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Conserved domains on  [gi|46877082|ref|NP_997570|]
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espin isoform 1 [Mus musculus]

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];
52-324 1.14e-40

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 151.65  E-value: 1.14e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46877082  52 LRYLVEEVALPAVSRARNGATPAHDAAATGYLSCLQWLLTQGGCRVQEKDNSGATVLHLAARFGHPDVVKWLLYQGGANS 131
Cdd:COG0666   1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46877082 132 AITTDTGALPIHYAAAKGDLPSLKLLVGHYPEgVNAQTNNGATPLYLACQEGHLEVTKYLVqECSADPHLRAQDGMTPLH 211
Cdd:COG0666  81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGAD-VNARDKDGETPLHLAAYNGNLEIVKLLL-EAGADVNAQDNDGNTPLH 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46877082 212 AAAQMGHNPVLVWLVSF-ADVSfsEQDHDGATAMHFAASRGHTKVLSWLLLHGAEIS-QDLWGGTPLHDAAENGELECCQ 289
Cdd:COG0666 159 LAAANGNLEIVKLLLEAgADVN--ARDNDGETPLHLAAENGHLEIVKLLLEAGADVNaKDNDGKTALDLAAENGNLEIVK 236
                       250       260       270
                ....*....|....*....|....*....|....*
gi 46877082 290 ILAVNGAGLDVRDHDGYTAADLAEFNGHTHCSRYL 324
Cdd:COG0666 237 LLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLL 271
Ank_2 pfam12796
Ankyrin repeats (3 copies);
8-93 4.00e-12

Ankyrin repeats (3 copies);


:

Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 62.83  E-value: 4.00e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46877082     8 QAARRGDLDVLRSLHAAGLlGPSLRDSLDALPVHHAARSGKLHCLRYLVEEValpAVSRARNGATPAHDAAATGYLSCLQ 87
Cdd:pfam12796   3 LAAKNGNLELVKLLLENGA-DANLQDKNGRTALHLAAKNGHLEIVKLLLEHA---DVNLKDNGRTALHYAARSGHLEIVK 78

                  ....*.
gi 46877082    88 WLLTQG 93
Cdd:pfam12796  79 LLLEKG 84
WH2 pfam02205
WH2 motif; The WH2 motif (for Wiskott Aldrich syndrome homology region 2) has been shown in ...
666-691 9.05e-03

WH2 motif; The WH2 motif (for Wiskott Aldrich syndrome homology region 2) has been shown in WASP and Scar1 (mammalian homolog) to be the region that interacts with actin.


:

Pssm-ID: 460490  Cd Length: 28  Bit Score: 34.40  E-value: 9.05e-03
                          10        20
                  ....*....|....*....|....*.
gi 46877082   666 PTGDNSELLAEIKAGKSLKPTPQSKG 691
Cdd:pfam02205   1 GGGGRGALLADIRAGKKLKKVEETND 26
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
52-324 1.14e-40

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 151.65  E-value: 1.14e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46877082  52 LRYLVEEVALPAVSRARNGATPAHDAAATGYLSCLQWLLTQGGCRVQEKDNSGATVLHLAARFGHPDVVKWLLYQGGANS 131
Cdd:COG0666   1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46877082 132 AITTDTGALPIHYAAAKGDLPSLKLLVGHYPEgVNAQTNNGATPLYLACQEGHLEVTKYLVqECSADPHLRAQDGMTPLH 211
Cdd:COG0666  81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGAD-VNARDKDGETPLHLAAYNGNLEIVKLLL-EAGADVNAQDNDGNTPLH 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46877082 212 AAAQMGHNPVLVWLVSF-ADVSfsEQDHDGATAMHFAASRGHTKVLSWLLLHGAEIS-QDLWGGTPLHDAAENGELECCQ 289
Cdd:COG0666 159 LAAANGNLEIVKLLLEAgADVN--ARDNDGETPLHLAAENGHLEIVKLLLEAGADVNaKDNDGKTALDLAAENGNLEIVK 236
                       250       260       270
                ....*....|....*....|....*....|....*
gi 46877082 290 ILAVNGAGLDVRDHDGYTAADLAEFNGHTHCSRYL 324
Cdd:COG0666 237 LLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLL 271
Ank_2 pfam12796
Ankyrin repeats (3 copies);
176-266 2.31e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 86.32  E-value: 2.31e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46877082   176 LYLACQEGHLEVTKYLVqECSADPHLRAQDGMTPLHAAAQMGHNPVLVWLVSFADVsfsEQDHDGATAMHFAASRGHTKV 255
Cdd:pfam12796   1 LHLAAKNGNLELVKLLL-ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV---NLKDNGRTALHYAARSGHLEI 76
                          90
                  ....*....|.
gi 46877082   256 LSWLLLHGAEI 266
Cdd:pfam12796  77 VKLLLEKGADI 87
PHA02874 PHA02874
ankyrin repeat protein; Provisional
94-279 4.77e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 75.39  E-value: 4.77e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46877082   94 GCRVQEKDNSGATVLHLAARFGHPDVVKwLLYQGGANSAITTDTGALPIHYAAAKGDLPSLKLLV--GHYpegVNAQTNN 171
Cdd:PHA02874 114 GIDVNIKDAELKTFLHYAIKKGDLESIK-MLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLekGAY---ANVKDNN 189
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46877082  172 GATPLYLACQEGHLEVTKYLVQECSaDPHLRAQDGMTPLHAAaqMGHNPVLVWLVsFADVSFSEQDHDGATAMHFAASRG 251
Cdd:PHA02874 190 GESPLHNAAEYGDYACIKLLIDHGN-HIMNKCKNGFTPLHNA--IIHNRSAIELL-INNASINDQDIDGSTPLHHAINPP 265
                        170       180       190
                 ....*....|....*....|....*....|
gi 46877082  252 HTK-VLSWLLLHGAEIS-QDLWGGTPLHDA 279
Cdd:PHA02874 266 CDIdIIDILLYHKADISiKDNKGENPIDTA 295
Ank_2 pfam12796
Ankyrin repeats (3 copies);
8-93 4.00e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 62.83  E-value: 4.00e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46877082     8 QAARRGDLDVLRSLHAAGLlGPSLRDSLDALPVHHAARSGKLHCLRYLVEEValpAVSRARNGATPAHDAAATGYLSCLQ 87
Cdd:pfam12796   3 LAAKNGNLELVKLLLENGA-DANLQDKNGRTALHLAAKNGHLEIVKLLLEHA---DVNLKDNGRTALHYAARSGHLEIVK 78

                  ....*.
gi 46877082    88 WLLTQG 93
Cdd:pfam12796  79 LLLEKG 84
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
140-312 1.96e-07

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 54.63  E-value: 1.96e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46877082 140 LPIHYAAAKGDLPSLKLLVGHYPEGVNAQTNNGATPLYLACQEGHLEVTKYLV--------QECSADPHLraqdGMTPLH 211
Cdd:cd22192  19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMeaapelvnEPMTSDLYQ----GETALH 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46877082 212 AAAqMGHNPVLVWLV--SFADVS--------FSEQDHD----GATAMHFAASRGHTKVLSWLLLHGAEI-SQDLWGGTPL 276
Cdd:cd22192  95 IAV-VNQNLNLVRELiaRGADVVspratgtfFRPGPKNliyyGEHPLSFAACVGNEEIVRLLIEHGADIrAQDSLGNTVL 173
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 46877082 277 HD-AAENGELECCQ----ILAV----NGAGLD-VRDHDGYTAADLA 312
Cdd:cd22192 174 HIlVLQPNKTFACQmydlILSYdkedDLQPLDlVPNNQGLTPFKLA 219
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
171-201 8.74e-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: 37.57  E-value: 8.74e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 46877082    171 NGATPLYLACQEGHLEVTKYLVQEcSADPHL 201
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDK-GADINA 30
WH2 pfam02205
WH2 motif; The WH2 motif (for Wiskott Aldrich syndrome homology region 2) has been shown in ...
666-691 9.05e-03

WH2 motif; The WH2 motif (for Wiskott Aldrich syndrome homology region 2) has been shown in WASP and Scar1 (mammalian homolog) to be the region that interacts with actin.


Pssm-ID: 460490  Cd Length: 28  Bit Score: 34.40  E-value: 9.05e-03
                          10        20
                  ....*....|....*....|....*.
gi 46877082   666 PTGDNSELLAEIKAGKSLKPTPQSKG 691
Cdd:pfam02205   1 GGGGRGALLADIRAGKKLKKVEETND 26
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
52-324 1.14e-40

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 151.65  E-value: 1.14e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46877082  52 LRYLVEEVALPAVSRARNGATPAHDAAATGYLSCLQWLLTQGGCRVQEKDNSGATVLHLAARFGHPDVVKWLLYQGGANS 131
Cdd:COG0666   1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46877082 132 AITTDTGALPIHYAAAKGDLPSLKLLVGHYPEgVNAQTNNGATPLYLACQEGHLEVTKYLVqECSADPHLRAQDGMTPLH 211
Cdd:COG0666  81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGAD-VNARDKDGETPLHLAAYNGNLEIVKLLL-EAGADVNAQDNDGNTPLH 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46877082 212 AAAQMGHNPVLVWLVSF-ADVSfsEQDHDGATAMHFAASRGHTKVLSWLLLHGAEIS-QDLWGGTPLHDAAENGELECCQ 289
Cdd:COG0666 159 LAAANGNLEIVKLLLEAgADVN--ARDNDGETPLHLAAENGHLEIVKLLLEAGADVNaKDNDGKTALDLAAENGNLEIVK 236
                       250       260       270
                ....*....|....*....|....*....|....*
gi 46877082 290 ILAVNGAGLDVRDHDGYTAADLAEFNGHTHCSRYL 324
Cdd:COG0666 237 LLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLL 271
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
33-309 2.82e-40

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 150.49  E-value: 2.82e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46877082  33 DSLDALPVHHAARSGKLHCLRYLVEEVALPAVSRARNGATPAHDAAATGYLSCLQWLLTQGGCRVQEKDNSGATVLHLAA 112
Cdd:COG0666  16 LLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAA 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46877082 113 RFGHPDVVKWLLyQGGANSAITTDTGALPIHYAAAKGDLPSLKLLVGHypeG--VNAQTNNGATPLYLACQEGHLEVTKY 190
Cdd:COG0666  96 RNGDLEIVKLLL-EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA---GadVNAQDNDGNTPLHLAAANGNLEIVKL 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46877082 191 LVqECSADPHLRAQDGMTPLHAAAQMGHNPVLVWLVSF-ADVSFseQDHDGATAMHFAASRGHTKVLSWLLLHGAEIS-Q 268
Cdd:COG0666 172 LL-EAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAgADVNA--KDNDGKTALDLAAENGNLEIVKLLLEAGADLNaK 248
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 46877082 269 DLWGGTPLHDAAENGELECCQILAVNGAGLDVRDHDGYTAA 309
Cdd:COG0666 249 DKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
2-277 1.22e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 145.87  E-value: 1.22e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46877082   2 ALEQALQAARRGDLDVLRSLHAAGLLGPSLRDSLDALPVHHAARSGKLHCLRYLVEEVALPAVsRARNGATPAHDAAATG 81
Cdd:COG0666  20 LLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA-KDDGGNTLLHAAARNG 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46877082  82 YLSCLQWLLTQGGcRVQEKDNSGATVLHLAARFGHPDVVKWLLyQGGANSAITTDTGALPIHYAAAKGDLPSLKLLVGHY 161
Cdd:COG0666  99 DLEIVKLLLEAGA-DVNARDKDGETPLHLAAYNGNLEIVKLLL-EAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAG 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46877082 162 PEgVNAQTNNGATPLYLACQEGHLEVTKYLVqECSADPHLRAQDGMTPLHAAAQMGHNPVLVWLVSFADVSfSEQDHDGA 241
Cdd:COG0666 177 AD-VNARDNDGETPLHLAAENGHLEIVKLLL-EAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADL-NAKDKDGL 253
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 46877082 242 TAMHFAASRGHTKVLSWLLLHGAEISQDLWGGTPLH 277
Cdd:COG0666 254 TALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
101-325 1.18e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 140.09  E-value: 1.18e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46877082 101 DNSGATVLHLAARFGHPDVVKWLLYQGGANSAITTDTGALPIHYAAAKGDLPSLKLLVGHYPEGVNAQTNNGATPLYLAC 180
Cdd:COG0666  16 LLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAA 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46877082 181 QEGHLEVTKYLVqECSADPHLRAQDGMTPLHAAAQMGHNPVLVWLVSF-ADVSfsEQDHDGATAMHFAASRGHTKVLSWL 259
Cdd:COG0666  96 RNGDLEIVKLLL-EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAgADVN--AQDNDGNTPLHLAAANGNLEIVKLL 172
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 46877082 260 LLHGAEI-SQDLWGGTPLHDAAENGELECCQILAVNGAGLDVRDHDGYTAADLAEFNGHTHCSRYLR 325
Cdd:COG0666 173 LEAGADVnARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239
Ank_2 pfam12796
Ankyrin repeats (3 copies);
176-266 2.31e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 86.32  E-value: 2.31e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46877082   176 LYLACQEGHLEVTKYLVqECSADPHLRAQDGMTPLHAAAQMGHNPVLVWLVSFADVsfsEQDHDGATAMHFAASRGHTKV 255
Cdd:pfam12796   1 LHLAAKNGNLELVKLLL-ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV---NLKDNGRTALHYAARSGHLEI 76
                          90
                  ....*....|.
gi 46877082   256 LSWLLLHGAEI 266
Cdd:pfam12796  77 VKLLLEKGADI 87
Ank_2 pfam12796
Ankyrin repeats (3 copies);
210-302 2.78e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.55  E-value: 2.78e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46877082   210 LHAAAQMGHNPVLVWLVSfADVSFSEQDHDGATAMHFAASRGHTKVLSWLLLHgAEISQDLWGGTPLHDAAENGELECCQ 289
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLE-NGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGRTALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 46877082   290 ILAVNGAGLDVRD 302
Cdd:pfam12796  79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
108-202 7.14e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.39  E-value: 7.14e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46877082   108 LHLAARFGHPDVVKWLLyQGGANSAITTDTGALPIHYAAAKGDLPSLKLLVGHypEGVNAQtNNGATPLYLACQEGHLEV 187
Cdd:pfam12796   1 LHLAAKNGNLELVKLLL-ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH--ADVNLK-DNGRTALHYAARSGHLEI 76
                          90
                  ....*....|....*
gi 46877082   188 TKYLVqECSADPHLR 202
Cdd:pfam12796  77 VKLLL-EKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
142-227 1.23e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 78.62  E-value: 1.23e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46877082   142 IHYAAAKGDLPSLKLLVgHYPEGVNAQTNNGATPLYLACQEGHLEVTKYLVQECSADphlRAQDGMTPLHAAAQMGHNPV 221
Cdd:pfam12796   1 LHLAAKNGNLELVKLLL-ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN---LKDNGRTALHYAARSGHLEI 76

                  ....*.
gi 46877082   222 LVWLVS 227
Cdd:pfam12796  77 VKLLLE 82
Ank_2 pfam12796
Ankyrin repeats (3 copies);
75-168 2.82e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 71.69  E-value: 2.82e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46877082    75 HDAAATGYLSCLQWLLtQGGCRVQEKDNSGATVLHLAARFGHPDVVKWLLYQGGANSaitTDTGALPIHYAAAKGDLPSL 154
Cdd:pfam12796   2 HLAAKNGNLELVKLLL-ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL---KDNGRTALHYAARSGHLEIV 77
                          90
                  ....*....|....
gi 46877082   155 KLLVGHYPEgVNAQ 168
Cdd:pfam12796  78 KLLLEKGAD-INVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
41-127 4.08e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 71.30  E-value: 4.08e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46877082    41 HHAARSGKLHCLRYLVEEVALPAVSRArNGATPAHDAAATGYLSCLQWLLTQGGCRVQekdNSGATVLHLAARFGHPDVV 120
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENGADANLQDK-NGRTALHLAAKNGHLEIVKLLLEHADVNLK---DNGRTALHYAARSGHLEIV 77

                  ....*..
gi 46877082   121 KWLLYQG 127
Cdd:pfam12796  78 KLLLEKG 84
PHA02874 PHA02874
ankyrin repeat protein; Provisional
94-279 4.77e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 75.39  E-value: 4.77e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46877082   94 GCRVQEKDNSGATVLHLAARFGHPDVVKwLLYQGGANSAITTDTGALPIHYAAAKGDLPSLKLLV--GHYpegVNAQTNN 171
Cdd:PHA02874 114 GIDVNIKDAELKTFLHYAIKKGDLESIK-MLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLekGAY---ANVKDNN 189
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46877082  172 GATPLYLACQEGHLEVTKYLVQECSaDPHLRAQDGMTPLHAAaqMGHNPVLVWLVsFADVSFSEQDHDGATAMHFAASRG 251
Cdd:PHA02874 190 GESPLHNAAEYGDYACIKLLIDHGN-HIMNKCKNGFTPLHNA--IIHNRSAIELL-INNASINDQDIDGSTPLHHAINPP 265
                        170       180       190
                 ....*....|....*....|....*....|
gi 46877082  252 HTK-VLSWLLLHGAEIS-QDLWGGTPLHDA 279
Cdd:PHA02874 266 CDIdIIDILLYHKADISiKDNKGENPIDTA 295
Ank_2 pfam12796
Ankyrin repeats (3 copies);
244-324 1.86e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 66.68  E-value: 1.86e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46877082   244 MHFAASRGHTKVLSWLLLHGAEI-SQDLWGGTPLHDAAENGELECCQILaVNGAGLDVRDHdGYTAADLAEFNGHTHCSR 322
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADAnLQDKNGRTALHLAAKNGHLEIVKLL-LEHADVNLKDN-GRTALHYAARSGHLEIVK 78

                  ..
gi 46877082   323 YL 324
Cdd:pfam12796  79 LL 80
PHA03100 PHA03100
ankyrin repeat protein; Provisional
88-214 7.73e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 71.23  E-value: 7.73e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46877082   88 WLLTQGGCRVQEKDNSGATVLHLAA--RFGHPDVVKWLLyQGGANSAITTDTGALPIHYAAA--KGDLPSLKLLVGH--- 160
Cdd:PHA03100  90 KLLLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEYLL-DNGANVNIKNSDGENLLHLYLEsnKIDLKILKLLIDKgvd 168
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46877082  161 ------------YPEGVNAQTNNGATPLYLACQEGHLEVTKYLVqECSADPHLRAQDGMTPLHAAA 214
Cdd:PHA03100 169 inaknrvnyllsYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLL-DLGANPNLVNKYGDTPLHIAI 233
PHA03095 PHA03095
ankyrin-like protein; Provisional
89-325 1.43e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 70.82  E-value: 1.43e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46877082   89 LLTQGGcRVQEKDNSGATVLHLAARFGHPDVVK--WLLYQGGANSAITTDTGALPIH-YAAAKGDLPSLKLLVGHypeG- 164
Cdd:PHA03095  33 LLAAGA-DVNFRGEYGKTPLHLYLHYSSEKVKDivRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKA---Ga 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46877082  165 -VNAQTNNGATPL--YLACQEGHLEVTKYLVQEcSADPHLRAQDGMTPLHAAaqMGHNPVLVWLVSF---ADVSFSEQDH 238
Cdd:PHA03095 109 dVNAKDKVGRTPLhvYLSGFNINPKVIRLLLRK-GADVNALDLYGMTPLAVL--LKSRNANVELLRLlidAGADVYAVDD 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46877082  239 DGATAMH-FAAS-RGHTKVLSWLLLHGAE-ISQDLWGGTPLHDAAENGEleCCQILAVN----GAGLDVRDHDGYTAADL 311
Cdd:PHA03095 186 RFRSLLHhHLQSfKPRARIVRELIRAGCDpAATDMLGNTPLHSMATGSS--CKRSLVLPlliaGISINARNRYGQTPLHY 263
                        250
                 ....*....|....*
gi 46877082  312 AE-FNGHTHCSRYLR 325
Cdd:PHA03095 264 AAvFNNPRACRRLIA 278
Ank_2 pfam12796
Ankyrin repeats (3 copies);
8-93 4.00e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 62.83  E-value: 4.00e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46877082     8 QAARRGDLDVLRSLHAAGLlGPSLRDSLDALPVHHAARSGKLHCLRYLVEEValpAVSRARNGATPAHDAAATGYLSCLQ 87
Cdd:pfam12796   3 LAAKNGNLELVKLLLENGA-DANLQDKNGRTALHLAAKNGHLEIVKLLLEHA---DVNLKDNGRTALHYAARSGHLEIVK 78

                  ....*.
gi 46877082    88 WLLTQG 93
Cdd:pfam12796  79 LLLEKG 84
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
198-365 4.36e-12

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 69.90  E-value: 4.36e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46877082  198 DPHLRAQDGMTPLHAAAQMGHNP-VLVWLVSFADVSFseQDHDGATAMHFAASRGHTKVLsWLLLHGAEISQDLWGGTPL 276
Cdd:PLN03192 550 DPDIGDSKGRTPLHIAASKGYEDcVLVLLKHACNVHI--RDANGNTALWNAISAKHHKIF-RILYHFASISDPHAAGDLL 626
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46877082  277 HDAAENGELECCQILAVNGAGLDVRDHDGYTAADLAEFNGHTHCSRYLRT----VQTLSLEHRVLSRDQSMDLEAKQLDS 352
Cdd:PLN03192 627 CTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMngadVDKANTDDDFSPTELRELLQKRELGH 706
                        170
                 ....*....|...
gi 46877082  353 GMSSPNTTMSVQP 365
Cdd:PLN03192 707 SITIVDSVPADEP 719
Ank_4 pfam13637
Ankyrin repeats (many copies);
206-260 2.82e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 59.21  E-value: 2.82e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 46877082   206 GMTPLHAAAQMGHNPVLVWLVSFaDVSFSEQDHDGATAMHFAASRGHTKVLSWLL 260
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEK-GADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
72-124 4.44e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.74  E-value: 4.44e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 46877082    72 TPAHDAAATGYLSCLQWLLtQGGCRVQEKDNSGATVLHLAARFGHPDVVKWLL 124
Cdd:pfam13637   3 TALHAAAASGHLELLRLLL-EKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
111-309 6.97e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 61.93  E-value: 6.97e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46877082  111 AARFGHPDVVKWLLyQGGANSAITTDTGALPIHYAAAKGDLPSLKLLVGH--YPegvNAQTNNGATPLYLACQEGHLEVT 188
Cdd:PHA02875   9 AILFGELDIARRLL-DIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHgaIP---DVKYPDIESELHDAVEEGDVKAV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46877082  189 KYLVQECSADPHLRAQDGMTPLHAAAQMGHNPVLVWLVSF-ADVSFSEQDHdgATAMHFAASRGHTKVLSWLLLHGAEIS 267
Cdd:PHA02875  85 EELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARgADPDIPNTDK--FSPLHLAVMMGDIKGIELLIDHKACLD 162
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 46877082  268 -QDLWGGTPLHDAAENGELECCQILAVNGAGLDVRDHDGYTAA 309
Cdd:PHA02875 163 iEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAA 205
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
70-210 1.18e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 62.19  E-value: 1.18e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46877082   70 GATPAHDAAATGYLSCLQWLLTQGgCRVQEKDNSGATVLHLAARFGHPDVVkWLLYQGGANSaiTTDTGALPIHYAAAKG 149
Cdd:PLN03192 558 GRTPLHIAASKGYEDCVLVLLKHA-CNVHIRDANGNTALWNAISAKHHKIF-RILYHFASIS--DPHAAGDLLCTAAKRN 633
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 46877082  150 DLPSLKLLVGHypeGVNAQTNN--GATPLYLACQEGHLEVTKYLVQECSADPHLRAQDGMTPL 210
Cdd:PLN03192 634 DLTAMKELLKQ---GLNVDSEDhqGATALQVAMAEDHVDMVRLLIMNGADVDKANTDDDFSPT 693
PHA02876 PHA02876
ankyrin repeat protein; Provisional
123-279 1.98e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 61.23  E-value: 1.98e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46877082  123 LLYQGGANSAITTDTGALPIHYAAAKgdlPSLKLLVGHYPE---GVNAQTNNGATPLYLACQEGH-LEVTKYLVQEcSAD 198
Cdd:PHA02876 258 LLYDAGFSVNSIDDCKNTPLHHASQA---PSLSRLVPKLLErgaDVNAKNIKGETPLYLMAKNGYdTENIRTLIML-GAD 333
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46877082  199 phLRAQDGM--TPLHAAAQMGHNPVLVWLVSFADVSFSEQDHDGATAMHFAASRGHTKVLSWLLLHGAEI---SQDLwgG 273
Cdd:PHA02876 334 --VNAADRLyiTPLHQASTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIealSQKI--G 409

                 ....*.
gi 46877082  274 TPLHDA 279
Cdd:PHA02876 410 TALHFA 415
Ank_4 pfam13637
Ankyrin repeats (many copies);
141-192 5.34e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.66  E-value: 5.34e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 46877082   141 PIHYAAAKGDLPSLKLLVGHYPEgVNAQTNNGATPLYLACQEGHLEVTKYLV 192
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKGAD-INAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
242-291 1.46e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.51  E-value: 1.46e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 46877082   242 TAMHFAASRGHTKVLSWLLLHGAEIS-QDLWGGTPLHDAAENGELECCQIL 291
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINaVDGNGETALHFAASNGNVEVLKLL 53
Ank_4 pfam13637
Ankyrin repeats (many copies);
106-158 9.51e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.20  E-value: 9.51e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 46877082   106 TVLHLAARFGHPDVVKWLLyQGGANSAITTDTGALPIHYAAAKGDLPSLKLLV 158
Cdd:pfam13637   3 TALHAAAASGHLELLRLLL-EKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
174-226 1.34e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.81  E-value: 1.34e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 46877082   174 TPLYLACQEGHLEVTKYLVQEcSADPHLRAQDGMTPLHAAAQMGHNPVLVWLV 226
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEK-GADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
140-312 1.96e-07

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 54.63  E-value: 1.96e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46877082 140 LPIHYAAAKGDLPSLKLLVGHYPEGVNAQTNNGATPLYLACQEGHLEVTKYLV--------QECSADPHLraqdGMTPLH 211
Cdd:cd22192  19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMeaapelvnEPMTSDLYQ----GETALH 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46877082 212 AAAqMGHNPVLVWLV--SFADVS--------FSEQDHD----GATAMHFAASRGHTKVLSWLLLHGAEI-SQDLWGGTPL 276
Cdd:cd22192  95 IAV-VNQNLNLVRELiaRGADVVspratgtfFRPGPKNliyyGEHPLSFAACVGNEEIVRLLIEHGADIrAQDSLGNTVL 173
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 46877082 277 HD-AAENGELECCQ----ILAV----NGAGLD-VRDHDGYTAADLA 312
Cdd:cd22192 174 HIlVLQPNKTFACQmydlILSYdkedDLQPLDlVPNNQGLTPFKLA 219
PHA03100 PHA03100
ankyrin repeat protein; Provisional
108-307 4.17e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 53.13  E-value: 4.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46877082  108 LHLAARFGHPDVVKWLLYQgGANSAITTDTGALPIHYAA-----AKGDLPSLKLLVgHYPEGVNAQTNNGATPLYLACQE 182
Cdd:PHA03100  39 LYLAKEARNIDVVKILLDN-GADINSSTKNNSTPLHYLSnikynLTDVKEIVKLLL-EYGANVNAPDNNGITPLLYAISK 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46877082  183 --GHLEVTKYLVQEcSADPHLRAQDGMTPLHAAAQMGHNpvlvwlvsfadvsfseqdhdgatamhfaasrgHTKVLSWLL 260
Cdd:PHA03100 117 ksNSYSIVEYLLDN-GANVNIKNSDGENLLHLYLESNKI--------------------------------DLKILKLLI 163
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 46877082  261 LHGAEISQ-----------------DLWGGTPLHDAAENGELECCQILAVNGAGLDVRDHDGYT 307
Cdd:PHA03100 164 DKGVDINAknrvnyllsygvpinikDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDT 227
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
72-260 4.91e-07

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 53.48  E-value: 4.91e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46877082  72 TPAHDAAATGYLSCLQWLLTQGGCRVQEKDNSGATVLHLAARFGHPDVVKWLLYQ--GGANSAITTD--TGALPIHYAAA 147
Cdd:cd22192  19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAapELVNEPMTSDlyQGETALHIAVV 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46877082 148 KGDLPSLKLLVGHYPEGVNAQTNN-------------GATPL-YLACQeGHLEVTKYLVQEcSADphLRAQD--GMTPLH 211
Cdd:cd22192  99 NQNLNLVRELIARGADVVSPRATGtffrpgpknliyyGEHPLsFAACV-GNEEIVRLLIEH-GAD--IRAQDslGNTVLH 174
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 46877082 212 ---------AAAQMgHNPVLVWLVSFADVSFSE-QDHDGATAMHFAASRGHTKVLSWLL 260
Cdd:cd22192 175 ilvlqpnktFACQM-YDLILSYDKEDDLQPLDLvPNNQGLTPFKLAAKEGNIVMFQHLV 232
PHA02875 PHA02875
ankyrin repeat protein; Provisional
13-225 1.08e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 51.92  E-value: 1.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46877082   13 GDLDVLRSLHAAGLlGPSLRDSLDALPVHHAARSGKLHCLRYLVEEVALPAVSRArNGATPAHDAAATGYLSCLQWLLTQ 92
Cdd:PHA02875  13 GELDIARRLLDIGI-NPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYP-DIESELHDAVEEGDVKAVEELLDL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46877082   93 GGCRVQEKDNSGATVLHLAARFGHPDVVKWLLYQGGANSAITTDTGAlPIHYAAAKGDLPSLKLLVGHyPEGVNAQTNNG 172
Cdd:PHA02875  91 GKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFS-PLHLAVMMGDIKGIELLIDH-KACLDIEDCCG 168
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 46877082  173 ATPLYLACQEGHLEVTKYLVqECSADPHLRAQDGMTPLHAAAQMGHNPVLVWL 225
Cdd:PHA02875 169 CTPLIIAMAKGDIAICKMLL-DSGANIDYFGKNGCVAALCYAIENNKIDIVRL 220
Ank_5 pfam13857
Ankyrin repeats (many copies);
259-312 1.12e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.19  E-value: 1.12e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 46877082   259 LLLHGAE--ISQDLWGGTPLHDAAENGELECCQILAVNGAGLDVRDHDGYTAADLA 312
Cdd:pfam13857   1 LLEHGPIdlNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA03100 PHA03100
ankyrin repeat protein; Provisional
94-162 1.25e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 51.97  E-value: 1.25e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 46877082   94 GCRVQEKDNSGATVLHLAARFGHPDVVKWLLYQgGANSAITTDTGALPIHYAAAKGDLPSLKLLVGHYP 162
Cdd:PHA03100 182 GVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDL-GANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249
Ank_4 pfam13637
Ankyrin repeats (many copies);
272-324 1.63e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.73  E-value: 1.63e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 46877082   272 GGTPLHDAAENGELECCQILAVNGAGLDVRDHDGYTAADLAEFNGHTHCSRYL 324
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PHA02874 PHA02874
ankyrin repeat protein; Provisional
48-307 1.86e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 51.12  E-value: 1.86e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46877082   48 KLHCLRYLVEEVAlpavsrarngaTPAHDAAATGYLSCLQWLLtqggcrvqekdNSGATVLHLAARFGHP---------- 117
Cdd:PHA02874  24 KGNCINISVDETT-----------TPLIDAIRSGDAKIVELFI-----------KHGADINHINTKIPHPlltaikigah 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46877082  118 DVVKWLLYQGgansaitTDTGALPIhyAAAKGDLPSLKLLVGhypEGVNAQTNNGATPLYLACQEGHLEVTKYLVqECSA 197
Cdd:PHA02874  82 DIIKLLIDNG-------VDTSILPI--PCIEKDMIKTILDCG---IDVNIKDAELKTFLHYAIKKGDLESIKMLF-EYGA 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46877082  198 DPHLRAQDGMTPLHAAAQmgHNpvlvwlvsfadvSFseqdhdgatamhfaasrghtKVLSWLLLHGAEIS-QDLWGGTPL 276
Cdd:PHA02874 149 DVNIEDDNGCYPIHIAIK--HN------------FF--------------------DIIKLLLEKGAYANvKDNNGESPL 194
                        250       260       270
                 ....*....|....*....|....*....|.
gi 46877082  277 HDAAENGELECCQILAVNGAGLDVRDHDGYT 307
Cdd:PHA02874 195 HNAAEYGDYACIKLLIDHGNHIMNKCKNGFT 225
Ank_4 pfam13637
Ankyrin repeats (many copies);
39-90 3.41e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.96  E-value: 3.41e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 46877082    39 PVHHAARSGKLHCLRYLVEEVALPAVSRaRNGATPAHDAAATGYLSCLQWLL 90
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKGADINAVD-GNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
89-145 4.36e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.64  E-value: 4.36e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 46877082    89 LLTQGGCRVQEKDNSGATVLHLAARFGHPDVVKWLLYQGGANSaITTDTGALPIHYA 145
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLN-LKDEEGLTALDLA 56
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
7-193 1.45e-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: 48.86  E-value: 1.45e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46877082   7 LQAARRGDLDVLRSL--------HAAGLLGPSlrdsldALpvHHAARSGKLHCLRYLVEE----VALPAVSRARNGATPA 74
Cdd:cd22192  22 LLAAKENDVQAIKKLlkcpscdlFQRGALGET------AL--HVAALYDNLEAAVVLMEAapelVNEPMTSDLYQGETAL 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46877082  75 HDAAATGYLSCLQWLLTQGG----------CRVQEKDN---SGATVLHLAARFGHPDVVKwLLYQGGANSAITTDTGALP 141
Cdd:cd22192  94 HIAVVNQNLNLVRELIARGAdvvspratgtFFRPGPKNliyYGEHPLSFAACVGNEEIVR-LLIEHGADIRAQDSLGNTV 172
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 46877082 142 IHYAA-------------------AKGDLPSLKLLvghypegvnaQTNNGATPLYLACQEGHLEVTKYLVQ 193
Cdd:cd22192 173 LHILVlqpnktfacqmydlilsydKEDDLQPLDLV----------PNNQGLTPFKLAAKEGNIVMFQHLVQ 233
PHA02878 PHA02878
ankyrin repeat protein; Provisional
229-360 2.80e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 47.57  E-value: 2.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46877082  229 ADVSFSEQdHDGATAMHFAASRGHTKVLSWLLLHGAEI-SQDLWGGTPLHDAAENGELECCQILAVNGAGLDVRDHDGYT 307
Cdd:PHA02878 158 ADINMKDR-HKGNTALHYATENKDQRLTELLLSYGANVnIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNT 236
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 46877082  308 AADLAEfnghTHCSRYlrTVQTLSLEHRVLSRDQSMDLEAKQLDSGMSSPNTT 360
Cdd:PHA02878 237 PLHISV----GYCKDY--DILKLLLEHGVDVNAKSYILGLTALHSSIKSERKL 283
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
146-234 3.37e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.59  E-value: 3.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46877082  146 AAKGDLPSLKLLV--GHYPegvNAQTNNGATPLYLACQEGHLEVTKYLVqECSADPHLRAQDGMTPLHAAAQMGHNPVLV 223
Cdd:PTZ00322  90 AASGDAVGARILLtgGADP---NCRDYDGRTPLHIACANGHVQVVRVLL-EFGADPTLLDKDGKTPLELAEENGFREVVQ 165
                         90
                 ....*....|.
gi 46877082  224 WLVSFADVSFS 234
Cdd:PTZ00322 166 LLSRHSQCHFE 176
PHA02946 PHA02946
ankyin-like protein; Provisional
90-276 5.05e-05

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 46.59  E-value: 5.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46877082   90 LTQGGCRVQEKDNSGATVLHLAARFGHPDVVKWLLYQGGANSAITTDTGAlPIHYAAAKGD--LPSLKLLVGHYPEGVNA 167
Cdd:PHA02946  58 LLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKT-PLYYLSGTDDevIERINLLVQYGAKINNS 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46877082  168 QTNNGATPLyLACQEGHLEVTKYLVQeCSADPHLRAQDGMTPLHAAAqMGHNP---VLVWLVSFAdVSFSEQDHDGATAM 244
Cdd:PHA02946 137 VDEEGCGPL-LACTDPSERVFKKIMS-IGFEARIVDKFGKNHIHRHL-MSDNPkasTISWMMKLG-ISPSKPDHDGNTPL 212
                        170       180       190
                 ....*....|....*....|....*....|....
gi 46877082  245 HFAASRGHTKV-LSWLLLHGAEIS-QDLWGGTPL 276
Cdd:PHA02946 213 HIVCSKTVKNVdIINLLLPSTDVNkQNKFGDSPL 246
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
197-268 7.91e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.43  E-value: 7.91e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 46877082  197 ADPHLRAQDGMTPLHAAAQMGHNPVLVWLVSF-ADVSFSeqDHDGATAMHFAASRGHTKVLSWLLLHGAEISQ 268
Cdd:PTZ00322 106 ADPNCRDYDGRTPLHIACANGHVQVVRVLLEFgADPTLL--DKDGKTPLELAEENGFREVVQLLSRHSQCHFE 176
PHA03095 PHA03095
ankyrin-like protein; Provisional
66-267 1.83e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 45.02  E-value: 1.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46877082   66 RARNGATPAHdaaatgYLSCLQW------LLTQGGCRVQEKDNSGATVLH--LAARFGHPDVVKWLLyQGGANSAITTDT 137
Cdd:PHA03095  79 PERCGFTPLH------LYLYNATtldvikLLIKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLL-RKGADVNALDLY 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46877082  138 GALPIH-YAAAKG-DLPSLKLLV--GHYPEGVNaqtNNGATPLylacqEGHLEVTK--------YLVQECsaDPHLRAQD 205
Cdd:PHA03095 152 GMTPLAvLLKSRNaNVELLRLLIdaGADVYAVD---DRFRSLL-----HHHLQSFKprarivreLIRAGC--DPAATDML 221
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 46877082  206 GMTPLHAAAQMGHNPVLVwLVSF--ADVSFSEQDHDGATAMHFAASRGHTKVLSWLLLHGAEIS 267
Cdd:PHA03095 222 GNTPLHSMATGSSCKRSL-VLPLliAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADIN 284
PHA02874 PHA02874
ankyrin repeat protein; Provisional
149-326 1.95e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 44.95  E-value: 1.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46877082  149 GDLPSLKLLVGHYPEGVNAQTNNGATPLYLACQEGHLEVTKYLVQECSADPHLRAQDGmTPLHAAAQMGHNPVL-VWLVS 227
Cdd:PHA02874  12 GDIEAIEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIP-HPLLTAIKIGAHDIIkLLIDN 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46877082  228 FADVSF---------------------SEQDHDGATAMHFAASRGHTKVLSWLLLHGAEIS-QDLWGGTPLHDAAENGEL 285
Cdd:PHA02874  91 GVDTSIlpipciekdmiktildcgidvNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNiEDDNGCYPIHIAIKHNFF 170
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 46877082  286 ECCQILAVNGAGLDVRDHDGYTAADLAEFNGHTHCSRYLRT 326
Cdd:PHA02874 171 DIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLID 211
PHA02875 PHA02875
ankyrin repeat protein; Provisional
150-324 1.98e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 44.60  E-value: 1.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46877082  150 DLPSLKLLVGHYPegvNAQTNNGATPLYLACQEGHLEVTKYLVQEcSADPHLRAQDGMTPLHAAAQMGHN---PVLVWLV 226
Cdd:PHA02875  16 DIARRLLDIGINP---NFEIYDGISPIKLAMKFRDSEAIKLLMKH-GAIPDVKYPDIESELHDAVEEGDVkavEELLDLG 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46877082  227 SFADVSFSEqdhDGATAMHFAASRGHTKVLSWLLLHGAEI---SQDLWggTPLHDAAENGELECCQILAVNGAGLDVRDH 303
Cdd:PHA02875  92 KFADDVFYK---DGMTPLHLATILKKLDIMKLLIARGADPdipNTDKF--SPLHLAVMMGDIKGIELLIDHKACLDIEDC 166
                        170       180
                 ....*....|....*....|.
gi 46877082  304 DGYTAADLAEFNGHTHCSRYL 324
Cdd:PHA02875 167 CGCTPLIIAMAKGDIAICKML 187
PHA03100 PHA03100
ankyrin repeat protein; Provisional
68-193 2.19e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 44.66  E-value: 2.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46877082   68 RNGATPAHDAAAT--GYLSCLQWLLtQGGCRVQEKDNSGATVLHLAARFGHPD--VVKWLLYQG---------------G 128
Cdd:PHA03100 104 NNGITPLLYAISKksNSYSIVEYLL-DNGANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKGvdinaknrvnyllsyG 182
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46877082  129 ANSAITTDTGALPIHYAAAKGDLPSLKLLVgHYPEGVNAQTNNGATPLYLACQEGHLEVTKYLVQ 193
Cdd:PHA03100 183 VPINIKDVYGFTPLHYAVYNNNPEFVKYLL-DLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLN 246
Ank_4 pfam13637
Ankyrin repeats (many copies);
8-56 2.81e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.57  E-value: 2.81e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 46877082     8 QAARRGDLDVLRSLHAAGLLgPSLRDSLDALPVHHAARSGKLHCLRYLV 56
Cdd:pfam13637   7 AAAASGHLELLRLLLEKGAD-INAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
191-247 4.17e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.87  E-value: 4.17e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 46877082   191 LVQECSADPHLRAQDGMTPLHAAAQMGHNPVLVWLVSFaDVSFSEQDHDGATAMHFA 247
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAY-GVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
245-372 6.81e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 43.35  E-value: 6.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46877082  245 HFAASrGHTKVLSWLLLHGAEI-SQDLWGGTPLHDAAENGELECCQILAVNGAGLDVRDHDGYTAADLAEFNGHTHCSRY 323
Cdd:PTZ00322  88 QLAAS-GDAVGARILLTGGADPnCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 46877082  324 LRTVQTLSLEHRVLSRDQSMD-LEAKQLDSGMSS--PNTTMSVQPMtfdLGS 372
Cdd:PTZ00322 167 LSRHSQCHFELGANAKPDSFTgKPPSLEDSPISShhPDFSAVPQPM---MGS 215
Ank_5 pfam13857
Ankyrin repeats (many copies);
123-179 8.06e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.10  E-value: 8.06e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 46877082   123 LLYQGGANSAITTDTGALPIHYAAAKGDLPSLKLLVGhYPEGVNAQTNNGATPLYLA 179
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLA-YGVDLNLKDEEGLTALDLA 56
PHA02878 PHA02878
ankyrin repeat protein; Provisional
118-294 8.43e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 42.95  E-value: 8.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46877082  118 DVVKWLLYQGGANSAITTDTGALPIHYAAAKGDLPSLKLLVGhYPEGVNAQTNNGATPLYLACQEGHLEVTKYLVQECSA 197
Cdd:PHA02878 148 EITKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLS-YGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAS 226
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46877082  198 DPHlRAQDGMTPLHAAAQMGHNPVLVWLVSFADVSFSEQDH-DGATAMHFAASrgHTKVLSWLLLHGAEI-SQDLWGGTP 275
Cdd:PHA02878 227 TDA-RDKCGNTPLHISVGYCKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIK--SERKLKLLLEYGADInSLNSYKLTP 303
                        170       180
                 ....*....|....*....|
gi 46877082  276 LHDAAEN-GELECCQILAVN 294
Cdd:PHA02878 304 LSSAVKQyLCINIGRILISN 323
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
171-201 8.74e-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: 37.57  E-value: 8.74e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 46877082    171 NGATPLYLACQEGHLEVTKYLVQEcSADPHL 201
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDK-GADINA 30
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
80-260 1.02e-03

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 42.56  E-value: 1.02e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46877082  80 TGYLSCLQWLLTQggcRVQEKDNSGATVLHLAARFGHPDVVK--WLLYQGGANS--------AITTDT---GALPIHYAA 146
Cdd:cd21882   5 LGLLECLRWYLTD---SAYQRGATGKTCLHKAALNLNDGVNEaiMLLLEAAPDSgnpkelvnAPCTDEfyqGQTALHIAI 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46877082 147 AKGDLPSLKLLVGHYPEgVNAQTNN-------------GATPLYLACQEGHLEVTKYLVQEcSADPH-LRAQD--GMTPL 210
Cdd:cd21882  82 ENRNLNLVRLLVENGAD-VSARATGrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLEN-GAQPAaLEAQDslGNTVL 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46877082 211 HA--------------AAQMgHNPVLVW------LVSFADVSfseqDHDGATAMHFAASRGHTKVLSWLL 260
Cdd:cd21882 160 HAlvlqadntpensafVCQM-YNLLLSYgahldpTQQLEEIP----NHQGLTPLKLAAVEGKIVMFQHIL 224
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
239-267 1.22e-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: 36.85  E-value: 1.22e-03
                          10        20
                  ....*....|....*....|....*....
gi 46877082   239 DGATAMHFAASRGHTKVLSWLLLHGAEIS 267
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
Ank_5 pfam13857
Ankyrin repeats (many copies);
55-111 1.28e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.71  E-value: 1.28e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 46877082    55 LVEEVALPAVSRARNGATPAHDAAATGYLSCLQWLLTqGGCRVQEKDNSGATVLHLA 111
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLA-YGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
89-188 1.36e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 42.19  E-value: 1.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46877082   89 LLTQGGCRVQEKDNSGATVLHLAARFGHPDVVKWLLyQGGANSAITTDTGALPIHYAAAKGDLPSLKLLVGHYPEGVNAQ 168
Cdd:PTZ00322 100 ILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLL-EFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELG 178
                         90       100
                 ....*....|....*....|
gi 46877082  169 TNngATPLYLACQEGHLEVT 188
Cdd:PTZ00322 179 AN--AKPDSFTGKPPSLEDS 196
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
104-124 1.76e-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: 36.47  E-value: 1.76e-03
                          10        20
                  ....*....|....*....|.
gi 46877082   104 GATVLHLAARFGHPDVVKWLL 124
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLL 22
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
104-128 3.67e-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: 35.64  E-value: 3.67e-03
                           10        20
                   ....*....|....*....|....*
gi 46877082    104 GATVLHLAARFGHPDVVKWLLYQGG 128
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGA 26
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
239-266 4.56e-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: 35.26  E-value: 4.56e-03
                           10        20
                   ....*....|....*....|....*...
gi 46877082    239 DGATAMHFAASRGHTKVLSWLLLHGAEI 266
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
PHA02875 PHA02875
ankyrin repeat protein; Provisional
183-316 4.62e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 40.36  E-value: 4.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46877082  183 GHLEVTKYLVqECSADPHLRAQDGMTPLHAAAQMGHNPVLVWLVSFADVSfSEQDHDGATAMHFAASRGHTKVLSWLLLH 262
Cdd:PHA02875  13 GELDIARRLL-DIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIP-DVKYPDIESELHDAVEEGDVKAVEELLDL 90
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 46877082  263 GAEISQDLW--GGTPLHDAAENGELECCQILAVNGAGLDVRDHDGYTAADLAEFNG 316
Cdd:PHA02875  91 GKFADDVFYkdGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMG 146
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
104-136 5.42e-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: 5.42e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 46877082   104 GATVLHLAA-RFGHPDVVKWLLyQGGANSAITTD 136
Cdd:pfam00023   2 GNTPLHLAAgRRGNLEIVKLLL-SKGADVNARDK 34
Ank_5 pfam13857
Ankyrin repeats (many copies);
157-213 5.62e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.79  E-value: 5.62e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 46877082   157 LVGHYPEGVNAQTNNGATPLYLACQEGHLEVTKYLVqECSADPHLRAQDGMTPLHAA 213
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLL-AYGVDLNLKDEEGLTALDLA 56
PHA02876 PHA02876
ankyrin repeat protein; Provisional
72-267 6.92e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 40.05  E-value: 6.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46877082   72 TPAHDAAATGYLSCLQWLLTQGGCRVQEKDNSGATVLHLAARFGHPDVVKWLLYQGGANSAITTDTGALPIHYAAAKGDL 151
Cdd:PHA02876 275 TPLHHASQAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYDTENIRTLIMLGADVNAADRLYITPLHQASTLDRN 354
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46877082  152 PSLKLLVGHYPEGVNAQTNNGATPLYLACQEGHLEVTKYLVqECSADPHLRAQDGMTPLHAAAqMGHNPVL-VWLVSFAD 230
Cdd:PHA02876 355 KDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLL-DYGADIEALSQKIGTALHFAL-CGTNPYMsVKTLIDRG 432
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 46877082  231 VSFSEQDHDGATAMHFAASRG-HTKVLSWLLLHGAEIS 267
Cdd:PHA02876 433 ANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVN 470
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
171-202 7.73e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 34.96  E-value: 7.73e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 46877082   171 NGATPLYLAC-QEGHLEVTKYLVQeCSADPHLR 202
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLS-KGADVNAR 32
WH2 pfam02205
WH2 motif; The WH2 motif (for Wiskott Aldrich syndrome homology region 2) has been shown in ...
666-691 9.05e-03

WH2 motif; The WH2 motif (for Wiskott Aldrich syndrome homology region 2) has been shown in WASP and Scar1 (mammalian homolog) to be the region that interacts with actin.


Pssm-ID: 460490  Cd Length: 28  Bit Score: 34.40  E-value: 9.05e-03
                          10        20
                  ....*....|....*....|....*.
gi 46877082   666 PTGDNSELLAEIKAGKSLKPTPQSKG 691
Cdd:pfam02205   1 GGGGRGALLADIRAGKKLKKVEETND 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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