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Conserved domains on  [gi|1572616298|ref|NP_659106|]
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ribosomal RNA processing protein 36 homolog isoform 1 [Mus musculus]

Protein Classification

rRNA biogenesis protein RRP36( domain architecture ID 12068757)

rRNA biogenesis protein RRP36 which is involved in the early processing steps of the pre-rRNA and production of the 40S ribosomal subunit

Gene Ontology:  GO:0030490

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RRP36 pfam06102
rRNA biogenesis protein RRP36; RRP36 is involved in the early processing steps of the pre-rRNA.
76-230 3.09e-42

rRNA biogenesis protein RRP36; RRP36 is involved in the early processing steps of the pre-rRNA.


:

Pssm-ID: 461829 [Multi-domain]  Cd Length: 158  Bit Score: 141.16  E-value: 3.09e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616298  76 KHRPLEMSAKVRVPFLRQVVPISKKVARDPRFDDLSGDYNPEVFDKTYQFLNDIRAKEKQLVKKQLKKHRSGEEHDKLQQ 155
Cdd:pfam06102   4 KHAPTEMSSKKPVSRKRQVVEVKKKKSRDPRFDSLSGEFDEDKFRKNYGFLDEYRKKEIEELKKQLKKTKDPEEKEELKR 83
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1572616298 156 LLQRMEQQEMAQQERKQQQELRLALKQERRAQAQQGHRPYFLKKSEQRQLALAEKFKELRRSKKLESFLSRKRRR 230
Cdd:pfam06102  84 TLQSMESRLKAKKRKDREREVLKEHKKEEKEKVKQGKKPFYLKKSEKKKLLLKEKFEELKKSGKLDKAIEKKRKK 158
 
Name Accession Description Interval E-value
RRP36 pfam06102
rRNA biogenesis protein RRP36; RRP36 is involved in the early processing steps of the pre-rRNA.
76-230 3.09e-42

rRNA biogenesis protein RRP36; RRP36 is involved in the early processing steps of the pre-rRNA.


Pssm-ID: 461829 [Multi-domain]  Cd Length: 158  Bit Score: 141.16  E-value: 3.09e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616298  76 KHRPLEMSAKVRVPFLRQVVPISKKVARDPRFDDLSGDYNPEVFDKTYQFLNDIRAKEKQLVKKQLKKHRSGEEHDKLQQ 155
Cdd:pfam06102   4 KHAPTEMSSKKPVSRKRQVVEVKKKKSRDPRFDSLSGEFDEDKFRKNYGFLDEYRKKEIEELKKQLKKTKDPEEKEELKR 83
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1572616298 156 LLQRMEQQEMAQQERKQQQELRLALKQERRAQAQQGHRPYFLKKSEQRQLALAEKFKELRRSKKLESFLSRKRRR 230
Cdd:pfam06102  84 TLQSMESRLKAKKRKDREREVLKEHKKEEKEKVKQGKKPFYLKKSEKKKLLLKEKFEELKKSGKLDKAIEKKRKK 158
HpsJ_fam NF038305
HpsJ family protein; HpsJ (hormogornium polysaccharide J) is thought to be involved in the ...
151-237 5.37e-03

HpsJ family protein; HpsJ (hormogornium polysaccharide J) is thought to be involved in the biosynthesis or secretion of an extracellular polysaccharide shared by many Cyanobacteria.


Pssm-ID: 468465 [Multi-domain]  Cd Length: 230  Bit Score: 37.18  E-value: 5.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616298 151 DKLQQLLQRMEQQEMAQQERKQQ-------QELRLALKQERRaQAQQGHRPyflkKSEQRQLALAEKFKElrRSKKLESF 223
Cdd:NF038305  108 QALQQINQQAGQQETQLQQQLNQlqaqtspQQLNQLLKSEQK-QGQALASG----QLPEEQKEQLQQFKS--NPQALDKF 180
                          90       100
                  ....*....|....*....|
gi 1572616298 224 LS------RKRRRNAGKDRR 237
Cdd:NF038305  181 LAqqltqiRTQAEEAEKQAR 200
 
Name Accession Description Interval E-value
RRP36 pfam06102
rRNA biogenesis protein RRP36; RRP36 is involved in the early processing steps of the pre-rRNA.
76-230 3.09e-42

rRNA biogenesis protein RRP36; RRP36 is involved in the early processing steps of the pre-rRNA.


Pssm-ID: 461829 [Multi-domain]  Cd Length: 158  Bit Score: 141.16  E-value: 3.09e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616298  76 KHRPLEMSAKVRVPFLRQVVPISKKVARDPRFDDLSGDYNPEVFDKTYQFLNDIRAKEKQLVKKQLKKHRSGEEHDKLQQ 155
Cdd:pfam06102   4 KHAPTEMSSKKPVSRKRQVVEVKKKKSRDPRFDSLSGEFDEDKFRKNYGFLDEYRKKEIEELKKQLKKTKDPEEKEELKR 83
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1572616298 156 LLQRMEQQEMAQQERKQQQELRLALKQERRAQAQQGHRPYFLKKSEQRQLALAEKFKELRRSKKLESFLSRKRRR 230
Cdd:pfam06102  84 TLQSMESRLKAKKRKDREREVLKEHKKEEKEKVKQGKKPFYLKKSEKKKLLLKEKFEELKKSGKLDKAIEKKRKK 158
HpsJ_fam NF038305
HpsJ family protein; HpsJ (hormogornium polysaccharide J) is thought to be involved in the ...
151-237 5.37e-03

HpsJ family protein; HpsJ (hormogornium polysaccharide J) is thought to be involved in the biosynthesis or secretion of an extracellular polysaccharide shared by many Cyanobacteria.


Pssm-ID: 468465 [Multi-domain]  Cd Length: 230  Bit Score: 37.18  E-value: 5.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1572616298 151 DKLQQLLQRMEQQEMAQQERKQQ-------QELRLALKQERRaQAQQGHRPyflkKSEQRQLALAEKFKElrRSKKLESF 223
Cdd:NF038305  108 QALQQINQQAGQQETQLQQQLNQlqaqtspQQLNQLLKSEQK-QGQALASG----QLPEEQKEQLQQFKS--NPQALDKF 180
                          90       100
                  ....*....|....*....|
gi 1572616298 224 LS------RKRRRNAGKDRR 237
Cdd:NF038305  181 LAqqltqiRTQAEEAEKQAR 200
 
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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