NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|386766475|ref|NP_001163715|]
View 

uncharacterized protein Dmel_CG11168, isoform C [Drosophila melanogaster]

Protein Classification

ankyrin repeat domain-containing protein( domain architecture ID 13837771)

ankyrin repeat (ANK) domain-containing protein 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

CATH:  1.25.40.20
Gene Ontology:  GO:0005515
PubMed:  33435370|15152081|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];
42-271 4.90e-39

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 139.70  E-value: 4.90e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475  42 INCQDMNGYTSLHHACLNGHSNIVRLLLSHNALLDVPDIRGSTPLFLAAWAGHQDIVKMLLMHsptGANPNAQTIENETP 121
Cdd:COG0666   80 INAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA---GADVNAQDNDGNTP 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475 122 LHSGAQHGHNAVVAILLSYGADPAIRNNSFQTALDLAAQFGRLQVVQTLLRVYPDLilpykRLEDDNEEllgcmpikhif 201
Cdd:COG0666  157 LHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADV-----NAKDNDGK----------- 220

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386766475 202 thTCLHLASRNGHKKVVETLLAAGVDVNILTNAG-SALHEAALCGKKSVVVTLLKAGIYVHATDGNGRTAL 271
Cdd:COG0666  221 --TALDLAAENGNLEIVKLLLEAGADLNAKDKDGlTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
Ank_4 pfam13637
Ankyrin repeats (many copies);
6-69 3.13e-05

Ankyrin repeats (many copies);


:

Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.11  E-value: 3.13e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386766475    6 HLLEASRAGDIKTVDKLLEHSskrhgplssfrrsPSINCQDMNGYTSLHHACLNGHSNIVRLLL 69
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKG-------------ADINAVDGNGETALHFAASNGNVEVLKLLL 54
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
42-271 4.90e-39

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 139.70  E-value: 4.90e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475  42 INCQDMNGYTSLHHACLNGHSNIVRLLLSHNALLDVPDIRGSTPLFLAAWAGHQDIVKMLLMHsptGANPNAQTIENETP 121
Cdd:COG0666   80 INAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA---GADVNAQDNDGNTP 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475 122 LHSGAQHGHNAVVAILLSYGADPAIRNNSFQTALDLAAQFGRLQVVQTLLRVYPDLilpykRLEDDNEEllgcmpikhif 201
Cdd:COG0666  157 LHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADV-----NAKDNDGK----------- 220

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386766475 202 thTCLHLASRNGHKKVVETLLAAGVDVNILTNAG-SALHEAALCGKKSVVVTLLKAGIYVHATDGNGRTAL 271
Cdd:COG0666  221 --TALDLAAENGNLEIVKLLLEAGADLNAKDKDGlTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
Ank_2 pfam12796
Ankyrin repeats (3 copies);
53-148 3.90e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.93  E-value: 3.90e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475   53 LHHACLNGHSNIVRLLLSHNALLDVPDIRGSTPLFLAAWAGHQDIVKMLLMHsptgANPNAQTiENETPLHSGAQHGHNA 132
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH----ADVNLKD-NGRTALHYAARSGHLE 75

                          90
                  ....*....|....*.
gi 386766475  133 VVAILLSYGADPAIRN 148
Cdd:pfam12796  76 IVKLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 42-271 1.64e-17

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 82.77  E-value: 1.64e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475  42 INCQDMNGYTSLHHACLNGHS-NIVRLLLSHNALLDVPDIRGSTPL--FLAAWAGHQDIVKMLLMHsptGANPNAQTIEN 118
Cdd:PHA03095  76 VNAPERCGFTPLHLYLYNATTlDVIKLLIKAGADVNAKDKVGRTPLhvYLSGFNINPKVIRLLLRK---GADVNALDLYG 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475 119 ETPLH----SgaqhgHNA---VVAILLSYGADPAIRNNSFQTALDLAAQFGRlqvvqtllrvypdlilPYKRLeddNEEL 191
Cdd:PHA03095 153 MTPLAvllkS-----RNAnveLLRLLIDAGADVYAVDDRFRSLLHHHLQSFK----------------PRARI---VREL 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475 192 --LGCMPI-KHIFTHTCLHLASRNGHKK--VVETLLAAGVDVNILTNAG-SALHEAALCGKKSVVVTLLKAGIYVHATDG 265
Cdd:PHA03095 209 irAGCDPAaTDMLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYGqTPLHYAAVFNNPRACRRLIALGADINAVSS 288


                 ....*.
gi 386766475 266 NGRTAL 271
Cdd:PHA03095 289 DGNTPL 294
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 49-172 1.00e-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: 56.56  E-value: 1.00e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475  49 GYTSLHHACLNGHSNIVRLLLSHNAllDVPDIR----------------GSTPLFLAAWAGHQDIVKMLLMHsptGANPN 112
Cdd:cd22192   89 GETALHIAVVNQNLNLVRELIARGA--DVVSPRatgtffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEH---GADIR 163

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386766475 113 AQTIENETPLHSGAQHGhNAVVA-----ILLSYGA--DPA----IRNNSFQTALDLAAQFGRLQVVQTLLR 172
Cdd:cd22192  164 AQDSLGNTVLHILVLQP-NKTFAcqmydLILSYDKedDLQpldlVPNNQGLTPFKLAAKEGNIVMFQHLVQ 233
Ank_4 pfam13637
Ankyrin repeats (many copies);
6-69 3.13e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.11  E-value: 3.13e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386766475    6 HLLEASRAGDIKTVDKLLEHSskrhgplssfrrsPSINCQDMNGYTSLHHACLNGHSNIVRLLL 69
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKG-------------ADINAVDGNGETALHFAASNGNVEVLKLLL 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 48-77 1.62e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 38.34  E-value: 1.62e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 386766475    48 NGYTSLHHACLNGHSNIVRLLLSHNALLDV 77
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
42-271 4.90e-39

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 139.70  E-value: 4.90e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475  42 INCQDMNGYTSLHHACLNGHSNIVRLLLSHNALLDVPDIRGSTPLFLAAWAGHQDIVKMLLMHsptGANPNAQTIENETP 121
Cdd:COG0666   80 INAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA---GADVNAQDNDGNTP 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475 122 LHSGAQHGHNAVVAILLSYGADPAIRNNSFQTALDLAAQFGRLQVVQTLLRVYPDLilpykRLEDDNEEllgcmpikhif 201
Cdd:COG0666  157 LHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADV-----NAKDNDGK----------- 220

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386766475 202 thTCLHLASRNGHKKVVETLLAAGVDVNILTNAG-SALHEAALCGKKSVVVTLLKAGIYVHATDGNGRTAL 271
Cdd:COG0666  221 --TALDLAAENGNLEIVKLLLEAGADLNAKDKDGlTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
7-192 7.90e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 136.62  E-value: 7.90e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475   7 LLEASRAGDIKTVDKLLEHSskrhgplssfrrsPSINCQDMNGYTSLHHACLNGHSNIVRLLLSHNALLDVPDIRGSTPL 86
Cdd:COG0666   91 LHAAARNGDLEIVKLLLEAG-------------ADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPL 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475  87 FLAAWAGHQDIVKMLLMHsptGANPNAQTIENETPLHSGAQHGHNAVVAILLSYGADPAIRNNSFQTALDLAAQFGRLQV 166
Cdd:COG0666  158 HLAAANGNLEIVKLLLEA---GADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEI 234

                        170       180
                 ....*....|....*....|....*.
gi 386766475 167 VQTLLRVYPDLILPYKRLEDDNEELL 192
Cdd:COG0666  235 VKLLLEAGADLNAKDKDGLTALLLAA 260
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
42-273 9.65e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 120.44  E-value: 9.65e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475  42 INCQDMNGYTSLHHACLNGHSNIVRLLLSHNALLDVPDIRGSTPLFLAAWAGHQDIVKMLLMHsptGANPNAQTIENETP 121
Cdd:COG0666   14 ALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAA---GADINAKDDGGNTL 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475 122 LHSGAQHGHNAVVAILLSYGADPAIRNNSFQTALDLAAQFGRLQVVQTLLrvypdlilpyKRLEDDNeellgcmpIKHIF 201
Cdd:COG0666   91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLL----------EAGADVN--------AQDND 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386766475 202 THTCLHLASRNGHKKVVETLLAAGVDVNILTNAG-SALHEAALCGKKSVVVTLLKAGIYVHATDGNGRTALDI 273
Cdd:COG0666  153 GNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGeTPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDL 225
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
7-188 2.14e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 116.59  E-value: 2.14e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475   7 LLEASRAGDIKTVDKLLEHSSKrhgplssfrrspsINCQDMNGYTSLHHACLNGHSNIVRLLLSHNALLDVPDIRGSTPL 86
Cdd:COG0666  124 LHLAAYNGNLEIVKLLLEAGAD-------------VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPL 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475  87 FLAAWAGHQDIVKMLLMHsptGANPNAQTIENETPLHSGAQHGHNAVVAILLSYGADPAIRNNSFQTALDLAAQFGRLQV 166
Cdd:COG0666  191 HLAAENGHLEIVKLLLEA---GADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALI 267

                        170       180
                 ....*....|....*....|..
gi 386766475 167 VQTLLRVYPDLILPYKRLEDDN 188
Cdd:COG0666  268 VKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
64-273 1.79e-21

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 92.32  E-value: 1.79e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475  64 IVRLLLSHNALLDVPDIRGSTPLFLAAWAGHQDIVKMLLMHSPtGANPNAQTIENETPLHSGAQHGHNAVVAILLSYGAD 143
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLA-LLALALADALGALLLLAAALAGDLLVALLLLAAGAD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475 144 PAIRNNSFQTALDLAAQFGRLQVVQTLLRVYPDLILPYKRLEddneellgcmpikhifthTCLHLASRNGHKKVVETLLA 223
Cdd:COG0666   80 INAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGE------------------TPLHLAAYNGNLEIVKLLLE 141

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 386766475 224 AGVDVNILTNAG-SALHEAALCGKKSVVVTLLKAGIYVHATDGNGRTALDI 273
Cdd:COG0666  142 AGADVNAQDNDGnTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHL 192
Ank_2 pfam12796
Ankyrin repeats (3 copies);
53-148 3.90e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.93  E-value: 3.90e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475   53 LHHACLNGHSNIVRLLLSHNALLDVPDIRGSTPLFLAAWAGHQDIVKMLLMHsptgANPNAQTiENETPLHSGAQHGHNA 132
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH----ADVNLKD-NGRTALHYAARSGHLE 75

                          90
                  ....*....|....*.
gi 386766475  133 VVAILLSYGADPAIRN 148
Cdd:pfam12796  76 IVKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
7-114 5.44e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.46  E-value: 5.44e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475    7 LLEASRAGDIKTVDKLLEHSSkrhgplssfrrspSINCQDMNGYTSLHHACLNGHSNIVRLLLSHNALLDVPDirGSTPL 86
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGA-------------DANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN--GRTAL 65

                          90       100
                  ....*....|....*....|....*...
gi 386766475   87 FLAAWAGHQDIVKMLLMHsptGANPNAQ 114
Cdd:pfam12796  66 HYAARSGHLEIVKLLLEK---GADINVK 90
PHA03095 PHA03095
ankyrin-like protein; Provisional
 42-271 1.64e-17

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 82.77  E-value: 1.64e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475  42 INCQDMNGYTSLHHACLNGHS-NIVRLLLSHNALLDVPDIRGSTPL--FLAAWAGHQDIVKMLLMHsptGANPNAQTIEN 118
Cdd:PHA03095  76 VNAPERCGFTPLHLYLYNATTlDVIKLLIKAGADVNAKDKVGRTPLhvYLSGFNINPKVIRLLLRK---GADVNALDLYG 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475 119 ETPLH----SgaqhgHNA---VVAILLSYGADPAIRNNSFQTALDLAAQFGRlqvvqtllrvypdlilPYKRLeddNEEL 191
Cdd:PHA03095 153 MTPLAvllkS-----RNAnveLLRLLIDAGADVYAVDDRFRSLLHHHLQSFK----------------PRARI---VREL 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475 192 --LGCMPI-KHIFTHTCLHLASRNGHKK--VVETLLAAGVDVNILTNAG-SALHEAALCGKKSVVVTLLKAGIYVHATDG 265
Cdd:PHA03095 209 irAGCDPAaTDMLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYGqTPLHYAAVFNNPRACRRLIALGADINAVSS 288


                 ....*.
gi 386766475 266 NGRTAL 271
Cdd:PHA03095 289 DGNTPL 294
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 16-231 2.09e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 73.55  E-value: 2.09e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475  16 IKTVDKLLEHSSkrhgplssfrrspSINCQDMNGYTSLHHACLNGHS-----NIVRLLLSHNALLDVPDIRGSTPLFLAA 90
Cdd:PHA03100  48 IDVVKILLDNGA-------------DINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAI 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475  91 WA--GHQDIVKMLLMHsptGANPNAQTIENETPLHSGA--------------QHGHNA----VVAILLSYGADPAIRNNS 150
Cdd:PHA03100 115 SKksNSYSIVEYLLDN---GANVNIKNSDGENLLHLYLesnkidlkilklliDKGVDInaknRVNYLLSYGVPINIKDVY 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475 151 FQTALDLAAQFGRLQVVQTLLRvypdlilpykrleddneelLGCMP-IKHIFTHTCLHLASRNGHKKVVETLLAAGVDVN 229
Cdd:PHA03100 192 GFTPLHYAVYNNNPEFVKYLLD-------------------LGANPnLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252


                 ..
gi 386766475 230 IL 231
Cdd:PHA03100 253 TI 254
Ank_2 pfam12796
Ankyrin repeats (3 copies);
122-230 1.91e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 62.44  E-value: 1.91e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475  122 LHSGAQHGHNAVVAILLSYGADPAIRNNSFQTALDLAAQFGRLQVVQTLlrvypdliLPYKRLEDDNEellgcmpikhif 201
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL--------LEHADVNLKDN------------ 60

                          90       100
                  ....*....|....*....|....*....
gi 386766475  202 THTCLHLASRNGHKKVVETLLAAGVDVNI 230
Cdd:pfam12796  61 GRTALHYAARSGHLEIVKLLLEKGADINV 89
PHA03095 PHA03095
ankyrin-like protein; Provisional
 41-235 3.04e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 66.97  E-value: 3.04e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475  41 SINCQDMNGYTSLHhACLNG---HSNIVRLLLSHNALLDVPDIRGSTPL--FLAAWAGHQDIVKMLLMHsptGANPNAQT 115
Cdd:PHA03095 109 DVNAKDKVGRTPLH-VYLSGfniNPKVIRLLLRKGADVNALDLYGMTPLavLLKSRNANVELLRLLIDA---GADVYAVD 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475 116 IENETPLHSGAQ--HGHNAVVAILLSYGADPAIRNNSFQTALDLAAQFGRLQVVqtllrvypdLILPYkrLE---DDNEE 190
Cdd:PHA03095 185 DRFRSLLHHHLQsfKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRS---------LVLPL--LIagiSINAR 253

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 386766475 191 llgcmpikHIFTHTCLHLASRNGHKKVVETLLAAGVDVNILTNAG 235
Cdd:PHA03095 254 --------NRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDG 290
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 13-271 1.32e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 64.98  E-value: 1.32e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475  13 AGDIKTVDKLLEHsskrhgplssfrRSPSINCQDMNGYTSLHHACLNGHSNIVRLLLSHNALLDVPDIRGSTPLFLAAWA 92
Cdd:PHA02874  11 SGDIEAIEKIIKN------------KGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475  93 GHQDIVKMLLMHSPTGANPNAQTIENETplhsgaqhghnavVAILLSYGADPAIRNNSFQTALDLAAQFGRLQVVQTLLR 172
Cdd:PHA02874  79 GAHDIIKLLIDNGVDTSILPIPCIEKDM-------------IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFE 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475 173 VYPDLilpykRLEDDNeellGCMPIkhifthtclHLASRNGHKKVVETLLAAGVDVNILTNAG-SALHEAALCGKKSVVV 251
Cdd:PHA02874 146 YGADV-----NIEDDN----GCYPI---------HIAIKHNFFDIIKLLLEKGAYANVKDNNGeSPLHNAAEYGDYACIK 207

                        250       260
                 ....*....|....*....|
gi 386766475 252 TLLKAGIYVHATDGNGRTAL 271
Cdd:PHA02874 208 LLIDHGNHIMNKCKNGFTPL 227
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 42-264 1.38e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 64.98  E-value: 1.38e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475  42 INCQDMNGYTSLHHACLNGHSNIVRLLLSHNALLDVPDIRGSTPLFLAAWAGHQDIVKMLLmhsPTGANPNAQTIENETP 121
Cdd:PHA02874 117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLL---EKGAYANVKDNNGESP 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475 122 LHSGAQHGHNAVVAILLSYGADPAIRNNSFQTALDLAAQFGRLQVvqtllrvypDLILPYKRLEDdnEELLGCMPIKHIF 201
Cdd:PHA02874 194 LHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAI---------ELLINNASIND--QDIDGSTPLHHAI 262

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386766475 202 THTClhlasrngHKKVVETLLAAGVDVNILTNAGSALHEAAL--CGKKSVVVTLLKAGIYVHATD 264
Cdd:PHA02874 263 NPPC--------DIDIIDILLYHKADISIKDNKGENPIDTAFkyINKDPVIKDIIANAVLIKEAD 319
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 62-231 5.25e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 63.36  E-value: 5.25e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475  62 SNIVRLLLSHNALLDVPDI-RGSTPLFLAAWAGHQDIVKMLLMHsptGANPNAQTIENETPLHSGAQHGHNAVVAILLSY 140
Cdd:PHA02878 147 AEITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSY---GANVNIPDKTNNSPLHHAVKHYNKPIVHILLEN 223

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475 141 GADPAIRNNSFQTALDLAAqfGRL---QVVQTLLrvypdlilpykrleddneELLGCMPIK-HIFTHTCLHLASRNghKK 216
Cdd:PHA02878 224 GASTDARDKCGNTPLHISV--GYCkdyDILKLLL------------------EHGVDVNAKsYILGLTALHSSIKS--ER 281

                        170
                 ....*....|....*
gi 386766475 217 VVETLLAAGVDVNIL 231
Cdd:PHA02878 282 KLKLLLEYGADINSL 296
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 42-189 5.29e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 63.15  E-value: 5.29e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475  42 INCQDMNGYTSLHHACLN--GHSNIVRLLLSHNALLDVPDIRGSTPLFLAAWAGHQD--IVKMLLMHsptGANPNAQT-- 115
Cdd:PHA03100  99 VNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDlkILKLLIDK---GVDINAKNrv 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475 116 --------------IENETPLHSGAQHGHNAVVAILLSYGADPAIRNNSFQTALDLAAQFGRLQVVQTLLRVYPDL--IL 179
Cdd:PHA03100 176 nyllsygvpinikdVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIktII 255

                        170
                 ....*....|
gi 386766475 180 PYKRLEDDNE 189
Cdd:PHA03100 256 ETLLYFKDKD 265
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 48-289 8.79e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 62.32  E-value: 8.79e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475  48 NGYTSLHHACLNGHSNIVRLLLSHNALLDV--PDIRgsTPLFLAAWAGHQDIVKMLLMhSPTGANpNAQTIENETPLHSG 125
Cdd:PHA02875  34 DGISPIKLAMKFRDSEAIKLLMKHGAIPDVkyPDIE--SELHDAVEEGDVKAVEELLD-LGKFAD-DVFYKDGMTPLHLA 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475 126 AQHGHNAVVAILLSYGADPAIRNNSFQTALDLAAQFGRLQVVQTLLRvypdlilpyKRLEDDNEELLGCMPikhifthtc 205
Cdd:PHA02875 110 TILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLID---------HKACLDIEDCCGCTP--------- 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475 206 LHLASRNGHKKVVETLLAAGVDVNILTNAGSAlheAALC-----GKKSVVVTLLKAGI---YVHATDGNGRTALDILSDY 277
Cdd:PHA02875 172 LIIAMAKGDIAICKMLLDSGANIDYFGKNGCV---AALCyaienNKIDIVRLFIKRGAdcnIMFMIEGEECTILDMICNM 248

                        250
                 ....*....|..
gi 386766475 278 PPHVTYDIVGAI 289
Cdd:PHA02875 249 CTNLESEAIDAL 260
Ank_2 pfam12796
Ankyrin repeats (3 copies);
155-264 5.68e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 55.51  E-value: 5.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475  155 LDLAAQFGRLQVVQTLLRVYPDlilpyKRLEDDNEEllgcmpikhifthTCLHLASRNGHKKVVEtLLAAGVDVNILTNA 234
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGAD-----ANLQDKNGR-------------TALHLAAKNGHLEIVK-LLLEHADVNLKDNG 61

                          90       100       110
                  ....*....|....*....|....*....|
gi 386766475  235 GSALHEAALCGKKSVVVTLLKAGIYVHATD 264
Cdd:pfam12796  62 RTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 10-171 1.14e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 59.21  E-value: 1.14e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475  10 ASRAGDIKTVDKLLEHSSkrhgplssfrrspSINCQDMNGYTSLHHACLNGHSNIVRLLLSHNALLDVPDIRGSTPLFLA 89
Cdd:PHA02874 131 AIKKGDLESIKMLFEYGA-------------DVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNA 197

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475  90 AWAGHQDIVKMLLMHSP-------TGANP---------------------NAQTIENETPLHSGAQHGHNA-VVAILLSY 140
Cdd:PHA02874 198 AEYGDYACIKLLIDHGNhimnkckNGFTPlhnaiihnrsaiellinnasiNDQDIDGSTPLHHAINPPCDIdIIDILLYH 277

                        170       180       190
                 ....*....|....*....|....*....|..
gi 386766475 141 GADPAIRNNSFQTALDLAAQF-GRLQVVQTLL 171
Cdd:PHA02874 278 KADISIKDNKGENPIDTAFKYiNKDPVIKDII 309
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 43-113 1.90e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 58.76  E-value: 1.90e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386766475  43 NCQDMNGYTSLHHACLNGHSNIVRLLLSHNALLDVPDIRGSTPLFLAAWAGHQDIVKMLLMHSPTGANPNA 113
Cdd:PTZ00322 109 NCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELGA 179
PHA03095 PHA03095
ankyrin-like protein; Provisional
 96-278 4.00e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 57.34  E-value: 4.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475  96 DIVKMLLmhsPTGANPNAQTIENETPLHsgaQHGHNA------VVAILLSYGADPAIRNNSFQTALDLAAQFG-RLQVVQ 168
Cdd:PHA03095  28 EEVRRLL---AAGADVNFRGEYGKTPLH---LYLHYSsekvkdIVRLLLEAGADVNAPERCGFTPLHLYLYNAtTLDVIK 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475 169 TLLRVYPDLilpykrleddNEellgcmpiKHIFTHTCLH--LASRNGHKKVVETLLAAGVDVNILTNAG-SALHeaALCG 245
Cdd:PHA03095 102 LLIKAGADV----------NA--------KDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGmTPLA--VLLK 161

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 386766475 246 KKSVVV----TLLKAGIYVHATDGNGRTALDILSDYP 278
Cdd:PHA03095 162 SRNANVellrLLIDAGADVYAVDDRFRSLLHHHLQSF 198
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 108-172 6.09e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 57.22  E-value: 6.09e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386766475 108 GANPNAQTIENETPLHSGAQHGHNAVVAILLSYGADPAIRNNSFQTALDLAAQFGRLQVVQTLLR 172
Cdd:PTZ00322 105 GADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 49-172 1.00e-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: 56.56  E-value: 1.00e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475  49 GYTSLHHACLNGHSNIVRLLLSHNAllDVPDIR----------------GSTPLFLAAWAGHQDIVKMLLMHsptGANPN 112
Cdd:cd22192   89 GETALHIAVVNQNLNLVRELIARGA--DVVSPRatgtffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEH---GADIR 163

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386766475 113 AQTIENETPLHSGAQHGhNAVVA-----ILLSYGA--DPA----IRNNSFQTALDLAAQFGRLQVVQTLLR 172
Cdd:cd22192  164 AQDSLGNTVLHILVLQP-NKTFAcqmydLILSYDKedDLQpldlVPNNQGLTPFKLAAKEGNIVMFQHLVQ 233
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 42-177 1.05e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 56.43  E-value: 1.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475  42 INCQDMNGYTSLHHACLNGHSNIVRLLLSHNALLDVPDIRGSTPLFLA-AWAGHQDIVKMLLMHsptGANPNAQ-TIENE 119
Cdd:PHA02878 194 VNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEH---GVDVNAKsYILGL 270

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386766475 120 TPLHSGAQHghNAVVAILLSYGADPAIRNNSFQTALDLAA------QFGRLQVVQTLL--RVYPDL 177
Cdd:PHA02878 271 TALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSAVkqylciNIGRILISNICLlkRIKPDI 334
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 3-228 2.53e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 55.26  E-value: 2.53e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475   3 KDQHLLEA--SRAGDIKTVDK-LLEHSSKRHGplssfrrspsINCQDMNGYTSLHHACLNGHSNIVRLLLSHNALL---- 75
Cdd:PLN03192 475 KTSTLIEAmqTRQEDNVVILKnFLQHHKELHD----------LNVGDLLGDNGGEHDDPNMASNLLTVASTGNAALleel 544

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475  76 -------DVPDIRGSTPLFLAAWAGHQDIVKMLLMHsptGANPNAQTIENETPLHSGAQHGHNAVVAILLSYGA--DPAI 146
Cdd:PLN03192 545 lkakldpDIGDSKGRTPLHIAASKGYEDCVLVLLKH---ACNVHIRDANGNTALWNAISAKHHKIFRILYHFASisDPHA 621

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475 147 RNNsfqtALDLAAQFGRLQVVQTLLRvypdlilpyKRLEDDNEELLGCmpikhifthTCLHLASRNGHKKVVETLLAAGV 226
Cdd:PLN03192 622 AGD----LLCTAAKRNDLTAMKELLK---------QGLNVDSEDHQGA---------TALQVAMAEDHVDMVRLLIMNGA 679


                 ..
gi 386766475 227 DV 228
Cdd:PLN03192 680 DV 681
Ank_4 pfam13637
Ankyrin repeats (many copies);
120-171 2.58e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.58  E-value: 2.58e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 386766475  120 TPLHSGAQHGHNAVVAILLSYGADPAIRNNSFQTALDLAAQFGRLQVVQTLL 171
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
49-102 2.84e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.58  E-value: 2.84e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 386766475   49 GYTSLHHACLNGHSNIVRLLLSHNALLDVPDIRGSTPLFLAAWAGHQDIVKMLL 102
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
37-89 3.26e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 49.27  E-value: 3.26e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 386766475   37 RRSPSINCQDMNGYTSLHHACLNGHSNIVRLLLSHNALLDVPDIRGSTPLFLA 89
Cdd:pfam13857   4 HGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 15-118 5.33e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 53.90  E-value: 5.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475  15 DIKT-VDKLLEHSSKrhgplssfrrspsINCQDMNGYTSLHHACLNGHSNIVRLLLSHNALLDVPDIRGSTPLFLAAWAG 93
Cdd:PHA03100 170 NAKNrVNYLLSYGVP-------------INIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNN 236

                         90       100
                 ....*....|....*....|....*
gi 386766475  94 HQDIVKMLLMHsptgaNPNAQTIEN 118
Cdd:PHA03100 237 NKEIFKLLLNN-----GPSIKTIIE 256
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 112-286 1.42e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 52.66  E-value: 1.42e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475 112 NAQTIENETPLHSGAQHGHNAVVAILLSYGADPAIRNNSFQTALDLAAQFGRLQVVQTLLRVYPDL-ILPYKRLEDDN-E 189
Cdd:PHA02874  29 NISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTsILPIPCIEKDMiK 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475 190 ELLGC---MPIKHIFTHTCLHLASRNGHKKVVETLLAAGVDVNILTNAGS-ALHEAALCGKKSVVVTLLKAGIYVHATDG 265
Cdd:PHA02874 109 TILDCgidVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCyPIHIAIKHNFFDIIKLLLEKGAYANVKDN 188

                        170       180
                 ....*....|....*....|.
gi 386766475 266 NGRTALDILSDYPPHVTYDIV 286
Cdd:PHA02874 189 NGESPLHNAAEYGDYACIKLL 209
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 36-229 1.71e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 52.76  E-value: 1.71e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475  36 FRRSPSINCQDMNGYTSLHHACLNGH-SNIVRLLLSHNALLDVPDIRGSTPLFLAAWAG-HQDIVKMLLmhsPTGANPNA 113
Cdd:PHA02876 294 LERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITLL---ELGANVNA 370

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475 114 QTIENETPLHSGAQHGHNAVVAILLSYGADPAIRNNSFQTALDLAaqfgrlqvvqtLLRVYPdlILPYKRLEDDNEELLG 193
Cdd:PHA02876 371 RDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFA-----------LCGTNP--YMSVKTLIDRGANVNS 437

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 386766475 194 cmpiKHIFTHTCLHLASRNGHK-KVVETLLAAGVDVN 229
Cdd:PHA02876 438 ----KNKDLSTPLHYACKKNCKlDVIEMLLDNGADVN 470
PHA03095 PHA03095
ankyrin-like protein; Provisional
 63-277 1.76e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 52.33  E-value: 1.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475  63 NIVRLLLSHNALLDVPDIRGSTPLFLAAWAGHQ---DIVKMLLmhsPTGANPNAQTIENETPLHSGAQHGHNA-VVAILL 138
Cdd:PHA03095  28 EEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEkvkDIVRLLL---EAGADVNAPERCGFTPLHLYLYNATTLdVIKLLI 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475 139 SYGADPAIRNNSFQTALD--LAAQFGRLQVVQTLLRVYPDLilpykrledDNEELLGCMPIkHIFthtclhLASRNGHKK 216
Cdd:PHA03095 105 KAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADV---------NALDLYGMTPL-AVL------LKSRNANVE 168

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386766475 217 VVETLLAAGVDVNILTNAG-SALHEAALCGKKS--VVVTLLKAGIYVHATDGNGRTALDILSDY 277
Cdd:PHA03095 169 LLRLLIDAGADVYAVDDRFrSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTPLHSMATG 232
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 7-172 2.04e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 52.30  E-value: 2.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475   7 LLEASRAGDIKTVDKLLEhsskrhgpLSSFrrspsinCQDM---NGYTSLHHACLNGHSNIVRLLLSHNALLDVPDIRGS 83
Cdd:PHA02875  72 LHDAVEEGDVKAVEELLD--------LGKF-------ADDVfykDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKF 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475  84 TPLFLAAWAGHQDIVKMLLMHSptgANPNAQTIENETPLHSGAQHGHNAVVAILLSYGADPA-IRNNSFQTALDLAAQFG 162
Cdd:PHA02875 137 SPLHLAVMMGDIKGIELLIDHK---ACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDyFGKNGCVAALCYAIENN 213

                        170
                 ....*....|
gi 386766475 163 RLQVVQTLLR 172
Cdd:PHA02875 214 KIDIVRLFIK 223
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 42-143 3.34e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 51.42  E-value: 3.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475  42 INCQDMN-GYTSLHHACLNGHSNIVRLLLSHNALLDVPDIRGSTPLFLAAWAGHQDIVKMLLMHsptGANPNAQTIENET 120
Cdd:PHA02878 160 INMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLEN---GASTDARDKCGNT 236

                         90       100
                 ....*....|....*....|....
gi 386766475 121 PLHSGAQHGHN-AVVAILLSYGAD 143
Cdd:PHA02878 237 PLHISVGYCKDyDILKLLLEHGVD 260
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 118-274 3.85e-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: 51.55  E-value: 3.85e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475 118 NETPLHSGAQHghNAVVAI---LLSYGADPAIRNNSFQTALDLAAQFGRLQVVQTLLRVYPDLIlpykrleddNEELLGC 194
Cdd:cd22192   17 SESPLLLAAKE--NDVQAIkklLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELV---------NEPMTSD 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475 195 MpikhIFTHTCLHLASRNGHKKVVETLLAAGVDVNILTNAGSA---------------LHEAALCGKKSVVVTLLKAGIY 259
Cdd:cd22192   86 L----YQGETALHIAVVNQNLNLVRELIARGADVVSPRATGTFfrpgpknliyygehpLSFAACVGNEEIVRLLIEHGAD 161

                        170
                 ....*....|....*
gi 386766475 260 VHATDGNGRTALDIL 274
Cdd:cd22192  162 IRAQDSLGNTVLHIL 176
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 94-264 9.14e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 50.45  E-value: 9.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475  94 HQDIVKMLLMHSPTGANPNAQTIENETPLHSGAQHGHNAVVAILLSYGAD------------------------------ 143
Cdd:PHA02876 154 QQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADvniialddlsvlecavdsknidtikaiidn 233

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475 144 ------------PAIRNNSFQTAL------------DLAAQFGRLQVVQT--LLRVYPDLIlpyKRLEDDNEellgcmpi 197
Cdd:PHA02876 234 rsninkndlsllKAIRNEDLETSLllydagfsvnsiDDCKNTPLHHASQApsLSRLVPKLL---ERGADVNA-------- 302

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475 198 KHIFTHTCLHLASRNGH-KKVVETLLAAGVDVNILTNA-GSALHEAALCGK-KSVVVTLLKAGIYVHATD 264
Cdd:PHA02876 303 KNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLyITPLHQASTLDRnKDIVITLLELGANVNARD 372
Ank_2 pfam12796
Ankyrin repeats (3 copies);
7-79 1.01e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 46.26  E-value: 1.01e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386766475    7 LLEASRAGDIKTVDKLLEHsskrhgplssfrrsPSINCQDmNGYTSLHHACLNGHSNIVRLLLSHNALLDVPD 79
Cdd:pfam12796  34 LHLAAKNGHLEIVKLLLEH--------------ADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
Ank_4 pfam13637
Ankyrin repeats (many copies);
82-138 1.52e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.57  E-value: 1.52e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 386766475   82 GSTPLFLAAWAGHQDIVKMLLMHsptGANPNAQTIENETPLHSGAQHGHNAVVAILL 138
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEK---GADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
204-254 1.41e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.88  E-value: 1.41e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 386766475  204 TCLHLASRNGHKKVVETLLAAGVDVNILTNAG-SALHEAALCGKKSVVVTLL 254
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGeTALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 79-271 1.60e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 46.60  E-value: 1.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475  79 DIRGSTPLFLAAWAGH-QDIVKMLLMHsptGANPNAQTIENETPLHSGAQHGHNAV-VAILLSYGADPAIRNNSFQTALD 156
Cdd:PHA02876 270 DDCKNTPLHHASQAPSlSRLVPKLLER---GADVNAKNIKGETPLYLMAKNGYDTEnIRTLIMLGADVNAADRLYITPLH 346

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475 157 LAAQFGRLQ-VVQTLLrvypdlilpykrleddneELLGCMPIKHIFTHTCLHLASRNGHKKVVETLLAAGVDVNILTNA- 234
Cdd:PHA02876 347 QASTLDRNKdIVITLL------------------ELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKi 408

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 386766475 235 GSALHeAALCGKK--SVVVTLLKAGIYVHATDGNGRTAL 271
Cdd:PHA02876 409 GTALH-FALCGTNpyMSVKTLIDRGANVNSKNKDLSTPL 446
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 22-172 2.01e-05

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 46.03  E-value: 2.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475  22 LLEHSSKRHGPLSSFRRSPSInCQDMNGYTSLHHACLNGHSNIVRLLLSHNAllDV--------------PDIR-GSTPL 86
Cdd:cd21882   47 LLLEAAPDSGNPKELVNAPCT-DEFYQGQTALHIAIENRNLNLVRLLVENGA--DVsaratgrffrkspgNLFYfGELPL 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475  87 FLAAWAGHQDIVKMLLMHSPTGANPNAQTIENETPLHSGAQHGHNAVVA---------ILLSYGA--DPA-----IRNNS 150
Cdd:cd21882  124 SLAACTNQEEIVRLLLENGAQPAALEAQDSLGNTVLHALVLQADNTPENsafvcqmynLLLSYGAhlDPTqqleeIPNHQ 203

                        170       180
                 ....*....|....*....|..
gi 386766475 151 FQTALDLAAQFGRLQVVQTLLR 172
Cdd:cd21882  204 GLTPLKLAAVEGKIVMFQHILQ 225
Ank_5 pfam13857
Ankyrin repeats (many copies);
103-158 2.17e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.56  E-value: 2.17e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 386766475  103 MHSPTGANPNAQTIENETPLHSGAQHGHNAVVAILLSYGADPAIRNNSFQTALDLA 158
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 53-140 2.24e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.04  E-value: 2.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475  53 LHHACLNGHSNIVRLLLSHNALLDVPDIRGSTPLFLAAWAGHQDIVKMLLmhsPTGANPNAQTIENETPLHSGAQHGHNA 132
Cdd:PTZ00322  86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLL---EFGADPTLLDKDGKTPLELAEENGFRE 162


                 ....*...
gi 386766475 133 VVAILLSY 140
Cdd:PTZ00322 163 VVQLLSRH 170
Ank_5 pfam13857
Ankyrin repeats (many copies);
68-123 2.37e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.18  E-value: 2.37e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 386766475   68 LLSH-NALLDVPDIRGSTPLFLAAWAGHQDIVKMLLMHsptGANPNAQTIENETPLH 123
Cdd:pfam13857   1 LLEHgPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAY---GVDLNLKDEEGLTALD 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
6-69 3.13e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.11  E-value: 3.13e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386766475    6 HLLEASRAGDIKTVDKLLEHSskrhgplssfrrsPSINCQDMNGYTSLHHACLNGHSNIVRLLL 69
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKG-------------ADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 93-277 5.00e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 44.60  E-value: 5.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475  93 GHQDIVKMLLmhsPTGANPNAQTIENETPLHSGAQHGHNAVVAILLSYGADPAIRNNSFQTALDLAAQFGRLQVVQTLLR 172
Cdd:PHA02875  13 GELDIARRLL---DIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLD 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475 173 V--YPDLILpYKRleddneellGCMPikhifthtcLHLASRNGHKKVVETLLAAGVDVNIL-TNAGSALHEAALCGKKSV 249
Cdd:PHA02875  90 LgkFADDVF-YKD---------GMTP---------LHLATILKKLDIMKLLIARGADPDIPnTDKFSPLHLAVMMGDIKG 150

                        170       180
                 ....*....|....*....|....*...
gi 386766475 250 VVTLLKAGIYVHATDGNGRTALDILSDY 277
Cdd:PHA02875 151 IELLIDHKACLDIEDCCGCTPLIIAMAK 178
PHA03095 PHA03095
ankyrin-like protein; Provisional
 6-158 1.10e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 43.86  E-value: 1.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475   6 HLLEASRAGDIKTVDKLLEHSSKRHGplssfrrspsincQDMNGYTSLHHACLNGHSN--IVRLLLSHNALLDVPDIRGS 83
Cdd:PHA03095 157 AVLLKSRNANVELLRLLIDAGADVYA-------------VDDRFRSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGN 223

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386766475  84 TPLFLAAWAG---HQDIVKMLLmhspTGANPNAQTIENETPLHSGAQHGHNAVVAILLSYGADPAIRNNSFQTALDLA 158
Cdd:PHA03095 224 TPLHSMATGSsckRSLVLPLLI----AGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLM 297
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 48-77 1.62e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 38.34  E-value: 1.62e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 386766475    48 NGYTSLHHACLNGHSNIVRLLLSHNALLDV 77
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 120-264 1.92e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 42.73  E-value: 1.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475 120 TPLHSGAQHGHNAVVAILLSYGADPAIRNNSFQTALDLAAQfgrLQVVQTLLRVYPDLILPY---KRLEDDNeellGCMP 196
Cdd:PHA03100  37 LPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSN---IKYNLTDVKEIVKLLLEYganVNAPDNN----GITP 109

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386766475 197 IkHIFTHTCLhlasrnGHKKVVETLLAAGVDVNILTNAG-SALHEAALCG--KKSVVVTLLKAGIYVHATD 264
Cdd:PHA03100 110 L-LYAISKKS------NSYSIVEYLLDNGANVNIKNSDGeNLLHLYLESNkiDLKILKLLIDKGVDINAKN 173
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 126-222 2.05e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 42.96  E-value: 2.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475 126 AQHGHNAVVAILLSYGADPAIRNNSFQTALDLAAQFGRLQVVQTLLRVYPDLILPYKrleDDNeellgcmpikhifthTC 205
Cdd:PTZ00322  90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDK---DGK---------------TP 151

                         90
                 ....*....|....*..
gi 386766475 206 LHLASRNGHKKVVETLL 222
Cdd:PTZ00322 152 LELAEENGFREVVQLLS 168
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 45-171 2.34e-04

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: 42.82  E-value: 2.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475  45 QDMNGYTSLHHACLNGHSNIVRLLLSHNALLDV--------PDIR------GSTPLFLAAWAGHQDIVKMLLMHSPTgaN 110
Cdd:cd22194  137 EAYEGQTALNIAIERRQGDIVKLLIAKGADVNAhakgvffnPKYKhegfyfGETPLALAACTNQPEIVQLLMEKEST--D 214

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386766475 111 PNAQTIENETPLH-----SGAQHGHNAVV-----AILLSYGAD--PAIRNNSFQTALDLAAQFGRLQVVQTLL 171
Cdd:cd22194  215 ITSQDSRGNTVLHalvtvAEDSKTQNDFVkrmydMILLKSENKnlETIRNNEGLTPLQLAAKMGKAEILKYIL 287
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 203-230 2.50e-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: 37.95  E-value: 2.50e-04
                           10        20
                   ....*....|....*....|....*...
gi 386766475   203 HTCLHLASRNGHKKVVETLLAAGVDVNI 230
Cdd:smart00248   3 RTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02946 PHA02946
ankyin-like protein; Provisional
 102-274 3.23e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 42.35  E-value: 3.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475 102 LMHSptGANPNAQTIENETPLHSGAQHGHNAVVAILLSYGADPAIRNNSFQTALDLAAQFGRlQVVQTLlrvypDLILPY 181
Cdd:PHA02946  58 LLHR--GYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDD-EVIERI-----NLLVQY 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475 182 KRLEDDNEELLGCMPIkhifthtclhLASRNGHKKVVETLLAAGVDVNILTNAG-SALHEAALCG--KKSVVVTLLKAGI 258
Cdd:PHA02946 130 GAKINNSVDEEGCGPL----------LACTDPSERVFKKIMSIGFEARIVDKFGkNHIHRHLMSDnpKASTISWMMKLGI 199

                        170
                 ....*....|....*.
gi 386766475 259 YVHATDGNGRTALDIL 274
Cdd:PHA02946 200 SPSKPDHDGNTPLHIV 215
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 48-77 3.36e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.24  E-value: 3.36e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 386766475   48 NGYTSLHHACLNGHSNIVRLLLSHNALLDV 77
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 213-271 4.01e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 42.16  E-value: 4.01e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475 213 GHKKVVETLLAAGVDVNILTNAG-SALHEAALCGKKSVVVTLLKAGIYVHATDGNGRTAL 271
Cdd:PLN03192 536 GNAALLEELLKAKLDPDIGDSKGrTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTAL 595
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 203-233 4.54e-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: 4.54e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 386766475  203 HTCLHLAS-RNGHKKVVETLLAAGVDVNILTN 233
Cdd:pfam00023   3 NTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 204-286 4.80e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 41.79  E-value: 4.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475 204 TCLHLASRNGHKKVVETLLAAGVDVNILTNAG-SALHEAALCGKKSVVVTLLKAGIYVHATDGNGRTALDILSDYPphVT 282
Cdd:PHA02878 170 TALHYATENKDQRLTELLLSYGANVNIPDKTNnSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYC--KD 247


                 ....
gi 386766475 283 YDIV 286
Cdd:PHA02878 248 YDIL 251
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 81-115 5.53e-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: 36.88  E-value: 5.53e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 386766475   81 RGSTPLFLAAW-AGHQDIVKMLLMHsptGANPNAQT 115
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSK---GADVNARD 33
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 48-79 1.60e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 35.73  E-value: 1.60e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 386766475   48 NGYTSLHHACL-NGHSNIVRLLLSHNALLDVPD 79
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 81-113 3.09e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.87  E-value: 3.09e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 386766475    81 RGSTPLFLAAWAGHQDIVKMLLMHsptGANPNA 113
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDK---GADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 204-230 4.50e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 34.16  E-value: 4.50e-03
                          10        20
                  ....*....|....*....|....*..
gi 386766475  204 TCLHLASRNGHKKVVETLLAAGVDVNI 230
Cdd:pfam13606   4 TPLHLAARNGRLEIVKLLLENGADINA 30
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 82-172 4.84e-03

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


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 38.62  E-value: 4.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766475  82 GSTPLFLAAWAGHQDIVKMLLMHSPTGANPNAQTIENETPLHSGAQHGHNA---------VVAILLSYGAD-------PA 145
Cdd:cd22193  123 GELPLSLAACTNQPDIVQYLLENEHQPADIEAQDSRGNTVLHALVTVADNTkentkfvtrMYDMILIRGAKlcptvelEE 202

                         90       100
                 ....*....|....*....|....*..
gi 386766475 146 IRNNSFQTALDLAAQFGRLQVVQTLLR 172
Cdd:cd22193  203 IRNNDGLTPLQLAAKMGKIEILKYILQ 229
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 119-149 5.64e-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: 34.19  E-value: 5.64e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 386766475  119 ETPLHSGA-QHGHNAVVAILLSYGADPAIRNN 149
Cdd:pfam00023   3 NTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 84-158 7.01e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 37.66  E-value: 7.01e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386766475  84 TPLFLAAWAGHQDIVKMLLMHsptGANPNaqTIENE---TPLHSGAQHGHNAVVAILLSYGADPAIRNNSFQTALDLA 158
Cdd:PHA02884  72 NPLIYAIDCDNDDAAKLLIRY---GADVN--RYAEEakiTPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPIELA 144
PHA02946 PHA02946
ankyin-like protein; Provisional
 79-142 9.80e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 37.73  E-value: 9.80e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386766475  79 DIRGSTPLFLAAWAGHQDIVKMLLMHsptGANPNAQTIENETPLH--SGAQHGHNAVVAILLSYGA 142
Cdd:PHA02946  69 DDDGNYPLHIASKINNNRIVAMLLTH---GADPNACDKQHKTPLYylSGTDDEVIERINLLVQYGA 131
 
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