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Conserved domains on  [gi|544346294|ref|NP_001269721|]
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tRNA endonuclease ANKZF1 isoform 2 [Homo sapiens]

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 ...
 1-141 4.57e-69

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: 217.76  E-value: 4.57e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346294    1 MAAAGHFAGAIFQGREVVTHKTFHRYTVRAKRGTAQGLRDARGGPSHSAGANLRRYNEATLYKDVRDLLAgpSWAKALEE 80
Cdd:pfam18826   5 MIGGGHFAGAVFSGGEVLAHKTFHRYTTRRKQGGSQSSNDNAKGKAKSAGASLRRYNEQALQEDIRELLS--EWKEDIDK 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 544346294   81 AGTILLRAPRSGRSLFFGGKGAPLQRGDPRLWDIPLATRRPTFQELQRVLHKLTTLHVYEE 141
Cdd:pfam18826  83 CELIFIRAPGSNRKILFGYEGAPLDKDDPRLRSIPFPTRRPTFSELKRVFSELTTVKVSHK 143
VATC pfam18716
Vms1-associating treble clef domain; Treble clef fold domain found at C-terminus of many, but ...
 473-514 1.44e-20

Vms1-associating treble clef domain; Treble clef fold domain found at C-terminus of many, but not all, Vms1/ANKZF1-like proteins.


:

Pssm-ID: 465846  Cd Length: 43  Bit Score: 84.68  E-value: 1.44e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 544346294  473 VNTRRCWSCGASLQGLTPFHYLDFSFCSTRCLQDHRRQAGRP 514
Cdd:pfam18716   1 KNYRRCWICGESLLGKVPFHKLDFSYCSTKCLRAHRRAGFAP 42
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
285-390 1.40e-11

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 65.36  E-value: 1.40e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346294 285 WNALLAACRAGDVGVLKLQLApSPADPRVLSllsaplgSGGFTLLHAAAAAGRGSVVRLLLEAGADPTVQDSRARPPYTV 364
Cdd:COG0666  154 NTPLHLAAANGNLEIVKLLLE-AGADVNARD-------NDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDL 225

                         90       100
                 ....*....|....*....|....*.
gi 544346294 365 AADKSTRNEFRRFMEKNPDAYDYNKA 390
Cdd:COG0666  226 AAENGNLEIVKLLLEAGADLNAKDKD 251
 
Name Accession Description Interval E-value
bVLRF1 pfam18826
Bacteroidetes VLRF1 release factor; Archaeo-eukaryotic release factor domain family belonging ...
 1-141 4.57e-69

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: 217.76  E-value: 4.57e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346294    1 MAAAGHFAGAIFQGREVVTHKTFHRYTVRAKRGTAQGLRDARGGPSHSAGANLRRYNEATLYKDVRDLLAgpSWAKALEE 80
Cdd:pfam18826   5 MIGGGHFAGAVFSGGEVLAHKTFHRYTTRRKQGGSQSSNDNAKGKAKSAGASLRRYNEQALQEDIRELLS--EWKEDIDK 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 544346294   81 AGTILLRAPRSGRSLFFGGKGAPLQRGDPRLWDIPLATRRPTFQELQRVLHKLTTLHVYEE 141
Cdd:pfam18826  83 CELIFIRAPGSNRKILFGYEGAPLDKDDPRLRSIPFPTRRPTFSELKRVFSELTTVKVSHK 143
VATC pfam18716
Vms1-associating treble clef domain; Treble clef fold domain found at C-terminus of many, but ...
 473-514 1.44e-20

Vms1-associating treble clef domain; Treble clef fold domain found at C-terminus of many, but not all, Vms1/ANKZF1-like proteins.


Pssm-ID: 465846  Cd Length: 43  Bit Score: 84.68  E-value: 1.44e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 544346294  473 VNTRRCWSCGASLQGLTPFHYLDFSFCSTRCLQDHRRQAGRP 514
Cdd:pfam18716   1 KNYRRCWICGESLLGKVPFHKLDFSYCSTKCLRAHRRAGFAP 42
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
285-390 1.40e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 65.36  E-value: 1.40e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346294 285 WNALLAACRAGDVGVLKLQLApSPADPRVLSllsaplgSGGFTLLHAAAAAGRGSVVRLLLEAGADPTVQDSRARPPYTV 364
Cdd:COG0666  154 NTPLHLAAANGNLEIVKLLLE-AGADVNARD-------NDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDL 225

                         90       100
                 ....*....|....*....|....*.
gi 544346294 365 AADKSTRNEFRRFMEKNPDAYDYNKA 390
Cdd:COG0666  226 AAENGNLEIVKLLLEAGADLNAKDKD 251
Ank_2 pfam12796
Ankyrin repeats (3 copies);
285-355 1.31e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 49.34  E-value: 1.31e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 544346294  285 WNALLAACRAGDVGVLKLqlapspadprVLSLLSAPLGSGGFTLLHAAAAAGRGSVVRLLLEAGADPTVQD 355
Cdd:pfam12796  31 RTALHLAAKNGHLEIVKL----------LLEHADVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 325-397 1.94e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.67  E-value: 1.94e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 544346294 325 GFTLLHAAAAAGRGSVVRLLLEAGADPTVQDSRARPPYTVAADKSTRNEFRRFMEKNPDAYDYNKAQVPGPLT 397
Cdd:PTZ00322 115 GRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELGANAKPDSFT 187
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 325-353 2.86e-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: 2.86e-03
                           10        20
                   ....*....|....*....|....*....
gi 544346294   325 GFTLLHAAAAAGRGSVVRLLLEAGADPTV 353
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
bVLRF1 pfam18826
Bacteroidetes VLRF1 release factor; Archaeo-eukaryotic release factor domain family belonging ...
 1-141 4.57e-69

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: 217.76  E-value: 4.57e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346294    1 MAAAGHFAGAIFQGREVVTHKTFHRYTVRAKRGTAQGLRDARGGPSHSAGANLRRYNEATLYKDVRDLLAgpSWAKALEE 80
Cdd:pfam18826   5 MIGGGHFAGAVFSGGEVLAHKTFHRYTTRRKQGGSQSSNDNAKGKAKSAGASLRRYNEQALQEDIRELLS--EWKEDIDK 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 544346294   81 AGTILLRAPRSGRSLFFGGKGAPLQRGDPRLWDIPLATRRPTFQELQRVLHKLTTLHVYEE 141
Cdd:pfam18826  83 CELIFIRAPGSNRKILFGYEGAPLDKDDPRLRSIPFPTRRPTFSELKRVFSELTTVKVSHK 143
VATC pfam18716
Vms1-associating treble clef domain; Treble clef fold domain found at C-terminus of many, but ...
 473-514 1.44e-20

Vms1-associating treble clef domain; Treble clef fold domain found at C-terminus of many, but not all, Vms1/ANKZF1-like proteins.


Pssm-ID: 465846  Cd Length: 43  Bit Score: 84.68  E-value: 1.44e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 544346294  473 VNTRRCWSCGASLQGLTPFHYLDFSFCSTRCLQDHRRQAGRP 514
Cdd:pfam18716   1 KNYRRCWICGESLLGKVPFHKLDFSYCSTKCLRAHRRAGFAP 42
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
285-390 1.40e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 65.36  E-value: 1.40e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346294 285 WNALLAACRAGDVGVLKLQLApSPADPRVLSllsaplgSGGFTLLHAAAAAGRGSVVRLLLEAGADPTVQDSRARPPYTV 364
Cdd:COG0666  154 NTPLHLAAANGNLEIVKLLLE-AGADVNARD-------NDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDL 225

                         90       100
                 ....*....|....*....|....*.
gi 544346294 365 AADKSTRNEFRRFMEKNPDAYDYNKA 390
Cdd:COG0666  226 AAENGNLEIVKLLLEAGADLNAKDKD 251
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
283-368 2.45e-10

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 61.51  E-value: 2.45e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346294 283 ELWNALLAACRAGDVGVLKLQLApSPADPRVLSllsaplgSGGFTLLHAAAAAGRGSVVRLLLEAGADPTVQDSRARPPY 362
Cdd:COG0666   86 GGNTLLHAAARNGDLEIVKLLLE-AGADVNARD-------KDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPL 157


                 ....*.
gi 544346294 363 TVAADK 368
Cdd:COG0666  158 HLAAAN 163
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
285-368 9.03e-10

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 59.97  E-value: 9.03e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346294 285 WNALLAACRAGDVGVLKLQLApSPADPRVLsllsaplGSGGFTLLHAAAAAGRGSVVRLLLEAGADPTVQDSRARPPYTV 364
Cdd:COG0666  121 ETPLHLAAYNGNLEIVKLLLE-AGADVNAQ-------DNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHL 192


                 ....
gi 544346294 365 AADK 368
Cdd:COG0666  193 AAEN 196
Ank_2 pfam12796
Ankyrin repeats (3 copies);
285-355 1.31e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 49.34  E-value: 1.31e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 544346294  285 WNALLAACRAGDVGVLKLqlapspadprVLSLLSAPLGSGGFTLLHAAAAAGRGSVVRLLLEAGADPTVQD 355
Cdd:pfam12796  31 RTALHLAAKNGHLEIVKL----------LLEHADVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
264-402 1.03e-06

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 50.34  E-value: 1.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544346294 264 AVAAPLGPLLDEAKAPGQPELWNALLAACRAGDVGVLKLQLAPSPADprvlsllsAPLGSGGFTLLHAAAAAGRGSVVRL 343
Cdd:COG0666   34 LLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI--------NAKDDGGNTLLHAAARNGDLEIVKL 105

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 544346294 344 LLEAGADPTVQDSRARPPYTVAADKSTRNEFRRFMEK--NPDAYDYNKAqvpgplTPEMEA 402
Cdd:COG0666  106 LLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAgaDVNAQDNDGN------TPLHLA 160
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 325-397 1.94e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.67  E-value: 1.94e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 544346294 325 GFTLLHAAAAAGRGSVVRLLLEAGADPTVQDSRARPPYTVAADKSTRNEFRRFMEKNPDAYDYNKAQVPGPLT 397
Cdd:PTZ00322 115 GRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELGANAKPDSFT 187
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 325-355 1.10e-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: 42.28  E-value: 1.10e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 544346294  325 GFTLLHAAAA-AGRGSVVRLLLEAGADPTVQD 355
Cdd:pfam00023   2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
Ank_5 pfam13857
Ankyrin repeats (many copies);
324-365 2.75e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.87  E-value: 2.75e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 544346294  324 GGFTLLHAAAAAGRGSVVRLLLEAGADPTVQDSRARPPYTVA 365
Cdd:pfam13857  15 EGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_2 pfam12796
Ankyrin repeats (3 copies);
288-346 4.56e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 39.33  E-value: 4.56e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 544346294  288 LLAACRAGDVGVLKLqLAPSPADPRVLSLLsaplgsgGFTLLHAAAAAGRGSVVRLLLE 346
Cdd:pfam12796   1 LHLAAKNGNLELVKL-LLENGADANLQDKN-------GRTALHLAAKNGHLEIVKLLLE 51
Ank_2 pfam12796
Ankyrin repeats (3 copies);
329-402 1.69e-03

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 37.79  E-value: 1.69e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 544346294  329 LHAAAAAGRGSVVRLLLEAGADPTVQDSRARPPYTVAADKSTRNEFRRFMEK-NPDAYDYNKaqvpgplTPEMEA 402
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHaDVNLKDNGR-------TALHYA 68
Ank_4 pfam13637
Ankyrin repeats (many copies);
285-345 2.33e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.10  E-value: 2.33e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 544346294  285 WNALLAACRAGDVGVLKLqLAPSPADPRVLSllsaplgSGGFTLLHAAAAAGRGSVVRLLL 345
Cdd:pfam13637   2 LTALHAAAASGHLELLRL-LLEKGADINAVD-------GNGETALHFAASNGNVEVLKLLL 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 325-353 2.86e-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: 2.86e-03
                           10        20
                   ....*....|....*....|....*....
gi 544346294   325 GFTLLHAAAAAGRGSVVRLLLEAGADPTV 353
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
327-366 3.20e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 35.71  E-value: 3.20e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 544346294  327 TLLHAAAAAGRGSVVRLLLEAGADPTVQDSRARPPYTVAA 366
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAA 42
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 325-351 3.80e-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: 3.80e-03
                          10        20
                  ....*....|....*....|....*..
gi 544346294  325 GFTLLHAAAAAGRGSVVRLLLEAGADP 351
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADI 28
 
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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