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Conserved domains on  [gi|647806374|gb|AIC21458|]
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30S ribosomal protein S1 [Pseudomonas chlororaphis]

Protein Classification

30S ribosomal protein S1( domain architecture ID 11482186)

30S ribosomal protein S1 is required for translation of most natural mRNAs except for leaderless mRNA; it binds mRNA upstream of the Shine-Dalgarno (SD) sequence and helps it bind to the 30S ribosomal subunit

Gene Ontology:  GO:0000028|GO:0006412

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
rpsA PRK06299
30S ribosomal protein S1; Reviewed
1-563 0e+00

30S ribosomal protein S1; Reviewed


:

Pssm-ID: 235775 [Multi-domain]  Cd Length: 565  Bit Score: 932.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374   1 MSESFAELFEESLKTLNLQAGSIITGVIVDIDyqARWVTVHAGLKSEALIPLEQFYNDAGELSINVGDEVHVALDSVEDG 80
Cdd:PRK06299  11 MEESFAELFEESLKESETREGSIVKGTVVAID--KDYVLVDVGLKSEGRIPLEEFKNEQGELEVKVGDEVEVYVERIEDG 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374  81 FGETKLSREKAKRAECWIVLEAAFAAEEVVKGVINGKVKGGFTVDVNGIRAFLPGSLVDVRPVRDTTHLEGKELEFKVIK 160
Cdd:PRK06299  89 FGETVLSREKAKRLEAWDKLEKAFENGEIVEGVINGKVKGGFTVDLNGVEAFLPGSQVDVRPVRDTDPLEGKELEFKVIK 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374 161 LDQKRNNVVVSRRSVLEAENSAEREALLESLQEGQQVKGIVKNLTDYGAFVDLGGVDGLLHITDMAWKRIKHPSEIVNVG 240
Cdd:PRK06299 169 LDKKRNNIVVSRRAVLEEERAEEREELLENLEEGQVVEGVVKNITDYGAFVDLGGVDGLLHITDISWKRVNHPSEVVNVG 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374 241 DEIDVKVLKYDRERNRVSLGLKQLGEDPWVAIKARYPESTRVTARVTNLTDYGCFAELEEGVEGLVHVSEMDWTNKNIHP 320
Cdd:PRK06299 249 DEVKVKVLKFDKEKKRVSLGLKQLGEDPWEAIEKKYPVGSKVKGKVTNITDYGAFVELEEGIEGLVHVSEMSWTKKNKHP 328
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374 321 SKVVQVGDEVEVMVLDIDEERRRISLGIKQCKSNPWEDFSGQFNKGDKISGTIKSITDFGIFIGLDGGIDGLVHLSDISW 400
Cdd:PRK06299 329 SKVVSVGQEVEVMVLEIDEEKRRISLGLKQCKENPWEEFAEKYPVGDVVEGKVKNITDFGAFVGLEGGIDGLVHLSDISW 408
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374 401 NEVGEEAVRRFKKGDELDTVILSVDPERERISLGIKQLESDPFSEYVQENDKGAIVKGVVKEVDAKGAIITLANDIEATL 480
Cdd:PRK06299 409 DKKGEEAVELYKKGDEVEAVVLKVDVEKERISLGIKQLEEDPFEEFAKKHKKGSIVTGTVTEVKDKGAFVELEDGVEGLI 488
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374 481 KASEISRDRIEDARNVLKEGEEVEAKIISVDRKSRVIQLSIKSKDVEDEKEAIQSLRDKpaasdiAAGPTTLGDLLRAQM 560
Cdd:PRK06299 489 RASELSRDRVEDATEVLKVGDEVEAKVINIDRKNRRISLSIKALDEAEEKEAIAEYNSA------SDSKTTLGDLLKAAL 562

                 ...
gi 647806374 561 EKQ 563
Cdd:PRK06299 563 KGK 565
 
Name Accession Description Interval E-value
rpsA PRK06299
30S ribosomal protein S1; Reviewed
1-563 0e+00

30S ribosomal protein S1; Reviewed


Pssm-ID: 235775 [Multi-domain]  Cd Length: 565  Bit Score: 932.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374   1 MSESFAELFEESLKTLNLQAGSIITGVIVDIDyqARWVTVHAGLKSEALIPLEQFYNDAGELSINVGDEVHVALDSVEDG 80
Cdd:PRK06299  11 MEESFAELFEESLKESETREGSIVKGTVVAID--KDYVLVDVGLKSEGRIPLEEFKNEQGELEVKVGDEVEVYVERIEDG 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374  81 FGETKLSREKAKRAECWIVLEAAFAAEEVVKGVINGKVKGGFTVDVNGIRAFLPGSLVDVRPVRDTTHLEGKELEFKVIK 160
Cdd:PRK06299  89 FGETVLSREKAKRLEAWDKLEKAFENGEIVEGVINGKVKGGFTVDLNGVEAFLPGSQVDVRPVRDTDPLEGKELEFKVIK 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374 161 LDQKRNNVVVSRRSVLEAENSAEREALLESLQEGQQVKGIVKNLTDYGAFVDLGGVDGLLHITDMAWKRIKHPSEIVNVG 240
Cdd:PRK06299 169 LDKKRNNIVVSRRAVLEEERAEEREELLENLEEGQVVEGVVKNITDYGAFVDLGGVDGLLHITDISWKRVNHPSEVVNVG 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374 241 DEIDVKVLKYDRERNRVSLGLKQLGEDPWVAIKARYPESTRVTARVTNLTDYGCFAELEEGVEGLVHVSEMDWTNKNIHP 320
Cdd:PRK06299 249 DEVKVKVLKFDKEKKRVSLGLKQLGEDPWEAIEKKYPVGSKVKGKVTNITDYGAFVELEEGIEGLVHVSEMSWTKKNKHP 328
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374 321 SKVVQVGDEVEVMVLDIDEERRRISLGIKQCKSNPWEDFSGQFNKGDKISGTIKSITDFGIFIGLDGGIDGLVHLSDISW 400
Cdd:PRK06299 329 SKVVSVGQEVEVMVLEIDEEKRRISLGLKQCKENPWEEFAEKYPVGDVVEGKVKNITDFGAFVGLEGGIDGLVHLSDISW 408
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374 401 NEVGEEAVRRFKKGDELDTVILSVDPERERISLGIKQLESDPFSEYVQENDKGAIVKGVVKEVDAKGAIITLANDIEATL 480
Cdd:PRK06299 409 DKKGEEAVELYKKGDEVEAVVLKVDVEKERISLGIKQLEEDPFEEFAKKHKKGSIVTGTVTEVKDKGAFVELEDGVEGLI 488
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374 481 KASEISRDRIEDARNVLKEGEEVEAKIISVDRKSRVIQLSIKSKDVEDEKEAIQSLRDKpaasdiAAGPTTLGDLLRAQM 560
Cdd:PRK06299 489 RASELSRDRVEDATEVLKVGDEVEAKVINIDRKNRRISLSIKALDEAEEKEAIAEYNSA------SDSKTTLGDLLKAAL 562

                 ...
gi 647806374 561 EKQ 563
Cdd:PRK06299 563 KGK 565
rpsA TIGR00717
ribosomal protein S1; This model describes ribosomal protein S1, RpsA. This protein is found ...
3-522 0e+00

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: 667.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374    3 ESFAELFEESLKTLNLQAGSIITGVIVDIdyQARWVTVHAGLKSEALIPLEQFYNDagELSINVGDEVHVALDSVEDGFG 82
Cdd:TIGR00717   1 ESFAQLLEESLKTEETRPGSIVKGTVVAI--NKDTVFVDVGLKSEGRIPKEEFLDA--PLEIQVGDEVEVYLDRVEDRFG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374   83 ETKLSREKAKRAECWIVLEAAFAAEEVVKGVINGKVKGGFTVDVNGIRAFLPGSLVDVRPVRDTTHLEGKELEFKVIKLD 162
Cdd:TIGR00717  77 ETVLSREKAQRHELWIKLEKAYEEGSIVEGKIVGKVKGGFIVDLNGVEAFLPGSQVDVKPIKDLDSLIGKTLKFKIIKLD 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374  163 QKRNNVVVSRRSVLEAENSAEREALLESLQEGQQVKGIVKNLTDYGAFVDLGGVDGLLHITDMAWKRIKHPSEIVNVGDE 242
Cdd:TIGR00717 157 QKRNNIVVSRRAYLEEERSQAREELLENLKEGDVVKGVVKNITDFGAFVDLGGVDGLLHITDMSWKRVKHPSEYVKVGQE 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374  243 IDVKVLKYDRERNRVSLGLKQLGEDPWVAIKARYPESTRVTARVTNLTDYGCFAELEEGVEGLVHVSEMDWTNKNIHPSK 322
Cdd:TIGR00717 237 VKVKVIKFDKEKGRISLSLKQLGEDPWEAIEKKFPVGDKITGRVTNLTDYGVFVEIEEGIEGLVHVSEMSWVKKNSHPSK 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374  323 VVQVGDEVEVMVLDIDEERRRISLGIKQCKSNPWEDFSGQFNKGDKISGTIKSITDFGIFIGLDGGIDGLVHLSDISWNE 402
Cdd:TIGR00717 317 VVKKGDEVEVMILDIDPERRRLSLGLKQCKANPWEQFEEKHPVGDRVTGKIKKITDFGAFVELEGGIDGLIHLSDISWDK 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374  403 VGEEAVRRFKKGDELDTVILSVDPERERISLGIKQLESDPFSEYVQENDKGAIVKGVVKEVDAKGAIITLANDIEATLKA 482
Cdd:TIGR00717 397 DGREADHLYKKGDEIEAVVLAVDKEKKRISLGVKQLTENPWEKFAAKYKVGSVVKGKVTEIKDFGAFVELPGGVEGLIRN 476
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|
gi 647806374  483 SEISRDRIEDARNVLKEGEEVEAKIISVDRKSRVIQLSIK 522
Cdd:TIGR00717 477 SELSENRDEDKTDEIKVGDEVEAKVVDIDKKNRKVSLSVK 516
RpsA COG0539
Ribosomal protein S1 [Translation, ribosomal structure and biogenesis]; Ribosomal protein S1 ...
1-352 0e+00

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: 573.91  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374   1 MSESFAELFEESLKtlNLQAGSIITGVIVDIDyqARWVTVHAGLKSEALIPLEQFYNDAGELSINVGDEVHVALDSVEDG 80
Cdd:COG0539    1 MSESFAELLEESLK--ELKEGDIVKGTVVSID--DDEVLVDIGYKSEGIIPLSEFSDEPGELEVKVGDEVEVYVEKVEDG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374  81 FGETKLSREKAKRAECWIVLEAAFAAEEVVKGVINGKVKGGFTVDVNGIRAFLPGSLVDVRPVRDTTHLEGKELEFKVIK 160
Cdd:COG0539   77 EGEIVLSKKKADREKAWEELEEAFENGEPVEGKVKGVVKGGLIVDIGGVRAFLPASQVDVRPVRDLDEYVGKTLEFKIIK 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374 161 LDQKRNNVVVSRRSVLEAENSAEREALLESLQEGQQVKGIVKNLTDYGAFVDLGGVDGLLHITDMAWKRIKHPSEIVNVG 240
Cdd:COG0539  157 LDRKRNNVVVSRRAVLEEEREEKREELLEKLEEGDVVEGTVKNITDFGAFVDLGGVDGLLHISEISWGRVKHPSEVLKVG 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374 241 DEIDVKVLKYDRERNRVSLGLKQLGEDPWVAIKARYPESTRVTARVTNLTDYGCFAELEEGVEGLVHVSEMDWTNKNIHP 320
Cdd:COG0539  237 DEVEVKVLKIDREKERISLSLKQLQPDPWENIAEKYPVGDVVKGKVTRLTDFGAFVELEPGVEGLVHISEMSWTKRVAHP 316
                        330       340       350
                 ....*....|....*....|....*....|..
gi 647806374 321 SKVVQVGDEVEVMVLDIDEERRRISLGIKQCK 352
Cdd:COG0539  317 SDVVKVGDEVEVKVLDIDPEERRISLSIKQLA 348
S1_RPS1_repeat_ec4 cd05689
S1_RPS1_repeat_ec4: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
276-347 1.86e-40

S1_RPS1_repeat_ec4: 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 (ec4) 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: 240194 [Multi-domain]  Cd Length: 72  Bit Score: 140.79  E-value: 1.86e-40
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 647806374 276 YPESTRVTARVTNLTDYGCFAELEEGVEGLVHVSEMDWTNKNIHPSKVVQVGDEVEVMVLDIDEERRRISLG 347
Cdd:cd05689    1 YPEGTRLFGKVTNLTDYGCFVELEEGVEGLVHVSEMDWTNKNIHPSKVVSLGDEVEVMVLDIDEERRRISLG 72
S1 smart00316
Ribosomal protein S1-like RNA-binding domain;
192-262 2.06e-19

Ribosomal protein S1-like RNA-binding domain;


Pssm-ID: 197648 [Multi-domain]  Cd Length: 72  Bit Score: 82.27  E-value: 2.06e-19
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 647806374   192 QEGQQVKGIVKNLTDYGAFVDLG-GVDGLLHITDMAWKRIKHPSEIVNVGDEIDVKVLKYDRERNRVSLGLK 262
Cdd:smart00316   1 EVGDVVEGTVTEITPGGAFVDLGnGVEGLIPISELSDKRVKDPEEVLKVGDEVKVKVLSVDEEKGRIILSLK 72
S1 pfam00575
S1 RNA binding domain; The S1 domain occurs in a wide range of RNA associated proteins. It is ...
191-261 1.81e-15

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: 71.16  E-value: 1.81e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 647806374  191 LQEGQQVKGIVKNLTDYGAFVDLG-GVDGLLHITDMAWKRIKHPSEIVNVGDEIDVKVLKYDRERNRVSLGL 261
Cdd:pfam00575   1 PEKGDVVEGEVTRVTKGGAFVDLGnGVEGFIPISELSDDHVEDPDEVIKVGDEVKVKVLKVDKDRRRIILSI 72
 
Name Accession Description Interval E-value
rpsA PRK06299
30S ribosomal protein S1; Reviewed
1-563 0e+00

30S ribosomal protein S1; Reviewed


Pssm-ID: 235775 [Multi-domain]  Cd Length: 565  Bit Score: 932.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374   1 MSESFAELFEESLKTLNLQAGSIITGVIVDIDyqARWVTVHAGLKSEALIPLEQFYNDAGELSINVGDEVHVALDSVEDG 80
Cdd:PRK06299  11 MEESFAELFEESLKESETREGSIVKGTVVAID--KDYVLVDVGLKSEGRIPLEEFKNEQGELEVKVGDEVEVYVERIEDG 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374  81 FGETKLSREKAKRAECWIVLEAAFAAEEVVKGVINGKVKGGFTVDVNGIRAFLPGSLVDVRPVRDTTHLEGKELEFKVIK 160
Cdd:PRK06299  89 FGETVLSREKAKRLEAWDKLEKAFENGEIVEGVINGKVKGGFTVDLNGVEAFLPGSQVDVRPVRDTDPLEGKELEFKVIK 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374 161 LDQKRNNVVVSRRSVLEAENSAEREALLESLQEGQQVKGIVKNLTDYGAFVDLGGVDGLLHITDMAWKRIKHPSEIVNVG 240
Cdd:PRK06299 169 LDKKRNNIVVSRRAVLEEERAEEREELLENLEEGQVVEGVVKNITDYGAFVDLGGVDGLLHITDISWKRVNHPSEVVNVG 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374 241 DEIDVKVLKYDRERNRVSLGLKQLGEDPWVAIKARYPESTRVTARVTNLTDYGCFAELEEGVEGLVHVSEMDWTNKNIHP 320
Cdd:PRK06299 249 DEVKVKVLKFDKEKKRVSLGLKQLGEDPWEAIEKKYPVGSKVKGKVTNITDYGAFVELEEGIEGLVHVSEMSWTKKNKHP 328
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374 321 SKVVQVGDEVEVMVLDIDEERRRISLGIKQCKSNPWEDFSGQFNKGDKISGTIKSITDFGIFIGLDGGIDGLVHLSDISW 400
Cdd:PRK06299 329 SKVVSVGQEVEVMVLEIDEEKRRISLGLKQCKENPWEEFAEKYPVGDVVEGKVKNITDFGAFVGLEGGIDGLVHLSDISW 408
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374 401 NEVGEEAVRRFKKGDELDTVILSVDPERERISLGIKQLESDPFSEYVQENDKGAIVKGVVKEVDAKGAIITLANDIEATL 480
Cdd:PRK06299 409 DKKGEEAVELYKKGDEVEAVVLKVDVEKERISLGIKQLEEDPFEEFAKKHKKGSIVTGTVTEVKDKGAFVELEDGVEGLI 488
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374 481 KASEISRDRIEDARNVLKEGEEVEAKIISVDRKSRVIQLSIKSKDVEDEKEAIQSLRDKpaasdiAAGPTTLGDLLRAQM 560
Cdd:PRK06299 489 RASELSRDRVEDATEVLKVGDEVEAKVINIDRKNRRISLSIKALDEAEEKEAIAEYNSA------SDSKTTLGDLLKAAL 562

                 ...
gi 647806374 561 EKQ 563
Cdd:PRK06299 563 KGK 565
rpsA TIGR00717
ribosomal protein S1; This model describes ribosomal protein S1, RpsA. This protein is found ...
3-522 0e+00

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: 667.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374    3 ESFAELFEESLKTLNLQAGSIITGVIVDIdyQARWVTVHAGLKSEALIPLEQFYNDagELSINVGDEVHVALDSVEDGFG 82
Cdd:TIGR00717   1 ESFAQLLEESLKTEETRPGSIVKGTVVAI--NKDTVFVDVGLKSEGRIPKEEFLDA--PLEIQVGDEVEVYLDRVEDRFG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374   83 ETKLSREKAKRAECWIVLEAAFAAEEVVKGVINGKVKGGFTVDVNGIRAFLPGSLVDVRPVRDTTHLEGKELEFKVIKLD 162
Cdd:TIGR00717  77 ETVLSREKAQRHELWIKLEKAYEEGSIVEGKIVGKVKGGFIVDLNGVEAFLPGSQVDVKPIKDLDSLIGKTLKFKIIKLD 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374  163 QKRNNVVVSRRSVLEAENSAEREALLESLQEGQQVKGIVKNLTDYGAFVDLGGVDGLLHITDMAWKRIKHPSEIVNVGDE 242
Cdd:TIGR00717 157 QKRNNIVVSRRAYLEEERSQAREELLENLKEGDVVKGVVKNITDFGAFVDLGGVDGLLHITDMSWKRVKHPSEYVKVGQE 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374  243 IDVKVLKYDRERNRVSLGLKQLGEDPWVAIKARYPESTRVTARVTNLTDYGCFAELEEGVEGLVHVSEMDWTNKNIHPSK 322
Cdd:TIGR00717 237 VKVKVIKFDKEKGRISLSLKQLGEDPWEAIEKKFPVGDKITGRVTNLTDYGVFVEIEEGIEGLVHVSEMSWVKKNSHPSK 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374  323 VVQVGDEVEVMVLDIDEERRRISLGIKQCKSNPWEDFSGQFNKGDKISGTIKSITDFGIFIGLDGGIDGLVHLSDISWNE 402
Cdd:TIGR00717 317 VVKKGDEVEVMILDIDPERRRLSLGLKQCKANPWEQFEEKHPVGDRVTGKIKKITDFGAFVELEGGIDGLIHLSDISWDK 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374  403 VGEEAVRRFKKGDELDTVILSVDPERERISLGIKQLESDPFSEYVQENDKGAIVKGVVKEVDAKGAIITLANDIEATLKA 482
Cdd:TIGR00717 397 DGREADHLYKKGDEIEAVVLAVDKEKKRISLGVKQLTENPWEKFAAKYKVGSVVKGKVTEIKDFGAFVELPGGVEGLIRN 476
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|
gi 647806374  483 SEISRDRIEDARNVLKEGEEVEAKIISVDRKSRVIQLSIK 522
Cdd:TIGR00717 477 SELSENRDEDKTDEIKVGDEVEAKVVDIDKKNRKVSLSVK 516
RpsA COG0539
Ribosomal protein S1 [Translation, ribosomal structure and biogenesis]; Ribosomal protein S1 ...
1-352 0e+00

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: 573.91  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374   1 MSESFAELFEESLKtlNLQAGSIITGVIVDIDyqARWVTVHAGLKSEALIPLEQFYNDAGELSINVGDEVHVALDSVEDG 80
Cdd:COG0539    1 MSESFAELLEESLK--ELKEGDIVKGTVVSID--DDEVLVDIGYKSEGIIPLSEFSDEPGELEVKVGDEVEVYVEKVEDG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374  81 FGETKLSREKAKRAECWIVLEAAFAAEEVVKGVINGKVKGGFTVDVNGIRAFLPGSLVDVRPVRDTTHLEGKELEFKVIK 160
Cdd:COG0539   77 EGEIVLSKKKADREKAWEELEEAFENGEPVEGKVKGVVKGGLIVDIGGVRAFLPASQVDVRPVRDLDEYVGKTLEFKIIK 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374 161 LDQKRNNVVVSRRSVLEAENSAEREALLESLQEGQQVKGIVKNLTDYGAFVDLGGVDGLLHITDMAWKRIKHPSEIVNVG 240
Cdd:COG0539  157 LDRKRNNVVVSRRAVLEEEREEKREELLEKLEEGDVVEGTVKNITDFGAFVDLGGVDGLLHISEISWGRVKHPSEVLKVG 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374 241 DEIDVKVLKYDRERNRVSLGLKQLGEDPWVAIKARYPESTRVTARVTNLTDYGCFAELEEGVEGLVHVSEMDWTNKNIHP 320
Cdd:COG0539  237 DEVEVKVLKIDREKERISLSLKQLQPDPWENIAEKYPVGDVVKGKVTRLTDFGAFVELEPGVEGLVHISEMSWTKRVAHP 316
                        330       340       350
                 ....*....|....*....|....*....|..
gi 647806374 321 SKVVQVGDEVEVMVLDIDEERRRISLGIKQCK 352
Cdd:COG0539  317 SDVVKVGDEVEVKVLDIDPEERRISLSIKQLA 348
rpsA PRK06676
30S ribosomal protein S1; Reviewed
5-360 2.01e-114

30S ribosomal protein S1; Reviewed


Pssm-ID: 235851 [Multi-domain]  Cd Length: 390  Bit Score: 345.32  E-value: 2.01e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374   5 FAELFEESLKTLN-LQAGSIITGVIVDIDyqARWVTVH-AGLKSEALIPLEQFYNDA---GELSINVGDEVHVALDSVED 79
Cdd:PRK06676   1 MMEEFEESLNSVKeVEVGDVVTGEVLKVE--DKQVFVNiEGYKVEGVIPISELSNDHiedINDVVKVGDELEVYVLKVED 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374  80 GFGETKLSREKAKRAECWIVLEAAFAAEEVVKGVINGKVKGGFTVDVNGIRAFLPGSLVDVRPVRDTTHLEGKELEFKVI 159
Cdd:PRK06676  79 GEGNLLLSKRRLEAEKAWDKLEEKFEEGEVVEVKVTEVVKGGLVVDVEGVRGFIPASLISTRFVEDFSDFKGKTLEVKII 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374 160 KLDQKRNNVVVSRRSVLEAENSAEREALLESLQEGQQVKGIVKNLTDYGAFVDLGGVDGLLHITDMAWKRIKHPSEIVNV 239
Cdd:PRK06676 159 ELDPEKNRVILSRRAVVEEERAAKKEELLSSLKEGDVVEGTVARLTDFGAFVDIGGVDGLVHISELSHERVEKPSEVVSV 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374 240 GDEIDVKVLKYDRERNRVSLGLKQLGEDPWVAIKARYPESTRVTARVTNLTDYGCFAELEEGVEGLVHVSEMdwTNKNI- 318
Cdd:PRK06676 239 GQEVEVKVLSIDWETERISLSLKDTLPGPWEGVEEKLPEGDVIEGTVKRLTDFGAFVEVLPGVEGLVHISQI--SHKHIa 316
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 647806374 319 HPSKVVQVGDEVEVMVLDIDEERRRISLGIKQCKSNPWEDFS 360
Cdd:PRK06676 317 TPSEVLEEGQEVKVKVLEVNEEEKRISLSIKALEEAPAEEED 358
PRK00087 PRK00087
bifunctional 4-hydroxy-3-methylbut-2-enyl diphosphate reductase/30S ribosomal protein S1;
3-355 1.36e-110

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


Pssm-ID: 234623 [Multi-domain]  Cd Length: 647  Bit Score: 343.85  E-value: 1.36e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374   3 ESFAELFEESLKTLNLQAGSIITGVIVDIDYQArwVTVHAGLKSEALIPLEQF--YNDAGEL-SINVGDEVHVALDSVED 79
Cdd:PRK00087 285 EENEQLEYMNELEKQIRRGDIVKGTVVSVNENE--VFVDVGYKSEGVIPLRELtlDEISSLKeSVKVGDEIEVKVLKLED 362
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374  80 GFGETKLSREKAKRAECWIVLEAAFAAEEVVKGVINGKVKGGFTVDVNGIRAFLPGSLVDVRPVRDTTHLEGKELEFKVI 159
Cdd:PRK00087 363 EDGYVVLSKKEADREKAWKELEEAFENGEPVKGKVKEVVKGGLLVDYGGVRAFLPASHVELGYVEDLSEYKGQELEVKII 442
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374 160 KLD-QKRNNVVVSRRSVLEAENSAEREALLESLQEGQQVKGIVKNLTDYGAFVDLGGVDGLLHITDMAWKRIKHPSEIVN 238
Cdd:PRK00087 443 EFNrKRRKKVVLSRKAILEEEKEKKKEETWNSLEEGDVVEGEVKRLTDFGAFVDIGGVDGLLHVSEISWGRVEKPSDVLK 522
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374 239 VGDEIDVKVLKYDRERNRVSLGLKQLGEDPWVAIKARYPESTRVTARVTNLTDYGCFAELEEGVEGLVHVSEMDWtNKNI 318
Cdd:PRK00087 523 VGDEIKVYILDIDKENKKLSLSLKKLLPDPWENVEEKYPVGSIVLGKVVRIAPFGAFVELEPGVDGLVHISQISW-KRID 601
                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 647806374 319 HPSKVVQVGDEVEVMVLDIDEERRRISLGIKQCKSNP 355
Cdd:PRK00087 602 KPEDVLSEGEEVKAKILEVDPEEKRIRLSIKEVEEEP 638
rpsA PRK13806
30S ribosomal protein S1; Provisional
1-434 4.75e-109

30S ribosomal protein S1; Provisional


Pssm-ID: 237516 [Multi-domain]  Cd Length: 491  Bit Score: 335.16  E-value: 4.75e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374   1 MSESFAELFEESLKTLN--LQAGSIITGVIVDIDYQArwVTVHAGLKSEALIPLEQFYNDAGELSINVGDEVHVALDSVE 78
Cdd:PRK13806  13 ESESFAELLEAYEGERKteLRVGDKITGTVIAITEDS--VFVDTGSKVDGVVDRAELLDADGELTVAVGDEVELYVVSVN 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374  79 DGfgETKLSReKAKRAECWIVLEAAFAAEEVVKGVINGKVKGGFTVDVNGIRAFLPGSLVDVRPVRDTTHLEGKELEFKV 158
Cdd:PRK13806  91 GQ--EIRLSK-ALSGQGGAAMLEEAYENGVPVEGKVTGTCKGGFNVEVLGRRAFCPVSQIDLRYVEDPESYVGQTFQFLI 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374 159 IKLDQKRNNVVVSRRSVLEAENSAEREALLESLQEGQQVKGIVKNLTDYGAFVDLG-GVDGLLHITDMAWKRIKHPSEIV 237
Cdd:PRK13806 168 TRVEENGRNIVVSRRALLEREQKEALEAFMETVKEGDVVEGTVTRLAPFGAFVELApGVEGMVHISELSWSRVQKADEAV 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374 238 NVGDEIDVKVLKYDR----ERNRVSLGLKQLGEDPWVAIKARYPESTRVTARVTNLTDYGCFAELEEGVEGLVHVSEMDW 313
Cdd:PRK13806 248 SVGDTVRVKVLGIERakkgKGLRISLSIKQAGGDPWDTVGDRLKAGDKVTGKVVRLAPFGAFVEILPGIEGLVHVSEMSW 327
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374 314 TNKNIHPSKVVQVGDEVEVMVLDIDEERRRISLGIKQCKSNPWEDFSGQFNKGDKISGTIKSITDFGIFIGLDGGIDGLV 393
Cdd:PRK13806 328 TRRVNKPEDVVAPGDAVAVKIKDIDPAKRRISLSLRDAEGDPWADVAERFAPGTTVTGTVEKRAQFGLFVNLAPGVTGLL 407
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 647806374 394 HLSDISwNEVGEEAVRRFKKGDELDTVILSVDPERERISLG 434
Cdd:PRK13806 408 PASVIS-RAGKPATYEKLKPGDSVTLVVEEIDTAKRKISLA 447
PRK12269 PRK12269
bifunctional cytidylate kinase/ribosomal protein S1; Provisional
19-557 1.61e-99

bifunctional cytidylate kinase/ribosomal protein S1; Provisional


Pssm-ID: 105491 [Multi-domain]  Cd Length: 863  Bit Score: 320.89  E-value: 1.61e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374  19 QAGSIITGVIVDIDyqARWVTVHAGLKSEALIPLEQFyndagELSINVGDEVHVALDSVEDgFGeTKLSREKAKRAECWI 98
Cdd:PRK12269 320 EPGSVRMGTVVQVN--AGTVFVDIGGKSEGRVPVEEF-----EAPPKAGDGVRVYVERVTP-YG-PELSKTKADRLGLKV 390
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374  99 VLEAAFAAEEVVKGVIN--GKVKGGFTVDVN-GIRAFLPGSLVDVRPVRDTTHLEGKELEFKVIKLDQKR-----NNVVV 170
Cdd:PRK12269 391 KLRDAERDGTPVEGRIVrlTEKKSGFEVDLGaGMMAFLPISQSDCQKVDAPESLIGLTSKFYIERISQSKqhrgnDNIVI 470
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374 171 SRRSVLEAENSAEREALLESLQEGQQVKGIVKNLTDYGAFVDLGGVDGLLHITDMAWKRIKHPSEIVNVGDEIDVKVLKY 250
Cdd:PRK12269 471 NRRRYLEERARQAREEFFNSVHIEDSVSGVVKSFTSFGAFIDLGGFDGLLHVNDMSWGHVARPREFVKKGQTIELKVIRL 550
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374 251 DRERNRVSLGLKQLGEDPWVAIKARYPESTRVTARVTNLTDYGCFAELEEGVEGLVHVSEMDWTNKNIHPSKVVQVGDEV 330
Cdd:PRK12269 551 DQAEKRINLSLKHFQPDPWLEFENKFGVNDVVKGRVTKIADFGAFIELAEGIEGLAHISEFSWVKKTSKPSDMVKIGDEV 630
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374 331 EVMVLDIDEERRRISLGIKQCKSNPWEDFSGQFNKGDKISGTIKSITDFGIFIGLDGGIDGLVHLSDISWNEVGEEAVRR 410
Cdd:PRK12269 631 ECMILGYDIQAGRVSLGLKQVTANPWEEIEARYPVGARFTRRIVKVTNAGAFIEMEEGIDGFLHVDDLSWVKRTRPADHE 710
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374 411 FKKGDELDTVILSVDPERERISLGIKQLESDPFSEYVQENDKGAIVKGVVKEVDAKGAIITLANDIEATLKASEISRDRI 490
Cdd:PRK12269 711 LEVGKEIECMVIECDPQARRIRLGVKQLSDNPWQVFANAYGVGSTVEGEVSSVTDFGIFVRVPGGVEGLVRKQHLVENRD 790
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374 491 EDARNVLKE---GEEVEAKIISVDRKSRVIQLSIKSKDVEDEKEAIQSLRDKPAASDiaAGPTTLGDLLR 557
Cdd:PRK12269 791 GDPGEALRKyavGDRVKAVIVDMNVKDRKVAFSVRDYQRKVQRDELSRYMSAPRGED--EGSFTLGDLMR 858
rpsA PRK07899
30S ribosomal protein S1; Reviewed
3-350 5.24e-93

30S ribosomal protein S1; Reviewed


Pssm-ID: 236126 [Multi-domain]  Cd Length: 486  Bit Score: 293.49  E-value: 5.24e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374   3 ESFAELFEESLKTLNlqAGSIITGVIVDIDYQArwVTVHAGLKSEALIPleqfyndAGELSI----------NVGDEVHV 72
Cdd:PRK07899  20 EDFLAAIDKTIKYFN--DGDIVEGTVVKVDRDE--VLLDIGYKTEGVIP-------SRELSIkhdvdpnevvEVGDEVEA 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374  73 ALDSVEDGFGETKLSREKAKRAECWIVLEAAFAAEEVVKGVINGKVKGGFTVDVnGIRAFLPGSLVDVRPVRDTTHLEGK 152
Cdd:PRK07899  89 LVLQKEDKEGRLILSKKRAQYERAWGTIEKIKEKDGVVTGTVIEVVKGGLILDI-GLRGFLPASLVEMRRVRDLQPYIGQ 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374 153 ELEFKVIKLDQKRNNVVVSRRSVLEAENSAEREALLESLQEGQQVKGIVKNLTDYGAFVDLGGVDGLLHITDMAWKRIKH 232
Cdd:PRK07899 168 EIEAKIIELDKNRNNVVLSRRAWLEQTQSEVRSEFLNQLQKGQVRKGVVSSIVNFGAFVDLGGVDGLVHVSELSWKHIDH 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374 233 PSEIVNVGDEIDVKVLKYDRERNRVSLGLKQLGEDPWVAIKARYPESTRVTARVTNLTDYGCFAELEEGVEGLVHVSEMD 312
Cdd:PRK07899 248 PSEVVEVGQEVTVEVLDVDMDRERVSLSLKATQEDPWQQFARTHAIGQIVPGKVTKLVPFGAFVRVEEGIEGLVHISELA 327
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 647806374 313 WTNKNIhPSKVVQVGDEVEVMVLDIDEERRRISLGIKQ 350
Cdd:PRK07899 328 ERHVEV-PEQVVQVGDEVFVKVIDIDLERRRISLSLKQ 364
S1_RPS1_repeat_ec4 cd05689
S1_RPS1_repeat_ec4: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
276-347 1.86e-40

S1_RPS1_repeat_ec4: 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 (ec4) 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: 240194 [Multi-domain]  Cd Length: 72  Bit Score: 140.79  E-value: 1.86e-40
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 647806374 276 YPESTRVTARVTNLTDYGCFAELEEGVEGLVHVSEMDWTNKNIHPSKVVQVGDEVEVMVLDIDEERRRISLG 347
Cdd:cd05689    1 YPEGTRLFGKVTNLTDYGCFVELEEGVEGLVHVSEMDWTNKNIHPSKVVSLGDEVEVMVLDIDEERRRISLG 72
S1_RPS1_repeat_ec3 cd05688
S1_RPS1_repeat_ec3: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
193-260 4.36e-36

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: 128.90  E-value: 4.36e-36
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 647806374 193 EGQQVKGIVKNLTDYGAFVDLGGVDGLLHITDMAWKRIKHPSEIVNVGDEIDVKVLKYDRERNRVSLG 260
Cdd:cd05688    1 EGDVVEGTVKSITDFGAFVDLGGVDGLLHISDMSWGRVKHPSEVVNVGDEVEVKVLKIDKERKRISLG 68
S1_RPS1_repeat_ec5 cd05690
S1_RPS1_repeat_ec5: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
366-434 3.30e-30

S1_RPS1_repeat_ec5: 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 5 (ec5) 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: 240195 [Multi-domain]  Cd Length: 69  Bit Score: 112.59  E-value: 3.30e-30
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 647806374 366 GDKISGTIKSITDFGIFIGLDGGIDGLVHLSDISWNEVGEEAVRRFKKGDELDTVILSVDPERERISLG 434
Cdd:cd05690    1 GTVVSGKIKSITDFGIFVGLDGGIDGLVHISDISWTQRVRHPSEIYKKGQEVEAVVLNIDVERERISLG 69
PRK07400 PRK07400
30S ribosomal protein S1; Reviewed
3-268 8.65e-30

30S ribosomal protein S1; Reviewed


Pssm-ID: 180960 [Multi-domain]  Cd Length: 318  Bit Score: 119.52  E-value: 8.65e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374   3 ESFAELFEESlkTLNLQAGSIITGVIVDIdyQARWVTVHAGLKSEALIPLEqfyndagELSINVGDEVHVAL-------- 74
Cdd:PRK07400  16 EDFAALLDKY--DYHFKPGDIVNGTVFSL--EPRGALIDIGAKTAAFMPIQ-------EMSINRVEGPEEVLqpnetref 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374  75 ----DSVEDGFGETKLSREKAKRAecWIVLEAAFAAEEVVKGVINGKVKGGFTVDVNGIRAFLPGSLVDVRPVRDttHLE 150
Cdd:PRK07400  85 filsDENEDGQLTLSIRRIEYMRA--WERVRQLQKEDATVRSEVFATNRGGALVRIEGLRGFIPGSHISTRKPKE--ELV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374 151 GKELEFKVIKLDQKRNNVVVSRRSVLeaensAEREalLESLQEGQQVKGIVKNLTDYGAFVDLGGVDGLLHITDMAWKRI 230
Cdd:PRK07400 161 GEELPLKFLEVDEERNRLVLSHRRAL-----VERK--MNRLEVGEVVVGTVRGIKPYGAFIDIGGVSGLLHISEISHEHI 233
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 647806374 231 KHPSEIVNVGDEIDVKVLKYDRERNRVSLGLKQLGEDP 268
Cdd:PRK07400 234 ETPHSVFNVNDEMKVMIIDLDAERGRISLSTKQLEPEP 271
S1_RPS1_repeat_ec6 cd05691
S1_RPS1_repeat_ec6: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
453-525 8.16e-29

S1_RPS1_repeat_ec6: 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 6 (ec6) 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: 240196 [Multi-domain]  Cd Length: 73  Bit Score: 108.90  E-value: 8.16e-29
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 647806374 453 GAIVKGVVKEVDAKGAIITLANDIEATLKASEISRDRIEDARNVLKEGEEVEAKIISVDRKSRVIQLSIKSKD 525
Cdd:cd05691    1 GSIVTGKVTEVDAKGATVKLGDGVEGFLRAAELSRDRVEDATERFKVGDEVEAKITNVDRKNRKISLSIKAKE 73
S1_RPS1_repeat_ec2_hs2 cd04465
S1_RPS1_repeat_ec2_hs2: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
107-173 4.15e-28

S1_RPS1_repeat_ec2_hs2: 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 2 of the Escherichia coli and Homo sapiens RPS1 (ec2 and hs2, respectively). Autoantibodies to double-stranded DNA from patients with systemic lupus erythematosus cross-react with the human RPS1 homolog.


Pssm-ID: 239911 [Multi-domain]  Cd Length: 67  Bit Score: 106.77  E-value: 4.15e-28
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 647806374 107 EEVVKGVINGKVKGGFTVDVNGIRAFLPGSLVDVRPVRDTTHLEGKELEFKVIKLDQKRNNVVVSRR 173
Cdd:cd04465    1 GEIVEGKVTEKVKGGLIVDIEGVRAFLPASQVDLRPVEDLDEYVGKELKFKIIEIDRERNNIVLSRR 67
Tex COG2183
Transcriptional accessory protein Tex/SPT6 [Transcription];
188-268 3.50e-21

Transcriptional accessory protein Tex/SPT6 [Transcription];


Pssm-ID: 441786 [Multi-domain]  Cd Length: 719  Bit Score: 97.79  E-value: 3.50e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374 188 LESLQEGQQVKGIVKNLTDYGAFVDLGgV--DGLLHITDMAWKRIKHPSEIVNVGDEIDVKVLKYDRERNRVSLGLKQLG 265
Cdd:COG2183  636 IEDLKPGMILEGTVTNVTDFGAFVDIG-VhqDGLVHISQLSDRFVKDPREVVKVGDIVKVKVLEVDLKRKRISLSMKLDD 714

                 ...
gi 647806374 266 EDP 268
Cdd:COG2183  715 EAG 717
S1_RPS1_repeat_ec3 cd05688
S1_RPS1_repeat_ec3: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
365-434 4.04e-20

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: 84.22  E-value: 4.04e-20
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374 365 KGDKISGTIKSITDFGIFIGLdGGIDGLVHLSDISWNEVgEEAVRRFKKGDELDTVILSVDPERERISLG 434
Cdd:cd05688    1 EGDVVEGTVKSITDFGAFVDL-GGVDGLLHISDMSWGRV-KHPSEVVNVGDEVEVKVLKIDKERKRISLG 68
S1 smart00316
Ribosomal protein S1-like RNA-binding domain;
192-262 2.06e-19

Ribosomal protein S1-like RNA-binding domain;


Pssm-ID: 197648 [Multi-domain]  Cd Length: 72  Bit Score: 82.27  E-value: 2.06e-19
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 647806374   192 QEGQQVKGIVKNLTDYGAFVDLG-GVDGLLHITDMAWKRIKHPSEIVNVGDEIDVKVLKYDRERNRVSLGLK 262
Cdd:smart00316   1 EVGDVVEGTVTEITPGGAFVDLGnGVEGLIPISELSDKRVKDPEEVLKVGDEVKVKVLSVDEEKGRIILSLK 72
S1_RPS1_repeat_ec5 cd05690
S1_RPS1_repeat_ec5: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
194-260 2.56e-19

S1_RPS1_repeat_ec5: 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 5 (ec5) 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: 240195 [Multi-domain]  Cd Length: 69  Bit Score: 82.16  E-value: 2.56e-19
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 647806374 194 GQQVKGIVKNLTDYGAFVDL-GGVDGLLHITDMAW-KRIKHPSEIVNVGDEIDVKVLKYDRERNRVSLG 260
Cdd:cd05690    1 GTVVSGKIKSITDFGIFVGLdGGIDGLVHISDISWtQRVRHPSEIYKKGQEVEAVVLNIDVERERISLG 69
S1_RPS1_repeat_ec5 cd05690
S1_RPS1_repeat_ec5: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
280-347 3.11e-19

S1_RPS1_repeat_ec5: 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 5 (ec5) 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: 240195 [Multi-domain]  Cd Length: 69  Bit Score: 81.77  E-value: 3.11e-19
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 647806374 280 TRVTARVTNLTDYGCFAELEEGVEGLVHVSEMDWTNKNIHPSKVVQVGDEVEVMVLDIDEERRRISLG 347
Cdd:cd05690    2 TVVSGKIKSITDFGIFVGLDGGIDGLVHISDISWTQRVRHPSEIYKKGQEVEAVVLNIDVERERISLG 69
S1_Tex cd05685
S1_Tex: The C-terminal S1 domain of a transcription accessory factor called Tex, which has ...
194-259 1.10e-18

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: 80.35  E-value: 1.10e-18
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 647806374 194 GQQVKGIVKNLTDYGAFVDLG-GVDGLLHITDMAWKRIKHPSEIVNVGDEIDVKVLKYDRERNRVSL 259
Cdd:cd05685    1 GMVLEGVVTNVTDFGAFVDIGvKQDGLIHISKMADRFVSHPSDVVSVGDIVEVKVISIDEERGRISL 67
Pnp COG1185
Polyribonucleotide nucleotidyltransferase (polynucleotide phosphorylase) [Translation, ...
185-262 1.35e-18

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


Pssm-ID: 440798 [Multi-domain]  Cd Length: 686  Bit Score: 89.29  E-value: 1.35e-18
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 647806374 185 EALLESLQEGQQVKGIVKNLTDYGAFVD-LGGVDGLLHITDMAWKRIKHPSEIVNVGDEIDVKVLKYDReRNRVSLGLK 262
Cdd:COG1185  608 EGITAEPEVGEIYEGKVVRIMDFGAFVEiLPGKDGLVHISELADERVEKVEDVLKEGDEVKVKVLEIDD-QGRIKLSRK 685
PRK11824 PRK11824
polynucleotide phosphorylase/polyadenylase; Provisional
185-264 1.14e-17

polynucleotide phosphorylase/polyadenylase; Provisional


Pssm-ID: 236995 [Multi-domain]  Cd Length: 693  Bit Score: 86.64  E-value: 1.14e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374 185 EALLESLQEGQQVKGIVKNLTDYGAFVD-LGGVDGLLHITDMAWKRIKHPSEIVNVGDEIDVKVLKYDrERNRVSLGLKQ 263
Cdd:PRK11824 613 EGITAEPEVGEIYEGKVVRIVDFGAFVEiLPGKDGLVHISEIADERVEKVEDVLKEGDEVKVKVLEID-KRGRIRLSRKA 691

                 .
gi 647806374 264 L 264
Cdd:PRK11824 692 V 692
S1_like cd00164
S1_like: Ribosomal protein S1-like RNA-binding domain. Found in a wide variety of ...
282-347 1.73e-17

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: 76.65  E-value: 1.73e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 647806374 282 VTARVTNLTDYGCFAELEEGVEGLVHVSEMDWTnKNIHPSKVVQVGDEVEVMVLDIDEERRRISLG 347
Cdd:cd00164    1 VTGKVVSITKFGVFVELEDGVEGLVHISELSDK-FVKDPSEVFKVGDEVEVKVLEVDPEKGRISLS 65
S1 smart00316
Ribosomal protein S1-like RNA-binding domain;
280-349 4.94e-17

Ribosomal protein S1-like RNA-binding domain;


Pssm-ID: 197648 [Multi-domain]  Cd Length: 72  Bit Score: 75.72  E-value: 4.94e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374   280 TRVTARVTNLTDYGCFAELEEGVEGLVHVSEMDWtNKNIHPSKVVQVGDEVEVMVLDIDEERRRISLGIK 349
Cdd:smart00316   4 DVVEGTVTEITPGGAFVDLGNGVEGLIPISELSD-KRVKDPEEVLKVGDEVKVKVLSVDEEKGRIILSLK 72
S1_like cd00164
S1_like: Ribosomal protein S1-like RNA-binding domain. Found in a wide variety of ...
197-260 9.91e-17

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: 74.72  E-value: 9.91e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 647806374 197 VKGIVKNLTDYGAFVDLG-GVDGLLHITDMAWKRIKHPSEIVNVGDEIDVKVLKYDRERNRVSLG 260
Cdd:cd00164    1 VTGKVVSITKFGVFVELEdGVEGLVHISELSDKFVKDPSEVFKVGDEVEVKVLEVDPEKGRISLS 65
PRK07400 PRK07400
30S ribosomal protein S1; Reviewed
194-442 2.36e-16

30S ribosomal protein S1; Reviewed


Pssm-ID: 180960 [Multi-domain]  Cd Length: 318  Bit Score: 80.23  E-value: 2.36e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374 194 GQQVKGIVKNLTDYGAFVDLGG-VDGLLHITDMAWKRIKHPSEIVNVGDEIDVKVLKYDRERNRVSLGLKQLG-EDPWVA 271
Cdd:PRK07400  32 GDIVNGTVFSLEPRGALIDIGAkTAAFMPIQEMSINRVEGPEEVLQPNETREFFILSDENEDGQLTLSIRRIEyMRAWER 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374 272 IKARYPESTRVTARVTNLTDYGCFAELEeGVEGLV---HVSemdwTNKnihpSKVVQVGDEVEVMVLDIDEERRRISLGI 348
Cdd:PRK07400 112 VRQLQKEDATVRSEVFATNRGGALVRIE-GLRGFIpgsHIS----TRK----PKEELVGEELPLKFLEVDEERNRLVLSH 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374 349 KQC----KSNPWEdfsgqfnKGDKISGTIKSITDFGIFIGLdGGIDGLVHLSDISWNEVgEEAVRRFKKGDELDTVILSV 424
Cdd:PRK07400 183 RRAlverKMNRLE-------VGEVVVGTVRGIKPYGAFIDI-GGVSGLLHISEISHEHI-ETPHSVFNVNDEMKVMIIDL 253
                        250
                 ....*....|....*...
gi 647806374 425 DPERERISLGIKQLESDP 442
Cdd:PRK07400 254 DAERGRISLSTKQLEPEP 271
S1_RPS1_repeat_ec4 cd05689
S1_RPS1_repeat_ec4: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
193-260 2.87e-16

S1_RPS1_repeat_ec4: 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 (ec4) 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: 240194 [Multi-domain]  Cd Length: 72  Bit Score: 73.38  E-value: 2.87e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 647806374 193 EGQQVKGIVKNLTDYGAFVDLG-GVDGLLHITDMAW--KRIkHPSEIVNVGDEIDVKVLKYDRERNRVSLG 260
Cdd:cd05689    3 EGTRLFGKVTNLTDYGCFVELEeGVEGLVHVSEMDWtnKNI-HPSKVVSLGDEVEVMVLDIDEERRRISLG 72
YabR COG1098
Predicted RNA-binding protein, contains ribosomal protein S1 (RPS1) domain [General function ...
281-369 4.40e-16

Predicted RNA-binding protein, contains ribosomal protein S1 (RPS1) domain [General function prediction only];


Pssm-ID: 440715 [Multi-domain]  Cd Length: 130  Bit Score: 74.83  E-value: 4.40e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374 281 RVTARVTNLTDYGCFAELEEGVEGLVHVSEMdwTN---KNIHpsKVVQVGDEVEVMVLDIDeERRRISLGIKQCKSNPWE 357
Cdd:COG1098    8 IVEGKVTGITPFGAFVELPEGTTGLVHISEI--ADgyvKDIN--DYLKVGDEVKVKVLSID-EDGKISLSIKQAEEKPKR 82
                         90
                 ....*....|..
gi 647806374 358 DFSGQFNKGDKI 369
Cdd:COG1098   83 PPRPRRNSRPKA 94
S1_Rrp5_repeat_sc12 cd05708
S1_Rrp5_repeat_sc12: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ...
366-436 6.68e-16

S1_Rrp5_repeat_sc12: 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 S. cerevisiae S1 repeat 12 (sc12). Rrp5 is found in eukaryotes but not in prokaryotes or archaea.


Pssm-ID: 240213 [Multi-domain]  Cd Length: 77  Bit Score: 72.75  E-value: 6.68e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 647806374 366 GDKISGTIKSITDFGIFIGLDG-GIDGLVHLSDISWNEVgEEAVRRFKKGDELDTVILSVDPERERISLGIK 436
Cdd:cd05708    3 GQKIDGTVRRVEDYGVFIDIDGtNVSGLCHKSEISDNRV-ADASKLFRVGDKVRAKVLKIDAEKKRISLGLK 73
S1_Rrp5_repeat_sc12 cd05708
S1_Rrp5_repeat_sc12: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ...
193-262 1.41e-15

S1_Rrp5_repeat_sc12: 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 S. cerevisiae S1 repeat 12 (sc12). Rrp5 is found in eukaryotes but not in prokaryotes or archaea.


Pssm-ID: 240213 [Multi-domain]  Cd Length: 77  Bit Score: 71.59  E-value: 1.41e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 647806374 193 EGQQVKGIVKNLTDYGAFVDLGGVD--GLLHITDMAWKRIKHPSEIVNVGDEIDVKVLKYDRERNRVSLGLK 262
Cdd:cd05708    2 VGQKIDGTVRRVEDYGVFIDIDGTNvsGLCHKSEISDNRVADASKLFRVGDKVRAKVLKIDAEKKRISLGLK 73
S1 pfam00575
S1 RNA binding domain; The S1 domain occurs in a wide range of RNA associated proteins. It is ...
191-261 1.81e-15

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: 71.16  E-value: 1.81e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 647806374  191 LQEGQQVKGIVKNLTDYGAFVDLG-GVDGLLHITDMAWKRIKHPSEIVNVGDEIDVKVLKYDRERNRVSLGL 261
Cdd:pfam00575   1 PEKGDVVEGEVTRVTKGGAFVDLGnGVEGFIPISELSDDHVEDPDEVIKVGDEVKVKVLKVDKDRRRIILSI 72
PRK08059 PRK08059
general stress protein 13; Validated
282-357 1.87e-15

general stress protein 13; Validated


Pssm-ID: 181215 [Multi-domain]  Cd Length: 123  Bit Score: 72.77  E-value: 1.87e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 647806374 282 VTARVTNLTDYGCFAELEEGVEGLVHVSEMdwTN---KNIHpsKVVQVGDEVEVMVLDIDEERRRISLGIKQCKSNPWE 357
Cdd:PRK08059  11 VTGKVTGIQPYGAFVALDEETQGLVHISEI--THgfvKDIH--DFLSVGDEVKVKVLSVDEEKGKISLSIRATEEAPEA 85
S1 smart00316
Ribosomal protein S1-like RNA-binding domain;
452-522 2.24e-15

Ribosomal protein S1-like RNA-binding domain;


Pssm-ID: 197648 [Multi-domain]  Cd Length: 72  Bit Score: 71.10  E-value: 2.24e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 647806374   452 KGAIVKGVVKEVDAKGAIITLANDIEATLKASEISRDRIEDARNVLKEGEEVEAKIISVDRKSRVIQLSIK 522
Cdd:smart00316   2 VGDVVEGTVTEITPGGAFVDLGNGVEGLIPISELSDKRVKDPEEVLKVGDEVKVKVLSVDEEKGRIILSLK 72
S1_Tex cd05685
S1_Tex: The C-terminal S1 domain of a transcription accessory factor called Tex, which has ...
280-346 2.62e-15

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: 70.72  E-value: 2.62e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 647806374 280 TRVTARVTNLTDYGCFAELEEGVEGLVHVSEMdwTNKNI-HPSKVVQVGDEVEVMVLDIDEERRRISL 346
Cdd:cd05685    2 MVLEGVVTNVTDFGAFVDIGVKQDGLIHISKM--ADRFVsHPSDVVSVGDIVEVKVISIDEERGRISL 67
Tex COG2183
Transcriptional accessory protein Tex/SPT6 [Transcription];
286-350 8.66e-15

Transcriptional accessory protein Tex/SPT6 [Transcription];


Pssm-ID: 441786 [Multi-domain]  Cd Length: 719  Bit Score: 77.37  E-value: 8.66e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 647806374 286 VTNLTDYGCFAELeeGV--EGLVHVSEMdwTNKNI-HPSKVVQVGDEVEVMVLDIDEERRRISLGIKQ 350
Cdd:COG2183  649 VTNVTDFGAFVDI--GVhqDGLVHISQL--SDRFVkDPREVVKVGDIVKVKVLEVDLKRKRISLSMKL 712
S1_RPS1_repeat_hs4 cd05692
S1_RPS1_repeat_hs4: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
194-262 1.11e-14

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: 68.85  E-value: 1.11e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374 194 GQQVKGIVKNLTDYGAFVDLG-GVDGLLHITDMAWKRIKHPSEIVNVGDEIDVKVLKYDrERNRVSLGLK 262
Cdd:cd05692    1 GSVVEGTVTRLKPFGAFVELGgGISGLVHISQIAHKRVKDVKDVLKEGDKVKVKVLSID-ARGRISLSIK 69
S1 smart00316
Ribosomal protein S1-like RNA-binding domain;
364-436 1.41e-14

Ribosomal protein S1-like RNA-binding domain;


Pssm-ID: 197648 [Multi-domain]  Cd Length: 72  Bit Score: 68.78  E-value: 1.41e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 647806374   364 NKGDKISGTIKSITDFGIFIGLDGGIDGLVHLSDISWNEVgEEAVRRFKKGDELDTVILSVDPERERISLGIK 436
Cdd:smart00316   1 EVGDVVEGTVTEITPGGAFVDLGNGVEGLIPISELSDKRV-KDPEEVLKVGDEVKVKVLSVDEEKGRIILSLK 72
S1 pfam00575
S1 RNA binding domain; The S1 domain occurs in a wide range of RNA associated proteins. It is ...
363-435 2.80e-14

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: 67.70  E-value: 2.80e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 647806374  363 FNKGDKISGTIKSITDFGIFIGLDGGIDGLVHLSDISWNEVgEEAVRRFKKGDELDTVILSVDPERERISLGI 435
Cdd:pfam00575   1 PEKGDVVEGEVTRVTKGGAFVDLGNGVEGFIPISELSDDHV-EDPDEVIKVGDEVKVKVLKVDKDRRRIILSI 72
S1 pfam00575
S1 RNA binding domain; The S1 domain occurs in a wide range of RNA associated proteins. It is ...
280-348 5.13e-14

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: 66.93  E-value: 5.13e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 647806374  280 TRVTARVTNLTDYGCFAELEEGVEGLVHVSEMDWtNKNIHPSKVVQVGDEVEVMVLDIDEERRRISLGI 348
Cdd:pfam00575   5 DVVEGEVTRVTKGGAFVDLGNGVEGFIPISELSD-DHVEDPDEVIKVGDEVKVKVLKVDKDRRRIILSI 72
YabR COG1098
Predicted RNA-binding protein, contains ribosomal protein S1 (RPS1) domain [General function ...
189-281 6.35e-14

Predicted RNA-binding protein, contains ribosomal protein S1 (RPS1) domain [General function prediction only];


Pssm-ID: 440715 [Multi-domain]  Cd Length: 130  Bit Score: 68.67  E-value: 6.35e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374 189 ESLQEGQQVKGIVKNLTDYGAFVDL-GGVDGLLHITDMAWKRIKHPSEIVNVGDEIDVKVLKYDrERNRVSLGLKQLGED 267
Cdd:COG1098    1 MSIEVGDIVEGKVTGITPFGAFVELpEGTTGLVHISEIADGYVKDINDYLKVGDEVKVKVLSID-EDGKISLSIKQAEEK 79
                         90
                 ....*....|....
gi 647806374 268 PWVAIKARYPESTR 281
Cdd:COG1098   80 PKRPPRPRRNSRPK 93
S1_RPS1_repeat_hs4 cd05692
S1_RPS1_repeat_hs4: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
282-349 8.27e-14

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: 66.54  E-value: 8.27e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 647806374 282 VTARVTNLTDYGCFAELEEGVEGLVHVSEMdwTNKNI-HPSKVVQVGDEVEVMVLDIDeERRRISLGIK 349
Cdd:cd05692    4 VEGTVTRLKPFGAFVELGGGISGLVHISQI--AHKRVkDVKDVLKEGDKVKVKVLSID-ARGRISLSIK 69
S1_PNPase cd04472
S1_PNPase: Polynucleotide phosphorylase (PNPase), ), S1-like RNA-binding domain. PNPase is a ...
194-259 1.68e-13

S1_PNPase: Polynucleotide phosphorylase (PNPase), ), S1-like RNA-binding domain. PNPase is a polyribonucleotide nucleotidyl transferase that degrades mRNA. It is a trimeric multidomain protein. The C-terminus contains the S1 domain which binds ssRNA. This family is classified based on the S1 domain. PNPase nonspecifically removes the 3' nucleotides from mRNA, but is stalled by double-stranded RNA structures such as a stem-loop. Evidence shows that a minimum of 7-10 unpaired nucleotides at the 3' end, is required for PNPase degradation. It is suggested that PNPase also dephosphorylates the RNA 5' end. This additional activity may regulate the 5'-dependent activity of RNaseE in vivo.


Pssm-ID: 239918 [Multi-domain]  Cd Length: 68  Bit Score: 65.26  E-value: 1.68e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 647806374 194 GQQVKGIVKNLTDYGAFVD-LGGVDGLLHITDMAWKRIKHPSEIVNVGDEIDVKVLKYDrERNRVSL 259
Cdd:cd04472    1 GKIYEGKVVKIKDFGAFVEiLPGKDGLVHISELSDERVEKVEDVLKVGDEVKVKVIEVD-DRGRISL 66
S1_DHX8_helicase cd05684
S1_DHX8_helicase: The N-terminal S1 domain of human ATP-dependent RNA helicase DHX8, a DEAH ...
285-349 3.17e-13

S1_DHX8_helicase: The N-terminal S1 domain of human ATP-dependent RNA helicase DHX8, a DEAH (Asp-Glu-Ala-His) box polypeptide. The DEAH-box RNA helicases are thought to play key roles in pre-mRNA splicing and DHX8 facilitates nuclear export of spliced mRNA by releasing the RNA from the spliceosome. DHX8 is also known as HRH1 (human RNA helicase 1) in Homo sapiens and PRP22 in Saccharomyces cerevisiae.


Pssm-ID: 240189 [Multi-domain]  Cd Length: 79  Bit Score: 64.95  E-value: 3.17e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 647806374 285 RVTNLTDYGCFAELE---EGVEGLVHVSEMDWTNKNIHPSKVVQVGDEVEVMVLDIdeERRRISLGIK 349
Cdd:cd05684    7 KVTSIMDFGCFVQLEglkGRKEGLVHISQLSFEGRVANPSDVVKRGQKVKVKVISI--QNGKISLSMK 72
YabR COG1098
Predicted RNA-binding protein, contains ribosomal protein S1 (RPS1) domain [General function ...
366-442 3.67e-13

Predicted RNA-binding protein, contains ribosomal protein S1 (RPS1) domain [General function prediction only];


Pssm-ID: 440715 [Multi-domain]  Cd Length: 130  Bit Score: 66.36  E-value: 3.67e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 647806374 366 GDKISGTIKSITDFGIFIGLDGGIDGLVHLSDISWNEVGEeaVRRF-KKGDELDTVILSVDpERERISLGIKQLESDP 442
Cdd:COG1098    6 GDIVEGKVTGITPFGAFVELPEGTTGLVHISEIADGYVKD--INDYlKVGDEVKVKVLSID-EDGKISLSIKQAEEKP 80
PRK11824 PRK11824
polynucleotide phosphorylase/polyadenylase; Provisional
283-349 6.01e-13

polynucleotide phosphorylase/polyadenylase; Provisional


Pssm-ID: 236995 [Multi-domain]  Cd Length: 693  Bit Score: 71.62  E-value: 6.01e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 647806374 283 TARVTNLTDYGCFAELEEGVEGLVHVSEMDWTNKNiHPSKVVQVGDEVEVMVLDIDeERRRISLGIK 349
Cdd:PRK11824 626 EGKVVRIVDFGAFVEILPGKDGLVHISEIADERVE-KVEDVLKEGDEVKVKVLEID-KRGRIRLSRK 690
PRK08059 PRK08059
general stress protein 13; Validated
187-268 1.33e-12

general stress protein 13; Validated


Pssm-ID: 181215 [Multi-domain]  Cd Length: 123  Bit Score: 64.68  E-value: 1.33e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374 187 LLESLQEGQQVKGIVKNLTDYGAFVDL-GGVDGLLHITDMAWKRIKHPSEIVNVGDEIDVKVLKYDRERNRVSLGLKQLG 265
Cdd:PRK08059   1 MMSQYEVGSVVTGKVTGIQPYGAFVALdEETQGLVHISEITHGFVKDIHDFLSVGDEVKVKVLSVDEEKGKISLSIRATE 80

                 ...
gi 647806374 266 EDP 268
Cdd:PRK08059  81 EAP 83
PRK08582 PRK08582
RNA-binding protein S1;
280-355 5.37e-12

RNA-binding protein S1;


Pssm-ID: 236305 [Multi-domain]  Cd Length: 139  Bit Score: 63.51  E-value: 5.37e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 647806374 280 TRVTARVTNLTDYGCFAELEEGVEGLVHVSEM-DWTNKNIHpsKVVQVGDEVEVMVLDIDEErRRISLGIKQCKSNP 355
Cdd:PRK08582   7 SKLQGKVTGITNFGAFVELPEGKTGLVHISEVaDNYVKDIN--DHLKVGDEVEVKVLNVEDD-GKIGLSIKKAKDRP 80
S1_RPS1_repeat_ec4 cd05689
S1_RPS1_repeat_ec4: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
363-434 7.48e-12

S1_RPS1_repeat_ec4: 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 (ec4) 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: 240194 [Multi-domain]  Cd Length: 72  Bit Score: 61.05  E-value: 7.48e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 647806374 363 FNKGDKISGTIKSITDFGIFIGLDGGIDGLVHLSDISWNEVGEEAVRRFKKGDELDTVILSVDPERERISLG 434
Cdd:cd05689    1 YPEGTRLFGKVTNLTDYGCFVELEEGVEGLVHVSEMDWTNKNIHPSKVVSLGDEVEVMVLDIDEERRRISLG 72
S1_RPS1_repeat_hs4 cd05692
S1_RPS1_repeat_hs4: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
453-522 1.74e-11

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: 59.61  E-value: 1.74e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374 453 GAIVKGVVKEVDAKGAIITLANDIEATLKASEISRDRIEDARNVLKEGEEVEAKIISVDRKSRvIQLSIK 522
Cdd:cd05692    1 GSVVEGTVTRLKPFGAFVELGGGISGLVHISQIAHKRVKDVKDVLKEGDKVKVKVLSIDARGR-ISLSIK 69
S1_like cd00164
S1_like: Ribosomal protein S1-like RNA-binding domain. Found in a wide variety of ...
369-434 2.39e-11

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: 59.32  E-value: 2.39e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 647806374 369 ISGTIKSITDFGIFIGLDGGIDGLVHLSDISWNEVGEEAvRRFKKGDELDTVILSVDPERERISLG 434
Cdd:cd00164    1 VTGKVVSITKFGVFVELEDGVEGLVHISELSDKFVKDPS-EVFKVGDEVEVKVLEVDPEKGRISLS 65
S1_RPS1_repeat_hs4 cd05692
S1_RPS1_repeat_hs4: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
366-436 2.50e-11

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: 59.22  E-value: 2.50e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 647806374 366 GDKISGTIKSITDFGIFIGLDGGIDGLVHLSDISWNEVgeEAVRRF-KKGDELDTVILSVDpERERISLGIK 436
Cdd:cd05692    1 GSVVEGTVTRLKPFGAFVELGGGISGLVHISQIAHKRV--KDVKDVlKEGDKVKVKVLSID-ARGRISLSIK 69
S1_PNPase cd04472
S1_PNPase: Polynucleotide phosphorylase (PNPase), ), S1-like RNA-binding domain. PNPase is a ...
285-346 4.01e-11

S1_PNPase: Polynucleotide phosphorylase (PNPase), ), S1-like RNA-binding domain. PNPase is a polyribonucleotide nucleotidyl transferase that degrades mRNA. It is a trimeric multidomain protein. The C-terminus contains the S1 domain which binds ssRNA. This family is classified based on the S1 domain. PNPase nonspecifically removes the 3' nucleotides from mRNA, but is stalled by double-stranded RNA structures such as a stem-loop. Evidence shows that a minimum of 7-10 unpaired nucleotides at the 3' end, is required for PNPase degradation. It is suggested that PNPase also dephosphorylates the RNA 5' end. This additional activity may regulate the 5'-dependent activity of RNaseE in vivo.


Pssm-ID: 239918 [Multi-domain]  Cd Length: 68  Bit Score: 58.71  E-value: 4.01e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 647806374 285 RVTNLTDYGCFAELEEGVEGLVHVSEMDwtNKNI-HPSKVVQVGDEVEVMVLDIDeERRRISL 346
Cdd:cd04472    7 KVVKIKDFGAFVEILPGKDGLVHISELS--DERVeKVEDVLKVGDEVKVKVIEVD-DRGRISL 66
S1_DHX8_helicase cd05684
S1_DHX8_helicase: The N-terminal S1 domain of human ATP-dependent RNA helicase DHX8, a DEAH ...
194-262 6.04e-11

S1_DHX8_helicase: The N-terminal S1 domain of human ATP-dependent RNA helicase DHX8, a DEAH (Asp-Glu-Ala-His) box polypeptide. The DEAH-box RNA helicases are thought to play key roles in pre-mRNA splicing and DHX8 facilitates nuclear export of spliced mRNA by releasing the RNA from the spliceosome. DHX8 is also known as HRH1 (human RNA helicase 1) in Homo sapiens and PRP22 in Saccharomyces cerevisiae.


Pssm-ID: 240189 [Multi-domain]  Cd Length: 79  Bit Score: 58.40  E-value: 6.04e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 647806374 194 GQQVKGIVKNLTDYGAFVDL----GGVDGLLHITDMAWKR-IKHPSEIVNVGDEIDVKVLKYdrERNRVSLGLK 262
Cdd:cd05684    1 GKIYKGKVTSIMDFGCFVQLeglkGRKEGLVHISQLSFEGrVANPSDVVKRGQKVKVKVISI--QNGKISLSMK 72
S1 pfam00575
S1 RNA binding domain; The S1 domain occurs in a wide range of RNA associated proteins. It is ...
452-521 6.84e-11

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: 58.07  E-value: 6.84e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374  452 KGAIVKGVVKEVDAKGAIITLANDIEATLKASEISRDRIEDARNVLKEGEEVEAKIISVDRKSRVIQLSI 521
Cdd:pfam00575   3 KGDVVEGEVTRVTKGGAFVDLGNGVEGFIPISELSDDHVEDPDEVIKVGDEVKVKVLKVDKDRRRIILSI 72
YabR COG1098
Predicted RNA-binding protein, contains ribosomal protein S1 (RPS1) domain [General function ...
453-531 1.59e-10

Predicted RNA-binding protein, contains ribosomal protein S1 (RPS1) domain [General function prediction only];


Pssm-ID: 440715 [Multi-domain]  Cd Length: 130  Bit Score: 59.04  E-value: 1.59e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 647806374 453 GAIVKGVVKEVDAKGAIITLANDIEATLKASEISRDRIEDARNVLKEGEEVEAKIISVDRKSRvIQLSIksKDVEDEKE 531
Cdd:COG1098    6 GDIVEGKVTGITPFGAFVELPEGTTGLVHISEIADGYVKDINDYLKVGDEVKVKVLSIDEDGK-ISLSI--KQAEEKPK 81
S1_Rrp5_repeat_sc12 cd05708
S1_Rrp5_repeat_sc12: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ...
278-349 1.59e-10

S1_Rrp5_repeat_sc12: 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 S. cerevisiae S1 repeat 12 (sc12). Rrp5 is found in eukaryotes but not in prokaryotes or archaea.


Pssm-ID: 240213 [Multi-domain]  Cd Length: 77  Bit Score: 57.34  E-value: 1.59e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 647806374 278 ESTRVTARVTNLTDYGCFAELE-EGVEGLVHVSEM-DWTNKNIhpSKVVQVGDEVEVMVLDIDEERRRISLGIK 349
Cdd:cd05708    2 VGQKIDGTVRRVEDYGVFIDIDgTNVSGLCHKSEIsDNRVADA--SKLFRVGDKVRAKVLKIDAEKKRISLGLK 73
PRK08059 PRK08059
general stress protein 13; Validated
360-442 1.83e-10

general stress protein 13; Validated


Pssm-ID: 181215 [Multi-domain]  Cd Length: 123  Bit Score: 58.52  E-value: 1.83e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374 360 SGQFNKGDKISGTIKSITDFGIFIGLDGGIDGLVHLSDISWNEVgeEAVRRF-KKGDELDTVILSVDPERERISLGIKQL 438
Cdd:PRK08059   2 MSQYEVGSVVTGKVTGIQPYGAFVALDEETQGLVHISEITHGFV--KDIHDFlSVGDEVKVKVLSVDEEKGKISLSIRAT 79

                 ....
gi 647806374 439 ESDP 442
Cdd:PRK08059  80 EEAP 83
S1_RPS1_repeat_ec1_hs1 cd05687
S1_RPS1_repeat_ec1_hs1: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
21-89 4.33e-10

S1_RPS1_repeat_ec1_hs1: 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 1 of the Escherichia coli and Homo sapiens RPS1 (ec1 and hs1, respectively). Autoantibodies to double-stranded DNA from patients with systemic lupus erythematosus cross-react with the human RPS1 homolog.


Pssm-ID: 240192 [Multi-domain]  Cd Length: 70  Bit Score: 56.00  E-value: 4.33e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 647806374  21 GSIITGVIVDIDyqARWVTVHAGLKSEALIPLEQFYND---AGELSINVGDEVHVALDSVEDGFGETKLSRE 89
Cdd:cd05687    1 GDIVKGTVVSVD--DDEVLVDIGYKSEGIIPISEFSDDpieNGEDEVKVGDEVEVYVLRVEDEEGNVVLSKR 70
S1_Rrp5_repeat_hs5 cd05697
S1_Rrp5_repeat_hs5: Rrp5 is a trans-acting factor important for biogenesis of both the 40S and ...
194-261 6.13e-10

S1_Rrp5_repeat_hs5: 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 5 (hs5) and S. cerevisiae S1 repeat 5 (sc5). Rrp5 is found in eukaryotes but not in prokaryotes or archaea.


Pssm-ID: 240202 [Multi-domain]  Cd Length: 69  Bit Score: 55.32  E-value: 6.13e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 647806374 194 GQQVKGIVKNLTDYGAFVDL-GGVDGLLHITDMAWKRIKHPSEIVNVGDEIDVKVLKYDRERNRVSLGL 261
Cdd:cd05697    1 GQVVKGTIRKLRPSGIFVKLsDHIKGLVPPMHLADVRLKHPEKKFKPGLKVKCRVLSVEPERKRLVLTL 69
PRK11824 PRK11824
polynucleotide phosphorylase/polyadenylase; Provisional
371-439 8.75e-10

polynucleotide phosphorylase/polyadenylase; Provisional


Pssm-ID: 236995 [Multi-domain]  Cd Length: 693  Bit Score: 61.60  E-value: 8.75e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 647806374 371 GTIKSITDFGIFIGLDGGIDGLVHLSDISWNEVG--EEAVrrfKKGDELDTVILSVDpERERISLGIKQLE 439
Cdd:PRK11824 627 GKVVRIVDFGAFVEILPGKDGLVHISEIADERVEkvEDVL---KEGDEVKVKVLEID-KRGRIRLSRKAVL 693
S1_like cd00164
S1_like: Ribosomal protein S1-like RNA-binding domain. Found in a wide variety of ...
456-520 9.46e-10

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: 54.69  E-value: 9.46e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 647806374 456 VKGVVKEVDAKGAIITLANDIEATLKASEISRDRIEDARNVLKEGEEVEAKIISVDRKSRVIQLS 520
Cdd:cd00164    1 VTGKVVSITKFGVFVELEDGVEGLVHISELSDKFVKDPSEVFKVGDEVEVKVLEVDPEKGRISLS 65
S1_IF2_alpha cd04452
S1_IF2_alpha: The alpha subunit of translation Initiation Factor 2, S1-like RNA-binding domain. ...
451-522 1.28e-09

S1_IF2_alpha: The alpha subunit of translation Initiation Factor 2, S1-like RNA-binding domain. S1-like RNA-binding domains are found in a wide variety of RNA-associated proteins. Eukaryotic and archaeal Initiation Factor 2 (e- and aIF2, respectively) are heterotrimeric proteins with three subunits (alpha, beta, and gamma). IF2 plays a crucial role in the process of translation initiation. The IF2 gamma subunit contains a GTP-binding site. The IF2 beta and gamma subunits together are thought to be responsible for binding methionyl-initiator tRNA. The ternary complex consisting of IF2, GTP, and the methionyl-initiator tRNA binds to the small subunit of the ribosome, as part of a pre-initiation complex that scans the mRNA to find the AUG start codon. The IF2-bound GTP is hydrolyzed to GDP when the methionyl-initiator tRNA binds the AUG start codon, at which time the IF2 is released with its bound GDP. The large ribosomal subunit then joins with the small subunit to complete the initiation complex, which is competent to begin translation. The IF2a subunit is a major site of control of the translation initiation process, via phosphorylation of a specific serine residue. This alpha subunit is well conserved in eukaryotes and archaea but is not present in bacteria. IF2 is a cold-shock-inducible protein.


Pssm-ID: 239899 [Multi-domain]  Cd Length: 76  Bit Score: 54.51  E-value: 1.28e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 647806374 451 DKGAIVKGVVKEVDAKGAIITLA--NDIEATLKASEISRDRIEDARNVLKEGEEVEAKIISVDRKSRVIQLSIK 522
Cdd:cd04452    2 EEGELVVVTVKSIADMGAYVSLLeyGNIEGMILLSELSRRRIRSIRKLVKVGRKEVVKVIRVDKEKGYIDLSKK 75
PRK08059 PRK08059
general stress protein 13; Validated
453-564 1.47e-09

general stress protein 13; Validated


Pssm-ID: 181215 [Multi-domain]  Cd Length: 123  Bit Score: 55.82  E-value: 1.47e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374 453 GAIVKGVVKEVDAKGAIITLANDIEATLKASEISRDRIEDARNVLKEGEEVEAKIISVDRKSRVIQLSIKSkdVEDEKEA 532
Cdd:PRK08059   8 GSVVTGKVTGIQPYGAFVALDEETQGLVHISEITHGFVKDIHDFLSVGDEVKVKVLSVDEEKGKISLSIRA--TEEAPEA 85
                         90       100       110
                 ....*....|....*....|....*....|..
gi 647806374 533 IQSLRDKPAASDIAAGPTTLGDLLRAQMEKQN 564
Cdd:PRK08059  86 KRKKGKILIPNPSEQGFNTLRDKLEEWIEQSN 117
S1_Rrp5_repeat_hs5 cd05697
S1_Rrp5_repeat_hs5: Rrp5 is a trans-acting factor important for biogenesis of both the 40S and ...
366-433 1.48e-09

S1_Rrp5_repeat_hs5: 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 5 (hs5) and S. cerevisiae S1 repeat 5 (sc5). Rrp5 is found in eukaryotes but not in prokaryotes or archaea.


Pssm-ID: 240202 [Multi-domain]  Cd Length: 69  Bit Score: 54.17  E-value: 1.48e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 647806374 366 GDKISGTIKSITDFGIFIGLDGGIDGLV---HLSDIswNEVGEEavRRFKKGDELDTVILSVDPERERISL 433
Cdd:cd05697    1 GQVVKGTIRKLRPSGIFVKLSDHIKGLVppmHLADV--RLKHPE--KKFKPGLKVKCRVLSVEPERKRLVL 67
PRK05807 PRK05807
RNA-binding protein S1;
190-263 1.91e-09

RNA-binding protein S1;


Pssm-ID: 235614 [Multi-domain]  Cd Length: 136  Bit Score: 55.91  E-value: 1.91e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 647806374 190 SLQEGQQVKGIVKNLTDYGAFVDLGGVDGLLHITDMAWKRIKHPSEIVNVGDEIDVKVLKYDrERNRVSLGLKQ 263
Cdd:PRK05807   2 TLKAGSILEGTVVNITNFGAFVEVEGKTGLVHISEVADTYVKDIREHLKEQDKVKVKVISID-DNGKISLSIKQ 74
S1_RPS1_repeat_ec6 cd05691
S1_RPS1_repeat_ec6: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
194-264 1.97e-09

S1_RPS1_repeat_ec6: 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 6 (ec6) 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: 240196 [Multi-domain]  Cd Length: 73  Bit Score: 54.20  E-value: 1.97e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 647806374 194 GQQVKGIVKNLTDYGAFVDLG-GVDGLLHITDMAWKRIKHPSEIVNVGDEIDVKVLKYDRERNRVSLGLKQL 264
Cdd:cd05691    1 GSIVTGKVTEVDAKGATVKLGdGVEGFLRAAELSRDRVEDATERFKVGDEVEAKITNVDRKNRKISLSIKAK 72
PRK03987 PRK03987
translation initiation factor IF-2 subunit alpha; Validated
451-532 3.23e-09

translation initiation factor IF-2 subunit alpha; Validated


Pssm-ID: 235188 [Multi-domain]  Cd Length: 262  Bit Score: 57.91  E-value: 3.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374 451 DKGAIVKGVVKEVDAKGAIITLA--NDIEATLKASEISRDRIEDARNVLKEGEEVEAKIISVDRKSRVIQLSIksKDV-E 527
Cdd:PRK03987   7 EEGELVVGTVKEVKDFGAFVTLDeyPGKEGFIHISEVASGWVKNIRDHVKEGQKVVCKVIRVDPRKGHIDLSL--KRVnE 84

                 ....*
gi 647806374 528 DEKEA 532
Cdd:PRK03987  85 HQRRE 89
S1_IF2_alpha cd04452
S1_IF2_alpha: The alpha subunit of translation Initiation Factor 2, S1-like RNA-binding domain. ...
193-263 4.99e-09

S1_IF2_alpha: The alpha subunit of translation Initiation Factor 2, S1-like RNA-binding domain. S1-like RNA-binding domains are found in a wide variety of RNA-associated proteins. Eukaryotic and archaeal Initiation Factor 2 (e- and aIF2, respectively) are heterotrimeric proteins with three subunits (alpha, beta, and gamma). IF2 plays a crucial role in the process of translation initiation. The IF2 gamma subunit contains a GTP-binding site. The IF2 beta and gamma subunits together are thought to be responsible for binding methionyl-initiator tRNA. The ternary complex consisting of IF2, GTP, and the methionyl-initiator tRNA binds to the small subunit of the ribosome, as part of a pre-initiation complex that scans the mRNA to find the AUG start codon. The IF2-bound GTP is hydrolyzed to GDP when the methionyl-initiator tRNA binds the AUG start codon, at which time the IF2 is released with its bound GDP. The large ribosomal subunit then joins with the small subunit to complete the initiation complex, which is competent to begin translation. The IF2a subunit is a major site of control of the translation initiation process, via phosphorylation of a specific serine residue. This alpha subunit is well conserved in eukaryotes and archaea but is not present in bacteria. IF2 is a cold-shock-inducible protein.


Pssm-ID: 239899 [Multi-domain]  Cd Length: 76  Bit Score: 52.97  E-value: 4.99e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 647806374 193 EGQQVKGIVKNLTDYGAFVDL---GGVDGLLHITDMAWKRIKHPSEIVNVGDEIDVKVLKYDRERNRVSLGLKQ 263
Cdd:cd04452    3 EGELVVVTVKSIADMGAYVSLleyGNIEGMILLSELSRRRIRSIRKLVKVGRKEVVKVIRVDKEKGYIDLSKKR 76
PRK11824 PRK11824
polynucleotide phosphorylase/polyadenylase; Provisional
445-522 6.91e-09

polynucleotide phosphorylase/polyadenylase; Provisional


Pssm-ID: 236995 [Multi-domain]  Cd Length: 693  Bit Score: 58.52  E-value: 6.91e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 647806374 445 EYVQENDKGAIVKGVVKEVDAKGAIITLANDIEATLKASEISRDRIEDARNVLKEGEEVEAKIISVDRKSRvIQLSIK 522
Cdd:PRK11824 614 GITAEPEVGEIYEGKVVRIVDFGAFVEILPGKDGLVHISEIADERVEKVEDVLKEGDEVKVKVLEIDKRGR-IRLSRK 690
S1_RPS1_repeat_ec1_hs1 cd05687
S1_RPS1_repeat_ec1_hs1: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
453-522 7.60e-09

S1_RPS1_repeat_ec1_hs1: 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 1 of the Escherichia coli and Homo sapiens RPS1 (ec1 and hs1, respectively). Autoantibodies to double-stranded DNA from patients with systemic lupus erythematosus cross-react with the human RPS1 homolog.


Pssm-ID: 240192 [Multi-domain]  Cd Length: 70  Bit Score: 52.15  E-value: 7.60e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374 453 GAIVKGVVKEVDAKGAIITLANDIEATLKASEISRDRIEDARNVLKEGEEVEAKIISVDRKSRVIQLSIK 522
Cdd:cd05687    1 GDIVKGTVVSVDDDEVLVDIGYKSEGIIPISEFSDDPIENGEDEVKVGDEVEVYVLRVEDEEGNVVLSKR 70
S1_pNO40 cd05686
S1_pNO40: pNO40 , S1-like RNA-binding domain. pNO40 is a nucleolar protein of unknown function ...
198-262 7.99e-09

S1_pNO40: pNO40 , S1-like RNA-binding domain. pNO40 is a nucleolar protein of unknown function with an N-terminal S1 RNA binding domain, a CCHC type zinc finger, and clusters of basic amino acids representing a potential nucleolar targeting signal. pNO40 was identified through a yeast two-hybrid interaction screen of a human kidney cDNA library using the pinin (pnn) protein as bait. pNO40 is thought to play a role in ribosome maturation and/or biogenesis.


Pssm-ID: 240191 [Multi-domain]  Cd Length: 73  Bit Score: 52.48  E-value: 7.99e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 647806374 198 KGIVKNLTDYGAFVDLGGV--DGLLHITDMAWKRIKHPSEIVNVGDEIDVKVLKYDrERNRVSLGLK 262
Cdd:cd05686    8 KGEVASVTEYGAFVKIPGCrkQGLVHKSHMSSCRVDDPSEVVDVGEKVWVKVIGRE-MKDKMKLSLS 73
PRK08582 PRK08582
RNA-binding protein S1;
190-248 8.57e-09

RNA-binding protein S1;


Pssm-ID: 236305 [Multi-domain]  Cd Length: 139  Bit Score: 54.27  E-value: 8.57e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374 190 SLQEGQQVKGIVKNLTDYGAFVDL-GGVDGLLHITDMAWKRIKHPSEIVNVGDEIDVKVL 248
Cdd:PRK08582   2 SIEVGSKLQGKVTGITNFGAFVELpEGKTGLVHISEVADNYVKDINDHLKVGDEVEVKVL 61
S1_RNase_R cd04471
S1_RNase_R: RNase R C-terminal S1 domain. RNase R is a processive 3' to 5' exoribonuclease, ...
283-346 1.11e-08

S1_RNase_R: RNase R C-terminal S1 domain. RNase R is a processive 3' to 5' exoribonuclease, which is a homolog of RNase II. RNase R degrades RNA with secondary structure having a 3' overhang of at least 7 nucleotides. RNase R and PNPase play an important role in the degradation of RNA with extensive secondary structure, such as rRNA, tRNA, and certain mRNA which contains repetitive extragenic palindromic sequences. The C-terminal S1 domain binds ssRNA.


Pssm-ID: 239917 [Multi-domain]  Cd Length: 83  Bit Score: 52.40  E-value: 1.11e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 647806374 283 TARVTNLTDYGCFAELEE-GVEGLVHVSEMD--------------WTNKNihpsKVVQVGDEVEVMVLDIDEERRRISL 346
Cdd:cd04471    6 DGVISGVTSFGLFVELDNlTVEGLVHVSTLGddyyefdeenhalvGERTG----KVFRLGDKVKVRVVRVDLDRRKIDF 80
PRK03987 PRK03987
translation initiation factor IF-2 subunit alpha; Validated
193-267 1.12e-08

translation initiation factor IF-2 subunit alpha; Validated


Pssm-ID: 235188 [Multi-domain]  Cd Length: 262  Bit Score: 56.37  E-value: 1.12e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 647806374 193 EGQQVKGIVKNLTDYGAFVDL---GGVDGLLHITDMAWKRIKHPSEIVNVGDEIDVKVLKYDRERNRVSLGLKQLGED 267
Cdd:PRK03987   8 EGELVVGTVKEVKDFGAFVTLdeyPGKEGFIHISEVASGWVKNIRDHVKEGQKVVCKVIRVDPRKGHIDLSLKRVNEH 85
PRK07252 PRK07252
S1 RNA-binding domain-containing protein;
281-349 2.29e-08

S1 RNA-binding domain-containing protein;


Pssm-ID: 180908 [Multi-domain]  Cd Length: 120  Bit Score: 52.40  E-value: 2.29e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 647806374 281 RVTARVTNLTDYGCFAELEEGVEGLVHVSEMDwTN--KNIHpsKVVQVGDEVEVMVLDIDEERRRISLGIK 349
Cdd:PRK07252   6 KLKGTITGIKPYGAFVALENGTTGLIHISEIK-TGfiDNIH--QLLKVGEEVLVQVVDFDEYTGKASLSLR 73
VacB COG0557
Exoribonuclease R [Transcription];
283-344 2.82e-08

Exoribonuclease R [Transcription];


Pssm-ID: 440323 [Multi-domain]  Cd Length: 711  Bit Score: 56.65  E-value: 2.82e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 647806374 283 TARVTNLTDYGCFAELEE-GVEGLVHVSEM--DW--------------TNknihpsKVVQVGDEVEVMVLDIDEERRRI 344
Cdd:COG0557  627 EGVISGVTSFGLFVELDElGVEGLVHVSSLgdDYyeyderrqalvgerTG------KRYRLGDRVEVRVVRVDLDRRQI 699
PRK05807 PRK05807
RNA-binding protein S1;
363-437 3.16e-08

RNA-binding protein S1;


Pssm-ID: 235614 [Multi-domain]  Cd Length: 136  Bit Score: 52.44  E-value: 3.16e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 647806374 363 FNKGDKISGTIKSITDFGIFIGLDGGIdGLVHLSDISWNEVGEeaVRRF-KKGDELDTVILSVDpERERISLGIKQ 437
Cdd:PRK05807   3 LKAGSILEGTVVNITNFGAFVEVEGKT-GLVHISEVADTYVKD--IREHlKEQDKVKVKVISID-DNGKISLSIKQ 74
S1 pfam00575
S1 RNA binding domain; The S1 domain occurs in a wide range of RNA associated proteins. It is ...
104-172 3.90e-08

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: 50.36  E-value: 3.90e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 647806374  104 FAAEEVVKGVINGKVKGGFTVDV-NGIRAFLPGSLV--DVRPVRDTTHLEGKELEFKVIKLDQKRNNVVVSR 172
Cdd:pfam00575   1 PEKGDVVEGEVTRVTKGGAFVDLgNGVEGFIPISELsdDHVEDPDEVIKVGDEVKVKVLKVDKDRRRIILSI 72
S1_Rrp5_repeat_hs8_sc7 cd04461
S1_Rrp5_repeat_hs8_sc7: Rrp5 Homo sapiens S1 repeat 8 (hs8) and Saccharomyces cerevisiae S1 ...
188-261 4.13e-08

S1_Rrp5_repeat_hs8_sc7: Rrp5 Homo sapiens S1 repeat 8 (hs8) and Saccharomyces cerevisiae S1 repeat 7 (sc7)-like domains. 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 S. cerevisiae Rrp5 and 14 S1 repeats in H. 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 8 and S. cerevisiae S1 repeat 7. Rrp5 is found in eukaryotes but not in prokaryotes or archaea.


Pssm-ID: 239908 [Multi-domain]  Cd Length: 83  Bit Score: 50.66  E-value: 4.13e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 647806374 188 LESLQEGQQVKGIVKNLTDYGAFVD-LGGVDGLLHITDMAWKRIKHPSEIVNVGDEIDVKVLKYDRERNRVSLGL 261
Cdd:cd04461    9 FSDLKPGMVVHGYVRNITPYGVFVEfLGGLTGLAPKSYISDEFVTDPSFGFKKGQSVTAKVTSVDEEKQRFLLSL 83
Pnp COG1185
Polyribonucleotide nucleotidyltransferase (polynucleotide phosphorylase) [Translation, ...
371-436 4.50e-08

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


Pssm-ID: 440798 [Multi-domain]  Cd Length: 686  Bit Score: 56.17  E-value: 4.50e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 647806374 371 GTIKSITDFGIFIGLDGGIDGLVHLSDISWNEVG--EEAVrrfKKGDELDTVILSVDPeRERISLGIK 436
Cdd:COG1185  622 GKVVRIMDFGAFVEILPGKDGLVHISELADERVEkvEDVL---KEGDEVKVKVLEIDD-QGRIKLSRK 685
S1_RPS1_repeat_ec6 cd05691
S1_RPS1_repeat_ec6: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
366-439 8.03e-08

S1_RPS1_repeat_ec6: 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 6 (ec6) 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: 240196 [Multi-domain]  Cd Length: 73  Bit Score: 49.58  E-value: 8.03e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 647806374 366 GDKISGTIKSITDFGIFIGLDGGIDGLVHLSDISWNEVgEEAVRRFKKGDELDTVILSVDPERERISLGIKQLE 439
Cdd:cd05691    1 GSIVTGKVTEVDAKGATVKLGDGVEGFLRAAELSRDRV-EDATERFKVGDEVEAKITNVDRKNRKISLSIKAKE 73
S1_RNase_R cd04471
S1_RNase_R: RNase R C-terminal S1 domain. RNase R is a processive 3' to 5' exoribonuclease, ...
366-433 1.10e-07

S1_RNase_R: RNase R C-terminal S1 domain. RNase R is a processive 3' to 5' exoribonuclease, which is a homolog of RNase II. RNase R degrades RNA with secondary structure having a 3' overhang of at least 7 nucleotides. RNase R and PNPase play an important role in the degradation of RNA with extensive secondary structure, such as rRNA, tRNA, and certain mRNA which contains repetitive extragenic palindromic sequences. The C-terminal S1 domain binds ssRNA.


Pssm-ID: 239917 [Multi-domain]  Cd Length: 83  Bit Score: 49.32  E-value: 1.10e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 647806374 366 GDKISGTIKSITDFGIFIGLDG-GIDGLVHLSDIS-----WNE-----VGEEAVRRFKKGDELDTVILSVDPERERISL 433
Cdd:cd04471    2 GEEFDGVISGVTSFGLFVELDNlTVEGLVHVSTLGddyyeFDEenhalVGERTGKVFRLGDKVKVRVVRVDLDRRKIDF 80
S1_Tex cd05685
S1_Tex: The C-terminal S1 domain of a transcription accessory factor called Tex, which has ...
366-433 1.37e-07

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: 48.77  E-value: 1.37e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 647806374 366 GDKISGTIKSITDFGIFIGLDGGIDGLVHLSDISwNEVGEEAVRRFKKGDELDTVILSVDPERERISL 433
Cdd:cd05685    1 GMVLEGVVTNVTDFGAFVDIGVKQDGLIHISKMA-DRFVSHPSDVVSVGDIVEVKVISIDEERGRISL 67
PRK05807 PRK05807
RNA-binding protein S1;
282-350 1.77e-07

RNA-binding protein S1;


Pssm-ID: 235614 [Multi-domain]  Cd Length: 136  Bit Score: 50.51  E-value: 1.77e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374 282 VTARVTNLTDYGCFAELeEGVEGLVHVSEM-DWTNKNIHpsKVVQVGDEVEVMVLDIDeERRRISLGIKQ 350
Cdd:PRK05807   9 LEGTVVNITNFGAFVEV-EGKTGLVHISEVaDTYVKDIR--EHLKEQDKVKVKVISID-DNGKISLSIKQ 74
S1 smart00316
Ribosomal protein S1-like RNA-binding domain;
108-173 2.08e-07

Ribosomal protein S1-like RNA-binding domain;


Pssm-ID: 197648 [Multi-domain]  Cd Length: 72  Bit Score: 48.37  E-value: 2.08e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 647806374   108 EVVKGVINGKVKGGFTVDV-NGIRAFLPGSLVDVRPVRDTTH--LEGKELEFKVIKLDQKRNNVVVSRR 173
Cdd:smart00316   4 DVVEGTVTEITPGGAFVDLgNGVEGLIPISELSDKRVKDPEEvlKVGDEVKVKVLSVDEEKGRIILSLK 72
S1_PNPase cd04472
S1_PNPase: Polynucleotide phosphorylase (PNPase), ), S1-like RNA-binding domain. PNPase is a ...
366-433 2.73e-07

S1_PNPase: Polynucleotide phosphorylase (PNPase), ), S1-like RNA-binding domain. PNPase is a polyribonucleotide nucleotidyl transferase that degrades mRNA. It is a trimeric multidomain protein. The C-terminus contains the S1 domain which binds ssRNA. This family is classified based on the S1 domain. PNPase nonspecifically removes the 3' nucleotides from mRNA, but is stalled by double-stranded RNA structures such as a stem-loop. Evidence shows that a minimum of 7-10 unpaired nucleotides at the 3' end, is required for PNPase degradation. It is suggested that PNPase also dephosphorylates the RNA 5' end. This additional activity may regulate the 5'-dependent activity of RNaseE in vivo.


Pssm-ID: 239918 [Multi-domain]  Cd Length: 68  Bit Score: 47.92  E-value: 2.73e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 647806374 366 GDKISGTIKSITDFGIFIGLDGGIDGLVHLSDISwnevgEEAVRR----FKKGDELDTVILSVDpERERISL 433
Cdd:cd04472    1 GKIYEGKVVKIKDFGAFVEILPGKDGLVHISELS-----DERVEKvedvLKVGDEVKVKVIEVD-DRGRISL 66
PRK07252 PRK07252
S1 RNA-binding domain-containing protein;
194-310 2.73e-07

S1 RNA-binding domain-containing protein;


Pssm-ID: 180908 [Multi-domain]  Cd Length: 120  Bit Score: 49.31  E-value: 2.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374 194 GQQVKGIVKNLTDYGAFVDL-GGVDGLLHITDMAWKRIKHPSEIVNVGDEIDVKVLKYDRERNRVSLGLKQLGEDpwvai 272
Cdd:PRK07252   4 GDKLKGTITGIKPYGAFVALeNGTTGLIHISEIKTGFIDNIHQLLKVGEEVLVQVVDFDEYTGKASLSLRTLEEE----- 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 647806374 273 KARYPESTRVTarvTNLTDYGcFAELEEGV-----EGLVHVSE 310
Cdd:PRK07252  79 KQHFPHRHRFS---NSRHKIG-FKPLEEQLpiwieEALQYLKK 117
S1_IF2_alpha cd04452
S1_IF2_alpha: The alpha subunit of translation Initiation Factor 2, S1-like RNA-binding domain. ...
282-350 3.07e-07

S1_IF2_alpha: The alpha subunit of translation Initiation Factor 2, S1-like RNA-binding domain. S1-like RNA-binding domains are found in a wide variety of RNA-associated proteins. Eukaryotic and archaeal Initiation Factor 2 (e- and aIF2, respectively) are heterotrimeric proteins with three subunits (alpha, beta, and gamma). IF2 plays a crucial role in the process of translation initiation. The IF2 gamma subunit contains a GTP-binding site. The IF2 beta and gamma subunits together are thought to be responsible for binding methionyl-initiator tRNA. The ternary complex consisting of IF2, GTP, and the methionyl-initiator tRNA binds to the small subunit of the ribosome, as part of a pre-initiation complex that scans the mRNA to find the AUG start codon. The IF2-bound GTP is hydrolyzed to GDP when the methionyl-initiator tRNA binds the AUG start codon, at which time the IF2 is released with its bound GDP. The large ribosomal subunit then joins with the small subunit to complete the initiation complex, which is competent to begin translation. The IF2a subunit is a major site of control of the translation initiation process, via phosphorylation of a specific serine residue. This alpha subunit is well conserved in eukaryotes and archaea but is not present in bacteria. IF2 is a cold-shock-inducible protein.


Pssm-ID: 239899 [Multi-domain]  Cd Length: 76  Bit Score: 47.96  E-value: 3.07e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 647806374 282 VTARVTNLTDYGCFAELEE--GVEGLVHVSEMD--WTnKNIHpsKVVQVGDEVEVMVLDIDEERRRISLGIKQ 350
Cdd:cd04452    7 VVVTVKSIADMGAYVSLLEygNIEGMILLSELSrrRI-RSIR--KLVKVGRKEVVKVIRVDKEKGYIDLSKKR 76
S1_DHX8_helicase cd05684
S1_DHX8_helicase: The N-terminal S1 domain of human ATP-dependent RNA helicase DHX8, a DEAH ...
370-436 3.32e-07

S1_DHX8_helicase: The N-terminal S1 domain of human ATP-dependent RNA helicase DHX8, a DEAH (Asp-Glu-Ala-His) box polypeptide. The DEAH-box RNA helicases are thought to play key roles in pre-mRNA splicing and DHX8 facilitates nuclear export of spliced mRNA by releasing the RNA from the spliceosome. DHX8 is also known as HRH1 (human RNA helicase 1) in Homo sapiens and PRP22 in Saccharomyces cerevisiae.


Pssm-ID: 240189 [Multi-domain]  Cd Length: 79  Bit Score: 48.00  E-value: 3.32e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374 370 SGTIKSITDFGIFI---GLDGGIDGLVHLSDISWNEVGEEAVRRFKKGDELDTVILSVdpERERISLGIK 436
Cdd:cd05684    5 KGKVTSIMDFGCFVqleGLKGRKEGLVHISQLSFEGRVANPSDVVKRGQKVKVKVISI--QNGKISLSMK 72
S1_RPS1_repeat_ec1_hs1 cd05687
S1_RPS1_repeat_ec1_hs1: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
194-259 7.72e-07

S1_RPS1_repeat_ec1_hs1: 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 1 of the Escherichia coli and Homo sapiens RPS1 (ec1 and hs1, respectively). Autoantibodies to double-stranded DNA from patients with systemic lupus erythematosus cross-react with the human RPS1 homolog.


Pssm-ID: 240192 [Multi-domain]  Cd Length: 70  Bit Score: 46.75  E-value: 7.72e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 647806374 194 GQQVKGIVKNLTDYGAFVDLGG-VDGLLHITDMAWKRIKHPSEIVNVGDEIDVKVLKYDRERNRVSL 259
Cdd:cd05687    1 GDIVKGTVVSVDDDEVLVDIGYkSEGIIPISEFSDDPIENGEDEVKVGDEVEVYVLRVEDEEGNVVL 67
PRK08582 PRK08582
RNA-binding protein S1;
366-445 2.42e-06

RNA-binding protein S1;


Pssm-ID: 236305 [Multi-domain]  Cd Length: 139  Bit Score: 47.33  E-value: 2.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374 366 GDKISGTIKSITDFGIFIGLDGGIDGLVHLSDISWNEVgEEAVRRFKKGDELDTVILSVDPErERISLGIKQLESDPFSE 445
Cdd:PRK08582   6 GSKLQGKVTGITNFGAFVELPEGKTGLVHISEVADNYV-KDINDHLKVGDEVEVKVLNVEDD-GKIGLSIKKAKDRPKRQ 83
S1_Rrp5_repeat_hs8_sc7 cd04461
S1_Rrp5_repeat_hs8_sc7: Rrp5 Homo sapiens S1 repeat 8 (hs8) and Saccharomyces cerevisiae S1 ...
365-433 2.71e-06

S1_Rrp5_repeat_hs8_sc7: Rrp5 Homo sapiens S1 repeat 8 (hs8) and Saccharomyces cerevisiae S1 repeat 7 (sc7)-like domains. 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 S. cerevisiae Rrp5 and 14 S1 repeats in H. 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 8 and S. cerevisiae S1 repeat 7. Rrp5 is found in eukaryotes but not in prokaryotes or archaea.


Pssm-ID: 239908 [Multi-domain]  Cd Length: 83  Bit Score: 45.66  E-value: 2.71e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 647806374 365 KGDKISGTIKSITDFGIFIGLDGGIDGLVHLSDISwNEVGEEAVRRFKKGDELDTVILSVDPERERISL 433
Cdd:cd04461   14 PGMVVHGYVRNITPYGVFVEFLGGLTGLAPKSYIS-DEFVTDPSFGFKKGQSVTAKVTSVDEEKQRFLL 81
S1_Rrp5_repeat_sc11 cd05707
S1_Rrp5_repeat_sc11: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ...
453-520 2.79e-06

S1_Rrp5_repeat_sc11: 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 S. cerevisiae S1 repeat 11 (sc11). Rrp5 is found in eukaryotes but not in prokaryotes or archaea.


Pssm-ID: 240212 [Multi-domain]  Cd Length: 68  Bit Score: 44.98  E-value: 2.79e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 647806374 453 GAIVKGVVKEVDAKGAIITLANDIEATLKASEISRDRIEDARNVLKEGEEVEAKIISVDRKSRVIQLS 520
Cdd:cd05707    1 GDVVRGFVKNIANNGVFVTLGRGVDARVRVSELSDSYLKDWKKRFKVGQLVKGKIVSIDPDNGRIEMT 68
Tex COG2183
Transcriptional accessory protein Tex/SPT6 [Transcription];
371-442 4.12e-06

Transcriptional accessory protein Tex/SPT6 [Transcription];


Pssm-ID: 441786 [Multi-domain]  Cd Length: 719  Bit Score: 49.64  E-value: 4.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374 371 GTIKSITDFGIFIglDGGI--DGLVHLSDISwnevgeeavRRF--------KKGDELDTVILSVDPERERISLGIKQLES 440
Cdd:COG2183  647 GTVTNVTDFGAFV--DIGVhqDGLVHISQLS---------DRFvkdprevvKVGDIVKVKVLEVDLKRKRISLSMKLDDE 715

                 ..
gi 647806374 441 DP 442
Cdd:COG2183  716 AG 717
S1_Rrp5_repeat_hs6_sc5 cd05698
S1_Rrp5_repeat_hs6_sc5: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ...
453-522 4.34e-06

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: 44.52  E-value: 4.34e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374 453 GAIVKGVVKEVDAKGAIITLANDIEATLKASEISRDRIEDARNVLKEGEEVEAKIISVDRKSRVIQLSIK 522
Cdd:cd05698    1 GLKTHGTIVKVKPNGCIVSFYNNVKGFLPKSELSEAFIKDPEEHFRVGQVVKVKVLSCDPEQQRLLLSCK 70
PRK03987 PRK03987
translation initiation factor IF-2 subunit alpha; Validated
282-349 5.86e-06

translation initiation factor IF-2 subunit alpha; Validated


Pssm-ID: 235188 [Multi-domain]  Cd Length: 262  Bit Score: 47.90  E-value: 5.86e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 647806374 282 VTARVTNLTDYGCFAELEE--GVEGLVHVSEM--DWTnKNIHpsKVVQVGDEVEVMVLDIDEERRRISLGIK 349
Cdd:PRK03987  12 VVGTVKEVKDFGAFVTLDEypGKEGFIHISEVasGWV-KNIR--DHVKEGQKVVCKVIRVDPRKGHIDLSLK 80
PRK07252 PRK07252
S1 RNA-binding domain-containing protein;
366-441 7.79e-06

S1 RNA-binding domain-containing protein;


Pssm-ID: 180908 [Multi-domain]  Cd Length: 120  Bit Score: 45.08  E-value: 7.79e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 647806374 366 GDKISGTIKSITDFGIFIGLDGGIDGLVHLSDISWNEVgEEAVRRFKKGDELDTVILSVDPERERISLGIKQLESD 441
Cdd:PRK07252   4 GDKLKGTITGIKPYGAFVALENGTTGLIHISEIKTGFI-DNIHQLLKVGEEVLVQVVDFDEYTGKASLSLRTLEEE 78
PLN00207 PLN00207
polyribonucleotide nucleotidyltransferase; Provisional
235-339 8.62e-06

polyribonucleotide nucleotidyltransferase; Provisional


Pssm-ID: 215104 [Multi-domain]  Cd Length: 891  Bit Score: 48.74  E-value: 8.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374 235 EIVNVGDEIDVKVLKYDRERNRVSLG-LKQLGEDPWVAIKARYPEstrvtarVTNLTDYGCFAELEEGVEGLVHVSEM-- 311
Cdd:PLN00207 717 EAIDTQDDGTVKITAKDLSSLEKSKAiISSLTMVPTVGDIYRNCE-------IKSIAPYGAFVEIAPGREGLCHISELss 789
                         90       100
                 ....*....|....*....|....*...
gi 647806374 312 DWTNKnihPSKVVQVGDEVEVMVLDIDE 339
Cdd:PLN00207 790 NWLAK---PEDAFKVGDRIDVKLIEVND 814
S1_Rrp5_repeat_hs8_sc7 cd04461
S1_Rrp5_repeat_hs8_sc7: Rrp5 Homo sapiens S1 repeat 8 (hs8) and Saccharomyces cerevisiae S1 ...
282-346 9.40e-06

S1_Rrp5_repeat_hs8_sc7: Rrp5 Homo sapiens S1 repeat 8 (hs8) and Saccharomyces cerevisiae S1 repeat 7 (sc7)-like domains. 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 S. cerevisiae Rrp5 and 14 S1 repeats in H. 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 8 and S. cerevisiae S1 repeat 7. Rrp5 is found in eukaryotes but not in prokaryotes or archaea.


Pssm-ID: 239908 [Multi-domain]  Cd Length: 83  Bit Score: 44.12  E-value: 9.40e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 647806374 282 VTARVTNLTDYGCFAELEEGVEGLVHVSEMDwTNKNIHPSKVVQVGDEVEVMVLDIDEERRRISL 346
Cdd:cd04461   18 VHGYVRNITPYGVFVEFLGGLTGLAPKSYIS-DEFVTDPSFGFKKGQSVTAKVTSVDEEKQRFLL 81
S1_RPS1_repeat_ec2_hs2 cd04465
S1_RPS1_repeat_ec2_hs2: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
453-522 1.35e-05

S1_RPS1_repeat_ec2_hs2: 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 2 of the Escherichia coli and Homo sapiens RPS1 (ec2 and hs2, respectively). Autoantibodies to double-stranded DNA from patients with systemic lupus erythematosus cross-react with the human RPS1 homolog.


Pssm-ID: 239911 [Multi-domain]  Cd Length: 67  Bit Score: 42.83  E-value: 1.35e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374 453 GAIVKGVVKEVdAKGAIITLANDIEATLKASEISRDRIEDARNVLkeGEEVEAKIISVDRKSRVIQLSIK 522
Cdd:cd04465    1 GEIVEGKVTEK-VKGGLIVDIEGVRAFLPASQVDLRPVEDLDEYV--GKELKFKIIEIDRERNNIVLSRR 67
PLN00207 PLN00207
polyribonucleotide nucleotidyltransferase; Provisional
201-268 1.37e-05

polyribonucleotide nucleotidyltransferase; Provisional


Pssm-ID: 215104 [Multi-domain]  Cd Length: 891  Bit Score: 47.97  E-value: 1.37e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 647806374 201 VKNLTDYGAFVDLG-GVDGLLHITDMAWKRIKHPSEIVNVGDEIDVKVLKYDrERNRVSLGLKQLGEDP 268
Cdd:PLN00207 762 IKSIAPYGAFVEIApGREGLCHISELSSNWLAKPEDAFKVGDRIDVKLIEVN-DKGQLRLSRRALLPEA 829
S1_Rrp5_repeat_hs6_sc5 cd05698
S1_Rrp5_repeat_hs6_sc5: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ...
286-349 1.38e-05

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: 42.98  E-value: 1.38e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 647806374 286 VTNLTDYGCFAELEEGVEGLVHVSEMDwTNKNIHPSKVVQVGDEVEVMVLDIDEERRRISLGIK 349
Cdd:cd05698    8 IVKVKPNGCIVSFYNNVKGFLPKSELS-EAFIKDPEEHFRVGQVVKVKVLSCDPEQQRLLLSCK 70
S1_RPS1_repeat_ec6 cd05691
S1_RPS1_repeat_ec6: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
280-350 2.12e-05

S1_RPS1_repeat_ec6: 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 6 (ec6) 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: 240196 [Multi-domain]  Cd Length: 73  Bit Score: 42.64  E-value: 2.12e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 647806374 280 TRVTARVTNLTDYGCFAELEEGVEGLVHVSEMDwTNKNIHPSKVVQVGDEVEVMVLDIDEERRRISLGIKQ 350
Cdd:cd05691    2 SIVTGKVTEVDAKGATVKLGDGVEGFLRAAELS-RDRVEDATERFKVGDEVEAKITNVDRKNRKISLSIKA 71
S1_Rrp5_repeat_hs6_sc5 cd05698
S1_Rrp5_repeat_hs6_sc5: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ...
366-436 3.09e-05

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: 42.21  E-value: 3.09e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 647806374 366 GDKISGTIKSITDFGIFIGLDGGIDGLVHLSDISWNEVgEEAVRRFKKGDELDTVILSVDPERERISLGIK 436
Cdd:cd05698    1 GLKTHGTIVKVKPNGCIVSFYNNVKGFLPKSELSEAFI-KDPEEHFRVGQVVKVKVLSCDPEQQRLLLSCK 70
S1_IF2_alpha cd04452
S1_IF2_alpha: The alpha subunit of translation Initiation Factor 2, S1-like RNA-binding domain. ...
364-437 4.19e-05

S1_IF2_alpha: The alpha subunit of translation Initiation Factor 2, S1-like RNA-binding domain. S1-like RNA-binding domains are found in a wide variety of RNA-associated proteins. Eukaryotic and archaeal Initiation Factor 2 (e- and aIF2, respectively) are heterotrimeric proteins with three subunits (alpha, beta, and gamma). IF2 plays a crucial role in the process of translation initiation. The IF2 gamma subunit contains a GTP-binding site. The IF2 beta and gamma subunits together are thought to be responsible for binding methionyl-initiator tRNA. The ternary complex consisting of IF2, GTP, and the methionyl-initiator tRNA binds to the small subunit of the ribosome, as part of a pre-initiation complex that scans the mRNA to find the AUG start codon. The IF2-bound GTP is hydrolyzed to GDP when the methionyl-initiator tRNA binds the AUG start codon, at which time the IF2 is released with its bound GDP. The large ribosomal subunit then joins with the small subunit to complete the initiation complex, which is competent to begin translation. The IF2a subunit is a major site of control of the translation initiation process, via phosphorylation of a specific serine residue. This alpha subunit is well conserved in eukaryotes and archaea but is not present in bacteria. IF2 is a cold-shock-inducible protein.


Pssm-ID: 239899 [Multi-domain]  Cd Length: 76  Bit Score: 41.80  E-value: 4.19e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 647806374 364 NKGDKISGTIKSITDFGIFIGLD--GGIDGLVHLSDISWNEVGeeAVRRF-KKGDELDTVILSVDPERERISLGIKQ 437
Cdd:cd04452    2 EEGELVVVTVKSIADMGAYVSLLeyGNIEGMILLSELSRRRIR--SIRKLvKVGRKEVVKVIRVDKEKGYIDLSKKR 76
S1_Rrp5_repeat_hs14 cd05705
S1_Rrp5_repeat_hs14: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ...
365-433 8.40e-05

S1_Rrp5_repeat_hs14: 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 14 (hs14). Rrp5 is found in eukaryotes but not in prokaryotes or archaea.


Pssm-ID: 240210 [Multi-domain]  Cd Length: 74  Bit Score: 40.84  E-value: 8.40e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 647806374 365 KGDKISGTIKSITDFGIFIGLDGGIDGLVHLSDISWNEVGEEAV--RRFKKGDELDTVILSVDPERERISL 433
Cdd:cd05705    3 EGQLLRGYVSSVTKQGVFFRLSSSIVGRVLFQNVTKYFVSDPSLynKYLPEGKLLTAKVLSVNSEKNLVEL 73
PRK00087 PRK00087
bifunctional 4-hydroxy-3-methylbut-2-enyl diphosphate reductase/30S ribosomal protein S1;
434-534 1.34e-04

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


Pssm-ID: 234623 [Multi-domain]  Cd Length: 647  Bit Score: 44.94  E-value: 1.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374 434 GIKQLESDPFSEYVQENDK----GAIVKGVVKEVDAKGAIITLANDIEATLKASEISRDRIEDARNVLKEGEEVEAKIIS 509
Cdd:PRK00087 280 NMEEVEENEQLEYMNELEKqirrGDIVKGTVVSVNENEVFVDVGYKSEGVIPLRELTLDEISSLKESVKVGDEIEVKVLK 359
                         90       100
                 ....*....|....*....|....*
gi 647806374 510 VDRKSRVIQLSIKSKDVEDEKEAIQ 534
Cdd:PRK00087 360 LEDEDGYVVLSKKEADREKAWKELE 384
S1_Rrp5_repeat_hs5 cd05697
S1_Rrp5_repeat_hs5: Rrp5 is a trans-acting factor important for biogenesis of both the 40S and ...
282-346 2.15e-04

S1_Rrp5_repeat_hs5: 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 5 (hs5) and S. cerevisiae S1 repeat 5 (sc5). Rrp5 is found in eukaryotes but not in prokaryotes or archaea.


Pssm-ID: 240202 [Multi-domain]  Cd Length: 69  Bit Score: 39.53  E-value: 2.15e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 647806374 282 VTARVTNLTDYGCFAELEEGVEGLV---HVSEMDWTnkniHPSKVVQVGDEVEVMVLDIDEERRRISL 346
Cdd:cd05697    4 VKGTIRKLRPSGIFVKLSDHIKGLVppmHLADVRLK----HPEKKFKPGLKVKCRVLSVEPERKRLVL 67
PLN00207 PLN00207
polyribonucleotide nucleotidyltransferase; Provisional
373-495 2.49e-04

polyribonucleotide nucleotidyltransferase; Provisional


Pssm-ID: 215104 [Multi-domain]  Cd Length: 891  Bit Score: 44.11  E-value: 2.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374 373 IKSITDFGIFIGLDGGIDGLVHLSDIS--WNEVGEEAvrrFKKGDELDTVILSVDpERERISLGIKQLESDPFSE----- 445
Cdd:PLN00207 762 IKSIAPYGAFVEIAPGREGLCHISELSsnWLAKPEDA---FKVGDRIDVKLIEVN-DKGQLRLSRRALLPEANSEkssqk 837
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 647806374 446 --YVQENDKGAIVKGVVKEVDAKGAIITLANDIE-ATLKASEISRDRIEDARN 495
Cdd:PLN00207 838 qqGGSTKDKAPQKKYVNTSSRPRRAAQAEKNSAEnAAVPKKKDYKRATSGSKD 890
PRK05807 PRK05807
RNA-binding protein S1;
453-522 3.14e-04

RNA-binding protein S1;


Pssm-ID: 235614 [Multi-domain]  Cd Length: 136  Bit Score: 40.88  E-value: 3.14e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374 453 GAIVKGVVKEVDAKGAIITLaNDIEATLKASEISRDRIEDARNVLKEGEEVEAKIISVDRKSRvIQLSIK 522
Cdd:PRK05807   6 GSILEGTVVNITNFGAFVEV-EGKTGLVHISEVADTYVKDIREHLKEQDKVKVKVISIDDNGK-ISLSIK 73
S1_Rrp5_repeat_hs6_sc5 cd05698
S1_Rrp5_repeat_hs6_sc5: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ...
194-262 3.49e-04

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: 39.13  E-value: 3.49e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374 194 GQQVKGIVKNLTDYGAFVD-LGGVDGLLHITDMAWKRIKHPSEIVNVGDEIDVKVLKYDRERNRVSLGLK 262
Cdd:cd05698    1 GLKTHGTIVKVKPNGCIVSfYNNVKGFLPKSELSEAFIKDPEEHFRVGQVVKVKVLSCDPEQQRLLLSCK 70
S1_RNase_E cd04453
S1_RNase_E: RNase E and RNase G, S1-like RNA-binding domain. RNase E is an essential ...
196-249 3.50e-04

S1_RNase_E: RNase E and RNase G, S1-like RNA-binding domain. RNase E is an essential endoribonuclease in the processing and degradation of RNA. In addition to its role in mRNA degradation, RNase E has also been implicated in the processing of rRNA, and the maturation of tRNA, 10Sa RNA and the M1 precursor of RNase P. RNase E associates with PNPase (3' to 5' exonuclease), Rhl B (DEAD-box RNA helicase) and enolase (glycolytic enzyme) to form the RNA degradosome. RNase E tends to cut mRNA within single-stranded regions that are rich in A/U nucleotides. The N-terminal region of RNase E contains the catalytic site. Within the conserved N-terminal domain of RNAse E and RNase G, there is an S1-like subdomain, which is an ancient single-stranded RNA-binding domain. S1 domain is an RNA-binding module originally identified in the ribosomal protein S1. The S1 domain is required for RNA cleavage by RNase E. RNase G is paralogous to RNase E with an N-terminal catalytic domain that is highly homologous to that of RNase E. RNase G not only shares sequence similarity with RNase E, but also functionally overlaps with RNase E. In Escherichia coli, RNase G is involved in the maturation of the 5' end of the 16S rRNA. RNase G plays a secondary role in mRNA decay.


Pssm-ID: 239900 [Multi-domain]  Cd Length: 88  Bit Score: 39.50  E-value: 3.50e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 647806374 196 QVKGIVKNLTdyGAFVDLG-GVDGLLHITDMAW---KRIKHPSEIVNVGDEIDVKVLK 249
Cdd:cd04453   14 RVKKIVPGLQ--AAFVDIGlGKNGFLHLSDILPayfKKHKKIAKLLKEGQEILVQVVK 69
S1_Tex cd05685
S1_Tex: The C-terminal S1 domain of a transcription accessory factor called Tex, which has ...
453-520 4.44e-04

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: 38.75  E-value: 4.44e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 647806374 453 GAIVKGVVKEVDAKGAIITLANDIEATLKASEISRDRIEDARNVLKEGEEVEAKIISVDRKSRVIQLS 520
Cdd:cd05685    1 GMVLEGVVTNVTDFGAFVDIGVKQDGLIHISKMADRFVSHPSDVVSVGDIVEVKVISIDEERGRISLS 68
S1_Rrp5_repeat_hs8_sc7 cd04461
S1_Rrp5_repeat_hs8_sc7: Rrp5 Homo sapiens S1 repeat 8 (hs8) and Saccharomyces cerevisiae S1 ...
452-521 4.86e-04

S1_Rrp5_repeat_hs8_sc7: Rrp5 Homo sapiens S1 repeat 8 (hs8) and Saccharomyces cerevisiae S1 repeat 7 (sc7)-like domains. 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 S. cerevisiae Rrp5 and 14 S1 repeats in H. 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 8 and S. cerevisiae S1 repeat 7. Rrp5 is found in eukaryotes but not in prokaryotes or archaea.


Pssm-ID: 239908 [Multi-domain]  Cd Length: 83  Bit Score: 39.11  E-value: 4.86e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374 452 KGAIVKGVVKEVDAKGAIITLANDIEATLKASEISRDRIEDARNVLKEGEEVEAKIISVDRKSRVIQLSI 521
Cdd:cd04461   14 PGMVVHGYVRNITPYGVFVEFLGGLTGLAPKSYISDEFVTDPSFGFKKGQSVTAKVTSVDEEKQRFLLSL 83
PRK08563 PRK08563
DNA-directed RNA polymerase subunit E'; Provisional
197-271 5.30e-04

DNA-directed RNA polymerase subunit E'; Provisional


Pssm-ID: 236289 [Multi-domain]  Cd Length: 187  Bit Score: 41.35  E-value: 5.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374 197 VKGIVKNLTDYGAFVDLGGVDGLLHIT---------DMAWKRI--KHPSEIVNVGDEIDVKV----LKYDRERN-RVSLG 260
Cdd:PRK08563  85 VEGEVVEVVEFGAFVRIGPVDGLLHISqimddyisyDPKNGRLigKESKRVLKVGDVVRARIvavsLKERRPRGsKIGLT 164
                         90
                 ....*....|...
gi 647806374 261 LKQ--LGEDPWVA 271
Cdd:PRK08563 165 MRQpgLGKLEWIE 177
PRK08563 PRK08563
DNA-directed RNA polymerase subunit E'; Provisional
369-437 5.81e-04

DNA-directed RNA polymerase subunit E'; Provisional


Pssm-ID: 236289 [Multi-domain]  Cd Length: 187  Bit Score: 40.96  E-value: 5.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374 369 ISGTIKSITDFGIFIGLdGGIDGLVHLSDISWNEV----------GEEAVRRFKKGDELDTVILSV-----DPERERISL 433
Cdd:PRK08563  85 VEGEVVEVVEFGAFVRI-GPVDGLLHISQIMDDYIsydpkngrliGKESKRVLKVGDVVRARIVAVslkerRPRGSKIGL 163

                 ....
gi 647806374 434 GIKQ 437
Cdd:PRK08563 164 TMRQ 167
S1_RpoE cd04460
S1_RpoE: RpoE, S1-like RNA-binding domain. S1-like RNA-binding domains are found in a wide ...
369-437 5.81e-04

S1_RpoE: RpoE, S1-like RNA-binding domain. S1-like RNA-binding domains are found in a wide variety of RNA-associated proteins. RpoE is subunit E of archaeal RNA polymerase. Archaeal cells contain a single RNA polymerase made up of 12 subunits, which are homologous to the 12 subunits (RPB1-12) of eukaryotic RNA polymerase II. RpoE is homologous to Rpa43 of eukaryotic RNA polymerase I, RPB7 of eukaryotic RNA polymerase II, and Rpc25 of eukaryotic RNA polymerase III. RpoE is composed of two domains, the N-terminal RNP (ribonucleoprotein) domain and the C-terminal S1 domain. This S1 domain binds ssRNA and ssDNA. This family is classified based on the C-terminal S1 domain. The function of RpoE is not fully understood. In eukaryotes, RPB7 and RPB4 form a heterodimer that reversibly associates with the RNA polymerase II core.


Pssm-ID: 239907 [Multi-domain]  Cd Length: 99  Bit Score: 39.19  E-value: 5.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374 369 ISGTIKSITDFGIFIGLdGGIDGLVHLSDISWNEV----------GEEAVRRFKKGDELDTVILSV-----DPERERISL 433
Cdd:cd04460    3 VEGEVVEVVDFGAFVRI-GPVDGLLHISQIMDDYIsydpknkrliGEETKRVLKVGDVVRARIVAVslkerRPRESKIGL 81

                 ....
gi 647806374 434 GIKQ 437
Cdd:cd04460   82 TMRQ 85
COG1107 COG1107
Archaea-specific RecJ-like exonuclease, contains DnaJ-type Zn finger domain [Replication, ...
188-280 6.15e-04

Archaea-specific RecJ-like exonuclease, contains DnaJ-type Zn finger domain [Replication, recombination and repair];


Pssm-ID: 440724 [Multi-domain]  Cd Length: 626  Bit Score: 42.52  E-value: 6.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374 188 LESLQEGQQVKGIVKNLTDYGAFVDLG-GVDGLLHITDMA--WKrikhpseivnVGDEIDVKVLKYdRERNRVSLGLKQL 264
Cdd:COG1107   34 PDDLEPGRYYRGTVDGVADFGVFVDLNdHVTGLLHRSELDqdWE----------VGDEVFVQVKEV-RDNGNVDLGWVSI 102
                         90
                 ....*....|....*.
gi 647806374 265 GEDPWVAIKARYPEST 280
Cdd:COG1107  103 DSYETVEVEKELPRTT 118
S1_Rrp5_repeat_sc11 cd05707
S1_Rrp5_repeat_sc11: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ...
366-433 9.06e-04

S1_Rrp5_repeat_sc11: 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 S. cerevisiae S1 repeat 11 (sc11). Rrp5 is found in eukaryotes but not in prokaryotes or archaea.


Pssm-ID: 240212 [Multi-domain]  Cd Length: 68  Bit Score: 38.04  E-value: 9.06e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 647806374 366 GDKISGTIKSITDFGIFIGLDGGIDGLVHLSDISwNEVGEEAVRRFKKGDELDTVILSVDPERERISL 433
Cdd:cd05707    1 GDVVRGFVKNIANNGVFVTLGRGVDARVRVSELS-DSYLKDWKKRFKVGQLVKGKIVSIDPDNGRIEM 67
S1_Rrp5_repeat_sc10 cd05706
S1_Rrp5_repeat_sc10: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ...
284-346 1.39e-03

S1_Rrp5_repeat_sc10: 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 S. cerevisiae S1 repeat 10 (sc10). Rrp5 is found in eukaryotes but not in prokaryotes or archaea.


Pssm-ID: 240211 [Multi-domain]  Cd Length: 73  Bit Score: 37.62  E-value: 1.39e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 647806374 284 ARVTNLTDYGCFAELEEGVEGLVHVSEM--DWTNKNIHPSKVvqvGDEVEVMVLDIDEERRRISL 346
Cdd:cd05706    9 GRVTKVNDRYVLVQLGNKVTGPSFITDAldDYSEALPYKFKK---NDIVRACVLSVDVPNKKIAL 70
S1_RecJ_like cd04473
S1_RecJ_like: The S1 domain of the archaea-specific RecJ-like exonuclease. The function of ...
188-255 1.52e-03

S1_RecJ_like: The S1 domain of the archaea-specific RecJ-like exonuclease. The function of this family is not fully understood. In Escherichia coli, RecJ degrades single-stranded DNA in the 5'-3' direction and participates in homologous recombination and mismatch repair.


Pssm-ID: 239919 [Multi-domain]  Cd Length: 77  Bit Score: 37.59  E-value: 1.52e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 647806374 188 LESLQEGQQVKGIVKNLTDYGAFVDLGG-VDGLLHITDMawkrikhpSEIVNVGDEIDVKVLKYDRERN 255
Cdd:cd04473   11 MEDLEVGKLYKGKVNGVAKYGVFVDLNDhVRGLIHRSNL--------LRDYEVGDEVIVQVTDIPENGN 71
PTZ00248 PTZ00248
eukaryotic translation initiation factor 2 subunit 1; Provisional
275-376 1.91e-03

eukaryotic translation initiation factor 2 subunit 1; Provisional


Pssm-ID: 240329 [Multi-domain]  Cd Length: 319  Bit Score: 40.42  E-value: 1.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374 275 RYPESTR-VTARVTNLTDYGCFAELEE--GVEGLVHVSEMdwTNKNIHP-SKVVQVGDEVEVMVLDIDEERRRISLGIKQ 350
Cdd:PTZ00248  13 KFPEEDDlVMVKVVRITEMGAYVSLLEydDIEGMILMSEL--SKRRIRSiNKLIRVGRHEVVVVLRVDKEKGYIDLSKKR 90
                         90       100
                 ....*....|....*....|....*.
gi 647806374 351 CKSNPWEDFSGQFNKGDKISGTIKSI 376
Cdd:PTZ00248  91 VSPEDIEACEEKFSKSKKVHSIMRHI 116
S1_Rrp5_repeat_sc11 cd05707
S1_Rrp5_repeat_sc11: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ...
194-259 2.03e-03

S1_Rrp5_repeat_sc11: 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 S. cerevisiae S1 repeat 11 (sc11). Rrp5 is found in eukaryotes but not in prokaryotes or archaea.


Pssm-ID: 240212 [Multi-domain]  Cd Length: 68  Bit Score: 36.89  E-value: 2.03e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 647806374 194 GQQVKGIVKNLTDYGAFVDLG-GVDGLLHITD------MAWKRIKHPSEIVNvgdeidVKVLKYDRERNRVSL 259
Cdd:cd05707    1 GDVVRGFVKNIANNGVFVTLGrGVDARVRVSElsdsylKDWKKRFKVGQLVK------GKIVSIDPDNGRIEM 67
S1_RpoE cd04460
S1_RpoE: RpoE, S1-like RNA-binding domain. S1-like RNA-binding domains are found in a wide ...
197-222 2.79e-03

S1_RpoE: RpoE, S1-like RNA-binding domain. S1-like RNA-binding domains are found in a wide variety of RNA-associated proteins. RpoE is subunit E of archaeal RNA polymerase. Archaeal cells contain a single RNA polymerase made up of 12 subunits, which are homologous to the 12 subunits (RPB1-12) of eukaryotic RNA polymerase II. RpoE is homologous to Rpa43 of eukaryotic RNA polymerase I, RPB7 of eukaryotic RNA polymerase II, and Rpc25 of eukaryotic RNA polymerase III. RpoE is composed of two domains, the N-terminal RNP (ribonucleoprotein) domain and the C-terminal S1 domain. This S1 domain binds ssRNA and ssDNA. This family is classified based on the C-terminal S1 domain. The function of RpoE is not fully understood. In eukaryotes, RPB7 and RPB4 form a heterodimer that reversibly associates with the RNA polymerase II core.


Pssm-ID: 239907 [Multi-domain]  Cd Length: 99  Bit Score: 37.27  E-value: 2.79e-03
                         10        20
                 ....*....|....*....|....*.
gi 647806374 197 VKGIVKNLTDYGAFVDLGGVDGLLHI 222
Cdd:cd04460    3 VEGEVVEVVDFGAFVRIGPVDGLLHI 28
PRK07252 PRK07252
S1 RNA-binding domain-containing protein;
453-535 2.82e-03

S1 RNA-binding domain-containing protein;


Pssm-ID: 180908 [Multi-domain]  Cd Length: 120  Bit Score: 37.76  E-value: 2.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374 453 GAIVKGVVKEVDAKGAIITLANDIEATLKASEISRDRIEDARNVLKEGEEVEAKIISVDRKSRVIQLSIKSkdVEDEKEA 532
Cdd:PRK07252   4 GDKLKGTITGIKPYGAFVALENGTTGLIHISEIKTGFIDNIHQLLKVGEEVLVQVVDFDEYTGKASLSLRT--LEEEKQH 81

                 ...
gi 647806374 533 IQS 535
Cdd:PRK07252  82 FPH 84
S1_RPS1_repeat_ec1_hs1 cd05687
S1_RPS1_repeat_ec1_hs1: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
366-436 2.88e-03

S1_RPS1_repeat_ec1_hs1: 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 1 of the Escherichia coli and Homo sapiens RPS1 (ec1 and hs1, respectively). Autoantibodies to double-stranded DNA from patients with systemic lupus erythematosus cross-react with the human RPS1 homolog.


Pssm-ID: 240192 [Multi-domain]  Cd Length: 70  Bit Score: 36.35  E-value: 2.88e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 647806374 366 GDKISGTIKSITDFGIFIGLDGGIDGLVHLSDISWNEVgEEAVRRFKKGDELDTVILSVDPERERISLGIK 436
Cdd:cd05687    1 GDIVKGTVVSVDDDEVLVDIGYKSEGIIPISEFSDDPI-ENGEDEVKVGDEVEVYVLRVEDEEGNVVLSKR 70
PRK07400 PRK07400
30S ribosomal protein S1; Reviewed
453-522 5.77e-03

30S ribosomal protein S1; Reviewed


Pssm-ID: 180960 [Multi-domain]  Cd Length: 318  Bit Score: 39.01  E-value: 5.77e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374 453 GAIVKGVVKEVDAKGAIITLANDIEATLKASEISRDRIEDARNVLKEGEEVEAKIISVDRKSRVIQLSIK 522
Cdd:PRK07400  32 GDIVNGTVFSLEPRGALIDIGAKTAAFMPIQEMSINRVEGPEEVLQPNETREFFILSDENEDGQLTLSIR 101
rpsA TIGR00717
ribosomal protein S1; This model describes ribosomal protein S1, RpsA. This protein is found ...
365-536 6.49e-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: 6.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374  365 KGDKISGTIKSITDFGIFIGLDGGIDGLVHLSDIswnevgEEAVRRFKKGDELDTVILSVDPERERISLG-IKQLESDPF 443
Cdd:TIGR00717  18 PGSIVKGTVVAINKDTVFVDVGLKSEGRIPKEEF------LDAPLEIQVGDEVEVYLDRVEDRFGETVLSrEKAQRHELW 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647806374  444 SEYVQENDKGAIVKG-VVKEVdaKGAIITLANDIEATLKASEISRDRIEDARNVLkeGEEVEAKIISVDRKSRVIQLSIK 522
Cdd:TIGR00717  92 IKLEKAYEEGSIVEGkIVGKV--KGGFIVDLNGVEAFLPGSQVDVKPIKDLDSLI--GKTLKFKIIKLDQKRNNIVVSRR 167
                         170
                  ....*....|....*
gi 647806374  523 SK-DVEDEKEAIQSL 536
Cdd:TIGR00717 168 AYlEEERSQAREELL 182
PRK08582 PRK08582
RNA-binding protein S1;
453-525 6.51e-03

RNA-binding protein S1;


Pssm-ID: 236305 [Multi-domain]  Cd Length: 139  Bit Score: 37.32  E-value: 6.51e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 647806374 453 GAIVKGVVKEVDAKGAIITLANDIEATLKASEISRDRIEDARNVLKEGEEVEAKIISVDRKSRvIQLSI-KSKD 525
Cdd:PRK08582   6 GSKLQGKVTGITNFGAFVELPEGKTGLVHISEVADNYVKDINDHLKVGDEVEVKVLNVEDDGK-IGLSIkKAKD 78
COG1107 COG1107
Archaea-specific RecJ-like exonuclease, contains DnaJ-type Zn finger domain [Replication, ...
284-347 7.92e-03

Archaea-specific RecJ-like exonuclease, contains DnaJ-type Zn finger domain [Replication, recombination and repair];


Pssm-ID: 440724 [Multi-domain]  Cd Length: 626  Bit Score: 39.05  E-value: 7.92e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 647806374 284 ARVTNLTDYGCFAELEEGVEGLVHVSEMDWTNKnihpskvvqVGDEVEVMVLDIdEERRRISLG 347
Cdd:COG1107   45 GTVDGVADFGVFVDLNDHVTGLLHRSELDQDWE---------VGDEVFVQVKEV-RDNGNVDLG 98
 
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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