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Conserved domains on  [gi|1907131500|ref|XP_036017280|]
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KN motif and ankyrin repeat domain-containing protein 1 isoform X2 [Mus musculus]

Protein Classification

KN_motif domain-containing protein( domain architecture ID 13778393)

KN_motif domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1148-1337 3.50e-34

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 133.54  E-value: 3.50e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907131500 1148 IAAFEAVSPDVLRYII------NMADGNGNTALHYSVSHSNFQIVKLLLDADVcNVDHQNKAGYTPIMLAALAaveaeKD 1221
Cdd:COG0666     92 HAAARNGDLEIVKLLLeagadvNARDKDGETPLHLAAYNGNLEIVKLLLEAGA-DVNAQDNDGNTPLHLAAAN-----GN 165

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907131500 1222 MQVVEELFSCG-DVNAKaSQAGQTALMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQpGC 1300
Cdd:COG0666    166 LEIVKLLLEAGaDVNAR-DNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA-GA 243

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1907131500 1301 NGHLEDNDGSTALSIALEAGHKDIAVLLYAHLNFSKA 1337
Cdd:COG0666    244 DLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAA 280
KN_motif pfam12075
KN motif; This small motif is found at the N-terminus of Kank proteins and has been called the ...
 30-68 6.22e-18

KN motif; This small motif is found at the N-terminus of Kank proteins and has been called the KN (for Kank N-terminal) motif. This protein is found in eukaryotes. Proteins in this family are typically between 413 to 1202 amino acids in length. This protein is found associated with pfam00023. This protein has two conserved sequence motifs: TPYG and LDLDF. Kank1 was obtained by positional cloning of a tumor suppressor gene in renal cell carcinoma, while the other members were found by homology search. The family is involved in the regulation of actin polymerization and cell motility through signaling pathways containing PI3K/Akt and/or unidentified modulators/effectors.


:

Pssm-ID: 432311  Cd Length: 39  Bit Score: 78.16  E-value: 6.22e-18
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1907131500   30 PYFVETPYGFQLDLDFVKYVDDIQKGNTIKKLNIQKRRK 68
Cdd:pfam12075    1 PYSVETPYGFHLDLDFLKYVEDIESGQTIRRARVQRRPR 39
YhaN super family cl34808
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
269-500 2.22e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


The actual alignment was detected with superfamily member COG4717:

Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 2.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907131500  269 IALKRLKELEEQVRTIPVLQVKISVLQEEKRQLASQLKSQRASSQNEACGVRKRSYSAGNASQLELLARARRgggELyid 348
Cdd:COG4717     68 LNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEA---EL--- 141

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907131500  349 yeEEEMESVEQSTQRIQEFRQLTADMQALERKIQDSSCEVASELRENGQcpsrecksvavgsdenmndvvVYHRDLRPCK 428
Cdd:COG4717    142 --AELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSL---------------------ATEEELQDLA 198

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907131500  429 DTavgtvtetrnvgisvteamlgvITEADKEIELQQQTIEALKEKIYRLEVQLKETTHDREMTKLKQELQAA 500
Cdd:COG4717    199 EE----------------------LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEA 248
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1148-1337 3.50e-34

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 133.54  E-value: 3.50e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907131500 1148 IAAFEAVSPDVLRYII------NMADGNGNTALHYSVSHSNFQIVKLLLDADVcNVDHQNKAGYTPIMLAALAaveaeKD 1221
Cdd:COG0666     92 HAAARNGDLEIVKLLLeagadvNARDKDGETPLHLAAYNGNLEIVKLLLEAGA-DVNAQDNDGNTPLHLAAAN-----GN 165

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907131500 1222 MQVVEELFSCG-DVNAKaSQAGQTALMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQpGC 1300
Cdd:COG0666    166 LEIVKLLLEAGaDVNAR-DNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA-GA 243

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1907131500 1301 NGHLEDNDGSTALSIALEAGHKDIAVLLYAHLNFSKA 1337
Cdd:COG0666    244 DLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAA 280
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1246-1331 1.42e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 93.26  E-value: 1.42e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907131500 1246 LMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQPGCNghlEDNDGSTALSIALEAGHKDIA 1325
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN---LKDNGRTALHYAARSGHLEIV 77


                   ....*.
gi 1907131500 1326 VLLYAH 1331
Cdd:pfam12796   78 KLLLEK 83
KN_motif pfam12075
KN motif; This small motif is found at the N-terminus of Kank proteins and has been called the ...
 30-68 6.22e-18

KN motif; This small motif is found at the N-terminus of Kank proteins and has been called the KN (for Kank N-terminal) motif. This protein is found in eukaryotes. Proteins in this family are typically between 413 to 1202 amino acids in length. This protein is found associated with pfam00023. This protein has two conserved sequence motifs: TPYG and LDLDF. Kank1 was obtained by positional cloning of a tumor suppressor gene in renal cell carcinoma, while the other members were found by homology search. The family is involved in the regulation of actin polymerization and cell motility through signaling pathways containing PI3K/Akt and/or unidentified modulators/effectors.


Pssm-ID: 432311  Cd Length: 39  Bit Score: 78.16  E-value: 6.22e-18
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1907131500   30 PYFVETPYGFQLDLDFVKYVDDIQKGNTIKKLNIQKRRK 68
Cdd:pfam12075    1 PYSVETPYGFHLDLDFLKYVEDIESGQTIRRARVQRRPR 39
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 1163-1333 1.31e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 71.62  E-value: 1.31e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907131500 1163 INMADGNGNTALHYSVSHS--NFQIVKLLLDADvCNVDHQNKAGYTPImlaALAAVEAEKDMQVVEELFSCG-DVNAKas 1239
Cdd:PHA03100    99 VNAPDNNGITPLLYAISKKsnSYSIVEYLLDNG-ANVNIKNSDGENLL---HLYLESNKIDLKILKLLIDKGvDINAK-- 172

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907131500 1240 qagqtalmlavshgriDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQpGCNGHLEDNDGSTALSIALEA 1319
Cdd:PHA03100   173 ----------------NRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDL-GANPNLVNKYGDTPLHIAILN 235

                          170
                   ....*....|....*
gi 1907131500 1320 GHKDI-AVLLYAHLN 1333
Cdd:PHA03100   236 NNKEIfKLLLNNGPS 250
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 1170-1329 5.30e-06

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: 50.78  E-value: 5.30e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907131500 1170 GNTALHYSVSHSNFQIVKLLLDADvcnvdhqnkagytPIMLaalaaveaekDMQVVEELFscgdvnakasqAGQTALMLA 1249
Cdd:cd22192     51 GETALHVAALYDNLEAAVVLMEAA-------------PELV----------NEPMTSDLY-----------QGETALHIA 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907131500 1250 VSHGRIDMVKGLLACGADVNIQDDEGS------TALMCASEH--------GHVEIVKLLLaQPGCNGHLEDNDGSTALSI 1315
Cdd:cd22192     97 VVNQNLNLVRELIARGADVVSPRATGTffrpgpKNLIYYGEHplsfaacvGNEEIVRLLI-EHGADIRAQDSLGNTVLHI 175

                          170
                   ....*....|....
gi 1907131500 1316 ALEAGHKDIAVLLY 1329
Cdd:cd22192    176 LVLQPNKTFACQMY 189
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 1242-1270 4.55e-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: 41.42  E-value: 4.55e-05
                            10        20
                    ....*....|....*....|....*....
gi 1907131500  1242 GQTALMLAVSHGRIDMVKGLLACGADVNI 1270
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
269-500 2.22e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 2.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907131500  269 IALKRLKELEEQVRTIPVLQVKISVLQEEKRQLASQLKSQRASSQNEACGVRKRSYSAGNASQLELLARARRgggELyid 348
Cdd:COG4717     68 LNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEA---EL--- 141

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907131500  349 yeEEEMESVEQSTQRIQEFRQLTADMQALERKIQDSSCEVASELRENGQcpsrecksvavgsdenmndvvVYHRDLRPCK 428
Cdd:COG4717    142 --AELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSL---------------------ATEEELQDLA 198

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907131500  429 DTavgtvtetrnvgisvteamlgvITEADKEIELQQQTIEALKEKIYRLEVQLKETTHDREMTKLKQELQAA 500
Cdd:COG4717    199 EE----------------------LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEA 248
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1148-1337 3.50e-34

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 133.54  E-value: 3.50e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907131500 1148 IAAFEAVSPDVLRYII------NMADGNGNTALHYSVSHSNFQIVKLLLDADVcNVDHQNKAGYTPIMLAALAaveaeKD 1221
Cdd:COG0666     92 HAAARNGDLEIVKLLLeagadvNARDKDGETPLHLAAYNGNLEIVKLLLEAGA-DVNAQDNDGNTPLHLAAAN-----GN 165

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907131500 1222 MQVVEELFSCG-DVNAKaSQAGQTALMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQpGC 1300
Cdd:COG0666    166 LEIVKLLLEAGaDVNAR-DNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA-GA 243

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1907131500 1301 NGHLEDNDGSTALSIALEAGHKDIAVLLYAHLNFSKA 1337
Cdd:COG0666    244 DLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAA 280
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1148-1331 1.00e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 132.00  E-value: 1.00e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907131500 1148 IAAFEAVSPDVLRYIINMADGNGNTALHYSVSHSNFQIVKLLLDADVcNVDHQNKAGYTPIMLAALAaveaeKDMQVVEE 1227
Cdd:COG0666     32 LLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGA-DINAKDDGGNTLLHAAARN-----GDLEIVKL 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907131500 1228 LFSCG-DVNAKASQaGQTALMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQpGCNGHLED 1306
Cdd:COG0666    106 LLEAGaDVNARDKD-GETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEA-GADVNARD 183

                          170       180
                   ....*....|....*....|....*
gi 1907131500 1307 NDGSTALSIALEAGHKDIAVLLYAH 1331
Cdd:COG0666    184 NDGETPLHLAAENGHLEIVKLLLEA 208
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1157-1331 6.51e-25

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 106.58  E-value: 6.51e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907131500 1157 DVLRYIINMADGNGNTALHYSVSHSNFQIVKLLLDADVCNVDHQNKAGYTPIMLAALAAveaeKDMQVVEELFSCGDVNA 1236
Cdd:COG0666      6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALA----GDLLVALLLLAAGADIN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907131500 1237 KASQAGQTALMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQpGCNGHLEDNDGSTALSIA 1316
Cdd:COG0666     82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA-GADVNAQDNDGNTPLHLA 160

                          170
                   ....*....|....*
gi 1907131500 1317 LEAGHKDIAVLLYAH 1331
Cdd:COG0666    161 AANGNLEIVKLLLEA 175
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1246-1331 1.42e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 93.26  E-value: 1.42e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907131500 1246 LMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQPGCNghlEDNDGSTALSIALEAGHKDIA 1325
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN---LKDNGRTALHYAARSGHLEIV 77


                   ....*.
gi 1907131500 1326 VLLYAH 1331
Cdd:pfam12796   78 KLLLEK 83
KN_motif pfam12075
KN motif; This small motif is found at the N-terminus of Kank proteins and has been called the ...
 30-68 6.22e-18

KN motif; This small motif is found at the N-terminus of Kank proteins and has been called the KN (for Kank N-terminal) motif. This protein is found in eukaryotes. Proteins in this family are typically between 413 to 1202 amino acids in length. This protein is found associated with pfam00023. This protein has two conserved sequence motifs: TPYG and LDLDF. Kank1 was obtained by positional cloning of a tumor suppressor gene in renal cell carcinoma, while the other members were found by homology search. The family is involved in the regulation of actin polymerization and cell motility through signaling pathways containing PI3K/Akt and/or unidentified modulators/effectors.


Pssm-ID: 432311  Cd Length: 39  Bit Score: 78.16  E-value: 6.22e-18
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1907131500   30 PYFVETPYGFQLDLDFVKYVDDIQKGNTIKKLNIQKRRK 68
Cdd:pfam12075    1 PYSVETPYGFHLDLDFLKYVEDIESGQTIRRARVQRRPR 39
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1174-1272 8.71e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 74.00  E-value: 8.71e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907131500 1174 LHYSVSHSNFQIVKLLLDADvCNVDHQNKAGYTPIMLAALAaveaeKDMQVVEELFSCGDVNAKASqaGQTALMLAVSHG 1253
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENG-ADANLQDKNGRTALHLAAKN-----GHLEIVKLLLEHADVNLKDN--GRTALHYAARSG 72

                           90
                   ....*....|....*....
gi 1907131500 1254 RIDMVKGLLACGADVNIQD 1272
Cdd:pfam12796   73 HLEIVKLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 1163-1333 1.31e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 71.62  E-value: 1.31e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907131500 1163 INMADGNGNTALHYSVSHS--NFQIVKLLLDADvCNVDHQNKAGYTPImlaALAAVEAEKDMQVVEELFSCG-DVNAKas 1239
Cdd:PHA03100    99 VNAPDNNGITPLLYAISKKsnSYSIVEYLLDNG-ANVNIKNSDGENLL---HLYLESNKIDLKILKLLIDKGvDINAK-- 172

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907131500 1240 qagqtalmlavshgriDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQpGCNGHLEDNDGSTALSIALEA 1319
Cdd:PHA03100   173 ----------------NRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDL-GANPNLVNKYGDTPLHIAILN 235

                          170
                   ....*....|....*
gi 1907131500 1320 GHKDI-AVLLYAHLN 1333
Cdd:PHA03100   236 NNKEIfKLLLNNGPS 250
Ank_4 pfam13637
Ankyrin repeats (many copies);
1244-1295 1.87e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 60.37  E-value: 1.87e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907131500 1244 TALMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLL 1295
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 1146-1327 2.67e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 64.28  E-value: 2.67e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907131500 1146 DYIAAFEAVSPDVLRYIINM-ADGN-----GNTALHYSVSHSNFQ---IVKLLLDADVcNVDHQNKAGYTPIMLAALAAV 1216
Cdd:PHA03095    17 DYLLNASNVTVEEVRRLLAAgADVNfrgeyGKTPLHLYLHYSSEKvkdIVRLLLEAGA-DVNAPERCGFTPLHLYLYNAT 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907131500 1217 EAEkdmqVVEELFSCG-DVNAKaSQAGQTALMLAVSHGRID--MVKGLLACGADVNIQDDEGSTALMC--ASEHGHVEIV 1291
Cdd:PHA03095    96 TLD----VIKLLIKAGaDVNAK-DKVGRTPLHVYLSGFNINpkVIRLLLRKGADVNALDLYGMTPLAVllKSRNANVELL 170

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1907131500 1292 KLLLAQpGCNGHLEDNDGSTALSIALEAGHKDIAVL 1327
Cdd:PHA03095   171 RLLIDA-GADVYAVDDRFRSLLHHHLQSFKPRARIV 205
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 1220-1342 1.83e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 62.19  E-value: 1.83e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907131500 1220 KDMQVVEELFSCGDVNAKASQAGQtaLMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQpG 1299
Cdd:PLN03192   505 HDLNVGDLLGDNGGEHDDPNMASN--LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKH-A 581

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1907131500 1300 CNGHLEDNDGSTALSIALEAGHKDIAVLLYahlNFSKAQSPST 1342
Cdd:PLN03192   582 CNVHIRDANGNTALWNAISAKHHKIFRILY---HFASISDPHA 621
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 1220-1333 5.08e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 60.36  E-value: 5.08e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907131500 1220 KDMqvVEELFSCG-DVNAKASQAgQTALMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLaQP 1298
Cdd:PHA02874   104 KDM--IKTILDCGiDVNIKDAEL-KTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLL-EK 179

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1907131500 1299 GCNGHLEDNDGSTALSIALEAGHKDIAVLLYAHLN 1333
Cdd:PHA02874   180 GAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGN 214
Ank_5 pfam13857
Ankyrin repeats (many copies);
1261-1316 5.45e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 53.50  E-value: 5.45e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907131500 1261 LLACG-ADVNIQDDEGSTALMCASEHGHVEIVKLLLAqPGCNGHLEDNDGSTALSIA 1316
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLA-YGVDLNLKDEEGLTALDLA 56
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1279-1343 6.46e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 54.35  E-value: 6.46e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907131500 1279 LMCASEHGHVEIVKLLLaQPGCNGHLEDNDGSTALSIALEAGHKDIAVLLYAHLNFSKAQSPSTP 1343
Cdd:pfam12796    1 LHLAAKNGNLELVKLLL-ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGRTA 64
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 1157-1295 8.64e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 59.51  E-value: 8.64e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907131500 1157 DVLRYII------NMADGNGNTALHYSVSHSNFQIVKLLLDaDVCNVDHQNKAGYTPImlaaLAAVEAEKDMQVVEELFS 1230
Cdd:PHA02878   182 RLTELLLsyganvNIPDKTNNSPLHHAVKHYNKPIVHILLE-NGASTDARDKCGNTPL----HISVGYCKDYDILKLLLE 256

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907131500 1231 CG-DVNAKASQAGQTALMLAVSHGRIdmVKGLLACGADVNIQDDEGSTAL-MCASEHGHVEIVKLLL 1295
Cdd:PHA02878   257 HGvDVNAKSYILGLTALHSSIKSERK--LKLLLEYGADINSLNSYKLTPLsSAVKQYLCINIGRILI 321
Ank_5 pfam13857
Ankyrin repeats (many copies);
1233-1279 3.30e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.50  E-value: 3.30e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1907131500 1233 DVNAKaSQAGQTALMLAVSHGRIDMVKGLLACGADVNIQDDEGSTAL 1279
Cdd:pfam13857    8 DLNRL-DGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 1258-1331 3.52e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.90  E-value: 3.52e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907131500 1258 VKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLaQPGCNGHLEDNDGSTALSIALEAGHKDIAVLLYAH 1331
Cdd:PTZ00322    98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLL-EFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 1242-1328 5.30e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 54.49  E-value: 5.30e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907131500 1242 GQTALMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLL--------------------------- 1294
Cdd:PLN03192   558 GRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILyhfasisdphaagdllctaakrndlta 637

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1907131500 1295 ---LAQPGCNGHLEDNDGSTALSIALEAGHKDIAVLL 1328
Cdd:PLN03192   638 mkeLLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLL 674
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 1164-1295 3.40e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 51.79  E-value: 3.40e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907131500 1164 NMADGNGNTALHYSVSHSNFQIVKLLLDaDVCNVDHQNKAGYTPIMLAALAaveaeKDMQVVEELFSCgdvnAKAS--QA 1241
Cdd:PLN03192   552 DIGDSKGRTPLHIAASKGYEDCVLVLLK-HACNVHIRDANGNTALWNAISA-----KHHKIFRILYHF----ASISdpHA 621

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907131500 1242 GQTALMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLL 1295
Cdd:PLN03192   622 AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLI 675
Ank_4 pfam13637
Ankyrin repeats (many copies);
1275-1328 3.72e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.34  E-value: 3.72e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907131500 1275 GSTALMCASEHGHVEIVKLLLaQPGCNGHLEDNDGSTALSIALEAGHKDIAVLL 1328
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLL-EKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 1157-1297 3.72e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 51.15  E-value: 3.72e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907131500 1157 DVLRYIINMADGNGNTALHYSVSHSNFQIVKLLL----DADVCNVDHqnkagYTPImlaalAAVEAEKDMQVVEELF--- 1229
Cdd:PHA02875    89 DLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIargaDPDIPNTDK-----FSPL-----HLAVMMGDIKGIELLIdhk 158

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907131500 1230 SCGDVNakaSQAGQTALMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMC-ASEHGHVEIVKLLLAQ 1297
Cdd:PHA02875   159 ACLDIE---DCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCyAIENNKIDIVRLFIKR 224
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 1242-1273 4.73e-06

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: 44.59  E-value: 4.73e-06
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1907131500 1242 GQTALMLAVSH-GRIDMVKGLLACGADVNIQDD 1273
Cdd:pfam00023    2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 1170-1329 5.30e-06

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: 50.78  E-value: 5.30e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907131500 1170 GNTALHYSVSHSNFQIVKLLLDADvcnvdhqnkagytPIMLaalaaveaekDMQVVEELFscgdvnakasqAGQTALMLA 1249
Cdd:cd22192     51 GETALHVAALYDNLEAAVVLMEAA-------------PELV----------NEPMTSDLY-----------QGETALHIA 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907131500 1250 VSHGRIDMVKGLLACGADVNIQDDEGS------TALMCASEH--------GHVEIVKLLLaQPGCNGHLEDNDGSTALSI 1315
Cdd:cd22192     97 VVNQNLNLVRELIARGADVVSPRATGTffrpgpKNLIYYGEHplsfaacvGNEEIVRLLI-EHGADIRAQDSLGNTVLHI 175

                          170
                   ....*....|....
gi 1907131500 1316 ALEAGHKDIAVLLY 1329
Cdd:cd22192    176 LVLQPNKTFACQMY 189
Ank_4 pfam13637
Ankyrin repeats (many copies);
1157-1190 1.37e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.80  E-value: 1.37e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1907131500 1157 DVLRYI------INMADGNGNTALHYSVSHSNFQIVKLLL 1190
Cdd:pfam13637   15 ELLRLLlekgadINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 1163-1296 1.66e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 48.81  E-value: 1.66e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907131500 1163 INMADGNGNTALHYSVSHSNFQIVKLLLDaDVCNVDHQNKAGYTPImlaalaAVEAEKDMQVVEELFSCGDVNAKASQaG 1242
Cdd:PHA02874   183 ANVKDNNGESPLHNAAEYGDYACIKLLID-HGNHIMNKCKNGFTPL------HNAIIHNRSAIELLINNASINDQDID-G 254

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907131500 1243 QTALMLAVSHG-RIDMVKGLLACGADVNIQDDEGSTALMCASEH-GHVEIVKLLLA 1296
Cdd:PHA02874   255 STPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTAFKYiNKDPVIKDIIA 310
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 1242-1340 2.14e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.13  E-value: 2.14e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907131500 1242 GQTALMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQPGCNGHLEDNdgSTALSIALEAGH 1321
Cdd:PTZ00322   115 GRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELGAN--AKPDSFTGKPPS 192

                           90
                   ....*....|....*....
gi 1907131500 1322 KDIAVLLYAHLNFSKAQSP 1340
Cdd:PTZ00322   193 LEDSPISSHHPDFSAVPQP 211
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 1174-1328 2.68e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 48.45  E-value: 2.68e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907131500 1174 LHYSVSHSNFQIVKLLLDADVCNVDHQNKAGYTPImlaalAAVEAEKDMQVVEELFSCGDVNAKASQAGQTALMLAVSHG 1253
Cdd:PHA02875    72 LHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPL-----HLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMG 146

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907131500 1254 RIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQPGCNGHLEDNDGSTALSIALEAGHKDIAVLL 1328
Cdd:PHA02875   147 DIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLF 221
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 1163-1323 2.96e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 48.04  E-value: 2.96e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907131500 1163 INMADGNGNTALHYSVSHSNFQIVKLLLDADV-CNVDHQNkaGYTPImlaalAAVEAEKDMQVVEELFSCGDVNAKASQA 1241
Cdd:PHA02874   150 VNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAyANVKDNN--GESPL-----HNAAEYGDYACIKLLIDHGNHIMNKCKN 222

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907131500 1242 GQTALMLAVSHGRidMVKGLLACGADVNIQDDEGSTALMCASEHG-HVEIVKLLLAQPGcNGHLEDNDGSTALSIALEAG 1320
Cdd:PHA02874   223 GFTPLHNAIIHNR--SAIELLINNASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKA-DISIKDNKGENPIDTAFKYI 299


                   ...
gi 1907131500 1321 HKD 1323
Cdd:PHA02874   300 NKD 302
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 1172-1270 3.10e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 48.06  E-value: 3.10e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907131500 1172 TALHYSVSHSNFQIVKLLLDADVCnVDHQNKAGYTPIMLAALAaveaeKDMQVVEELFSCG-DVNAKASQAGQTALMLAV 1250
Cdd:PHA02875   137 SPLHLAVMMGDIKGIELLIDHKAC-LDIEDCCGCTPLIIAMAK-----GDIAICKMLLDSGaNIDYFGKNGCVAALCYAI 210

                           90       100
                   ....*....|....*....|
gi 1907131500 1251 SHGRIDMVKGLLACGADVNI 1270
Cdd:PHA02875   211 ENNKIDIVRLFIKRGADCNI 230
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 1242-1270 4.55e-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: 41.42  E-value: 4.55e-05
                            10        20
                    ....*....|....*....|....*....
gi 1907131500  1242 GQTALMLAVSHGRIDMVKGLLACGADVNI 1270
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA03095 PHA03095
ankyrin-like protein; Provisional
 1154-1297 4.75e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 47.71  E-value: 4.75e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907131500 1154 VSPDVLRYIINM------ADGNGNTALHY--SVSHSNFQIVKLLLDADvCNVDHQNKAGYTPImlAALAAVEAEKDMQVV 1225
Cdd:PHA03095   165 ANVELLRLLIDAgadvyaVDDRFRSLLHHhlQSFKPRARIVRELIRAG-CDPAATDMLGNTPL--HSMATGSSCKRSLVL 241

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907131500 1226 EELFSCGDVNAKaSQAGQTALMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQ 1297
Cdd:PHA03095   242 PLLIAGISINAR-NRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAK 312
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 1242-1270 2.05e-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: 39.55  E-value: 2.05e-04
                           10        20
                   ....*....|....*....|....*....
gi 1907131500 1242 GQTALMLAVSHGRIDMVKGLLACGADVNI 1270
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 1163-1279 3.35e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 45.24  E-value: 3.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907131500 1163 INMADGNGNTALHYSVSHSNFQIVKLLldadvcnvdHQNKAGYTP-IMLAALAAVEAEKDMQVVEELFSCG-DVNAKASQ 1240
Cdd:PLN03192   584 VHIRDANGNTALWNAISAKHHKIFRIL---------YHFASISDPhAAGDLLCTAAKRNDLTAMKELLKQGlNVDSEDHQ 654

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1907131500 1241 aGQTALMLAVSHGRIDMVKGLLACGADV---NIQDDEGSTAL 1279
Cdd:PLN03192   655 -GATALQVAMAEDHVDMVRLLIMNGADVdkaNTDDDFSPTEL 695
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 1169-1202 5.43e-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: 38.81  E-value: 5.43e-04
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1907131500 1169 NGNTALHYSVSHS-NFQIVKLLLDADvCNVDHQNK 1202
Cdd:pfam00023    1 DGNTPLHLAAGRRgNLEIVKLLLSKG-ADVNARDK 34
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 1242-1313 5.59e-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: 44.36  E-value: 5.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907131500 1242 GQTALMLAVSHGRIDMVKGLLACGADVNIQ----------DDE----GSTALMCASEHGHVEIVKLLLAQPGCNGHLEDN 1307
Cdd:cd22194    141 GQTALNIAIERRQGDIVKLLIAKGADVNAHakgvffnpkyKHEgfyfGETPLALAACTNQPEIVQLLMEKESTDITSQDS 220


                   ....*.
gi 1907131500 1308 DGSTAL 1313
Cdd:cd22194    221 RGNTVL 226
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 1157-1316 5.61e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 44.10  E-value: 5.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907131500 1157 DVLRYIINMADGNGNTALHYSVSHSNFQIVKLLLdadvcnVDHQNKAGYTPIMLAALAAVEAEKDMQVVEELFSCG-DVN 1235
Cdd:PHA02878    88 EMIRSINKCSVFYTLVAIKDAFNNRNVEIFKIIL------TNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGaDIN 161

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907131500 1236 AKASQAGQTALMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLaQPGCNGHLEDNDGSTALSI 1315
Cdd:PHA02878   162 MKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILL-ENGASTDARDKCGNTPLHI 240


                   .
gi 1907131500 1316 A 1316
Cdd:PHA02878   241 S 241
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 1246-1331 1.07e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 43.12  E-value: 1.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907131500 1246 LMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHV-----EIVKLLLaQPGCNGHLEDNDGSTALSIALEA- 1319
Cdd:PHA03100    39 LYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLL-EYGANVNAPDNNGITPLLYAISKk 117

                           90
                   ....*....|...
gi 1907131500 1320 -GHKDIAVLLYAH 1331
Cdd:PHA03100   118 sNSYSIVEYLLDN 130
Ank_5 pfam13857
Ankyrin repeats (many copies);
1163-1208 2.18e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.71  E-value: 2.18e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1907131500 1163 INMADGNGNTALHYSVSHSNFQIVKLLLDADV-CNVdhQNKAGYTPI 1208
Cdd:pfam13857    9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVdLNL--KDEEGLTAL 53
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
269-500 2.22e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 2.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907131500  269 IALKRLKELEEQVRTIPVLQVKISVLQEEKRQLASQLKSQRASSQNEACGVRKRSYSAGNASQLELLARARRgggELyid 348
Cdd:COG4717     68 LNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEA---EL--- 141

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907131500  349 yeEEEMESVEQSTQRIQEFRQLTADMQALERKIQDSSCEVASELRENGQcpsrecksvavgsdenmndvvVYHRDLRPCK 428
Cdd:COG4717    142 --AELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSL---------------------ATEEELQDLA 198

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907131500  429 DTavgtvtetrnvgisvteamlgvITEADKEIELQQQTIEALKEKIYRLEVQLKETTHDREMTKLKQELQAA 500
Cdd:COG4717    199 EE----------------------LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEA 248
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 1274-1295 2.22e-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: 36.80  E-value: 2.22e-03
                            10        20
                    ....*....|....*....|..
gi 1907131500  1274 EGSTALMCASEHGHVEIVKLLL 1295
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLL 22
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 1169-1194 4.60e-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: 36.03  E-value: 4.60e-03
                            10        20
                    ....*....|....*....|....*.
gi 1907131500  1169 NGNTALHYSVSHSNFQIVKLLLDADV 1194
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGA 26
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 1274-1307 7.36e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 35.34  E-value: 7.36e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1907131500 1274 EGSTALMCASEH-GHVEIVKLLLaQPGCNGHLEDN 1307
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLL-SKGADVNARDK 34
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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