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Conserved domains on  [gi|117676403|ref|NP_008974|]
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KRR1 small subunit processome component homolog [Homo sapiens]

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 5.22e-67

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: 206.65  E-value: 5.22e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117676403 140 VACDIIKIGSLVRNKERFVKRRQRLIGPKGSTLKALELLTNCYIMVQGNTVSAIGPFSGLKEVRKVVLDTMKNIHPIYNI 219
Cdd:cd22394    1 VACDIIKIGNLVRNKERFVKRRQRLIGPNGSTLKAIELLTKCYILVQGNTVSAIGPYKGLKEVRKIVEDCMKNIHPIYNI 80

                         90
                 ....*....|..
gi 117676403 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 1.27e-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: 169.26  E-value: 1.27e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117676403  54 LLEESSFATLFPKYREAYLKECWPLVQKALNEHHVNATLDLIEGSMTVCTTKKTFDPYIIIRARDLIKLLARSVSFEQAV 133
Cdd:cd22393    1 FLEESSFATLFPKYREKYLKEVWPLVTKALKEHGIKCELDLVEGSMTVKTTRKTRDPYIIIKARDLIKLLARSVPFEQAV 80


                 ...
gi 117676403 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 5.22e-67

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: 206.65  E-value: 5.22e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117676403 140 VACDIIKIGSLVRNKERFVKRRQRLIGPKGSTLKALELLTNCYIMVQGNTVSAIGPFSGLKEVRKVVLDTMKNIHPIYNI 219
Cdd:cd22394    1 VACDIIKIGNLVRNKERFVKRRQRLIGPNGSTLKAIELLTKCYILVQGNTVSAIGPYKGLKEVRKIVEDCMKNIHPIYNI 80

                         90
                 ....*....|..
gi 117676403 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 1.27e-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: 169.26  E-value: 1.27e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117676403  54 LLEESSFATLFPKYREAYLKECWPLVQKALNEHHVNATLDLIEGSMTVCTTKKTFDPYIIIRARDLIKLLARSVSFEQAV 133
Cdd:cd22393    1 FLEESSFATLFPKYREKYLKEVWPLVTKALKEHGIKCELDLVEGSMTVKTTRKTRDPYIIIKARDLIKLLARSVPFEQAV 80


                 ...
gi 117676403 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 1.24e-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: 103.97  E-value: 1.24e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117676403   58 SSFATLFPKYREAYLKECWPLVQKALNEHHVNATLDLIEGSMTVCTTKKTFDPYIIIRARDLIKLLARSVSFEQAVRILQ 137
Cdd:pfam17903   1 SSFEILFPKHREQYLKGVEEYIRELLEEKKIKCEVDYDERSIKVSTTEKTRDPYVILKARDFIKLVSRGVPLEEAVKVFE 80


                  .
gi 117676403  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 6.82e-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: 77.60  E-value: 6.82e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117676403   89 NATLDLIEGSMTVCTTKKTFDPYIIIRARDLIKLLARSVSFEQAVRILQDDVACDIIKIGSLVRNKERFVKRRQRLIGPK 168
Cdd:TIGR03665  28 GVKLDIDSETGEVKIEPEDEDPLAVMKAREVVKAIGRGFSPEKALKLLDDDYMLEVIDLKEYGKSPNALRRIKGRIIGEG 107

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 117676403  169 GSTLKALELLTNCYIMVQGNTVSAIGPFSGLKEVRKVV 206
Cdd:TIGR03665 108 GKTRRIIEELTGVSISVYGKTVGIIGDPEQVQIAREAI 145
PRK13763 PRK13763
putative RNA-processing protein; Provisional
 87-206 8.24e-16

putative RNA-processing protein; Provisional


Pssm-ID: 237494 [Multi-domain]  Cd Length: 180  Bit Score: 74.90  E-value: 8.24e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117676403  87 HVNATLDLIEGSMTVcTTKKTFDPYIIIRARDLIKLLARSVSFEQAVRILQDDVACDIIKIGSLVRNKERFVKRRQRLIG 166
Cdd:PRK13763  33 GVKLEIDSETGEVII-EPTDGEDPLAVLKARDIVKAIGRGFSPEKALRLLDDDYVLEVIDLSDYGDSPNALRRIKGRIIG 111

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 117676403 167 PKGSTLKALELLTNCYIMVQGNTVSAIGPFSGLKEVRKVV 206
Cdd:PRK13763 112 EGGKTRRIIEELTGVDISVYGKTVAIIGDPEQVEIAREAI 151
KH smart00322
K homology RNA-binding domain;
158-208 6.58e-05

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 40.74  E-value: 6.58e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 117676403   158 VKRRQRLIGPKGSTLKALELLTNCYIMVQG-----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 5.22e-67

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: 206.65  E-value: 5.22e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117676403 140 VACDIIKIGSLVRNKERFVKRRQRLIGPKGSTLKALELLTNCYIMVQGNTVSAIGPFSGLKEVRKVVLDTMKNIHPIYNI 219
Cdd:cd22394    1 VACDIIKIGNLVRNKERFVKRRQRLIGPNGSTLKAIELLTKCYILVQGNTVSAIGPYKGLKEVRKIVEDCMKNIHPIYNI 80

                         90
                 ....*....|..
gi 117676403 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 1.27e-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: 169.26  E-value: 1.27e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117676403  54 LLEESSFATLFPKYREAYLKECWPLVQKALNEHHVNATLDLIEGSMTVCTTKKTFDPYIIIRARDLIKLLARSVSFEQAV 133
Cdd:cd22393    1 FLEESSFATLFPKYREKYLKEVWPLVTKALKEHGIKCELDLVEGSMTVKTTRKTRDPYIIIKARDLIKLLARSVPFEQAV 80


                 ...
gi 117676403 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 1.24e-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: 103.97  E-value: 1.24e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117676403   58 SSFATLFPKYREAYLKECWPLVQKALNEHHVNATLDLIEGSMTVCTTKKTFDPYIIIRARDLIKLLARSVSFEQAVRILQ 137
Cdd:pfam17903   1 SSFEILFPKHREQYLKGVEEYIRELLEEKKIKCEVDYDERSIKVSTTEKTRDPYVILKARDFIKLVSRGVPLEEAVKVFE 80


                  .
gi 117676403  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 6.82e-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: 77.60  E-value: 6.82e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117676403   89 NATLDLIEGSMTVCTTKKTFDPYIIIRARDLIKLLARSVSFEQAVRILQDDVACDIIKIGSLVRNKERFVKRRQRLIGPK 168
Cdd:TIGR03665  28 GVKLDIDSETGEVKIEPEDEDPLAVMKAREVVKAIGRGFSPEKALKLLDDDYMLEVIDLKEYGKSPNALRRIKGRIIGEG 107

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 117676403  169 GSTLKALELLTNCYIMVQGNTVSAIGPFSGLKEVRKVV 206
Cdd:TIGR03665 108 GKTRRIIEELTGVSISVYGKTVGIIGDPEQVQIAREAI 145
PRK13763 PRK13763
putative RNA-processing protein; Provisional
 87-206 8.24e-16

putative RNA-processing protein; Provisional


Pssm-ID: 237494 [Multi-domain]  Cd Length: 180  Bit Score: 74.90  E-value: 8.24e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117676403  87 HVNATLDLIEGSMTVcTTKKTFDPYIIIRARDLIKLLARSVSFEQAVRILQDDVACDIIKIGSLVRNKERFVKRRQRLIG 166
Cdd:PRK13763  33 GVKLEIDSETGEVII-EPTDGEDPLAVLKARDIVKAIGRGFSPEKALRLLDDDYVLEVIDLSDYGDSPNALRRIKGRIIG 111

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 117676403 167 PKGSTLKALELLTNCYIMVQGNTVSAIGPFSGLKEVRKVV 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 1.39e-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: 63.01  E-value: 1.39e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 117676403 134 RILQDDVACDIIKIGSLV-RNKERFVKRRQRLIGPKGSTLKALELLTNCYIMVQGNTVSAIGPFSGLKEVRKVV 206
Cdd:cd22390    2 LLLDDDYVLEVIDLRDYAgRSKKALRRVKGRVIGSGGKTRRLIEELTGCYISVYGKTVSIIGDFENLQIAKEAI 75
KH smart00322
K homology RNA-binding domain;
158-208 6.58e-05

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 40.74  E-value: 6.58e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 117676403   158 VKRRQRLIGPKGSTLKALELLTNCYIMVQG-----NTVSAIGPFSGLKEVRKVVLD 208
Cdd:smart00322  11 ADKVGLIIGKGGSTIKKIEEETGVKIDIPGpgseeRVVEITGPPENVEKAAELILE 66
KH-I_Hqk_like cd22383
type I K homology (KH) RNA-binding domain found in protein quaking (Hqk) family; The Hqk ...
 163-187 7.32e-04

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: 38.49  E-value: 7.32e-04
                         10        20
                 ....*....|....*....|....*
gi 117676403 163 RLIGPKGSTLKALELLTNCYIMVQG 187
Cdd:cd22383   21 RILGPRGMTAKQLEQDTGCKIMIRG 45
KH-I_Vigilin_rpt4 cd22408
fourth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 158-207 1.56e-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: 36.38  E-value: 1.56e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 117676403 158 VKRRQR--LIGPKGSTLKALELLTNCYIMVQ-----GNTVSAIGPFSGLKEVRKVVL 207
Cdd:cd22408    6 VPKSQHrfVIGPRGSTIQEILEETGCSVEVPpndsdSETITLRGPADKLGAALTLVY 62
KH-I_SF1 cd22382
type I K homology (KH) RNA-binding domain found in splicing factor 1 (SF1) and similar ...
 164-187 3.46e-03

type I K homology (KH) RNA-binding domain found in splicing factor 1 (SF1) and similar proteins; SF1, also called branch point-binding protein, or BBP, or transcription factor ZFM1, or zinc finger gene in MEN1 locus, or zinc finger protein 162, is necessary for the ATP-dependent first step of spliceosome assembly. Binds to the intron branch point sequence (BPS) 5'-UACUAAC-3' of the pre-mRNA. It may act as transcription repressor.


Pssm-ID: 411810 [Multi-domain]  Cd Length: 93  Bit Score: 36.52  E-value: 3.46e-03
                         10        20
                 ....*....|....*....|....
gi 117676403 164 LIGPKGSTLKALELLTNCYIMVQG 187
Cdd:cd22382   22 LIGPRGNTLKKIEKETGAKIMIRG 45
KH-II_Jag cd02414
type II K-homology (KH) RNA-binding domain found in protein Jag and similar proteins; Protein ...
 163-183 7.81e-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: 35.19  E-value: 7.81e-03
                         10        20
                 ....*....|....*....|.
gi 117676403 163 RLIGPKGSTLKALELLTNCYI 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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