NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|469741876|gb|EMQ54541|]
View 

ank repeat family protein [Vibrio cholerae O1 str. NHCC-004A]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-103 9.18e-16

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 71.14  E-value: 9.18e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469741876   1 MNEFLSAGFPINQRNAESYTALMVAAYQGNAQTVELLLRFGANACLQDKRGNTALMGALLKREIQIARALYQAECADNLR 80
Cdd:COG0666  103 VKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNAR 182

                         90       100
                 ....*....|....*....|...
gi 469741876  81 NKAGLSVQEFAELYGQSETLKAL 103
Cdd:COG0666  183 DNDGETPLHLAAENGHLEIVKLL 205
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-103 9.18e-16

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 71.14  E-value: 9.18e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469741876   1 MNEFLSAGFPINQRNAESYTALMVAAYQGNAQTVELLLRFGANACLQDKRGNTALMGALLKREIQIARALYQAECADNLR 80
Cdd:COG0666  103 VKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNAR 182

                         90       100
                 ....*....|....*....|...
gi 469741876  81 NKAGLSVQEFAELYGQSETLKAL 103
Cdd:COG0666  183 DNDGETPLHLAAENGHLEIVKLL 205
Ank_2 pfam12796
Ankyrin repeats (3 copies);
22-103 7.46e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 48.96  E-value: 7.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469741876   22 LMVAAYQGNAQTVELLLRFGANACLQDKRGNTALMGALLKREIQIARALYQAECADNLRNkaGLSVQEFAELYGQSETLK 101
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN--GRTALHYAARSGHLEIVK 78


                  ..
gi 469741876  102 AL 103
Cdd:pfam12796  79 LL 80
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 1-112 1.17e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 48.71  E-value: 1.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469741876   1 MNEFLSAGFPINQRNAESYTALMVAAYQGNAQTVELLLRFGANACLQDKRGNTALMGALLKREIQIARALYQAECADNlr 80
Cdd:PLN03192 541 LEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISD-- 618

                         90       100       110
                 ....*....|....*....|....*....|..
gi 469741876  81 NKAGLSVQEFAELYGQSETLKALHQEKLAVSS 112
Cdd:PLN03192 619 PHAAGDLLCTAAKRNDLTAMKELLKQGLNVDS 650
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 22-86 1.75e-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: 36.53  E-value: 1.75e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 469741876  22 LMVAAYQGNAQTVELLLRFGANACLQDKRGNTALMGALLKREIQIARALY----------QAECADNLRNKAGLS 86
Cdd:cd22192  140 LSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTFACQMYdlilsydkedDLQPLDLVPNNQGLT 214
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 19-43 1.93e-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: 33.72  E-value: 1.93e-03
                           10        20
                   ....*....|....*....|....*
gi 469741876    19 YTALMVAAYQGNAQTVELLLRFGAN 43
Cdd:smart00248   3 RTPLHLAAENGNLEVVKLLLDKGAD 27
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-103 9.18e-16

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 71.14  E-value: 9.18e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469741876   1 MNEFLSAGFPINQRNAESYTALMVAAYQGNAQTVELLLRFGANACLQDKRGNTALMGALLKREIQIARALYQAECADNLR 80
Cdd:COG0666  103 VKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNAR 182

                         90       100
                 ....*....|....*....|...
gi 469741876  81 NKAGLSVQEFAELYGQSETLKAL 103
Cdd:COG0666  183 DNDGETPLHLAAENGHLEIVKLL 205
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
5-110 1.96e-13

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 64.59  E-value: 1.96e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469741876   5 LSAGFPINQRNAESYTALMVAAYQGNAQTVELLLRFGANACLQDKRGNTALMGALLKREIQIARALYQAECADNLRNKAG 84
Cdd:COG0666  173 LEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDG 252

                         90       100
                 ....*....|....*....|....*.
gi 469741876  85 LSVQEFAELYGQSETLKALHQEKLAV 110
Cdd:COG0666  253 LTALLLAAAAGAALIVKLLLLALLLL 278
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-103 2.74e-10

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 55.73  E-value: 2.74e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469741876   1 MNEFLSAGFPINQRNAESYTALMVAAYQGNAQTVELLLRFGANACLQDKRGNTALMGALLKREIQIARALYQAECADNLR 80
Cdd:COG0666   70 ALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQ 149

                         90       100
                 ....*....|....*....|...
gi 469741876  81 NKAGLSVQEFAELYGQSETLKAL 103
Cdd:COG0666  150 DNDGNTPLHLAAANGNLEIVKLL 172
Ank_2 pfam12796
Ankyrin repeats (3 copies);
22-103 7.46e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 48.96  E-value: 7.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469741876   22 LMVAAYQGNAQTVELLLRFGANACLQDKRGNTALMGALLKREIQIARALYQAECADNLRNkaGLSVQEFAELYGQSETLK 101
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN--GRTALHYAARSGHLEIVK 78


                  ..
gi 469741876  102 AL 103
Cdd:pfam12796  79 LL 80
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1-81 3.79e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 47.42  E-value: 3.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469741876    1 MNEFLSAGFPINQRNAESYTALMVAAYQGNAQTVELLLRFgANACLQDKrGNTALMGALLKREIQIARALYQAECADNLR 80
Cdd:pfam12796  13 VKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINVK 90


                  .
gi 469741876   81 N 81
Cdd:pfam12796  91 D 91
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 1-112 1.17e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 48.71  E-value: 1.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469741876   1 MNEFLSAGFPINQRNAESYTALMVAAYQGNAQTVELLLRFGANACLQDKRGNTALMGALLKREIQIARALYQAECADNlr 80
Cdd:PLN03192 541 LEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISD-- 618

                         90       100       110
                 ....*....|....*....|....*....|..
gi 469741876  81 NKAGLSVQEFAELYGQSETLKALHQEKLAVSS 112
Cdd:PLN03192 619 PHAAGDLLCTAAKRNDLTAMKELLKQGLNVDS 650
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 1-103 4.77e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 46.88  E-value: 4.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469741876   1 MNEFLSAGFPINQRNAESYTALMVAAYQGNAQTVELLLRFGANACLQDKRGNTALMGALLKREIQIARALYQAECADNLR 80
Cdd:PHA02874 107 IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVK 186

                         90       100
                 ....*....|....*....|...
gi 469741876  81 NKAGLSVQEFAELYGQSETLKAL 103
Cdd:PHA02874 187 DNNGESPLHNAAEYGDYACIKLL 209
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 2-70 1.10e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 45.81  E-value: 1.10e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 469741876   2 NEFLSAGFPINQRNAESYTALMVAAYQGNAQTVELLLRFGANACLQDKRGNTALMGALLKREIQIARAL 70
Cdd:PHA03100 176 NYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLL 244
Ank_5 pfam13857
Ankyrin repeats (many copies);
11-55 3.57e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.18  E-value: 3.57e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 469741876   11 INQRNAESYTALMVAAYQGNAQTVELLLRFGANACLQDKRGNTAL 55
Cdd:pfam13857   9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
PHA03095 PHA03095
ankyrin-like protein; Provisional
 4-69 6.54e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 43.47  E-value: 6.54e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 469741876   4 FLSAGFPINQRNAESYTALMVAAYQGNAQTVELLLRFGANACLQDKRGNTALMGALLKREIQIARA 69
Cdd:PHA03095 243 LLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRA 308
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 5-55 4.10e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.42  E-value: 4.10e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 469741876   5 LSAGFPINQRNAESYTALMVAAYQGNAQTVELLLRFGANACLQDKRGNTAL 55
Cdd:PTZ00322 102 LTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPL 152
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
5-85 9.11e-05

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 40.32  E-value: 9.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469741876   5 LSAGFPINQRNAESYTALMVAAYQGNAQTVELLLRFGANACLQDKRGNTALMGALLKREIQIARALYQAECADNLRNKAG 84
Cdd:COG0666  206 LEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDL 285


                 .
gi 469741876  85 L 85
Cdd:COG0666  286 L 286
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
5-103 9.29e-05

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 40.32  E-value: 9.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469741876   5 LSAGFPINQRNAESYTALMVAAYQGNAQTVELLLRFGANACLQDKRGNTALMGALLKREIQIARALYQAECADNLRNKAG 84
Cdd:COG0666   41 LLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDG 120

                         90
                 ....*....|....*....
gi 469741876  85 LSVQEFAELYGQSETLKAL 103
Cdd:COG0666  121 ETPLHLAAYNGNLEIVKLL 139
Ank_4 pfam13637
Ankyrin repeats (many copies);
19-70 3.50e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.10  E-value: 3.50e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 469741876   19 YTALMVAAYQGNAQTVELLLRFGANACLQDKRGNTALMGALLKREIQIARAL 70
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 19-49 5.02e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 35.34  E-value: 5.02e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 469741876   19 YTALMVAAYQ-GNAQTVELLLRFGANACLQDK 49
Cdd:pfam00023   3 NTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 22-86 1.75e-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: 36.53  E-value: 1.75e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 469741876  22 LMVAAYQGNAQTVELLLRFGANACLQDKRGNTALMGALLKREIQIARALY----------QAECADNLRNKAGLS 86
Cdd:cd22192  140 LSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTFACQMYdlilsydkedDLQPLDLVPNNQGLT 214
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 19-43 1.93e-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: 33.72  E-value: 1.93e-03
                           10        20
                   ....*....|....*....|....*
gi 469741876    19 YTALMVAAYQGNAQTVELLLRFGAN 43
Cdd:smart00248   3 RTPLHLAAENGNLEVVKLLLDKGAD 27
Ank_4 pfam13637
Ankyrin repeats (many copies);
4-38 7.39e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 32.63  E-value: 7.39e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 469741876    4 FLSAGFPINQRNAESYTALMVAAYQGNAQTVELLL 38
Cdd:pfam13637  20 LLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
36-91 9.13e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 32.32  E-value: 9.13e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 469741876   36 LLLRFGANACLQDKRGNTALMGALLKREIQIARALYQAECADNLRNKAGLSVQEFA 91
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH