIAAKLLSFNANTEIKTKNGYTPLILAVLENKQEMVELLL 186
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 116-247 2.50e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 44.59  E-value: 2.50e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958678629  116 VKILLENGADPNA----VDAYHITALHYAV-YNNDTAIAAkLLSFNANteIKTKNGY---TPLILAVLENKQEMVELLLR 187
Cdd:PHA02884    49 IDAILKLGADPEApfplSENSKTNPLIYAIdCDNDDAAKL-LIRYGAD--VNRYAEEakiTPLYISVLHGCLKCLEILLS 125

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958678629  188 AAANINALDNCKRSALIHAVRIQSKNMISLLlqqgADPSLVDIYGATAQSYAVFETFQVL 247
Cdd:PHA02884   126 YGADINIQTNDMVTPIELALMICNNFLAFMI----CDNEISNFYKHPKKILINFDILKIL 181
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 165-194 3.41e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.11  E-value: 3.41e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 1958678629   165 NGYTPLILAVLENKQEMVELLLRAAANINA 194
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02798 PHA02798
ankyrin-like protein; Provisional
 116-224 1.01e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 43.28  E-value: 1.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958678629  116 VKILLENGADPNAVDAYHITAL-----HYAVYNNDTAIAAKLLSFNANTEIKTKNGYTPLiLAVLENK----QEMVELLL 186
Cdd:PHA02798    54 VKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPL-YCLLSNGyinnLEILLFMI 132

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1958678629  187 RAAANINALDNCKRSALihAVRIQSKN-----MISLLLQQGAD 224
Cdd:PHA02798   133 ENGADTTLLDKDGFTML--QVYLQSNHhidieIIKLLLEKGVD 173
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 34-131 1.61e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 42.58  E-value: 1.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958678629   34 VKRIHKAASmGDIPQVQKLLEfGNIDVNITDRKKRTALHYACAHGQSEMVSLLLWYDCNIEARDREESTALIKATQRQHE 113
Cdd:PTZ00322    84 VELCQLAAS-GDAVGARILLT-GGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFR 161

                           90
                   ....*....|....*...
gi 1958678629  114 ICVKILLENGADPNAVDA 131
Cdd:PTZ00322   162 EVVQLLSRHSQCHFELGA 179
PHA02798 PHA02798
ankyrin-like protein; Provisional
 49-234 1.73e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 42.51  E-value: 1.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958678629   49 VQKLLEFGNIDVNITDRKKRTALHYACAHG---QSEMVSLLLWYDCNIEARDREESTALIKATQRQHEI---CVKILLEN 122
Cdd:PHA02798    91 IVKILIENGADINKKNSDGETPLYCLLSNGyinNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHHIdieIIKLLLEK 170

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958678629  123 GADPNAV-DAYHITALH-YAVYNND--TAIAAKLLSFNA---NTEIK-TKNGYTPLILAVLEN----KQEMVELLLrAAA 190
Cdd:PHA02798   171 GVDINTHnNKEKYDTLHcYFKYNIDriDADILKLFVDNGfiiNKENKsHKKKFMEYLNSLLYDnkrfKKNILDFIF-SYI 249

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1958678629  191 NINALDNCKRSALIHAVRIQSKNMISLLLQQGADPSLVDIYGAT 234
Cdd:PHA02798   250 DINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNT 293
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 102-130 2.05e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. 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: 36.88  E-value: 2.05e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1958678629  102 TALIKA-TQRQHEICVKILLENGADPNAVD 130
Cdd:pfam00023    4 TPLHLAaGRRGNLEIVKLLLSKGADVNARD 33
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 94-213 4.51e-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: 41.28  E-value: 4.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958678629   94 EARDREESTAL-IKATQRQHEIcVKILLENGADPNAvdayhitalhyavynndtaiAAKLLSFNAnteiKTKN-----GY 167
Cdd:cd22194    135 TEEAYEGQTALnIAIERRQGDI-VKLLIAKGADVNA--------------------HAKGVFFNP----KYKHegfyfGE 189

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1958678629  168 TPLILAVLENKQEMVELLLRAAANINALDNCKRSALIHAVRIQSKN 213
Cdd:cd22194    190 TPLALAACTNQPEIVQLLMEKESTDITSQDSRGNTVLHALVTVAED 235
 
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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