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Conserved domains on  [gi|472581581|gb|EMS19309|]
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protein of Cgr1 family [Rhodotorula toruloides NP11]

Protein Classification

CGR1 family protein( domain architecture ID 11145969)

CGR1 family protein similar to rRNA-processing proteins, CgrA and CGR1, which are involved in nucleolar integrity and required for processing of the pre-rRNA for the 60S ribosome subunit

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Cgr1 pfam03879
Cgr1 family; Members of this family are coiled-coil proteins that are involved in pre-rRNA ...
35-141 1.34e-15

Cgr1 family; Members of this family are coiled-coil proteins that are involved in pre-rRNA processing.


:

Pssm-ID: 427562 [Multi-domain]  Cd Length: 107  Bit Score: 67.65  E-value: 1.34e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472581581   35 SSTNVSGRWWKTEHKATTRVQsgkKAPQQLDKAWKQREERRKRDEAIKKLERELKQEKEDEADRKKRINLERREKEAEKK 114
Cdd:pfam03879   2 KGMRVSGKPWKAEKKAFRRSS---LVVGPKSKSWEKRQEKRLELKAIKAKEKELKDEKEAERQRRIQAIKERREAKEEKE 78
                          90       100
                  ....*....|....*....|....*..
gi 472581581  115 RLAEMAARMSAKKLQRMKKRLGRSKKV 141
Cdd:pfam03879  79 RYEELAAKMHAKKVERLKRKEKRNKLL 105
 
Name Accession Description Interval E-value
Cgr1 pfam03879
Cgr1 family; Members of this family are coiled-coil proteins that are involved in pre-rRNA ...
35-141 1.34e-15

Cgr1 family; Members of this family are coiled-coil proteins that are involved in pre-rRNA processing.


Pssm-ID: 427562 [Multi-domain]  Cd Length: 107  Bit Score: 67.65  E-value: 1.34e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472581581   35 SSTNVSGRWWKTEHKATTRVQsgkKAPQQLDKAWKQREERRKRDEAIKKLERELKQEKEDEADRKKRINLERREKEAEKK 114
Cdd:pfam03879   2 KGMRVSGKPWKAEKKAFRRSS---LVVGPKSKSWEKRQEKRLELKAIKAKEKELKDEKEAERQRRIQAIKERREAKEEKE 78
                          90       100
                  ....*....|....*....|....*..
gi 472581581  115 RLAEMAARMSAKKLQRMKKRLGRSKKV 141
Cdd:pfam03879  79 RYEELAAKMHAKKVERLKRKEKRNKLL 105
PRK00247 PRK00247
putative inner membrane protein translocase component YidC; Validated
43-137 2.47e-05

putative inner membrane protein translocase component YidC; Validated


Pssm-ID: 178945 [Multi-domain]  Cd Length: 429  Bit Score: 42.53  E-value: 2.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472581581  43 WWK----TEHKATTRVQSGKKAPQQLDKAWKQREERRKRDEAI-------------KKLERELKQEKEDEADRKKRINLE 105
Cdd:PRK00247 274 ERKypltDEFKEHHAEQRAQYREKQKEKKAFLWTLRRNRLRMIitpwrapelhaenAEIKKTRTAEKNEAKARKKEIAQK 353
                         90       100       110
                 ....*....|....*....|....*....|....
gi 472581581 106 RR--EKEAEKKRLAEMAARMSAKKLQRMKKRLGR 137
Cdd:PRK00247 354 RRaaEREINREARQERAAAMARARARRAAVKAKK 387
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
71-133 3.21e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 36.37  E-value: 3.21e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 472581581  71 REERRKRDEAIKKLEREL---KQEKEDEADRKKRINLERREKEAEKKRLAE--MAARMSAKKLQRMKK 133
Cdd:COG2433  433 EAELEEKDERIERLERELseaRSEERREIRKDREISRLDREIERLERELEEerERIEELKRKLERLKE 500
 
Name Accession Description Interval E-value
Cgr1 pfam03879
Cgr1 family; Members of this family are coiled-coil proteins that are involved in pre-rRNA ...
35-141 1.34e-15

Cgr1 family; Members of this family are coiled-coil proteins that are involved in pre-rRNA processing.


Pssm-ID: 427562 [Multi-domain]  Cd Length: 107  Bit Score: 67.65  E-value: 1.34e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472581581   35 SSTNVSGRWWKTEHKATTRVQsgkKAPQQLDKAWKQREERRKRDEAIKKLERELKQEKEDEADRKKRINLERREKEAEKK 114
Cdd:pfam03879   2 KGMRVSGKPWKAEKKAFRRSS---LVVGPKSKSWEKRQEKRLELKAIKAKEKELKDEKEAERQRRIQAIKERREAKEEKE 78
                          90       100
                  ....*....|....*....|....*..
gi 472581581  115 RLAEMAARMSAKKLQRMKKRLGRSKKV 141
Cdd:pfam03879  79 RYEELAAKMHAKKVERLKRKEKRNKLL 105
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
75-125 1.69e-05

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 43.22  E-value: 1.69e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 472581581   75 RKRDEAIKKLERELKQEKEDEADRKKRINLErREKEAEKKRLAEMAARMSA 125
Cdd:pfam03154 587 KKREEALEKAKREAEQKAREEKEREKEKEKE-REREREREREAERAAKASS 636
PRK00247 PRK00247
putative inner membrane protein translocase component YidC; Validated
43-137 2.47e-05

putative inner membrane protein translocase component YidC; Validated


Pssm-ID: 178945 [Multi-domain]  Cd Length: 429  Bit Score: 42.53  E-value: 2.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472581581  43 WWK----TEHKATTRVQSGKKAPQQLDKAWKQREERRKRDEAI-------------KKLERELKQEKEDEADRKKRINLE 105
Cdd:PRK00247 274 ERKypltDEFKEHHAEQRAQYREKQKEKKAFLWTLRRNRLRMIitpwrapelhaenAEIKKTRTAEKNEAKARKKEIAQK 353
                         90       100       110
                 ....*....|....*....|....*....|....
gi 472581581 106 RR--EKEAEKKRLAEMAARMSAKKLQRMKKRLGR 137
Cdd:PRK00247 354 RRaaEREINREARQERAAAMARARARRAAVKAKK 387
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
71-133 3.21e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 36.37  E-value: 3.21e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 472581581  71 REERRKRDEAIKKLEREL---KQEKEDEADRKKRINLERREKEAEKKRLAE--MAARMSAKKLQRMKK 133
Cdd:COG2433  433 EAELEEKDERIERLERELseaRSEERREIRKDREISRLDREIERLERELEEerERIEELKRKLERLKE 500
CCDC47 pfam07946
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ...
58-115 3.51e-03

PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of the PAT complex, an endoplasmic reticulum (ER)-resident membrane multiprotein complex that facilitates multi-pass membrane proteins insertion into membranes. The PAT complex, formed by CCDC47 and Asterix proteins, acts as an intramembrane chaperone by directly interacting with nascent transmembrane domains (TMDs), releasing its substrates upon correct folding, and is needed for optimal biogenesis of multi-pass membrane proteins. CCDC47 is required to maintain the stability of Asterix. CCDC47 is associated with various membrane-associated processes and is component of a ribosome-associated ER translocon complex involved in multi-pass membrane protein transport into the ER membrane and biogenesis. It is also involved in the regulation of calcium ion homeostasis in the ER, being also required for proper protein degradation via the ERAD (ER-associated degradation) pathway.


Pssm-ID: 462322  Cd Length: 323  Bit Score: 36.39  E-value: 3.51e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 472581581   58 KKAPQQLDKAWK------QREERRKRDEAIKKLERELKQEKEDEADRKKrinLERREKEAEKKR 115
Cdd:pfam07946 263 KKTREEEIEKIKkaaeeeRAEEAQEKKEEAKKKEREEKLAKLSPEEQRK---YEEKERKKEQRK 323
PTZ00121 PTZ00121
MAEBL; Provisional
45-140 7.03e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 35.50  E-value: 7.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 472581581   45 KTEHKATTRVQSGKKAPQQLDKAWKQREERRKRDEAIKKLERELKQEKEDEADRKKRINLERREKEAEKKRLAEMAARMS 124
Cdd:PTZ00121 1361 AAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKA 1440
                          90
                  ....*....|....*...
gi 472581581  125 --AKKLQRMKKRLGRSKK 140
Cdd:PTZ00121 1441 eeAKKADEAKKKAEEAKK 1458
 
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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