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Conserved domains on  [gi|1832470187|ref|XP_033372137|]
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ankyrin repeat and zinc finger domain-containing protein 1 isoform X3 [Parus major]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
bVLRF1 pfam18826
Bacteroidetes VLRF1 release factor; Archaeo-eukaryotic release factor domain family belonging ...
 195-339 8.42e-75

Bacteroidetes VLRF1 release factor; Archaeo-eukaryotic release factor domain family belonging to the VLRF1 clade observed primarily in the bacteroidetes bacterial lineage. Contains a conserved glutamine residue in the release factor catalytic loop, suggesting it functions as an active peptidyl-tRNA hydrolase at the ribosome.


:

Pssm-ID: 465880  Cd Length: 143  Bit Score: 237.02  E-value: 8.42e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832470187 195 WVVLMMGGGHFAGAVFRGLQVQEHKTFHRYTVRARRGTAQGLRDAQTpgSAPRSAGASLRRYNEAALLKDIQDLLAAWAQ 274
Cdd:pfam18826   1 WALLMIGGGHFAGAVFSGGEVLAHKTFHRYTTRRKQGGSQSSNDNAK--GKAKSAGASLRRYNEQALQEDIRELLSEWKE 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1832470187 275 HLNEAQRIFLRAPRQNRALLFGGRNPLLTRGDPRICHIPLSTRRATLREVLRVHTTLASLQVYGK 339
Cdd:pfam18826  79 DIDKCELIFIRAPGSNRKILFGYEGAPLDKDDPRLRSIPFPTRRPTFSELKRVFSELTTVKVSHK 143
ANKYR super family cl34000
Ankyrin repeat [Signal transduction mechanisms];
476-563 4.59e-09

Ankyrin repeat [Signal transduction mechanisms];


The actual alignment was detected with superfamily member COG0666:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 58.04  E-value: 4.59e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832470187 476 DALFTACKTGDIRTLRHLLgvpeDGGLPGDSEDGE------------SLDMARSLLNQ-----PVDERGCTLLHVAARAG 538
Cdd:COG0666    89 TLLHAAARNGDLEIVKLLL----EAGADVNARDKDgetplhlaayngNLEIVKLLLEAgadvnAQDNDGNTPLHLAAANG 164

                          90       100
                  ....*....|....*....|....*
gi 1832470187 539 KAEAVCLLLEAGADPALRDRQERTP 563
Cdd:COG0666   165 NLEIVKLLLEAGADVNARDNDGETP 189
 
Name Accession Description Interval E-value
bVLRF1 pfam18826
Bacteroidetes VLRF1 release factor; Archaeo-eukaryotic release factor domain family belonging ...
 195-339 8.42e-75

Bacteroidetes VLRF1 release factor; Archaeo-eukaryotic release factor domain family belonging to the VLRF1 clade observed primarily in the bacteroidetes bacterial lineage. Contains a conserved glutamine residue in the release factor catalytic loop, suggesting it functions as an active peptidyl-tRNA hydrolase at the ribosome.


Pssm-ID: 465880  Cd Length: 143  Bit Score: 237.02  E-value: 8.42e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832470187 195 WVVLMMGGGHFAGAVFRGLQVQEHKTFHRYTVRARRGTAQGLRDAQTpgSAPRSAGASLRRYNEAALLKDIQDLLAAWAQ 274
Cdd:pfam18826   1 WALLMIGGGHFAGAVFSGGEVLAHKTFHRYTTRRKQGGSQSSNDNAK--GKAKSAGASLRRYNEQALQEDIRELLSEWKE 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1832470187 275 HLNEAQRIFLRAPRQNRALLFGGRNPLLTRGDPRICHIPLSTRRATLREVLRVHTTLASLQVYGK 339
Cdd:pfam18826  79 DIDKCELIFIRAPGSNRKILFGYEGAPLDKDDPRLRSIPFPTRRPTFSELKRVFSELTTVKVSHK 143
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
476-563 4.59e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 58.04  E-value: 4.59e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832470187 476 DALFTACKTGDIRTLRHLLgvpeDGGLPGDSEDGE------------SLDMARSLLNQ-----PVDERGCTLLHVAARAG 538
Cdd:COG0666    89 TLLHAAARNGDLEIVKLLL----EAGADVNARDKDgetplhlaayngNLEIVKLLLEAgadvnAQDNDGNTPLHLAAANG 164

                          90       100
                  ....*....|....*....|....*
gi 1832470187 539 KAEAVCLLLEAGADPALRDRQERTP 563
Cdd:COG0666   165 NLEIVKLLLEAGADVNARDNDGETP 189
Ank_2 pfam12796
Ankyrin repeats (3 copies);
478-557 1.50e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 52.43  E-value: 1.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832470187 478 LFTACKTGDIRTLRHLLGVPEDGGLPGDSED--------GESLDMARSLLNQP---VDERGCTLLHVAARAGKAEAVCLL 546
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRtalhlaakNGHLEIVKLLLEHAdvnLKDNGRTALHYAARSGHLEIVKLL 80

                          90
                  ....*....|.
gi 1832470187 547 LEAGADPALRD 557
Cdd:pfam12796  81 LEKGADINVKD 91
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 523-599 7.39e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.04  E-value: 7.39e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1832470187 523 VDERGCTLLHVAARAGKAEAVCLLLEAGADPALRDRQERTPYCVSADRVTRNAFRKFMVVHPDKYDYSRAKVPGPLT 599
Cdd:PTZ00322  111 RDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELGANAKPDSFT 187
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 526-553 1.55e-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: 36.41  E-value: 1.55e-03
                           10        20
                   ....*....|....*....|....*...
gi 1832470187  526 RGCTLLHVAARAGKAEAVCLLLEAGADP 553
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
 
Name Accession Description Interval E-value
bVLRF1 pfam18826
Bacteroidetes VLRF1 release factor; Archaeo-eukaryotic release factor domain family belonging ...
 195-339 8.42e-75

Bacteroidetes VLRF1 release factor; Archaeo-eukaryotic release factor domain family belonging to the VLRF1 clade observed primarily in the bacteroidetes bacterial lineage. Contains a conserved glutamine residue in the release factor catalytic loop, suggesting it functions as an active peptidyl-tRNA hydrolase at the ribosome.


Pssm-ID: 465880  Cd Length: 143  Bit Score: 237.02  E-value: 8.42e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832470187 195 WVVLMMGGGHFAGAVFRGLQVQEHKTFHRYTVRARRGTAQGLRDAQTpgSAPRSAGASLRRYNEAALLKDIQDLLAAWAQ 274
Cdd:pfam18826   1 WALLMIGGGHFAGAVFSGGEVLAHKTFHRYTTRRKQGGSQSSNDNAK--GKAKSAGASLRRYNEQALQEDIRELLSEWKE 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1832470187 275 HLNEAQRIFLRAPRQNRALLFGGRNPLLTRGDPRICHIPLSTRRATLREVLRVHTTLASLQVYGK 339
Cdd:pfam18826  79 DIDKCELIFIRAPGSNRKILFGYEGAPLDKDDPRLRSIPFPTRRPTFSELKRVFSELTTVKVSHK 143
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
476-563 4.59e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 58.04  E-value: 4.59e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832470187 476 DALFTACKTGDIRTLRHLLgvpeDGGLPGDSEDGE------------SLDMARSLLNQ-----PVDERGCTLLHVAARAG 538
Cdd:COG0666    89 TLLHAAARNGDLEIVKLLL----EAGADVNARDKDgetplhlaayngNLEIVKLLLEAgadvnAQDNDGNTPLHLAAANG 164

                          90       100
                  ....*....|....*....|....*
gi 1832470187 539 KAEAVCLLLEAGADPALRDRQERTP 563
Cdd:COG0666   165 NLEIVKLLLEAGADVNARDNDGETP 189
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
477-563 6.42e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 57.66  E-value: 6.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832470187 477 ALFTACKTGDIRTLRHLL--GVP-----EDGGLP-------GDsedgesLDMARSLLNQPVD-----ERGCTLLHVAARA 537
Cdd:COG0666   123 PLHLAAYNGNLEIVKLLLeaGADvnaqdNDGNTPlhlaaanGN------LEIVKLLLEAGADvnardNDGETPLHLAAEN 196

                          90       100
                  ....*....|....*....|....*.
gi 1832470187 538 GKAEAVCLLLEAGADPALRDRQERTP 563
Cdd:COG0666   197 GHLEIVKLLLEAGADVNAKDNDGKTA 222
Ank_2 pfam12796
Ankyrin repeats (3 copies);
478-557 1.50e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 52.43  E-value: 1.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832470187 478 LFTACKTGDIRTLRHLLGVPEDGGLPGDSED--------GESLDMARSLLNQP---VDERGCTLLHVAARAGKAEAVCLL 546
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRtalhlaakNGHLEIVKLLLEHAdvnLKDNGRTALHYAARSGHLEIVKLL 80

                          90
                  ....*....|.
gi 1832470187 547 LEAGADPALRD 557
Cdd:pfam12796  81 LEKGADINVKD 91
Ank_5 pfam13857
Ankyrin repeats (many copies);
524-564 1.22e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.10  E-value: 1.22e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1832470187 524 DERGCTLLHVAARAGKAEAVCLLLEAGADPALRDRQERTPY 564
Cdd:pfam13857  13 DGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
515-570 1.41e-05

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 47.64  E-value: 1.41e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1832470187 515 ARSLLNQPVDERGCTLLHVAARAGKAEAVCLLLEAGADPALRDRQERTPYCVSADR 570
Cdd:COG0666    75 AAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYN 130
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 526-558 2.17e-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: 2.17e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1832470187 526 RGCTLLHVAA-RAGKAEAVCLLLEAGADPALRDR 558
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 523-599 7.39e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.04  E-value: 7.39e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1832470187 523 VDERGCTLLHVAARAGKAEAVCLLLEAGADPALRDRQERTPYCVSADRVTRNAFRKFMVVHPDKYDYSRAKVPGPLT 599
Cdd:PTZ00322  111 RDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELGANAKPDSFT 187
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 526-553 8.62e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.24  E-value: 8.62e-04
                          10        20
                  ....*....|....*....|....*...
gi 1832470187 526 RGCTLLHVAARAGKAEAVCLLLEAGADP 553
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADI 28
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 526-553 1.55e-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: 36.41  E-value: 1.55e-03
                           10        20
                   ....*....|....*....|....*...
gi 1832470187  526 RGCTLLHVAARAGKAEAVCLLLEAGADP 553
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
Ank_2 pfam12796
Ankyrin repeats (3 copies);
531-563 1.68e-03

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 38.17  E-value: 1.68e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1832470187 531 LHVAARAGKAEAVCLLLEAGADPALRDRQERTP 563
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTA 33
 
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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