NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2462559640|ref|XP_054174195|]
View 

ankyrin repeat domain-containing protein 29 isoform X7 [Homo sapiens]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
12-172 3.35e-43

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 145.87  E-value: 3.35e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462559640  12 LANAAFWAARRGNLALLKLLLNSGRVDVDCRDSHGTTLLMVAAYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGH 91
Cdd:COG0666    53 LGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGN 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462559640  92 NDVVRFLFGFGASTEFRTKDGGTALLAASQYGHMQVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLASGAKV 171
Cdd:COG0666   133 LEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADV 212


                  .
gi 2462559640 172 N 172
Cdd:COG0666   213 N 213
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
12-172 3.35e-43

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 145.87  E-value: 3.35e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462559640  12 LANAAFWAARRGNLALLKLLLNSGRVDVDCRDSHGTTLLMVAAYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGH 91
Cdd:COG0666    53 LGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGN 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462559640  92 NDVVRFLFGFGASTEFRTKDGGTALLAASQYGHMQVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLASGAKV 171
Cdd:COG0666   133 LEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADV 212


                  .
gi 2462559640 172 N 172
Cdd:COG0666   213 N 213
Ank_2 pfam12796
Ankyrin repeats (3 copies);
50-141 2.26e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 89.02  E-value: 2.26e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462559640  50 LMVAAYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTEfrTKDGGTALLAASQYGHMQVVE 129
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|..
gi 2462559640 130 TLLKHGANIHDQ 141
Cdd:pfam12796  79 LLLEKGADINVK 90
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 38-176 3.02e-22

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 93.39  E-value: 3.02e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462559640  38 DVDCRDSHGTTLLMVAAYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTEFRTkdGGTALL 117
Cdd:PLN03192  550 DPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHA--AGDLLC 627

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462559640 118 AASQYGHMQVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLASGAKVNQPRT 176
Cdd:PLN03192  628 TAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANT 686
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 9-149 5.31e-08

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 51.94  E-value: 5.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462559640   9 ETPLanaaFWAARRGNLALLKLLLNSGRVDVDCRDSHGTTLLMVAAYAGH-------IDCVRELVLQGADINLQResGTT 81
Cdd:cd22192    18 ESPL----LLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNleaavvlMEAAPELVNEPMTSDLYQ--GET 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462559640  82 ALFFAAQQGHNDVVRFLFGFGAS--------TEFRTkdGGTALL---------AASQyGHMQVVETLLKHGANIHDQLYD 144
Cdd:cd22192    92 ALHIAVVNQNLNLVRELIARGADvvspratgTFFRP--GPKNLIyygehplsfAACV-GNEEIVRLLIEHGADIRAQDSL 168


                  ....*
gi 2462559640 145 GATAL 149
Cdd:cd22192   169 GNTVL 173
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 45-74 3.33e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.49  E-value: 3.33e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 2462559640   45 HGTTLLMVAAYAGHIDCVRELVLQGADINL 74
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 41-166 1.23e-04

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 41.99  E-value: 1.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462559640  41 CRDSHGTTLLMVAAYAGHIDCVRELVLQGADINL-------QRESGTTALF-------FAAQQGHNDVVRFLFGFGASte 106
Cdd:TIGR00870 123 SEFTPGITALHLAAHRQNYEIVKLLLERGASVPAracgdffVKSQGVDSFYhgesplnAAACLGSPSIVALLSEDPAD-- 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462559640 107 frtkdggtaLLAASQYG----HMQVVET----------------LLKHGANIHDQL-------YDGATALFLAAQGGYLD 159
Cdd:TIGR00870 201 ---------ILTADSLGntllHLLVMENefkaeyeelscqmynfALSLLDKLRDSKelevilnHQGLTPLKLAAKEGRIV 271


                  ....*..
gi 2462559640 160 VIRLLLA 166
Cdd:TIGR00870 272 LFRLKLA 278
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
12-172 3.35e-43

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 145.87  E-value: 3.35e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462559640  12 LANAAFWAARRGNLALLKLLLNSGRVDVDCRDSHGTTLLMVAAYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGH 91
Cdd:COG0666    53 LGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGN 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462559640  92 NDVVRFLFGFGASTEFRTKDGGTALLAASQYGHMQVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLASGAKV 171
Cdd:COG0666   133 LEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADV 212


                  .
gi 2462559640 172 N 172
Cdd:COG0666   213 N 213
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
15-172 3.16e-42

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 143.56  E-value: 3.16e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462559640  15 AAFWAARRGNLALLKLLLNSGrVDVDCRDSHGTTLLMVAAYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDV 94
Cdd:COG0666    90 LLHAAARNGDLEIVKLLLEAG-ADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEI 168

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462559640  95 VRFLFGFGASTEFRTKDGGTALLAASQYGHMQVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLASGAKVN 172
Cdd:COG0666   169 VKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN 246
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
9-172 6.97e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 119.29  E-value: 6.97e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462559640   9 ETPLanaaFWAARRGNLALLKLLLNSGrVDVDCRDSHGTTLLMVAAYAGHIDCVRELVLQGADINLQRESGTTALFFAAQ 88
Cdd:COG0666   121 ETPL----HLAAYNGNLEIVKLLLEAG-ADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAE 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462559640  89 QGHNDVVRFLFGFGASTEFRTKDGGTALLAASQYGHMQVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLASG 168
Cdd:COG0666   196 NGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLAL 275


                  ....
gi 2462559640 169 AKVN 172
Cdd:COG0666   276 LLLA 279
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
12-174 1.81e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 118.13  E-value: 1.81e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462559640  12 LANAAFWAARRGNLALLKLLLNSGRVDVDCRDSHGTTLLMVAAYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGH 91
Cdd:COG0666    20 LLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGD 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462559640  92 NDVVRFLFGFGASTEFRTKDGGTALLAASQYGHMQVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLASGAKV 171
Cdd:COG0666   100 LEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADV 179


                  ...
gi 2462559640 172 NQP 174
Cdd:COG0666   180 NAR 182
Ank_2 pfam12796
Ankyrin repeats (3 copies);
50-141 2.26e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 89.02  E-value: 2.26e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462559640  50 LMVAAYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTEfrTKDGGTALLAASQYGHMQVVE 129
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|..
gi 2462559640 130 TLLKHGANIHDQ 141
Cdd:pfam12796  79 LLLEKGADINVK 90
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 38-176 3.02e-22

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 93.39  E-value: 3.02e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462559640  38 DVDCRDSHGTTLLMVAAYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTEFRTkdGGTALL 117
Cdd:PLN03192  550 DPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHA--AGDLLC 627

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462559640 118 AASQYGHMQVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLASGAKVNQPRT 176
Cdd:PLN03192  628 TAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANT 686
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
38-174 1.58e-21

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 89.24  E-value: 1.58e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462559640  38 DVDCRDSHGTTLLMVAAYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTEFRTKDGGTALL 117
Cdd:COG0666    13 AALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLH 92

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462559640 118 AASQYGHMQVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLASGAKVNQP 174
Cdd:COG0666    93 AAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQ 149
Ank_2 pfam12796
Ankyrin repeats (3 copies);
83-173 1.80e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 84.01  E-value: 1.80e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462559640  83 LFFAAQQGHNDVVRFLFGFGASTEFRTKDGGTALLAASQYGHMQVVETLLKHGANihDQLYDGATALFLAAQGGYLDVIR 162
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|.
gi 2462559640 163 LLLASGAKVNQ 173
Cdd:pfam12796  79 LLLEKGADINV 89
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
9-149 1.14e-20

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 86.93  E-value: 1.14e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462559640   9 ETPLanaaFWAARRGNLALLKLLLNSGrVDVDCRDSHGTTLLMVAAYAGHIDCVRELVLQGADINLQRESGTTALFFAAQ 88
Cdd:COG0666   154 NTPL----HLAAANGNLEIVKLLLEAG-ADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAE 228

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462559640  89 QGHNDVVRFLFGFGASTEFRTKDGGTALLAASQYGHMQVVETLLKHGANIHDQLYDGATAL 149
Cdd:COG0666   229 NGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
Ank_2 pfam12796
Ankyrin repeats (3 copies);
17-104 2.50e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.83  E-value: 2.50e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462559640  17 FWAARRGNLALLKLLLNSGrVDVDCRDSHGTTLLMVAAYAGHIDCVRELvLQGADINLQrESGTTALFFAAQQGHNDVVR 96
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENG-ADANLQDKNGRTALHLAAKNGHLEIVKLL-LEHADVNLK-DNGRTALHYAARSGHLEIVK 78


                  ....*...
gi 2462559640  97 FLFGFGAS 104
Cdd:pfam12796  79 LLLEKGAD 86
PHA03095 PHA03095
ankyrin-like protein; Provisional
 38-171 3.15e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 61.19  E-value: 3.15e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462559640  38 DVDCRDSHGTTLLMVAAYAGHIDC---VRELVLQGADINLQRESGTTALFFAAQQGHN-DVVRFLFGFGASTEFRTKDGG 113
Cdd:PHA03095   39 DVNFRGEYGKTPLHLYLHYSSEKVkdiVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKAGADVNAKDKVGR 118

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462559640 114 TALLA--ASQYGHMQVVETLLKHGANIHDQLYDGATAL--FLAAQGGYLDVIRLLLASGAKV 171
Cdd:PHA03095  119 TPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLavLLKSRNANVELLRLLIDAGADV 180
Ank_4 pfam13637
Ankyrin repeats (many copies);
46-98 6.43e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.36  E-value: 6.43e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462559640  46 GTTLLMVAAYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFL 98
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 38-173 1.92e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 58.91  E-value: 1.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462559640  38 DVDCRDSHGTTLLMVAAYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHN-----DVVRFLFGFGASTEFRTKDG 112
Cdd:PHA03100   27 LNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNG 106

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462559640 113 GTALLAASQY--GHMQVVETLLKHGANIHDQLYDGATALFLAAQGGY--LDVIRLLLASGAKVNQ 173
Cdd:PHA03100  107 ITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINA 171
Ank_4 pfam13637
Ankyrin repeats (many copies);
112-165 6.28e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.66  E-value: 6.28e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462559640 112 GGTALLAASQYGHMQVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLL 165
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 19-172 8.70e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 56.92  E-value: 8.70e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462559640  19 AARRGNLALLKLLLNSGRVDVDCRDSHGTTLLMVAAYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFL 98
Cdd:PHA02875   75 AVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELL 154

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462559640  99 FGFGASTEFRTKDGGTALLAASQYGHMQVVETLLKHGANIHDQLYDG-ATALFLAAQGGYLDVIRLLLASGAKVN 172
Cdd:PHA02875  155 IDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCN 229
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 37-152 1.71e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 56.13  E-value: 1.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462559640  37 VDVDCRDSHGTTLLMVAAYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTEFRTKDGGTAL 116
Cdd:PHA02874  115 IDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPL 194

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2462559640 117 LAASQYGHMQVVETLLKHGANIHDQLYDGATALFLA 152
Cdd:PHA02874  195 HNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNA 230
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 38-172 2.70e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 55.66  E-value: 2.70e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462559640  38 DVDCRDSH-GTTLLMVAAYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTEFRTKDGGTAL 116
Cdd:PHA02878  159 DINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPL 238

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462559640 117 -LAASQYGHMQVVETLLKHGANIHDQLY-DGATALFLAAQGGylDVIRLLLASGAKVN 172
Cdd:PHA02878  239 hISVGYCKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIKSE--RKLKLLLEYGADIN 294
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 62-172 3.42e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 55.27  E-value: 3.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462559640  62 VRELVLQGADINLQ-RESGTTALFFAAQQGHNDVVRFLFGFGASTEFRTKDGGTALLAASQYGHMQVVETLLKHGANIHD 140
Cdd:PHA02878  150 TKLLLSYGADINMKdRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDA 229

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2462559640 141 QLYDGATALFLAAqgGYL---DVIRLLLASGAKVN 172
Cdd:PHA02878  230 RDKCGNTPLHISV--GYCkdyDILKLLLEHGVDVN 262
Ank_5 pfam13857
Ankyrin repeats (many copies);
35-86 1.30e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 49.27  E-value: 1.30e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462559640  35 GRVDVDCRDSHGTTLLMVAAYAGHIDCVRELVLQGADINLQRESGTTALFFA 86
Cdd:pfam13857   5 GPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 34-100 2.19e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.98  E-value: 2.19e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462559640  34 SGRVDVDCRDSHGTTLLMVAAYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFG 100
Cdd:PTZ00322  103 TGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 62-151 3.20e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.59  E-value: 3.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462559640  62 VRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTEFRTKDGGTALLAASQYGHMQVVETLLKH------- 134
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHsqchfel 177

                          90
                  ....*....|....*..
gi 2462559640 135 GANIHDQLYDGATALFL 151
Cdd:PTZ00322  178 GANAKPDSFTGKPPSLE 194
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 5-172 4.86e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 51.99  E-value: 4.86e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462559640   5 SFKKETPLanaaFWAARRGNLALLKLLLNSGRVDVDCRDS-HGTTLLMVAAYAGHIDCVRELVLQGADINLQRESGTTAL 83
Cdd:PHA02876  304 NIKGETPL----YLMAKNGYDTENIRTLIMLGADVNAADRlYITPLHQASTLDRNKDIVITLLELGANVNARDYCDKTPI 379

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462559640  84 FFAAQQGHNDVVRFLFGFGASTEFRTKDGGTAL-LAASQYGHMQVVETLLKHGANIHDQLYDGATALFLAAQGG-YLDVI 161
Cdd:PHA02876  380 HYAAVRNNVVIINTLLDYGADIEALSQKIGTALhFALCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVI 459

                         170
                  ....*....|.
gi 2462559640 162 RLLLASGAKVN 172
Cdd:PHA02876  460 EMLLDNGADVN 470
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 9-149 5.31e-08

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 51.94  E-value: 5.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462559640   9 ETPLanaaFWAARRGNLALLKLLLNSGRVDVDCRDSHGTTLLMVAAYAGH-------IDCVRELVLQGADINLQResGTT 81
Cdd:cd22192    18 ESPL----LLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNleaavvlMEAAPELVNEPMTSDLYQ--GET 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462559640  82 ALFFAAQQGHNDVVRFLFGFGAS--------TEFRTkdGGTALL---------AASQyGHMQVVETLLKHGANIHDQLYD 144
Cdd:cd22192    92 ALHIAVVNQNLNLVRELIARGADvvspratgTFFRP--GPKNLIyygehplsfAACV-GNEEIVRLLIEHGADIRAQDSL 168


                  ....*
gi 2462559640 145 GATAL 149
Cdd:cd22192   169 GNTVL 173
Ank_4 pfam13637
Ankyrin repeats (many copies);
79-132 6.84e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.27  E-value: 6.84e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462559640  79 GTTALFFAAQQGHNDVVRFLFGFGASTEFRTKDGGTALLAASQYGHMQVVETLL 132
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 53-176 1.20e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 50.76  E-value: 1.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462559640  53 AAYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTEFRTKDGGTALLAASQYGHMQVVETLL 132
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2462559640 133 KHGANIHDQLY-DGATALFLAAQGGYLDVIRLLLASGAKVNQPRT 176
Cdd:PHA02875   89 DLGKFADDVFYkDGMTPLHLATILKKLDIMKLLIARGADPDIPNT 133
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 37-172 1.42e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 50.43  E-value: 1.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462559640  37 VDVDCRDSHGTTLLMVAAYA--GHIDCVRELVLQGADINLQRESGTTALFFAAQQGHND--VVRFLF------------- 99
Cdd:PHA03100   97 ANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDlkILKLLIdkgvdinaknrvn 176

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462559640 100 ---GFGASTEFRTKDGGTALLAASQYGHMQVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLASGAKVN 172
Cdd:PHA03100  177 yllSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 66-177 1.58e-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: 50.40  E-value: 1.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462559640  66 VLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFgASTEFRTKD--GGTALLAASQYGHMQVVETLLKHG---AN--I 138
Cdd:cd22192     4 MLDELHLLQQKRISESPLLLAAKENDVQAIKKLLKC-PSCDLFQRGalGETALHVAALYDNLEAAVVLMEAApelVNepM 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2462559640 139 HDQLYDGATALFLAAQGGYLDVIRLLLASGAKVNQPR-TG 177
Cdd:cd22192    83 TSDLYQGETALHIAVVNQNLNLVRELIARGADVVSPRaTG 122
Ank_2 pfam12796
Ankyrin repeats (3 copies);
14-75 4.83e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 45.88  E-value: 4.83e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462559640  14 NAAFWAARRGNLALLKLLLNSGRVDVDCrdsHGTTLLMVAAYAGHIDCVRELVLQGADINLQ 75
Cdd:pfam12796  32 TALHLAAKNGHLEIVKLLLEHADVNLKD---NGRTALHYAARSGHLEIVKLLLEKGADINVK 90
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 95-165 4.83e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.13  E-value: 4.83e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462559640  95 VRFLFGFGASTEFRTKDGGTALLAASQYGHMQVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLL 165
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
PHA03095 PHA03095
ankyrin-like protein; Provisional
 59-172 5.05e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 48.87  E-value: 5.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462559640  59 IDCVRELVLQGADINLQRESGTTALffaAQQGHN------DVVRFLFGFGASTEFRTKDGGTALLAASQYGH-MQVVETL 131
Cdd:PHA03095   27 VEEVRRLLAAGADVNFRGEYGKTPL---HLYLHYssekvkDIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLL 103

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2462559640 132 LKHGANIHDQLYDGATAL--FLAAQGGYLDVIRLLLASGAKVN 172
Cdd:PHA03095  104 IKAGADVNAKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVN 146
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 36-172 5.20e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 48.81  E-value: 5.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462559640  36 RVDVDCRDSHGTTLLMVAAYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTEFRTKDGGTA 115
Cdd:PHA02874  147 GADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTP 226

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462559640 116 LLAASQYGHmQVVEtLLKHGANIHDQLYDGATALFLAAQ-GGYLDVIRLLLASGAKVN 172
Cdd:PHA02874  227 LHNAIIHNR-SAIE-LLINNASINDQDIDGSTPLHHAINpPCDIDIIDILLYHKADIS 282
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 60-180 2.25e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 46.88  E-value: 2.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462559640  60 DCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTEFRTKDGGTALLAASQYGHMQVVETLLKHGANIH 139
Cdd:PHA02874  105 DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2462559640 140 DQLYDGATALFLAAQGGYLDVIRLLLASGAKV-NQPRTGQRP 180
Cdd:PHA02874  185 VKDNNGESPLHNAAEYGDYACIKLLIDHGNHImNKCKNGFTP 226
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 10-172 7.43e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 45.34  E-value: 7.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462559640  10 TPLANAAfwaaRRGNLALLKLLLNSGrVDVDCRDSHGTTLLMVAAYAGHIDCVRELVLQGADINLqresgttalfFAAQQ 89
Cdd:PHA02874   37 TPLIDAI----RSGDAKIVELFIKHG-ADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSI----------LPIPC 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462559640  90 GHNDVVRFLFGFGASTEFRTKDGGTALLAASQYGHMQVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLASGA 169
Cdd:PHA02874  102 IEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGA 181


                  ...
gi 2462559640 170 KVN 172
Cdd:PHA02874  182 YAN 184
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 37-107 1.09e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 45.04  E-value: 1.09e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462559640  37 VDVDCRDSHGTTLLMVAAYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTEF 107
Cdd:PHA03100  183 VPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 35-172 1.56e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 44.67  E-value: 1.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462559640  35 GRVDVDCRDSHGTTLLMVAAYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVR------------------ 96
Cdd:PHA02876  167 GGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKaiidnrsninkndlsllk 246

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462559640  97 -----------FLFGFGASTEFRTKDGGTALLAASQYGHM-QVVETLLKHGANIHDQLYDGATALFLAAQGGY-LDVIRL 163
Cdd:PHA02876  247 airnedletslLLYDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRT 326


                  ....*....
gi 2462559640 164 LLASGAKVN 172
Cdd:PHA02876  327 LIMLGADVN 335
PHA02798 PHA02798
ankyrin-like protein; Provisional
 59-173 2.20e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 44.06  E-value: 2.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462559640  59 IDCVRELVLQGADIN-LQRESGT---TALFFAAQQGHN-DVVRFLFGFGASTEFRTKDGGT---ALLAASQYGHMQVVET 130
Cdd:PHA02798   51 TDIVKLFINLGANVNgLDNEYSTplcTILSNIKDYKHMlDIVKILIENGADINKKNSDGETplyCLLSNGYINNLEILLF 130

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2462559640 131 LLKHGANIHDQLYDGATALFLAAQGGY---LDVIRLLLASGAKVNQ 173
Cdd:PHA02798  131 MIENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDINT 176
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 45-74 3.33e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.49  E-value: 3.33e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 2462559640   45 HGTTLLMVAAYAGHIDCVRELVLQGADINL 74
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
70-116 3.82e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.02  E-value: 3.82e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2462559640  70 ADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTEFRTKDGGTAL 116
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 111-141 6.12e-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: 38.81  E-value: 6.12e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2462559640 111 DGGTAL-LAASQYGHMQVVETLLKHGANIHDQ 141
Cdd:pfam00023   1 DGNTPLhLAAGRRGNLEIVKLLLSKGADVNAR 32
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 41-166 1.23e-04

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 41.99  E-value: 1.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462559640  41 CRDSHGTTLLMVAAYAGHIDCVRELVLQGADINL-------QRESGTTALF-------FAAQQGHNDVVRFLFGFGASte 106
Cdd:TIGR00870 123 SEFTPGITALHLAAHRQNYEIVKLLLERGASVPAracgdffVKSQGVDSFYhgesplnAAACLGSPSIVALLSEDPAD-- 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462559640 107 frtkdggtaLLAASQYG----HMQVVET----------------LLKHGANIHDQL-------YDGATALFLAAQGGYLD 159
Cdd:TIGR00870 201 ---------ILTADSLGntllHLLVMENefkaeyeelscqmynfALSLLDKLRDSKelevilnHQGLTPLKLAAKEGRIV 271


                  ....*..
gi 2462559640 160 VIRLLLA 166
Cdd:TIGR00870 272 LFRLKLA 278
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 144-172 1.57e-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: 37.57  E-value: 1.57e-04
                           10        20
                   ....*....|....*....|....*....
gi 2462559640  144 DGATALFLAAQGGYLDVIRLLLASGAKVN 172
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 45-75 2.20e-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: 37.27  E-value: 2.20e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2462559640  45 HGTTLLMVAAY-AGHIDCVRELVLQGADINLQ 75
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNAR 32
PHA03095 PHA03095
ankyrin-like protein; Provisional
 37-96 2.26e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 41.16  E-value: 2.26e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462559640  37 VDVDCRDSHGTTLLMVAAYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGHNDVVR 96
Cdd:PHA03095  248 ISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVR 307
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 71-172 3.38e-04

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 40.45  E-value: 3.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462559640  71 DINLQRESGTTALFFAAQQGHNDVVRFLFGFgasTEFRTKDGGTALLAASQyGHMQVVETLLKHGANIH----------- 139
Cdd:TIGR00870  44 NINCPDRLGRSALFVAAIENENLELTELLLN---LSCRGAVGDTLLHAISL-EYVDAVEAILLHLLAAFrksgpleland 119

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2462559640 140 ---DQLYDGATALFLAAQGGYLDVIRLLLASGAKVN 172
Cdd:TIGR00870 120 qytSEFTPGITALHLAAHRQNYEIVKLLLERGASVP 155
PHA03095 PHA03095
ankyrin-like protein; Provisional
 37-133 3.43e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 40.39  E-value: 3.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462559640  37 VDVDCRDSHGTTLLMVAAYagHIDCVRELVLQ----GADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTEFRTKDG 112
Cdd:PHA03095  213 CDPAATDMLGNTPLHSMAT--GSSCKRSLVLPlliaGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDG 290

                          90       100
                  ....*....|....*....|.
gi 2462559640 113 GTALLAASQYGHMQVVETLLK 133
Cdd:PHA03095  291 NTPLSLMVRNNNGRAVRAALA 311
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 111-140 5.25e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.03  E-value: 5.25e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 2462559640  111 DGGTALLAASQYGHMQVVETLLKHGANIHD 140
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 144-173 8.11e-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: 35.73  E-value: 8.11e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2462559640 144 DGATALFLAA-QGGYLDVIRLLLASGAKVNQ 173
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNA 31
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 62-172 1.06e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 39.28  E-value: 1.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462559640  62 VRELVLQ-GADINLQRESGTTALFFAAQQGHNDVVRFLFGFGASTEFRTKDGGTALLAASQYGHMQVVETLLKHGANIHD 140
Cdd:PHA02876  160 IAEMLLEgGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINK 239

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2462559640 141 QlydgATALFLAAQGGYLDVIRLLLASGAKVN 172
Cdd:PHA02876  240 N----DLSLLKAIRNEDLETSLLLYDAGFSVN 267
PHA02795 PHA02795
ankyrin-like protein; Provisional
 38-90 1.36e-03

ankyrin-like protein; Provisional


Pssm-ID: 165157 [Multi-domain]  Cd Length: 437  Bit Score: 38.82  E-value: 1.36e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462559640  38 DVDCRDSHGTTLLMVAAYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQG 90
Cdd:PHA02795  213 DINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDVAVDRG 265
PHA02798 PHA02798
ankyrin-like protein; Provisional
 47-139 1.92e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 38.28  E-value: 1.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462559640  47 TTLLMVAAYAGHIDCVRELVLQGADINLQRESGTTALFFAAQQGH---NDVVRFLFGFGASTEFRTKDGGTALLAASQYG 123
Cdd:PHA02798   77 TILSNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYinnLEILLFMIENGADTTLLDKDGFTMLQVYLQSN 156

                          90
                  ....*....|....*....
gi 2462559640 124 H---MQVVETLLKHGANIH 139
Cdd:PHA02798  157 HhidIEIIKLLLEKGVDIN 175
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 48-73 3.92e-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: 33.77  E-value: 3.92e-03
                          10        20
                  ....*....|....*....|....*.
gi 2462559640  48 TLLMVAAYAGHIDCVRELVLQGADIN 73
Cdd:pfam13606   4 TPLHLAARNGRLEIVKLLLENGADIN 29
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 117-171 4.24e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 37.19  E-value: 4.24e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2462559640 117 LAASqyGHMQVVETLLKHGANIHDQLYDGATALFLAAQGGYLDVIRLLLASGAKV 171
Cdd:PTZ00322   89 LAAS--GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADP 141
PHA03095 PHA03095
ankyrin-like protein; Provisional
 60-167 4.68e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 36.93  E-value: 4.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462559640  60 DCVRELVLQGADINLQRESGTTALFFAAQQG--HNDVVRFLFGFGASTEFRTKDGGTALLAASQYGHMQVVETLLKHGAN 137
Cdd:PHA03095  203 RIVRELIRAGCDPAATDMLGNTPLHSMATGSscKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGAD 282

                          90       100       110
                  ....*....|....*....|....*....|
gi 2462559640 138 IHDQLYDGATALFLAAQGGYLDVIRLLLAS 167
Cdd:PHA03095  283 INAVSSDGNTPLSLMVRNNNGRAVRAALAK 312
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 111-139 6.52e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 33.00  E-value: 6.52e-03
                          10        20
                  ....*....|....*....|....*....
gi 2462559640 111 DGGTALLAASQYGHMQVVETLLKHGANIH 139
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH