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Conserved domains on  [gi|451994179|gb|EMD86650|]
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hypothetical protein COCHEDRAFT_1051713, partial [Bipolaris maydis C5]

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];
1-65 2.65e-15

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 67.29  E-value: 2.65e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 451994179   1 LNWVDKNGNTALICAASRGIPKMVELLLEFGADIDAQNRHGRTALMEAVLWGHLASVNYILDKGA 65
Cdd:COG0666  146 VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGA 210
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-65 2.65e-15

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 67.29  E-value: 2.65e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 451994179   1 LNWVDKNGNTALICAASRGIPKMVELLLEFGADIDAQNRHGRTALMEAVLWGHLASVNYILDKGA 65
Cdd:COG0666  146 VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGA 210
Ank_2 pfam12796
Ankyrin repeats (3 copies);
2-65 5.29e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 60.13  E-value: 5.29e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 451994179   2 NWVDKNGNTALICAASRGIPKMVELLLEFgADIDAQNrHGRTALMEAVLWGHLASVNYILDKGA 65
Cdd:pfam12796 24 NLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGA 85
PHA03095 PHA03095
ankyrin-like protein; Provisional
 1-65 2.64e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 45.02  E-value: 2.64e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 451994179   1 LNWVDKNGNTAL-ICAASRGI-PKMVELLLEFGADIDAQNRHGRTALmeAVLWGH----LASVNYILDKGA 65
Cdd:PHA03095 110 VNAKDKVGRTPLhVYLSGFNInPKVIRLLLRKGADVNALDLYGMTPL--AVLLKSrnanVELLRLLIDAGA 178
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 15-50 1.66e-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: 1.66e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 451994179  15 AASRGIPKMVELLLEFGADIDAQNRHGRTALMEAVL 50
Cdd:cd22192  143 AACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVL 178
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 7-36 3.43e-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: 31.40  E-value: 3.43e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 451994179    7 NGNTALICAASRGIPKMVELLLEFGADIDA 36
Cdd:smart00248  1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-65 2.65e-15

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 67.29  E-value: 2.65e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 451994179   1 LNWVDKNGNTALICAASRGIPKMVELLLEFGADIDAQNRHGRTALMEAVLWGHLASVNYILDKGA 65
Cdd:COG0666  146 VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGA 210
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-65 5.13e-14

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 63.82  E-value: 5.13e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 451994179   1 LNWVDKNGNTALICAASRGIPKMVELLLEFGADIDAQNRHGRTALMEAVLWGHLASVNYILDKGA 65
Cdd:COG0666  113 VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGA 177
Ank_2 pfam12796
Ankyrin repeats (3 copies);
2-65 5.29e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 60.13  E-value: 5.29e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 451994179   2 NWVDKNGNTALICAASRGIPKMVELLLEFgADIDAQNrHGRTALMEAVLWGHLASVNYILDKGA 65
Cdd:pfam12796 24 NLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGA 85
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-65 8.78e-12

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 57.66  E-value: 8.78e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 451994179   1 LNWVDKNGNTALICAASRGIPKMVELLLEFGADIDAQNRHGRTALMEAVLWGHLASVNYILDKGA 65
Cdd:COG0666  179 VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-65 2.92e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 56.12  E-value: 2.92e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 451994179   1 LNWVDKNGNTALICAASRGIPKMVELLLEFGADIDAQNRHGRTALMEAVLWGHLASVNYILDKGA 65
Cdd:COG0666   80 INAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGA 144
Ank_4 pfam13637
Ankyrin repeats (many copies);
8-61 6.02e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.50  E-value: 6.02e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 451994179   8 GNTALICAASRGIPKMVELLLEFGADIDAQNRHGRTALMEAVLWGHLASVNYIL 61
Cdd:pfam13637  1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
12-63 6.29e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 47.42  E-value: 6.29e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 451994179  12 LICAASRGIPKMVELLLEFGADIDAQNRHGRTALMEAVLWGHLASVNYILDK 63
Cdd:pfam12796  1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH 52
PHA03095 PHA03095
ankyrin-like protein; Provisional
 1-65 2.64e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 45.02  E-value: 2.64e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 451994179   1 LNWVDKNGNTAL-ICAASRGI-PKMVELLLEFGADIDAQNRHGRTALmeAVLWGH----LASVNYILDKGA 65
Cdd:PHA03095 110 VNAKDKVGRTPLhVYLSGFNInPKVIRLLLRKGADVNALDLYGMTPL--AVLLKSrnanVELLRLLIDAGA 178
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 24-65 2.05e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 42.73  E-value: 2.05e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 451994179  24 VELLLEFGADIDAQNRHGRTALMEAVLWGHLASVNYILDKGA 65
Cdd:PHA03100 175 VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGA 216
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 12-65 2.91e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 42.16  E-value: 2.91e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 451994179  12 LIC-AASRGIPKMVELLLEFGADIDAQNRHGRTALMEAVLWGHLASVNYILDKGA 65
Cdd:PLN03192 625 LLCtAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGA 679
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 1-65 3.22e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 41.96  E-value: 3.22e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 451994179   1 LNWVDKNGNTALICAASRGIPKMVELLLEFGADIDAQNRHGRTALMEAVLWGHLASVNYILDKGA 65
Cdd:PHA03100 185 INIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 7-39 3.98e-06

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: 38.81  E-value: 3.98e-06
                         10        20        30
                 ....*....|....*....|....*....|....
gi 451994179   7 NGNTALICAASR-GIPKMVELLLEFGADIDAQNR 39
Cdd:pfam00023  1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
Ank_5 pfam13857
Ankyrin repeats (many copies);
1-45 7.13e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.87  E-value: 7.13e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 451994179   1 LNWVDKNGNTALICAASRGIPKMVELLLEFGADIDAQNRHGRTAL 45
Cdd:pfam13857  9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
Ank_2 pfam12796
Ankyrin repeats (3 copies);
4-38 1.30e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 38.94  E-value: 1.30e-05
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 451994179   4 VDKNGNTALICAASRGIPKMVELLLEFGADIDAQN 38
Cdd:pfam12796 57 LKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 5-53 7.54e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 38.31  E-value: 7.54e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 451994179   5 DKNGNTALICAASRGIPKMVELLLEFGADIDAQNRHGRTALMEAVLWGH 53
Cdd:PLN03192 555 DSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKH 603
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 1-64 1.42e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 37.64  E-value: 1.42e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 451994179   1 LNWVDKNGNTALICAASRGIPKMVELLLEFGADIDAQNRHGRTALMEAVLWGHLASVNYILDKG 64
Cdd:PHA02874 150 VNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHG 213
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 2-49 1.45e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 37.57  E-value: 1.45e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 451994179   2 NWVDKNGNTALICAASRGIPKMVELLLEFGADIDAQNRHGRTALMEAV 49
Cdd:PTZ00322 109 NCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAE 156
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 24-65 1.52e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 37.57  E-value: 1.52e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 451994179  24 VELLLEFGADIDAQNRHGRTALMEAVLWGHLASVNYILDKGA 65
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGA 139
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 7-36 2.07e-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: 34.54  E-value: 2.07e-04
                         10        20        30
                 ....*....|....*....|....*....|
gi 451994179   7 NGNTALICAASRGIPKMVELLLEFGADIDA 36
Cdd:pfam13606  1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
5-65 2.46e-04

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 36.86  E-value: 2.46e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 451994179   5 DKNGNTALICAASRGIPKMVELLLEFGADIDAQNRHGRTALMEAVLWGHLASVNYILDKGA 65
Cdd:COG0666  216 DNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALL 276
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
5-65 2.93e-04

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 36.47  E-value: 2.93e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 451994179   5 DKNGNTALICAASRGIPKMVELLLEFGADIDAQNRHGRTALMEAVLWGHLASVNYILDKGA 65
Cdd:COG0666   51 DALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGA 111
PHA03095 PHA03095
ankyrin-like protein; Provisional
 1-65 8.85e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 35.39  E-value: 8.85e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 451994179   1 LNWVDKNGNTALICAASRGI-PKMVELLLEFGADIDAQNRHGRTALME--AVLWGHLASVNYILDKGA 65
Cdd:PHA03095  76 VNAPERCGFTPLHLYLYNATtLDVIKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGA 143
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 2-65 1.10e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 35.03  E-value: 1.10e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 451994179   2 NWVDKNGNTALICAASR--GIPKMVELLLEFGADIDAQNRHGRTALMEAVLWGH--LASVNYILDKGA 65
Cdd:PHA03100 100 NAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGV 167
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 15-50 1.66e-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: 1.66e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 451994179  15 AASRGIPKMVELLLEFGADIDAQNRHGRTALMEAVL 50
Cdd:cd22192  143 AACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVL 178
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 7-36 3.43e-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: 31.40  E-value: 3.43e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 451994179    7 NGNTALICAASRGIPKMVELLLEFGADIDA 36
Cdd:smart00248  1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 15-62 3.57e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 33.50  E-value: 3.57e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 451994179  15 AASRGIPKMVELLLEFGADIDAQNRHGRTALMEAVLWGHLASVNYILD 62
Cdd:PHA02876 185 AAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIID 232
Se-cys_synth_N pfam12390
Selenocysteine synthase N terminal; This domain family is found in bacteria, and is ...
 18-49 4.56e-03

Selenocysteine synthase N terminal; This domain family is found in bacteria, and is approximately 40 amino acids in length. The family is found in association with pfam03841. There is a single completely conserved residue P that may be functionally important. This family is the N terminal region of selenocysteine synthase which catalyzes the conversion of seryl-tRNA(Sec) into selenocysteyl-tRNA(Sec).


Pssm-ID: 432519  Cd Length: 40  Bit Score: 31.21  E-value: 4.56e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 451994179  18 RGIPKmVELLLEFGADIDAQNRHGRTALMEAV 49
Cdd:pfam12390  2 RRLPS-VDELLADPELAALLARYGRTLVVEAV 32
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 22-65 5.00e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 33.11  E-value: 5.00e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 451994179  22 KMVELLLEFGADIDAQNRHGRTALMEAVLWGHLASVNYILDKGA 65
Cdd:PHA02876 159 LIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGA 202
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 40-65 5.92e-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: 30.63  E-value: 5.92e-03
                          10        20
                  ....*....|....*....|....*.
gi 451994179   40 HGRTALMEAVLWGHLASVNYILDKGA 65
Cdd:smart00248  1 DGRTPLHLAAENGNLEVVKLLLDKGA 26
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 10-65 7.79e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 32.66  E-value: 7.79e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 451994179  10 TALICAASRGIPKMVELLLEFGADIDAQNRHGRTALMEAVLWGHLASVNYILDKGA 65
Cdd:PHA02875 137 SPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGA 192
TRPV4 cd22195
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed ...
 8-42 8.87e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed broadly in neuronal and non-neuronal cells. It is activated by various stimuli, including hypo-osmolarity, warm temperature, and chemical ligands. TRPV4 acts in physiological functions such as osmoregulation and thermoregulation. It also has a role in mechanosensation in the vascular endothelium and urinary tract, and in cell barrier formation in vascular and epidermal tissues. Knockout mice studies suggested the functional importance of TRPV4 in the central nervous system, nociception, and bone formation. TRPV4 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411979 [Multi-domain]  Cd Length: 733  Bit Score: 32.52  E-value: 8.87e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 451994179   8 GNTALICAASRGIPKMVELLLEFGADIDAQNRhGR 42
Cdd:cd22195  137 GQTALHIAIERRCKHYVELLVEKGADVHAQAR-GR 170
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 20-65 9.40e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 32.33  E-value: 9.40e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 451994179  20 IPKMVELLLEFGADIDAQNRHGRTALMEAVLW--GHLASVNYILDKGA 65
Cdd:PHA03100  85 VKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGA 132
 
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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