NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|148667962|gb|EDL00379|]
View 

mCG133867, isoform CRA_c [Mus musculus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
bVLRF1 pfam18826
Bacteroidetes VLRF1 release factor; Archaeo-eukaryotic release factor domain family belonging ...
 231-375 5.90e-70

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: 225.46  E-value: 5.90e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148667962  231 YVVLMAAAGHFAGAIFQGREVVAHKTFHRYTVRAKRGTAQGLQDAHGRASRSAGANLRRYNEAMLYKDVRNLLAGpiWSK 310
Cdd:pfam18826   1 WALLMIGGGHFAGAVFSGGEVLAHKTFHRYTTRRKQGGSQSSNDNAKGKAKSAGASLRRYNEQALQEDIRELLSE--WKE 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148667962  311 ALGEAETVLFRAPRSGRSLFFGGQGAPLQRDDPRLWDIPLTTRRPTFGELQRVLHKLTTLQVYDE 375
Cdd:pfam18826  79 DIDKCELIFIRAPGSNRKILFGYEGAPLDKDDPRLRSIPFPTRRPTFSELKRVFSELTTVKVSHK 143
VATC pfam18716
Vms1-associating treble clef domain; Treble clef fold domain found at C-terminus of many, but ...
 709-746 1.26e-17

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: 76.59  E-value: 1.26e-17
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 148667962  709 RCWSCGVSLQGLIPFHYLDFSFCSTRCLRDHRSQAGRP 746
Cdd:pfam18716   5 RCWICGESLLGKVPFHKLDFSYCSTKCLRAHRRAGFAP 42
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
520-622 6.11e-11

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 64.20  E-value: 6.11e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148667962 520 LLAACRAGEVEVLKLQLATGlVDPgvksllNAPlGSGGFTLLHAAAAAGRGLVVRLLLEAGADPTVQDSRARPPYTVAAD 599
Cdd:COG0666  157 LHLAAANGNLEIVKLLLEAG-ADV------NAR-DNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAE 228

                         90       100
                 ....*....|....*....|...
gi 148667962 600 KSTRNEFRRFMEKNLDAYDYNKA 622
Cdd:COG0666  229 NGNLEIVKLLLEAGADLNAKDKD 251
 
Name Accession Description Interval E-value
bVLRF1 pfam18826
Bacteroidetes VLRF1 release factor; Archaeo-eukaryotic release factor domain family belonging ...
 231-375 5.90e-70

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: 225.46  E-value: 5.90e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148667962  231 YVVLMAAAGHFAGAIFQGREVVAHKTFHRYTVRAKRGTAQGLQDAHGRASRSAGANLRRYNEAMLYKDVRNLLAGpiWSK 310
Cdd:pfam18826   1 WALLMIGGGHFAGAVFSGGEVLAHKTFHRYTTRRKQGGSQSSNDNAKGKAKSAGASLRRYNEQALQEDIRELLSE--WKE 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148667962  311 ALGEAETVLFRAPRSGRSLFFGGQGAPLQRDDPRLWDIPLTTRRPTFGELQRVLHKLTTLQVYDE 375
Cdd:pfam18826  79 DIDKCELIFIRAPGSNRKILFGYEGAPLDKDDPRLRSIPFPTRRPTFSELKRVFSELTTVKVSHK 143
VATC pfam18716
Vms1-associating treble clef domain; Treble clef fold domain found at C-terminus of many, but ...
 709-746 1.26e-17

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: 76.59  E-value: 1.26e-17
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 148667962  709 RCWSCGVSLQGLIPFHYLDFSFCSTRCLRDHRSQAGRP 746
Cdd:pfam18716   5 RCWICGESLLGKVPFHKLDFSYCSTKCLRAHRRAGFAP 42
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
520-622 6.11e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 64.20  E-value: 6.11e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148667962 520 LLAACRAGEVEVLKLQLATGlVDPgvksllNAPlGSGGFTLLHAAAAAGRGLVVRLLLEAGADPTVQDSRARPPYTVAAD 599
Cdd:COG0666  157 LHLAAANGNLEIVKLLLEAG-ADV------NAR-DNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAE 228

                         90       100
                 ....*....|....*....|...
gi 148667962 600 KSTRNEFRRFMEKNLDAYDYNKA 622
Cdd:COG0666  229 NGNLEIVKLLLEAGADLNAKDKD 251
Ank_2 pfam12796
Ankyrin repeats (3 copies);
520-587 1.05e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 47.42  E-value: 1.05e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148667962  520 LLAACRAGEVEVLKLQLATGLVDpgvksllnapLGSGGFTLLHAAAAAGRGLVVRLLLEAGADPTVQD 587
Cdd:pfam12796  34 LHLAAKNGHLEIVKLLLEHADVN----------LKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 557-629 9.98e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.13  E-value: 9.98e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148667962 557 GFTLLHAAAAAGRGLVVRLLLEAGADPTVQDSRARPPYTVAADKSTRNEFRRFMEKNLDAYDYNKARVPGPLT 629
Cdd:PTZ00322 115 GRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELGANAKPDSFT 187
 
Name Accession Description Interval E-value
bVLRF1 pfam18826
Bacteroidetes VLRF1 release factor; Archaeo-eukaryotic release factor domain family belonging ...
 231-375 5.90e-70

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: 225.46  E-value: 5.90e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148667962  231 YVVLMAAAGHFAGAIFQGREVVAHKTFHRYTVRAKRGTAQGLQDAHGRASRSAGANLRRYNEAMLYKDVRNLLAGpiWSK 310
Cdd:pfam18826   1 WALLMIGGGHFAGAVFSGGEVLAHKTFHRYTTRRKQGGSQSSNDNAKGKAKSAGASLRRYNEQALQEDIRELLSE--WKE 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148667962  311 ALGEAETVLFRAPRSGRSLFFGGQGAPLQRDDPRLWDIPLTTRRPTFGELQRVLHKLTTLQVYDE 375
Cdd:pfam18826  79 DIDKCELIFIRAPGSNRKILFGYEGAPLDKDDPRLRSIPFPTRRPTFSELKRVFSELTTVKVSHK 143
VATC pfam18716
Vms1-associating treble clef domain; Treble clef fold domain found at C-terminus of many, but ...
 709-746 1.26e-17

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: 76.59  E-value: 1.26e-17
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 148667962  709 RCWSCGVSLQGLIPFHYLDFSFCSTRCLRDHRSQAGRP 746
Cdd:pfam18716   5 RCWICGESLLGKVPFHKLDFSYCSTKCLRAHRRAGFAP 42
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
520-622 6.11e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 64.20  E-value: 6.11e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148667962 520 LLAACRAGEVEVLKLQLATGlVDPgvksllNAPlGSGGFTLLHAAAAAGRGLVVRLLLEAGADPTVQDSRARPPYTVAAD 599
Cdd:COG0666  157 LHLAAANGNLEIVKLLLEAG-ADV------NAR-DNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAE 228

                         90       100
                 ....*....|....*....|...
gi 148667962 600 KSTRNEFRRFMEKNLDAYDYNKA 622
Cdd:COG0666  229 NGNLEIVKLLLEAGADLNAKDKD 251
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
517-600 4.96e-10

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 61.12  E-value: 4.96e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148667962 517 WDTLLAACRAGEVEVLKLqlatgLVDPGVKslLNAPlGSGGFTLLHAAAAAGRGLVVRLLLEAGADPTVQDSRARPPYTV 596
Cdd:COG0666  121 ETPLHLAAYNGNLEIVKL-----LLEAGAD--VNAQ-DNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHL 192


                 ....
gi 148667962 597 AADK 600
Cdd:COG0666  193 AAEN 196
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
515-600 1.62e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 59.58  E-value: 1.62e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148667962 515 ELWDTLLAACRAGEVEVLKLQLATGlVDPgvksllNAPlGSGGFTLLHAAAAAGRGLVVRLLLEAGADPTVQDSRARPPY 594
Cdd:COG0666   86 GGNTLLHAAARNGDLEIVKLLLEAG-ADV------NAR-DKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPL 157


                 ....*.
gi 148667962 595 TVAADK 600
Cdd:COG0666  158 HLAAAN 163
Ank_2 pfam12796
Ankyrin repeats (3 copies);
520-587 1.05e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 47.42  E-value: 1.05e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148667962  520 LLAACRAGEVEVLKLQLATGLVDpgvksllnapLGSGGFTLLHAAAAAGRGLVVRLLLEAGADPTVQD 587
Cdd:pfam12796  34 LHLAAKNGHLEIVKLLLEHADVN----------LKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
516-600 3.99e-06

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 49.18  E-value: 3.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148667962 516 LWDTLLAACRAGEVEVLKLQLAtglvdpgvKSLLNAPLGSGGFTLLHAAAAAGRGLVVRLLLEAGADPTVQDSRARPPYT 595
Cdd:COG0666   54 GALLLLAAALAGDLLVALLLLA--------AGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLH 125


                 ....*
gi 148667962 596 VAADK 600
Cdd:COG0666  126 LAAYN 130
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 557-629 9.98e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.13  E-value: 9.98e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148667962 557 GFTLLHAAAAAGRGLVVRLLLEAGADPTVQDSRARPPYTVAADKSTRNEFRRFMEKNLDAYDYNKARVPGPLT 629
Cdd:PTZ00322 115 GRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELGANAKPDSFT 187
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 557-587 3.66e-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: 41.12  E-value: 3.66e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 148667962  557 GFTLLHAAAA-AGRGLVVRLLLEAGADPTVQD 587
Cdd:pfam00023   2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
520-623 1.97e-04

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 44.17  E-value: 1.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148667962 520 LLAACRAGEVEVLKLQLATGlVDPGVKSllnaplgSGGFTLLHAAAAAGRGLVVRLLLEAGADPTVQDSRARPPYTVAAD 599
Cdd:COG0666  190 LHLAAENGHLEIVKLLLEAG-ADVNAKD-------NDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAA 261

                         90       100
                 ....*....|....*....|....
gi 148667962 600 KSTRNEFRRFMEKNLDAYDYNKAR 623
Cdd:COG0666  262 AGAALIVKLLLLALLLLAAALLDL 285
Ank_5 pfam13857
Ankyrin repeats (many copies);
556-597 3.72e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.17  E-value: 3.72e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 148667962  556 GGFTLLHAAAAAGRGLVVRLLLEAGADPTVQDSRARPPYTVA 597
Cdd:pfam13857  15 EGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_2 pfam12796
Ankyrin repeats (3 copies);
561-621 6.11e-03

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 36.63  E-value: 6.11e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148667962  561 LHAAAAAGRGLVVRLLLEAGADPTVQDSRARPPYTVAADKSTRNEFRRFMEK-NLDAYDYNK 621
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHaDVNLKDNGR 62
Ank_2 pfam12796
Ankyrin repeats (3 copies);
520-578 6.81e-03

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 36.63  E-value: 6.81e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 148667962  520 LLAACRAGEVEVLKLQLATGlVDPGVKSLLnaplgsgGFTLLHAAAAAGRGLVVRLLLE 578
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENG-ADANLQDKN-------GRTALHLAAKNGHLEIVKLLLE 51
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 557-583 8.05e-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: 34.54  E-value: 8.05e-03
                          10        20
                  ....*....|....*....|....*..
gi 148667962  557 GFTLLHAAAAAGRGLVVRLLLEAGADP 583
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH