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Conserved domains on  [gi|2307248126|emb|CAG8231360|]
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unnamed protein product [Penicillium salamii]

Protein Classification

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

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
3-90 4.08e-15

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 68.06  E-value: 4.08e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307248126   3 ELLLNRrELDINIQNQARHSALSYAIHYGNFSTVKSVLEQpNVRVDIKHKHGRTALHLAVFAGRIGFVHLLLSRGSDPDL 82
Cdd:COG0666   137 KLLLEA-GADVNAQDNDGNTPLHLAAANGNLEIVKLLLEA-GADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNA 214


                  ....*...
gi 2307248126  83 EDDSGHSA 90
Cdd:COG0666   215 KDNDGKTA 222
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
3-90 4.08e-15

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 68.06  E-value: 4.08e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307248126   3 ELLLNRrELDINIQNQARHSALSYAIHYGNFSTVKSVLEQpNVRVDIKHKHGRTALHLAVFAGRIGFVHLLLSRGSDPDL 82
Cdd:COG0666   137 KLLLEA-GADVNAQDNDGNTPLHLAAANGNLEIVKLLLEA-GADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNA 214


                  ....*...
gi 2307248126  83 EDDSGHSA 90
Cdd:COG0666   215 KDNDGKTA 222
Ank_2 pfam12796
Ankyrin repeats (3 copies);
3-84 5.17e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 61.29  E-value: 5.17e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307248126  3 ELLLNRRElDINIQNQARHSALSYAIHYGNFSTVKSVLEQPNVRVDikhKHGRTALHLAVFAGRIGFVHLLLSRGSDPDL 82
Cdd:pfam12796 14 KLLLENGA-DANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLK---DNGRTALHYAARSGHLEIVKLLLEKGADINV 89


                 ..
gi 2307248126 83 ED 84
Cdd:pfam12796 90 KD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 1-89 1.09e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 41.96  E-value: 1.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307248126   1 MRELLLNRReLDINIQNQARHSALSYAIHYGNFST------------------VKSVLEQpNVRVDIKHKHGRTALHLAV 62
Cdd:PHA03100  123 IVEYLLDNG-ANVNIKNSDGENLLHLYLESNKIDLkilkllidkgvdinaknrVNYLLSY-GVPINIKDVYGFTPLHYAV 200

                          90       100
                  ....*....|....*....|....*..
gi 2307248126  63 FAGRIGFVHLLLSRGSDPDLEDDSGHS 89
Cdd:PHA03100  201 YNNNPEFVKYLLDLGANPNLVNKYGDT 227
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 53-82 1.22e-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: 36.03  E-value: 1.22e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 2307248126  53 HGRTALHLAVFAGRIGFVHLLLSRGSDPDL 82
Cdd:smart00248  1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 1-79 1.27e-03

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: 36.14  E-value: 1.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307248126   1 MRELLLNRReldINIQNQARH--SALSYAIHYGNFSTVKSVLEqpNVRVDIKHK------HGRTALHLAVFAGRIGFVHL 72
Cdd:cd22192    33 IKKLLKCPS---CDLFQRGALgeTALHVAALYDNLEAAVVLME--AAPELVNEPmtsdlyQGETALHIAVVNQNLNLVRE 107


                  ....*..
gi 2307248126  73 LLSRGSD 79
Cdd:cd22192   108 LIARGAD 114
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
3-90 4.08e-15

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 68.06  E-value: 4.08e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307248126   3 ELLLNRrELDINIQNQARHSALSYAIHYGNFSTVKSVLEQpNVRVDIKHKHGRTALHLAVFAGRIGFVHLLLSRGSDPDL 82
Cdd:COG0666   137 KLLLEA-GADVNAQDNDGNTPLHLAAANGNLEIVKLLLEA-GADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNA 214


                  ....*...
gi 2307248126  83 EDDSGHSA 90
Cdd:COG0666   215 KDNDGKTA 222
Ank_2 pfam12796
Ankyrin repeats (3 copies);
3-84 5.17e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 61.29  E-value: 5.17e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307248126  3 ELLLNRRElDINIQNQARHSALSYAIHYGNFSTVKSVLEQPNVRVDikhKHGRTALHLAVFAGRIGFVHLLLSRGSDPDL 82
Cdd:pfam12796 14 KLLLENGA-DANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLK---DNGRTALHYAARSGHLEIVKLLLEKGADINV 89


                 ..
gi 2307248126 83 ED 84
Cdd:pfam12796 90 KD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
4-90 2.55e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 57.66  E-value: 2.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307248126   4 LLLNRRELDINIQNQARHSALSYAIHYGNFSTVKSVLEQpNVRVDIKHKHGRTALHLAVFAGRIGFVHLLLSRGSDPDLE 83
Cdd:COG0666    71 LLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEA-GADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQ 149


                  ....*..
gi 2307248126  84 DDSGHSA 90
Cdd:COG0666   150 DNDGNTP 156
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
3-90 3.35e-08

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 48.80  E-value: 3.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307248126   3 ELLLNRReLDINIQNQARHSALSYAIHYGNFSTVKSVLEQpNVRVDIKHKHGRTALHLAVFAGRIGFVHLLLSRGSDPDL 82
Cdd:COG0666   170 KLLLEAG-ADVNARDNDGETPLHLAAENGHLEIVKLLLEA-GADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNA 247


                  ....*...
gi 2307248126  83 EDDSGHSA 90
Cdd:COG0666   248 KDKDGLTA 255
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 1-89 1.09e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 41.96  E-value: 1.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307248126   1 MRELLLNRReLDINIQNQARHSALSYAIHYGNFST------------------VKSVLEQpNVRVDIKHKHGRTALHLAV 62
Cdd:PHA03100  123 IVEYLLDNG-ANVNIKNSDGENLLHLYLESNKIDLkilkllidkgvdinaknrVNYLLSY-GVPINIKDVYGFTPLHYAV 200

                          90       100
                  ....*....|....*....|....*..
gi 2307248126  63 FAGRIGFVHLLLSRGSDPDLEDDSGHS 89
Cdd:PHA03100  201 YNNNPEFVKYLLDLGANPNLVNKYGDT 227
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
3-90 2.91e-05

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 40.71  E-value: 2.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307248126   3 ELLLNRRELDINIQNQARHSALSYAIHYGNFSTVKSVLEQPNVRVDIKHKHGRTALHLAVFAGRIGFVHLLLSRGSDPDL 82
Cdd:COG0666    36 LLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNA 115


                  ....*...
gi 2307248126  83 EDDSGHSA 90
Cdd:COG0666   116 RDKDGETP 123
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 53-89 6.85e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 39.50  E-value: 6.85e-05
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2307248126  53 HGRTALHLAVFAGRIGFVHLLLSRGSDPDLEDDSGHS 89
Cdd:PTZ00322  114 DGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKT 150
Ank_4 pfam13637
Ankyrin repeats (many copies);
20-74 7.05e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.87  E-value: 7.05e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 2307248126 20 RHSALSYAIHYGNFSTVKSVLEQPnVRVDIKHKHGRTALHLAVFAGRIGFVHLLL 74
Cdd:pfam13637  1 ELTALHAAAASGHLELLRLLLEKG-ADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
5-61 7.88e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.94  E-value: 7.88e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 2307248126  5 LLNRRELDINIQNQARHSALSYAIHYGNFSTVKSVLEqPNVRVDIKHKHGRTALHLA 61
Cdd:pfam13857  1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLA-YGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 53-85 8.42e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.50  E-value: 8.42e-05
                         10        20        30
                 ....*....|....*....|....*....|....
gi 2307248126 53 HGRTALHLAV-FAGRIGFVHLLLSRGSDPDLEDD 85
Cdd:pfam00023  1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
Ank_5 pfam13857
Ankyrin repeats (many copies);
40-91 1.15e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.56  E-value: 1.15e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 2307248126 40 LEQPNVRVDIKHKHGRTALHLAVFAGRIGFVHLLLSRGSDPDLEDDSGHSAW 91
Cdd:pfam13857  2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 53-82 1.22e-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: 36.03  E-value: 1.22e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 2307248126  53 HGRTALHLAVFAGRIGFVHLLLSRGSDPDL 82
Cdd:smart00248  1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 22-82 1.47e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 38.82  E-value: 1.47e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2307248126  22 SALSYAIHYGNFSTVKSVLEQPNVRVDIKHKHGRTALHLAVFAGRIGFVHLLLSRGSDPDL 82
Cdd:PHA02875   70 SELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDI 130
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 11-89 3.33e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 37.64  E-value: 3.33e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2307248126  11 LDINIQNQARHSALSYAIHYGNFSTVKSVLEQpNVRVDIKHKHGRTALHLAVFAGRIGFVHLLLSRGSDPDLEDDSGHS 89
Cdd:PHA02874  115 IDVNIKDAELKTFLHYAIKKGDLESIKMLFEY-GADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGES 192
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 32-87 3.74e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 37.64  E-value: 3.74e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2307248126  32 NFSTVKSVLEQpNVRVDIKHKHGRTALHLAVFAGRIGFVHLLLSRGSDPDLEDDSG 87
Cdd:PHA02874  103 EKDMIKTILDC-GIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNG 157
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 13-78 4.04e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 37.25  E-value: 4.04e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2307248126  13 INIQNQARHSALSYAIHYGNFSTVKSVLEQPNvRVDIKHKHGRTALHLAVFAGRiGFVHLLLSRGS 78
Cdd:PHA02874  183 ANVKDNNGESPLHNAAEYGDYACIKLLIDHGN-HIMNKCKNGFTPLHNAIIHNR-SAIELLINNAS 246
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 1-79 1.27e-03

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: 36.14  E-value: 1.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307248126   1 MRELLLNRReldINIQNQARH--SALSYAIHYGNFSTVKSVLEqpNVRVDIKHK------HGRTALHLAVFAGRIGFVHL 72
Cdd:cd22192    33 IKKLLKCPS---CDLFQRGALgeTALHVAALYDNLEAAVVLME--AAPELVNEPmtsdlyQGETALHIAVVNQNLNLVRE 107


                  ....*..
gi 2307248126  73 LLSRGSD 79
Cdd:cd22192   108 LIARGAD 114
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 53-81 1.67e-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: 33.00  E-value: 1.67e-03
                         10        20
                 ....*....|....*....|....*....
gi 2307248126 53 HGRTALHLAVFAGRIGFVHLLLSRGSDPD 81
Cdd:pfam13606  1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 1-82 1.98e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 35.35  E-value: 1.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2307248126   1 MRELLLNRRELdINIQNQARHSALSYAIHYGNFSTVKSVLEQpNVRVDIKHKHGR-TALHLAVFAGRIGFVHLLLSRGSD 79
Cdd:PHA02875  150 GIELLIDHKAC-LDIEDCCGCTPLIIAMAKGDIAICKMLLDS-GANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGAD 227


                  ...
gi 2307248126  80 PDL 82
Cdd:PHA02875  228 CNI 230
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 13-82 3.46e-03

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: 34.60  E-value: 3.46e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2307248126  13 INIQNQAR--HSALSYAIHYGNFSTVKSVLEQPNVRVDIKHKHGRTALHLAVFAGRIGFVHLLLSrgSDPDL 82
Cdd:cd22192     8 LHLLQQKRisESPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPEL 77
Ank_2 pfam12796
Ankyrin repeats (3 copies);
58-90 4.88e-03

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 33.17  E-value: 4.88e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 2307248126 58 LHLAVFAGRIGFVHLLLSRGSDPDLEDDSGHSA 90
Cdd:pfam12796  1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTA 33
 
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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