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Conserved domains on  [gi|1063743498|ref|NP_001329967|]
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ankyrin repeat family protein [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
7-92 1.25e-18

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 84.24  E-value: 1.25e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063743498   7 LCLAAKSGDLKKVQTLIYSGADVTHFDNDGLTPLMHAAKIGNAEIVTALLESGAPWNALSPSNLSAGDFAMEAGHQETFD 86
Cdd:COG0666   124 LHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVK 203


                  ....*.
gi 1063743498  87 LLLKTG 92
Cdd:COG0666   204 LLLEAG 209
TrmR super family cl28097
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
 182-256 3.30e-07

tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; tRNA 5-hydroxyU34 O-methylase TrmR/YrrM is part of the Pathway/BioSystem: tRNA modification


The actual alignment was detected with superfamily member COG4122:

Pssm-ID: 443298  Cd Length: 173  Bit Score: 49.41  E-value: 3.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063743498 182 TIIEAHPEVY---KRMIESGwGEKENVKIVFGRWQDVLDKLDDNSFDGIFFDT----YGEYYEDLRefhqhlpRLLKPDG 254
Cdd:COG4122    45 TTIEIDPERAaiaRENFARA-GLADRIRLILGDALEVLPRLADGPFDLVFIDAdksnYPDYLELAL-------PLLRPGG 116


                  ..
gi 1063743498 255 VY 256
Cdd:COG4122   117 LI 118
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
7-92 1.25e-18

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 84.24  E-value: 1.25e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063743498   7 LCLAAKSGDLKKVQTLIYSGADVTHFDNDGLTPLMHAAKIGNAEIVTALLESGAPWNALSPSNLSAGDFAMEAGHQETFD 86
Cdd:COG0666   124 LHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVK 203


                  ....*.
gi 1063743498  87 LLLKTG 92
Cdd:COG0666   204 LLLEAG 209
Ank_2 pfam12796
Ankyrin repeats (3 copies);
7-93 5.75e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 69.37  E-value: 5.75e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063743498   7 LCLAAKSGDLKKVQTLIYSGADVTHFDNDGLTPLMHAAKIGNAEIVTALLESGAP------WNALspsnlsagDFAMEAG 80
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVnlkdngRTAL--------HYAARSG 72

                          90
                  ....*....|...
gi 1063743498  81 HQETFDLLLKTGI 93
Cdd:pfam12796  73 HLEIVKLLLEKGA 85
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 6-90 2.48e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.21  E-value: 2.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063743498   6 QLCLAAKSGDLKKVQTLIYSGADVTHFDNDGLTPLMHAAKIGNAEIVTALLESGAPWNALSPSNLSAGDFAMEAGHQETF 85
Cdd:PTZ00322   85 ELCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVV 164


                  ....*
gi 1063743498  86 DLLLK 90
Cdd:PTZ00322  165 QLLSR 169
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
 182-256 3.30e-07

tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; tRNA 5-hydroxyU34 O-methylase TrmR/YrrM is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443298  Cd Length: 173  Bit Score: 49.41  E-value: 3.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063743498 182 TIIEAHPEVY---KRMIESGwGEKENVKIVFGRWQDVLDKLDDNSFDGIFFDT----YGEYYEDLRefhqhlpRLLKPDG 254
Cdd:COG4122    45 TTIEIDPERAaiaRENFARA-GLADRIRLILGDALEVLPRLADGPFDLVFIDAdksnYPDYLELAL-------PLLRPGG 116


                  ..
gi 1063743498 255 VY 256
Cdd:COG4122   117 LI 118
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 159-256 6.88e-07

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 47.04  E-value: 6.88e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063743498 159 ILNVGFGMGLVDTAIQRYNPVKHTIIEAHPEVYKRMIESGWGEK-ENVKIVFGRWQDvLDKLDDNSFDGIFFD-TYGEYY 236
Cdd:cd02440     2 VLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLaDNVEVLKGDAEE-LPPEADESFDVIISDpPLHHLV 80

                          90       100
                  ....*....|....*....|
gi 1063743498 237 EDLREFHQHLPRLLKPDGVY 256
Cdd:cd02440    81 EDLARFLEEARRLLKPGGVL 100
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 35-60 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: 35.26  E-value: 1.93e-03
                           10        20
                   ....*....|....*....|....*.
gi 1063743498   35 DGLTPLMHAAKIGNAEIVTALLESGA 60
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGA 26
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
7-92 1.25e-18

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 84.24  E-value: 1.25e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063743498   7 LCLAAKSGDLKKVQTLIYSGADVTHFDNDGLTPLMHAAKIGNAEIVTALLESGAPWNALSPSNLSAGDFAMEAGHQETFD 86
Cdd:COG0666   124 LHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVK 203


                  ....*.
gi 1063743498  87 LLLKTG 92
Cdd:COG0666   204 LLLEAG 209
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
7-92 3.69e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 80.38  E-value: 3.69e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063743498   7 LCLAAKSGDLKKVQTLIYSGADVTHFDNDGLTPLMHAAKIGNAEIVTALLESGAPWNALSPSNLSAGDFAMEAGHQETFD 86
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170


                  ....*.
gi 1063743498  87 LLLKTG 92
Cdd:COG0666   171 LLLEAG 176
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
7-93 7.17e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 79.61  E-value: 7.17e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063743498   7 LCLAAKSGDLKKVQTLIYSGADVTHFDNDGLTPLMHAAKIGNAEIVTALLESGAPWNALSPSNLSAGDFAMEAGHQETFD 86
Cdd:COG0666   157 LHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVK 236


                  ....*..
gi 1063743498  87 LLLKTGI 93
Cdd:COG0666   237 LLLEAGA 243
Ank_2 pfam12796
Ankyrin repeats (3 copies);
7-93 5.75e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 69.37  E-value: 5.75e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063743498   7 LCLAAKSGDLKKVQTLIYSGADVTHFDNDGLTPLMHAAKIGNAEIVTALLESGAP------WNALspsnlsagDFAMEAG 80
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVnlkdngRTAL--------HYAARSG 72

                          90
                  ....*....|...
gi 1063743498  81 HQETFDLLLKTGI 93
Cdd:pfam12796  73 HLEIVKLLLEKGA 85
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
7-99 8.16e-13

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 67.67  E-value: 8.16e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063743498   7 LCLAAKSGDLKKVQTLIYSGADVTHFDNDGLTPLMHAAKIGNAEIVTALLESGAPWNALSPSNLSAGDFAMEAGHQETFD 86
Cdd:COG0666   190 LHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVK 269

                          90
                  ....*....|...
gi 1063743498  87 LLLKTGIQSELIL 99
Cdd:COG0666   270 LLLLALLLLAAAL 282
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
9-93 4.34e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 62.66  E-value: 4.34e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063743498   9 LAAKSGDLKKVQTLIYSGADVTHFDNDGLTPLMHAAKIGNAEIVTALLESGAPWNALSPSNLSAGDFAMEAGHQETFDLL 88
Cdd:COG0666    60 AAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLL 139


                  ....*
gi 1063743498  89 LKTGI 93
Cdd:COG0666   140 LEAGA 144
Ank_4 pfam13637
Ankyrin repeats (many copies);
7-56 9.72e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.74  E-value: 9.72e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1063743498   7 LCLAAKSGDLKKVQTLIYSGADVTHFDNDGLTPLMHAAKIGNAEIVTALL 56
Cdd:pfam13637   5 LHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 6-90 2.48e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.21  E-value: 2.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063743498   6 QLCLAAKSGDLKKVQTLIYSGADVTHFDNDGLTPLMHAAKIGNAEIVTALLESGAPWNALSPSNLSAGDFAMEAGHQETF 85
Cdd:PTZ00322   85 ELCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVV 164


                  ....*
gi 1063743498  86 DLLLK 90
Cdd:PTZ00322  165 QLLSR 169
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
 182-256 3.30e-07

tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; tRNA 5-hydroxyU34 O-methylase TrmR/YrrM is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443298  Cd Length: 173  Bit Score: 49.41  E-value: 3.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063743498 182 TIIEAHPEVY---KRMIESGwGEKENVKIVFGRWQDVLDKLDDNSFDGIFFDT----YGEYYEDLRefhqhlpRLLKPDG 254
Cdd:COG4122    45 TTIEIDPERAaiaRENFARA-GLADRIRLILGDALEVLPRLADGPFDLVFIDAdksnYPDYLELAL-------PLLRPGG 116


                  ..
gi 1063743498 255 VY 256
Cdd:COG4122   117 LI 118
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 159-256 6.88e-07

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 47.04  E-value: 6.88e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063743498 159 ILNVGFGMGLVDTAIQRYNPVKHTIIEAHPEVYKRMIESGWGEK-ENVKIVFGRWQDvLDKLDDNSFDGIFFD-TYGEYY 236
Cdd:cd02440     2 VLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLaDNVEVLKGDAEE-LPPEADESFDVIISDpPLHHLV 80

                          90       100
                  ....*....|....*....|
gi 1063743498 237 EDLREFHQHLPRLLKPDGVY 256
Cdd:cd02440    81 EDLARFLEEARRLLKPGGVL 100
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 139-255 7.44e-06

2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism]; 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 441829 [Multi-domain]  Cd Length: 126  Bit Score: 44.62  E-value: 7.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063743498 139 AWEKPLMEAHAKAIcLNGGHILNVGFGMGLVDTAIQRYNpVKHTIIEAHPEVYKRMIEsgWGEKENVKIVFGRWQDVldK 218
Cdd:COG2227     9 FWDRRLAALLARLL-PAGGRVLDVGCGTGRLALALARRG-ADVTGVDISPEALEIARE--RAAELNVDFVQGDLEDL--P 82

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1063743498 219 LDDNSFDGIFFDTYGEYYEDLREFHQHLPRLLKPDGV 255
Cdd:COG2227    83 LEDGSFDLVICSEVLEHLPDPAALLRELARLLKPGGL 119
Ank_5 pfam13857
Ankyrin repeats (many copies);
27-76 7.45e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.72  E-value: 7.45e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1063743498  27 ADVTHFDNDGLTPLMHAAKIGNAEIVTALLESGAPWNALSPSNLSAGDFA 76
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 10-59 2.36e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 45.72  E-value: 2.36e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1063743498  10 AAKSGDLKKVQTLIYSGADVTHFDNDGLTPLMHAAKIGNAEIVTALLESG 59
Cdd:PHA02874   42 AIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNG 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 15-109 4.82e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 44.66  E-value: 4.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063743498  15 DLKKVQTLIYSGADV----------THF------DNDGLTPLMHAAKIGNAEIVTALLESGAPWNALSPSNLSAGDFAME 78
Cdd:PHA03100  155 DLKILKLLIDKGVDInaknrvnyllSYGvpinikDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAIL 234

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1063743498  79 AGHQETFDLLLKTGIQSELILGTIARNQTKN 109
Cdd:PHA03100  235 NNNKEIFKLLLNNGPSIKTIIETLLYFKDKD 265
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 10-92 1.33e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 43.41  E-value: 1.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063743498  10 AAKSGDLKKVQTLIYSGADVTHFDNDGLTPLMHAAKIGNAEIVTALLESGAPWNALSPSNLSAGDFAMEAGHQETFDLLL 89
Cdd:PHA02874  131 AIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLI 210


                  ...
gi 1063743498  90 KTG 92
Cdd:PHA02874  211 DHG 213
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 5-84 2.11e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 42.93  E-value: 2.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063743498   5 DQLCLAAKSGDLKKVQTLIYSGADVTHFDNDGLTPLMHAAKIGNAEIVTALLESGAP------WNALSPSNLSAGDFAME 78
Cdd:PLN03192  624 DLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADvdkantDDDFSPTELRELLQKRE 703


                  ....*.
gi 1063743498  79 AGHQET 84
Cdd:PLN03192  704 LGHSIT 709
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 7-98 2.59e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 42.29  E-value: 2.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063743498   7 LCLAAKSGDLKKVQTLIYSGADVTHFDNDGLTPLMHAAKIGNAEIVTALLESGAPWNALSPS-NLSAGDFAMEAGHQETF 85
Cdd:PHA02875  139 LHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNgCVAALCYAIENNKIDIV 218

                          90
                  ....*....|...
gi 1063743498  86 DLLLKTGIQSELI 98
Cdd:PHA02875  219 RLFIKRGADCNIM 231
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 35-64 2.70e-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: 37.65  E-value: 2.70e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1063743498  35 DGLTPLMHAA-KIGNAEIVTALLESGAPWNA 64
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNA 31
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 15-89 3.35e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 42.36  E-value: 3.35e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063743498  15 DLKKVQTLIYSGADVTHFDNDGLTPLMHAAKIGNAEIVTALLESGAPWNALSPSNLSAGDFAMEAGHQETFDLLL 89
Cdd:PHA02876  157 ELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAII 231
PHA03095 PHA03095
ankyrin-like protein; Provisional
 18-104 7.98e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 40.78  E-value: 7.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063743498  18 KVQTLIYSGADVTHFDNDGLTPLMHAAKIGNAEIVTALLESGAPWNALSPSNLSAGDFAMEAGHQETFDLLLKTGIQSEL 97
Cdd:PHA03095  239 LVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAET 318


                  ....*..
gi 1063743498  98 ILGTIAR 104
Cdd:PHA03095  319 VAATLNT 325
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 7-64 1.01e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 40.82  E-value: 1.01e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063743498   7 LCLAAKSG-DLKKVQTLIYSGADVTHFDNDGLTPLMHAAKIG-NAEIVTALLESGAPWNA 64
Cdd:PHA02876  311 LYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGANVNA 370
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 35-60 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: 35.26  E-value: 1.93e-03
                           10        20
                   ....*....|....*....|....*.
gi 1063743498   35 DGLTPLMHAAKIGNAEIVTALLESGA 60
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGA 26
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 35-64 2.24e-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: 34.93  E-value: 2.24e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1063743498  35 DGLTPLMHAAKIGNAEIVTALLESGAPWNA 64
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
36-89 7.19e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 34.17  E-value: 7.19e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1063743498  36 GLTPLMHAAKIGNAEIVTALLESGAPWNALSPSNLSAGDFAMEAGHQETFDLLL 89
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 10-90 8.36e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 37.66  E-value: 8.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063743498  10 AAKSGDLKKVQTLIYSGA---DVthFDNDGLTPLMHAAKIGNAEIVTALLESGAPWNALSPSNLSAGDFAMEAGHQETFD 86
Cdd:PHA02875   75 AVEEGDVKAVEELLDLGKfadDV--FYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIE 152


                  ....
gi 1063743498  87 LLLK 90
Cdd:PHA02875  153 LLID 156
 
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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