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Conserved domains on  [gi|1907086802|ref|XP_036013200|]
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ankyrin repeat and MYND domain-containing protein 2 isoform X1 [Mus musculus]

Protein Classification

zf-MYND domain-containing protein( domain architecture ID 12790888)

zf-MYND 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];
36-123 1.26e-20

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 91.55  E-value: 1.26e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907086802  36 NGMTPLMHAAYKGKLEMCKLLLRHGADAScHQHEHGYTALMFAALSGNKDITWVMLEAGAETDVVNSVGRTAAQMAAFVG 115
Cdd:COG0666   152 DGNTPLHLAAANGNLEIVKLLLEAGADVN-ARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENG 230


                  ....*...
gi 1907086802 116 QHDCVAII 123
Cdd:COG0666   231 NLEIVKLL 238
zf-MYND pfam01753
MYND finger;
311-348 1.73e-10

MYND finger;


:

Pssm-ID: 460312  Cd Length: 39  Bit Score: 55.89  E-value: 1.73e-10
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1907086802 311 CTTCGEKGAS-KRCSVCKMVIYCDQTCQKTHWFAHKKMC 348
Cdd:pfam01753   1 CAVCGKEALKlLRCSRCKSVYYCSKECQKADWPYHKKEC 39
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
36-123 1.26e-20

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 91.55  E-value: 1.26e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907086802  36 NGMTPLMHAAYKGKLEMCKLLLRHGADAScHQHEHGYTALMFAALSGNKDITWVMLEAGAETDVVNSVGRTAAQMAAFVG 115
Cdd:COG0666   152 DGNTPLHLAAANGNLEIVKLLLEAGADVN-ARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENG 230


                  ....*...
gi 1907086802 116 QHDCVAII 123
Cdd:COG0666   231 NLEIVKLL 238
Ank_2 pfam12796
Ankyrin repeats (3 copies);
41-123 9.99e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 66.68  E-value: 9.99e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907086802  41 LMHAAYKGKLEMCKLLLRHGADASCHQHEhGYTALMFAALSGNKDITWVMLEaGAETDVVNSvGRTAAQMAAFVGQHDCV 120
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKN-GRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIV 77


                  ...
gi 1907086802 121 AII 123
Cdd:pfam12796  78 KLL 80
zf-MYND pfam01753
MYND finger;
311-348 1.73e-10

MYND finger;


Pssm-ID: 460312  Cd Length: 39  Bit Score: 55.89  E-value: 1.73e-10
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1907086802 311 CTTCGEKGAS-KRCSVCKMVIYCDQTCQKTHWFAHKKMC 348
Cdd:pfam01753   1 CAVCGKEALKlLRCSRCKSVYYCSKECQKADWPYHKKEC 39
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 36-62 4.84e-06

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: 42.96  E-value: 4.84e-06
                           10        20
                   ....*....|....*....|....*..
gi 1907086802   36 NGMTPLMHAAYKGKLEMCKLLLRHGAD 62
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 32-125 6.30e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 44.98  E-value: 6.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907086802  32 MVYENGMTPLMHAAYKGKLEMCKLLLRHGADA------------------------------SCHQHE--HGYTALMFAA 79
Cdd:PHA02875   97 VFYKDGMTPLHLATILKKLDIMKLLIARGADPdipntdkfsplhlavmmgdikgiellidhkACLDIEdcCGCTPLIIAM 176

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1907086802  80 LSGNKDITWVMLEAGAETDVVNSVGRTAAQmaafvgqhdCVAIINN 125
Cdd:PHA02875  177 AKGDIAICKMLLDSGANIDYFGKNGCVAAL---------CYAIENN 213
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 29-106 8.14e-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: 45.00  E-value: 8.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907086802  29 TSLMvYEnGMTPLMHAAYKGKLEMCKLLLRHGADAS----------------CHQHEHgytALMFAALSGNKDITWVMLE 92
Cdd:cd22192    83 TSDL-YQ-GETALHIAVVNQNLNLVRELIARGADVVspratgtffrpgpknlIYYGEH---PLSFAACVGNEEIVRLLIE 157

                          90
                  ....*....|....
gi 1907086802  93 AGAETDVVNSVGRT 106
Cdd:cd22192   158 HGADIRAQDSLGNT 171
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
36-123 1.26e-20

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 91.55  E-value: 1.26e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907086802  36 NGMTPLMHAAYKGKLEMCKLLLRHGADAScHQHEHGYTALMFAALSGNKDITWVMLEAGAETDVVNSVGRTAAQMAAFVG 115
Cdd:COG0666   152 DGNTPLHLAAANGNLEIVKLLLEAGADVN-ARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENG 230


                  ....*...
gi 1907086802 116 QHDCVAII 123
Cdd:COG0666   231 NLEIVKLL 238
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
35-122 4.21e-20

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 90.01  E-value: 4.21e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907086802  35 ENGMTPLMHAAYKGKLEMCKLLLRHGADAScHQHEHGYTALMFAALSGNKDITWVMLEAGAETDVVNSVGRTAAQMAAFV 114
Cdd:COG0666   118 KDGETPLHLAAYNGNLEIVKLLLEAGADVN-AQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAEN 196


                  ....*...
gi 1907086802 115 GQHDCVAI 122
Cdd:COG0666   197 GHLEIVKL 204
Ank_2 pfam12796
Ankyrin repeats (3 copies);
41-123 9.99e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 66.68  E-value: 9.99e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907086802  41 LMHAAYKGKLEMCKLLLRHGADASCHQHEhGYTALMFAALSGNKDITWVMLEaGAETDVVNSvGRTAAQMAAFVGQHDCV 120
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKN-GRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIV 77


                  ...
gi 1907086802 121 AII 123
Cdd:pfam12796  78 KLL 80
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
36-123 1.97e-13

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 70.37  E-value: 1.97e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907086802  36 NGMTPLMHAAYKGKLEMCKLLLRHGADAScHQHEHGYTALMFAALSGNKDITWVMLEAGAETDVVNSVGRTAAQMAAFVG 115
Cdd:COG0666   185 DGETPLHLAAENGHLEIVKLLLEAGADVN-AKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAG 263


                  ....*...
gi 1907086802 116 QHDCVAII 123
Cdd:COG0666   264 AALIVKLL 271
Ank_2 pfam12796
Ankyrin repeats (3 copies);
35-101 1.06e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 63.60  E-value: 1.06e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907086802  35 ENGMTPLMHAAYKGKLEMCKLLLRHG-ADASChqheHGYTALMFAALSGNKDITWVMLEAGAETDVVN 101
Cdd:pfam12796  28 KNGRTALHLAAKNGHLEIVKLLLEHAdVNLKD----NGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
zf-MYND pfam01753
MYND finger;
311-348 1.73e-10

MYND finger;


Pssm-ID: 460312  Cd Length: 39  Bit Score: 55.89  E-value: 1.73e-10
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1907086802 311 CTTCGEKGAS-KRCSVCKMVIYCDQTCQKTHWFAHKKMC 348
Cdd:pfam01753   1 CAVCGKEALKlLRCSRCKSVYYCSKECQKADWPYHKKEC 39
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
4-122 3.94e-08

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 54.57  E-value: 3.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907086802   4 STAWMRRQVCWGDEDFRLLGSDLRSTSLMVYENGMTPLMHAAYKGKLEMCKLLLRHGADASCHQHEHGYTALMFAALSGN 83
Cdd:COG0666    20 LLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGD 99

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1907086802  84 KDITWVMLEAGAETDVVNSVGRTAAQMAAFVGQHDCVAI 122
Cdd:COG0666   100 LEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKL 138
Ank_4 pfam13637
Ankyrin repeats (many copies);
37-86 9.81e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.42  E-value: 9.81e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907086802  37 GMTPLMHAAYKGKLEMCKLLLRHGADASChQHEHGYTALMFAALSGNKDI 86
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINA-VDGNGETALHFAASNGNVEV 49
Ank_2 pfam12796
Ankyrin repeats (3 copies);
75-136 2.40e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 48.57  E-value: 2.40e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907086802  75 LMFAALSGNKDITWVMLEAGAETDVVNSVGRTAAQMAAFVGQHDCV-AIINNFFPRERLDYYT 136
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVkLLLEHADVNLKDNGRT 63
Ank_5 pfam13857
Ankyrin repeats (many copies);
35-78 3.69e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.87  E-value: 3.69e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1907086802  35 ENGMTPLMHAAYKGKLEMCKLLLRHGADASCHQhEHGYTALMFA 78
Cdd:pfam13857  14 GEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKD-EEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 36-62 4.84e-06

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: 42.96  E-value: 4.84e-06
                           10        20
                   ....*....|....*....|....*..
gi 1907086802   36 NGMTPLMHAAYKGKLEMCKLLLRHGAD 62
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 36-62 1.14e-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: 41.89  E-value: 1.14e-05
                          10        20
                  ....*....|....*....|....*...
gi 1907086802  36 NGMTPLMHAAYK-GKLEMCKLLLRHGAD 62
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGAD 28
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 36-65 2.33e-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.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 41.09  E-value: 2.33e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 1907086802  36 NGMTPLMHAAYKGKLEMCKLLLRHGADASC 65
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 32-125 6.30e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 44.98  E-value: 6.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907086802  32 MVYENGMTPLMHAAYKGKLEMCKLLLRHGADA------------------------------SCHQHE--HGYTALMFAA 79
Cdd:PHA02875   97 VFYKDGMTPLHLATILKKLDIMKLLIARGADPdipntdkfsplhlavmmgdikgiellidhkACLDIEdcCGCTPLIIAM 176

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1907086802  80 LSGNKDITWVMLEAGAETDVVNSVGRTAAQmaafvgqhdCVAIINN 125
Cdd:PHA02875  177 AKGDIAICKMLLDSGANIDYFGKNGCVAAL---------CYAIENN 213
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 29-106 8.14e-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: 45.00  E-value: 8.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907086802  29 TSLMvYEnGMTPLMHAAYKGKLEMCKLLLRHGADAS----------------CHQHEHgytALMFAALSGNKDITWVMLE 92
Cdd:cd22192    83 TSDL-YQ-GETALHIAVVNQNLNLVRELIARGADVVspratgtffrpgpknlIYYGEH---PLSFAACVGNEEIVRLLIE 157

                          90
                  ....*....|....
gi 1907086802  93 AGAETDVVNSVGRT 106
Cdd:cd22192   158 HGADIRAQDSLGNT 171
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
35-108 2.14e-04

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 43.02  E-value: 2.14e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907086802  35 ENGMTPLMHAAYKGKLEMCKLLLRHGADAScHQHEHGYTALMFAALSGNKDITWVMLEAGAETDVVNSVGRTAA 108
Cdd:COG0666   217 NDGKTALDLAAENGNLEIVKLLLEAGADLN-AKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 37-103 2.54e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 43.06  E-value: 2.54e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907086802  37 GMTPLMHAAYKGKLEMCKLLLRHGADAScHQHEHGYTALMFAALSGNK-DITWVMLEAGAETDVVNSV 103
Cdd:PHA02875  168 GCTPLIIAMAKGDIAICKMLLDSGANID-YFGKNGCVAALCYAIENNKiDIVRLFIKRGADCNIMFMI 234
Ank_5 pfam13857
Ankyrin repeats (many copies);
56-111 2.71e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.87  E-value: 2.71e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907086802  56 LLRHGADASCHQHEHGYTALMFAALSGNKDITWVMLEAGAETDVVNSVGRTAAQMA 111
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 35-102 2.73e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 43.12  E-value: 2.73e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907086802  35 ENGMTPLMHAAYKGKLEMCKLLLRHGADASChQHEHGYTALMFAALSGNKDITWVMLEAGAETDVVNS 102
Cdd:PHA03100  190 VYGFTPLHYAVYNNNPEFVKYLLDLGANPNL-VNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256
Ank_4 pfam13637
Ankyrin repeats (many copies);
71-120 8.32e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 37.25  E-value: 8.32e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907086802  71 GYTALMFAALSGNKDITWVMLEAGAETDVVNSVGRTAAQMAAFVGQHDCV 120
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVL 50
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 39-123 1.90e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 40.33  E-value: 1.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907086802  39 TPLMHAAYKGKLEMCKLLLRHGADASChQHEHGYTALMFAALSGNKDITWVMLEAGAETDVVNSVGRTAAQMAAFVGQHD 118
Cdd:PHA02874  126 TFLHYAIKKGDLESIKMLFEYGADVNI-EDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYA 204


                  ....*
gi 1907086802 119 CVAII 123
Cdd:PHA02874  205 CIKLL 209
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 41-147 2.19e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 40.27  E-value: 2.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907086802  41 LMHAAYKGKLEMCKLLLRHGADASCHQHeHGYTALMFAALSGNKDITWVMLEAGAETDVVNSVGRTAAQMAAFVGQHDCV 120
Cdd:PTZ00322   86 LCQLAASGDAVGARILLTGGADPNCRDY-DGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVV 164

                          90       100
                  ....*....|....*....|....*...
gi 1907086802 121 AIINNFFPRE-RLDYYTKPQGLDKEPKL 147
Cdd:PTZ00322  165 QLLSRHSQCHfELGANAKPDSFTGKPPS 192
PHA03095 PHA03095
ankyrin-like protein; Provisional
 36-124 3.05e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 39.62  E-value: 3.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907086802  36 NGMTPL-MHAAYKGKLEMCKLLLRHGADAScHQHEHGYTALMfAALSG---NKDITWVMLEAGAETDVVNSVGRTAaqMA 111
Cdd:PHA03095   82 CGFTPLhLYLYNATTLDVIKLLIKAGADVN-AKDKVGRTPLH-VYLSGfniNPKVIRLLLRKGADVNALDLYGMTP--LA 157

                          90
                  ....*....|....
gi 1907086802 112 AFVGQHDC-VAIIN 124
Cdd:PHA03095  158 VLLKSRNAnVELLR 171
 
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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