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Conserved domains on  [gi|12053261|emb|CAB66814|]
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hypothetical protein [Homo sapiens]

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];
2-277 3.84e-42

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 155.88  E-value: 3.84e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261   2 ALEQALQAARQGELDVLRSLHAAGLLGPSLRDPLDALPVHHAARAGKLHcLRFLVEEAALPAAARARNGATPAHDASATG 81
Cdd:COG0666  20 LLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLL-VALLLLAAGADINAKDDGGNTLLHAAARNG 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261  82 HLACLQWLLSQGGcRVQDKDNSGATVLHLAARFGHPEVVNWLLHHgGGDPTAATDMGALPIHYAAAKGDFPSLRLLVEHY 161
Cdd:COG0666  99 DLEIVKLLLEAGA-DVNARDKDGETPLHLAAYNGNLEIVKLLLEA-GADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAG 176

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261 162 PEgVNAQTKNGATPLYLACQEGHLEVTQYLVqECGADPHARAHDGMTPLHAAAQMGHSPVIVWLVScTDVSLSEQDKDGA 241
Cdd:COG0666 177 AD-VNARDNDGETPLHLAAENGHLEIVKLLL-EAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE-AGADLNAKDKDGL 253

                       250       260       270
                ....*....|....*....|....*....|....*.
gi 12053261 242 TAMHFAASRGHTKVLSWLLLHGGEISADLWGGTPLH 277
Cdd:COG0666 254 TALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PLN03192 super family cl33658
Voltage-dependent potassium channel; Provisional
 196-365 2.20e-10

Voltage-dependent potassium channel; Provisional


The actual alignment was detected with superfamily member PLN03192:

Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 64.50  E-value: 2.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261  196 GADPHARAHDGMTPLHAAAQMGHSP-VIVWLVSCTDVSLseQDKDGATAMHFAASRGHTKVLsWLLLHGGEISADLWGGT 274
Cdd:PLN03192 548 KLDPDIGDSKGRTPLHIAASKGYEDcVLVLLKHACNVHI--RDANGNTALWNAISAKHHKIF-RILYHFASISDPHAAGD 624

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261  275 PLHDAAENGELECCQILVVNGAELDVRDRDGYTAADLSDFNGHSHCTRYLrTVENLSVEHRVLSRDPSAE-----LEAKQ 349
Cdd:PLN03192 625 LLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLL-IMNGADVDKANTDDDFSPTelrelLQKRE 703

                        170
                 ....*....|....*.
gi 12053261  350 PDSGMSSPNTTVSVQP 365
Cdd:PLN03192 704 LGHSITIVDSVPADEP 719
WH2 pfam02205
WH2 motif; The WH2 motif (for Wiskott Aldrich syndrome homology region 2) has been shown in ...
 648-673 4.97e-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: 35.17  E-value: 4.97e-03
                          10        20
                  ....*....|....*....|....*.
gi 12053261   648 PTGDNSELLAEIKAGKSLKPTPQSKG 673
Cdd:pfam02205   1 GGGGRGALLADIRAGKKLKKVEETND 26
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
2-277 3.84e-42

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 155.88  E-value: 3.84e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261   2 ALEQALQAARQGELDVLRSLHAAGLLGPSLRDPLDALPVHHAARAGKLHcLRFLVEEAALPAAARARNGATPAHDASATG 81
Cdd:COG0666  20 LLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLL-VALLLLAAGADINAKDDGGNTLLHAAARNG 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261  82 HLACLQWLLSQGGcRVQDKDNSGATVLHLAARFGHPEVVNWLLHHgGGDPTAATDMGALPIHYAAAKGDFPSLRLLVEHY 161
Cdd:COG0666  99 DLEIVKLLLEAGA-DVNARDKDGETPLHLAAYNGNLEIVKLLLEA-GADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAG 176

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261 162 PEgVNAQTKNGATPLYLACQEGHLEVTQYLVqECGADPHARAHDGMTPLHAAAQMGHSPVIVWLVScTDVSLSEQDKDGA 241
Cdd:COG0666 177 AD-VNARDNDGETPLHLAAENGHLEIVKLLL-EAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE-AGADLNAKDKDGL 253

                       250       260       270
                ....*....|....*....|....*....|....*.
gi 12053261 242 TAMHFAASRGHTKVLSWLLLHGGEISADLWGGTPLH 277
Cdd:COG0666 254 TALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
Ank_2 pfam12796
Ankyrin repeats (3 copies);
210-302 2.36e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 86.32  E-value: 2.36e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261   210 LHAAAQMGHSPVIVWLVSCtDVSLSEQDKDGATAMHFAASRGHTKVLSWLLLHGgEISADLWGGTPLHDAAENGELECCQ 289
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLEN-GADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 12053261   290 ILVVNGAELDVRD 302
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 89-325 6.33e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 75.06  E-value: 6.33e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261   89 LLSQGGcRVQDKDNSGATVLHLAARFGHP---EVVNWLLHhGGGDPTAATDMGALPIH-YAAAKGDFPSLRLLVEHypeG 164
Cdd:PHA03095  33 LLAAGA-DVNFRGEYGKTPLHLYLHYSSEkvkDIVRLLLE-AGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKA---G 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261  165 --VNAQTKNGATPL--YLACQEGHLEVTQYLVQEcGADPHARAHDGMTPLHAaaqmghspvivwLVSCTDVSL------- 233
Cdd:PHA03095 108 adVNAKDKVGRTPLhvYLSGFNINPKVIRLLLRK-GADVNALDLYGMTPLAV------------LLKSRNANVellrlli 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261  234 ------SEQDKDGATAMH-FAAS-RGHTKVLSWLLLHGGEISA-DLWGGTPLHDAAENGelECCQILVVN----GAELDV 300
Cdd:PHA03095 175 dagadvYAVDDRFRSLLHhHLQSfKPRARIVRELIRAGCDPAAtDMLGNTPLHSMATGS--SCKRSLVLPlliaGISINA 252

                        250       260
                 ....*....|....*....|....*.
gi 12053261  301 RDRDGYTAADL-SDFNGHSHCTRYLR 325
Cdd:PHA03095 253 RNRYGQTPLHYaAVFNNPRACRRLIA 278
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 196-365 2.20e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 64.50  E-value: 2.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261  196 GADPHARAHDGMTPLHAAAQMGHSP-VIVWLVSCTDVSLseQDKDGATAMHFAASRGHTKVLsWLLLHGGEISADLWGGT 274
Cdd:PLN03192 548 KLDPDIGDSKGRTPLHIAASKGYEDcVLVLLKHACNVHI--RDANGNTALWNAISAKHHKIF-RILYHFASISDPHAAGD 624

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261  275 PLHDAAENGELECCQILVVNGAELDVRDRDGYTAADLSDFNGHSHCTRYLrTVENLSVEHRVLSRDPSAE-----LEAKQ 349
Cdd:PLN03192 625 LLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLL-IMNGADVDKANTDDDFSPTelrelLQKRE 703

                        170
                 ....*....|....*.
gi 12053261  350 PDSGMSSPNTTVSVQP 365
Cdd:PLN03192 704 LGHSITIVDSVPADEP 719
Ank_4 pfam13637
Ankyrin repeats (many copies);
272-324 1.92e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.42  E-value: 1.92e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 12053261   272 GGTPLHDAAENGELECCQILVVNGAELDVRDRDGYTAADLSDFNGHSHCTRYL 324
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 72-211 1.11e-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: 1.11e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261  72 TPAHDASATGHLACLQWLLSQGGCRVQDKDNSGATVLHLAARFGHPEVVNWLLHhggGDPT-----AATDM--GALPIHY 144
Cdd:cd22192  19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME---AAPElvnepMTSDLyqGETALHI 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261 145 AAAKGDFPSLRLLVEHYPEGVNAQT---------KN----GATPL-YLACQeGHLEVTQYLVQEcGADPHARAHDGMTPL 210
Cdd:cd22192  96 AVVNQNLNLVRELIARGADVVSPRAtgtffrpgpKNliyyGEHPLsFAACV-GNEEIVRLLIEH-GADIRAQDSLGNTVL 173


                .
gi 12053261 211 H 211
Cdd:cd22192 174 H 174
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 171-201 3.91e-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: 38.34  E-value: 3.91e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 12053261    171 NGATPLYLACQEGHLEVTQYLVQEcGADPHA 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 ...
 648-673 4.97e-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: 35.17  E-value: 4.97e-03
                          10        20
                  ....*....|....*....|....*.
gi 12053261   648 PTGDNSELLAEIKAGKSLKPTPQSKG 673
Cdd:pfam02205   1 GGGGRGALLADIRAGKKLKKVEETND 26
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
2-277 3.84e-42

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 155.88  E-value: 3.84e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261   2 ALEQALQAARQGELDVLRSLHAAGLLGPSLRDPLDALPVHHAARAGKLHcLRFLVEEAALPAAARARNGATPAHDASATG 81
Cdd:COG0666  20 LLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLL-VALLLLAAGADINAKDDGGNTLLHAAARNG 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261  82 HLACLQWLLSQGGcRVQDKDNSGATVLHLAARFGHPEVVNWLLHHgGGDPTAATDMGALPIHYAAAKGDFPSLRLLVEHY 161
Cdd:COG0666  99 DLEIVKLLLEAGA-DVNARDKDGETPLHLAAYNGNLEIVKLLLEA-GADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAG 176

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261 162 PEgVNAQTKNGATPLYLACQEGHLEVTQYLVqECGADPHARAHDGMTPLHAAAQMGHSPVIVWLVScTDVSLSEQDKDGA 241
Cdd:COG0666 177 AD-VNARDNDGETPLHLAAENGHLEIVKLLL-EAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE-AGADLNAKDKDGL 253

                       250       260       270
                ....*....|....*....|....*....|....*.
gi 12053261 242 TAMHFAASRGHTKVLSWLLLHGGEISADLWGGTPLH 277
Cdd:COG0666 254 TALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
33-309 5.14e-42

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 155.50  E-value: 5.14e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261  33 DPLDALPVHHAARAGKLHCLRFLVEEAALPAAARARNGATPAHDASATGHLACLQWLLSQGGCRVQDKDNSGATVLHLAA 112
Cdd:COG0666  16 LLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAA 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261 113 RFGHPEVVNWLLHHgGGDPTAATDMGALPIHYAAAKGDFPSLRLLVEHypeG--VNAQTKNGATPLYLACQEGHLEVTQY 190
Cdd:COG0666  96 RNGDLEIVKLLLEA-GADVNARDKDGETPLHLAAYNGNLEIVKLLLEA---GadVNAQDNDGNTPLHLAAANGNLEIVKL 171

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261 191 LVqECGADPHARAHDGMTPLHAAAQMGHSPVIVWLVScTDVSLSEQDKDGATAMHFAASRGHTKVLSWLLLHGGEISA-D 269
Cdd:COG0666 172 LL-EAGADVNARDNDGETPLHLAAENGHLEIVKLLLE-AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAkD 249

                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 12053261 270 LWGGTPLHDAAENGELECCQILVVNGAELDVRDRDGYTAA 309
Cdd:COG0666 250 KDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
52-324 1.29e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 154.34  E-value: 1.29e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261  52 LRFLVEEAALPAAARARNGATPAHDASATGHLACLQWLLSQGGCRVQDKDNSGATVLHLAARFGHPEVVNWLLHHGGGDP 131
Cdd:COG0666   1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261 132 TAATDMGALPIHYAAAKGDFPSLRLLVEHYPEgVNAQTKNGATPLYLACQEGHLEVTQYLVqECGADPHARAHDGMTPLH 211
Cdd:COG0666  81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGAD-VNARDKDGETPLHLAAYNGNLEIVKLLL-EAGADVNAQDNDGNTPLH 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261 212 AAAQMGHSPVIVWLVSCtDVSLSEQDKDGATAMHFAASRGHTKVLSWLLLHGGEISA-DLWGGTPLHDAAENGELECCQI 290
Cdd:COG0666 159 LAAANGNLEIVKLLLEA-GADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAkDNDGKTALDLAAENGNLEIVKL 237

                       250       260       270
                ....*....|....*....|....*....|....
gi 12053261 291 LVVNGAELDVRDRDGYTAADLSDFNGHSHCTRYL 324
Cdd:COG0666 238 LLEAGADLNAKDKDGLTALLLAAAAGAALIVKLL 271
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
99-325 2.53e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 142.02  E-value: 2.53e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261  99 DKDNSGATVLHLAARFGHPEVVNWLLHHGGGDPTAATDMGALPIHYAAAKGDFPSLRLLVEHYPEGVNAQTKNGATPLYL 178
Cdd:COG0666  14 ALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHA 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261 179 ACQEGHLEVTQYLVqECGADPHARAHDGMTPLHAAAQMGHSPVIVWLVSCtDVSLSEQDKDGATAMHFAASRGHTKVLSW 258
Cdd:COG0666  94 AARNGDLEIVKLLL-EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA-GADVNAQDNDGNTPLHLAAANGNLEIVKL 171

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 12053261 259 LLLHGGEISA-DLWGGTPLHDAAENGELECCQILVVNGAELDVRDRDGYTAADLSDFNGHSHCTRYLR 325
Cdd:COG0666 172 LLEAGADVNArDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239
Ank_2 pfam12796
Ankyrin repeats (3 copies);
210-302 2.36e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 86.32  E-value: 2.36e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261   210 LHAAAQMGHSPVIVWLVSCtDVSLSEQDKDGATAMHFAASRGHTKVLSWLLLHGgEISADLWGGTPLHDAAENGELECCQ 289
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLEN-GADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 12053261   290 ILVVNGAELDVRD 302
Cdd:pfam12796  79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
176-268 2.82e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 83.24  E-value: 2.82e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261   176 LYLACQEGHLEVTQYLVqECGADPHARAHDGMTPLHAAAQMGHSPVIVWLVSCTDVSLSEqdkDGATAMHFAASRGHTKV 255
Cdd:pfam12796   1 LHLAAKNGNLELVKLLL-ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD---NGRTALHYAARSGHLEI 76

                          90
                  ....*....|...
gi 12053261   256 LSWLLLHGGEISA 268
Cdd:pfam12796  77 VKLLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
108-202 6.83e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 82.09  E-value: 6.83e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261   108 LHLAARFGHPEVVNWLLHHgGGDPTAATDMGALPIHYAAAKGDFPSLRLLVEHypEGVNAQTkNGATPLYLACQEGHLEV 187
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLEN-GADANLQDKNGRTALHLAAKNGHLEIVKLLLEH--ADVNLKD-NGRTALHYAARSGHLEI 76

                          90
                  ....*....|....*
gi 12053261   188 TQYLVqECGADPHAR 202
Cdd:pfam12796  77 VKLLL-EKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
142-228 1.12e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 78.62  E-value: 1.12e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261   142 IHYAAAKGDFPSLRLLVEHyPEGVNAQTKNGATPLYLACQEGHLEVTQYLVQECGADphaRAHDGMTPLHAAAQMGHSPV 221
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLEN-GADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN---LKDNGRTALHYAARSGHLEI 76


                  ....*..
gi 12053261   222 IVWLVSC 228
Cdd:pfam12796  77 VKLLLEK 83
Ank_2 pfam12796
Ankyrin repeats (3 copies);
41-127 1.09e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.84  E-value: 1.09e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261    41 HHAARAGKLHCLRFLVEEAALPAAARArNGATPAHDASATGHLACLQWLLSQGgcrVQDKDNSGATVLHLAARFGHPEVV 120
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENGADANLQDK-NGRTALHLAAKNGHLEIVKLLLEHA---DVNLKDNGRTALHYAARSGHLEIV 77


                  ....*..
gi 12053261   121 NWLLHHG 127
Cdd:pfam12796  78 KLLLEKG 84
Ank_2 pfam12796
Ankyrin repeats (3 copies);
75-168 1.86e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 69.37  E-value: 1.86e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261    75 HDASATGHLACLQWLLsQGGCRVQDKDNSGATVLHLAARFGHPEVVNWLLHHGGGDptaATDMGALPIHYAAAKGDFPSL 154
Cdd:pfam12796   2 HLAAKNGNLELVKLLL-ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN---LKDNGRTALHYAARSGHLEIV 77

                          90
                  ....*....|....
gi 12053261   155 RLLVEHYPEgVNAQ 168
Cdd:pfam12796  78 KLLLEKGAD-INVK 90
PHA03095 PHA03095
ankyrin-like protein; Provisional
 89-325 6.33e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 75.06  E-value: 6.33e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261   89 LLSQGGcRVQDKDNSGATVLHLAARFGHP---EVVNWLLHhGGGDPTAATDMGALPIH-YAAAKGDFPSLRLLVEHypeG 164
Cdd:PHA03095  33 LLAAGA-DVNFRGEYGKTPLHLYLHYSSEkvkDIVRLLLE-AGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKA---G 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261  165 --VNAQTKNGATPL--YLACQEGHLEVTQYLVQEcGADPHARAHDGMTPLHAaaqmghspvivwLVSCTDVSL------- 233
Cdd:PHA03095 108 adVNAKDKVGRTPLhvYLSGFNINPKVIRLLLRK-GADVNALDLYGMTPLAV------------LLKSRNANVellrlli 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261  234 ------SEQDKDGATAMH-FAAS-RGHTKVLSWLLLHGGEISA-DLWGGTPLHDAAENGelECCQILVVN----GAELDV 300
Cdd:PHA03095 175 dagadvYAVDDRFRSLLHhHLQSfKPRARIVRELIRAGCDPAAtDMLGNTPLHSMATGS--SCKRSLVLPlliaGISINA 252

                        250       260
                 ....*....|....*....|....*.
gi 12053261  301 RDRDGYTAADL-SDFNGHSHCTRYLR 325
Cdd:PHA03095 253 RNRYGQTPLHYaAVFNNPRACRRLIA 278
PHA03095 PHA03095
ankyrin-like protein; Provisional
 89-345 4.53e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 72.36  E-value: 4.53e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261   89 LLSQGGCRVQDKDNSGATVLHLAARFGH-PEVVNWLLHHGGgDPTAATDMGALPIH-YAAAKG-DFPSLRLLVEHypeG- 164
Cdd:PHA03095  68 LLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAGA-DVNAKDKVGRTPLHvYLSGFNiNPKVIRLLLRK---Ga 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261  165 -VNAQTKNGATPL--YLACQEGHLEVTQYLVqECGADPHARAHDGMTPLHAAAQMGH-SPVIVWLVSCTDVSLSEQDKDG 240
Cdd:PHA03095 144 dVNALDLYGMTPLavLLKSRNANVELLRLLI-DAGADVYAVDDRFRSLLHHHLQSFKpRARIVRELIRAGCDPAATDMLG 222

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261  241 ATAMHFAASRGHTK--VLSWLLLHGGEISA-DLWGGTPLHDAAENGELECCQILVVNGAELDVRDRDGYTAADLSDFNGH 317
Cdd:PHA03095 223 NTPLHSMATGSSCKrsLVLPLLIAGISINArNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNN 302

                        250       260
                 ....*....|....*....|....*...
gi 12053261  318 SHCTRylrtvenlsvehRVLSRDPSAEL 345
Cdd:PHA03095 303 GRAVR------------AALAKNPSAET 318
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 94-267 8.65e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 71.15  E-value: 8.65e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261   94 GCRVQDKDNSGATVLHLAARFGHPEVVNWLLHHgGGDPTAATDMGALPIHYAAAKGDFPSLRLLVEH--YpegVNAQTKN 171
Cdd:PHA02874 114 GIDVNIKDAELKTFLHYAIKKGDLESIKMLFEY-GADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKgaY---ANVKDNN 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261  172 GATPLYLACQEGHLEVTQYLVQEcGADPHARAHDGMTPLHAAAQMGHSpVIVWLVSctDVSLSEQDKDGATAMHFAASRG 251
Cdd:PHA02874 190 GESPLHNAAEYGDYACIKLLIDH-GNHIMNKCKNGFTPLHNAIIHNRS-AIELLIN--NASINDQDIDGSTPLHHAINPP 265

                        170
                 ....*....|....*..
gi 12053261  252 HTK-VLSWLLLHGGEIS 267
Cdd:PHA02874 266 CDIdIIDILLYHKADIS 282
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 70-223 1.09e-12

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 71.82  E-value: 1.09e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261   70 GATPAHDASATGHLACLQWLLSQGgCRVQDKDNSGATVLHLAARFGHPEVVnWLLHH--GGGDPTAATDMGALpihyAAA 147
Cdd:PLN03192 558 GRTPLHIAASKGYEDCVLVLLKHA-CNVHIRDANGNTALWNAISAKHHKIF-RILYHfaSISDPHAAGDLLCT----AAK 631

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261  148 KGDFPSLRLLVEHypeGVNAQTKN--GATPLYLACQEGHLEVTQYLVQEcGAD-PHARAHDGMTP-----LHAAAQMGHS 219
Cdd:PLN03192 632 RNDLTAMKELLKQ---GLNVDSEDhqGATALQVAMAEDHVDMVRLLIMN-GADvDKANTDDDFSPtelreLLQKRELGHS 707


                 ....
gi 12053261  220 PVIV 223
Cdd:PLN03192 708 ITIV 711
Ank_4 pfam13637
Ankyrin repeats (many copies);
206-260 1.18e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 60.37  E-value: 1.18e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 12053261   206 GMTPLHAAAQMGHSPVIVWLVsCTDVSLSEQDKDGATAMHFAASRGHTKVLSWLL 260
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLL-EKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
8-101 2.89e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 60.51  E-value: 2.89e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261     8 QAARQGELDVLRSLHAAGLlGPSLRDPLDALPVHHAARAGKLHCLRFLVEEaalPAAARARNGATPAHDASATGHLACLQ 87
Cdd:pfam12796   3 LAAKNGNLELVKLLLENGA-DANLQDKNGRTALHLAAKNGHLEIVKLLLEH---ADVNLKDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|....
gi 12053261    88 WLLSQgGCRVQDKD 101
Cdd:pfam12796  79 LLLEK-GADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 88-230 5.57e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 65.46  E-value: 5.57e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261   88 WLLSQGGCRVQDKDNSGATVLHLAA--RFGHPEVVNWLLHHGGgDPTAATDMGALPIHYAAA--KGDFPSLRLLVEH--- 160
Cdd:PHA03100  90 KLLLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNGA-NVNIKNSDGENLLHLYLEsnKIDLKILKLLIDKgvd 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261  161 ------------YPEGVNAQTKNGATPLYLACQEGHLEVTQYLVqECGADPHARAHDGMTPLHAAAQMGHSPVIVWLVSC 228
Cdd:PHA03100 169 inaknrvnyllsYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLL-DLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNN 247


                 ..
gi 12053261  229 TD 230
Cdd:PHA03100 248 GP 249
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 196-365 2.20e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 64.50  E-value: 2.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261  196 GADPHARAHDGMTPLHAAAQMGHSP-VIVWLVSCTDVSLseQDKDGATAMHFAASRGHTKVLsWLLLHGGEISADLWGGT 274
Cdd:PLN03192 548 KLDPDIGDSKGRTPLHIAASKGYEDcVLVLLKHACNVHI--RDANGNTALWNAISAKHHKIF-RILYHFASISDPHAAGD 624

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261  275 PLHDAAENGELECCQILVVNGAELDVRDRDGYTAADLSDFNGHSHCTRYLrTVENLSVEHRVLSRDPSAE-----LEAKQ 349
Cdd:PLN03192 625 LLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLL-IMNGADVDKANTDDDFSPTelrelLQKRE 703

                        170
                 ....*....|....*.
gi 12053261  350 PDSGMSSPNTTVSVQP 365
Cdd:PLN03192 704 LGHSITIVDSVPADEP 719
Ank_4 pfam13637
Ankyrin repeats (many copies);
174-226 3.69e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 56.13  E-value: 3.69e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 12053261   174 TPLYLACQEGHLEVTQYLVQEcGADPHARAHDGMTPLHAAAQMGHSPVIVWLV 226
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEK-GADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 48-307 4.31e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 62.67  E-value: 4.31e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261   48 KLHCLRFLVEEAalpaaararngATPAHDASATGHLACLQWLLsqggcrvqdkdNSGATVLHLAARFGHP---------- 117
Cdd:PHA02874  24 KGNCINISVDET-----------TTPLIDAIRSGDAKIVELFI-----------KHGADINHINTKIPHPlltaikigah 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261  118 EVVNWLLHHGggdptaaTDMGALPIhyaaakgdfPSLR--LLVEHYPEGVNAQTKNG--ATPLYLACQEGHLEVTQYLVq 193
Cdd:PHA02874  82 DIIKLLIDNG-------VDTSILPI---------PCIEkdMIKTILDCGIDVNIKDAelKTFLHYAIKKGDLESIKMLF- 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261  194 ECGADPHARAHDGMTPLHAAAQMGHSPVIVWLVScTDVSLSEQDKDGATAMHFAASRGHTKVLSWLLLHGGEISADLWGG 273
Cdd:PHA02874 145 EYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLE-KGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNG 223

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 12053261  274 -TPLHDAA--ENGELEccqiLVVNGAELDVRDRDGYT 307
Cdd:PHA02874 224 fTPLHNAIihNRSAIE----LLINNASINDQDIDGST 256
Ank_4 pfam13637
Ankyrin repeats (many copies);
141-192 1.18e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.59  E-value: 1.18e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 12053261   141 PIHYAAAKGDFPSLRLLVEHYPEgVNAQTKNGATPLYLACQEGHLEVTQYLV 192
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKGAD-INAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
72-124 1.60e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.20  E-value: 1.60e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 12053261    72 TPAHDASATGHLACLQWLLSQGgCRVQDKDNSGATVLHLAARFGHPEVVNWLL 124
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKG-ADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 76-309 2.78e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 60.00  E-value: 2.78e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261   76 DASATGHLACLQWLLSQG---GCRVQDkdnsGATVLHLAARFGHPEVVNWLLHHGGGDPTAATDMGAlPIHYAAAKGDFP 152
Cdd:PHA02875   8 DAILFGELDIARRLLDIGinpNFEIYD----GISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIES-ELHDAVEEGDVK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261  153 SLRLLVEHYPEGVNAQTKNGATPLYLACQEGHLEVTQYLVQEcGADPHARAHDGMTPLHAAAQMGHSPVIVWLV---SCT 229
Cdd:PHA02875  83 AVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIAR-GADPDIPNTDKFSPLHLAVMMGDIKGIELLIdhkACL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261  230 DVSlseqdkdgatamhfaasrghtkvlswlllhggeisaDLWGGTPLHDAAENGELECCQILVVNGAELDVRDRDGYTAA 309
Cdd:PHA02875 162 DIE------------------------------------DCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAA 205
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 123-304 8.87e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 59.31  E-value: 8.87e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261  123 LLHHGGGDPTAATDMGALPIHYAAAKgdfPSLRLLVEHYPE---GVNAQTKNGATPLYLACQEGH-LEVTQYLVQEcGAD 198
Cdd:PHA02876 258 LLYDAGFSVNSIDDCKNTPLHHASQA---PSLSRLVPKLLErgaDVNAKNIKGETPLYLMAKNGYdTENIRTLIML-GAD 333

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261  199 PHARAHDGMTPLHAAAQMGHSPVIVWLVSCTDVSLSEQDKDGATAMHFAASRGHTKVLSWLLLHGGEISA-DLWGGTPLH 277
Cdd:PHA02876 334 VNAADRLYITPLHQASTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEAlSQKIGTALH 413

                        170       180
                 ....*....|....*....|....*...
gi 12053261  278 DA-AENGELECCQILVVNGAELDVRDRD 304
Cdd:PHA02876 414 FAlCGTNPYMSVKTLIDRGANVNSKNKD 441
Ank_5 pfam13857
Ankyrin repeats (many copies);
89-145 6.18e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 49.65  E-value: 6.18e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 12053261    89 LLSQGGCRVQDKDNSGATVLHLAARFGHPEVVNWLLHHgGGDPTAATDMGALPIHYA 145
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAY-GVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
242-292 9.98e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.20  E-value: 9.98e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 12053261   242 TAMHFAASRGHTKVLSWLLLHGGEISA-DLWGGTPLHDAAENGELECCQILV 292
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAvDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
272-324 1.92e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.42  E-value: 1.92e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 12053261   272 GGTPLHDAAENGELECCQILVVNGAELDVRDRDGYTAADLSDFNGHSHCTRYL 324
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
Ank_4 pfam13637
Ankyrin repeats (many copies);
106-158 1.96e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.42  E-value: 1.96e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 12053261   106 TVLHLAARFGHPEVVNWLLHHgGGDPTAATDMGALPIHYAAAKGDFPSLRLLV 158
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEK-GADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 130-229 2.11e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.52  E-value: 2.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261  130 DPTAAtDMGALPIHYAAAKGDFPSLRLLVEHYPEgVNAQTKNGATPLYLACQEGHLEVTQYLVqECGADPHARAHDGMTP 209
Cdd:PTZ00322  75 DPVVA-HMLTVELCQLAASGDAVGARILLTGGAD-PNCRDYDGRTPLHIACANGHVQVVRVLL-EFGADPTLLDKDGKTP 151

                         90       100
                 ....*....|....*....|
gi 12053261  210 LHAAAQMGHSPVIVWLVSCT 229
Cdd:PTZ00322 152 LELAEENGFREVVQLLSRHS 171
Ank_2 pfam12796
Ankyrin repeats (3 copies);
276-324 2.67e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 49.34  E-value: 2.67e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 12053261   276 LHDAAENGELECCQILVVNGAELDVRDRDGYTAADLSDFNGHSHCTRYL 324
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL 49
Ank_5 pfam13857
Ankyrin repeats (many copies);
269-311 1.51e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.80  E-value: 1.51e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 12053261   269 DLWGGTPLHDAAENGELECCQILVVNGAELDVRDRDGYTAADL 311
Cdd:pfam13857  13 DGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 191-267 5.09e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.28  E-value: 5.09e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 12053261  191 LVQECGADPHARAHDGMTPLHAAAQMGHSPVI-VWLVSCTDVSLSeqDKDGATAMHFAASRGHTKVLSWLLLHGGEIS 267
Cdd:PTZ00322 100 ILLTGGADPNCRDYDGRTPLHIACANGHVQVVrVLLEFGADPTLL--DKDGKTPLELAEENGFREVVQLLSRHSQCHF 175
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 75-247 8.57e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 49.19  E-value: 8.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261   75 HDASATGHLACLQWLLSQGGcRVQDKDNSGATVLHLAARFGHPEVVNWLLHHGGGdPTAATDMGALPIHYAAAKGDFPSL 154
Cdd:PHA02874 129 HYAIKKGDLESIKMLFEYGA-DVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAY-ANVKDNNGESPLHNAAEYGDYACI 206

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261  155 RLLVEHyPEGVNAQTKNGATPLYLACQEGHlEVTQYLVQEcgADPHARAHDGMTPLHAAAQMGHSPVIVWLVSCTDVSLS 234
Cdd:PHA02874 207 KLLIDH-GNHIMNKCKNGFTPLHNAIIHNR-SAIELLINN--ASINDQDIDGSTPLHHAINPPCDIDIIDILLYHKADIS 282

                        170
                 ....*....|...
gi 12053261  235 EQDKDGATAMHFA 247
Cdd:PHA02874 283 IKDNKGENPIDTA 295
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 72-298 9.73e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 49.29  E-value: 9.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261   72 TPAHDASATGHLACLQWLLSQGGCRVQDKDNSGATVLHLAARFGH-PEVVNWLLHHgGGDPTAATDMGALPIHYAAAKGD 150
Cdd:PHA02876 275 TPLHHASQAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIML-GADVNAADRLYITPLHQASTLDR 353

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261  151 FPSLRLLVEHYPEGVNAQTKNGATPLYLACQEGHLEVTQYLVqECGADPHARAHDGMTPLHAAAQMGHSPVIVWLVSCTD 230
Cdd:PHA02876 354 NKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLL-DYGADIEALSQKIGTALHFALCGTNPYMSVKTLIDRG 432

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261  231 VSLSEQDKDGATAMHFAASRG-HTKVLSWLLLHGGEISA-DLWGGTPLHDAAENGELecCQILVVNGAEL 298
Cdd:PHA02876 433 ANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAiNIQNQYPLLIALEYHGI--VNILLHYGAEL 500
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 72-211 1.11e-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: 1.11e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261  72 TPAHDASATGHLACLQWLLSQGGCRVQDKDNSGATVLHLAARFGHPEVVNWLLHhggGDPT-----AATDM--GALPIHY 144
Cdd:cd22192  19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME---AAPElvnepMTSDLyqGETALHI 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261 145 AAAKGDFPSLRLLVEHYPEGVNAQT---------KN----GATPL-YLACQeGHLEVTQYLVQEcGADPHARAHDGMTPL 210
Cdd:cd22192  96 AVVNQNLNLVRELIARGADVVSPRAtgtffrpgpKNliyyGEHPLsFAACV-GNEEIVRLLIEH-GADIRAQDSLGNTVL 173


                .
gi 12053261 211 H 211
Cdd:cd22192 174 H 174
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 118-294 1.20e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 48.72  E-value: 1.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261  118 EVVNWLLHHGGGDPTAATDMGALPIHYAAAKGDFPSLRLLVEhYPEGVNAQTKNGATPLYLACQEGHLEVTQYLVQEcGA 197
Cdd:PHA02878 148 EITKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLS-YGANVNIPDKTNNSPLHHAVKHYNKPIVHILLEN-GA 225

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261  198 DPHARAHDGMTPLHAAAQ--MGHSPVIVWLVSCTDVSLSEQDKdGATAMHFAASrgHTKVLSWLLLHGGEISA-DLWGGT 274
Cdd:PHA02878 226 STDARDKCGNTPLHISVGycKDYDILKLLLEHGVDVNAKSYIL-GLTALHSSIK--SERKLKLLLEYGADINSlNSYKLT 302

                        170       180
                 ....*....|....*....|.
gi 12053261  275 PLHDAAEN-GELECCQILVVN 294
Cdd:PHA02878 303 PLSSAVKQyLCINIGRILISN 323
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 72-225 1.66e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 48.06  E-value: 1.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261   72 TPAHDASATGHLACLQWLLSQGGCRVQDKDNSGATVLHLAARFGHPEVVNWLLHHGGGDPTAATDMGAlPIHYAAAKGDF 151
Cdd:PHA02875  70 SELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFS-PLHLAVMMGDI 148

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 12053261  152 PSLRLLVEHyPEGVNAQTKNGATPLYLACQEGHLEVTQYLVqECGADPHARAHDGMTPLHAAAQMGHSPVIVWL 225
Cdd:PHA02875 149 KGIELLIDH-KACLDIEDCCGCTPLIIAMAKGDIAICKMLL-DSGANIDYFGKNGCVAALCYAIENNKIDIVRL 220
Ank_5 pfam13857
Ankyrin repeats (many copies);
123-179 2.20e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.72  E-value: 2.20e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 12053261   123 LLHHGGGDPTAATDMGALPIHYAAAKGDFPSLRLLVEhYPEGVNAQTKNGATPLYLA 179
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLA-YGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
39-90 2.43e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.26  E-value: 2.43e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 12053261    39 PVHHAARAGKLHCLRFLVEeAALPAAARARNGATPAHDASATGHLACLQWLL 90
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLE-KGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 149-326 2.47e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 47.65  E-value: 2.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261  149 GDFPSLRLLVEHYPEGVNAQTKNGATPLYLACQEGHLEVTQYLVQEcGADPHARAHDGMTPLHAAAQMGHSPVIVWL--- 225
Cdd:PHA02874  12 GDIEAIEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKH-GADINHINTKIPHPLLTAIKIGAHDIIKLLidn 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261  226 --------VSCTD-----------VSLSEQDKDGATAMHFAASRGHTKVLSWLLLHGGEIS-ADLWGGTPLHDAAENGEL 285
Cdd:PHA02874  91 gvdtsilpIPCIEkdmiktildcgIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNiEDDNGCYPIHIAIKHNFF 170

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 12053261  286 ECCQILVVNGAELDVRDRDGYTAADLSDFNGHSHCTRYLRT 326
Cdd:PHA02874 171 DIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLID 211
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 108-307 2.92e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 47.35  E-value: 2.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261  108 LHLAARFGHPEVVNWLLHHGGgDP--TAATDMGALPIH--YAAAKGDFPSLRLLVEHYPEGVNAQTKNGATPLYLACQE- 182
Cdd:PHA03100  39 LYLAKEARNIDVVKILLDNGA-DInsSTKNNSTPLHYLsnIKYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKk 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261  183 -GHLEVTQYLVQEcGADPHARAHDGMTPLHAAaqmghspvivwlVSCTDVSLseqdkdgatamhfaasrghtKVLSWLLL 261
Cdd:PHA03100 118 sNSYSIVEYLLDN-GANVNIKNSDGENLLHLY------------LESNKIDL--------------------KILKLLID 164

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 12053261  262 HGGEISA-----------------DLWGGTPLHDAAENGELECCQILVVNGAELDVRDRDGYT 307
Cdd:PHA03100 165 KGVDINAknrvnyllsygvpinikDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDT 227
Ank_5 pfam13857
Ankyrin repeats (many copies);
157-213 4.79e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.56  E-value: 4.79e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 12053261   157 LVEHYPEGVNAQTKNGATPLYLACQEGHLEVTQYLVqECGADPHARAHDGMTPLHAA 213
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLL-AYGVDLNLKDEEGLTALDLA 56
PHA02946 PHA02946
ankyin-like protein; Provisional
 94-250 4.93e-05

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 46.59  E-value: 4.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261   94 GCRVQDKDNSGATVLHLAARFGHPEVVNWLLHHgGGDPTAATDMGALPIHYAAAKGD--FPSLRLLVEHYPEGVNAQTKN 171
Cdd:PHA02946  62 GYSPNETDDDGNYPLHIASKINNNRIVAMLLTH-GADPNACDKQHKTPLYYLSGTDDevIERINLLVQYGAKINNSVDEE 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261  172 GATPLyLACQEGHLEVTQYLVQeCGADPHARAHDGMTPLHAAAqMGHSP---VIVWLVScTDVSLSEQDKDGATAMHFAA 248
Cdd:PHA02946 141 GCGPL-LACTDPSERVFKKIMS-IGFEARIVDKFGKNHIHRHL-MSDNPkasTISWMMK-LGISPSKPDHDGNTPLHIVC 216


                 ..
gi 12053261  249 SR 250
Cdd:PHA02946 217 SK 218
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 230-307 8.11e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 46.03  E-value: 8.11e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 12053261  230 DVSLSEQDKDgATAMHFAASRGHTKVLSWLLLHGGEI-SADLWGGTPLHDAAENGELECCQILVVNGAELDVRDRDGYT 307
Cdd:PHA02878 159 DINMKDRHKG-NTALHYATENKDQRLTELLLSYGANVnIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNT 236
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 183-324 3.73e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 43.83  E-value: 3.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261  183 GHLEVTQYLVqECGADPHARAHDGMTPLHAAAQMGHSPVIVWLVSCTDVSlSEQDKDGATAMHFAASRGHTKVLSWLLLH 262
Cdd:PHA02875  13 GELDIARRLL-DIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIP-DVKYPDIESELHDAVEEGDVKAVEELLDL 90

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 12053261  263 GGEISADLW--GGTPLHDAAENGELECCQILVVNGAELDVRDRDGYTAADLSDFNGHSHCTRYL 324
Cdd:PHA02875  91 GKFADDVFYkdGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELL 154
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 171-201 3.91e-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: 38.34  E-value: 3.91e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 12053261    171 NGATPLYLACQEGHLEVTQYLVQEcGADPHA 201
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDK-GADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 7-193 5.34e-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: 43.46  E-value: 5.34e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261   7 LQAARQGELDVLRSLhaagLLGPSL----RDPLDALPVHHAARAGKLHCLRFLVEEAALPAAARARN----GATPAHDAS 78
Cdd:cd22192  22 LLAAKENDVQAIKKL----LKCPSCdlfqRGALGETALHVAALYDNLEAAVVLMEAAPELVNEPMTSdlyqGETALHIAV 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261  79 ATGHLACLQWLLSQGG----------CRVQDKDN---SGATVLHLAARFGHPEVVNWLLHHGGgDPTAATDMGALPIHYA 145
Cdd:cd22192  98 VNQNLNLVRELIARGAdvvspratgtFFRPGPKNliyYGEHPLSFAACVGNEEIVRLLIEHGA-DIRAQDSLGNTVLHIL 176

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 12053261 146 A-------------------AKGDFPSLRLLvehypegvnaQTKNGATPLYLACQEGHLEVTQYLVQ 193
Cdd:cd22192 177 VlqpnktfacqmydlilsydKEDDLQPLDLV----------PNNQGLTPFKLAAKEGNIVMFQHLVQ 233
Ank_5 pfam13857
Ankyrin repeats (many copies);
191-247 5.38e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.87  E-value: 5.38e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 12053261   191 LVQECGADPHARAHDGMTPLHAAAQMGHSPVIVWLVScTDVSLSEQDKDGATAMHFA 247
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLA-YGVDLNLKDEEGLTALDLA 56
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 40-181 6.16e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 43.03  E-value: 6.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261   40 VHHAARAGKLHCLRFLVEeAALPAAARARNGATPAHDASATGHLACLQWLLSQGGcRVQDKDNSGATVLHLAARFGHPEV 119
Cdd:PHA02874 128 LHYAIKKGDLESIKMLFE-YGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGA-YANVKDNNGESPLHNAAEYGDYAC 205

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 12053261  120 VNWLLHHgGGDPTAATDMGALPIHYAAAKgDFPSLRLLVEHypEGVNAQTKNGATPLYLACQ 181
Cdd:PHA02874 206 IKLLIDH-GNHIMNKCKNGFTPLHNAIIH-NRSAIELLINN--ASINDQDIDGSTPLHHAIN 263
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 171-202 7.88e-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: 37.65  E-value: 7.88e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 12053261   171 NGATPLYLAC-QEGHLEVTQYLVQeCGADPHAR 202
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLS-KGADVNAR 32
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 174-307 9.24e-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: 9.24e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261 174 TPLYLACQEGHLEVTQYLVQECGADPHARAHDGMTPLHAAAQMGHSPVIVWLVSCT----DVSLSEQDKDGATAMHFAAS 249
Cdd:cd22192  19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAApelvNEPMTSDLYQGETALHIAVV 98

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 12053261 250 RGHTKVLSWLLLHGGEISADLWGGT---------------PLHDAAENGELECCQILVVNGAELDVRDRDGYT 307
Cdd:cd22192  99 NQNLNLVRELIARGADVVSPRATGTffrpgpknliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNT 171
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 104-127 1.10e-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: 37.24  E-value: 1.10e-03
                          10        20
                  ....*....|....*....|....
gi 12053261   104 GATVLHLAARFGHPEVVNWLLHHG 127
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENG 25
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 104-128 1.25e-03

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.80  E-value: 1.25e-03
                           10        20
                   ....*....|....*....|....*
gi 12053261    104 GATVLHLAARFGHPEVVNWLLHHGG 128
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGA 26
Ank_5 pfam13857
Ankyrin repeats (many copies);
225-277 1.86e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.33  E-value: 1.86e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 12053261   225 LVSCTDVSLSEQDKDGATAMHFAASRGHTKVLSWLLLHGGEISA-DLWGGTPLH 277
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLkDEEGLTALD 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 78-188 2.61e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.42  E-value: 2.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261   78 SATGHLACLQWLLSqGGCRVQDKDNSGATVLHLAARFGHPEVVNWLLHHgGGDPTAATDMGALPIHYAAAKGDFPSLRLL 157
Cdd:PTZ00322  90 AASGDAVGARILLT-GGADPNCRDYDGRTPLHIACANGHVQVVRVLLEF-GADPTLLDKDGKTPLELAEENGFREVVQLL 167

                         90       100       110
                 ....*....|....*....|....*....|.
gi 12053261  158 VEHYPEGVNAQTKngATPLYLACQEGHLEVT 188
Cdd:PTZ00322 168 SRHSQCHFELGAN--AKPDSFTGKPPSLEDS 196
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 159-286 2.90e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely related to TRPV1, sharing high sequence identity (>50%), but TRPV2 shows a higher temperature threshold and sensitivity for activation than TRPV1. TRPV2 can be stimulated by ligands or lipids, and is involved in osmosensation and mechanosensation. TRPV2 is expressed in both neuronal and non-neuronal tissues, and it has been implicated in diverse physiological and pathophysiological processes, including cardiac-structure maintenance, innate immunity, and cancer. TRPV2 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 Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 41.38  E-value: 2.90e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261 159 EHYPEGVNAQTKN----GATPLYLACQEGHLEVTQYLVqECGADPHARAHD-------------GMTPLHAAAQMGHSPV 221
Cdd:cd22197  77 GNPKPLVNAQCTDeyyrGHSALHIAIEKRSLQCVKLLV-ENGADVHARACGrffqkkqgtcfyfGELPLSLAACTKQWDV 155

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261 222 IVWLVS--CTDVSLSEQDKDGATAMH---FAASRGH------TKVLSWLLLHGGEISADL-------WGG-TPLHDAAEN 282
Cdd:cd22197 156 VNYLLEnpHQPASLQAQDSLGNTVLHalvMIADNSPensalvIKMYDGLLQAGARLCPTVqleeisnHEGlTPLKLAAKE 235


                ....
gi 12053261 283 GELE 286
Cdd:cd22197 236 GKIE 239
WH2 pfam02205
WH2 motif; The WH2 motif (for Wiskott Aldrich syndrome homology region 2) has been shown in ...
 648-673 4.97e-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: 35.17  E-value: 4.97e-03
                          10        20
                  ....*....|....*....|....*.
gi 12053261   648 PTGDNSELLAEIKAGKSLKPTPQSKG 673
Cdd:pfam02205   1 GGGGRGALLADIRAGKKLKKVEETND 26
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 123-203 5.04e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 40.65  E-value: 5.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261  123 LLHHGGGDPTAATDMGALPIHYAAAKGDFPSLRLLVEhYPEGVNAQTKNGATPLYLACQEGHLEVTQYLVQECGADPHAR 202
Cdd:PTZ00322 100 ILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLE-FGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELG 178


                 .
gi 12053261  203 A 203
Cdd:PTZ00322 179 A 179
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 239-268 5.14e-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: 35.31  E-value: 5.14e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 12053261   239 DGATAMHFAASRGHTKVLSWLLLHGGEISA 268
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 171-201 6.07e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 34.93  E-value: 6.07e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 12053261   171 NGATPLYLACQEGHLEVTQYLVqECGADPHA 201
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLL-ENGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 237-291 6.18e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 40.27  E-value: 6.18e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 12053261  237 DKDGATAMHFAASRGHTKVLSWLLLHGGEISA-DLWGGTPLHDAAENGELECCQIL 291
Cdd:PTZ00322 112 DYDGRTPLHIACANGHVQVVRVLLEFGADPTLlDKDGKTPLELAEENGFREVVQLL 167
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 104-127 6.29e-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: 6.29e-03
                          10        20
                  ....*....|....*....|....*
gi 12053261   104 GATVLHLAA-RFGHPEVVNWLLHHG 127
Cdd:pfam00023   2 GNTPLHLAAgRRGNLEIVKLLLSKG 26
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 272-303 6.47e-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: 6.47e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 12053261   272 GGTPLHDAA-ENGELECCQILVVNGAELDVRDR 303
Cdd:pfam00023   2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 7-223 9.43e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 39.66  E-value: 9.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261    7 LQAARQGELDVLRSLHAAGLLGPSLrDPLDALPVHHAARAGKLHCLRFLVEEAALPAAARARNGATPAHDASATGH-LAC 85
Cdd:PHA02876 245 LKAIRNEDLETSLLLYDAGFSVNSI-DDCKNTPLHHASQAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTEN 323

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12053261   86 LQWLLSQGGcRVQDKDNSGATVLHLAARFGHPEVVNWLLHHGGGDPTAATDMGALPIHYAAAKGDFPSLRLLVEhYPEGV 165
Cdd:PHA02876 324 IRTLIMLGA-DVNAADRLYITPLHQASTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLD-YGADI 401

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 12053261  166 NAQTKNGATPLYLA-CQEGHLEVTQYLVQEcGADPHARAHDGMTPLHAAAQMGHSPVIV 223
Cdd:PHA02876 402 EALSQKIGTALHFAlCGTNPYMSVKTLIDR-GANVNSKNKDLSTPLHYACKKNCKLDVI 459
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 245-316 9.88e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 39.50  E-value: 9.88e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 12053261  245 HFAASrGHTkVLSWLLLHGGEI--SADLWGGTPLHDAAENGELECCQILVVNGAELDVRDRDGYTAADLSDFNG 316
Cdd:PTZ00322  88 QLAAS-GDA-VGARILLTGGADpnCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENG 159
 
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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