NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|29351673|gb|AAH49283|]
View 

Pnpt1 protein, partial [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
PRK11824 super family cl36064
polynucleotide phosphorylase/polyadenylase; Provisional
 1-204 3.14e-48

polynucleotide phosphorylase/polyadenylase; Provisional


The actual alignment was detected with superfamily member PRK11824:

Pssm-ID: 236995 [Multi-domain]  Cd Length: 693  Bit Score: 168.30  E-value: 3.14e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29351673    1 GTNKGITALQADIKLPGVPIKIIMEAIQQASVAKKEILQIMNKTISKPRASRKENGPVVETVKVPLSKRAKFVGPGGYHL 80
Cdd:PRK11824 497 GTRDGITALQMDIKIDGITREILEEALEQAKEGRLHILGKMNEAISEPRAELSPYAPRIETIKIPPDKIRDVIGPGGKTI 576

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29351673   81 KKLQAETGVTISQVDEETFSIFAPTPTAMHEARDFITEICRDdqeqqLEFGAVYTATITEIRDTGVMVKLYPNmTAVLLH 160
Cdd:PRK11824 577 REITEETGAKIDIEDDGTVKIAATDGEAAEAAKERIEGITAE-----PEVGEIYEGKVVRIVDFGAFVEILPG-KDGLVH 650

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 29351673  161 NSQLDQRKIKHPTALgLEVGQEIQVKYFGRDPaDGRMRLSRKVL 204
Cdd:PRK11824 651 ISEIADERVEKVEDV-LKEGDEVKVKVLEIDK-RGRIRLSRKAV 692
 
Name Accession Description Interval E-value
PRK11824 PRK11824
polynucleotide phosphorylase/polyadenylase; Provisional
 1-204 3.14e-48

polynucleotide phosphorylase/polyadenylase; Provisional


Pssm-ID: 236995 [Multi-domain]  Cd Length: 693  Bit Score: 168.30  E-value: 3.14e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29351673    1 GTNKGITALQADIKLPGVPIKIIMEAIQQASVAKKEILQIMNKTISKPRASRKENGPVVETVKVPLSKRAKFVGPGGYHL 80
Cdd:PRK11824 497 GTRDGITALQMDIKIDGITREILEEALEQAKEGRLHILGKMNEAISEPRAELSPYAPRIETIKIPPDKIRDVIGPGGKTI 576

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29351673   81 KKLQAETGVTISQVDEETFSIFAPTPTAMHEARDFITEICRDdqeqqLEFGAVYTATITEIRDTGVMVKLYPNmTAVLLH 160
Cdd:PRK11824 577 REITEETGAKIDIEDDGTVKIAATDGEAAEAAKERIEGITAE-----PEVGEIYEGKVVRIVDFGAFVEILPG-KDGLVH 650

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 29351673  161 NSQLDQRKIKHPTALgLEVGQEIQVKYFGRDPaDGRMRLSRKVL 204
Cdd:PRK11824 651 ISEIADERVEKVEDV-LKEGDEVKVKVLEIDK-RGRIRLSRKAV 692
Pnp COG1185
Polyribonucleotide nucleotidyltransferase (polynucleotide phosphorylase) [Translation, ...
 1-203 2.79e-46

Polyribonucleotide nucleotidyltransferase (polynucleotide phosphorylase) [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440798 [Multi-domain]  Cd Length: 686  Bit Score: 162.87  E-value: 2.79e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29351673   1 GTNKGITALQADIKLPGVPIKIIMEAIQQASVAKKEILQIMNKTISKPRASRKENGPVVETVKVPLSKRAKFVGPGGYHL 80
Cdd:COG1185 492 GTRDGITALQMDIKIDGITREILEEALEQAKEGRLHILDKMLEAISEPREELSPYAPRIITIKIPPDKIRDVIGPGGKVI 571

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29351673  81 KKLQAETGVTISQVDEETFSIFAPTPTAMHEARDFITEICRDdqeqqLEFGAVYTATITEIRDTGVMVKLYPNMTAvLLH 160
Cdd:COG1185 572 RKIIEETGAKIDIEDDGTVKIAATDGEAAEKAIERIEGITAE-----PEVGEIYEGKVVRIMDFGAFVEILPGKDG-LVH 645

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 29351673 161 NSQLDQRKIKHPTALgLEVGQEIQVKYFGRDPaDGRMRLSRKV 203
Cdd:COG1185 646 ISELADERVEKVEDV-LKEGDEVKVKVLEIDD-QGRIKLSRKA 686
KH-I_PNPT1 cd09033
type I K homology (KH) RNA-binding domain found in mitochondrial polyribonucleotide ...
 53-119 1.27e-40

type I K homology (KH) RNA-binding domain found in mitochondrial polyribonucleotide nucleotidyltransferase 1 (PNPT1) and similar proteins; PNPT1, also called 3'-5' RNA exonuclease OLD35, or PNPase old-35, or polynucleotide phosphorylase 1, or PNPase 1, or polynucleotide phosphorylase-like protein, is an RNA-binding protein implicated in numerous RNA metabolic processes. It catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'-to-5' direction. It acts as a mitochondrial intermembrane factor with RNA-processing exoribonulease activity. PNPT1 is a component of the mitochondrial degradosome (mtEXO) complex, that degrades 3' overhang double-stranded RNA with a 3'-to-5' directionality in an ATP-dependent manner. It is involved in the degradation of non-coding mitochondrial transcripts (MT-ncRNA) and tRNA-like molecules and required for correct processing and polyadenylation of mitochondrial mRNAs. PNPT1 also plays a role as a cytoplasmic RNA import factor that mediates the translocation of small RNA components, like the 5S RNA, the RNA subunit of ribonuclease P and the mitochondrial RNA-processing (MRP) RNA, into the mitochondrial matrix.


Pssm-ID: 411809 [Multi-domain]  Cd Length: 67  Bit Score: 133.47  E-value: 1.27e-40
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 29351673  53 KENGPVVETVKVPLSKRAKFVGPGGYHLKKLQAETGVTISQVDEETFSIFAPTPTAMHEARDFITEI 119
Cdd:cd09033   1 KENGPVTETLEVPPSKRAKFVGPGGYNIKKLQAETGVTITQVDEETFSVFAPNQSAMDEAKEMIEEL 67
S1 pfam00575
S1 RNA binding domain; The S1 domain occurs in a wide range of RNA associated proteins. It is ...
 131-201 2.86e-05

S1 RNA binding domain; The S1 domain occurs in a wide range of RNA associated proteins. It is structurally similar to cold shock protein which binds nucleic acids. The S1 domain has an OB-fold structure.


Pssm-ID: 425760 [Multi-domain]  Cd Length: 72  Bit Score: 41.12  E-value: 2.86e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 29351673   131 GAVYTATITEIRDTGVMVKLYPNMTAvLLHNSQLDQRKIKHPTaLGLEVGQEIQVKYFGRDPADGRMRLSR 201
Cdd:pfam00575   4 GDVVEGEVTRVTKGGAFVDLGNGVEG-FIPISELSDDHVEDPD-EVIKVGDEVKVKVLKVDKDRRRIILSI 72
rpsA TIGR00717
ribosomal protein S1; This model describes ribosomal protein S1, RpsA. This protein is found ...
 131-202 4.60e-05

ribosomal protein S1; This model describes ribosomal protein S1, RpsA. This protein is found in most bacterial genomes in a single copy, but is not present in the Mycoplasmas. It is heterogeneous with respect to the number of repeats of the S1 RNA binding domain described by pfam00575: six repeats in E. coli and most other bacteria, four in Bacillus subtilis and some other species. rpsA is an essential gene in E. coli but not in B. subtilis. It is associated with the cytidylate kinase gene cmk in many species, and fused to it in Treponema pallidum. RpsA is proposed (Medline:97323001) to assist in mRNA degradation. This model provides trusted hits to most long form (6 repeat) examples of RpsA. Among homologs with only four repeats are some to which other (perhaps secondary) functions have been assigned. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 273232 [Multi-domain]  Cd Length: 516  Bit Score: 43.95  E-value: 4.60e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 29351673   131 GAVYTATITEIRDTGVMVKLyPNMTAVLLHNSQLDQRKIKHPTaLGLEVGQEIQVKYFGRDPADGRMRLSRK 202
Cdd:TIGR00717 447 GSVVKGKVTEIKDFGAFVEL-PGGVEGLIRNSELSENRDEDKT-DEIKVGDEVEAKVVDIDKKNRKVSLSVK 516
KH smart00322
K homology RNA-binding domain;
57-119 5.64e-05

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 39.97  E-value: 5.64e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 29351673     57 PVVETVKVPLSKRAKFVGPGGYHLKKLQAETGVTI----SQVDEETFSIFAPtPTAMHEARDFITEI 119
Cdd:smart00322   2 PVTIEVLIPADKVGLIIGKGGSTIKKIEEETGVKIdipgPGSEERVVEITGP-PENVEKAAELILEI 67
 
Name Accession Description Interval E-value
PRK11824 PRK11824
polynucleotide phosphorylase/polyadenylase; Provisional
 1-204 3.14e-48

polynucleotide phosphorylase/polyadenylase; Provisional


Pssm-ID: 236995 [Multi-domain]  Cd Length: 693  Bit Score: 168.30  E-value: 3.14e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29351673    1 GTNKGITALQADIKLPGVPIKIIMEAIQQASVAKKEILQIMNKTISKPRASRKENGPVVETVKVPLSKRAKFVGPGGYHL 80
Cdd:PRK11824 497 GTRDGITALQMDIKIDGITREILEEALEQAKEGRLHILGKMNEAISEPRAELSPYAPRIETIKIPPDKIRDVIGPGGKTI 576

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29351673   81 KKLQAETGVTISQVDEETFSIFAPTPTAMHEARDFITEICRDdqeqqLEFGAVYTATITEIRDTGVMVKLYPNmTAVLLH 160
Cdd:PRK11824 577 REITEETGAKIDIEDDGTVKIAATDGEAAEAAKERIEGITAE-----PEVGEIYEGKVVRIVDFGAFVEILPG-KDGLVH 650

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 29351673  161 NSQLDQRKIKHPTALgLEVGQEIQVKYFGRDPaDGRMRLSRKVL 204
Cdd:PRK11824 651 ISEIADERVEKVEDV-LKEGDEVKVKVLEIDK-RGRIRLSRKAV 692
Pnp COG1185
Polyribonucleotide nucleotidyltransferase (polynucleotide phosphorylase) [Translation, ...
 1-203 2.79e-46

Polyribonucleotide nucleotidyltransferase (polynucleotide phosphorylase) [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440798 [Multi-domain]  Cd Length: 686  Bit Score: 162.87  E-value: 2.79e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29351673   1 GTNKGITALQADIKLPGVPIKIIMEAIQQASVAKKEILQIMNKTISKPRASRKENGPVVETVKVPLSKRAKFVGPGGYHL 80
Cdd:COG1185 492 GTRDGITALQMDIKIDGITREILEEALEQAKEGRLHILDKMLEAISEPREELSPYAPRIITIKIPPDKIRDVIGPGGKVI 571

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29351673  81 KKLQAETGVTISQVDEETFSIFAPTPTAMHEARDFITEICRDdqeqqLEFGAVYTATITEIRDTGVMVKLYPNMTAvLLH 160
Cdd:COG1185 572 RKIIEETGAKIDIEDDGTVKIAATDGEAAEKAIERIEGITAE-----PEVGEIYEGKVVRIMDFGAFVEILPGKDG-LVH 645

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 29351673 161 NSQLDQRKIKHPTALgLEVGQEIQVKYFGRDPaDGRMRLSRKV 203
Cdd:COG1185 646 ISELADERVEKVEDV-LKEGDEVKVKVLEIDD-QGRIKLSRKA 686
KH-I_PNPT1 cd09033
type I K homology (KH) RNA-binding domain found in mitochondrial polyribonucleotide ...
 53-119 1.27e-40

type I K homology (KH) RNA-binding domain found in mitochondrial polyribonucleotide nucleotidyltransferase 1 (PNPT1) and similar proteins; PNPT1, also called 3'-5' RNA exonuclease OLD35, or PNPase old-35, or polynucleotide phosphorylase 1, or PNPase 1, or polynucleotide phosphorylase-like protein, is an RNA-binding protein implicated in numerous RNA metabolic processes. It catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'-to-5' direction. It acts as a mitochondrial intermembrane factor with RNA-processing exoribonulease activity. PNPT1 is a component of the mitochondrial degradosome (mtEXO) complex, that degrades 3' overhang double-stranded RNA with a 3'-to-5' directionality in an ATP-dependent manner. It is involved in the degradation of non-coding mitochondrial transcripts (MT-ncRNA) and tRNA-like molecules and required for correct processing and polyadenylation of mitochondrial mRNAs. PNPT1 also plays a role as a cytoplasmic RNA import factor that mediates the translocation of small RNA components, like the 5S RNA, the RNA subunit of ribonuclease P and the mitochondrial RNA-processing (MRP) RNA, into the mitochondrial matrix.


Pssm-ID: 411809 [Multi-domain]  Cd Length: 67  Bit Score: 133.47  E-value: 1.27e-40
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 29351673  53 KENGPVVETVKVPLSKRAKFVGPGGYHLKKLQAETGVTISQVDEETFSIFAPTPTAMHEARDFITEI 119
Cdd:cd09033   1 KENGPVTETLEVPPSKRAKFVGPGGYNIKKLQAETGVTITQVDEETFSVFAPNQSAMDEAKEMIEEL 67
RNase_PH_PNPase_2 cd11364
Polyribonucleotide nucleotidyltransferase, repeat 2; Polyribonucleotide nucleotidyltransferase ...
 1-48 2.28e-20

Polyribonucleotide nucleotidyltransferase, repeat 2; Polyribonucleotide nucleotidyltransferase (PNPase) is a member of the RNase_PH family, named after the bacterial Ribonuclease PH, a 3'-5' exoribonuclease. Structurally, all members of this family form hexameric rings. In the case of PNPase the complex is a trimer, since each monomer contains two tandem copies of the domain. PNPase is involved in mRNA degradation in a 3'-5' direction and in quality control of ribosomal RNA precursors, with the second repeat containing the active site. PNPase is part of the RNA degradosome complex and binds to the scaffolding domain of the endoribonuclease RNase E.


Pssm-ID: 206769 [Multi-domain]  Cd Length: 223  Bit Score: 85.68  E-value: 2.28e-20
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 29351673   1 GTNKGITALQADIKLPGVPIKIIMEAIQQASVAKKEILQIMNKTISKP 48
Cdd:cd11364 176 GTRDGITALQMDIKIPGITLEIMREALQQAKEGRLHILDIMEKAISEP 223
PLN00207 PLN00207
polyribonucleotide nucleotidyltransferase; Provisional
 1-210 1.09e-15

polyribonucleotide nucleotidyltransferase; Provisional


Pssm-ID: 215104 [Multi-domain]  Cd Length: 891  Bit Score: 75.70  E-value: 1.09e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29351673    1 GTNKGITALQADIKLPGVPIKIIMEAIQQASVAKKEILQIMNKTISKPRASRKENGPVVETVKVPLSKRAKFVGPGGYHL 80
Cdd:PLN00207 628 GNEDGITAFQMDIKVGGITLPIMERALLQAKDGRKHILAEMSKCSPPPSKRLSKYAPLIHIMKVKPEKVNMIIGSGGKKV 707

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29351673   81 KKLQAETGV-TISQVDEETFSIFAPTPTAMHEARDFITEICRDDQeqqleFGAVY-TATITEIRDTGVMVKLYPNMTAvL 158
Cdd:PLN00207 708 KSIIEETGVeAIDTQDDGTVKITAKDLSSLEKSKAIISSLTMVPT-----VGDIYrNCEIKSIAPYGAFVEIAPGREG-L 781

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 29351673  159 LHNSQLDQRKIKHPTAlGLEVGQEIQVKYFGRDpADGRMRLSRKVLQSPATT 210
Cdd:PLN00207 782 CHISELSSNWLAKPED-AFKVGDRIDVKLIEVN-DKGQLRLSRRALLPEANS 831
KH-I_PNPase cd02393
type I K homology (KH) RNA-binding domain found in polyribonucleotide nucleotidyltransferase ...
 55-122 2.50e-09

type I K homology (KH) RNA-binding domain found in polyribonucleotide nucleotidyltransferase (PNPase) and similar proteins; PNPase, also called polynucleotide phosphorylase, is a polyribonucleotide nucleotidyl transferase that degrades mRNA in prokaryotes and plant chloroplasts. It catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction. It is also involved, along with RNase II, in tRNA processing. The C-terminal region of PNPase contains domains homologous to those in other RNA binding proteins: a KH domain and an S1 domain. The model corresponds to the KH domain.


Pssm-ID: 411803 [Multi-domain]  Cd Length: 70  Bit Score: 52.09  E-value: 2.50e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 29351673  55 NGPVVETVKVPLSKRAKFVGPGGYHLKKLQAETGVTISQVDEETFSIFAPTPTAMHEARDFITEICRD 122
Cdd:cd02393   1 YAPRITTIKIPPDKIGDVIGPGGKTIRAIIEETGAKIDIEDDGTVTIFATDKESAEAAKAMIEDIVAE 68
rpsA PRK06299
30S ribosomal protein S1; Reviewed
 131-205 1.45e-07

30S ribosomal protein S1; Reviewed


Pssm-ID: 235775 [Multi-domain]  Cd Length: 565  Bit Score: 51.32  E-value: 1.45e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 29351673  131 GAVYTATITEIRDTGVMVKLYPNMTAvLLHNSQLDQRKIKHPTALgLEVGQEIQVKYFGRDPADGRMRLSRKVLQ 205
Cdd:PRK06299 461 GSIVTGTVTEVKDKGAFVELEDGVEG-LIRASELSRDRVEDATEV-LKVGDEVEAKVINIDRKNRRISLSIKALD 533
RpsA COG0539
Ribosomal protein S1 [Translation, ribosomal structure and biogenesis]; Ribosomal protein S1 ...
 126-205 1.09e-06

Ribosomal protein S1 [Translation, ribosomal structure and biogenesis]; Ribosomal protein S1 is part of the Pathway/BioSystem: Ribosome 30S subunit


Pssm-ID: 440305 [Multi-domain]  Cd Length: 348  Bit Score: 48.50  E-value: 1.09e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29351673 126 QQLEFGAVYTATITEIRDTGVMVKLYpnmtAV--LLHNSQLDQRKIKHPTALgLEVGQEIQVKYFGRDPADGRMRLSRKV 203
Cdd:COG0539 185 EKLEEGDVVEGTVKNITDFGAFVDLG----GVdgLLHISEISWGRVKHPSEV-LKVGDEVEVKVLKIDREKERISLSLKQ 259


                ..
gi 29351673 204 LQ 205
Cdd:COG0539 260 LQ 261
rpsA PRK06676
30S ribosomal protein S1; Reviewed
 122-225 3.64e-06

30S ribosomal protein S1; Reviewed


Pssm-ID: 235851 [Multi-domain]  Cd Length: 390  Bit Score: 47.18  E-value: 3.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29351673  122 DDQEQQLEFGAVYTATITEIRDTGVMVKLYPNMTAvLLHNSQLDQRKIKHPTALgLEVGQEIQVKYFGRDPADGRMRLSR 201
Cdd:PRK06676 269 EGVEEKLPEGDVIEGTVKRLTDFGAFVEVLPGVEG-LVHISQISHKHIATPSEV-LEEGQEVKVKVLEVNEEEKRISLSI 346

                         90       100
                 ....*....|....*....|....
gi 29351673  202 KVLQSPATTALKTLNDRSSIVMGE 225
Cdd:PRK06676 347 KALEEAPAEEEDRREEYRQYELPE 370
RpsA COG0539
Ribosomal protein S1 [Translation, ribosomal structure and biogenesis]; Ribosomal protein S1 ...
 122-205 4.23e-06

Ribosomal protein S1 [Translation, ribosomal structure and biogenesis]; Ribosomal protein S1 is part of the Pathway/BioSystem: Ribosome 30S subunit


Pssm-ID: 440305 [Multi-domain]  Cd Length: 348  Bit Score: 46.58  E-value: 4.23e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29351673 122 DDQEQQLEFGAVYTATITEIRDTGVMVKLYPNMTAvLLHNSQLDQ-RKIKHPTALgLEVGQEIQVKYFGRDPADGRMRLS 200
Cdd:COG0539 266 ENIAEKYPVGDVVKGKVTRLTDFGAFVELEPGVEG-LVHISEMSWtKRVAHPSDV-VKVGDEVEVKVLDIDPEERRISLS 343


                ....*
gi 29351673 201 RKVLQ 205
Cdd:COG0539 344 IKQLA 348
PRK00087 PRK00087
bifunctional 4-hydroxy-3-methylbut-2-enyl diphosphate reductase/30S ribosomal protein S1;
131-202 1.23e-05

bifunctional 4-hydroxy-3-methylbut-2-enyl diphosphate reductase/30S ribosomal protein S1;


Pssm-ID: 234623 [Multi-domain]  Cd Length: 647  Bit Score: 45.71  E-value: 1.23e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 29351673  131 GAVYTATITEIRDTGVMVKLYPNMTAvLLHNSQLDQRKIKHPTALgLEVGQEIQVKYFGRDPADGRMRLSRK 202
Cdd:PRK00087 563 GSIVLGKVVRIAPFGAFVELEPGVDG-LVHISQISWKRIDKPEDV-LSEGEEVKAKILEVDPEEKRIRLSIK 632
rpsA PRK06299
30S ribosomal protein S1; Reviewed
 131-225 1.59e-05

30S ribosomal protein S1; Reviewed


Pssm-ID: 235775 [Multi-domain]  Cd Length: 565  Bit Score: 45.16  E-value: 1.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29351673  131 GAVYTATITEIRDTGVMVKLYPNMTAvLLHNSQLD-QRKIKHPTALgLEVGQEIQVKYFGRDPADGRMRLSRKVL-QSPA 208
Cdd:PRK06299 374 GDVVEGKVKNITDFGAFVGLEGGIDG-LVHLSDISwDKKGEEAVEL-YKKGDEVEAVVLKVDVEKERISLGIKQLeEDPF 451

                         90
                 ....*....|....*..
gi 29351673  209 TTALKTlNDRSSIVMGE 225
Cdd:PRK06299 452 EEFAKK-HKKGSIVTGT 467
S1_like cd00164
S1_like: Ribosomal protein S1-like RNA-binding domain. Found in a wide variety of ...
 134-200 2.07e-05

S1_like: Ribosomal protein S1-like RNA-binding domain. Found in a wide variety of RNA-associated proteins. Originally identified in S1 ribosomal protein. This superfamily also contains the Cold Shock Domain (CSD), which is a homolog of the S1 domain. Both domains are members of the Oligonucleotide/oligosaccharide Binding (OB) fold.


Pssm-ID: 238094 [Multi-domain]  Cd Length: 65  Bit Score: 41.21  E-value: 2.07e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 29351673 134 YTATITEIRDTGVMVKLYPNMTAvLLHNSQLDQRKIKHPTALgLEVGQEIQVKYFGRDPADGRMRLS 200
Cdd:cd00164   1 VTGKVVSITKFGVFVELEDGVEG-LVHISELSDKFVKDPSEV-FKVGDEVEVKVLEVDPEKGRISLS 65
S1_RPS1_repeat_hs4 cd05692
S1_RPS1_repeat_hs4: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
 131-202 2.33e-05

S1_RPS1_repeat_hs4: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ribosomal subunit thought to be involved in the recognition and binding of mRNA's during translation initiation. The bacterial RPS1 domain architecture consists of 4-6 tandem S1 domains. In some bacteria, the tandem S1 array is located C-terminal to a 4-hydroxy-3-methylbut-2-enyl diphosphate reductase (HMBPP reductase) domain. While RPS1 is found primarily in bacteria, proteins with tandem RPS1-like domains have been identified in plants and humans, however these lack the N-terminal HMBPP reductase domain. This CD includes S1 repeat 4 (hs4) of the H. sapiens RPS1 homolog. Autoantibodies to double-stranded DNA from patients with systemic lupus erythematosus cross-react with the human RPS1 homolog.


Pssm-ID: 240197 [Multi-domain]  Cd Length: 69  Bit Score: 41.12  E-value: 2.33e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 29351673 131 GAVYTATITEIRDTGVMVKLYPNMTAvLLHNSQLDQRKIKHPTALgLEVGQEIQVKYFGRDPaDGRMRLSRK 202
Cdd:cd05692   1 GSVVEGTVTRLKPFGAFVELGGGISG-LVHISQIAHKRVKDVKDV-LKEGDKVKVKVLSIDA-RGRISLSIK 69
S1_RPS1_repeat_ec3 cd05688
S1_RPS1_repeat_ec3: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
 131-200 2.69e-05

S1_RPS1_repeat_ec3: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ribosomal subunit thought to be involved in the recognition and binding of mRNA's during translation initiation. The bacterial RPS1 domain architecture consists of 4-6 tandem S1 domains. In some bacteria, the tandem S1 array is located C-terminal to a 4-hydroxy-3-methylbut-2-enyl diphosphate reductase (HMBPP reductase) domain. While RPS1 is found primarily in bacteria, proteins with tandem RPS1-like domains have been identified in plants and humans, however these lack the N-terminal HMBPP reductase domain. This CD includes S1 repeat 3 (ec3) of the Escherichia coli RPS1. Autoantibodies to double-stranded DNA from patients with systemic lupus erythematosus cross-react with the human RPS1 homolog.


Pssm-ID: 240193 [Multi-domain]  Cd Length: 68  Bit Score: 41.08  E-value: 2.69e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 29351673 131 GAVYTATITEIRDTGVMVKLypnmTAV--LLHNSQLDQRKIKHPTALgLEVGQEIQVKYFGRDPADGRMRLS 200
Cdd:cd05688   2 GDVVEGTVKSITDFGAFVDL----GGVdgLLHISDMSWGRVKHPSEV-VNVGDEVEVKVLKIDKERKRISLG 68
S1 pfam00575
S1 RNA binding domain; The S1 domain occurs in a wide range of RNA associated proteins. It is ...
 131-201 2.86e-05

S1 RNA binding domain; The S1 domain occurs in a wide range of RNA associated proteins. It is structurally similar to cold shock protein which binds nucleic acids. The S1 domain has an OB-fold structure.


Pssm-ID: 425760 [Multi-domain]  Cd Length: 72  Bit Score: 41.12  E-value: 2.86e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 29351673   131 GAVYTATITEIRDTGVMVKLYPNMTAvLLHNSQLDQRKIKHPTaLGLEVGQEIQVKYFGRDPADGRMRLSR 201
Cdd:pfam00575   4 GDVVEGEVTRVTKGGAFVDLGNGVEG-FIPISELSDDHVEDPD-EVIKVGDEVKVKVLKVDKDRRRIILSI 72
rpsA TIGR00717
ribosomal protein S1; This model describes ribosomal protein S1, RpsA. This protein is found ...
 131-202 4.60e-05

ribosomal protein S1; This model describes ribosomal protein S1, RpsA. This protein is found in most bacterial genomes in a single copy, but is not present in the Mycoplasmas. It is heterogeneous with respect to the number of repeats of the S1 RNA binding domain described by pfam00575: six repeats in E. coli and most other bacteria, four in Bacillus subtilis and some other species. rpsA is an essential gene in E. coli but not in B. subtilis. It is associated with the cytidylate kinase gene cmk in many species, and fused to it in Treponema pallidum. RpsA is proposed (Medline:97323001) to assist in mRNA degradation. This model provides trusted hits to most long form (6 repeat) examples of RpsA. Among homologs with only four repeats are some to which other (perhaps secondary) functions have been assigned. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 273232 [Multi-domain]  Cd Length: 516  Bit Score: 43.95  E-value: 4.60e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 29351673   131 GAVYTATITEIRDTGVMVKLyPNMTAVLLHNSQLDQRKIKHPTaLGLEVGQEIQVKYFGRDPADGRMRLSRK 202
Cdd:TIGR00717 447 GSVVKGKVTEIKDFGAFVEL-PGGVEGLIRNSELSENRDEDKT-DEIKVGDEVEAKVVDIDKKNRKVSLSVK 516
KH smart00322
K homology RNA-binding domain;
57-119 5.64e-05

K homology RNA-binding domain;


Pssm-ID: 197652 [Multi-domain]  Cd Length: 68  Bit Score: 39.97  E-value: 5.64e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 29351673     57 PVVETVKVPLSKRAKFVGPGGYHLKKLQAETGVTI----SQVDEETFSIFAPtPTAMHEARDFITEI 119
Cdd:smart00322   2 PVTIEVLIPADKVGLIIGKGGSTIKKIEEETGVKIdipgPGSEERVVEITGP-PENVEKAAELILEI 67
PRK00087 PRK00087
bifunctional 4-hydroxy-3-methylbut-2-enyl diphosphate reductase/30S ribosomal protein S1;
128-207 8.01e-05

bifunctional 4-hydroxy-3-methylbut-2-enyl diphosphate reductase/30S ribosomal protein S1;


Pssm-ID: 234623 [Multi-domain]  Cd Length: 647  Bit Score: 43.01  E-value: 8.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29351673  128 LEFGAVYTATITEIRDTGVMVKLypNMTAVLLHNSQLDQRKIKHPTALgLEVGQEIQVKYFGRDPADGRMRLSRK-VLQS 206
Cdd:PRK00087 475 LEEGDVVEGEVKRLTDFGAFVDI--GGVDGLLHVSEISWGRVEKPSDV-LKVGDEIKVYILDIDKENKKLSLSLKkLLPD 551


                 .
gi 29351673  207 P 207
Cdd:PRK00087 552 P 552
KH_1 pfam00013
KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause ...
 59-118 1.02e-04

KH domain; KH motifs bind RNA in vitro. Autoantibodies to Nova, a KH domain protein, cause paraneoplastic opsoclonus ataxia.


Pssm-ID: 459630 [Multi-domain]  Cd Length: 65  Bit Score: 39.19  E-value: 1.02e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 29351673    59 VETVKVPLSKRAKFVGPGGYHLKKLQAETGVTI------SQVDEETFSIFApTPTAMHEARDFITE 118
Cdd:pfam00013   1 TVEILVPSSLVGLIIGKGGSNIKEIREETGAKIqippseSEGNERIVTITG-TPEAVEAAKALIEE 65
rpsA PRK06299
30S ribosomal protein S1; Reviewed
 122-205 1.22e-04

30S ribosomal protein S1; Reviewed


Pssm-ID: 235775 [Multi-domain]  Cd Length: 565  Bit Score: 42.46  E-value: 1.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29351673  122 DDQEQQLEFGAVYTATITEIRDTGVMVKLYPNMTAvLLHNSQLD-QRKIKHPTALgLEVGQEIQVKYFGRDPADGRMRLS 200
Cdd:PRK06299 278 EAIEKKYPVGSKVKGKVTNITDYGAFVELEEGIEG-LVHVSEMSwTKKNKHPSKV-VSVGQEVEVMVLEIDEEKRRISLG 355


                 ....*
gi 29351673  201 RKVLQ 205
Cdd:PRK06299 356 LKQCK 360
rpsA PRK06676
30S ribosomal protein S1; Reviewed
 121-207 1.53e-04

30S ribosomal protein S1; Reviewed


Pssm-ID: 235851 [Multi-domain]  Cd Length: 390  Bit Score: 42.17  E-value: 1.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29351673  121 RDDQEQQLEFGAVYTATITEIRDTGVMVKLypnmTAV--LLHNSQLDQRKIKHPTALgLEVGQEIQVKYFGRDPADGRMR 198
Cdd:PRK06676 183 KEELLSSLKEGDVVEGTVARLTDFGAFVDI----GGVdgLVHISELSHERVEKPSEV-VSVGQEVEVKVLSIDWETERIS 257

                         90
                 ....*....|
gi 29351673  199 LSRK-VLQSP 207
Cdd:PRK06676 258 LSLKdTLPGP 267
rpsA PRK06299
30S ribosomal protein S1; Reviewed
 126-206 2.75e-04

30S ribosomal protein S1; Reviewed


Pssm-ID: 235775 [Multi-domain]  Cd Length: 565  Bit Score: 41.69  E-value: 2.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29351673  126 QQLEFGAVYTATITEIRDTGVMVKLYpnmtAV--LLHNSQLDQRKIKHPTALgLEVGQEIQVKYFGRDPADGRMRLSRKV 203
Cdd:PRK06299 197 ENLEEGQVVEGVVKNITDYGAFVDLG----GVdgLLHITDISWKRVNHPSEV-VNVGDEVKVKVLKFDKEKKRVSLGLKQ 271


                 ...
gi 29351673  204 LQS 206
Cdd:PRK06299 272 LGE 274
PRK08059 PRK08059
general stress protein 13; Validated
 127-205 6.24e-04

general stress protein 13; Validated


Pssm-ID: 181215 [Multi-domain]  Cd Length: 123  Bit Score: 38.49  E-value: 6.24e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 29351673  127 QLEFGAVYTATITEIRDTGVMVKLyPNMTAVLLHNSQLDQRKIKHPTALgLEVGQEIQVKYFGRDPADGRMRLSRKVLQ 205
Cdd:PRK08059   4 QYEVGSVVTGKVTGIQPYGAFVAL-DEETQGLVHISEITHGFVKDIHDF-LSVGDEVKVKVLSVDEEKGKISLSIRATE 80
KH-I cd00105
K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found ...
 60-116 8.13e-04

K homology (KH) RNA-binding domain, type I; KH binds single-stranded RNA or DNA. It is found in a wide variety of proteins including ribosomal proteins, transcription factors and post-transcriptional modifiers of mRNA. There are two different KH domains that belong to different protein folds, but they share a single KH motif. The KH motif is folded into a beta alpha alpha beta unit. In addition to the core, type II KH domains (e.g. ribosomal protein S3) include an N-terminal extension and type I KH domains (e.g. hnRNP K) contain a C-terminal extension. Some KH-I superfamily members contain a divergent KH domain that lacks the RNA-binding GXXG motif. Some others have a mutated GXXG motif which may or may not have nucleic acid binding ability.


Pssm-ID: 411802 [Multi-domain]  Cd Length: 63  Bit Score: 36.89  E-value: 8.13e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 29351673  60 ETVKVPLSKRAKFVGPGGYHLKKLQAETGVTI------SQVDEETFSIFApTPTAMHEARDFI 116
Cdd:cd00105   1 EEIEVPSELVGLIIGKGGSTIKEIEEETGARIqipkegEGSGERVVTITG-TPEAVEKAKELI 62
S1_Rrp5_repeat_hs6_sc5 cd05698
S1_Rrp5_repeat_hs6_sc5: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ...
 136-202 1.09e-03

S1_Rrp5_repeat_hs6_sc5: Rrp5 is a trans-acting factor important for biogenesis of both the 40S and 60S eukaryotic ribosomal subunits. Rrp5 has two distinct regions, an N-terminal region containing tandemly repeated S1 RNA-binding domains (12 S1 repeats in Saccharomyces cerevisiae Rrp5 and 14 S1 repeats in Homo sapiens Rrp5) and a C-terminal region containing tetratricopeptide repeat (TPR) motifs thought to be involved in protein-protein interactions. Mutational studies have shown that each region represents a specific functional domain. Deletions within the S1-containing region inhibit pre-rRNA processing at either site A3 or A2, whereas deletions within the TPR region confer an inability to support cleavage of A0-A2. This CD includes H. sapiens S1 repeat 6 (hs6) and S. cerevisiae S1 repeat 5 (sc5). Rrp5 is found in eukaryotes but not in prokaryotes or archaea.


Pssm-ID: 240203 [Multi-domain]  Cd Length: 70  Bit Score: 36.43  E-value: 1.09e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 29351673 136 ATITEIRDTGVMVKLYPNMTAvLLHNSQLDQRKIKHPTALgLEVGQEIQVKYFGRDPADGRMRLSRK 202
Cdd:cd05698   6 GTIVKVKPNGCIVSFYNNVKG-FLPKSELSEAFIKDPEEH-FRVGQVVKVKVLSCDPEQQRLLLSCK 70
KH_I_FMR1_FXR_rpt2 cd22426
second type I K homology (KH) RNA-binding domain found in a family of fragile X mental ...
 57-116 1.34e-03

second type I K homology (KH) RNA-binding domain found in a family of fragile X mental retardation protein (FMR1) and fragile X related (FXR) proteins; The FMR1/FXR family includes FMR1 (also known as FMRP) and its two homologues, fragile X related 1 (FXR1) and 2 (FXR2). They are involved in translational regulation, particularly in neuronal cells and play an important role in the regulation of glutamate-mediated neuronal activity and plasticity. Each of these three proteins can form heteromers with the others, and each can also form homomers. Lack of expression of FMR1 results in mental retardation and macroorchidism. FXR1 and FXR2 may play important roles in the function of FMR1 and in the pathogenesis of the Fragile X Mental Retardation Syndrome. Members of this family contain three K-homology (KH) RNA-binding domains. The model corresponds to the second one.


Pssm-ID: 411854 [Multi-domain]  Cd Length: 63  Bit Score: 35.97  E-value: 1.34e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 29351673  57 PVVETVKVPLSKRAKFVGPGGYHLKKLQAETGVTISQVDEE--TFSIFAPTPTAMHEARDFI 116
Cdd:cd22426   1 GFIEEFKVDPDLIGLAIGSHGSNIQQARKIPGVESIDVDEEdgTFRIYGETPEAVEKARALL 62
rpsA TIGR00717
ribosomal protein S1; This model describes ribosomal protein S1, RpsA. This protein is found ...
 122-205 1.41e-03

ribosomal protein S1; This model describes ribosomal protein S1, RpsA. This protein is found in most bacterial genomes in a single copy, but is not present in the Mycoplasmas. It is heterogeneous with respect to the number of repeats of the S1 RNA binding domain described by pfam00575: six repeats in E. coli and most other bacteria, four in Bacillus subtilis and some other species. rpsA is an essential gene in E. coli but not in B. subtilis. It is associated with the cytidylate kinase gene cmk in many species, and fused to it in Treponema pallidum. RpsA is proposed (Medline:97323001) to assist in mRNA degradation. This model provides trusted hits to most long form (6 repeat) examples of RpsA. Among homologs with only four repeats are some to which other (perhaps secondary) functions have been assigned. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 273232 [Multi-domain]  Cd Length: 516  Bit Score: 39.33  E-value: 1.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29351673   122 DDQEQQLEFGAVYTATITEIRDTGVMVKLYPNMTAvLLHNSQLD-QRKIKHPTALgLEVGQEIQVKYFGRDPADGRMRLS 200
Cdd:TIGR00717 264 EAIEKKFPVGDKITGRVTNLTDYGVFVEIEEGIEG-LVHVSEMSwVKKNSHPSKV-VKKGDEVEVMILDIDPERRRLSLG 341


                  ....*
gi 29351673   201 RKVLQ 205
Cdd:TIGR00717 342 LKQCK 346
S1_Tex cd05685
S1_Tex: The C-terminal S1 domain of a transcription accessory factor called Tex, which has ...
 131-200 3.27e-03

S1_Tex: The C-terminal S1 domain of a transcription accessory factor called Tex, which has been characterized in Bordetella pertussis and Pseudomonas aeruginosa. The tex gene is essential in Bortella pertusis and is named for its role in toxin expression. Tex has two functional domains, an N-terminal domain homologous to the Escherichia coli maltose repression protein, which is a poorly defined transcriptional factor, and a C-terminal S1 RNA-binding domain. Tex is found in prokaryotes, eukaryotes, and archaea.


Pssm-ID: 240190 [Multi-domain]  Cd Length: 68  Bit Score: 35.29  E-value: 3.27e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29351673 131 GAVYTATITEIRDTGVMVKLYPNmTAVLLHNSQLDQRKIKHPTaLGLEVGQEIQVKYFGRDPADGRMRLS 200
Cdd:cd05685   1 GMVLEGVVTNVTDFGAFVDIGVK-QDGLIHISKMADRFVSHPS-DVVSVGDIVEVKVISIDEERGRISLS 68
KH-I_Vigilin_rpt4 cd22408
fourth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins; ...
 61-104 7.14e-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: 34.07  E-value: 7.14e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 29351673  61 TVKVPLSKRAKFVGPGGYHLKKLQAETGVTIS----QVDEETFSIFAP 104
Cdd:cd22408   3 SVEVPKSQHRFVIGPRGSTIQEILEETGCSVEvppnDSDSETITLRGP 50
 
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