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Conserved domains on  [gi|1777349951|ref|XP_009179500|]
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KRR1 small subunit processome component homolog isoform X1 [Papio anubis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KH-I_KRR1_rpt2 cd22394
second type I K homology (KH) RNA-binding domain found in KRR1 small subunit processome ...
 140-231 1.61e-66

second type I K homology (KH) RNA-binding domain found in KRR1 small subunit processome component and similar proteins; KRR1, also called HIV-1 Rev-binding protein 2, or KRR-R motif-containing protein 1, or Rev-interacting protein 1, or Rip-1, or ribosomal RNA assembly protein KRR1, is a nucleolar protein required for 40S ribosome biogenesis. It is involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly. KRR1 contains two K-homology (KH) RNA-binding domains. The model corresponds to the second one.


:

Pssm-ID: 411822  Cd Length: 93  Bit Score: 205.49  E-value: 1.61e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777349951 140 VACDIIKIGSLVRNKERFVKRRQRLIGPKGSTLKALELLTNCYVMVQGNTVSAIGPFSGLKEVRKVVLDTMKNIHPIYNI 219
Cdd:cd22394     1 VACDIIKIGNLVRNKERFVKRRQRLIGPNGSTLKAIELLTKCYILVQGNTVSAIGPYKGLKEVRKIVEDCMKNIHPIYNI 80

                          90
                  ....*....|..
gi 1777349951 220 KSLMIKRELAKD 231
Cdd:cd22394    81 KTLMIKRELEKD 92
KH-I_KRR1_rpt1 cd22393
first type I K homology (KH) RNA-binding domain found in KRR1 small subunit processome ...
 54-136 1.09e-52

first type I K homology (KH) RNA-binding domain found in KRR1 small subunit processome component and similar proteins; KRR1, also called HIV-1 Rev-binding protein 2, or KRR-R motif-containing protein 1, or Rev-interacting protein 1, or Rip-1, or ribosomal RNA assembly protein KRR1, is a ribosomal assembly factor required for 40S ribosome biogenesis. It is involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly. KRR1 contains two K-homology (KH) RNA-binding domains. The model corresponds to the first one. The KH1 domain is a divergent KH domain that lacks the RNA-binding GXXG motif and is involved in binding another assembly factor, Kri1.


:

Pssm-ID: 411821  Cd Length: 83  Bit Score: 169.64  E-value: 1.09e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777349951  54 LLEESSFSTLFPKYREAYLKECWPLVQKALNEHHVNATLDLIEGSMTVRTTKKTFDPYIIIRARDLIKLLARSVSFEQAV 133
Cdd:cd22393     1 FLEESSFATLFPKYREKYLKEVWPLVTKALKEHGIKCELDLVEGSMTVKTTRKTRDPYIIIKARDLIKLLARSVPFEQAV 80


                  ...
gi 1777349951 134 RIL 136
Cdd:cd22393    81 KIL 83
 
Name Accession Description Interval E-value
KH-I_KRR1_rpt2 cd22394
second type I K homology (KH) RNA-binding domain found in KRR1 small subunit processome ...
 140-231 1.61e-66

second type I K homology (KH) RNA-binding domain found in KRR1 small subunit processome component and similar proteins; KRR1, also called HIV-1 Rev-binding protein 2, or KRR-R motif-containing protein 1, or Rev-interacting protein 1, or Rip-1, or ribosomal RNA assembly protein KRR1, is a nucleolar protein required for 40S ribosome biogenesis. It is involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly. KRR1 contains two K-homology (KH) RNA-binding domains. The model corresponds to the second one.


Pssm-ID: 411822  Cd Length: 93  Bit Score: 205.49  E-value: 1.61e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777349951 140 VACDIIKIGSLVRNKERFVKRRQRLIGPKGSTLKALELLTNCYVMVQGNTVSAIGPFSGLKEVRKVVLDTMKNIHPIYNI 219
Cdd:cd22394     1 VACDIIKIGNLVRNKERFVKRRQRLIGPNGSTLKAIELLTKCYILVQGNTVSAIGPYKGLKEVRKIVEDCMKNIHPIYNI 80

                          90
                  ....*....|..
gi 1777349951 220 KSLMIKRELAKD 231
Cdd:cd22394    81 KTLMIKRELEKD 92
KH-I_KRR1_rpt1 cd22393
first type I K homology (KH) RNA-binding domain found in KRR1 small subunit processome ...
 54-136 1.09e-52

first type I K homology (KH) RNA-binding domain found in KRR1 small subunit processome component and similar proteins; KRR1, also called HIV-1 Rev-binding protein 2, or KRR-R motif-containing protein 1, or Rev-interacting protein 1, or Rip-1, or ribosomal RNA assembly protein KRR1, is a ribosomal assembly factor required for 40S ribosome biogenesis. It is involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly. KRR1 contains two K-homology (KH) RNA-binding domains. The model corresponds to the first one. The KH1 domain is a divergent KH domain that lacks the RNA-binding GXXG motif and is involved in binding another assembly factor, Kri1.


Pssm-ID: 411821  Cd Length: 83  Bit Score: 169.64  E-value: 1.09e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777349951  54 LLEESSFSTLFPKYREAYLKECWPLVQKALNEHHVNATLDLIEGSMTVRTTKKTFDPYIIIRARDLIKLLARSVSFEQAV 133
Cdd:cd22393     1 FLEESSFATLFPKYREKYLKEVWPLVTKALKEHGIKCELDLVEGSMTVKTTRKTRDPYIIIKARDLIKLLARSVPFEQAV 80


                  ...
gi 1777349951 134 RIL 136
Cdd:cd22393    81 KIL 83
KH_8 pfam17903
Krr1 KH1 domain; This entry represents the first KH domain in the KRR1 protein. Krr1 is a ...
 58-138 1.04e-27

Krr1 KH1 domain; This entry represents the first KH domain in the KRR1 protein. Krr1 is a ribosomal assembly factor. The KH1 domain is a divergent KH domain that lacks the RNA-binding GXXG motif and is involved in binding another assembly factor, Kri1.


Pssm-ID: 407755  Cd Length: 81  Bit Score: 104.36  E-value: 1.04e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777349951  58 SSFSTLFPKYREAYLKECWPLVQKALNEHHVNATLDLIEGSMTVRTTKKTFDPYIIIRARDLIKLLARSVSFEQAVRILQ 137
Cdd:pfam17903   1 SSFEILFPKHREQYLKGVEEYIRELLEEKKIKCEVDYDERSIKVSTTEKTRDPYVILKARDFIKLVSRGVPLEEAVKVFE 80


                  .
gi 1777349951 138 D 138
Cdd:pfam17903  81 D 81
arCOG04150 TIGR03665
arCOG04150 universal archaeal KH domain protein; This family of proteins is universal among ...
 89-206 4.59e-17

arCOG04150 universal archaeal KH domain protein; This family of proteins is universal among the 41 archaeal genomes analyzed, and is not observed outside of the archaea. The proteins contain a single KH domain (pfam00013) which is likely to confer the ability to bind RNA.


Pssm-ID: 274711 [Multi-domain]  Cd Length: 172  Bit Score: 77.99  E-value: 4.59e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777349951  89 NATLDLIEGSMTVRTTKKTFDPYIIIRARDLIKLLARSVSFEQAVRILQDDVACDIIKIGSLVRNKERFVKRRQRLIGPK 168
Cdd:TIGR03665  28 GVKLDIDSETGEVKIEPEDEDPLAVMKAREVVKAIGRGFSPEKALKLLDDDYMLEVIDLKEYGKSPNALRRIKGRIIGEG 107

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1777349951 169 GSTLKALELLTNCYVMVQGNTVSAIGPFSGLKEVRKVV 206
Cdd:TIGR03665 108 GKTRRIIEELTGVSISVYGKTVGIIGDPEQVQIAREAI 145
PRK13763 PRK13763
putative RNA-processing protein; Provisional
 87-206 2.07e-15

putative RNA-processing protein; Provisional


Pssm-ID: 237494 [Multi-domain]  Cd Length: 180  Bit Score: 73.75  E-value: 2.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777349951  87 HVNATLDLIEGSMTVrTTKKTFDPYIIIRARDLIKLLARSVSFEQAVRILQDDVACDIIKIGSLVRNKERFVKRRQRLIG 166
Cdd:PRK13763   33 GVKLEIDSETGEVII-EPTDGEDPLAVLKARDIVKAIGRGFSPEKALRLLDDDYVLEVIDLSDYGDSPNALRRIKGRIIG 111

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1777349951 167 PKGSTLKALELLTNCYVMVQGNTVSAIGPFSGLKEVRKVV 206
Cdd:PRK13763  112 EGGKTRRIIEELTGVDISVYGKTVAIIGDPEQVEIAREAI 151
KH smart00322
K homology RNA-binding domain;
158-208 2.38e-04

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 39.20  E-value: 2.38e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1777349951  158 VKRRQRLIGPKGSTLKALELLTNCYVMVQG-----NTVSAIGPFSGLKEVRKVVLD 208
Cdd:smart00322  11 ADKVGLIIGKGGSTIKKIEEETGVKIDIPGpgseeRVVEITGPPENVEKAAELILE 66
 
Name Accession Description Interval E-value
KH-I_KRR1_rpt2 cd22394
second type I K homology (KH) RNA-binding domain found in KRR1 small subunit processome ...
 140-231 1.61e-66

second type I K homology (KH) RNA-binding domain found in KRR1 small subunit processome component and similar proteins; KRR1, also called HIV-1 Rev-binding protein 2, or KRR-R motif-containing protein 1, or Rev-interacting protein 1, or Rip-1, or ribosomal RNA assembly protein KRR1, is a nucleolar protein required for 40S ribosome biogenesis. It is involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly. KRR1 contains two K-homology (KH) RNA-binding domains. The model corresponds to the second one.


Pssm-ID: 411822  Cd Length: 93  Bit Score: 205.49  E-value: 1.61e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777349951 140 VACDIIKIGSLVRNKERFVKRRQRLIGPKGSTLKALELLTNCYVMVQGNTVSAIGPFSGLKEVRKVVLDTMKNIHPIYNI 219
Cdd:cd22394     1 VACDIIKIGNLVRNKERFVKRRQRLIGPNGSTLKAIELLTKCYILVQGNTVSAIGPYKGLKEVRKIVEDCMKNIHPIYNI 80

                          90
                  ....*....|..
gi 1777349951 220 KSLMIKRELAKD 231
Cdd:cd22394    81 KTLMIKRELEKD 92
KH-I_KRR1_rpt1 cd22393
first type I K homology (KH) RNA-binding domain found in KRR1 small subunit processome ...
 54-136 1.09e-52

first type I K homology (KH) RNA-binding domain found in KRR1 small subunit processome component and similar proteins; KRR1, also called HIV-1 Rev-binding protein 2, or KRR-R motif-containing protein 1, or Rev-interacting protein 1, or Rip-1, or ribosomal RNA assembly protein KRR1, is a ribosomal assembly factor required for 40S ribosome biogenesis. It is involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly. KRR1 contains two K-homology (KH) RNA-binding domains. The model corresponds to the first one. The KH1 domain is a divergent KH domain that lacks the RNA-binding GXXG motif and is involved in binding another assembly factor, Kri1.


Pssm-ID: 411821  Cd Length: 83  Bit Score: 169.64  E-value: 1.09e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777349951  54 LLEESSFSTLFPKYREAYLKECWPLVQKALNEHHVNATLDLIEGSMTVRTTKKTFDPYIIIRARDLIKLLARSVSFEQAV 133
Cdd:cd22393     1 FLEESSFATLFPKYREKYLKEVWPLVTKALKEHGIKCELDLVEGSMTVKTTRKTRDPYIIIKARDLIKLLARSVPFEQAV 80


                  ...
gi 1777349951 134 RIL 136
Cdd:cd22393    81 KIL 83
KH_8 pfam17903
Krr1 KH1 domain; This entry represents the first KH domain in the KRR1 protein. Krr1 is a ...
 58-138 1.04e-27

Krr1 KH1 domain; This entry represents the first KH domain in the KRR1 protein. Krr1 is a ribosomal assembly factor. The KH1 domain is a divergent KH domain that lacks the RNA-binding GXXG motif and is involved in binding another assembly factor, Kri1.


Pssm-ID: 407755  Cd Length: 81  Bit Score: 104.36  E-value: 1.04e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777349951  58 SSFSTLFPKYREAYLKECWPLVQKALNEHHVNATLDLIEGSMTVRTTKKTFDPYIIIRARDLIKLLARSVSFEQAVRILQ 137
Cdd:pfam17903   1 SSFEILFPKHREQYLKGVEEYIRELLEEKKIKCEVDYDERSIKVSTTEKTRDPYVILKARDFIKLVSRGVPLEEAVKVFE 80


                  .
gi 1777349951 138 D 138
Cdd:pfam17903  81 D 81
arCOG04150 TIGR03665
arCOG04150 universal archaeal KH domain protein; This family of proteins is universal among ...
 89-206 4.59e-17

arCOG04150 universal archaeal KH domain protein; This family of proteins is universal among the 41 archaeal genomes analyzed, and is not observed outside of the archaea. The proteins contain a single KH domain (pfam00013) which is likely to confer the ability to bind RNA.


Pssm-ID: 274711 [Multi-domain]  Cd Length: 172  Bit Score: 77.99  E-value: 4.59e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777349951  89 NATLDLIEGSMTVRTTKKTFDPYIIIRARDLIKLLARSVSFEQAVRILQDDVACDIIKIGSLVRNKERFVKRRQRLIGPK 168
Cdd:TIGR03665  28 GVKLDIDSETGEVKIEPEDEDPLAVMKAREVVKAIGRGFSPEKALKLLDDDYMLEVIDLKEYGKSPNALRRIKGRIIGEG 107

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1777349951 169 GSTLKALELLTNCYVMVQGNTVSAIGPFSGLKEVRKVV 206
Cdd:TIGR03665 108 GKTRRIIEELTGVSISVYGKTVGIIGDPEQVQIAREAI 145
PRK13763 PRK13763
putative RNA-processing protein; Provisional
 87-206 2.07e-15

putative RNA-processing protein; Provisional


Pssm-ID: 237494 [Multi-domain]  Cd Length: 180  Bit Score: 73.75  E-value: 2.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777349951  87 HVNATLDLIEGSMTVrTTKKTFDPYIIIRARDLIKLLARSVSFEQAVRILQDDVACDIIKIGSLVRNKERFVKRRQRLIG 166
Cdd:PRK13763   33 GVKLEIDSETGEVII-EPTDGEDPLAVLKARDIVKAIGRGFSPEKALRLLDDDYVLEVIDLSDYGDSPNALRRIKGRIIG 111

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1777349951 167 PKGSTLKALELLTNCYVMVQGNTVSAIGPFSGLKEVRKVV 206
Cdd:PRK13763  112 EGGKTRRIIEELTGVDISVYGKTVAIIGDPEQVEIAREAI 151
KH-I_Dim2p_like_rpt2 cd22390
second type I K homology (KH) RNA-binding domain found in Pyrococcus horikoshii Dim2p and ...
 134-206 4.93e-12

second type I K homology (KH) RNA-binding domain found in Pyrococcus horikoshii Dim2p and similar proteins; The family includes a group of conserved KH domain-containing protein mainly from archaea, such as Dim2p homologues from Pyrococcus horikoshii and Aeropyrum pernix. Dim2p acts as a preribosomal RNA processing factor that has been identified as an essential protein for the maturation of 40S ribosomal subunit in Saccharomyces cerevisiae. It is required for the cleavage at processing site A2 to generate the pre-20S rRNA and for the dimethylation of the 18S rRNA by 18S rRNA dimethyltransferase, Dim1p. Dim2p contains two K-homology (KH) RNA-binding domains. The model corresponds to the second one.


Pssm-ID: 411818  Cd Length: 96  Bit Score: 61.47  E-value: 4.93e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1777349951 134 RILQDDVACDIIKIGSLV-RNKERFVKRRQRLIGPKGSTLKALELLTNCYVMVQGNTVSAIGPFSGLKEVRKVV 206
Cdd:cd22390     2 LLLDDDYVLEVIDLRDYAgRSKKALRRVKGRVIGSGGKTRRLIEELTGCYISVYGKTVSIIGDFENLQIAKEAI 75
KH smart00322
K homology RNA-binding domain;
158-208 2.38e-04

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 39.20  E-value: 2.38e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1777349951  158 VKRRQRLIGPKGSTLKALELLTNCYVMVQG-----NTVSAIGPFSGLKEVRKVVLD 208
Cdd:smart00322  11 ADKVGLIIGKGGSTIKKIEEETGVKIDIPGpgseeRVVEITGPPENVEKAAELILE 66
KH-I_Vigilin_rpt4 cd22408
fourth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 158-207 1.33e-03

fourth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; Vigilin, also called high density lipoprotein-binding protein, or HDL-binding protein, is a ubiquitous and highly conserved RNA-binding protein that shuttles between nucleus and cytoplasm presumably in contact with RNA molecules. It may be involved in chromosome partitioning at mitosis, facilitating translation and tRNA transport, and control of mRNA metabolism, including estrogen-mediated stabilization of vitellogenin mRNA. Vigilin is up-regulated by cholesterol loading of cells and functions to protect cells from over-accumulation of cholesterol. It may play a role in cell sterol metabolism. Disruption of human vigilin impairs chromosome condensation and segregation. Vigilin has a unique structure of 14-15 consecutively arranged, but non-identical K-homology (KH) domains which apparently mediate RNA-protein binding. The model corresponds to the fourth one.


Pssm-ID: 411836 [Multi-domain]  Cd Length: 62  Bit Score: 36.76  E-value: 1.33e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1777349951 158 VKRRQR--LIGPKGSTLKALELLTNCYVMVQ-----GNTVSAIGPFSGLKEVRKVVL 207
Cdd:cd22408     6 VPKSQHrfVIGPRGSTIQEILEETGCSVEVPpndsdSETITLRGPADKLGAALTLVY 62
KH-I_Hqk_like cd22383
type I K homology (KH) RNA-binding domain found in protein quaking (Hqk) family; The Hqk ...
 163-187 1.37e-03

type I K homology (KH) RNA-binding domain found in protein quaking (Hqk) family; The Hqk family includes Hqk and protein held out wings (how) found in Drosophila. Hqk, also called HqkI, is an RNA-binding protein that plays a central role in myelinization. It binds to the 5'-NACUAAY-N(1,20)-UAAY-3' RNA core sequence and regulates target mRNA stability. It acts by regulating pre-mRNA splicing, mRNA export and protein translation. Hqk is a regulator of oligodendrocyte differentiation and maturation in the brain that may play a role in myelin and oligodendrocyte dysfunction in schizophrenia. How, also called KH domain protein KH93F, or protein muscle-specific, or protein Struthio, or protein wings held out (who), or Quaking-related 93F (qkr93F), is an RNA-binding protein involved in the control of muscular and cardiac activity. It is required for integrin-mediated cell-adhesion in wing blade. It plays essential roles during embryogenesis, in late stages of somatic muscle development, for myotube migration and during metamorphosis for muscle reorganization.


Pssm-ID: 411811 [Multi-domain]  Cd Length: 101  Bit Score: 37.72  E-value: 1.37e-03
                          10        20
                  ....*....|....*....|....*
gi 1777349951 163 RLIGPKGSTLKALELLTNCYVMVQG 187
Cdd:cd22383    21 RILGPRGMTAKQLEQDTGCKIMIRG 45
KH-II_Jag cd02414
type II K-homology (KH) RNA-binding domain found in protein Jag and similar proteins; Protein ...
 163-183 4.73e-03

type II K-homology (KH) RNA-binding domain found in protein Jag and similar proteins; Protein Jag, also called SpoIIIJ-associated protein, is associated with SpoIIIJ and is necessary for the third stage of sporulation. Members of this family are mainly from bacteria and contain only one canonical type II K-homology (KH) domain that has the signature motif GXXG (where X represents any amino acid).


Pssm-ID: 411785  Cd Length: 79  Bit Score: 35.58  E-value: 4.73e-03
                          10        20
                  ....*....|....*....|.
gi 1777349951 163 RLIGPKGSTLKALELLTNCYV 183
Cdd:cd02414    39 LLIGKHGETLDALQYLANLVL 59
 
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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