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Conserved domains on  [gi|568939808|ref|XP_006505239|]
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ankyrin repeat, SAM and basic leucine zipper domain-containing protein 1 isoform X1 [Mus musculus]

Protein Classification

ANKYR and SAM_ASZ1 domain-containing protein( domain architecture ID 12789531)

ANKYR and SAM_ASZ1 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
2-85 1.24e-21

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 92.71  E-value: 1.24e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939808   2 TPIMYAARDGHTQVVALLVAHGAEVNAQDENGYTALTWAARQGHKNVILKLLELGANKMLQTKDGRTPSEIAKRNKHLEI 81
Cdd:COG0666  155 TPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEI 234


                 ....
gi 568939808  82 FNFL 85
Cdd:COG0666  235 VKLL 238
SAM_ASZ1 cd09521
SAM domain of ASZ1 subfamily; SAM (sterile alpha motif) domain of ASZ1 (Ankyrin, SAM, leucine ...
 124-184 4.54e-20

SAM domain of ASZ1 subfamily; SAM (sterile alpha motif) domain of ASZ1 (Ankyrin, SAM, leucine Zipper) also known as GASZ (Germ cell-specific Ankyrin, SAM, leucine Zipper) subfamily is a potential protein-protein interaction domain. Proteins of this group are involved in the repression of transposable elements during spermatogenesis, oogenesis, and preimplantation embryogenesis. They support synthesis of PIWI-interacting RNA via association with some PIWI proteins, such as MILI and MIWI. This association is required for initiation and maintenance of retrotransposon repression during the meiosis. In mice lacking ASZ1, DNA damage and delayed germ cell maturation was observed due to retrotransposons releasing from their repressed state.


:

Pssm-ID: 188920  Cd Length: 64  Bit Score: 82.33  E-value: 4.54e-20
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568939808 124 YTAFGDLEIFLHGLGLEHMTDSLKEKDITLRHLLTMKKDELTKNGIAS-KDQQKILAALKEL 184
Cdd:cd09521    2 YSKLDDLELFLHGLELGHLTPLFKEHDVTFSQLLKMTEEDLEKIGITQpGDQKKILDAIKEV 63
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
2-85 1.24e-21

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 92.71  E-value: 1.24e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939808   2 TPIMYAARDGHTQVVALLVAHGAEVNAQDENGYTALTWAARQGHKNVILKLLELGANKMLQTKDGRTPSEIAKRNKHLEI 81
Cdd:COG0666  155 TPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEI 234


                 ....
gi 568939808  82 FNFL 85
Cdd:COG0666  235 VKLL 238
SAM_ASZ1 cd09521
SAM domain of ASZ1 subfamily; SAM (sterile alpha motif) domain of ASZ1 (Ankyrin, SAM, leucine ...
 124-184 4.54e-20

SAM domain of ASZ1 subfamily; SAM (sterile alpha motif) domain of ASZ1 (Ankyrin, SAM, leucine Zipper) also known as GASZ (Germ cell-specific Ankyrin, SAM, leucine Zipper) subfamily is a potential protein-protein interaction domain. Proteins of this group are involved in the repression of transposable elements during spermatogenesis, oogenesis, and preimplantation embryogenesis. They support synthesis of PIWI-interacting RNA via association with some PIWI proteins, such as MILI and MIWI. This association is required for initiation and maintenance of retrotransposon repression during the meiosis. In mice lacking ASZ1, DNA damage and delayed germ cell maturation was observed due to retrotransposons releasing from their repressed state.


Pssm-ID: 188920  Cd Length: 64  Bit Score: 82.33  E-value: 4.54e-20
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568939808 124 YTAFGDLEIFLHGLGLEHMTDSLKEKDITLRHLLTMKKDELTKNGIAS-KDQQKILAALKEL 184
Cdd:cd09521    2 YSKLDDLELFLHGLELGHLTPLFKEHDVTFSQLLKMTEEDLEKIGITQpGDQKKILDAIKEV 63
Ank_2 pfam12796
Ankyrin repeats (3 copies);
4-85 5.92e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 66.68  E-value: 5.92e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939808    4 IMYAARDGHTQVVALLVAHGAEVNAQDENGYTALTWAARQGHKNVILKLLELGANKMlqTKDGRTPSEIAKRNKHLEIFN 83
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLEIVK 78


                  ..
gi 568939808   84 FL 85
Cdd:pfam12796  79 LL 80
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 8-86 1.31e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.06  E-value: 1.31e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568939808   8 ARDGHTQVVALLVAHGAEVNAQDENGYTALTWAARQGHKNVILKLLELGANKMLQTKDGRTPSEIAKRNKHLEIFNFLS 86
Cdd:PTZ00322  90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 133-184 1.19e-04

SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.


Pssm-ID: 425739  Cd Length: 64  Bit Score: 39.56  E-value: 1.19e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568939808  133 FLHGLGLEHMTDSLKEKDITLRHLLTMKKDELTKNGIASK-DQQKILAALKEL 184
Cdd:pfam00536  11 WLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLKLGVTLLgHRKKILYAIQRL 63
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 3-85 7.00e-04

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 41.15  E-value: 7.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939808   3 PIMYAARDGHTQVVALLVAHGAEVNAQDENGYTALTWAARQGHK-------NVIL---KLLELGANKMLQTKDGRTPSEI 72
Cdd:cd22192  139 PLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKtfacqmyDLILsydKEDDLQPLDLVPNNQGLTPFKL 218

                         90
                 ....*....|...
gi 568939808  73 AKRNKHLEIFNFL 85
Cdd:cd22192  219 AAKEGNIVMFQHL 231
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 32-58 2.89e-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: 34.87  E-value: 2.89e-03
                           10        20
                   ....*....|....*....|....*..
gi 568939808    32 NGYTALTWAARQGHKNVILKLLELGAN 58
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
2-85 1.24e-21

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 92.71  E-value: 1.24e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939808   2 TPIMYAARDGHTQVVALLVAHGAEVNAQDENGYTALTWAARQGHKNVILKLLELGANKMLQTKDGRTPSEIAKRNKHLEI 81
Cdd:COG0666  155 TPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEI 234


                 ....
gi 568939808  82 FNFL 85
Cdd:COG0666  235 VKLL 238
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-85 2.71e-21

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 91.94  E-value: 2.71e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939808   1 MTPIMYAARDGHTQVVALLVAHGAEVNAQDENGYTALTWAARQGHKNVILKLLELGANKMLQTKDGRTPSEIAKRNKHLE 80
Cdd:COG0666  121 ETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLE 200


                 ....*
gi 568939808  81 IFNFL 85
Cdd:COG0666  201 IVKLL 205
SAM_ASZ1 cd09521
SAM domain of ASZ1 subfamily; SAM (sterile alpha motif) domain of ASZ1 (Ankyrin, SAM, leucine ...
 124-184 4.54e-20

SAM domain of ASZ1 subfamily; SAM (sterile alpha motif) domain of ASZ1 (Ankyrin, SAM, leucine Zipper) also known as GASZ (Germ cell-specific Ankyrin, SAM, leucine Zipper) subfamily is a potential protein-protein interaction domain. Proteins of this group are involved in the repression of transposable elements during spermatogenesis, oogenesis, and preimplantation embryogenesis. They support synthesis of PIWI-interacting RNA via association with some PIWI proteins, such as MILI and MIWI. This association is required for initiation and maintenance of retrotransposon repression during the meiosis. In mice lacking ASZ1, DNA damage and delayed germ cell maturation was observed due to retrotransposons releasing from their repressed state.


Pssm-ID: 188920  Cd Length: 64  Bit Score: 82.33  E-value: 4.54e-20
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568939808 124 YTAFGDLEIFLHGLGLEHMTDSLKEKDITLRHLLTMKKDELTKNGIAS-KDQQKILAALKEL 184
Cdd:cd09521    2 YSKLDDLELFLHGLELGHLTPLFKEHDVTFSQLLKMTEEDLEKIGITQpGDQKKILDAIKEV 63
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-85 1.56e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 81.15  E-value: 1.56e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939808   1 MTPIMYAARDGHTQVVALLVAHGAEVNAQDENGYTALTWAARQGHKNVILKLLELGANKMLQTKDGRTPSEIAKRNKHLE 80
Cdd:COG0666   88 NTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLE 167


                 ....*
gi 568939808  81 IFNFL 85
Cdd:COG0666  168 IVKLL 172
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-101 6.25e-16

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 76.92  E-value: 6.25e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939808   1 MTPIMYAARDGHTQVVALLVAHGAEVNAQDENGYTALTWAARQGHKNVILKLLELGANKMLQTKDGRTPSEIAKRNKHLE 80
Cdd:COG0666  187 ETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAAL 266

                         90       100
                 ....*....|....*....|.
gi 568939808  81 IFNFLSLTLNPLEGKLQQLTK 101
Cdd:COG0666  267 IVKLLLLALLLLAAALLDLLT 287
Ank_2 pfam12796
Ankyrin repeats (3 copies);
4-85 5.92e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 66.68  E-value: 5.92e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939808    4 IMYAARDGHTQVVALLVAHGAEVNAQDENGYTALTWAARQGHKNVILKLLELGANKMlqTKDGRTPSEIAKRNKHLEIFN 83
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLEIVK 78


                  ..
gi 568939808   84 FL 85
Cdd:pfam12796  79 LL 80
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1-62 2.27e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 62.06  E-value: 2.27e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568939808    1 MTPIMYAARDGHTQVVALLVAHgAEVNAQDeNGYTALTWAARQGHKNVILKLLELGANKMLQ 62
Cdd:pfam12796  31 RTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADINVK 90
Ank_4 pfam13637
Ankyrin repeats (many copies);
1-53 4.00e-12

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 60.37  E-value: 4.00e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568939808    1 MTPIMYAARDGHTQVVALLVAHGAEVNAQDENGYTALTWAARQGHKNVILKLL 53
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
2-85 1.22e-10

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 61.12  E-value: 1.22e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939808   2 TPIMYAARDGHTQVVALLVAHGAEVNAQDENGYTALTWAARQGHKNVILKLLELGANKMLQTKDGRTPSEIAKRNKHLEI 81
Cdd:COG0666   56 LLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEI 135


                 ....
gi 568939808  82 FNFL 85
Cdd:COG0666  136 VKLL 139
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 8-86 1.31e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.06  E-value: 1.31e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568939808   8 ARDGHTQVVALLVAHGAEVNAQDENGYTALTWAARQGHKNVILKLLELGANKMLQTKDGRTPSEIAKRNKHLEIFNFLS 86
Cdd:PTZ00322  90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 16-85 2.09e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 55.06  E-value: 2.09e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939808  16 VALLVAHGAEVNAQDENGYTALTWAARQGHKNVILKLLELGANKMLQTKDGRTPSEIAKRNKHLEIFNFL 85
Cdd:PHA03100 175 VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLL 244
Ank_5 pfam13857
Ankyrin repeats (many copies);
19-73 2.28e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.96  E-value: 2.28e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568939808   19 LVAHG-AEVNAQDENGYTALTWAARQGHKNVILKLLELGANKMLQTKDGRTPSEIA 73
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA03095 PHA03095
ankyrin-like protein; Provisional
 2-91 4.61e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 51.18  E-value: 4.61e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939808   2 TPIMYAARDGHTQ--VVALLVAHGAEVNAQDENGYTALTWAARQGHKNVILKLLELGANKMLQTKDGRTPSEIAKRNKHL 79
Cdd:PHA03095 224 TPLHSMATGSSCKrsLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNG 303

                         90
                 ....*....|...
gi 568939808  80 EIFN-FLSLTLNP 91
Cdd:PHA03095 304 RAVRaALAKNPSA 316
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 129-183 1.40e-06

SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of approximately 70 amino acids. This domain is found in the Fungi/Metazoa group and in a restricted number of bacteria. Proteins with SAM domains are represented by a wide variety of domain architectures and have different intracellular localization, including nucleus, cytoplasm and membranes. SAM domains have diverse functions. They can interact with proteins, RNAs and membrane lipids, contain site of phosphorylation and/or kinase docking site, and play a role in protein homo and hetero dimerization/oligomerization in processes ranging from signal transduction to regulation of transcription. Mutations in SAM domains have been linked to several diseases.


Pssm-ID: 188886 [Multi-domain]  Cd Length: 56  Bit Score: 44.92  E-value: 1.40e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568939808 129 DLEIFLHGLGLEHMTDSLKEKDITLRHLLTMKKDELTKNGIASK-DQQKILAALKE 183
Cdd:cd09487    1 DVAEWLESLGLEQYADLFRKNEIDGDALLLLTDEDLKELGITSPgHRKKILRAIQR 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
1-37 7.60e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.72  E-value: 7.60e-06
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 568939808    1 MTPIMYAARDGHTQVVALLVAHGAEVNAQDENGYTAL 37
Cdd:pfam13857  17 YTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 2-85 9.06e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 47.17  E-value: 9.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939808   2 TPIMYAARDGHTQVVALLVAHGAEVNAQDENGYTALtW--------------------------------AARQGHKNVI 49
Cdd:PLN03192 560 TPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTAL-WnaisakhhkifrilyhfasisdphaagdllctAAKRNDLTAM 638

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 568939808  50 LKLLELGANKMLQTKDGRTPSEIAKRNKHLEIFNFL 85
Cdd:PLN03192 639 KELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLL 674
PHA03095 PHA03095
ankyrin-like protein; Provisional
 2-85 4.47e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 45.02  E-value: 4.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939808   2 TPIMYAARDGHT-QVVALLVAHGAEVNAQDENGYTAL-TWAARQG-HKNVILKLLELGANKMLQTKDGRTPSEIAKRNKH 78
Cdd:PHA03095  85 TPLHLYLYNATTlDVIKLLIKAGADVNAKDKVGRTPLhVYLSGFNiNPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRN 164


                 ....*....
gi 568939808  79 --LEIFNFL 85
Cdd:PHA03095 165 anVELLRLL 173
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 1-31 7.03e-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: 39.58  E-value: 7.03e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 568939808    1 MTPIMYAA-RDGHTQVVALLVAHGAEVNAQDE 31
Cdd:pfam00023   3 NTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 133-184 1.19e-04

SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.


Pssm-ID: 425739  Cd Length: 64  Bit Score: 39.56  E-value: 1.19e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568939808  133 FLHGLGLEHMTDSLKEKDITLRHLLTMKKDELTKNGIASK-DQQKILAALKEL 184
Cdd:pfam00536  11 WLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLKLGVTLLgHRKKILYAIQRL 63
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1-30 3.08e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 39.33  E-value: 3.08e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 568939808    1 MTPIMYAARDGHTQVVALLVAHGAEVNAQD 30
Cdd:pfam12796  62 RTALHYAARSGHLEIVKLLLEKGADINVKD 91
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 2-70 3.83e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 42.19  E-value: 3.83e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568939808   2 TPIMYAARDGHTQVVALLVAHGAEVNAQDENGYTALTWAARQGHKNVILKLL-------ELGANKMLQTKDGRTPS 70
Cdd:PTZ00322 117 TPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSrhsqchfELGANAKPDSFTGKPPS 192
Ank_4 pfam13637
Ankyrin repeats (many copies);
33-85 6.30e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 37.25  E-value: 6.30e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568939808   33 GYTALTWAARQGHKNVILKLLELGANKMLQTKDGRTPSEIAKRNKHLEIFNFL 85
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 3-85 7.00e-04

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 41.15  E-value: 7.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939808   3 PIMYAARDGHTQVVALLVAHGAEVNAQDENGYTALTWAARQGHK-------NVIL---KLLELGANKMLQTKDGRTPSEI 72
Cdd:cd22192  139 PLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKtfacqmyDLILsydKEDDLQPLDLVPNNQGLTPFKL 218

                         90
                 ....*....|...
gi 568939808  73 AKRNKHLEIFNFL 85
Cdd:cd22192  219 AAKEGNIVMFQHL 231
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 3-69 8.39e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 40.72  E-value: 8.39e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568939808   3 PIMYAARDGHTQVVALLVAHGAEVNAQDENGYTALTWAARQGHKNVILKLLELGANKMLQTKDGRTP 69
Cdd:PHA02874 160 PIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTP 226
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 2-58 8.76e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 40.80  E-value: 8.76e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568939808   2 TPIMYAARDGHTQVVALLVAHGAEVNAQDENGYTALTWAARQGHKNVILKLLELGAN 58
Cdd:PHA03100 194 TPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 2-85 1.07e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 40.82  E-value: 1.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939808   2 TPIMYAARDGH-TQVVALLVAHGAEVNAQDENGYTALTWAAR-QGHKNVILKLLELGANKMLQTKDGRTPSEIAKRNKHL 79
Cdd:PHA02876 309 TPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNV 388


                 ....*.
gi 568939808  80 EIFNFL 85
Cdd:PHA02876 389 VIINTL 394
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 2-69 1.76e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 39.95  E-value: 1.76e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568939808   2 TPIMYAARDGHTQVVALLVAHGAEVNAQDENGYTALTWAARQGHKNVILKLLELGANKMLQTKDGRTP 69
Cdd:PHA02874 126 TFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESP 193
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 2-73 2.01e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 39.86  E-value: 2.01e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568939808   2 TPIMYAARDGHTQVVALLVAHGAEVNAQDENGYTALTWAARQGHKNVILKLLELGANKMLQTKDGRTPSEIA 73
Cdd:PHA02878 170 TALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHIS 241
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 32-58 2.89e-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: 34.87  E-value: 2.89e-03
                           10        20
                   ....*....|....*....|....*..
gi 568939808    32 NGYTALTWAARQGHKNVILKLLELGAN 58
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 1-28 3.10e-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: 34.49  E-value: 3.10e-03
                           10        20
                   ....*....|....*....|....*...
gi 568939808     1 MTPIMYAARDGHTQVVALLVAHGAEVNA 28
Cdd:smart00248   3 RTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 1-28 4.87e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 34.16  E-value: 4.87e-03
                          10        20
                  ....*....|....*....|....*...
gi 568939808    1 MTPIMYAARDGHTQVVALLVAHGAEVNA 28
Cdd:pfam13606   3 NTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 1-58 5.79e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 38.51  E-value: 5.79e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568939808   1 MTPIMYAARDGHTQVVALLVAHGAEVNAQDENGYTALTWAARQGHKNVILKLLELGAN 58
Cdd:PHA02876 179 ITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSN 236
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 4-85 8.65e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 37.93  E-value: 8.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568939808   4 IMYAARDGHTQVVALLVAHGAEVNAQDENGYTALTWAARQGHKNVILKLLELGANKMLQTKDGRTPSEIAKRNKHLEIFN 83
Cdd:PLN03192 529 LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFR 608


                 ..
gi 568939808  84 FL 85
Cdd:PLN03192 609 IL 610
 
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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