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Conserved domains on  [gi|2024478129|ref|XP_040544799|]
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espin isoform X2 [Gallus gallus]

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 2.49e-42

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 157.04  E-value: 2.49e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129   52 LRYLAAEAALRGDARARNGATPAHDAAATGNLACLQWLLTQGGCGVQDTDNSGATILHLAARFGHHEVIEWLLRFGGSDP 131
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129  132 TAATDTGALPVHYAAAKGDFPSLRLLLGHcPSTLSAQTKTGATPLYLACQEGHLEIIQYLVkDCGADPHVRANDGMTPLH 211
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEA-GADVNARDKDGETPLHLAAYNGNLEIVKLLL-EAGADVNAQDNDGNTPLH 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129  212 AAAQMGHNTVIVWLMSFTtVSLSERDDDGATAMHFAASRGHAKVLSWLLLHGGEITA-DGWGGTPLHDAAENGELECCQI 290
Cdd:COG0666    159 LAAANGNLEIVKLLLEAG-ADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAkDNDGKTALDLAAENGNLEIVKL 237

                          250       260       270
                   ....*....|....*....|....*....|....
gi 2024478129  291 LVVNGADLSIRDQDGYTAADLADYNGHIHCAKYL 324
Cdd:COG0666    238 LLEAGADLNAKDKDGLTALLLAAAAGAALIVKLL 271
Ank_2 pfam12796
Ankyrin repeats (3 copies);
8-93 3.81e-12

Ankyrin repeats (3 copies);


:

Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 63.21  E-value: 3.81e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129    8 QAARQGDVEALRGLRAAGLlRPGLRDALGASPAHHAARAGRLACLRYLAAEAALRGDArarNGATPAHDAAATGNLACLQ 87
Cdd:pfam12796    3 LAAKNGNLELVKLLLENGA-DANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD---NGRTALHYAARSGHLEIVK 78


                   ....*.
gi 2024478129   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 ...
 615-640 4.24e-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: 35.94  E-value: 4.24e-03
                           10        20
                   ....*....|....*....|....*.
gi 2024478129  615 PTGDNSELLAEIKAGKSLKPTPQSKG 640
Cdd:pfam02205    1 GGGGRGALLADIRAGKKLKKVEETND 26
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
52-324 2.49e-42

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 157.04  E-value: 2.49e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129   52 LRYLAAEAALRGDARARNGATPAHDAAATGNLACLQWLLTQGGCGVQDTDNSGATILHLAARFGHHEVIEWLLRFGGSDP 131
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129  132 TAATDTGALPVHYAAAKGDFPSLRLLLGHcPSTLSAQTKTGATPLYLACQEGHLEIIQYLVkDCGADPHVRANDGMTPLH 211
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEA-GADVNARDKDGETPLHLAAYNGNLEIVKLLL-EAGADVNAQDNDGNTPLH 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129  212 AAAQMGHNTVIVWLMSFTtVSLSERDDDGATAMHFAASRGHAKVLSWLLLHGGEITA-DGWGGTPLHDAAENGELECCQI 290
Cdd:COG0666    159 LAAANGNLEIVKLLLEAG-ADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAkDNDGKTALDLAAENGNLEIVKL 237

                          250       260       270
                   ....*....|....*....|....*....|....
gi 2024478129  291 LVVNGADLSIRDQDGYTAADLADYNGHIHCAKYL 324
Cdd:COG0666    238 LLEAGADLNAKDKDGLTALLLAAAAGAALIVKLL 271
Ank_2 pfam12796
Ankyrin repeats (3 copies);
176-268 2.27e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 86.71  E-value: 2.27e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129  176 LYLACQEGHLEIIQYLVKdCGADPHVRANDGMTPLHAAAQMGHNTVIVWLMSFTTVslsERDDDGATAMHFAASRGHAKV 255
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLE-NGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV---NLKDNGRTALHYAARSGHLEI 76

                           90
                   ....*....|...
gi 2024478129  256 LSWLLLHGGEITA 268
Cdd:pfam12796   77 VKLLLEKGADINV 89
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 72-312 5.90e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 78.85  E-value: 5.90e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129   72 TPAHDAAATGNLACLQwLLTQGGCGVQDTDNSGATILHLAARFGHHEVIEWLLRFGgsdptaaTDTGALPV--------- 142
Cdd:PHA02874    37 TPLIDAIRSGDAKIVE-LFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNG-------VDTSILPIpciekdmik 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129  143 --------------------HYAAAKGDFPSLRLLLGHcPSTLSAQTKTGATPLYLACQEGHLEIIQYLVKDcGADPHVR 202
Cdd:PHA02874   109 tildcgidvnikdaelktflHYAIKKGDLESIKMLFEY-GADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEK-GAYANVK 186

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129  203 ANDGMTPLHAAAQMGHNTVIVWLMSFTTvSLSERDDDGATAMHFAASrgHAKVLSWLLLHGGEIT-ADGWGGTPLHDAAE 281
Cdd:PHA02874   187 DNNGESPLHNAAEYGDYACIKLLIDHGN-HIMNKCKNGFTPLHNAII--HNRSAIELLINNASINdQDIDGSTPLHHAIN 263

                          250       260       270
                   ....*....|....*....|....*....|..
gi 2024478129  282 NG-ELECCQILVVNGADLSIRDQDGYTAADLA 312
Cdd:PHA02874   264 PPcDIDIIDILLYHKADISIKDNKGENPIDTA 295
Ank_2 pfam12796
Ankyrin repeats (3 copies);
8-93 3.81e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 63.21  E-value: 3.81e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129    8 QAARQGDVEALRGLRAAGLlRPGLRDALGASPAHHAARAGRLACLRYLAAEAALRGDArarNGATPAHDAAATGNLACLQ 87
Cdd:pfam12796    3 LAAKNGNLELVKLLLENGA-DANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD---NGRTALHYAARSGHLEIVK 78


                   ....*.
gi 2024478129   88 WLLTQG 93
Cdd:pfam12796   79 LLLEKG 84
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 7-193 2.80e-08

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: 58.10  E-value: 2.80e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129    7 LQAARQGDVEALRGLRAAGLLRPGLRDALGASPAHHAARAGRLAclrylAAEAALRGDARARN---------GATPAHDA 77
Cdd:cd22192     22 LLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLE-----AAVVLMEAAPELVNepmtsdlyqGETALHIA 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129   78 AATGNLACLQWLLTQGGcgvqDTDNSGAT-----------------ILHLAARFGHHEVIEWLLRfGGSDPTAATDTGAL 140
Cdd:cd22192     97 VVNQNLNLVRELIARGA----DVVSPRATgtffrpgpknliyygehPLSFAACVGNEEIVRLLIE-HGADIRAQDSLGNT 171

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024478129  141 PVH---------YAAAKGDF--PSLRLLLGHCPSTLsaQTKTGATPLYLACQEGHLEIIQYLVK 193
Cdd:cd22192    172 VLHilvlqpnktFACQMYDLilSYDKEDDLQPLDLV--PNNQGLTPFKLAAKEGNIVMFQHLVQ 233
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 172-201 4.14e-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: 38.72  E-value: 4.14e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 2024478129   172 GATPLYLACQEGHLEIIQYLVkDCGADPHV 201
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLL-DKGADINA 30
WH2 pfam02205
WH2 motif; The WH2 motif (for Wiskott Aldrich syndrome homology region 2) has been shown in ...
 615-640 4.24e-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: 35.94  E-value: 4.24e-03
                           10        20
                   ....*....|....*....|....*.
gi 2024478129  615 PTGDNSELLAEIKAGKSLKPTPQSKG 640
Cdd:pfam02205    1 GGGGRGALLADIRAGKKLKKVEETND 26
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
52-324 2.49e-42

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 157.04  E-value: 2.49e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129   52 LRYLAAEAALRGDARARNGATPAHDAAATGNLACLQWLLTQGGCGVQDTDNSGATILHLAARFGHHEVIEWLLRFGGSDP 131
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129  132 TAATDTGALPVHYAAAKGDFPSLRLLLGHcPSTLSAQTKTGATPLYLACQEGHLEIIQYLVkDCGADPHVRANDGMTPLH 211
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEA-GADVNARDKDGETPLHLAAYNGNLEIVKLLL-EAGADVNAQDNDGNTPLH 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129  212 AAAQMGHNTVIVWLMSFTtVSLSERDDDGATAMHFAASRGHAKVLSWLLLHGGEITA-DGWGGTPLHDAAENGELECCQI 290
Cdd:COG0666    159 LAAANGNLEIVKLLLEAG-ADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAkDNDGKTALDLAAENGNLEIVKL 237

                          250       260       270
                   ....*....|....*....|....*....|....
gi 2024478129  291 LVVNGADLSIRDQDGYTAADLADYNGHIHCAKYL 324
Cdd:COG0666    238 LLEAGADLNAKDKDGLTALLLAAAAGAALIVKLL 271
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
6-269 4.98e-40

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 150.10  E-value: 4.98e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129    6 ALQAARQGDVEALRGLRAAGLLRPGLRDALGASPAHHAARAGRLACLRYLAAEAALRGDARARNGATPAHDAAATGNLAC 85
Cdd:COG0666     23 LLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEI 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129   86 LQWLLTQGGcGVQDTDNSGATILHLAARFGHHEVIEWLLRFGGsDPTAATDTGALPVHYAAAKGDFPSLRLLLGHCPStL 165
Cdd:COG0666    103 VKLLLEAGA-DVNARDKDGETPLHLAAYNGNLEIVKLLLEAGA-DVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGAD-V 179

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129  166 SAQTKTGATPLYLACQEGHLEIIQYLVkDCGADPHVRANDGMTPLHAAAQMGHNTVIVWLMSFTTVsLSERDDDGATAMH 245
Cdd:COG0666    180 NARDNDGETPLHLAAENGHLEIVKLLL-EAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD-LNAKDKDGLTALL 257

                          250       260
                   ....*....|....*....|....
gi 2024478129  246 FAASRGHAKVLSWLLLHGGEITAD 269
Cdd:COG0666    258 LAAAAGAALIVKLLLLALLLLAAA 281
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
101-325 1.13e-39

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 149.33  E-value: 1.13e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129  101 DNSGATILHLAARFGHHEVIEWLLRFGGSDPTAATDTGALPVHYAAAKGDFPSLRLLLGHCPSTLSAQTKTGATPLYLAC 180
Cdd:COG0666     16 LLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAA 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129  181 QEGHLEIIQYLVKDcGADPHVRANDGMTPLHAAAQMGHNTVIVWLMSFTtVSLSERDDDGATAMHFAASRGHAKVLSWLL 260
Cdd:COG0666     96 RNGDLEIVKLLLEA-GADVNARDKDGETPLHLAAYNGNLEIVKLLLEAG-ADVNAQDNDGNTPLHLAAANGNLEIVKLLL 173

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024478129  261 LHGGEITA-DGWGGTPLHDAAENGELECCQILVVNGADLSIRDQDGYTAADLADYNGHIHCAKYLR 325
Cdd:COG0666    174 EAGADVNArDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239
Ank_2 pfam12796
Ankyrin repeats (3 copies);
176-268 2.27e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 86.71  E-value: 2.27e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129  176 LYLACQEGHLEIIQYLVKdCGADPHVRANDGMTPLHAAAQMGHNTVIVWLMSFTTVslsERDDDGATAMHFAASRGHAKV 255
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLE-NGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV---NLKDNGRTALHYAARSGHLEI 76

                           90
                   ....*....|...
gi 2024478129  256 LSWLLLHGGEITA 268
Cdd:pfam12796   77 VKLLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
108-202 1.20e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 81.70  E-value: 1.20e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129  108 LHLAARFGHHEVIEWLLRFGgSDPTAATDTGALPVHYAAAKGDFPSLRLLLGHCPSTLSAQtktGATPLYLACQEGHLEI 187
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENG-ADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN---GRTALHYAARSGHLEI 76

                           90
                   ....*....|....*
gi 2024478129  188 IQYLVkDCGADPHVR 202
Cdd:pfam12796   77 VKLLL-EKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
210-302 1.62e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 81.32  E-value: 1.62e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129  210 LHAAAQMGHNTVIVWLMSFTtVSLSERDDDGATAMHFAASRGHAKVLSWLLLHG-GEITADGWggTPLHDAAENGELECC 288
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENG-ADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAdVNLKDNGR--TALHYAARSGHLEIV 77

                           90
                   ....*....|....
gi 2024478129  289 QILVVNGADLSIRD 302
Cdd:pfam12796   78 KLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
143-227 9.55e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 73.61  E-value: 9.55e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129  143 HYAAAKGDFPSLRLLLgHCPSTLSAQTKTGATPLYLACQEGHLEIIQYLVKDCGADphvRANDGMTPLHAAAQMGHNTVI 222
Cdd:pfam12796    2 HLAAKNGNLELVKLLL-ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN---LKDNGRTALHYAARSGHLEIV 77


                   ....*
gi 2024478129  223 VWLMS 227
Cdd:pfam12796   78 KLLLE 82
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 72-312 5.90e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 78.85  E-value: 5.90e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129   72 TPAHDAAATGNLACLQwLLTQGGCGVQDTDNSGATILHLAARFGHHEVIEWLLRFGgsdptaaTDTGALPV--------- 142
Cdd:PHA02874    37 TPLIDAIRSGDAKIVE-LFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNG-------VDTSILPIpciekdmik 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129  143 --------------------HYAAAKGDFPSLRLLLGHcPSTLSAQTKTGATPLYLACQEGHLEIIQYLVKDcGADPHVR 202
Cdd:PHA02874   109 tildcgidvnikdaelktflHYAIKKGDLESIKMLFEY-GADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEK-GAYANVK 186

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129  203 ANDGMTPLHAAAQMGHNTVIVWLMSFTTvSLSERDDDGATAMHFAASrgHAKVLSWLLLHGGEIT-ADGWGGTPLHDAAE 281
Cdd:PHA02874   187 DNNGESPLHNAAEYGDYACIKLLIDHGN-HIMNKCKNGFTPLHNAII--HNRSAIELLINNASINdQDIDGSTPLHHAIN 263

                          250       260       270
                   ....*....|....*....|....*....|..
gi 2024478129  282 NG-ELECCQILVVNGADLSIRDQDGYTAADLA 312
Cdd:PHA02874   264 PPcDIDIIDILLYHKADISIKDNKGENPIDTA 295
PHA03095 PHA03095
ankyrin-like protein; Provisional
 89-354 2.18e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 77.37  E-value: 2.18e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129   89 LLTQGGcGVQDTDNSGATILHLAARFGHH---EVIEWLLRfGGSDPTAATDTGALPVH-YAAAKGDFPSLRLLLGHCPST 164
Cdd:PHA03095    33 LLAAGA-DVNFRGEYGKTPLHLYLHYSSEkvkDIVRLLLE-AGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADV 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129  165 LsAQTKTGATPL--YLACQEGHLEIIQYLVKDcGADPHVRANDGMTPLHAAAQMGHNTV-IVWLMSFTTVSLSERDDDGA 241
Cdd:PHA03095   111 N-AKDKVGRTPLhvYLSGFNINPKVIRLLLRK-GADVNALDLYGMTPLAVLLKSRNANVeLLRLLIDAGADVYAVDDRFR 188

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129  242 TAMH-FAAS-RGHAKVLSWLLLHGGEITA-DGWGGTPLHDAAENGelECCQILVVN----GADLSIRDQDGYTAADLAD- 313
Cdd:PHA03095   189 SLLHhHLQSfKPRARIVRELIRAGCDPAAtDMLGNTPLHSMATGS--SCKRSLVLPlliaGISINARNRYGQTPLHYAAv 266

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 2024478129  314 YNGHIHCAKYLRTVENMSVEhrvlsrdpSADGECrqPDSGM 354
Cdd:PHA03095   267 FNNPRACRRLIALGADINAV--------SSDGNT--PLSLM 297
Ank_2 pfam12796
Ankyrin repeats (3 copies);
244-324 1.14e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.83  E-value: 1.14e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129  244 MHFAASRGHAKVLSWLLLHGGEITA-DGWGGTPLHDAAENGELECCQILVvNGADLSIRDqDGYTAADLADYNGHIHCAK 322
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLqDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKD-NGRTALHYAARSGHLEIVK 78


                   ..
gi 2024478129  323 YL 324
Cdd:pfam12796   79 LL 80
Ank_2 pfam12796
Ankyrin repeats (3 copies);
41-124 3.40e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 66.29  E-value: 3.40e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129   41 HHAARAGRLACLRYLAAEAAlRGDARARNGATPAHDAAATGNLACLQWLLTQggcGVQDTDNSGATILHLAARFGHHEVI 120
Cdd:pfam12796    2 HLAAKNGNLELVKLLLENGA-DANLQDKNGRTALHLAAKNGHLEIVKLLLEH---ADVNLKDNGRTALHYAARSGHLEIV 77


                   ....
gi 2024478129  121 EWLL 124
Cdd:pfam12796   78 KLLL 81
PHA03095 PHA03095
ankyrin-like protein; Provisional
 14-344 1.08e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 71.98  E-value: 1.08e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129   14 DVEALRGLRAAGllrPGL--RDALGASPAH---HAARAGRLACLRYLAaEAALRGDARARNGATPAHDAAATGNLACLQW 88
Cdd:PHA03095    26 TVEEVRRLLAAG---ADVnfRGEYGKTPLHlylHYSSEKVKDIVRLLL-EAGADVNAPERCGFTPLHLYLYNATTLDVIK 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129   89 LLTQGGCGVQDTDNSGATILH--LAARFGHHEVIEWLLRFGgSDPTAATDTGALPVHyaaakgdfpslrLLLGhcpstls 166
Cdd:PHA03095   102 LLIKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKG-ADVNALDLYGMTPLA------------VLLK------- 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129  167 aqtKTGATPlylacqeghlEIIQYLVkDCGADPHVRANDGMTPLHAAAQMGH-NTVIVWLMSFTTVSLSERDDDGATAMH 245
Cdd:PHA03095   162 ---SRNANV----------ELLRLLI-DAGADVYAVDDRFRSLLHHHLQSFKpRARIVRELIRAGCDPAATDMLGNTPLH 227

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129  246 FAA--SRGHAKVLSWLLLHGGEITA-DGWGGTPLHDAAENGELECCQILVVNGADLSIRDQDGYTAADLADYNGHIHCAK 322
Cdd:PHA03095   228 SMAtgSSCKRSLVLPLLIAGISINArNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVR 307

                          330       340
                   ....*....|....*....|..
gi 2024478129  323 ylrtvenmsvehRVLSRDPSAD 344
Cdd:PHA03095   308 ------------AALAKNPSAE 317
Ank_2 pfam12796
Ankyrin repeats (3 copies);
8-93 3.81e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 63.21  E-value: 3.81e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129    8 QAARQGDVEALRGLRAAGLlRPGLRDALGASPAHHAARAGRLACLRYLAAEAALRGDArarNGATPAHDAAATGNLACLQ 87
Cdd:pfam12796    3 LAAKNGNLELVKLLLENGA-DANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD---NGRTALHYAARSGHLEIVK 78


                   ....*.
gi 2024478129   88 WLLTQG 93
Cdd:pfam12796   79 LLLEKG 84
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 63-223 1.06e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 66.04  E-value: 1.06e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129   63 GDARARngaTPAHDAAATGNLACLQWLLTQGgCGVQDTDNSGATILHLAARFGHHEVIEWLLRFGG-SDPTAATDTGALp 141
Cdd:PLN03192   554 GDSKGR---TPLHIAASKGYEDCVLVLLKHA-CNVHIRDANGNTALWNAISAKHHKIFRILYHFASiSDPHAAGDLLCT- 628

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129  142 vhyAAAKGDFPSLRLLLGHcPSTLSAQTKTGATPLYLACQEGHLEIIQYLVKDcGAD-PHVRANDGMTP-----LHAAAQ 215
Cdd:PLN03192   629 ---AAKRNDLTAMKELLKQ-GLNVDSEDHQGATALQVAMAEDHVDMVRLLIMN-GADvDKANTDDDFSPtelreLLQKRE 703


                   ....*...
gi 2024478129  216 MGHNTVIV 223
Cdd:PLN03192   704 LGHSITIV 711
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 196-324 1.12e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 66.04  E-value: 1.12e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129  196 GADPHVRANDGMTPLHAAAQMGH-NTVIVWLMSFTTVSLseRDDDGATAMHFAASRGHAKVLsWLLLHGGEITADGWGGT 274
Cdd:PLN03192   548 KLDPDIGDSKGRTPLHIAASKGYeDCVLVLLKHACNVHI--RDANGNTALWNAISAKHHKIF-RILYHFASISDPHAAGD 624

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 2024478129  275 PLHDAAENGELECCQILVVNGADLSIRDQDGYTAADLADYNGHIHCAKYL 324
Cdd:PLN03192   625 LLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLL 674
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 76-309 1.37e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 65.01  E-value: 1.37e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129   76 DAAATGNLACLQWLLTQGgCGVQDTDNSGATILHLAARFGHHEVIEWLLRFGGSDPTAATDTGAlPVHYAAAKGDFPSLR 155
Cdd:PHA02875     8 DAILFGELDIARRLLDIG-INPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIES-ELHDAVEEGDVKAVE 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129  156 LLLGHCPSTLSAQTKTGATPLYLACQEGHLEIIQYLVKDcGADPHVRANDGMTPLHAAAQMGHNTVIVWLMSfttvslse 235
Cdd:PHA02875    86 ELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIAR-GADPDIPNTDKFSPLHLAVMMGDIKGIELLID-------- 156

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024478129  236 rdddgatamhfaasrgHAKVLSwlllhggeiTADGWGGTPLHDAAENGELECCQILVVNGADLSIRDQDGYTAA 309
Cdd:PHA02875   157 ----------------HKACLD---------IEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAA 205
Ank_4 pfam13637
Ankyrin repeats (many copies);
206-260 2.77e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 56.90  E-value: 2.77e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2024478129  206 GMTPLHAAAQMGHNTVIVWLMSFTtVSLSERDDDGATAMHFAASRGHAKVLSWLL 260
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKG-ADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
276-341 1.70e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 55.89  E-value: 1.70e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024478129  276 LHDAAENGELECCQILVVNGADLSIRDQDGYTAADLADYNGHIHCAKYLrtVENMSVEHRVLSRDP 341
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL--LEHADVNLKDNGRTA 64
Ank_4 pfam13637
Ankyrin repeats (many copies);
72-124 2.12e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.20  E-value: 2.12e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2024478129   72 TPAHDAAATGNLACLQWLLtQGGCGVQDTDNSGATILHLAARFGHHEVIEWLL 124
Cdd:pfam13637    3 TALHAAAASGHLELLRLLL-EKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
272-324 8.77e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.66  E-value: 8.77e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2024478129  272 GGTPLHDAAENGELECCQILVVNGADLSIRDQDGYTAADLADYNGHIHCAKYL 324
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 88-214 1.06e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 58.91  E-value: 1.06e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129   88 WLLTQGGCGVQDTDNSGATILHLAA--RFGHHEVIEWLLRFGgSDPTAATDTGALPVHYAAA--KGDFPSLRLLLGH--- 160
Cdd:PHA03100    90 KLLLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNG-ANVNIKNSDGENLLHLYLEsnKIDLKILKLLIDKgvd 168

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024478129  161 --------------CPstLSAQTKTGATPLYLACQEGHLEIIQYLVkDCGADPHVRANDGMTPLHAAA 214
Cdd:PHA03100   169 inaknrvnyllsygVP--INIKDVYGFTPLHYAVYNNNPEFVKYLL-DLGANPNLVNKYGDTPLHIAI 233
Ank_4 pfam13637
Ankyrin repeats (many copies);
174-225 1.81e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.51  E-value: 1.81e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2024478129  174 TPLYLACQEGHLEIIQYLVKDcGADPHVRANDGMTPLHAAAQMGHNTVIVWL 225
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEK-GADINAVDGNGETALHFAASNGNVEVLKLL 53
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 7-193 2.80e-08

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: 58.10  E-value: 2.80e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129    7 LQAARQGDVEALRGLRAAGLLRPGLRDALGASPAHHAARAGRLAclrylAAEAALRGDARARN---------GATPAHDA 77
Cdd:cd22192     22 LLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLE-----AAVVLMEAAPELVNepmtsdlyqGETALHIA 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129   78 AATGNLACLQWLLTQGGcgvqDTDNSGAT-----------------ILHLAARFGHHEVIEWLLRfGGSDPTAATDTGAL 140
Cdd:cd22192     97 VVNQNLNLVRELIARGA----DVVSPRATgtffrpgpknliyygehPLSFAACVGNEEIVRLLIE-HGADIRAQDSLGNT 171

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024478129  141 PVH---------YAAAKGDF--PSLRLLLGHCPSTLsaQTKTGATPLYLACQEGHLEIIQYLVK 193
Cdd:cd22192    172 VLHilvlqpnktFACQMYDLilSYDKEDDLQPLDLV--PNNQGLTPFKLAAKEGNIVMFQHLVQ 233
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 55-303 3.16e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 58.15  E-value: 3.16e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129   55 LAAEAALRG--DARARN--GATPAHDAAATGNLACLQWLLTQGGcGVQDTDNSGATILHLAARFGHHEVIE--------- 121
Cdd:PHA02876   159 LIAEMLLEGgaDVNAKDiyCITPIHYAAERGNAKMVNLLLSYGA-DVNIIALDDLSVLECAVDSKNIDTIKaiidnrsni 237

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129  122 -------------------WLLRFGGSDPTAATDTGALPVHYAAAKgdfPSLRLLLghcPSTL------SAQTKTGATPL 176
Cdd:PHA02876   238 nkndlsllkairnedletsLLLYDAGFSVNSIDDCKNTPLHHASQA---PSLSRLV---PKLLergadvNAKNIKGETPL 311

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129  177 YLACQEGH-LEIIQYLVKdCGADphVRANDGM--TPLHAAAQMGHNTVIVWLMSFTTVSLSERDDDGATAMHFAASRGHA 253
Cdd:PHA02876   312 YLMAKNGYdTENIRTLIM-LGAD--VNAADRLyiTPLHQASTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNV 388

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129  254 KVLSWLLLHGGEITA-----------------------------------DGWGGTPLHDAAENG-ELECCQILVVNGAD 297
Cdd:PHA02876   389 VIINTLLDYGADIEAlsqkigtalhfalcgtnpymsvktlidrganvnskNKDLSTPLHYACKKNcKLDVIEMLLDNGAD 468


                   ....*....
gi 2024478129  298 ---LSIRDQ 303
Cdd:PHA02876   469 vnaINIQNQ 477
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 174-324 5.83e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 56.60  E-value: 5.83e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129  174 TPLYLACQEGHLEIIQYLVKDcGADPHVRANDGMTPLHAAAQMGHNTV----IVWLMSFTTVSLSERDDDGATAMHFAAS 249
Cdd:PHA03100    37 LPLYLAKEARNIDVVKILLDN-GADINSSTKNNSTPLHYLSNIKYNLTdvkeIVKLLLEYGANVNAPDNNGITPLLYAIS 115

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129  250 R--GHAKVLSWLLLHGGEITAD-GWGGTPLHDAAENG--ELECCQILVVNGADLS----------------IRDQDGYTA 308
Cdd:PHA03100   116 KksNSYSIVEYLLDNGANVNIKnSDGENLLHLYLESNkiDLKILKLLIDKGVDINaknrvnyllsygvpinIKDVYGFTP 195

                          170
                   ....*....|....*.
gi 2024478129  309 ADLADYNGHIHCAKYL 324
Cdd:PHA03100   196 LHYAVYNNNPEFVKYL 211
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 72-251 8.43e-08

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: 56.56  E-value: 8.43e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129   72 TPAHDAAATGNLACLQWLLTQGGCGVQDTDNSGATILHLAARFGHHEVIEWLLRfggSDP-------TAATDTGALPVHY 144
Cdd:cd22192     19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME---AAPelvnepmTSDLYQGETALHI 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129  145 AAAKGDFPSLRLLLGHCPSTLSAQ-TKT------------GATPL-YLACQeGHLEIIQYLVKDcGADPHVRANDGMTPL 210
Cdd:cd22192     96 AVVNQNLNLVRELIARGADVVSPRaTGTffrpgpknliyyGEHPLsFAACV-GNEEIVRLLIEH-GADIRAQDSLGNTVL 173

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2024478129  211 HAAAqMGHNTVIVWLMSFTTVSLSERDD----------DGATAMHFAASRG 251
Cdd:cd22192    174 HILV-LQPNKTFACQMYDLILSYDKEDDlqpldlvpnnQGLTPFKLAAKEG 223
Ank_5 pfam13857
Ankyrin repeats (many copies);
259-312 1.19e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 49.27  E-value: 1.19e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2024478129  259 LLLHGGE--ITADGWGGTPLHDAAENGELECCQILVVNGADLSIRDQDGYTAADLA 312
Cdd:pfam13857    1 LLEHGPIdlNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 72-215 1.28e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 55.38  E-value: 1.28e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129   72 TPAHDAAATGNLACLQWLLTQGGCGVQDTDNSGATILHLAARFGHHEVIEWLLRFGGSDPTAATDTGAlPVHYAAAKGDF 151
Cdd:PHA02875    70 SELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFS-PLHLAVMMGDI 148

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024478129  152 PSLRLLLGHcPSTLSAQTKTGATPLYLACQEGHLEIIQYLVkDCGADP-HVRANDGMTPLHAAAQ 215
Cdd:PHA02875   149 KGIELLIDH-KACLDIEDCCGCTPLIIAMAKGDIAICKMLL-DSGANIdYFGKNGCVAALCYAIE 211
Ank_4 pfam13637
Ankyrin repeats (many copies);
141-192 1.67e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.81  E-value: 1.67e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2024478129  141 PVHYAAAKGDFPSLRLLLGHCPStLSAQTKTGATPLYLACQEGHLEIIQYLV 192
Cdd:pfam13637    4 ALHAAAASGHLELLRLLLEKGAD-INAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
106-158 2.81e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.42  E-value: 2.81e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2024478129  106 TILHLAARFGHHEVIEWLLRFGgSDPTAATDTGALPVHYAAAKGDFPSLRLLL 158
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKG-ADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 171-298 3.65e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 54.49  E-value: 3.65e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129  171 TGATPLYLACQEGHLEIIQYLVKDcGADPHVRANDGMTPLHAAAQMGHNTVIVWLMSFTTVSLSERDDDgatAMHFAASR 250
Cdd:PLN03192   557 KGRTPLHIAASKGYEDCVLVLLKH-ACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAGD---LLCTAAKR 632

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 2024478129  251 GHAKVLSWLLLHGGEI-TADGWGGTPLHDAAENGELECCQILVVNGADL 298
Cdd:PLN03192   633 NDLTAMKELLKQGLNVdSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
Ank_4 pfam13637
Ankyrin repeats (many copies);
242-292 4.20e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.65  E-value: 4.20e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2024478129  242 TAMHFAASRGHAKVLSWLLLHGGEITA-DGWGGTPLHDAAENGELECCQILV 292
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAvDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
38-90 4.37e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.65  E-value: 4.37e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2024478129   38 SPAHHAARAGRLACLRYLAaEAALRGDARARNGATPAHDAAATGNLACLQWLL 90
Cdd:pfam13637    3 TALHAAAASGHLELLRLLL-EKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 98-268 4.60e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 54.49  E-value: 4.60e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129   98 QDTDNSGATILHLAARFGHHEVIEWLLRfGGSDPTAATDTGALPVHYAAAKGDFPSLRLLLGH-CpsTLSAQTKTGATPL 176
Cdd:PLN03192   519 EHDDPNMASNLLTVASTGNAALLEELLK-AKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHaC--NVHIRDANGNTAL 595

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129  177 YLACQEGHLEIIQYLVKDCGA-DPHVrandGMTPLHAAAQMGHNTVIVWLMSFTtVSLSERDDDGATAMHFAASRGHAKV 255
Cdd:PLN03192   596 WNAISAKHHKIFRILYHFASIsDPHA----AGDLLCTAAKRNDLTAMKELLKQG-LNVDSEDHQGATALQVAMAEDHVDM 670

                          170
                   ....*....|...
gi 2024478129  256 LSWLLLHGGEITA 268
Cdd:PLN03192   671 VRLLIMNGADVDK 683
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 183-324 1.72e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 51.92  E-value: 1.72e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129  183 GHLEIIQYLVkDCGADPHVRANDGMTPLHAAAQMGHNTVIVWLMSFTTVSlSERDDDGATAMHFAASRGHAKVLSWLLLH 262
Cdd:PHA02875    13 GELDIARRLL-DIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIP-DVKYPDIESELHDAVEEGDVKAVEELLDL 90

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024478129  263 GGEITADGW--GGTPLHDAAENGELECCQILVVNGADLSIRDQDGYTAADLADYNGHIHCAKYL 324
Cdd:PHA02875    91 GKFADDVFYkdGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELL 154
Ank_5 pfam13857
Ankyrin repeats (many copies);
89-145 6.25e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.64  E-value: 6.25e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2024478129   89 LLTQGGCGVQDTDNSGATILHLAARFGHHEVIEWLLRFgGSDPTAATDTGALPVHYA 145
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAY-GVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 78-186 1.34e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.51  E-value: 1.34e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129   78 AATGNLACLQWLLTqGGCGVQDTDNSGATILHLAARFGHHEVIEWLLRFgGSDPTAATDTGALPVHYAAAKGDFPSLRLL 157
Cdd:PTZ00322    90 AASGDAVGARILLT-GGADPNCRDYDGRTPLHIACANGHVQVVRVLLEF-GADPTLLDKDGKTPLELAEENGFREVVQLL 167

                           90       100
                   ....*....|....*....|....*....
gi 2024478129  158 LGHCPSTLSAQTKtgATPLYLACQEGHLE 186
Cdd:PTZ00322   168 SRHSQCHFELGAN--AKPDSFTGKPPSLE 194
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 196-275 1.67e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.13  E-value: 1.67e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129  196 GADPHVRANDGMTPLHAAAQMGHNTVIVWLMSF-TTVSLSERddDGATAMHFAASRGHAKVLSWLLLHGGEITADGWGGT 274
Cdd:PTZ00322   105 GADPNCRDYDGRTPLHIACANGHVQVVRVLLEFgADPTLLDK--DGKTPLELAEENGFREVVQLLSRHSQCHFELGANAK 182


                   .
gi 2024478129  275 P 275
Cdd:PTZ00322   183 P 183
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 9-201 1.71e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 48.83  E-value: 1.71e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129    9 AARQGDVEALRGLRAAGLL----RPGLRdalgaSPAHHAARAGRLACLRYLAAEAALRGDARARNGATPAHDAAATGNLA 84
Cdd:PHA02875    42 AMKFRDSEAIKLLMKHGAIpdvkYPDIE-----SELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLD 116

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129   85 CLQWLLTQGGcgvqDTDNSGA---TILHLAARFGHHEVIEWLLrfggsDPTAATDT----GALPVHYAAAKGDFPSLRLL 157
Cdd:PHA02875   117 IMKLLIARGA----DPDIPNTdkfSPLHLAVMMGDIKGIELLI-----DHKACLDIedccGCTPLIIAMAKGDIAICKML 187

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 2024478129  158 LGHCPSTLSAQTKTGATPLYLACQEGHLEIIQYLVKDcGADPHV 201
Cdd:PHA02875   188 LDSGANIDYFGKNGCVAALCYAIENNKIDIVRLFIKR-GADCNI 230
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 165-307 1.94e-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: 1.94e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129  165 LSAQTKTGATPLYLACQEGHLEIIQYLVKDCGADPHVRANDGMTPLHAAAQMGHNTVIVWLMSFT--------TVSLSEr 236
Cdd:cd22192     10 LLQQKRISESPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAApelvnepmTSDLYQ- 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129  237 dddGATAMHFAASRGHAKVLSWLLLHGGEIT---ADG------------WGGTPLHDAAENGELECCQILVVNGADLSIR 301
Cdd:cd22192     89 ---GETALHIAVVNQNLNLVRELIARGADVVsprATGtffrpgpknliyYGEHPLSFAACVGNEEIVRLLIEHGADIRAQ 165


                   ....*.
gi 2024478129  302 DQDGYT 307
Cdd:cd22192    166 DSLGNT 171
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 174-326 2.63e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 48.04  E-value: 2.63e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129  174 TPLYLACQEGHLEIIQYLVKDcGAD-PHVRANDGmTPLHAAAQMGHNTVIVWLM-----------------SFTT----- 230
Cdd:PHA02874    37 TPLIDAIRSGDAKIVELFIKH-GADiNHINTKIP-HPLLTAIKIGAHDIIKLLIdngvdtsilpipciekdMIKTildcg 114

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129  231 VSLSERDDDGATAMHFAASRGHAKVLSWLLLHGGEIT-ADGWGGTPLHDAAENGELECCQILVVNGADLSIRDQDGYTAA 309
Cdd:PHA02874   115 IDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNiEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPL 194

                          170
                   ....*....|....*..
gi 2024478129  310 DLADYNGHIHCAKYLRT 326
Cdd:PHA02874   195 HNAAEYGDYACIKLLID 211
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 154-307 3.22e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 47.74  E-value: 3.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129  154 LRLLL--GHCPSTlsaQTKTGATPLYLACQEGH-----LEIIQYLVKDcGADPHVRANDGMTPLHAAAQ--MGHNTVIVW 224
Cdd:PHA03100    51 VKILLdnGADINS---STKNNSTPLHYLSNIKYnltdvKEIVKLLLEY-GANVNAPDNNGITPLLYAISkkSNSYSIVEY 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129  225 LMSF---TTVSLSerddDGATAMHFAASRGHA--KVLSWLLLHGGEITA-----------------DGWGGTPLHDAAEN 282
Cdd:PHA03100   127 LLDNganVNIKNS----DGENLLHLYLESNKIdlKILKLLIDKGVDINAknrvnyllsygvpinikDVYGFTPLHYAVYN 202

                          170       180
                   ....*....|....*....|....*
gi 2024478129  283 GELECCQILVVNGADLSIRDQDGYT 307
Cdd:PHA03100   203 NNPEFVKYLLDLGANPNLVNKYGDT 227
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 118-294 3.53e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 47.95  E-value: 3.53e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129  118 EVIEWLLRFGGSDPTAATDTGALPVHYAAAKGDFPSLRLLL--GHCPSTLSaqtKTGATPLYLACQEGHLEIIQYLVKDc 195
Cdd:PHA02878   148 EITKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLsyGANVNIPD---KTNNSPLHHAVKHYNKPIVHILLEN- 223

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129  196 GADPHVRANDGMTPLHAAAQMGHNTVIVWLMSFTTVSLSERDD-DGATAMHFAASrgHAKVLSWLLLHGGEITADGWGG- 273
Cdd:PHA02878   224 GASTDARDKCGNTPLHISVGYCKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIK--SERKLKLLLEYGADINSLNSYKl 301

                          170       180
                   ....*....|....*....|..
gi 2024478129  274 TPLHDAAEN-GELECCQILVVN 294
Cdd:PHA02878   302 TPLSSAVKQyLCINIGRILISN 323
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 146-227 5.84e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.20  E-value: 5.84e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129  146 AAKGDFPSLRLLLGHCPSTlSAQTKTGATPLYLACQEGHLEIIQYLVkDCGADPHVRANDGMTPLHAAAQMGHNTVIVWL 225
Cdd:PTZ00322    90 AASGDAVGARILLTGGADP-NCRDYDGRTPLHIACANGHVQVVRVLL-EFGADPTLLDKDGKTPLELAEENGFREVVQLL 167


                   ..
gi 2024478129  226 MS 227
Cdd:PTZ00322   168 SR 169
PHA02946 PHA02946
ankyin-like protein; Provisional
 90-250 1.13e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 46.20  E-value: 1.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129   90 LTQGGCGVQDTDNSGATILHLAARFGHHEVIEWLLRFgGSDPTAATDTGALPVHYAAAKGD--FPSLRLLLGHCPSTLSA 167
Cdd:PHA02946    58 LLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTH-GADPNACDKQHKTPLYYLSGTDDevIERINLLVQYGAKINNS 136

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129  168 QTKTGATPLyLACQEGHLEIIQYLVKdCGADPHVRANDGMTPLHAAAqMGHN---TVIVWLMSFtTVSLSERDDDGATAM 244
Cdd:PHA02946   137 VDEEGCGPL-LACTDPSERVFKKIMS-IGFEARIVDKFGKNHIHRHL-MSDNpkaSTISWMMKL-GISPSKPDHDGNTPL 212


                   ....*.
gi 2024478129  245 HFAASR 250
Cdd:PHA02946   213 HIVCSK 218
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 104-127 2.44e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 39.55  E-value: 2.44e-04
                           10        20
                   ....*....|....*....|....
gi 2024478129  104 GATILHLAARFGHHEVIEWLLRFG 127
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENG 25
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 7-215 2.77e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.05  E-value: 2.77e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129    7 LQAARQGDVEALRGLRAAGLLRPGLrDALGASPAHHAARAGRLACLRYLAAEAALRGDARARNGATPAHDAAATG-NLAC 85
Cdd:PHA02876   245 LKAIRNEDLETSLLLYDAGFSVNSI-DDCKNTPLHHASQAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGyDTEN 323

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129   86 LQWLLTQGGcGVQDTDNSGATILHLAARFGHHEVIEWLLRFGGSDPTAATDTGALPVHYAAAKGDFPSLRLLLGHCPSTL 165
Cdd:PHA02876   324 IRTLIMLGA-DVNAADRLYITPLHQASTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIE 402

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 2024478129  166 SAQTKTGATPLYLACQEGHLEIIQYLVkDCGADPHVRANDGMTPLHAAAQ 215
Cdd:PHA02876   403 ALSQKIGTALHFALCGTNPYMSVKTLI-DRGANVNSKNKDLSTPLHYACK 451
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 245-364 3.32e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.89  E-value: 3.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129  245 HFAASrGHAkVLSWLLLHGGEIT--ADGWGGTPLHDAAENGELECCQILVVNGADLSIRDQDGYTAADLADYNGhihcak 322
Cdd:PTZ00322    88 QLAAS-GDA-VGARILLTGGADPncRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENG------ 159

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2024478129  323 yLRTVENMSVEHrvlSRDPSADGECRQPDSGMSSPNTTASAP 364
Cdd:PTZ00322   160 -FREVVQLLSRH---SQCHFELGANAKPDSFTGKPPSLEDSP 197
Ank_5 pfam13857
Ankyrin repeats (many copies);
157-213 4.03e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.64  E-value: 4.03e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2024478129  157 LLGHCPSTLSAQTKTGATPLYLACQEGHLEIIQYLVKDcGADPHVRANDGMTPLHAA 213
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAY-GVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 172-201 4.14e-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: 38.72  E-value: 4.14e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 2024478129   172 GATPLYLACQEGHLEIIQYLVkDCGADPHV 201
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLL-DKGADINA 30
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 172-324 5.92e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 43.83  E-value: 5.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129  172 GATPLYLACQEGHLEIIQYLVKDcGADPHVRANDGMTPLHAAAQMGHNTVIVWLMSFTTVSLSERDDDGATAMHFAASRG 251
Cdd:PHA02875    35 GISPIKLAMKFRDSEAIKLLMKH-GAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILK 113

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024478129  252 HAKVLSWLLLHGGEI---TADGWggTPLHDAAENGELECCQILVVNGADLSIRDQDGYTAADLADYNGHIHCAKYL 324
Cdd:PHA02875   114 KLDIMKLLIARGADPdipNTDKF--SPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKML 187
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 172-204 6.17e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.42  E-value: 6.17e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 2024478129  172 GATPLYLAC-QEGHLEIIQYLVkDCGADPHVRAN 204
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLL-SKGADVNARDK 34
Ank_5 pfam13857
Ankyrin repeats (many copies);
191-247 6.73e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.87  E-value: 6.73e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2024478129  191 LVKDCGADPHVRANDGMTPLHAAAQMGHNTVIVWLMSFtTVSLSERDDDGATAMHFA 247
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAY-GVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 269-302 1.13e-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: 37.65  E-value: 1.13e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 2024478129  269 DGWggTPLHDAA-ENGELECCQILVVNGADLSIRD 302
Cdd:pfam00023    1 DGN--TPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 9-145 1.16e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 43.03  E-value: 1.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129    9 AARQGDVEALRGLRAAGLlRPGLRDALGASPAHHAARAGRLACLRYLAAEAALrGDARARNGATPAHDAAATGNLACLQW 88
Cdd:PHA02874   131 AIKKGDLESIKMLFEYGA-DVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAY-ANVKDNNGESPLHNAAEYGDYACIKL 208

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2024478129   89 LLTQGGcGVQDTDNSGATILHLAARFgHHEVIEWLLRFGGSDPTAAtdTGALPVHYA 145
Cdd:PHA02874   209 LIDHGN-HIMNKCKNGFTPLHNAIIH-NRSAIELLINNASINDQDI--DGSTPLHHA 261
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 235-317 1.68e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 42.55  E-value: 1.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129  235 ERDDDGATAMHF--AASRGHAKVLSWLLLHGGEI-TADGWGGTPLHDAAENGELECCQILVVNGADLSIRDQDGYTAADL 311
Cdd:PLN03192   518 GEHDDPNMASNLltVASTGNAALLEELLKAKLDPdIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWN 597


                   ....*.
gi 2024478129  312 ADYNGH 317
Cdd:PLN03192   598 AISAKH 603
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 104-129 1.69e-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: 1.69e-03
                            10        20
                    ....*....|....*....|....*.
gi 2024478129   104 GATILHLAARFGHHEVIEWLLRFGGS 129
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGAD 27
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 172-201 2.25e-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: 2.25e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 2024478129  172 GATPLYLACQEGHLEIIQYLVkDCGADPHV 201
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLL-ENGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
55-111 2.72e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.33  E-value: 2.72e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2024478129   55 LAAEAALRGDARARNGATPAHDAAATGNLACLQWLLTqGGCGVQDTDNSGATILHLA 111
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLA-YGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
8-55 3.66e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.87  E-value: 3.66e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 2024478129    8 QAARQGDVEALRGLRAAGLlRPGLRDALGASPAHHAARAGRLACLRYL 55
Cdd:pfam13637    7 AAAASGHLELLRLLLEKGA-DINAVDGNGETALHFAASNGNVEVLKLL 53
WH2 pfam02205
WH2 motif; The WH2 motif (for Wiskott Aldrich syndrome homology region 2) has been shown in ...
 615-640 4.24e-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: 35.94  E-value: 4.24e-03
                           10        20
                   ....*....|....*....|....*.
gi 2024478129  615 PTGDNSELLAEIKAGKSLKPTPQSKG 640
Cdd:pfam02205    1 GGGGRGALLADIRAGKKLKKVEETND 26
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 238-307 4.81e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 41.02  E-value: 4.81e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024478129  238 DDGATAMHFAASRGHAKVLSWLLLHGGEITA-DGWGGTPLHDAAENGELECCQILVVNGADLSIRDQDGYT 307
Cdd:PHA02878   166 HKGNTALHYATENKDQRLTELLLSYGANVNIpDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNT 236
Ank_5 pfam13857
Ankyrin repeats (many copies);
236-277 5.49e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.17  E-value: 5.49e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 2024478129  236 RDDDGATAMHFAASRGHAKVLSWLLLHGGEITA-DGWGGTPLH 277
Cdd:pfam13857   12 LDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLkDEEGLTALD 54
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 104-136 5.81e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 35.73  E-value: 5.81e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 2024478129  104 GATILHLAA-RFGHHEVIEWLLRFgGSDPTAATD 136
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSK-GADVNARDK 34
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 172-260 6.11e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 40.55  E-value: 6.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129  172 GATPLYLACQEGHLEIIQYLVKDCGADPHVRAND--GMTPLHAAAQMGHNTV-----------IVWLMS---FTTVSLSE 235
Cdd:cd22193    123 GELPLSLAACTNQPDIVQYLLENEHQPADIEAQDsrGNTVLHALVTVADNTKentkfvtrmydMILIRGaklCPTVELEE 202

                           90       100
                   ....*....|....*....|....*.
gi 2024478129  236 -RDDDGATAMHFAASRGHAKVLSWLL 260
Cdd:cd22193    203 iRNNDGLTPLQLAAKMGKIEILKYIL 228
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 100-213 7.84e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 40.25  E-value: 7.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024478129  100 TDNSGATILHLAARFGHHEVIEWLLRFgGSDPTAATDTGALPVHYAAAKGDFPSLRLLLGHCPSTlSAQTKTGATPLYLA 179
Cdd:PHA02878   164 DRHKGNTALHYATENKDQRLTELLLSY-GANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAST-DARDKCGNTPLHIS 241

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2024478129  180 CqeGHL---EIIQYLVKDcGADPHVRAN-DGMTPLHAA 213
Cdd:PHA02878   242 V--GYCkdyDILKLLLEH-GVDVNAKSYiLGLTALHSS 276
 
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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