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Conserved domains on  [gi|1622872815|ref|XP_001090427|]
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KN motif and ankyrin repeat domain-containing protein 1 isoform X3 [Macaca mulatta]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
997-1165 3.55e-40

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 150.49  E-value: 3.55e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872815  997 INLADGNGNTALHYSVSHSNFEIVKLLLDADVcNVDHQNKAGYTPIMLAALAaveaeKDMRVVEELFGCG-DVNAKASQa 1075
Cdd:COG0666     80 INAKDDGGNTLLHAAARNGDLEIVKLLLEAGA-DVNARDKDGETPLHLAAYN-----GNLEIVKLLLEAGaDVNAQDND- 152

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872815 1076 GQTALMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQpGCNGHLEDNDGSTALSIALEAGH 1155
Cdd:COG0666    153 GNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA-GADVNAKDNDGKTALDLAAENGN 231

                          170
                   ....*....|
gi 1622872815 1156 KDIAVLLYAH 1165
Cdd:COG0666    232 LEIVKLLLEA 241
YhaN super family cl34808
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
111-337 8.74e-04

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: 43.60  E-value: 8.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872815  111 IALKRLKELEEQVRTIPVLQVKISVLQEEKRQLASQLKNQRAASQNNVCGVRKRSYSAGNASQLEQLSRARGSGGELYID 190
Cdd:COG4717     68 LNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPER 147

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872815  191 YeeeemesvEQSTQRIKEFRQLTADMQALEQKIQdsscEASSEFREngECRSVAVGAEENMNDIIvyhrgsrscKDAAvg 270
Cdd:COG4717    148 L--------EELEERLEELRELEEELEELEAELA----ELQEELEE--LLEQLSLATEEELQDLA---------EELE-- 202

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622872815  271 tltemrncgvsvteamlgvttEADKEIELQQQTIEALKEKIYRLEVQLRETTHDREMTKLKQELQAA 337
Cdd:COG4717    203 ---------------------ELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEA 248
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
997-1165 3.55e-40

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 150.49  E-value: 3.55e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872815  997 INLADGNGNTALHYSVSHSNFEIVKLLLDADVcNVDHQNKAGYTPIMLAALAaveaeKDMRVVEELFGCG-DVNAKASQa 1075
Cdd:COG0666     80 INAKDDGGNTLLHAAARNGDLEIVKLLLEAGA-DVNARDKDGETPLHLAAYN-----GNLEIVKLLLEAGaDVNAQDND- 152

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872815 1076 GQTALMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQpGCNGHLEDNDGSTALSIALEAGH 1155
Cdd:COG0666    153 GNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA-GADVNAKDNDGKTALDLAAENGN 231

                          170
                   ....*....|
gi 1622872815 1156 KDIAVLLYAH 1165
Cdd:COG0666    232 LEIVKLLLEA 241
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1080-1165 1.24e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 93.26  E-value: 1.24e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872815 1080 LMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQPGCNghlEDNDGSTALSIALEAGHKDIA 1159
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN---LKDNGRTALHYAARSGHLEIV 77


                   ....*.
gi 1622872815 1160 VLLYAH 1165
Cdd:pfam12796   78 KLLLEK 83
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 997-1167 6.29e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 69.31  E-value: 6.29e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872815  997 INLADGNGNTALHYSVSHS--NFEIVKLLLDADvCNVDHQNKAGYTPImlaALAAVEAEKDMRVVEELFGCG-DVNAKas 1073
Cdd:PHA03100    99 VNAPDNNGITPLLYAISKKsnSYSIVEYLLDNG-ANVNIKNSDGENLL---HLYLESNKIDLKILKLLIDKGvDINAK-- 172

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872815 1074 qagqtalmlavshgriDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQpGCNGHLEDNDGSTALSIALEA 1153
Cdd:PHA03100   173 ----------------NRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDL-GANPNLVNKYGDTPLHIAILN 235

                          170
                   ....*....|....*
gi 1622872815 1154 GHKDI-AVLLYAHVN 1167
Cdd:PHA03100   236 NNKEIfKLLLNNGPS 250
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 1004-1163 2.97e-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: 51.55  E-value: 2.97e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872815 1004 GNTALHYSVSHSNFEIVKLLLDADvcnvdhqnkagytPIMLaalaaveaekDMRVVEELFgcgdvnakasqAGQTALMLA 1083
Cdd:cd22192     51 GETALHVAALYDNLEAAVVLMEAA-------------PELV----------NEPMTSDLY-----------QGETALHIA 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872815 1084 VSHGRIDMVKGLLACGADVNIQDDEGS------TALMCASEH--------GHVEIVKLLLaQPGCNGHLEDNDGSTALSI 1149
Cdd:cd22192     97 VVNQNLNLVRELIARGADVVSPRATGTffrpgpKNLIYYGEHplsfaacvGNEEIVRLLI-EHGADIRAQDSLGNTVLHI 175

                          170
                   ....*....|....
gi 1622872815 1150 ALEAGHKDIAVLLY 1163
Cdd:cd22192    176 LVLQPNKTFACQMY 189
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 1076-1104 4.00e-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: 4.00e-05
                            10        20
                    ....*....|....*....|....*....
gi 1622872815  1076 GQTALMLAVSHGRIDMVKGLLACGADVNI 1104
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
111-337 8.74e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.60  E-value: 8.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872815  111 IALKRLKELEEQVRTIPVLQVKISVLQEEKRQLASQLKNQRAASQNNVCGVRKRSYSAGNASQLEQLSRARGSGGELYID 190
Cdd:COG4717     68 LNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPER 147

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872815  191 YeeeemesvEQSTQRIKEFRQLTADMQALEQKIQdsscEASSEFREngECRSVAVGAEENMNDIIvyhrgsrscKDAAvg 270
Cdd:COG4717    148 L--------EELEERLEELRELEEELEELEAELA----ELQEELEE--LLEQLSLATEEELQDLA---------EELE-- 202

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622872815  271 tltemrncgvsvteamlgvttEADKEIELQQQTIEALKEKIYRLEVQLRETTHDREMTKLKQELQAA 337
Cdd:COG4717    203 ---------------------ELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEA 248
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 112-350 2.77e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.97  E-value: 2.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872815  112 ALKRLKELEEQVRTIPVLQVKIsvlqEEKRQLASQLKNQRAASQNNVCGVRKRsysagnasqLEQLSRARGSGGELYIDY 191
Cdd:TIGR02168  672 ILERRREIEELEEKIEELEEKI----AELEKALAELRKELEELEEELEQLRKE---------LEELSRQISALRKDLARL 738

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872815  192 EEEEMESVEQSTQRIKEFRQLTADMQALEQKIQDSSCEASSEFRENGECRSVAVGAEENMNDIivyhrgsRSCKDAAVGT 271
Cdd:TIGR02168  739 EAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAL-------REALDELRAE 811

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872815  272 LTEMRNCGVSVTEAMLGVTTEAD---KEIELQQQTIEALKEKIYRLEVQLRETThdREMTKLKQELQAAGSRKKVDKATM 348
Cdd:TIGR02168  812 LTLLNEEAANLRERLESLERRIAateRRLEDLEEQIEELSEDIESLAAEIEELE--ELIEELESELEALLNERASLEEAL 889


                   ..
gi 1622872815  349 AQ 350
Cdd:TIGR02168  890 AL 891
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
997-1165 3.55e-40

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 150.49  E-value: 3.55e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872815  997 INLADGNGNTALHYSVSHSNFEIVKLLLDADVcNVDHQNKAGYTPIMLAALAaveaeKDMRVVEELFGCG-DVNAKASQa 1075
Cdd:COG0666     80 INAKDDGGNTLLHAAARNGDLEIVKLLLEAGA-DVNARDKDGETPLHLAAYN-----GNLEIVKLLLEAGaDVNAQDND- 152

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872815 1076 GQTALMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQpGCNGHLEDNDGSTALSIALEAGH 1155
Cdd:COG0666    153 GNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA-GADVNAKDNDGKTALDLAAENGN 231

                          170
                   ....*....|
gi 1622872815 1156 KDIAVLLYAH 1165
Cdd:COG0666    232 LEIVKLLLEA 241
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
997-1162 5.42e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 135.47  E-value: 5.42e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872815  997 INLADGNGNTALHYSVSHSNFEIVKLLLDADVcNVDHQNKAGYTPIMLAALAaveaeKDMRVVEELFGCG-DVNAKaSQA 1075
Cdd:COG0666    113 VNARDKDGETPLHLAAYNGNLEIVKLLLEAGA-DVNAQDNDGNTPLHLAAAN-----GNLEIVKLLLEAGaDVNAR-DND 185

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872815 1076 GQTALMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQpGCNGHLEDNDGSTALSIALEAGH 1155
Cdd:COG0666    186 GETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA-GADLNAKDKDGLTALLLAAAAGA 264


                   ....*..
gi 1622872815 1156 KDIAVLL 1162
Cdd:COG0666    265 ALIVKLL 271
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
982-1165 2.18e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 130.84  E-value: 2.18e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872815  982 IAAFEAISPDVLRYVINLADGNGNTALHYSVSHSNFEIVKLLLDADVcNVDHQNKAGYTPIMLAALAaveaeKDMRVVEE 1061
Cdd:COG0666     32 LLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGA-DINAKDDGGNTLLHAAARN-----GDLEIVKL 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872815 1062 LFGCG-DVNAKASQaGQTALMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQpGCNGHLED 1140
Cdd:COG0666    106 LLEAGaDVNARDKD-GETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEA-GADVNARD 183

                          170       180
                   ....*....|....*....|....*
gi 1622872815 1141 NDGSTALSIALEAGHKDIAVLLYAH 1165
Cdd:COG0666    184 NDGETPLHLAAENGHLEIVKLLLEA 208
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
986-1177 2.74e-25

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 107.35  E-value: 2.74e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872815  986 EAISPDVLRYVINLADGNGNTALHYSVSHSNFEIVKLLLDADVCNVDHQNKAGYTPIMLAALAAveaeKDMRVVEELFGC 1065
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALA----GDLLVALLLLAA 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872815 1066 GDVNAKASQAGQTALMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQpGCNGHLEDNDGST 1145
Cdd:COG0666     77 GADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA-GADVNAQDNDGNT 155

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1622872815 1146 ALSIALEAGHKDIAVLL---YAHVNfAKAQSPGTP 1177
Cdd:COG0666    156 PLHLAAANGNLEIVKLLleaGADVN-ARDNDGETP 189
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1080-1165 1.24e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 93.26  E-value: 1.24e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872815 1080 LMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQPGCNghlEDNDGSTALSIALEAGHKDIA 1159
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN---LKDNGRTALHYAARSGHLEIV 77


                   ....*.
gi 1622872815 1160 VLLYAH 1165
Cdd:pfam12796   78 KLLLEK 83
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
997-1130 2.90e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 98.49  E-value: 2.90e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872815  997 INLADGNGNTALHYSVSHSNFEIVKLLLDADVcNVDHQNKAGYTPIMLAALAaveaeKDMRVVEELFGCG-DVNAKaSQA 1075
Cdd:COG0666    146 VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGA-DVNARDNDGETPLHLAAEN-----GHLEIVKLLLEAGaDVNAK-DND 218

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1622872815 1076 GQTALMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLA 1130
Cdd:COG0666    219 GKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLL 273
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1008-1106 1.60e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.84  E-value: 1.60e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872815 1008 LHYSVSHSNFEIVKLLLDADvCNVDHQNKAGYTPIMLAALAaveaeKDMRVVEELFGCGDVNAKASqaGQTALMLAVSHG 1087
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENG-ADANLQDKNGRTALHLAAKN-----GHLEIVKLLLEHADVNLKDN--GRTALHYAARSG 72

                           90
                   ....*....|....*....
gi 1622872815 1088 RIDMVKGLLACGADVNIQD 1106
Cdd:pfam12796   73 HLEIVKLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 997-1167 6.29e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 69.31  E-value: 6.29e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872815  997 INLADGNGNTALHYSVSHS--NFEIVKLLLDADvCNVDHQNKAGYTPImlaALAAVEAEKDMRVVEELFGCG-DVNAKas 1073
Cdd:PHA03100    99 VNAPDNNGITPLLYAISKKsnSYSIVEYLLDNG-ANVNIKNSDGENLL---HLYLESNKIDLKILKLLIDKGvDINAK-- 172

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872815 1074 qagqtalmlavshgriDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQpGCNGHLEDNDGSTALSIALEA 1153
Cdd:PHA03100   173 ----------------NRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDL-GANPNLVNKYGDTPLHIAILN 235

                          170
                   ....*....|....*
gi 1622872815 1154 GHKDI-AVLLYAHVN 1167
Cdd:PHA03100   236 NNKEIfKLLLNNGPS 250
Ank_4 pfam13637
Ankyrin repeats (many copies);
1078-1129 1.64e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 60.37  E-value: 1.64e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1622872815 1078 TALMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLL 1129
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 980-1161 1.83e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 64.66  E-value: 1.83e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872815  980 DYIAAFEAISPDVLRYVI------NLADGNGNTALHYSVSHSN---FEIVKLLLDADVcNVDHQNKAGYTPIMLAALAAV 1050
Cdd:PHA03095    17 DYLLNASNVTVEEVRRLLaagadvNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGA-DVNAPERCGFTPLHLYLYNAT 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872815 1051 EAekdmRVVEELFGCG-DVNAKaSQAGQTALMLAVSHGRID--MVKGLLACGADVNIQDDEGSTALMC--ASEHGHVEIV 1125
Cdd:PHA03095    96 TL----DVIKLLIKAGaDVNAK-DKVGRTPLHVYLSGFNINpkVIRLLLRKGADVNALDLYGMTPLAVllKSRNANVELL 170

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1622872815 1126 KLLLAQpGCNGHLEDNDGSTALSIALEAGHKDIAVL 1161
Cdd:PHA03095   171 RLLIDA-GADVYAVDDRFRSLLHHHLQSFKPRARIV 205
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 1054-1176 1.74e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 62.19  E-value: 1.74e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872815 1054 KDMRVVEELFGCGDVNAKASQAGQtaLMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQpG 1133
Cdd:PLN03192   505 HDLNVGDLLGDNGGEHDDPNMASN--LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKH-A 581

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1622872815 1134 CNGHLEDNDGSTALSIALEAGHKDIAVLLYahvNFAKAQSPGT 1176
Cdd:PLN03192   582 CNVHIRDANGNTALWNAISAKHHKIFRILY---HFASISDPHA 621
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 1018-1167 4.69e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 59.98  E-value: 4.69e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872815 1018 EIVKLLLDADVcnvdhqnKAGYTPImlaalaaVEAEKDMrvVEELFGCG-DVNAKASQAgQTALMLAVSHGRIDMVKGLL 1096
Cdd:PHA02874    82 DIIKLLIDNGV-------DTSILPI-------PCIEKDM--IKTILDCGiDVNIKDAEL-KTFLHYAIKKGDLESIKMLF 144

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622872815 1097 ACGADVNIQDDEGSTALMCASEHGHVEIVKLLLaQPGCNGHLEDNDGSTALSIALEAGHKDIAVLLYAHVN 1167
Cdd:PHA02874   145 EYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLL-EKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGN 214
Ank_5 pfam13857
Ankyrin repeats (many copies);
1095-1150 4.78e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 53.50  E-value: 4.78e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622872815 1095 LLACG-ADVNIQDDEGSTALMCASEHGHVEIVKLLLAqPGCNGHLEDNDGSTALSIA 1150
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLA-YGVDLNLKDEEGLTALDLA 56
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1113-1167 4.83e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 54.35  E-value: 4.83e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1622872815 1113 LMCASEHGHVEIVKLLLaQPGCNGHLEDNDGSTALSIALEAGHKDIAVLLYAHVN 1167
Cdd:pfam12796    1 LHLAAKNGNLELVKLLL-ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 997-1129 1.75e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 58.35  E-value: 1.75e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872815  997 INLADGNGNTALHYSVSHSNFEIVKLLLDaDVCNVDHQNKAGYTPImlaaLAAVEAEKDMRVVEELFGCG-DVNAKASQA 1075
Cdd:PHA02878   194 VNIPDKTNNSPLHHAVKHYNKPIVHILLE-NGASTDARDKCGNTPL----HISVGYCKDYDILKLLLEHGvDVNAKSYIL 268

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1622872815 1076 GQTALMLAVSHGRIdmVKGLLACGADVNIQDDEGSTAL-MCASEHGHVEIVKLLL 1129
Cdd:PHA02878   269 GLTALHSSIKSERK--LKLLLEYGADINSLNSYKLTPLsSAVKQYLCINIGRILI 321
Ank_5 pfam13857
Ankyrin repeats (many copies);
1067-1113 2.90e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.50  E-value: 2.90e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1622872815 1067 DVNAKaSQAGQTALMLAVSHGRIDMVKGLLACGADVNIQDDEGSTAL 1113
Cdd:pfam13857    8 DLNRL-DGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 1092-1165 3.01e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.90  E-value: 3.01e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622872815 1092 VKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLaQPGCNGHLEDNDGSTALSIALEAGHKDIAVLLYAH 1165
Cdd:PTZ00322    98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLL-EFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 998-1186 8.57e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 53.33  E-value: 8.57e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872815  998 NLADGNGNTALHYSVSHSNFEIVKLLLDaDVCNVDHQNKAGYTPIMLAALAaveaeKDMRVVEELFGCgdvnAKAS--QA 1075
Cdd:PLN03192   552 DIGDSKGRTPLHIAASKGYEDCVLVLLK-HACNVHIRDANGNTALWNAISA-----KHHKIFRILYHF----ASISdpHA 621

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872815 1076 GQTALMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAqpgcNG------HLEDNDGSTALSI 1149
Cdd:PLN03192   622 AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIM----NGadvdkaNTDDDFSPTELRE 697

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1622872815 1150 AL---EAGHKdIAVLLYAHVNFAKAQSPGTPRLGRKTSPG 1186
Cdd:PLN03192   698 LLqkrELGHS-ITIVDSVPADEPDLGRDGGSRPGRLQGTS 736
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 1003-1131 1.51e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 51.92  E-value: 1.51e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872815 1003 NGNTALHYSVSHSNFEIVKLLL----DADVCNVDHqnkagYTPImlaalAAVEAEKDMRVVEELF---GCGDVNakaSQA 1075
Cdd:PHA02875   101 DGMTPLHLATILKKLDIMKLLIargaDPDIPNTDK-----FSPL-----HLAVMMGDIKGIELLIdhkACLDIE---DCC 167

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622872815 1076 GQTALMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMC-ASEHGHVEIVKLLLAQ 1131
Cdd:PHA02875   168 GCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCyAIENNKIDIVRLFIKR 224
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 1004-1163 2.97e-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: 51.55  E-value: 2.97e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872815 1004 GNTALHYSVSHSNFEIVKLLLDADvcnvdhqnkagytPIMLaalaaveaekDMRVVEELFgcgdvnakasqAGQTALMLA 1083
Cdd:cd22192     51 GETALHVAALYDNLEAAVVLMEAA-------------PELV----------NEPMTSDLY-----------QGETALHIA 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872815 1084 VSHGRIDMVKGLLACGADVNIQDDEGS------TALMCASEH--------GHVEIVKLLLaQPGCNGHLEDNDGSTALSI 1149
Cdd:cd22192     97 VVNQNLNLVRELIARGADVVSPRATGTffrpgpKNLIYYGEHplsfaacvGNEEIVRLLI-EHGADIRAQDSLGNTVLHI 175

                          170
                   ....*....|....
gi 1622872815 1150 ALEAGHKDIAVLLY 1163
Cdd:cd22192    176 LVLQPNKTFACQMY 189
Ank_4 pfam13637
Ankyrin repeats (many copies);
1109-1162 3.26e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.34  E-value: 3.26e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1622872815 1109 GSTALMCASEHGHVEIVKLLLaQPGCNGHLEDNDGSTALSIALEAGHKDIAVLL 1162
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLL-EKGADINAVDGNGETALHFAASNGNVEVLKLL 53
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 1076-1107 4.28e-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: 4.28e-06
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1622872815 1076 GQTALMLAVSH-GRIDMVKGLLACGADVNIQDD 1107
Cdd:pfam00023    2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 995-1042 9.30e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 49.66  E-value: 9.30e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1622872815  995 YVINLADGNGNTALHYSVSHSNFEIVKLLLDADvCNVDHQNKAGYTPI 1042
Cdd:PHA03100   183 VPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLG-ANPNLVNKYGDTPL 229
Ank_2 pfam12796
Ankyrin repeats (3 copies);
989-1035 1.25e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 44.72  E-value: 1.25e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1622872815  989 SPDVLRYVINLADGN----GNTALHYSVSHSNFEIVKLLLDADvCNVDHQN 1035
Cdd:pfam12796   42 HLEIVKLLLEHADVNlkdnGRTALHYAARSGHLEIVKLLLEKG-ADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 997-1157 1.38e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 49.19  E-value: 1.38e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872815  997 INLADGNGNTALHYSVSHSNFEIVKLLLDADV-CNVDHQNkaGYTPImlaalAAVEAEKDMRVVEELFGCGDVNAKASQA 1075
Cdd:PHA02874   150 VNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAyANVKDNN--GESPL-----HNAAEYGDYACIKLLIDHGNHIMNKCKN 222

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872815 1076 GQTALMLAVSHGRidMVKGLLACGADVNIQDDEGSTALMCASEHG-HVEIVKLLLAQPGcNGHLEDNDGSTALSIALEAG 1154
Cdd:PHA02874   223 GFTPLHNAIIHNR--SAIELLINNASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKA-DISIKDNKGENPIDTAFKYI 299


                   ...
gi 1622872815 1155 HKD 1157
Cdd:PHA02874   300 NKD 302
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 1076-1141 3.17e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.36  E-value: 3.17e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622872815 1076 GQTALMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQPGCNGHLEDN 1141
Cdd:PTZ00322   115 GRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELGAN 180
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 1076-1104 4.00e-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: 4.00e-05
                            10        20
                    ....*....|....*....|....*....
gi 1622872815  1076 GQTALMLAVSHGRIDMVKGLLACGADVNI 1104
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
997-1024 5.15e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.88  E-value: 5.15e-05
                           10        20
                   ....*....|....*....|....*...
gi 1622872815  997 INLADGNGNTALHYSVSHSNFEIVKLLL 1024
Cdd:pfam13637   27 INAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 1008-1162 6.23e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 46.91  E-value: 6.23e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872815 1008 LHYSVSHSNFEIVKLLLDADVCNVDHQNKAGYTPImlaalAAVEAEKDMRVVEELFGCGDVNAKASQAGQTALMLAVSHG 1087
Cdd:PHA02875    72 LHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPL-----HLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMG 146

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622872815 1088 RIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQPGCNGHLEDNDGSTALSIALEAGHKDIAVLL 1162
Cdd:PHA02875   147 DIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLF 221
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 1006-1104 6.51e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 46.91  E-value: 6.51e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872815 1006 TALHYSVSHSNFEIVKLLLDADVCnVDHQNKAGYTPIMLAALAaveaeKDMRVVEELFGCG-DVNAKASQAGQTALMLAV 1084
Cdd:PHA02875   137 SPLHLAVMMGDIKGIELLIDHKAC-LDIEDCCGCTPLIIAMAK-----GDIAICKMLLDSGaNIDYFGKNGCVAALCYAI 210

                           90       100
                   ....*....|....*....|
gi 1622872815 1085 SHGRIDMVKGLLACGADVNI 1104
Cdd:PHA02875   211 ENNKIDIVRLFIKRGADCNI 230
PHA03095 PHA03095
ankyrin-like protein; Provisional
 988-1131 1.39e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 45.79  E-value: 1.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872815  988 ISPDVLRYVINL------ADGNGNTALHY--SVSHSNFEIVKLLLDADvCNVDHQNKAGYTPIMLAALAAVEAEKDMRVV 1059
Cdd:PHA03095   165 ANVELLRLLIDAgadvyaVDDRFRSLLHHhlQSFKPRARIVRELIRAG-CDPAATDMLGNTPLHSMATGSSCKRSLVLPL 243

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622872815 1060 eeLFGCGDVNAKaSQAGQTALMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQ 1131
Cdd:PHA03095   244 --LIAGISINAR-NRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAK 312
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 1076-1104 1.80e-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: 1.80e-04
                           10        20
                   ....*....|....*....|....*....
gi 1622872815 1076 GQTALMLAVSHGRIDMVKGLLACGADVNI 1104
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 1003-1036 2.13e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.58  E-value: 2.13e-04
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1622872815 1003 NGNTALHYSVSHS-NFEIVKLLLDADvCNVDHQNK 1036
Cdd:pfam00023    1 DGNTPLHLAAGRRgNLEIVKLLLSKG-ADVNARDK 34
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 1076-1147 4.82e-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: 4.82e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872815 1076 GQTALMLAVSHGRIDMVKGLLACGADVNIQ----------DDE----GSTALMCASEHGHVEIVKLLLAQPGCNGHLEDN 1141
Cdd:cd22194    141 GQTALNIAIERRQGDIVKLLIAKGADVNAHakgvffnpkyKHEgfyfGETPLALAACTNQPEIVQLLMEKESTDITSQDS 220


                   ....*.
gi 1622872815 1142 DGSTAL 1147
Cdd:cd22194    221 RGNTVL 226
Ank_5 pfam13857
Ankyrin repeats (many copies);
997-1042 6.59e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.87  E-value: 6.59e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1622872815  997 INLADGNGNTALHYSVSHSNFEIVKLLLDADV-CNVdhQNKAGYTPI 1042
Cdd:pfam13857    9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVdLNL--KDEEGLTAL 53
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 1005-1150 7.62e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 43.33  E-value: 7.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872815 1005 NTALHYSvshsNFEIVKLLLdadvcnVDHQNKAGYTPIMLAALAAVEAEKDMRVVEELFGCG-DVNAKASQAGQTALMLA 1083
Cdd:PHA02878   106 KDAFNNR----NVEIFKIIL------TNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGaDINMKDRHKGNTALHYA 175

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622872815 1084 VSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLaQPGCNGHLEDNDGSTALSIA 1150
Cdd:PHA02878   176 TENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILL-ENGASTDARDKCGNTPLHIS 241
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 1003-1028 8.47e-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: 8.47e-04
                            10        20
                    ....*....|....*....|....*.
gi 1622872815  1003 NGNTALHYSVSHSNFEIVKLLLDADV 1028
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGA 26
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
111-337 8.74e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.60  E-value: 8.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872815  111 IALKRLKELEEQVRTIPVLQVKISVLQEEKRQLASQLKNQRAASQNNVCGVRKRSYSAGNASQLEQLSRARGSGGELYID 190
Cdd:COG4717     68 LNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPER 147

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872815  191 YeeeemesvEQSTQRIKEFRQLTADMQALEQKIQdsscEASSEFREngECRSVAVGAEENMNDIIvyhrgsrscKDAAvg 270
Cdd:COG4717    148 L--------EELEERLEELRELEEELEELEAELA----ELQEELEE--LLEQLSLATEEELQDLA---------EELE-- 202

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622872815  271 tltemrncgvsvteamlgvttEADKEIELQQQTIEALKEKIYRLEVQLRETTHDREMTKLKQELQAA 337
Cdd:COG4717    203 ---------------------ELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEA 248
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 1080-1165 9.22e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 43.12  E-value: 9.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872815 1080 LMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHV-----EIVKLLLaQPGCNGHLEDNDGSTALSIALEA- 1153
Cdd:PHA03100    39 LYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLL-EYGANVNAPDNNGITPLLYAISKk 117

                           90
                   ....*....|...
gi 1622872815 1154 -GHKDIAVLLYAH 1165
Cdd:PHA03100   118 sNSYSIVEYLLDN 130
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 997-1151 9.88e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 43.03  E-value: 9.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872815  997 INLADGNGNTALHYSVSHSNFEIVKLLLD--ADVcNVDHQNkaGYTPImlaalaaveaekdmrvveelfgcgdvnakasq 1074
Cdd:PHA02874   117 VNIKDAELKTFLHYAIKKGDLESIKMLFEygADV-NIEDDN--GCYPI-------------------------------- 161

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622872815 1075 agqtalMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLLAQpGCNGHLEDNDGSTALSIAL 1151
Cdd:PHA02874   162 ------HIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDH-GNHIMNKCKNGFTPLHNAI 231
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 1108-1129 1.95e-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: 1.95e-03
                            10        20
                    ....*....|....*....|..
gi 1622872815  1108 EGSTALMCASEHGHVEIVKLLL 1129
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLL 22
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 112-350 2.77e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.97  E-value: 2.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872815  112 ALKRLKELEEQVRTIPVLQVKIsvlqEEKRQLASQLKNQRAASQNNVCGVRKRsysagnasqLEQLSRARGSGGELYIDY 191
Cdd:TIGR02168  672 ILERRREIEELEEKIEELEEKI----AELEKALAELRKELEELEEELEQLRKE---------LEELSRQISALRKDLARL 738

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872815  192 EEEEMESVEQSTQRIKEFRQLTADMQALEQKIQDSSCEASSEFRENGECRSVAVGAEENMNDIivyhrgsRSCKDAAVGT 271
Cdd:TIGR02168  739 EAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAL-------REALDELRAE 811

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872815  272 LTEMRNCGVSVTEAMLGVTTEAD---KEIELQQQTIEALKEKIYRLEVQLRETThdREMTKLKQELQAAGSRKKVDKATM 348
Cdd:TIGR02168  812 LTLLNEEAANLRERLESLERRIAateRRLEDLEEQIEELSEDIESLAAEIEELE--ELIEELESELEALLNERASLEEAL 889


                   ..
gi 1622872815  349 AQ 350
Cdd:TIGR02168  890 AL 891
Ank_4 pfam13637
Ankyrin repeats (many copies);
1004-1042 3.72e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.87  E-value: 3.72e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1622872815 1004 GNTALHYSVSHSNFEIVKLLLDADVcNVDHQNKAGYTPI 1042
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGA-DINAVDGNGETAL 38
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 1055-1129 5.19e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 40.82  E-value: 5.19e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622872815 1055 DMRVVEELFGCG-DVNAKASQAgQTALMLAVSHGRIDMVKGLLACGADVNIQDDEGSTALMCASEHGHVEIVKLLL 1129
Cdd:PHA02876   157 ELLIAEMLLEGGaDVNAKDIYC-ITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAII 231
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 1108-1141 6.53e-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: 6.53e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1622872815 1108 EGSTALMCASEH-GHVEIVKLLLaQPGCNGHLEDN 1141
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLL-SKGADVNARDK 34
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 1018-1167 6.92e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 40.25  E-value: 6.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622872815 1018 EIVKLLLD--ADVCNVDHQNkaGYTPImlaalAAVEAEKDMRVVEELFGCG-DVNAkASQAGQTALMLAVSHGRIDMVKG 1094
Cdd:PHA02878   148 EITKLLLSygADINMKDRHK--GNTAL-----HYATENKDQRLTELLLSYGaNVNI-PDKTNNSPLHHAVKHYNKPIVHI 219

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622872815 1095 LLACGADVNIQDDEGSTALMCASEH-GHVEIVKLLLAQPGCNGHLEDNDGSTALSIALEAGHKDIAVLLY-AHVN 1167
Cdd:PHA02878   220 LLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYILGLTALHSSIKSERKLKLLLEYgADIN 294
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 1003-1028 9.53e-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: 34.93  E-value: 9.53e-03
                           10        20
                   ....*....|....*....|....*.
gi 1622872815 1003 NGNTALHYSVSHSNFEIVKLLLDADV 1028
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGA 26
 
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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