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Conserved domains on  [gi|15229233|ref|NP_187064|]
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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];
83-412 3.03e-24

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 103.50  E-value: 3.03e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229233  83 LLEECEIGNGDNSLIRAGYGGWLLYTAASAGDLEFVKKLLERDPLLVFGEGEYGVTDILYAAARGRSDDVFRLLLDFALL 162
Cdd:COG0666   1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229233 163 PADIAGVEEIdgekltekqlivkeemvkrgVHSAARGGHVAILDELLlanKYDAVAKLRDAYGSTLLHSASSRAQIQVVK 242
Cdd:COG0666  81 NAKDDGGNTL--------------------LHAAARNGDLEIVKLLL---EAGADVNARDKDGETPLHLAAYNGNLEIVK 137

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229233 243 YLISKYDSImEVKDSHGNTALHIAAYKGHLDVVEALInESPPLISIVNGDGDTFLHtvvsgfAASGFKRLdrqmELLKML 322
Cdd:COG0666 138 LLLEAGADV-NAQDNDGNTPLHLAAANGNLEIVKLLL-EAGADVNARDNDGETPLH------LAAENGHL----EIVKLL 205

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229233 323 VSRswSVDfseiVNVRNCNGRTVIHLAVMDNlnavRPDVVEILMRIpGVDLNVVDSYGMTAVDLLKRQTPQTVVSDLLIK 402
Cdd:COG0666 206 LEA--GAD----VNAKDNDGKTALDLAAENG----NLEIVKLLLEA-GADLNAKDKDGLTALLLAAAAGAALIVKLLLLA 274

                       330
                ....*....|
gi 15229233 403 RLVSAGGRSN 412
Cdd:COG0666 275 LLLLAAALLD 284
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
83-412 3.03e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 103.50  E-value: 3.03e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229233  83 LLEECEIGNGDNSLIRAGYGGWLLYTAASAGDLEFVKKLLERDPLLVFGEGEYGVTDILYAAARGRSDDVFRLLLDFALL 162
Cdd:COG0666   1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229233 163 PADIAGVEEIdgekltekqlivkeemvkrgVHSAARGGHVAILDELLlanKYDAVAKLRDAYGSTLLHSASSRAQIQVVK 242
Cdd:COG0666  81 NAKDDGGNTL--------------------LHAAARNGDLEIVKLLL---EAGADVNARDKDGETPLHLAAYNGNLEIVK 137

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229233 243 YLISKYDSImEVKDSHGNTALHIAAYKGHLDVVEALInESPPLISIVNGDGDTFLHtvvsgfAASGFKRLdrqmELLKML 322
Cdd:COG0666 138 LLLEAGADV-NAQDNDGNTPLHLAAANGNLEIVKLLL-EAGADVNARDNDGETPLH------LAAENGHL----EIVKLL 205

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229233 323 VSRswSVDfseiVNVRNCNGRTVIHLAVMDNlnavRPDVVEILMRIpGVDLNVVDSYGMTAVDLLKRQTPQTVVSDLLIK 402
Cdd:COG0666 206 LEA--GAD----VNAKDNDGKTALDLAAENG----NLEIVKLLLEA-GADLNAKDKDGLTALLLAAAAGAALIVKLLLLA 274

                       330
                ....*....|
gi 15229233 403 RLVSAGGRSN 412
Cdd:COG0666 275 LLLLAAALLD 284
Ank_2 pfam12796
Ankyrin repeats (3 copies);
194-280 1.15e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.46  E-value: 1.15e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229233   194 HSAARGGHVAILdELLLANKYDAvaKLRDAYGSTLLHSASSRAQIQVVKYLISKYDSIMevkDSHGNTALHIAAYKGHLD 273
Cdd:pfam12796   2 HLAAKNGNLELV-KLLLENGADA--NLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL---KDNGRTALHYAARSGHLE 75


                  ....*..
gi 15229233   274 VVEALIN 280
Cdd:pfam12796  76 IVKLLLE 82
PHA03095 PHA03095
ankyrin-like protein; Provisional
 233-408 4.11e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 62.35  E-value: 4.11e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229233  233 SSRAQIQVVKYLIsKYDSIMEVKDSHGNTALHIAAYKGH---LDVVEALINESppliSIVNGD---GDTFLHTVVsgfaa 306
Cdd:PHA03095  22 ASNVTVEEVRRLL-AAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAG----ADVNAPercGFTPLHLYL----- 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229233  307 sgfkRLDRQMELLKMLVSRSwsVDfseiVNVRNCNGRTVIHlAVMDNLNaVRPDVVEILMRIpGVDLNVVDSYGMTAVD- 385
Cdd:PHA03095  92 ----YNATTLDVIKLLIKAG--AD----VNAKDKVGRTPLH-VYLSGFN-INPKVIRLLLRK-GADVNALDLYGMTPLAv 158

                        170       180
                 ....*....|....*....|...
gi 15229233  386 LLKRqtpqTVVSDLLIKRLVSAG 408
Cdd:PHA03095 159 LLKS----RNANVELLRLLIDAG 177
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 258-283 2.37e-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: 2.37e-05
                           10        20
                   ....*....|....*....|....*.
gi 15229233    258 HGNTALHIAAYKGHLDVVEALINESP 283
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGA 26
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 226-396 7.46e-04

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: 42.69  E-value: 7.46e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229233 226 STLLHSASSRAQIQVVKYLISKYDSIMEVKDSHGNTALHIAAYKGHLDVVEALINESPPLISI-VNGD---GDTFLHTVV 301
Cdd:cd22192  18 ESPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEpMTSDlyqGETALHIAV 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229233 302 sgfaasgfkrLDRQMELLKMLVSRSWSVdfseiVNVRNCN-------------GRTVIHLAVMDNLNavrpDVVEILMRi 368
Cdd:cd22192  98 ----------VNQNLNLVRELIARGADV-----VSPRATGtffrpgpknliyyGEHPLSFAACVGNE----EIVRLLIE- 157

                       170       180
                ....*....|....*....|....*...
gi 15229233 369 PGVDLNVVDSYGMTAVDLLKRQTPQTVV 396
Cdd:cd22192 158 HGADIRAQDSLGNTVLHILVLQPNKTFA 185
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
83-412 3.03e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 103.50  E-value: 3.03e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229233  83 LLEECEIGNGDNSLIRAGYGGWLLYTAASAGDLEFVKKLLERDPLLVFGEGEYGVTDILYAAARGRSDDVFRLLLDFALL 162
Cdd:COG0666   1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229233 163 PADIAGVEEIdgekltekqlivkeemvkrgVHSAARGGHVAILDELLlanKYDAVAKLRDAYGSTLLHSASSRAQIQVVK 242
Cdd:COG0666  81 NAKDDGGNTL--------------------LHAAARNGDLEIVKLLL---EAGADVNARDKDGETPLHLAAYNGNLEIVK 137

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229233 243 YLISKYDSImEVKDSHGNTALHIAAYKGHLDVVEALInESPPLISIVNGDGDTFLHtvvsgfAASGFKRLdrqmELLKML 322
Cdd:COG0666 138 LLLEAGADV-NAQDNDGNTPLHLAAANGNLEIVKLLL-EAGADVNARDNDGETPLH------LAAENGHL----EIVKLL 205

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229233 323 VSRswSVDfseiVNVRNCNGRTVIHLAVMDNlnavRPDVVEILMRIpGVDLNVVDSYGMTAVDLLKRQTPQTVVSDLLIK 402
Cdd:COG0666 206 LEA--GAD----VNAKDNDGKTALDLAAENG----NLEIVKLLLEA-GADLNAKDKDGLTALLLAAAAGAALIVKLLLLA 274

                       330
                ....*....|
gi 15229233 403 RLVSAGGRSN 412
Cdd:COG0666 275 LLLLAAALLD 284
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
51-298 6.22e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 99.64  E-value: 6.22e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229233  51 SLRRIRRLETVWDDGDGNNFHVALNRSRVARRLLEECEIGNGDNSLIRAGYGGWLLYTAASAGDLEFVKKLLERDPLLVF 130
Cdd:COG0666   2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229233 131 GEGEYGVTDILYAAARGRsDDVFRLLLDfalLPADIAGVEEIDGEKLtekqlivkeemvkrgvHSAARGGHVAILdELLL 210
Cdd:COG0666  82 AKDDGGNTLLHAAARNGD-LEIVKLLLE---AGADVNARDKDGETPL----------------HLAAYNGNLEIV-KLLL 140

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229233 211 ANKydAVAKLRDAYGSTLLHSASSRAQIQVVKYLISKYDSImEVKDSHGNTALHIAAYKGHLDVVEALInESPPLISIVN 290
Cdd:COG0666 141 EAG--ADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADV-NARDNDGETPLHLAAENGHLEIVKLLL-EAGADVNAKD 216


                ....*...
gi 15229233 291 GDGDTFLH 298
Cdd:COG0666 217 NDGKTALD 224
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
26-298 2.45e-21

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 94.64  E-value: 2.45e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229233  26 AAANGLYDVVIELLHQDTNLLVKLTSLRRIRRLETVWDDGDGNNFHVALNRSRVARRLLEeceIGNGDNSLIRAGYGGWL 105
Cdd:COG0666  14 ALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLL---LAAGADINAKDDGGNTL 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229233 106 LYTAASAGDLEFVKKLLER--DPLLVFGEGEYgvtdILYAAARGRSDDVFRLLLDfallpadiAG--VEEIDGEKLTekq 181
Cdd:COG0666  91 LHAAARNGDLEIVKLLLEAgaDVNARDKDGET----PLHLAAYNGNLEIVKLLLE--------AGadVNAQDNDGNT--- 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229233 182 LIvkeemvkrgvHSAARGGHVAILdELLLANKYDAVAklRDAYGSTLLHSASSRAQIQVVKYLIsKYDSIMEVKDSHGNT 261
Cdd:COG0666 156 PL----------HLAAANGNLEIV-KLLLEAGADVNA--RDNDGETPLHLAAENGHLEIVKLLL-EAGADVNAKDNDGKT 221

                       250       260       270
                ....*....|....*....|....*....|....*..
gi 15229233 262 ALHIAAYKGHLDVVEALInESPPLISIVNGDGDTFLH 298
Cdd:COG0666 222 ALDLAAENGNLEIVKLLL-EAGADLNAKDKDGLTALL 257
Ank_2 pfam12796
Ankyrin repeats (3 copies);
194-280 1.15e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.46  E-value: 1.15e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229233   194 HSAARGGHVAILdELLLANKYDAvaKLRDAYGSTLLHSASSRAQIQVVKYLISKYDSIMevkDSHGNTALHIAAYKGHLD 273
Cdd:pfam12796   2 HLAAKNGNLELV-KLLLENGADA--NLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL---KDNGRTALHYAARSGHLE 75


                  ....*..
gi 15229233   274 VVEALIN 280
Cdd:pfam12796  76 IVKLLLE 82
PHA03095 PHA03095
ankyrin-like protein; Provisional
 233-408 4.11e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 62.35  E-value: 4.11e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229233  233 SSRAQIQVVKYLIsKYDSIMEVKDSHGNTALHIAAYKGH---LDVVEALINESppliSIVNGD---GDTFLHTVVsgfaa 306
Cdd:PHA03095  22 ASNVTVEEVRRLL-AAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAG----ADVNAPercGFTPLHLYL----- 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229233  307 sgfkRLDRQMELLKMLVSRSwsVDfseiVNVRNCNGRTVIHlAVMDNLNaVRPDVVEILMRIpGVDLNVVDSYGMTAVD- 385
Cdd:PHA03095  92 ----YNATTLDVIKLLIKAG--AD----VNAKDKVGRTPLH-VYLSGFN-INPKVIRLLLRK-GADVNALDLYGMTPLAv 158

                        170       180
                 ....*....|....*....|...
gi 15229233  386 LLKRqtpqTVVSDLLIKRLVSAG 408
Cdd:PHA03095 159 LLKS----RNANVELLRLLIDAG 177
Ank_2 pfam12796
Ankyrin repeats (3 copies);
229-325 2.23e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 54.74  E-value: 2.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229233   229 LHSASSRAQIQVVKYLIsKYDSIMEVKDSHGNTALHIAAYKGHLDVVEALINESPPLIsivNGDGDTFLHtvvsgFAASG 308
Cdd:pfam12796   1 LHLAAKNGNLELVKLLL-ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL---KDNGRTALH-----YAARS 71

                          90
                  ....*....|....*..
gi 15229233   309 fkrldRQMELLKMLVSR 325
Cdd:pfam12796  72 -----GHLEIVKLLLEK 83
Ank_4 pfam13637
Ankyrin repeats (many copies);
225-279 2.71e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.35  E-value: 2.71e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 15229233   225 GSTLLHSASSRAQIQVVKYLISKYDSIMEVkDSHGNTALHIAAYKGHLDVVEALI 279
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAV-DGNGETALHFAASNGNVEVLKLLL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 207-336 1.17e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 51.20  E-value: 1.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229233  207 ELLLanKYDAVAKLRDAYGSTLLHSASSRAQIQVVKYLISKYDSImEVKDSHGNTALHIAAYKGHLDVVEALINeSPPLI 286
Cdd:PHA03100 176 NYLL--SYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANP-NLVNKYGDTPLHIAILNNNKEIFKLLLN-NGPSI 251

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15229233  287 SIVNG----DGDTFLHTVVSgfaASGFKRLDRQMELL--------KMLVSrswSVDFSEIVN 336
Cdd:PHA03100 252 KTIIEtllyFKDKDLNTITK---IKMLKKSIMYMFLLdpgfyknrKLIEN---SKSLKDVIN 307
Ank_4 pfam13637
Ankyrin repeats (many copies);
259-323 1.24e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.73  E-value: 1.24e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15229233   259 GNTALHIAAYKGHLDVVEALInESPPLISIVNGDGDTFLHtvvsgFAASGfkrldRQMELLKMLV 323
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLL-EKGADINAVDGNGETALH-----FAASN-----GNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 207-387 1.30e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 51.18  E-value: 1.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229233  207 ELLLANKYDAVAklRDAYGSTLLHS--ASSRAQIQVVKYLISKYDSIMEVkDSHGNTALHIAA--YKGHLDVVEALInES 282
Cdd:PHA03095 136 RLLLRKGADVNA--LDLYGMTPLAVllKSRNANVELLRLLIDAGADVYAV-DDRFRSLLHHHLqsFKPRARIVRELI-RA 211

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229233  283 PPLISIVNGDGDTFLHTVVSGfaaSGFKRLDRQMELLKMLvsrswsvdfseIVNVRNCNGRTVIHLA-VMDNLNAVRPdv 361
Cdd:PHA03095 212 GCDPAATDMLGNTPLHSMATG---SSCKRSLVLPLLIAGI-----------SINARNRYGQTPLHYAaVFNNPRACRR-- 275

                        170       180
                 ....*....|....*....|....*.
gi 15229233  362 veiLMRIpGVDLNVVDSYGMTAVDLL 387
Cdd:PHA03095 276 ---LIAL-GADINAVSSDGNTPLSLM 297
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 184-405 1.20e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 48.06  E-value: 1.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229233  184 VKEEMVKRGVHSAARGGHVAILDELLLANKY--DAVAKlrdaYGSTLLHSASSRAQIQVVKYLIsKYDSIMEVKDSHGNT 261
Cdd:PHA02875  63 VKYPDIESELHDAVEEGDVKAVEELLDLGKFadDVFYK----DGMTPLHLATILKKLDIMKLLI-ARGADPDIPNTDKFS 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229233  262 ALHIAAYKGHLDVVEALINESPPLiSIVNGDGDTFLHTVVSgfaasgfkrlDRQMELLKMLVSRSWSVDFseiVNVRNCn 341
Cdd:PHA02875 138 PLHLAVMMGDIKGIELLIDHKACL-DIEDCCGCTPLIIAMA----------KGDIAICKMLLDSGANIDY---FGKNGC- 202

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15229233  342 gRTVIHLAVMDNlnavRPDVVEILMRiPGVDLNV---VDSYGMTAVDLLKRQ--TPQTVVSDLLIKRLV 405
Cdd:PHA02875 203 -VAALCYAIENN----KIDIVRLFIK-RGADCNImfmIEGEECTILDMICNMctNLESEAIDALIADIA 265
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 207-298 1.63e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 47.74  E-value: 1.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229233  207 ELLLANKYDAvaKLRDAYGSTLLHSA--SSRAQIQVVKYLISK---------------YDSIMEVKDSHGNTALHIAAYK 269
Cdd:PHA03100 125 EYLLDNGANV--NIKNSDGENLLHLYleSNKIDLKILKLLIDKgvdinaknrvnyllsYGVPINIKDVYGFTPLHYAVYN 202

                         90       100
                 ....*....|....*....|....*....
gi 15229233  270 GHLDVVEALINESPPlISIVNGDGDTFLH 298
Cdd:PHA03100 203 NNPEFVKYLLDLGAN-PNLVNKYGDTPLH 230
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 258-283 2.37e-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: 2.37e-05
                           10        20
                   ....*....|....*....|....*.
gi 15229233    258 HGNTALHIAAYKGHLDVVEALINESP 283
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGA 26
Ank_2 pfam12796
Ankyrin repeats (3 copies);
106-219 7.09e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 42.03  E-value: 7.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229233   106 LYTAASAGDLEFVKKLLER--DPLLVFGEGEYgvtdILYAAARGRSDDVFRLLLDFAllpadiagveeiDGEKLTEKQLI 183
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENgaDANLQDKNGRT----ALHLAAKNGHLEIVKLLLEHA------------DVNLKDNGRTA 64

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 15229233   184 vkeemvkrgVHSAARGGHVAILdELLLANKYDAVAK 219
Cdd:pfam12796  65 ---------LHYAARSGHLEIV-KLLLEKGADINVK 90
Ank_4 pfam13637
Ankyrin repeats (many copies);
193-245 7.15e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 40.72  E-value: 7.15e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 15229233   193 VHSAARGGHVAILDeLLLANKYDAVAklRDAYGSTLLHSASSRAQIQVVKYLI 245
Cdd:pfam13637   5 LHAAAASGHLELLR-LLLEKGADINA--VDGNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
141-251 1.45e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 40.87  E-value: 1.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229233   141 LYAAARGRSDDVFRLLLDFallpadIAGVEEIDGEKLTekqlivkeemvkrGVHSAARGGHVAILDELLlankyDAVAKL 220
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLEN------GADANLQDKNGRT-------------ALHLAAKNGHLEIVKLLL-----EHADVN 56

                          90       100       110
                  ....*....|....*....|....*....|.
gi 15229233   221 RDAYGSTLLHSASSRAQIQVVKYLISKYDSI 251
Cdd:pfam12796  57 LKDNGRTALHYAARSGHLEIVKLLLEKGADI 87
Ank_5 pfam13857
Ankyrin repeats (many copies);
244-295 1.59e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.02  E-value: 1.59e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 15229233   244 LISKYDSIMEVKDSHGNTALHIAAYKGHLDVVEALINEsPPLISIVNGDGDT 295
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAY-GVDLNLKDEEGLT 51
Ank_5 pfam13857
Ankyrin repeats (many copies);
331-386 1.87e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.64  E-value: 1.87e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 15229233   331 FSEIVNVRNCNGRTVIHLAVmdnlNAVRPDVVEILMrIPGVDLNVVDSYGMTAVDL 386
Cdd:pfam13857   5 GPIDLNRLDGEGYTPLHVAA----KYGALEIVRVLL-AYGVDLNLKDEEGLTALDL 55
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 193-298 2.99e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 43.80  E-value: 2.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229233  193 VHSAARGGHVAILdELLLANkyDAVAKLRDAYGSTLLHSASSRAQIQVVKYLISKYDSIMeVKDSHGNTALHIAAYKGHl 272
Cdd:PHA02874 161 IHIAIKHNFFDII-KLLLEK--GAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIM-NKCKNGFTPLHNAIIHNR- 235

                         90       100
                 ....*....|....*....|....*.
gi 15229233  273 DVVEALINESPplISIVNGDGDTFLH 298
Cdd:PHA02874 236 SAIELLINNAS--INDQDIDGSTPLH 259
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 258-280 3.43e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.42  E-value: 3.43e-04
                          10        20
                  ....*....|....*....|....
gi 15229233   258 HGNTALHIAAYK-GHLDVVEALIN 280
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLS 24
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 220-382 4.19e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 43.41  E-value: 4.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229233  220 LRDAYGSTLLHSASSRAQIQVVKYLIsKYDSIMEVKDSHGNTALHIAAYKGHLDVVEALInESPPLISIVNGDGDTFLHT 299
Cdd:PHA02874 119 IKDAELKTFLHYAIKKGDLESIKMLF-EYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLL-EKGAYANVKDNNGESPLHN 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229233  300 VVSGFAASGFKRLdrqmellkmlvsrswsVDFSEIVNVRNCNGRTVIHLAVMDNLNavrpdVVEILmrIPGVDLNVVDSY 379
Cdd:PHA02874 197 AAEYGDYACIKLL----------------IDHGNHIMNKCKNGFTPLHNAIIHNRS-----AIELL--INNASINDQDID 253


                 ...
gi 15229233  380 GMT 382
Cdd:PHA02874 254 GST 256
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 258-280 7.37e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.24  E-value: 7.37e-04
                          10        20
                  ....*....|....*....|...
gi 15229233   258 HGNTALHIAAYKGHLDVVEALIN 280
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLE 23
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 226-396 7.46e-04

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: 42.69  E-value: 7.46e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229233 226 STLLHSASSRAQIQVVKYLISKYDSIMEVKDSHGNTALHIAAYKGHLDVVEALINESPPLISI-VNGD---GDTFLHTVV 301
Cdd:cd22192  18 ESPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEpMTSDlyqGETALHIAV 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229233 302 sgfaasgfkrLDRQMELLKMLVSRSWSVdfseiVNVRNCN-------------GRTVIHLAVMDNLNavrpDVVEILMRi 368
Cdd:cd22192  98 ----------VNQNLNLVRELIARGADV-----VSPRATGtffrpgpknliyyGEHPLSFAACVGNE----EIVRLLIE- 157

                       170       180
                ....*....|....*....|....*...
gi 15229233 369 PGVDLNVVDSYGMTAVDLLKRQTPQTVV 396
Cdd:cd22192 158 HGADIRAQDSLGNTVLHILVLQPNKTFA 185
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 223-349 9.70e-04

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 42.44  E-value: 9.70e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229233 223 AY-GSTLLHSASSRAQIQVVKYLISKYDSI--------MEVKDSH-----GNTALHIAAYKGHLDVVEALINESPPLISI 288
Cdd:cd22194 138 AYeGQTALNIAIERRQGDIVKLLIAKGADVnahakgvfFNPKYKHegfyfGETPLALAACTNQPEIVQLLMEKESTDITS 217

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15229233 289 VNGDGDTFLHTVVSgfAASGFK-RLDRQMELLKMLVSRS--WSVDfseivNVRNCNGRTVIHLA 349
Cdd:cd22194 218 QDSRGNTVLHALVT--VAEDSKtQNDFVKRMYDMILLKSenKNLE-----TIRNNEGLTPLQLA 274
Ank_2 pfam12796
Ankyrin repeats (3 copies);
70-158 1.26e-03

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 38.56  E-value: 1.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229233    70 FHVA--LNRSRVARRLLEE-CEIGNGDNSLIRAgyggwlLYTAASAGDLEFVKKLLERDPLLVFGEGEygvtDILYAAAR 146
Cdd:pfam12796   1 LHLAakNGNLELVKLLLENgADANLQDKNGRTA------LHLAAKNGHLEIVKLLLEHADVNLKDNGR----TALHYAAR 70

                          90
                  ....*....|..
gi 15229233   147 GRSDDVFRLLLD 158
Cdd:pfam12796  71 SGHLEIVKLLLE 82
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 195-271 1.31e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 42.16  E-value: 1.31e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15229233  195 SAARGGHVAILDELLLANKYdavAKLRDAYGSTLLHSASSRAQIQVVKYLIsKYDSIMEVKDSHGNTALHIAAYKGH 271
Cdd:PLN03192 531 TVASTGNAALLEELLKAKLD---PDIGDSKGRTPLHIAASKGYEDCVLVLL-KHACNVHIRDANGNTALWNAISAKH 603
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 194-278 3.36e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 40.65  E-value: 3.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229233  194 HSAARGGHVAIldELLLANKYDAvaKLRDAYGSTLLHSASSRAQIQVVKYLIsKYDSIMEVKDSHGNTALHIAAYKGHLD 273
Cdd:PTZ00322  88 QLAASGDAVGA--RILLTGGADP--NCRDYDGRTPLHIACANGHVQVVRVLL-EFGADPTLLDKDGKTPLELAEENGFRE 162


                 ....*
gi 15229233  274 VVEAL 278
Cdd:PTZ00322 163 VVQLL 167
PHA03095 PHA03095
ankyrin-like protein; Provisional
 202-364 4.80e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 40.01  E-value: 4.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229233  202 VAILDELLLANKYDAVaklRDAYGSTLLHS--ASSRAQIQVVKYLISKYDSIMEVkDSHGNTALHIAAYKG---HLDVVE 276
Cdd:PHA03095 167 VELLRLLIDAGADVYA---VDDRFRSLLHHhlQSFKPRARIVRELIRAGCDPAAT-DMLGNTPLHSMATGSsckRSLVLP 242

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229233  277 ALINESPplISIVNGDGDTFLHtvvsgfAASGFkrlDRQM---ELLKMLVSrswsvdfseiVNVRNCNGRTVIHLAVMDN 353
Cdd:PHA03095 243 LLIAGIS--INARNRYGQTPLH------YAAVF---NNPRacrRLIALGAD----------INAVSSDGNTPLSLMVRNN 301

                        170
                 ....*....|....*...
gi 15229233  354 ----LNAV---RPDVVEI 364
Cdd:PHA03095 302 ngraVRAAlakNPSAETV 319
Ank_5 pfam13857
Ankyrin repeats (many copies);
210-266 5.77e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.40  E-value: 5.77e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 15229233   210 LANKYDAVAKLRDAYGSTLLHSASSRAQIQVVKYLIsKYDSIMEVKDSHGNTALHIA 266
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLL-AYGVDLNLKDEEGLTALDLA 56
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 207-382 9.11e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 39.09  E-value: 9.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229233  207 ELLLANKYDAVAKLRDAYGSTLLHSASSRAQIqvVKYLISkYDSIMEVKDSH-GNTALHIAAYKGHLDVVEALI------ 279
Cdd:PHA02878 118 KIILTNRYKNIQTIDLVYIDKKSKDDIIEAEI--TKLLLS-YGADINMKDRHkGNTALHYATENKDQRLTELLLsyganv 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229233  280 ------NESP----------PLISIV--NGD--------GDTFLHTVVSGFaasgfkrldRQMELLKMLVSRSWSVDF-S 332
Cdd:PHA02878 195 nipdktNNSPlhhavkhynkPIVHILleNGAstdardkcGNTPLHISVGYC---------KDYDILKLLLEHGVDVNAkS 265

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 15229233  333 EIVNVrncngrTVIHLAVMDnlnavrPDVVEILMRIpGVDLNVVDSYGMT 382
Cdd:PHA02878 266 YILGL------TALHSSIKS------ERKLKLLLEY-GADINSLNSYKLT 302
 
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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