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Conserved domains on  [gi|15232175|ref|NP_186824|]
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Ankyrin repeat family protein [Arabidopsis thaliana]

Protein Classification

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

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
190-400 2.64e-27

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 112.35  E-value: 2.64e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232175 190 NRAVHSASRGGNLILLKELLSDcsvEHVLAFRDKQGSTILHSAAGKGKTQVVKELVASSYHlVDAVDNQGNTALHVAAYR 269
Cdd:COG0666  55 ALLLLAAALAGDLLVALLLLAA---GADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGAD-VNARDKDGETPLHLAAYN 130

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232175 270 GHADLVDVLISASPSlISARNNAGDTFLH-AGISGfqtpaferldkHTELMNRLItsaaskSQGDFVNYRNNEGRTALHL 348
Cdd:COG0666 131 GNLEIVKLLLEAGAD-VNAQDNDGNTPLHlAAANG-----------NLEIVKLLL------EAGADVNARDNDGETPLHL 192

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 15232175 349 AI-SGNvpLEFVEMLMSvKSIDINIRDNAGMTPLDLIRQKPLSPTSDLLFRRL 400
Cdd:COG0666 193 AAeNGH--LEIVKLLLE-AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAG 242
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
190-400 2.64e-27

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 112.35  E-value: 2.64e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232175 190 NRAVHSASRGGNLILLKELLSDcsvEHVLAFRDKQGSTILHSAAGKGKTQVVKELVASSYHlVDAVDNQGNTALHVAAYR 269
Cdd:COG0666  55 ALLLLAAALAGDLLVALLLLAA---GADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGAD-VNARDKDGETPLHLAAYN 130

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232175 270 GHADLVDVLISASPSlISARNNAGDTFLH-AGISGfqtpaferldkHTELMNRLItsaaskSQGDFVNYRNNEGRTALHL 348
Cdd:COG0666 131 GNLEIVKLLLEAGAD-VNAQDNDGNTPLHlAAANG-----------NLEIVKLLL------EAGADVNARDNDGETPLHL 192

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 15232175 349 AI-SGNvpLEFVEMLMSvKSIDINIRDNAGMTPLDLIRQKPLSPTSDLLFRRL 400
Cdd:COG0666 193 AAeNGH--LEIVKLLLE-AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAG 242
Ank_2 pfam12796
Ankyrin repeats (3 copies);
194-280 1.94e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 63.60  E-value: 1.94e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232175   194 HSASRGGNLILLKELLSDCSVEHVLafrDKQGSTILHSAAGKGKTQVVKELVasSYHLVDAVDNqGNTALHVAAYRGHAD 273
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENGADANLQ---DKNGRTALHLAAKNGHLEIVKLLL--EHADVNLKDN-GRTALHYAARSGHLE 75


                  ....*..
gi 15232175   274 LVDVLIS 280
Cdd:pfam12796  76 IVKLLLE 82
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 193-382 3.67e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 53.04  E-value: 3.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232175  193 VHSASRGGNLILLKELL---SDCSVEhvlafrDKQGSTILHSAAGKGKTQVVKELVASSYHLvDAVDNQGNTALHVAAYR 269
Cdd:PHA02874 128 LHYAIKKGDLESIKMLFeygADVNIE------DDNGCYPIHIAIKHNFFDIIKLLLEKGAYA-NVKDNNGESPLHNAAEY 200

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232175  270 GHADLVDVLISASpSLISARNNAGDTFLHAGIsgfqtpaferldkhteLMNR-----LITSAAsksqgdfVNYRNNEGRT 344
Cdd:PHA02874 201 GDYACIKLLIDHG-NHIMNKCKNGFTPLHNAI----------------IHNRsaielLINNAS-------INDQDIDGST 256

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 15232175  345 ALHLAISGNVPLEFVEMLMSVKSiDINIRDNAGMTPLD 382
Cdd:PHA02874 257 PLHHAINPPCDIDIIDILLYHKA-DISIKDNKGENPID 293
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 196-383 2.50e-05

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: 47.31  E-value: 2.50e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232175 196 ASRGGNLILLKELLSDCSVEhvLAFRDKQGSTILHSAAGKGKTQVVKELVASSYHLVDAVDN----QGNTALHVAAYRGH 271
Cdd:cd22192  24 AAKENDVQAIKKLLKCPSCD--LFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEPMTsdlyQGETALHIAVVNQN 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232175 272 ADLVDVLISASPSLISARnnAGDTFLHAGIS-----GFQTPAFERLDKHTELMNRLITSAAS-KSQGDFvnyrnneGRTA 345
Cdd:cd22192 102 LNLVRELIARGADVVSPR--ATGTFFRPGPKnliyyGEHPLSFAACVGNEEIVRLLIEHGADiRAQDSL-------GNTV 172

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 15232175 346 LHLAI---SGNVPLEFVEMLMS-VKSIDI----NIRDNAGMTPLDL 383
Cdd:cd22192 173 LHILVlqpNKTFACQMYDLILSyDKEDDLqpldLVPNNQGLTPFKL 218
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 258-285 3.71e-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: 3.71e-04
                           10        20
                   ....*....|....*....|....*...
gi 15232175    258 QGNTALHVAAYRGHADLVDVLISASPSL 285
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
190-400 2.64e-27

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 112.35  E-value: 2.64e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232175 190 NRAVHSASRGGNLILLKELLSDcsvEHVLAFRDKQGSTILHSAAGKGKTQVVKELVASSYHlVDAVDNQGNTALHVAAYR 269
Cdd:COG0666  55 ALLLLAAALAGDLLVALLLLAA---GADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGAD-VNARDKDGETPLHLAAYN 130

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232175 270 GHADLVDVLISASPSlISARNNAGDTFLH-AGISGfqtpaferldkHTELMNRLItsaaskSQGDFVNYRNNEGRTALHL 348
Cdd:COG0666 131 GNLEIVKLLLEAGAD-VNAQDNDGNTPLHlAAANG-----------NLEIVKLLL------EAGADVNARDNDGETPLHL 192

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 15232175 349 AI-SGNvpLEFVEMLMSvKSIDINIRDNAGMTPLDLIRQKPLSPTSDLLFRRL 400
Cdd:COG0666 193 AAeNGH--LEIVKLLLE-AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAG 242
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
142-400 3.49e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 100.41  E-value: 3.49e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232175 142 DILYAAARSKNDDVFRLIYDFAVTPRFGTGGIEQQTGEIPAAYKWEMKNRAVHSASRGGNLILLKELLS---DcsvehvL 218
Cdd:COG0666  40 LLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEagaD------V 113

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232175 219 AFRDKQGSTILHSAAGKGKTQVVKELV---ASsyhlVDAVDNQGNTALHVAAYRGHADLVDVLISASPSlISARNNAGDT 295
Cdd:COG0666 114 NARDKDGETPLHLAAYNGNLEIVKLLLeagAD----VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGAD-VNARDNDGET 188

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232175 296 FLHAgisgfqtpAFERldKHTELMNRLItsaaskSQGDFVNYRNNEGRTALHLAISGNVpLEFVEMLMSvKSIDINIRDN 375
Cdd:COG0666 189 PLHL--------AAEN--GHLEIVKLLL------EAGADVNAKDNDGKTALDLAAENGN-LEIVKLLLE-AGADLNAKDK 250

                       250       260
                ....*....|....*....|....*
gi 15232175 376 AGMTPLDLIRQKPLSPTSDLLFRRL 400
Cdd:COG0666 251 DGLTALLLAAAAGAALIVKLLLLAL 275
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
95-376 1.05e-19

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 90.01  E-value: 1.05e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232175  95 KRNTLIRSGYGGWLIYTAASAGDLAFVHDLLERNPLLVFGEGEYGVTdILYAAARSKNDDVFRLIydfavtprfgtggIE 174
Cdd:COG0666  43 ALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNT-LLHAAARNGDLEIVKLL-------------LE 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232175 175 QqtGEIPAAyKWEMKNRAVHSASRGGNLILLKELLsdcsvEH---VLAfRDKQGSTILHSAAGKGKTQVVKELVASSYHl 251
Cdd:COG0666 109 A--GADVNA-RDKDGETPLHLAAYNGNLEIVKLLL-----EAgadVNA-QDNDGNTPLHLAAANGNLEIVKLLLEAGAD- 178

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232175 252 VDAVDNQGNTALHVAAYRGHADLVDVLISASPSlISARNNAGDTFLHagisgfqtpaFERLDKHTELMNRLITSAASksq 331
Cdd:COG0666 179 VNARDNDGETPLHLAAENGHLEIVKLLLEAGAD-VNAKDNDGKTALD----------LAAENGNLEIVKLLLEAGAD--- 244

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 15232175 332 gdfVNYRNNEGRTALHLAISGNVPLEFVEMLMSVKSIDINIRDNA 376
Cdd:COG0666 245 ---LNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLL 286
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
201-383 4.51e-19

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 88.09  E-value: 4.51e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232175 201 NLILLKELLSDCSVEHVLAFRDKQGSTILHSAAGKGKTQVVKELVASSYHLVDAVDNQGNTALHVAAYRGHADLVDVLIS 280
Cdd:COG0666  29 ALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLE 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232175 281 ASPSlISARNNAGDTFLHAGISGfqtpaferldKHTELMNRLITSAASksqgdfVNYRNNEGRTALHLAI-SGNvpLEFV 359
Cdd:COG0666 109 AGAD-VNARDKDGETPLHLAAYN----------GNLEIVKLLLEAGAD------VNAQDNDGNTPLHLAAaNGN--LEIV 169

                       170       180
                ....*....|....*....|....
gi 15232175 360 EMLMSvKSIDINIRDNAGMTPLDL 383
Cdd:COG0666 170 KLLLE-AGADVNARDNDGETPLHL 192
Ank_2 pfam12796
Ankyrin repeats (3 copies);
194-280 1.94e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 63.60  E-value: 1.94e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232175   194 HSASRGGNLILLKELLSDCSVEHVLafrDKQGSTILHSAAGKGKTQVVKELVasSYHLVDAVDNqGNTALHVAAYRGHAD 273
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENGADANLQ---DKNGRTALHLAAKNGHLEIVKLLL--EHADVNLKDN-GRTALHYAARSGHLE 75


                  ....*..
gi 15232175   274 LVDVLIS 280
Cdd:pfam12796  76 IVKLLLE 82
Ank_2 pfam12796
Ankyrin repeats (3 copies);
263-374 3.43e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 57.05  E-value: 3.43e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232175   263 LHVAAYRGHADLVDVLISASPSlISARNNAGDTFLHAGISGfqtpaferldKHTELMNRLITSAASKSQgdfvnyrnNEG 342
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGAD-ANLQDKNGRTALHLAAKN----------GHLEIVKLLLEHADVNLK--------DNG 61

                          90       100       110
                  ....*....|....*....|....*....|..
gi 15232175   343 RTALHLAISGNvPLEFVEMLMSvKSIDINIRD 374
Cdd:pfam12796  62 RTALHYAARSG-HLEIVKLLLE-KGADINVKD 91
Ank_4 pfam13637
Ankyrin repeats (many copies);
225-279 4.36e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.36  E-value: 4.36e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 15232175   225 GSTILHSAAGKGKTQVVKELVASSYHlVDAVDNQGNTALHVAAYRGHADLVDVLI 279
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGAD-INAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 193-382 3.67e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 53.04  E-value: 3.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232175  193 VHSASRGGNLILLKELL---SDCSVEhvlafrDKQGSTILHSAAGKGKTQVVKELVASSYHLvDAVDNQGNTALHVAAYR 269
Cdd:PHA02874 128 LHYAIKKGDLESIKMLFeygADVNIE------DDNGCYPIHIAIKHNFFDIIKLLLEKGAYA-NVKDNNGESPLHNAAEY 200

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232175  270 GHADLVDVLISASpSLISARNNAGDTFLHAGIsgfqtpaferldkhteLMNR-----LITSAAsksqgdfVNYRNNEGRT 344
Cdd:PHA02874 201 GDYACIKLLIDHG-NHIMNKCKNGFTPLHNAI----------------IHNRsaielLINNAS-------INDQDIDGST 256

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 15232175  345 ALHLAISGNVPLEFVEMLMSVKSiDINIRDNAGMTPLD 382
Cdd:PHA02874 257 PLHHAINPPCDIDIIDILLYHKA-DISIKDNKGENPID 293
Ank_5 pfam13857
Ankyrin repeats (many copies);
335-383 2.43e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.33  E-value: 2.43e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 15232175   335 VNYRNNEGRTALHLAISGNvPLEFVEMLMSVKSiDINIRDNAGMTPLDL 383
Cdd:pfam13857   9 LNRLDGEGYTPLHVAAKYG-ALEIVRVLLAYGV-DLNLKDEEGLTALDL 55
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 196-383 2.50e-05

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: 47.31  E-value: 2.50e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232175 196 ASRGGNLILLKELLSDCSVEhvLAFRDKQGSTILHSAAGKGKTQVVKELVASSYHLVDAVDN----QGNTALHVAAYRGH 271
Cdd:cd22192  24 AAKENDVQAIKKLLKCPSCD--LFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEPMTsdlyQGETALHIAVVNQN 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232175 272 ADLVDVLISASPSLISARnnAGDTFLHAGIS-----GFQTPAFERLDKHTELMNRLITSAAS-KSQGDFvnyrnneGRTA 345
Cdd:cd22192 102 LNLVRELIARGADVVSPR--ATGTFFRPGPKnliyyGEHPLSFAACVGNEEIVRLLIEHGADiRAQDSL-------GNTV 172

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 15232175 346 LHLAI---SGNVPLEFVEMLMS-VKSIDI----NIRDNAGMTPLDL 383
Cdd:cd22192 173 LHILVlqpNKTFACQMYDLILSyDKEDDLqpldLVPNNQGLTPFKL 218
Ank_2 pfam12796
Ankyrin repeats (3 copies);
314-381 3.59e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 42.80  E-value: 3.59e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15232175   314 KHTELMNRLITSAASksqgdfVNYRNNEGRTALHLAISGNVpLEFVEMLmsVKSIDINIRDNaGMTPL 381
Cdd:pfam12796   8 GNLELVKLLLENGAD------ANLQDKNGRTALHLAAKNGH-LEIVKLL--LEHADVNLKDN-GRTAL 65
PHA03095 PHA03095
ankyrin-like protein; Provisional
 252-404 4.78e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.17  E-value: 4.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232175  252 VDAVDNQGNTALHVAAYRGHADLVDV---LISASPSlISARNNAGDTFLHAGISGFQTPaferldkhtELMNRLITSAAS 328
Cdd:PHA03095  40 VNFRGEYGKTPLHLYLHYSSEKVKDIvrlLLEAGAD-VNAPERCGFTPLHLYLYNATTL---------DVIKLLIKAGAD 109

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15232175  329 ksqgdfVNYRNNEGRTALHLAISG-NVPLEFVEMLMSvKSIDINIRDNAGMTPLD-LIRQKPLSPtsDLLfRRLVSAG 404
Cdd:PHA03095 110 ------VNAKDKVGRTPLHVYLSGfNINPKVIRLLLR-KGADVNALDLYGMTPLAvLLKSRNANV--ELL-RLLIDAG 177
PHA03095 PHA03095
ankyrin-like protein; Provisional
 240-383 5.54e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.17  E-value: 5.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232175  240 VVKELVASSYHLVdAVDNQGNTALHVAA--YRGHADLVDVLISASPSlISARNNAGDTFLHagisgfqTPAFERLDKHTE 317
Cdd:PHA03095 169 LLRLLIDAGADVY-AVDDRFRSLLHHHLqsFKPRARIVRELIRAGCD-PAATDMLGNTPLH-------SMATGSSCKRSL 239

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15232175  318 LMNRLITSAAsksqgdfVNYRNNEGRTALHLA-ISGNVPleFVEMLMSVKSiDINIRDNAGMTPLDL 383
Cdd:PHA03095 240 VLPLLIAGIS-------INARNRYGQTPLHYAaVFNNPR--ACRRLIALGA-DINAVSSDGNTPLSL 296
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 252-381 1.85e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 44.27  E-value: 1.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232175  252 VDAVDNQGNTALHVAAYR--GHADLVDVLISASpSLISARNNAGDTFLHAGISG--FQTPAFERLDKHT---ELMNR--- 321
Cdd:PHA03100  99 VNAPDNNGITPLLYAISKksNSYSIVEYLLDNG-ANVNIKNSDGENLLHLYLESnkIDLKILKLLIDKGvdiNAKNRvny 177

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232175  322 LITSAASksqgdfVNYRNNEGRTALHLAISgNVPLEFVEMLMSvKSIDINIRDNAGMTPL 381
Cdd:PHA03100 178 LLSYGVP------INIKDVYGFTPLHYAVY-NNNPEFVKYLLD-LGANPNLVNKYGDTPL 229
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
262-381 2.64e-04

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 43.40  E-value: 2.64e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232175 262 ALHVAAYRGHADLVDVLISASPSLISARNNAGDTFLHAGISGFQTPAFERLDKHTELMNRLITSAASKSQGDFVNYRNNE 341
Cdd:COG0666   7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 15232175 342 GRTALHLAISGNvPLEFVEMLMSvKSIDINIRDNAGMTPL 381
Cdd:COG0666  87 GNTLLHAAARNG-DLEIVKLLLE-AGADVNARDKDGETPL 124
Ank_5 pfam13857
Ankyrin repeats (many copies);
251-295 2.65e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.25  E-value: 2.65e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 15232175   251 LVDAVDNQGNTALHVAAYRGHADLVDVLIsASPSLISARNNAGDT 295
Cdd:pfam13857   8 DLNRLDGEGYTPLHVAAKYGALEIVRVLL-AYGVDLNLKDEEGLT 51
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 258-285 3.71e-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: 3.71e-04
                           10        20
                   ....*....|....*....|....*...
gi 15232175    258 QGNTALHVAAYRGHADLVDVLISASPSL 285
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
Ank_4 pfam13637
Ankyrin repeats (many copies);
259-303 4.01e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.79  E-value: 4.01e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 15232175   259 GNTALHVAAYRGHADLVDVLISASPSlISARNNAGDTFLHAGISG 303
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGAD-INAVDGNGETALHFAASN 44
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 225-288 9.68e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 42.55  E-value: 9.68e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15232175  225 GSTILHSAAGKGKTQVVKELVASSYHlVDAVDNQGNTALHVAAYRGHADLVDVLISASPSLISA 288
Cdd:PLN03192 622 AGDLLCTAAKRNDLTAMKELLKQGLN-VDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKA 684
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 224-349 1.42e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 41.67  E-value: 1.42e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232175 224 QGSTILHSAAGKGKTQVVKELVASSYHlVDA---------VDNQ-----GNTALHVAAYRGHADLVDVLISASPSLISAR 289
Cdd:cd22194 140 EGQTALNIAIERRQGDIVKLLIAKGAD-VNAhakgvffnpKYKHegfyfGETPLALAACTNQPEIVQLLMEKESTDITSQ 218

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15232175 290 NNAGDTFLHAGISgfqtpAFERLDKHTELMNRLITSAASKSQG-DFVNYRNNEGRTALHLA 349
Cdd:cd22194 219 DSRGNTVLHALVT-----VAEDSKTQNDFVKRMYDMILLKSENkNLETIRNNEGLTPLQLA 274
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 212-383 1.49e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 41.72  E-value: 1.49e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232175 212 CSVEHVLAFRDKQGSTILHSAAGKGKTQVVKELVASSYhlvdaVDN--QGNTALHVAAYRGHADLVDVLISASPSlISAR 289
Cdd:cd22196  50 CLLKAMLNLHNGQNDTISLLLDIAEKTGNLKEFVNAAY-----TDSyyKGQTALHIAIERRNMHLVELLVQNGAD-VHAR 123

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232175 290 NNaGDTF-LHAGISGFQtpaFERLDkhtelmnrlITSAASKSQGDFVNY-------------RNNEGRTALH--LAISGN 353
Cdd:cd22196 124 AS-GEFFkKKKGGPGFY---FGELP---------LSLAACTNQLDIVKFllenphspadisaRDSMGNTVLHalVEVADN 190

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 15232175 354 VP--LEFVEMLMS---VKSIDIN-------IRDNAGMTPLDL 383
Cdd:cd22196 191 TPenTKFVTKMYNeilILGAKIRpllkleeITNKKGLTPLKL 232
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 258-291 2.39e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.11  E-value: 2.39e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 15232175   258 QGNTALHVAAYR-GHADLVDVLISASPSlISARNN 291
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGAD-VNARDK 34
Ank_2 pfam12796
Ankyrin repeats (3 copies);
144-247 2.51e-03

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 37.40  E-value: 2.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232175   144 LYAAARSKNDDVFRLIYDFAVTPrfgtgGIEQQTGEIPaaykwemknraVHSASRGGNLILLKELLsdcsvEHVLAFRDK 223
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADA-----NLQDKNGRTA-----------LHLAAKNGHLEIVKLLL-----EHADVNLKD 59

                          90       100
                  ....*....|....*....|....
gi 15232175   224 QGSTILHSAAGKGKTQVVKELVAS 247
Cdd:pfam12796  60 NGRTALHYAARSGHLEIVKLLLEK 83
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 341-375 2.90e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 35.73  E-value: 2.90e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 15232175   341 EGRTALHLAISGNVPLEFVEMLMSvKSIDINIRDN 375
Cdd:pfam00023   1 DGNTPLHLAAGRRGNLEIVKLLLS-KGADVNARDK 34
Ank_5 pfam13857
Ankyrin repeats (many copies);
208-266 3.27e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.17  E-value: 3.27e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 15232175   208 LLSDCSVEHVLafRDKQGSTILHSAAGKGKTQVVKELVASSYHLvDAVDNQGNTALHVA 266
Cdd:pfam13857   1 LLEHGPIDLNR--LDGEGYTPLHVAAKYGALEIVRVLLAYGVDL-NLKDEEGLTALDLA 56
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 207-416 5.44e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 39.85  E-value: 5.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232175  207 ELLSDCSVEHVlafrDKQGSTILHSAAGKGKTQVVKELVASSYHlVDAVDNQGNTALHVAAYRGHADLVDVLISASPSlI 286
Cdd:PLN03192 511 DLLGDNGGEHD----DPNMASNLLTVASTGNAALLEELLKAKLD-PDIGDSKGRTPLHIAASKGYEDCVLVLLKHACN-V 584

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232175  287 SARNNAGDTFLHAGISGFQTPAFERLDKHTELMN-----RLITSAASKS----------QGDFVNYRNNEGRTALHLAIS 351
Cdd:PLN03192 585 HIRDANGNTALWNAISAKHHKIFRILYHFASISDphaagDLLCTAAKRNdltamkellkQGLNVDSEDHQGATALQVAMA 664

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15232175  352 gNVPLEFVEML-MSVKSID-INIRDNAGMTPLDLIRQK---------PLSPTSDLlfRRLVSAGGMFSCRDQSITS 416
Cdd:PLN03192 665 -EDHVDMVRLLiMNGADVDkANTDDDFSPTELRELLQKrelghsitiVDSVPADE--PDLGRDGGSRPGRLQGTSS 737
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 273-381 7.50e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 39.36  E-value: 7.50e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232175 273 DLVDVLISASpslISARNNAGDTFLHAGIsgfqtpafERldKHTELMNRLITSAA---SKSQGDFVNYRNNE-----GRT 344
Cdd:cd22194 124 GILDRFINAE---YTEEAYEGQTALNIAI--------ER--RQGDIVKLLIAKGAdvnAHAKGVFFNPKYKHegfyfGET 190

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 15232175 345 ALHLAISGNVPlEFVEMLMSVKSIDINIRDNAGMTPL 381
Cdd:cd22194 191 PLALAACTNQP-EIVQLLMEKESTDITSQDSRGNTVL 226
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 238-383 7.79e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 39.09  E-value: 7.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232175  238 TQVVKELVASSYHLVDAVDNQGNTALHVAAYRGHADLVDVLIS--ASPSLISARNNAGdtfLHAGISGFQTPAFERLDKH 315
Cdd:PHA02878 147 AEITKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSygANVNIPDKTNNSP---LHHAVKHYNKPIVHILLEN 223

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15232175  316 telmnrlitsaasksqGDFVNYRNNEGRTALHLAISGNVPLEFVEMLMSvKSIDINIRDNA-GMTPLDL 383
Cdd:PHA02878 224 ----------------GASTDARDKCGNTPLHISVGYCKDYDILKLLLE-HGVDVNAKSYIlGLTALHS 275
 
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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