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Conserved domains on  [gi|2258881609|gb|USO01925|]
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MAG: 30S ribosomal protein S1 [Alphaproteobacteria bacterium]

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
10-557 0e+00

30S ribosomal protein S1; Reviewed


:

Pssm-ID: 235775 [Multi-domain]  Cd Length: 565  Bit Score: 782.04  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609  10 FSALLDDHMGEHTL-LGKVLKGRIVRQDREAVTIDVGLKSEGRVPLREFATGGNVPELKVGDLVDVYVERMEGATGDIVL 88
Cdd:PRK06299   15 FAELFEESLKESETrEGSIVKGTVVAIDKDYVLVDVGLKSEGRIPLEEFKNEQGELEVKVGDEVEVYVERIEDGFGETVL 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609  89 SHERARREASWIELEKKSESEEHVTGVIFSRVKGGFTVDLGGAIAFLPGSQVDVRPVKDVDALMGVAQPFVILKMDRPRG 168
Cdd:PRK06299   95 SREKAKRLEAWDKLEKAFENGEIVEGVINGKVKGGFTVDLNGVEAFLPGSQVDVRPVRDTDPLEGKELEFKVIKLDKKRN 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 169 NIVVSRRAILEEGQAGAREELVGRLEEGAVLDGMIKNVTDYGAFIDLGGVDGLLHVTDISWQRVNHPSQVLKVGETIKVK 248
Cdd:PRK06299  175 NIVVSRRAVLEEERAEEREELLENLEEGQVVEGVVKNITDYGAFVDLGGVDGLLHITDISWKRVNHPSEVVNVGDEVKVK 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 249 VIKYNKENHRISLGIKQLSDDPWKDVETKFALGSTLKGKVTNVTDYGAFVEIGGGVEGLIHVSEISWTRKNVQPSNVLSV 328
Cdd:PRK06299  255 VLKFDKEKKRVSLGLKQLGEDPWEAIEKKYPVGSKVKGKVTNITDYGAFVELEEGIEGLVHVSEMSWTKKNKHPSKVVSV 334
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 329 GDEINVRVLEIEPVKRRIALGYKQCLENPWEQLARVYPSGSEAKGEIRNITEFGLFVSLTDDIDGMVHMNDLSWEKNADE 408
Cdd:PRK06299  335 GQEVEVMVLEIDEEKRRISLGLKQCKENPWEEFAEKYPVGDVVEGKVKNITDFGAFVGLEGGIDGLVHLSDISWDKKGEE 414
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 409 AIKEYKKGQVVQVKILEVDSQKERVALGIKQLQSDPFAGAVADLRKGQVVTCEVSAVQSDGIMVTFGEGMSSFIKRAELS 488
Cdd:PRK06299  415 AVELYKKGDEVEAVVLKVDVEKERISLGIKQLEEDPFEEFAKKHKKGSIVTGTVTEVKDKGAFVELEDGVEGLIRASELS 494
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 489 SDRNERRPDRFAVGEKVDAKITTIDPSSRRVSVSIRAREQEEERVAMEKYGST-DSGASLGDILGEALAK 557
Cdd:PRK06299  495 RDRVEDATEVLKVGDEVEAKVINIDRKNRRISLSIKALDEAEEKEAIAEYNSAsDSKTTLGDLLKAALKG 564
 
Name Accession Description Interval E-value
rpsA PRK06299
30S ribosomal protein S1; Reviewed
10-557 0e+00

30S ribosomal protein S1; Reviewed


Pssm-ID: 235775 [Multi-domain]  Cd Length: 565  Bit Score: 782.04  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609  10 FSALLDDHMGEHTL-LGKVLKGRIVRQDREAVTIDVGLKSEGRVPLREFATGGNVPELKVGDLVDVYVERMEGATGDIVL 88
Cdd:PRK06299   15 FAELFEESLKESETrEGSIVKGTVVAIDKDYVLVDVGLKSEGRIPLEEFKNEQGELEVKVGDEVEVYVERIEDGFGETVL 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609  89 SHERARREASWIELEKKSESEEHVTGVIFSRVKGGFTVDLGGAIAFLPGSQVDVRPVKDVDALMGVAQPFVILKMDRPRG 168
Cdd:PRK06299   95 SREKAKRLEAWDKLEKAFENGEIVEGVINGKVKGGFTVDLNGVEAFLPGSQVDVRPVRDTDPLEGKELEFKVIKLDKKRN 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 169 NIVVSRRAILEEGQAGAREELVGRLEEGAVLDGMIKNVTDYGAFIDLGGVDGLLHVTDISWQRVNHPSQVLKVGETIKVK 248
Cdd:PRK06299  175 NIVVSRRAVLEEERAEEREELLENLEEGQVVEGVVKNITDYGAFVDLGGVDGLLHITDISWKRVNHPSEVVNVGDEVKVK 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 249 VIKYNKENHRISLGIKQLSDDPWKDVETKFALGSTLKGKVTNVTDYGAFVEIGGGVEGLIHVSEISWTRKNVQPSNVLSV 328
Cdd:PRK06299  255 VLKFDKEKKRVSLGLKQLGEDPWEAIEKKYPVGSKVKGKVTNITDYGAFVELEEGIEGLVHVSEMSWTKKNKHPSKVVSV 334
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 329 GDEINVRVLEIEPVKRRIALGYKQCLENPWEQLARVYPSGSEAKGEIRNITEFGLFVSLTDDIDGMVHMNDLSWEKNADE 408
Cdd:PRK06299  335 GQEVEVMVLEIDEEKRRISLGLKQCKENPWEEFAEKYPVGDVVEGKVKNITDFGAFVGLEGGIDGLVHLSDISWDKKGEE 414
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 409 AIKEYKKGQVVQVKILEVDSQKERVALGIKQLQSDPFAGAVADLRKGQVVTCEVSAVQSDGIMVTFGEGMSSFIKRAELS 488
Cdd:PRK06299  415 AVELYKKGDEVEAVVLKVDVEKERISLGIKQLEEDPFEEFAKKHKKGSIVTGTVTEVKDKGAFVELEDGVEGLIRASELS 494
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 489 SDRNERRPDRFAVGEKVDAKITTIDPSSRRVSVSIRAREQEEERVAMEKYGST-DSGASLGDILGEALAK 557
Cdd:PRK06299  495 RDRVEDATEVLKVGDEVEAKVINIDRKNRRISLSIKALDEAEEKEAIAEYNSAsDSKTTLGDLLKAALKG 564
rpsA TIGR00717
ribosomal protein S1; This model describes ribosomal protein S1, RpsA. This protein is found ...
20-524 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: 562.82  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609  20 EHTLLGKVLKGRIVRQDREAVTIDVGLKSEGRVPLREFAtggNVP-ELKVGDLVDVYVERMEGATGDIVLSHERARREAS 98
Cdd:TIGR00717  14 EETRPGSIVKGTVVAINKDTVFVDVGLKSEGRIPKEEFL---DAPlEIQVGDEVEVYLDRVEDRFGETVLSREKAQRHEL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609  99 WIELEKKSESEEHVTGVIFSRVKGGFTVDLGGAIAFLPGSQVDVRPVKDVDALMGVAQPFVILKMDRPRGNIVVSRRAIL 178
Cdd:TIGR00717  91 WIKLEKAYEEGSIVEGKIVGKVKGGFIVDLNGVEAFLPGSQVDVKPIKDLDSLIGKTLKFKIIKLDQKRNNIVVSRRAYL 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 179 EEGQAGAREELVGRLEEGAVLDGMIKNVTDYGAFIDLGGVDGLLHVTDISWQRVNHPSQVLKVGETIKVKVIKYNKENHR 258
Cdd:TIGR00717 171 EEERSQAREELLENLKEGDVVKGVVKNITDFGAFVDLGGVDGLLHITDMSWKRVKHPSEYVKVGQEVKVKVIKFDKEKGR 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 259 ISLGIKQLSDDPWKDVETKFALGSTLKGKVTNVTDYGAFVEIGGGVEGLIHVSEISWTRKNVQPSNVLSVGDEINVRVLE 338
Cdd:TIGR00717 251 ISLSLKQLGEDPWEAIEKKFPVGDKITGRVTNLTDYGVFVEIEEGIEGLVHVSEMSWVKKNSHPSKVVKKGDEVEVMILD 330
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 339 IEPVKRRIALGYKQCLENPWEQLARVYPSGSEAKGEIRNITEFGLFVSLTDDIDGMVHMNDLSWEKNADEAIKEYKKGQV 418
Cdd:TIGR00717 331 IDPERRRLSLGLKQCKANPWEQFEEKHPVGDRVTGKIKKITDFGAFVELEGGIDGLIHLSDISWDKDGREADHLYKKGDE 410
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 419 VQVKILEVDSQKERVALGIKQLQSDPFAGAVADLRKGQVVTCEVSAVQSDGIMVTFGEGMSSFIKRAELSSDRNERRPDR 498
Cdd:TIGR00717 411 IEAVVLAVDKEKKRISLGVKQLTENPWEKFAAKYKVGSVVKGKVTEIKDFGAFVELPGGVEGLIRNSELSENRDEDKTDE 490
                         490       500
                  ....*....|....*....|....*.
gi 2258881609 499 FAVGEKVDAKITTIDPSSRRVSVSIR 524
Cdd:TIGR00717 491 IKVGDEVEAKVVDIDKKNRKVSLSVK 516
RpsA COG0539
Ribosomal protein S1 [Translation, ribosomal structure and biogenesis]; Ribosomal protein S1 ...
25-353 3.14e-171

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: 488.79  E-value: 3.14e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609  25 GKVLKGRIVRQDREAVTIDVGLKSEGRVPLREFATGGNVPELKVGDLVDVYVERMEGATGDIVLSHERARREASWIELEK 104
Cdd:COG0539    19 GDIVKGTVVSIDDDEVLVDIGYKSEGIIPLSEFSDEPGELEVKVGDEVEVYVEKVEDGEGEIVLSKKKADREKAWEELEE 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 105 KSESEEHVTGVIFSRVKGGFTVDLGGAIAFLPGSQVDVRPVKDVDALMGVAQPFVILKMDRPRGNIVVSRRAILEEGQAG 184
Cdd:COG0539    99 AFENGEPVEGKVKGVVKGGLIVDIGGVRAFLPASQVDVRPVRDLDEYVGKTLEFKIIKLDRKRNNVVVSRRAVLEEEREE 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 185 AREELVGRLEEGAVLDGMIKNVTDYGAFIDLGGVDGLLHVTDISWQRVNHPSQVLKVGETIKVKVIKYNKENHRISLGIK 264
Cdd:COG0539   179 KREELLEKLEEGDVVEGTVKNITDFGAFVDLGGVDGLLHISEISWGRVKHPSEVLKVGDEVEVKVLKIDREKERISLSLK 258
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 265 QLSDDPWKDVETKFALGSTLKGKVTNVTDYGAFVEIGGGVEGLIHVSEISWTRKNVQPSNVLSVGDEINVRVLEIEPVKR 344
Cdd:COG0539   259 QLQPDPWENIAEKYPVGDVVKGKVTRLTDFGAFVELEPGVEGLVHISEMSWTKRVAHPSDVVKVGDEVEVKVLDIDPEER 338

                  ....*....
gi 2258881609 345 RIALGYKQC 353
Cdd:COG0539   339 RISLSIKQL 347
S1_RPS1_repeat_ec3 cd05688
S1_RPS1_repeat_ec3: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
195-262 3.86e-33

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: 120.81  E-value: 3.86e-33
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2258881609 195 EGAVLDGMIKNVTDYGAFIDLGGVDGLLHVTDISWQRVNHPSQVLKVGETIKVKVIKYNKENHRISLG 262
Cdd:cd05688     1 EGDVVEGTVKSITDFGAFVDLGGVDGLLHISDMSWGRVKHPSEVVNVGDEVEVKVLKIDKERKRISLG 68
S1 smart00316
Ribosomal protein S1-like RNA-binding domain;
281-351 1.93e-19

Ribosomal protein S1-like RNA-binding domain;


Pssm-ID: 197648 [Multi-domain]  Cd Length: 72  Bit Score: 82.65  E-value: 1.93e-19
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2258881609  281 GSTLKGKVTNVTDYGAFVEIGGGVEGLIHVSEISWtRKNVQPSNVLSVGDEINVRVLEIEPVKRRIALGYK 351
Cdd:smart00316   3 GDVVEGTVTEITPGGAFVDLGNGVEGLIPISELSD-KRVKDPEEVLKVGDEVKVKVLSVDEEKGRIILSLK 72
S1 pfam00575
S1 RNA binding domain; The S1 domain occurs in a wide range of RNA associated proteins. It is ...
278-350 4.80e-16

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: 72.71  E-value: 4.80e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2258881609 278 FALGSTLKGKVTNVTDYGAFVEIGGGVEGLIHVSEISWtRKNVQPSNVLSVGDEINVRVLEIEPVKRRIALGY 350
Cdd:pfam00575   1 PEKGDVVEGEVTRVTKGGAFVDLGNGVEGFIPISELSD-DHVEDPDEVIKVGDEVKVKVLKVDKDRRRIILSI 72
S1_dom_CvfD NF040579
CvfD/Ygs/GSP13 family RNA-binding post-transcriptional regulator; CvfD, Ygs, and GSP13 form a ...
281-348 6.44e-15

CvfD/Ygs/GSP13 family RNA-binding post-transcriptional regulator; CvfD, Ygs, and GSP13 form a family of full-length homologs of RNA-binding proteins from the Firmicutes with a single copy of the S1 domain. Several members of the family have been characterized as general stress proteins, and the most recently characterized, CvfD, was shown to act as a post-transcriptional regulator.


Pssm-ID: 468553 [Multi-domain]  Cd Length: 113  Bit Score: 70.92  E-value: 6.44e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 281 GSTLKGKVTNVTDYGAFVEIGGGVEGLIHVSEISwTR--KNVqpSNVLSVGDEINVRVLEIEPVKRRIAL 348
Cdd:NF040579    4 GDIVEGKVTGIQPYGAFVALDEHTQGLIHISEIK-HGyvKDI--NDFLKVGQEVKVKVLDIDEYTGKISL 70
 
Name Accession Description Interval E-value
rpsA PRK06299
30S ribosomal protein S1; Reviewed
10-557 0e+00

30S ribosomal protein S1; Reviewed


Pssm-ID: 235775 [Multi-domain]  Cd Length: 565  Bit Score: 782.04  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609  10 FSALLDDHMGEHTL-LGKVLKGRIVRQDREAVTIDVGLKSEGRVPLREFATGGNVPELKVGDLVDVYVERMEGATGDIVL 88
Cdd:PRK06299   15 FAELFEESLKESETrEGSIVKGTVVAIDKDYVLVDVGLKSEGRIPLEEFKNEQGELEVKVGDEVEVYVERIEDGFGETVL 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609  89 SHERARREASWIELEKKSESEEHVTGVIFSRVKGGFTVDLGGAIAFLPGSQVDVRPVKDVDALMGVAQPFVILKMDRPRG 168
Cdd:PRK06299   95 SREKAKRLEAWDKLEKAFENGEIVEGVINGKVKGGFTVDLNGVEAFLPGSQVDVRPVRDTDPLEGKELEFKVIKLDKKRN 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 169 NIVVSRRAILEEGQAGAREELVGRLEEGAVLDGMIKNVTDYGAFIDLGGVDGLLHVTDISWQRVNHPSQVLKVGETIKVK 248
Cdd:PRK06299  175 NIVVSRRAVLEEERAEEREELLENLEEGQVVEGVVKNITDYGAFVDLGGVDGLLHITDISWKRVNHPSEVVNVGDEVKVK 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 249 VIKYNKENHRISLGIKQLSDDPWKDVETKFALGSTLKGKVTNVTDYGAFVEIGGGVEGLIHVSEISWTRKNVQPSNVLSV 328
Cdd:PRK06299  255 VLKFDKEKKRVSLGLKQLGEDPWEAIEKKYPVGSKVKGKVTNITDYGAFVELEEGIEGLVHVSEMSWTKKNKHPSKVVSV 334
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 329 GDEINVRVLEIEPVKRRIALGYKQCLENPWEQLARVYPSGSEAKGEIRNITEFGLFVSLTDDIDGMVHMNDLSWEKNADE 408
Cdd:PRK06299  335 GQEVEVMVLEIDEEKRRISLGLKQCKENPWEEFAEKYPVGDVVEGKVKNITDFGAFVGLEGGIDGLVHLSDISWDKKGEE 414
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 409 AIKEYKKGQVVQVKILEVDSQKERVALGIKQLQSDPFAGAVADLRKGQVVTCEVSAVQSDGIMVTFGEGMSSFIKRAELS 488
Cdd:PRK06299  415 AVELYKKGDEVEAVVLKVDVEKERISLGIKQLEEDPFEEFAKKHKKGSIVTGTVTEVKDKGAFVELEDGVEGLIRASELS 494
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 489 SDRNERRPDRFAVGEKVDAKITTIDPSSRRVSVSIRAREQEEERVAMEKYGST-DSGASLGDILGEALAK 557
Cdd:PRK06299  495 RDRVEDATEVLKVGDEVEAKVINIDRKNRRISLSIKALDEAEEKEAIAEYNSAsDSKTTLGDLLKAALKG 564
rpsA TIGR00717
ribosomal protein S1; This model describes ribosomal protein S1, RpsA. This protein is found ...
20-524 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: 562.82  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609  20 EHTLLGKVLKGRIVRQDREAVTIDVGLKSEGRVPLREFAtggNVP-ELKVGDLVDVYVERMEGATGDIVLSHERARREAS 98
Cdd:TIGR00717  14 EETRPGSIVKGTVVAINKDTVFVDVGLKSEGRIPKEEFL---DAPlEIQVGDEVEVYLDRVEDRFGETVLSREKAQRHEL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609  99 WIELEKKSESEEHVTGVIFSRVKGGFTVDLGGAIAFLPGSQVDVRPVKDVDALMGVAQPFVILKMDRPRGNIVVSRRAIL 178
Cdd:TIGR00717  91 WIKLEKAYEEGSIVEGKIVGKVKGGFIVDLNGVEAFLPGSQVDVKPIKDLDSLIGKTLKFKIIKLDQKRNNIVVSRRAYL 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 179 EEGQAGAREELVGRLEEGAVLDGMIKNVTDYGAFIDLGGVDGLLHVTDISWQRVNHPSQVLKVGETIKVKVIKYNKENHR 258
Cdd:TIGR00717 171 EEERSQAREELLENLKEGDVVKGVVKNITDFGAFVDLGGVDGLLHITDMSWKRVKHPSEYVKVGQEVKVKVIKFDKEKGR 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 259 ISLGIKQLSDDPWKDVETKFALGSTLKGKVTNVTDYGAFVEIGGGVEGLIHVSEISWTRKNVQPSNVLSVGDEINVRVLE 338
Cdd:TIGR00717 251 ISLSLKQLGEDPWEAIEKKFPVGDKITGRVTNLTDYGVFVEIEEGIEGLVHVSEMSWVKKNSHPSKVVKKGDEVEVMILD 330
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 339 IEPVKRRIALGYKQCLENPWEQLARVYPSGSEAKGEIRNITEFGLFVSLTDDIDGMVHMNDLSWEKNADEAIKEYKKGQV 418
Cdd:TIGR00717 331 IDPERRRLSLGLKQCKANPWEQFEEKHPVGDRVTGKIKKITDFGAFVELEGGIDGLIHLSDISWDKDGREADHLYKKGDE 410
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 419 VQVKILEVDSQKERVALGIKQLQSDPFAGAVADLRKGQVVTCEVSAVQSDGIMVTFGEGMSSFIKRAELSSDRNERRPDR 498
Cdd:TIGR00717 411 IEAVVLAVDKEKKRISLGVKQLTENPWEKFAAKYKVGSVVKGKVTEIKDFGAFVELPGGVEGLIRNSELSENRDEDKTDE 490
                         490       500
                  ....*....|....*....|....*.
gi 2258881609 499 FAVGEKVDAKITTIDPSSRRVSVSIR 524
Cdd:TIGR00717 491 IKVGDEVEAKVVDIDKKNRKVSLSVK 516
RpsA COG0539
Ribosomal protein S1 [Translation, ribosomal structure and biogenesis]; Ribosomal protein S1 ...
25-353 3.14e-171

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: 488.79  E-value: 3.14e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609  25 GKVLKGRIVRQDREAVTIDVGLKSEGRVPLREFATGGNVPELKVGDLVDVYVERMEGATGDIVLSHERARREASWIELEK 104
Cdd:COG0539    19 GDIVKGTVVSIDDDEVLVDIGYKSEGIIPLSEFSDEPGELEVKVGDEVEVYVEKVEDGEGEIVLSKKKADREKAWEELEE 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 105 KSESEEHVTGVIFSRVKGGFTVDLGGAIAFLPGSQVDVRPVKDVDALMGVAQPFVILKMDRPRGNIVVSRRAILEEGQAG 184
Cdd:COG0539    99 AFENGEPVEGKVKGVVKGGLIVDIGGVRAFLPASQVDVRPVRDLDEYVGKTLEFKIIKLDRKRNNVVVSRRAVLEEEREE 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 185 AREELVGRLEEGAVLDGMIKNVTDYGAFIDLGGVDGLLHVTDISWQRVNHPSQVLKVGETIKVKVIKYNKENHRISLGIK 264
Cdd:COG0539   179 KREELLEKLEEGDVVEGTVKNITDFGAFVDLGGVDGLLHISEISWGRVKHPSEVLKVGDEVEVKVLKIDREKERISLSLK 258
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 265 QLSDDPWKDVETKFALGSTLKGKVTNVTDYGAFVEIGGGVEGLIHVSEISWTRKNVQPSNVLSVGDEINVRVLEIEPVKR 344
Cdd:COG0539   259 QLQPDPWENIAEKYPVGDVVKGKVTRLTDFGAFVELEPGVEGLVHISEMSWTKRVAHPSDVVKVGDEVEVKVLDIDPEER 338

                  ....*....
gi 2258881609 345 RIALGYKQC 353
Cdd:COG0539   339 RISLSIKQL 347
PRK12269 PRK12269
bifunctional cytidylate kinase/ribosomal protein S1; Provisional
25-557 3.61e-110

bifunctional cytidylate kinase/ribosomal protein S1; Provisional


Pssm-ID: 105491 [Multi-domain]  Cd Length: 863  Bit Score: 349.01  E-value: 3.61e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609  25 GKVLKGRIVRQDREAVTIDVGLKSEGRVPLREFatggNVPElKVGDLVDVYVERMEGATGDivLSHERARREASWIELEK 104
Cdd:PRK12269  322 GSVRMGTVVQVNAGTVFVDIGGKSEGRVPVEEF----EAPP-KAGDGVRVYVERVTPYGPE--LSKTKADRLGLKVKLRD 394
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 105 KSESEEHVTGVI--FSRVKGGFTVDLG-GAIAFLPGSQVDVRPVKDVDALMGVAQPFVI-----LKMDRPRGNIVVSRRA 176
Cdd:PRK12269  395 AERDGTPVEGRIvrLTEKKSGFEVDLGaGMMAFLPISQSDCQKVDAPESLIGLTSKFYIerisqSKQHRGNDNIVINRRR 474
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 177 ILEEGQAGAREELVGRLEEGAVLDGMIKNVTDYGAFIDLGGVDGLLHVTDISWQRVNHPSQVLKVGETIKVKVIKYNKEN 256
Cdd:PRK12269  475 YLEERARQAREEFFNSVHIEDSVSGVVKSFTSFGAFIDLGGFDGLLHVNDMSWGHVARPREFVKKGQTIELKVIRLDQAE 554
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 257 HRISLGIKQLSDDPWKDVETKFALGSTLKGKVTNVTDYGAFVEIGGGVEGLIHVSEISWTRKNVQPSNVLSVGDEINVRV 336
Cdd:PRK12269  555 KRINLSLKHFQPDPWLEFENKFGVNDVVKGRVTKIADFGAFIELAEGIEGLAHISEFSWVKKTSKPSDMVKIGDEVECMI 634
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 337 LEIEPVKRRIALGYKQCLENPWEQLARVYPSGSEAKGEIRNITEFGLFVSLTDDIDGMVHMNDLSWEKNADEAIKEYKKG 416
Cdd:PRK12269  635 LGYDIQAGRVSLGLKQVTANPWEEIEARYPVGARFTRRIVKVTNAGAFIEMEEGIDGFLHVDDLSWVKRTRPADHELEVG 714
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 417 QVVQVKILEVDSQKERVALGIKQLQSDPFAGAVADLRKGQVVTCEVSAVQSDGIMVTFGEGMSSFIKRAELSSDRNERRP 496
Cdd:PRK12269  715 KEIECMVIECDPQARRIRLGVKQLSDNPWQVFANAYGVGSTVEGEVSSVTDFGIFVRVPGGVEGLVRKQHLVENRDGDPG 794
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2258881609 497 D---RFAVGEKVDAKITTIDPSSRRVSVSIRAREQEEERVAMEKYGSTDSGA-----SLGDILGEALAK 557
Cdd:PRK12269  795 EalrKYAVGDRVKAVIVDMNVKDRKVAFSVRDYQRKVQRDELSRYMSAPRGEdegsfTLGDLMRQTSGK 863
PRK00087 PRK00087
bifunctional 4-hydroxy-3-methylbut-2-enyl diphosphate reductase/30S ribosomal protein S1;
25-366 2.36e-108

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


Pssm-ID: 234623 [Multi-domain]  Cd Length: 647  Bit Score: 338.46  E-value: 2.36e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609  25 GKVLKGRIVRQDREAVTIDVGLKSEGRVPLREFATGGN---VPELKVGDLVDVYVERMEGATGDIVLSHERARREASWIE 101
Cdd:PRK00087  303 GDIVKGTVVSVNENEVFVDVGYKSEGVIPLRELTLDEIsslKESVKVGDEIEVKVLKLEDEDGYVVLSKKEADREKAWKE 382
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 102 LEKKSESEEHVTGVIFSRVKGGFTVDLGGAIAFLPGSQVDVRPVKDVDALMGVAQPFVILKMDRP-RGNIVVSRRAILEE 180
Cdd:PRK00087  383 LEEAFENGEPVKGKVKEVVKGGLLVDYGGVRAFLPASHVELGYVEDLSEYKGQELEVKIIEFNRKrRKKVVLSRKAILEE 462
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 181 GQAGAREELVGRLEEGAVLDGMIKNVTDYGAFIDLGGVDGLLHVTDISWQRVNHPSQVLKVGETIKVKVIKYNKENHRIS 260
Cdd:PRK00087  463 EKEKKKEETWNSLEEGDVVEGEVKRLTDFGAFVDIGGVDGLLHVSEISWGRVEKPSDVLKVGDEIKVYILDIDKENKKLS 542
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 261 LGIKQLSDDPWKDVETKFALGSTLKGKVTNVTDYGAFVEIGGGVEGLIHVSEISWTRkNVQPSNVLSVGDEINVRVLEIE 340
Cdd:PRK00087  543 LSLKKLLPDPWENVEEKYPVGSIVLGKVVRIAPFGAFVELEPGVDGLVHISQISWKR-IDKPEDVLSEGEEVKAKILEVD 621
                         330       340
                  ....*....|....*....|....*.
gi 2258881609 341 PVKRRIALGYKQCLENPWEQLARVYP 366
Cdd:PRK00087  622 PEEKRIRLSIKEVEEEPGDIEKVELE 647
rpsA PRK13806
30S ribosomal protein S1; Provisional
7-436 1.91e-98

30S ribosomal protein S1; Provisional


Pssm-ID: 237516 [Multi-domain]  Cd Length: 491  Bit Score: 307.81  E-value: 1.91e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609   7 EGAFSALLDDHMGE-HTLL--GKVLKGRIVRQDREAVTIDVGLKSEGRVPLREFA-TGGNVPeLKVGDLVDVYVERMEGa 82
Cdd:PRK13806   14 SESFAELLEAYEGErKTELrvGDKITGTVIAITEDSVFVDTGSKVDGVVDRAELLdADGELT-VAVGDEVELYVVSVNG- 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609  83 tGDIVLSHE-------RARREASwielekksESEEHVTGVIFSRVKGGFTVDLGGAIAFLPGSQVDVRPVKDVDALMGVA 155
Cdd:PRK13806   92 -QEIRLSKAlsgqggaAMLEEAY--------ENGVPVEGKVTGTCKGGFNVEVLGRRAFCPVSQIDLRYVEDPESYVGQT 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 156 QPFVILKMDRPRGNIVVSRRAILEEGQAGAREELVGRLEEGAVLDGMIKNVTDYGAFIDLG-GVDGLLHVTDISWQRVNH 234
Cdd:PRK13806  163 FQFLITRVEENGRNIVVSRRALLEREQKEALEAFMETVKEGDVVEGTVTRLAPFGAFVELApGVEGMVHISELSWSRVQK 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 235 PSQVLKVGETIKVKVIKYNKENH----RISLGIKQLSDDPWKDVETKFALGSTLKGKVTNVTDYGAFVEIGGGVEGLIHV 310
Cdd:PRK13806  243 ADEAVSVGDTVRVKVLGIERAKKgkglRISLSIKQAGGDPWDTVGDRLKAGDKVTGKVVRLAPFGAFVEILPGIEGLVHV 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 311 SEISWTRKNVQPSNVLSVGDEINVRVLEIEPVKRRIALGYKQCLENPWEQLARVYPSGSEAKGEIRNITEFGLFVSLTDD 390
Cdd:PRK13806  323 SEMSWTRRVNKPEDVVAPGDAVAVKIKDIDPAKRRISLSLRDAEGDPWADVAERFAPGTTVTGTVEKRAQFGLFVNLAPG 402
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 2258881609 391 IDGMVHMNDLSWEKNADEAIKeYKKGQVVQVKILEVDSQKERVALG 436
Cdd:PRK13806  403 VTGLLPASVISRAGKPATYEK-LKPGDSVTLVVEEIDTAKRKISLA 447
rpsA PRK06676
30S ribosomal protein S1; Reviewed
25-357 2.98e-96

30S ribosomal protein S1; Reviewed


Pssm-ID: 235851 [Multi-domain]  Cd Length: 390  Bit Score: 298.71  E-value: 2.98e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609  25 GKVLKGRIVRQDREAVTIDV-GLKSEGRVPLREFATGGNVP---ELKVGDLVDVYVERMEGATGDIVLSHERARREASWI 100
Cdd:PRK06676   18 GDVVTGEVLKVEDKQVFVNIeGYKVEGVIPISELSNDHIEDindVVKVGDELEVYVLKVEDGEGNLLLSKRRLEAEKAWD 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 101 ELEKKSESEEHVTGVIFSRVKGGFTVDLGGAIAFLPGSQVDVRPVKDVDALMGVAQPFVILKMDRPRGNIVVSRRAILEE 180
Cdd:PRK06676   98 KLEEKFEEGEVVEVKVTEVVKGGLVVDVEGVRGFIPASLISTRFVEDFSDFKGKTLEVKIIELDPEKNRVILSRRAVVEE 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 181 GQAGAREELVGRLEEGAVLDGMIKNVTDYGAFIDLGGVDGLLHVTDISWQRVNHPSQVLKVGETIKVKVIKYNKENHRIS 260
Cdd:PRK06676  178 ERAAKKEELLSSLKEGDVVEGTVARLTDFGAFVDIGGVDGLVHISELSHERVEKPSEVVSVGQEVEVKVLSIDWETERIS 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 261 LGIKQLSDDPWKDVETKFALGSTLKGKVTNVTDYGAFVEIGGGVEGLIHVSEISWTRKNvQPSNVLSVGDEINVRVLEIE 340
Cdd:PRK06676  258 LSLKDTLPGPWEGVEEKLPEGDVIEGTVKRLTDFGAFVEVLPGVEGLVHISQISHKHIA-TPSEVLEEGQEVKVKVLEVN 336
                         330
                  ....*....|....*..
gi 2258881609 341 PVKRRIALGYKQCLENP 357
Cdd:PRK06676  337 EEEKRISLSIKALEEAP 353
rpsA PRK07899
30S ribosomal protein S1; Reviewed
25-355 8.53e-79

30S ribosomal protein S1; Reviewed


Pssm-ID: 236126 [Multi-domain]  Cd Length: 486  Bit Score: 256.51  E-value: 8.53e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609  25 GKVLKGRIVRQDREAVTIDVGLKSEGRVPLREFATGGNV-PE--LKVGDLVDVYVERMEGATGDIVLSHERARREASWIE 101
Cdd:PRK07899   36 GDIVEGTVVKVDRDEVLLDIGYKTEGVIPSRELSIKHDVdPNevVEVGDEVEALVLQKEDKEGRLILSKKRAQYERAWGT 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 102 LEKKSESEEHVTGVIFSRVKGGFTVDLGgAIAFLPGSQVDVRPVKDVdalmgvaQPFV-------ILKMDRPRGNIVVSR 174
Cdd:PRK07899  116 IEKIKEKDGVVTGTVIEVVKGGLILDIG-LRGFLPASLVEMRRVRDL-------QPYIgqeieakIIELDKNRNNVVLSR 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 175 RAILEEGQAGAREELVGRLEEGAVLDGMIKNVTDYGAFIDLGGVDGLLHVTDISWQRVNHPSQVLKVGETIKVKVIKYNK 254
Cdd:PRK07899  188 RAWLEQTQSEVRSEFLNQLQKGQVRKGVVSSIVNFGAFVDLGGVDGLVHVSELSWKHIDHPSEVVEVGQEVTVEVLDVDM 267
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 255 ENHRISLGIKQLSDDPWKDVETKFALGSTLKGKVTNVTDYGAFVEIGGGVEGLIHVSEISwTRKNVQPSNVLSVGDEINV 334
Cdd:PRK07899  268 DRERVSLSLKATQEDPWQQFARTHAIGQIVPGKVTKLVPFGAFVRVEEGIEGLVHISELA-ERHVEVPEQVVQVGDEVFV 346
                         330       340
                  ....*....|....*....|.
gi 2258881609 335 RVLEIEPVKRRIALGYKQCLE 355
Cdd:PRK07899  347 KVIDIDLERRRISLSLKQANE 367
S1_RPS1_repeat_ec3 cd05688
S1_RPS1_repeat_ec3: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
195-262 3.86e-33

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: 120.81  E-value: 3.86e-33
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2258881609 195 EGAVLDGMIKNVTDYGAFIDLGGVDGLLHVTDISWQRVNHPSQVLKVGETIKVKVIKYNKENHRISLG 262
Cdd:cd05688     1 EGDVVEGTVKSITDFGAFVDLGGVDGLLHISDMSWGRVKHPSEVVNVGDEVEVKVLKIDKERKRISLG 68
PRK07400 PRK07400
30S ribosomal protein S1; Reviewed
10-270 2.44e-29

30S ribosomal protein S1; Reviewed


Pssm-ID: 180960 [Multi-domain]  Cd Length: 318  Bit Score: 118.36  E-value: 2.44e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609  10 FSALLDDHmGEHTLLGKVLKGRIVRQDREAVTIDVGLKSEGRVPLREFATGG-NVPE--LKVGDLVDVYVERMEGATGDI 86
Cdd:PRK07400   18 FAALLDKY-DYHFKPGDIVNGTVFSLEPRGALIDIGAKTAAFMPIQEMSINRvEGPEevLQPNETREFFILSDENEDGQL 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609  87 VLSHERARREASWIELEKKSESEEHVTGVIFSRVKGGFTVDLGGAIAFLPGSQVDVRPVKDvdALMGVAQPFVILKMDRP 166
Cdd:PRK07400   97 TLSIRRIEYMRAWERVRQLQKEDATVRSEVFATNRGGALVRIEGLRGFIPGSHISTRKPKE--ELVGEELPLKFLEVDEE 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 167 RGNIVVS-RRAILEEGqagareelVGRLEEGAVLDGMIKNVTDYGAFIDLGGVDGLLHVTDISWQRVNHPSQVLKVGETI 245
Cdd:PRK07400  175 RNRLVLShRRALVERK--------MNRLEVGEVVVGTVRGIKPYGAFIDIGGVSGLLHISEISHEHIETPHSVFNVNDEM 246
                         250       260
                  ....*....|....*....|....*
gi 2258881609 246 KVKVIKYNKENHRISLGIKQLSDDP 270
Cdd:PRK07400  247 KVMIIDLDAERGRISLSTKQLEPEP 271
S1_RPS1_repeat_ec4 cd05689
S1_RPS1_repeat_ec4: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
281-349 1.67e-24

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: 96.88  E-value: 1.67e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2258881609 281 GSTLKGKVTNVTDYGAFVEIGGGVEGLIHVSEISWTRKNVQPSNVLSVGDEINVRVLEIEPVKRRIALG 349
Cdd:cd05689     4 GTRLFGKVTNLTDYGCFVELEEGVEGLVHVSEMDWTNKNIHPSKVVSLGDEVEVMVLDIDEERRRISLG 72
S1_RPS1_repeat_ec6 cd05691
S1_RPS1_repeat_ec6: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
455-527 7.96e-23

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: 91.95  E-value: 7.96e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2258881609 455 GQVVTCEVSAVQSDGIMVTFGEGMSSFIKRAELSSDRNERRPDRFAVGEKVDAKITTIDPSSRRVSVSIRARE 527
Cdd:cd05691     1 GSIVTGKVTEVDAKGATVKLGDGVEGFLRAAELSRDRVEDATERFKVGDEVEAKITNVDRKNRKISLSIKAKE 73
S1_RPS1_repeat_ec3 cd05688
S1_RPS1_repeat_ec3: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
281-349 2.23e-21

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: 87.68  E-value: 2.23e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2258881609 281 GSTLKGKVTNVTDYGAFVEIGGgVEGLIHVSEISWTRKNvQPSNVLSVGDEINVRVLEIEPVKRRIALG 349
Cdd:cd05688     2 GDVVEGTVKSITDFGAFVDLGG-VDGLLHISDMSWGRVK-HPSEVVNVGDEVEVKVLKIDKERKRISLG 68
S1_RPS1_repeat_ec2_hs2 cd04465
S1_RPS1_repeat_ec2_hs2: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
112-175 3.27e-21

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: 87.13  E-value: 3.27e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2258881609 112 VTGVIFSRVKGGFTVDLGGAIAFLPGSQVDVRPVKDVDALMGVAQPFVILKMDRPRGNIVVSRR 175
Cdd:cd04465     4 VEGKVTEKVKGGLIVDIEGVRAFLPASQVDLRPVEDLDEYVGKELKFKIIEIDRERNNIVLSRR 67
S1_RPS1_repeat_ec5 cd05690
S1_RPS1_repeat_ec5: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
368-436 9.45e-20

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: 83.31  E-value: 9.45e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2258881609 368 GSEAKGEIRNITEFGLFVSLTDDIDGMVHMNDLSWEKNADEAIKEYKKGQVVQVKILEVDSQKERVALG 436
Cdd:cd05690     1 GTVVSGKIKSITDFGIFVGLDGGIDGLVHISDISWTQRVRHPSEIYKKGQEVEAVVLNIDVERERISLG 69
YabR COG1098
Predicted RNA-binding protein, contains ribosomal protein S1 (RPS1) domain [General function ...
277-415 1.62e-19

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


Pssm-ID: 440715 [Multi-domain]  Cd Length: 130  Bit Score: 84.85  E-value: 1.62e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 277 KFALGSTLKGKVTNVTDYGAFVEIGGGVEGLIHVSEISWTR-KNVqpSNVLSVGDEINVRVLEIEPvKRRIALGYKQCLE 355
Cdd:COG1098     2 SIEVGDIVEGKVTGITPFGAFVELPEGTTGLVHISEIADGYvKDI--NDYLKVGDEVKVKVLSIDE-DGKISLSIKQAEE 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 356 NPwEQLARVYPSGSEAKGeirnitefglFVSLTDdidgmvHMNdlSWEKNADEAIKEYKK 415
Cdd:COG1098    79 KP-KRPPRPRRNSRPKAG----------FESFED------KLS--KFLKDSDERLSDLKK 119
S1 smart00316
Ribosomal protein S1-like RNA-binding domain;
281-351 1.93e-19

Ribosomal protein S1-like RNA-binding domain;


Pssm-ID: 197648 [Multi-domain]  Cd Length: 72  Bit Score: 82.65  E-value: 1.93e-19
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2258881609  281 GSTLKGKVTNVTDYGAFVEIGGGVEGLIHVSEISWtRKNVQPSNVLSVGDEINVRVLEIEPVKRRIALGYK 351
Cdd:smart00316   3 GDVVEGTVTEITPGGAFVDLGNGVEGLIPISELSD-KRVKDPEEVLKVGDEVKVKVLSVDEEKGRIILSLK 72
S1 smart00316
Ribosomal protein S1-like RNA-binding domain;
194-264 1.33e-18

Ribosomal protein S1-like RNA-binding domain;


Pssm-ID: 197648 [Multi-domain]  Cd Length: 72  Bit Score: 79.96  E-value: 1.33e-18
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2258881609  194 EEGAVLDGMIKNVTDYGAFIDLG-GVDGLLHVTDISWQRVNHPSQVLKVGETIKVKVIKYNKENHRISLGIK 264
Cdd:smart00316   1 EVGDVVEGTVTEITPGGAFVDLGnGVEGLIPISELSDKRVKDPEEVLKVGDEVKVKVLSVDEEKGRIILSLK 72
Pnp COG1185
Polyribonucleotide nucleotidyltransferase (polynucleotide phosphorylase) [Translation, ...
272-351 2.12e-18

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


Pssm-ID: 440798 [Multi-domain]  Cd Length: 686  Bit Score: 88.91  E-value: 2.12e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 272 KDVEtkfaLGSTLKGKVTNVTDYGAFVEIGGGVEGLIHVSEISWTR-KNVqpSNVLSVGDEINVRVLEIEPvKRRIALGY 350
Cdd:COG1185   612 AEPE----VGEIYEGKVVRIMDFGAFVEILPGKDGLVHISELADERvEKV--EDVLKEGDEVKVKVLEIDD-QGRIKLSR 684

                  .
gi 2258881609 351 K 351
Cdd:COG1185   685 K 685
S1_RPS1_repeat_ec5 cd05690
S1_RPS1_repeat_ec5: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
196-262 2.29e-18

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: 79.46  E-value: 2.29e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2258881609 196 GAVLDGMIKNVTDYGAFIDL-GGVDGLLHVTDISW-QRVNHPSQVLKVGETIKVKVIKYNKENHRISLG 262
Cdd:cd05690     1 GTVVSGKIKSITDFGIFVGLdGGIDGLVHISDISWtQRVRHPSEIYKKGQEVEAVVLNIDVERERISLG 69
PRK11824 PRK11824
polynucleotide phosphorylase/polyadenylase; Provisional
281-354 3.61e-18

polynucleotide phosphorylase/polyadenylase; Provisional


Pssm-ID: 236995 [Multi-domain]  Cd Length: 693  Bit Score: 88.18  E-value: 3.61e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2258881609 281 GSTLKGKVTNVTDYGAFVEIGGGVEGLIHVSEISWTR-KNVqpSNVLSVGDEINVRVLEIEPvKRRIALGYKQCL 354
Cdd:PRK11824  622 GEIYEGKVVRIVDFGAFVEILPGKDGLVHISEIADERvEKV--EDVLKEGDEVKVKVLEIDK-RGRIRLSRKAVL 693
Pnp COG1185
Polyribonucleotide nucleotidyltransferase (polynucleotide phosphorylase) [Translation, ...
187-264 9.17e-18

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


Pssm-ID: 440798 [Multi-domain]  Cd Length: 686  Bit Score: 86.98  E-value: 9.17e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2258881609 187 EELVGRLEEGAVLDGMIKNVTDYGAFID-LGGVDGLLHVTDISWQRVNHPSQVLKVGETIKVKVIKYNKENhRISLGIK 264
Cdd:COG1185   608 EGITAEPEVGEIYEGKVVRIMDFGAFVEiLPGKDGLVHISELADERVEKVEDVLKEGDEVKVKVLEIDDQG-RIKLSRK 685
PRK11824 PRK11824
polynucleotide phosphorylase/polyadenylase; Provisional
187-266 1.57e-17

polynucleotide phosphorylase/polyadenylase; Provisional


Pssm-ID: 236995 [Multi-domain]  Cd Length: 693  Bit Score: 86.26  E-value: 1.57e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 187 EELVGRLEEGAVLDGMIKNVTDYGAFID-LGGVDGLLHVTDISWQRVNHPSQVLKVGETIKVKVIKYNKENhRISLGIKQ 265
Cdd:PRK11824  613 EGITAEPEVGEIYEGKVVRIVDFGAFVEiLPGKDGLVHISEIADERVEKVEDVLKEGDEVKVKVLEIDKRG-RIRLSRKA 691

                  .
gi 2258881609 266 L 266
Cdd:PRK11824  692 V 692
S1_Tex cd05685
S1_Tex: The C-terminal S1 domain of a transcription accessory factor called Tex, which has ...
281-348 2.18e-17

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: 76.50  E-value: 2.18e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2258881609 281 GSTLKGKVTNVTDYGAFVEIGGGVEGLIHVSEISwTRKNVQPSNVLSVGDEINVRVLEIEPVKRRIAL 348
Cdd:cd05685     1 GMVLEGVVTNVTDFGAFVDIGVKQDGLIHISKMA-DRFVSHPSDVVSVGDIVEVKVISIDEERGRISL 67
S1_RPS1_repeat_hs4 cd05692
S1_RPS1_repeat_hs4: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
196-264 5.50e-17

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: 75.40  E-value: 5.50e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 196 GAVLDGMIKNVTDYGAFIDLG-GVDGLLHVTDISWQRVNHPSQVLKVGETIKVKVIKYnKENHRISLGIK 264
Cdd:cd05692     1 GSVVEGTVTRLKPFGAFVELGgGISGLVHISQIAHKRVKDVKDVLKEGDKVKVKVLSI-DARGRISLSIK 69
S1_RPS1_repeat_ec5 cd05690
S1_RPS1_repeat_ec5: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
281-349 8.71e-17

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: 74.84  E-value: 8.71e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2258881609 281 GSTLKGKVTNVTDYGAFVEIGGGVEGLIHVSEISWTRKNVQPSNVLSVGDEINVRVLEIEPVKRRIALG 349
Cdd:cd05690     1 GTVVSGKIKSITDFGIFVGLDGGIDGLVHISDISWTQRVRHPSEIYKKGQEVEAVVLNIDVERERISLG 69
S1_like cd00164
S1_like: Ribosomal protein S1-like RNA-binding domain. Found in a wide variety of ...
284-349 2.12e-16

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: 73.57  E-value: 2.12e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2258881609 284 LKGKVTNVTDYGAFVEIGGGVEGLIHVSEISWTRKnVQPSNVLSVGDEINVRVLEIEPVKRRIALG 349
Cdd:cd00164     1 VTGKVVSITKFGVFVELEDGVEGLVHISELSDKFV-KDPSEVFKVGDEVEVKVLEVDPEKGRISLS 65
S1_Tex cd05685
S1_Tex: The C-terminal S1 domain of a transcription accessory factor called Tex, which has ...
196-261 2.40e-16

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: 73.42  E-value: 2.40e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2258881609 196 GAVLDGMIKNVTDYGAFIDLG-GVDGLLHVTDISWQRVNHPSQVLKVGETIKVKVIKYNKENHRISL 261
Cdd:cd05685     1 GMVLEGVVTNVTDFGAFVDIGvKQDGLIHISKMADRFVSHPSDVVSVGDIVEVKVISIDEERGRISL 67
Tex COG2183
Transcriptional accessory protein Tex/SPT6 [Transcription];
193-270 4.72e-16

Transcriptional accessory protein Tex/SPT6 [Transcription];


Pssm-ID: 441786 [Multi-domain]  Cd Length: 719  Bit Score: 81.61  E-value: 4.72e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 193 LEEGAVLDGMIKNVTDYGAFIDLGgV--DGLLHVTDISWQRVNHPSQVLKVGETIKVKVIKYNKENHRISLGIKQLSDDP 270
Cdd:COG2183   639 LKPGMILEGTVTNVTDFGAFVDIG-VhqDGLVHISQLSDRFVKDPREVVKVGDIVKVKVLEVDLKRKRISLSMKLDDEAG 717
S1 pfam00575
S1 RNA binding domain; The S1 domain occurs in a wide range of RNA associated proteins. It is ...
278-350 4.80e-16

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: 72.71  E-value: 4.80e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2258881609 278 FALGSTLKGKVTNVTDYGAFVEIGGGVEGLIHVSEISWtRKNVQPSNVLSVGDEINVRVLEIEPVKRRIALGY 350
Cdd:pfam00575   1 PEKGDVVEGEVTRVTKGGAFVDLGNGVEGFIPISELSD-DHVEDPDEVIKVGDEVKVKVLKVDKDRRRIILSI 72
S1_RPS1_repeat_hs4 cd05692
S1_RPS1_repeat_hs4: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
281-351 5.94e-16

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: 72.32  E-value: 5.94e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2258881609 281 GSTLKGKVTNVTDYGAFVEIGGGVEGLIHVSEISWTRKNvQPSNVLSVGDEINVRVLEIEPvKRRIALGYK 351
Cdd:cd05692     1 GSVVEGTVTRLKPFGAFVELGGGISGLVHISQIAHKRVK-DVKDVLKEGDKVKVKVLSIDA-RGRISLSIK 69
Tex COG2183
Transcriptional accessory protein Tex/SPT6 [Transcription];
281-348 1.05e-15

Transcriptional accessory protein Tex/SPT6 [Transcription];


Pssm-ID: 441786 [Multi-domain]  Cd Length: 719  Bit Score: 80.45  E-value: 1.05e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2258881609 281 GSTLKGKVTNVTDYGAFVEIGGGVEGLIHVSEISwtRKNVQ-PSNVLSVGDEINVRVLEIEPVKRRIAL 348
Cdd:COG2183   642 GMILEGTVTNVTDFGAFVDIGVHQDGLVHISQLS--DRFVKdPREVVKVGDIVKVKVLEVDLKRKRISL 708
PRK08059 PRK08059
general stress protein 13; Validated
276-360 1.70e-15

general stress protein 13; Validated


Pssm-ID: 181215 [Multi-domain]  Cd Length: 123  Bit Score: 73.16  E-value: 1.70e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 276 TKFALGSTLKGKVTNVTDYGAFVEIGGGVEGLIHVSEISWTR-KNVQpsNVLSVGDEINVRVLEIEPVKRRIALGYKQCL 354
Cdd:PRK08059    3 SQYEVGSVVTGKVTGIQPYGAFVALDEETQGLVHISEITHGFvKDIH--DFLSVGDEVKVKVLSVDEEKGKISLSIRATE 80

                  ....*.
gi 2258881609 355 ENPWEQ 360
Cdd:PRK08059   81 EAPEAK 86
YabR COG1098
Predicted RNA-binding protein, contains ribosomal protein S1 (RPS1) domain [General function ...
193-270 4.10e-15

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


Pssm-ID: 440715 [Multi-domain]  Cd Length: 130  Bit Score: 72.13  E-value: 4.10e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2258881609 193 LEEGAVLDGMIKNVTDYGAFIDL-GGVDGLLHVTDISWQRVNHPSQVLKVGETIKVKVIKYnKENHRISLGIKQLSDDP 270
Cdd:COG1098     3 IEVGDIVEGKVTGITPFGAFVELpEGTTGLVHISEIADGYVKDINDYLKVGDEVKVKVLSI-DEDGKISLSIKQAEEKP 80
S1_dom_CvfD NF040579
CvfD/Ygs/GSP13 family RNA-binding post-transcriptional regulator; CvfD, Ygs, and GSP13 form a ...
281-348 6.44e-15

CvfD/Ygs/GSP13 family RNA-binding post-transcriptional regulator; CvfD, Ygs, and GSP13 form a family of full-length homologs of RNA-binding proteins from the Firmicutes with a single copy of the S1 domain. Several members of the family have been characterized as general stress proteins, and the most recently characterized, CvfD, was shown to act as a post-transcriptional regulator.


Pssm-ID: 468553 [Multi-domain]  Cd Length: 113  Bit Score: 70.92  E-value: 6.44e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 281 GSTLKGKVTNVTDYGAFVEIGGGVEGLIHVSEISwTR--KNVqpSNVLSVGDEINVRVLEIEPVKRRIAL 348
Cdd:NF040579    4 GDIVEGKVTGIQPYGAFVALDEHTQGLIHISEIK-HGyvKDI--NDFLKVGQEVKVKVLDIDEYTGKISL 70
S1 pfam00575
S1 RNA binding domain; The S1 domain occurs in a wide range of RNA associated proteins. It is ...
193-263 1.54e-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: 68.47  E-value: 1.54e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2258881609 193 LEEGAVLDGMIKNVTDYGAFIDLG-GVDGLLHVTDISWQRVNHPSQVLKVGETIKVKVIKYNKENHRISLGI 263
Cdd:pfam00575   1 PEKGDVVEGEVTRVTKGGAFVDLGnGVEGFIPISELSDDHVEDPDEVIKVGDEVKVKVLKVDKDRRRIILSI 72
PRK08582 PRK08582
RNA-binding protein S1;
281-380 1.56e-14

RNA-binding protein S1;


Pssm-ID: 236305 [Multi-domain]  Cd Length: 139  Bit Score: 70.83  E-value: 1.56e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 281 GSTLKGKVTNVTDYGAFVEIGGGVEGLIHVSEISWTR-KNVQpsNVLSVGDEINVRVLEIEPvKRRIALGYKQCLENPWE 359
Cdd:PRK08582    6 GSKLQGKVTGITNFGAFVELPEGKTGLVHISEVADNYvKDIN--DHLKVGDEVEVKVLNVED-DGKIGLSIKKAKDRPKR 82
                          90       100
                  ....*....|....*....|.
gi 2258881609 360 QLARVYPSGSEAKGEIRNITE 380
Cdd:PRK08582   83 QHDRPRHEDNRGGGNDVAPKE 103
S1_Rrp5_repeat_sc12 cd05708
S1_Rrp5_repeat_sc12: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ...
194-264 1.70e-14

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: 68.51  E-value: 1.70e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2258881609 194 EEGAVLDGMIKNVTDYGAFIDLGGVD--GLLHVTDISWQRVNHPSQVLKVGETIKVKVIKYNKENHRISLGIK 264
Cdd:cd05708     1 KVGQKIDGTVRRVEDYGVFIDIDGTNvsGLCHKSEISDNRVADASKLFRVGDKVRAKVLKIDAEKKRISLGLK 73
S1_DHX8_helicase cd05684
S1_DHX8_helicase: The N-terminal S1 domain of human ATP-dependent RNA helicase DHX8, a DEAH ...
196-264 2.19e-14

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: 68.42  E-value: 2.19e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2258881609 196 GAVLDGMIKNVTDYGAFIDL----GGVDGLLHVTDISWQR-VNHPSQVLKVGETIKVKVIKYnkENHRISLGIK 264
Cdd:cd05684     1 GKIYKGKVTSIMDFGCFVQLeglkGRKEGLVHISQLSFEGrVANPSDVVKRGQKVKVKVISI--QNGKISLSMK 72
S1_PNPase cd04472
S1_PNPase: Polynucleotide phosphorylase (PNPase), ), S1-like RNA-binding domain. PNPase is a ...
281-340 2.95e-14

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: 67.57  E-value: 2.95e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 281 GSTLKGKVTNVTDYGAFVEIGGGVEGLIHVSEISWTRKNvQPSNVLSVGDEINVRVLEIE 340
Cdd:cd04472     1 GKIYEGKVVKIKDFGAFVEILPGKDGLVHISELSDERVE-KVEDVLKVGDEVKVKVIEVD 59
S1_DHX8_helicase cd05684
S1_DHX8_helicase: The N-terminal S1 domain of human ATP-dependent RNA helicase DHX8, a DEAH ...
281-340 5.27e-14

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: 67.26  E-value: 5.27e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2258881609 281 GSTLKGKVTNVTDYGAFVEI---GGGVEGLIHVSEISWTRKNVQPSNVLSVGDEINVRVLEIE 340
Cdd:cd05684     1 GKIYKGKVTSIMDFGCFVQLeglKGRKEGLVHISQLSFEGRVANPSDVVKRGQKVKVKVISIQ 63
S1_RPS1_repeat_ec4 cd05689
S1_RPS1_repeat_ec4: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
195-262 3.84e-13

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: 64.52  E-value: 3.84e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 195 EGAVLDGMIKNVTDYGAFIDLG-GVDGLLHVTDISWQRVN-HPSQVLKVGETIKVKVIKYNKENHRISLG 262
Cdd:cd05689     3 EGTRLFGKVTNLTDYGCFVELEeGVEGLVHVSEMDWTNKNiHPSKVVSLGDEVEVMVLDIDEERRRISLG 72
S1_RPS1_repeat_ec1_hs1 cd05687
S1_RPS1_repeat_ec1_hs1: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
25-91 7.41e-13

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: 63.70  E-value: 7.41e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609  25 GKVLKGRIVRQDREAVTIDVGLKSEGRVPLREFATGGNV---PELKVGDLVDVYVERMEGATGDIVLSHE 91
Cdd:cd05687     1 GDIVKGTVVSVDDDEVLVDIGYKSEGIIPISEFSDDPIEngeDEVKVGDEVEVYVLRVEDEEGNVVLSKR 70
S1_Rrp5_repeat_sc12 cd05708
S1_Rrp5_repeat_sc12: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ...
281-351 1.14e-12

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: 63.50  E-value: 1.14e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2258881609 281 GSTLKGKVTNVTDYGAFVEIGG-GVEGLIHVSEISWTRKNvQPSNVLSVGDEINVRVLEIEPVKRRIALGYK 351
Cdd:cd05708     3 GQKIDGTVRRVEDYGVFIDIDGtNVSGLCHKSEISDNRVA-DASKLFRVGDKVRAKVLKIDAEKKRISLGLK 73
S1_like cd00164
S1_like: Ribosomal protein S1-like RNA-binding domain. Found in a wide variety of ...
199-262 1.80e-12

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: 62.40  E-value: 1.80e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2258881609 199 LDGMIKNVTDYGAFIDLG-GVDGLLHVTDISWQRVNHPSQVLKVGETIKVKVIKYNKENHRISLG 262
Cdd:cd00164     1 VTGKVVSITKFGVFVELEdGVEGLVHISELSDKFVKDPSEVFKVGDEVEVKVLEVDPEKGRISLS 65
S1 smart00316
Ribosomal protein S1-like RNA-binding domain;
368-438 2.86e-12

Ribosomal protein S1-like RNA-binding domain;


Pssm-ID: 197648 [Multi-domain]  Cd Length: 72  Bit Score: 62.24  E-value: 2.86e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2258881609  368 GSEAKGEIRNITEFGLFVSLTDDIDGMVHMNDLSWEKNADEAIKeYKKGQVVQVKILEVDSQKERVALGIK 438
Cdd:smart00316   3 GDVVEGTVTEITPGGAFVDLGNGVEGLIPISELSDKRVKDPEEV-LKVGDEVKVKVLSVDEEKGRIILSLK 72
PRK05807 PRK05807
RNA-binding protein S1;
193-265 3.78e-12

RNA-binding protein S1;


Pssm-ID: 235614 [Multi-domain]  Cd Length: 136  Bit Score: 64.00  E-value: 3.78e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2258881609 193 LEEGAVLDGMIKNVTDYGAFIDLGGVDGLLHVTDISWQRVNHPSQVLKVGETIKVKVIKYNkENHRISLGIKQ 265
Cdd:PRK05807    3 LKAGSILEGTVVNITNFGAFVEVEGKTGLVHISEVADTYVKDIREHLKEQDKVKVKVISID-DNGKISLSIKQ 74
S1 smart00316
Ribosomal protein S1-like RNA-binding domain;
453-524 5.18e-12

Ribosomal protein S1-like RNA-binding domain;


Pssm-ID: 197648 [Multi-domain]  Cd Length: 72  Bit Score: 61.47  E-value: 5.18e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2258881609  453 RKGQVVTCEVSAVQSDGIMVTFGEGMSSFIKRAELSSDRNERRPDRFAVGEKVDAKITTIDPSSRRVSVSIR 524
Cdd:smart00316   1 EVGDVVEGTVTEITPGGAFVDLGNGVEGLIPISELSDKRVKDPEEVLKVGDEVKVKVLSVDEEKGRIILSLK 72
S1_PNPase cd04472
S1_PNPase: Polynucleotide phosphorylase (PNPase), ), S1-like RNA-binding domain. PNPase is a ...
196-261 5.52e-12

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: 61.02  E-value: 5.52e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2258881609 196 GAVLDGMIKNVTDYGAFID-LGGVDGLLHVTDISWQRVNHPSQVLKVGETIKVKVIKYNKENhRISL 261
Cdd:cd04472     1 GKIYEGKVVKIKDFGAFVEiLPGKDGLVHISELSDERVEKVEDVLKVGDEVKVKVIEVDDRG-RISL 66
S1_RPS1_repeat_ec3 cd05688
S1_RPS1_repeat_ec3: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
368-436 1.52e-11

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: 59.95  E-value: 1.52e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2258881609 368 GSEAKGEIRNITEFGLFVSLtDDIDGMVHMNDLSWE--KNADEAIKEykkGQVVQVKILEVDSQKERVALG 436
Cdd:cd05688     2 GDVVEGTVKSITDFGAFVDL-GGVDGLLHISDMSWGrvKHPSEVVNV---GDEVEVKVLKIDKERKRISLG 68
S1_RPS1_repeat_ec4 cd05689
S1_RPS1_repeat_ec4: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
365-436 2.79e-11

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: 59.51  E-value: 2.79e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2258881609 365 YPSGSEAKGEIRNITEFGLFVSLTDDIDGMVHMNDLSWEKNADEAIKEYKKGQVVQVKILEVDSQKERVALG 436
Cdd:cd05689     1 YPEGTRLFGKVTNLTDYGCFVELEEGVEGLVHVSEMDWTNKNIHPSKVVSLGDEVEVMVLDIDEERRRISLG 72
S1_Rrp5_repeat_sc12 cd05708
S1_Rrp5_repeat_sc12: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ...
368-438 5.54e-11

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: 58.49  E-value: 5.54e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2258881609 368 GSEAKGEIRNITEFGLFVSL-TDDIDGMVHMNDLSwEKNADEAIKEYKKGQVVQVKILEVDSQKERVALGIK 438
Cdd:cd05708     3 GQKIDGTVRRVEDYGVFIDIdGTNVSGLCHKSEIS-DNRVADASKLFRVGDKVRAKVLKIDAEKKRISLGLK 73
S1_RPS1_repeat_ec6 cd05691
S1_RPS1_repeat_ec6: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
196-266 1.51e-10

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: 57.28  E-value: 1.51e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2258881609 196 GAVLDGMIKNVTDYGAFIDLG-GVDGLLHVTDISWQRVNHPSQVLKVGETIKVKVIKYNKENHRISLGIKQL 266
Cdd:cd05691     1 GSIVTGKVTEVDAKGATVKLGdGVEGFLRAAELSRDRVEDATERFKVGDEVEAKITNVDRKNRKISLSIKAK 72
S1 pfam00575
S1 RNA binding domain; The S1 domain occurs in a wide range of RNA associated proteins. It is ...
368-437 1.73e-10

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: 56.91  E-value: 1.73e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 368 GSEAKGEIRNITEFGLFVSLTDDIDGMVHMNDLSWEKNADEAiKEYKKGQVVQVKILEVDSQKERVALGI 437
Cdd:pfam00575   4 GDVVEGEVTRVTKGGAFVDLGNGVEGFIPISELSDDHVEDPD-EVIKVGDEVKVKVLKVDKDRRRIILSI 72
S1_RPS1_repeat_ec6 cd05691
S1_RPS1_repeat_ec6: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
281-352 3.36e-10

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: 56.12  E-value: 3.36e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2258881609 281 GSTLKGKVTNVTDYGAFVEIGGGVEGLIHVSEISWTRKNVQPSNvLSVGDEINVRVLEIEPVKRRIALGYKQ 352
Cdd:cd05691     1 GSIVTGKVTEVDAKGATVKLGDGVEGFLRAAELSRDRVEDATER-FKVGDEVEAKITNVDRKNRKISLSIKA 71
PRK08059 PRK08059
general stress protein 13; Validated
191-270 5.59e-10

general stress protein 13; Validated


Pssm-ID: 181215 [Multi-domain]  Cd Length: 123  Bit Score: 57.36  E-value: 5.59e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 191 GRLEEGAVLDGMIKNVTDYGAFIDL-GGVDGLLHVTDISWQRVNHPSQVLKVGETIKVKVIKYNKENHRISLGIKQLSDD 269
Cdd:PRK08059    3 SQYEVGSVVTGKVTGIQPYGAFVALdEETQGLVHISEITHGFVKDIHDFLSVGDEVKVKVLSVDEEKGKISLSIRATEEA 82

                  .
gi 2258881609 270 P 270
Cdd:PRK08059   83 P 83
S1_like cd00164
S1_like: Ribosomal protein S1-like RNA-binding domain. Found in a wide variety of ...
372-436 8.82e-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: 8.82e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2258881609 372 KGEIRNITEFGLFVSLTDDIDGMVHMNDLSWEKNADEAiKEYKKGQVVQVKILEVDSQKERVALG 436
Cdd:cd00164     2 TGKVVSITKFGVFVELEDGVEGLVHISELSDKFVKDPS-EVFKVGDEVEVKVLEVDPEKGRISLS 65
PRK05807 PRK05807
RNA-binding protein S1;
278-356 2.62e-09

RNA-binding protein S1;


Pssm-ID: 235614 [Multi-domain]  Cd Length: 136  Bit Score: 55.52  E-value: 2.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 278 FALGSTLKGKVTNVTDYGAFVEIGGGVeGLIHVSEISWTR-KNVQpsNVLSVGDEINVRVLEIEPvKRRIALGYKQCLEN 356
Cdd:PRK05807    3 LKAGSILEGTVVNITNFGAFVEVEGKT-GLVHISEVADTYvKDIR--EHLKEQDKVKVKVISIDD-NGKISLSIKQAMKQ 78
PRK11824 PRK11824
polynucleotide phosphorylase/polyadenylase; Provisional
359-440 3.17e-09

polynucleotide phosphorylase/polyadenylase; Provisional


Pssm-ID: 236995 [Multi-domain]  Cd Length: 693  Bit Score: 59.68  E-value: 3.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 359 EQLARVYPSGSEAKGEIRNITEFGLFVSLTDDIDGMVHMNDLSWE--KNADEAIKEykkGQVVQVKILEVDSQKeRVALG 436
Cdd:PRK11824  613 EGITAEPEVGEIYEGKVVRIVDFGAFVEILPGKDGLVHISEIADErvEKVEDVLKE---GDEVKVKVLEIDKRG-RIRLS 688

                  ....
gi 2258881609 437 IKQL 440
Cdd:PRK11824  689 RKAV 692
S1_pNO40 cd05686
S1_pNO40: pNO40 , S1-like RNA-binding domain. pNO40 is a nucleolar protein of unknown function ...
279-351 3.18e-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: 53.64  E-value: 3.18e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2258881609 279 ALGSTLKGKVTNVTDYGAFVEIGG-GVEGLIHVSEISWTRKNvQPSNVLSVGDEINVRVLEIEpVKRRIALGYK 351
Cdd:cd05686     2 ALYQIFKGEVASVTEYGAFVKIPGcRKQGLVHKSHMSSCRVD-DPSEVVDVGEKVWVKVIGRE-MKDKMKLSLS 73
PRK08059 PRK08059
general stress protein 13; Validated
365-459 6.00e-09

general stress protein 13; Validated


Pssm-ID: 181215 [Multi-domain]  Cd Length: 123  Bit Score: 54.28  E-value: 6.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 365 YPSGSEAKGEIRNITEFGLFVSLTDDIDGMVHMNDLSWEKNADeaIKEY-KKGQVVQVKILEVDSQKERVALGIKQLQSD 443
Cdd:PRK08059    5 YEVGSVVTGKVTGIQPYGAFVALDEETQGLVHISEITHGFVKD--IHDFlSVGDEVKVKVLSVDEEKGKISLSIRATEEA 82
                          90
                  ....*....|....*.
gi 2258881609 444 PFAGAvadlRKGQVVT 459
Cdd:PRK08059   83 PEAKR----KKGKILI 94
S1 pfam00575
S1 RNA binding domain; The S1 domain occurs in a wide range of RNA associated proteins. It is ...
452-523 7.46e-09

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: 52.29  E-value: 7.46e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2258881609 452 LRKGQVVTCEVSAVQSDGIMVTFGEGMSSFIKRAELSSDRNERRPDRFAVGEKVDAKITTIDPSSRRVSVSI 523
Cdd:pfam00575   1 PEKGDVVEGEVTRVTKGGAFVDLGNGVEGFIPISELSDDHVEDPDEVIKVGDEVKVKVLKVDKDRRRIILSI 72
S1_pNO40 cd05686
S1_pNO40: pNO40 , S1-like RNA-binding domain. pNO40 is a nucleolar protein of unknown function ...
197-250 8.63e-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: 8.63e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2258881609 197 AVLDGMIKNVTDYGAFIDLGGV--DGLLHVTDISWQRVNHPSQVLKVGETIKVKVI 250
Cdd:cd05686     5 QIFKGEVASVTEYGAFVKIPGCrkQGLVHKSHMSSCRVDDPSEVVDVGEKVWVKVI 60
PRK07252 PRK07252
S1 RNA-binding domain-containing protein;
280-340 9.84e-09

S1 RNA-binding domain-containing protein;


Pssm-ID: 180908 [Multi-domain]  Cd Length: 120  Bit Score: 53.55  E-value: 9.84e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2258881609 280 LGSTLKGKVTNVTDYGAFVEIGGGVEGLIHVSEI-SWTRKNVQpsNVLSVGDEINVRVLEIE 340
Cdd:PRK07252    3 IGDKLKGTITGIKPYGAFVALENGTTGLIHISEIkTGFIDNIH--QLLKVGEEVLVQVVDFD 62
S1_RecJ_like cd04473
S1_RecJ_like: The S1 domain of the archaea-specific RecJ-like exonuclease. The function of ...
281-350 1.33e-08

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: 51.84  E-value: 1.33e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 281 GSTLKGKVTNVTDYGAFVEIGGGVEGLIHvseiswtRKNVQPSnvLSVGDEINVRVLEIePVKRRIALGY 350
Cdd:cd04473    17 GKLYKGKVNGVAKYGVFVDLNDHVRGLIH-------RSNLLRD--YEVGDEVIVQVTDI-PENGNIDLIP 76
S1_RPS1_repeat_ec1_hs1 cd05687
S1_RPS1_repeat_ec1_hs1: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
281-340 1.64e-08

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: 51.38  E-value: 1.64e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 281 GSTLKGKVTNVTDYGAFVEIGGGVEGLIHVSEISWTRkNVQPSNVLSVGDEINVRVLEIE 340
Cdd:cd05687     1 GDIVKGTVVSVDDDEVLVDIGYKSEGIIPISEFSDDP-IENGEDEVKVGDEVEVYVLRVE 59
S1_Rrp5_repeat_hs6_sc5 cd05698
S1_Rrp5_repeat_hs6_sc5: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ...
286-351 2.04e-08

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: 51.07  E-value: 2.04e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2258881609 286 GKVTNVTDYGAFVEIGGGVEGLIHVSEISWTRKNvQPSNVLSVGDEINVRVLEIEPVKRRIALGYK 351
Cdd:cd05698     6 GTIVKVKPNGCIVSFYNNVKGFLPKSELSEAFIK-DPEEHFRVGQVVKVKVLSCDPEQQRLLLSCK 70
PRK08582 PRK08582
RNA-binding protein S1;
193-270 2.12e-08

RNA-binding protein S1;


Pssm-ID: 236305 [Multi-domain]  Cd Length: 139  Bit Score: 53.11  E-value: 2.12e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2258881609 193 LEEGAVLDGMIKNVTDYGAFIDL-GGVDGLLHVTDISWQRVNHPSQVLKVGETIKVKVIKYNKENhRISLGIKQLSDDP 270
Cdd:PRK08582    3 IEVGSKLQGKVTGITNFGAFVELpEGKTGLVHISEVADNYVKDINDHLKVGDEVEVKVLNVEDDG-KIGLSIKKAKDRP 80
S1_IF2_alpha cd04452
S1_IF2_alpha: The alpha subunit of translation Initiation Factor 2, S1-like RNA-binding domain. ...
194-265 2.93e-08

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: 50.66  E-value: 2.93e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2258881609 194 EEGAVLDGMIKNVTDYGAFIDL---GGVDGLLHVTDISWQRVNHPSQVLKVGETIKVKVIKYNKENHRISLGIKQ 265
Cdd:cd04452     2 EEGELVVVTVKSIADMGAYVSLleyGNIEGMILLSELSRRRIRSIRKLVKVGRKEVVKVIRVDKEKGYIDLSKKR 76
S1_Rrp5_repeat_hs8_sc7 cd04461
S1_Rrp5_repeat_hs8_sc7: Rrp5 Homo sapiens S1 repeat 8 (hs8) and Saccharomyces cerevisiae S1 ...
193-261 3.86e-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: 3.86e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 193 LEEGAVLDGMIKNVTDYGAFID-LGGVDGLLHVTDISWQRVNHPSQVLKVGETIKVKVIKYNKENHRISL 261
Cdd:cd04461    12 LKPGMVVHGYVRNITPYGVFVEfLGGLTGLAPKSYISDEFVTDPSFGFKKGQSVTAKVTSVDEEKQRFLL 81
S1_RNase_R cd04471
S1_RNase_R: RNase R C-terminal S1 domain. RNase R is a processive 3' to 5' exoribonuclease, ...
280-346 3.94e-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: 50.86  E-value: 3.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 280 LGSTLKGKVTNVTDYGAFVEIGG-GVEGLIHVSEIS--------------WTRKNvqpsNVLSVGDEINVRVLEIEPVKR 344
Cdd:cd04471     1 VGEEFDGVISGVTSFGLFVELDNlTVEGLVHVSTLGddyyefdeenhalvGERTG----KVFRLGDKVKVRVVRVDLDRR 76

                  ..
gi 2258881609 345 RI 346
Cdd:cd04471    77 KI 78
S1_Rrp5_repeat_hs6_sc5 cd05698
S1_Rrp5_repeat_hs6_sc5: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ...
201-264 5.49e-08

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: 49.92  E-value: 5.49e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2258881609 201 GMIKNVTDYGAFID-LGGVDGLLHVTDISWQRVNHPSQVLKVGETIKVKVIKYNKENHRISLGIK 264
Cdd:cd05698     6 GTIVKVKPNGCIVSfYNNVKGFLPKSELSEAFIKDPEEHFRVGQVVKVKVLSCDPEQQRLLLSCK 70
Tex COG2183
Transcriptional accessory protein Tex/SPT6 [Transcription];
368-439 6.07e-08

Transcriptional accessory protein Tex/SPT6 [Transcription];


Pssm-ID: 441786 [Multi-domain]  Cd Length: 719  Bit Score: 55.80  E-value: 6.07e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2258881609 368 GSEAKGEIRNITEFGLFVsltdDI----DGMVHMNDLSWE--KNADEAIKeykKGQVVQVKILEVDSQKERVALGIKQ 439
Cdd:COG2183   642 GMILEGTVTNVTDFGAFV----DIgvhqDGLVHISQLSDRfvKDPREVVK---VGDIVKVKVLEVDLKRKRISLSMKL 712
S1_Rrp5_repeat_hs5 cd05697
S1_Rrp5_repeat_hs5: Rrp5 is a trans-acting factor important for biogenesis of both the 40S and ...
281-348 7.33e-08

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: 49.54  E-value: 7.33e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2258881609 281 GSTLKGKVTNVTDYGAFVEIGGGVEGLIHVSEISWTRKnVQPSNVLSVGDEINVRVLEIEPVKRRIAL 348
Cdd:cd05697     1 GQVVKGTIRKLRPSGIFVKLSDHIKGLVPPMHLADVRL-KHPEKKFKPGLKVKCRVLSVEPERKRLVL 67
RpsA COG0539
Ribosomal protein S1 [Translation, ribosomal structure and biogenesis]; Ribosomal protein S1 ...
281-532 9.40e-08

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: 54.28  E-value: 9.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 281 GSTLKGKVTNVTDYGAFVEIGGGVEGLIHVSEISWTRKNVQpsnvLSVGDEINVRVLEIEPVKRRIALGYKQCLEnpweq 360
Cdd:COG0539    19 GDIVKGTVVSIDDDEVLVDIGYKSEGIIPLSEFSDEPGELE----VKVGDEVEVYVEKVEDGEGEIVLSKKKADR----- 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 361 larvypsgseakgeirnitefglfvsltddidgmvhmndlswEKNADEAIKEYKKGQVVQVKIlevdsqKERValgikql 440
Cdd:COG0539    90 ------------------------------------------EKAWEELEEAFENGEPVEGKV------KGVV------- 114
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 441 qsdpfagavadlrKGqvvtcevsavqsdGIMVTFGeGMSSFIKrAELSSDRNERRPDRFaVGEKVDAKITTIDPSSRRVS 520
Cdd:COG0539   115 -------------KG-------------GLIVDIG-GVRAFLP-ASQVDVRPVRDLDEY-VGKTLEFKIIKLDRKRNNVV 165
                         250
                  ....*....|....*
gi 2258881609 521 VSIRA---REQEEER 532
Cdd:COG0539   166 VSRRAvleEEREEKR 180
PRK03987 PRK03987
translation initiation factor IF-2 subunit alpha; Validated
194-269 1.18e-07

translation initiation factor IF-2 subunit alpha; Validated


Pssm-ID: 235188 [Multi-domain]  Cd Length: 262  Bit Score: 53.29  E-value: 1.18e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2258881609 194 EEGAVLDGMIKNVTDYGAFIDL---GGVDGLLHVTDISWQRVNHPSQVLKVGETIKVKVIKYNKENHRISLGIKQLSDD 269
Cdd:PRK03987    7 EEGELVVGTVKEVKDFGAFVTLdeyPGKEGFIHISEVASGWVKNIRDHVKEGQKVVCKVIRVDPRKGHIDLSLKRVNEH 85
S1_DHX8_helicase cd05684
S1_DHX8_helicase: The N-terminal S1 domain of human ATP-dependent RNA helicase DHX8, a DEAH ...
372-430 1.49e-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: 48.77  E-value: 1.49e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2258881609 372 KGEIRNITEFGLFVSLTD---DIDGMVHMNDLSWEKNADEAIKEYKKGQVVQVKILEVDSQK 430
Cdd:cd05684     5 KGKVTSIMDFGCFVQLEGlkgRKEGLVHISQLSFEGRVANPSDVVKRGQKVKVKVISIQNGK 66
S1_Rrp5_repeat_hs8_sc7 cd04461
S1_Rrp5_repeat_hs8_sc7: Rrp5 Homo sapiens S1 repeat 8 (hs8) and Saccharomyces cerevisiae S1 ...
281-348 1.65e-07

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: 49.12  E-value: 1.65e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2258881609 281 GSTLKGKVTNVTDYGAFVEIGGGVEGLIHVSEISwtRKNV-QPSNVLSVGDEINVRVLEIEPVKRRIAL 348
Cdd:cd04461    15 GMVVHGYVRNITPYGVFVEFLGGLTGLAPKSYIS--DEFVtDPSFGFKKGQSVTAKVTSVDEEKQRFLL 81
PRK07252 PRK07252
S1 RNA-binding domain-containing protein;
196-269 1.68e-07

S1 RNA-binding domain-containing protein;


Pssm-ID: 180908 [Multi-domain]  Cd Length: 120  Bit Score: 50.09  E-value: 1.68e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2258881609 196 GAVLDGMIKNVTDYGAFIDL-GGVDGLLHVTDISWQRVNHPSQVLKVGETIKVKVIKYNKENHRISLGIKQLSDD 269
Cdd:PRK07252    4 GDKLKGTITGIKPYGAFVALeNGTTGLIHISEIKTGFIDNIHQLLKVGEEVLVQVVDFDEYTGKASLSLRTLEEE 78
COG1107 COG1107
Archaea-specific RecJ-like exonuclease, contains DnaJ-type Zn finger domain [Replication, ...
281-350 4.98e-07

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: 52.53  E-value: 4.98e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2258881609 281 GSTLKGKVTNVTDYGAFVEIGGGVEGLIHVSEI--SWtrknvqpsnvlSVGDEINVRVLEIEPvKRRIALGY 350
Cdd:COG1107    40 GRYYRGTVDGVADFGVFVDLNDHVTGLLHRSELdqDW-----------EVGDEVFVQVKEVRD-NGNVDLGW 99
VacB COG0557
Exoribonuclease R [Transcription];
280-346 5.06e-07

Exoribonuclease R [Transcription];


Pssm-ID: 440323 [Multi-domain]  Cd Length: 711  Bit Score: 52.80  E-value: 5.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 280 LGSTLKGKVTNVTDYGAFVEI-GGGVEGLIHVSEI----------------SWTRKnvqpsnVLSVGDEINVRVLEIEPV 342
Cdd:COG0557   622 VGEEFEGVISGVTSFGLFVELdELGVEGLVHVSSLgddyyeyderrqalvgERTGK------RYRLGDRVEVRVVRVDLD 695

                  ....
gi 2258881609 343 KRRI 346
Cdd:COG0557   696 RRQI 699
S1_Rrp5_repeat_hs6_sc5 cd05698
S1_Rrp5_repeat_hs6_sc5: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ...
368-438 7.29e-07

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: 46.84  E-value: 7.29e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2258881609 368 GSEAKGEIRNITEFGLFVSLTDDIDGMVHMNDLSWE--KNADEAikeYKKGQVVQVKILEVDSQKERVALGIK 438
Cdd:cd05698     1 GLKTHGTIVKVKPNGCIVSFYNNVKGFLPKSELSEAfiKDPEEH---FRVGQVVKVKVLSCDPEQQRLLLSCK 70
PLN00207 PLN00207
polyribonucleotide nucleotidyltransferase; Provisional
288-339 8.25e-07

polyribonucleotide nucleotidyltransferase; Provisional


Pssm-ID: 215104 [Multi-domain]  Cd Length: 891  Bit Score: 52.20  E-value: 8.25e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2258881609 288 VTNVTDYGAFVEIGGGVEGLIHVSEIS--WTRKnvqPSNVLSVGDEINVRVLEI 339
Cdd:PLN00207  762 IKSIAPYGAFVEIAPGREGLCHISELSsnWLAK---PEDAFKVGDRIDVKLIEV 812
PRK03987 PRK03987
translation initiation factor IF-2 subunit alpha; Validated
286-351 1.30e-06

translation initiation factor IF-2 subunit alpha; Validated


Pssm-ID: 235188 [Multi-domain]  Cd Length: 262  Bit Score: 50.21  E-value: 1.30e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 286 GKVTNVTDYGAFVEIG--GGVEGLIHVSEIS--WTrKNVQpsNVLSVGDEINVRVLEIEPVKRRIALGYK 351
Cdd:PRK03987   14 GTVKEVKDFGAFVTLDeyPGKEGFIHISEVAsgWV-KNIR--DHVKEGQKVVCKVIRVDPRKGHIDLSLK 80
S1_Tex cd05685
S1_Tex: The C-terminal S1 domain of a transcription accessory factor called Tex, which has ...
368-435 1.41e-06

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: 45.69  E-value: 1.41e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2258881609 368 GSEAKGEIRNITEFGLFVSLTDDIDGMVHMNDLSwEKNADEAIKEYKKGQVVQVKILEVDSQKERVAL 435
Cdd:cd05685     1 GMVLEGVVTNVTDFGAFVDIGVKQDGLIHISKMA-DRFVSHPSDVVSVGDIVEVKVISIDEERGRISL 67
S1_IF2_alpha cd04452
S1_IF2_alpha: The alpha subunit of translation Initiation Factor 2, S1-like RNA-binding domain. ...
286-352 1.73e-06

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: 45.65  E-value: 1.73e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 286 GKVTNVTDYGAFVEIG--GGVEGLIHVSEISWTR-KNVQpsNVLSVGDEINVRVLEIEPVKRRIALGYKQ 352
Cdd:cd04452     9 VTVKSIADMGAYVSLLeyGNIEGMILLSELSRRRiRSIR--KLVKVGRKEVVKVIRVDKEKGYIDLSKKR 76
S1 smart00316
Ribosomal protein S1-like RNA-binding domain;
25-90 1.83e-06

Ribosomal protein S1-like RNA-binding domain;


Pssm-ID: 197648 [Multi-domain]  Cd Length: 72  Bit Score: 45.67  E-value: 1.83e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2258881609   25 GKVLKGRIVRQDREAVTIDVGLKSEGRVPLREFATGGNV---PELKVGDLVDVYVERMEGATGDIVLSH 90
Cdd:smart00316   3 GDVVEGTVTEITPGGAFVDLGNGVEGLIPISELSDKRVKdpeEVLKVGDEVKVKVLSVDEEKGRIILSL 71
PRK05807 PRK05807
RNA-binding protein S1;
367-439 1.95e-06

RNA-binding protein S1;


Pssm-ID: 235614 [Multi-domain]  Cd Length: 136  Bit Score: 47.43  E-value: 1.95e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2258881609 367 SGSEAKGEIRNITEFGLFVSLtDDIDGMVHMNDL--SWEKNADEAIKEYKKgqvVQVKILEVDsQKERVALGIKQ 439
Cdd:PRK05807    5 AGSILEGTVVNITNFGAFVEV-EGKTGLVHISEVadTYVKDIREHLKEQDK---VKVKVISID-DNGKISLSIKQ 74
S1_RPS1_repeat_hs4 cd05692
S1_RPS1_repeat_hs4: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
368-438 1.96e-06

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: 45.35  E-value: 1.96e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2258881609 368 GSEAKGEIRNITEFGLFVSLTDDIDGMVHMNDLSWEKNADeaIKEY-KKGQVVQVKILEVDsQKERVALGIK 438
Cdd:cd05692     1 GSVVEGTVTRLKPFGAFVELGGGISGLVHISQIAHKRVKD--VKDVlKEGDKVKVKVLSID-ARGRISLSIK 69
S1_Rrp5_repeat_hs5 cd05697
S1_Rrp5_repeat_hs5: Rrp5 is a trans-acting factor important for biogenesis of both the 40S and ...
368-435 2.09e-06

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: 45.31  E-value: 2.09e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2258881609 368 GSEAKGEIRNITEFGLFVSLTDDIDGMVHMNDLsweknADEAI----KEYKKGQVVQVKILEVDSQKERVAL 435
Cdd:cd05697     1 GQVVKGTIRKLRPSGIFVKLSDHIKGLVPPMHL-----ADVRLkhpeKKFKPGLKVKCRVLSVEPERKRLVL 67
S1_Rrp5_repeat_hs8_sc7 cd04461
S1_Rrp5_repeat_hs8_sc7: Rrp5 Homo sapiens S1 repeat 8 (hs8) and Saccharomyces cerevisiae S1 ...
368-435 2.74e-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: 2.74e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2258881609 368 GSEAKGEIRNITEFGLFVSLTDDIDGMVHMNDLSwEKNADEAIKEYKKGQVVQVKILEVDSQKERVAL 435
Cdd:cd04461    15 GMVVHGYVRNITPYGVFVEFLGGLTGLAPKSYIS-DEFVTDPSFGFKKGQSVTAKVTSVDEEKQRFLL 81
PLN00207 PLN00207
polyribonucleotide nucleotidyltransferase; Provisional
203-287 2.99e-06

polyribonucleotide nucleotidyltransferase; Provisional


Pssm-ID: 215104 [Multi-domain]  Cd Length: 891  Bit Score: 50.28  E-value: 2.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 203 IKNVTDYGAFIDLG-GVDGLLHVTDISWQRVNHPSQVLKVGETIKVKVIKYNKENHrISLGIKQLSDDPWKDVETKFALG 281
Cdd:PLN00207  762 IKSIAPYGAFVEIApGREGLCHISELSSNWLAKPEDAFKVGDRIDVKLIEVNDKGQ-LRLSRRALLPEANSEKSSQKQQG 840

                  ....*.
gi 2258881609 282 STLKGK 287
Cdd:PLN00207  841 GSTKDK 846
S1_IF2_alpha cd04452
S1_IF2_alpha: The alpha subunit of translation Initiation Factor 2, S1-like RNA-binding domain. ...
373-439 3.99e-06

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: 44.88  E-value: 3.99e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2258881609 373 GEIRNITEFGLFVSLT--DDIDGMVHMNDLS--WEKNADEAIKEykkGQVVQVKILEVDSQKERVALGIKQ 439
Cdd:cd04452     9 VTVKSIADMGAYVSLLeyGNIEGMILLSELSrrRIRSIRKLVKV---GRKEVVKVIRVDKEKGYIDLSKKR 76
S1_Rrp5_repeat_hs5 cd05697
S1_Rrp5_repeat_hs5: Rrp5 is a trans-acting factor important for biogenesis of both the 40S and ...
196-261 4.11e-06

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: 44.54  E-value: 4.11e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 196 GAVLDGMIKNVTDYGAFIDL-GGVDGL---LHVTDIswqRVNHPSQVLKVGETIKVKVIKYNKENHRISL 261
Cdd:cd05697     1 GQVVKGTIRKLRPSGIFVKLsDHIKGLvppMHLADV---RLKHPEKKFKPGLKVKCRVLSVEPERKRLVL 67
S1_RPS1_repeat_ec6 cd05691
S1_RPS1_repeat_ec6: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
368-440 5.74e-06

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: 44.18  E-value: 5.74e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2258881609 368 GSEAKGEIRNITEFGLFVSLTDDIDGMVHMNDLSWEKnADEAIKEYKKGQVVQVKILEVDSQKERVALGIKQL 440
Cdd:cd05691     1 GSIVTGKVTEVDAKGATVKLGDGVEGFLRAAELSRDR-VEDATERFKVGDEVEAKITNVDRKNRKISLSIKAK 72
S1_PNPase cd04472
S1_PNPase: Polynucleotide phosphorylase (PNPase), ), S1-like RNA-binding domain. PNPase is a ...
372-429 6.72e-06

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: 44.07  E-value: 6.72e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 372 KGEIRNITEFGLFVSLTDDIDGMVHMNDLSWE--KNADEAIKEykkGQVVQVKILEVDSQ 429
Cdd:cd04472     5 EGKVVKIKDFGAFVEILPGKDGLVHISELSDErvEKVEDVLKV---GDEVKVKVIEVDDR 61
S1_Rrp5_repeat_hs11_sc8 cd05702
S1_Rrp5_repeat_hs11_sc8: Rrp5 is a trans-acting factor important for biogenesis of both the ...
281-345 6.97e-06

S1_Rrp5_repeat_hs11_sc8: 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 11 (hs11) and S. cerevisiae S1 repeat 8 (sc8). Rrp5 is found in eukaryotes but not in prokaryotes or archaea.


Pssm-ID: 240207 [Multi-domain]  Cd Length: 70  Bit Score: 44.12  E-value: 6.97e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2258881609 281 GSTLKGKVTNVTDYGAFVEIGGGVEGLIHVSEI--SWTRKNvQPSNVLSVGDEINVRVLEIEPVKRR 345
Cdd:cd05702     1 GDLVKAKVKSVKPTQLNVQLADNVHGRIHVSEVfdEWPDGK-NPLSKFKIGQKIKARVIGGHDAKTH 66
S1_like cd00164
S1_like: Ribosomal protein S1-like RNA-binding domain. Found in a wide variety of ...
458-522 7.75e-06

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: 43.52  E-value: 7.75e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2258881609 458 VTCEVSAVQSDGIMVTFGEGMSSFIKRAELSSDRNERRPDRFAVGEKVDAKITTIDPSSRRVSVS 522
Cdd:cd00164     1 VTGKVVSITKFGVFVELEDGVEGLVHISELSDKFVKDPSEVFKVGDEVEVKVLEVDPEKGRISLS 65
S1_Rrp5_repeat_hs8_sc7 cd04461
S1_Rrp5_repeat_hs8_sc7: Rrp5 Homo sapiens S1 repeat 8 (hs8) and Saccharomyces cerevisiae S1 ...
451-523 1.11e-05

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: 43.73  E-value: 1.11e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2258881609 451 DLRKGQVVTCEVSAVQSDGIMVTFGEGMSSFIKRAELSSDRNERRPDRFAVGEKVDAKITTIDPSSRRVSVSI 523
Cdd:cd04461    11 DLKPGMVVHGYVRNITPYGVFVEFLGGLTGLAPKSYISDEFVTDPSFGFKKGQSVTAKVTSVDEEKQRFLLSL 83
PRK08563 PRK08563
DNA-directed RNA polymerase subunit E'; Provisional
286-352 4.27e-05

DNA-directed RNA polymerase subunit E'; Provisional


Pssm-ID: 236289 [Multi-domain]  Cd Length: 187  Bit Score: 44.43  E-value: 4.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 286 GKVTNVTDYGAFVEIGGgVEGLIHVSEISWTRKNVQPSN----------VLSVGDEINVRVLEI---EPVKR--RIALGY 350
Cdd:PRK08563   87 GEVVEVVEFGAFVRIGP-VDGLLHISQIMDDYISYDPKNgrligkeskrVLKVGDVVRARIVAVslkERRPRgsKIGLTM 165

                  ..
gi 2258881609 351 KQ 352
Cdd:PRK08563  166 RQ 167
PRK08059 PRK08059
general stress protein 13; Validated
455-532 4.62e-05

general stress protein 13; Validated


Pssm-ID: 181215 [Multi-domain]  Cd Length: 123  Bit Score: 43.11  E-value: 4.62e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2258881609 455 GQVVTCEVSAVQSDGIMVTFGEGMSSFIKRAELSSDRNERRPDRFAVGEKVDAKITTIDPSSRRVSVSIRAREQEEER 532
Cdd:PRK08059    8 GSVVTGKVTGIQPYGAFVALDEETQGLVHISEITHGFVKDIHDFLSVGDEVKVKVLSVDEEKGKISLSIRATEEAPEA 85
S1 pfam00575
S1 RNA binding domain; The S1 domain occurs in a wide range of RNA associated proteins. It is ...
25-90 5.28e-05

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


Pssm-ID: 425760 [Multi-domain]  Cd Length: 72  Bit Score: 41.50  E-value: 5.28e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2258881609  25 GKVLKGRIVRQDREAVTIDVGLKSEGRVPLREFATGGNVPE---LKVGDLVDVYVERMEGATGDIVLSH 90
Cdd:pfam00575   4 GDVVEGEVTRVTKGGAFVDLGNGVEGFIPISELSDDHVEDPdevIKVGDEVKVKVLKVDKDRRRIILSI 72
PRK08563 PRK08563
DNA-directed RNA polymerase subunit E'; Provisional
189-265 5.55e-05

DNA-directed RNA polymerase subunit E'; Provisional


Pssm-ID: 236289 [Multi-domain]  Cd Length: 187  Bit Score: 44.05  E-value: 5.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 189 LVGRLEEGAVLDGMIKNVTDYGAFIDLGGVDGLLHVTDISWQRVNHPSQ-----------VLKVGETIKVKVI-----KY 252
Cdd:PRK08563   75 LVFKPELQEVVEGEVVEVVEFGAFVRIGPVDGLLHISQIMDDYISYDPKngrligkeskrVLKVGDVVRARIVavslkER 154
                          90
                  ....*....|...
gi 2258881609 253 NKENHRISLGIKQ 265
Cdd:PRK08563  155 RPRGSKIGLTMRQ 167
S1_RpoE cd04460
S1_RpoE: RpoE, S1-like RNA-binding domain. S1-like RNA-binding domains are found in a wide ...
286-349 7.37e-05

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: 41.89  E-value: 7.37e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2258881609 286 GKVTNVTDYGAFVEIgGGVEGLIHVSEISWTRKNVQPSN----------VLSVGDEINVRVLEIEPVKRRIALG 349
Cdd:cd04460     5 GEVVEVVDFGAFVRI-GPVDGLLHISQIMDDYISYDPKNkrligeetkrVLKVGDVVRARIVAVSLKERRPRES 77
S1_Rrp5_repeat_sc11 cd05707
S1_Rrp5_repeat_sc11: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ...
368-435 9.73e-05

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: 40.74  E-value: 9.73e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2258881609 368 GSEAKGEIRNITEFGLFVSLTDDIDGMVHMNDLSweknaDEAIKEYKK----GQVVQVKILEVDSQKERVAL 435
Cdd:cd05707     1 GDVVRGFVKNIANNGVFVTLGRGVDARVRVSELS-----DSYLKDWKKrfkvGQLVKGKIVSIDPDNGRIEM 67
S1 pfam00575
S1 RNA binding domain; The S1 domain occurs in a wide range of RNA associated proteins. It is ...
112-174 1.14e-04

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: 40.73  E-value: 1.14e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2258881609 112 VTGVIFSRVKGGFTVDLG-GAIAFLPGSQVDVRPVKDVDA--LMGVAQPFVILKMDRPRGNIVVSR 174
Cdd:pfam00575   7 VEGEVTRVTKGGAFVDLGnGVEGFIPISELSDDHVEDPDEviKVGDEVKVKVLKVDKDRRRIILSI 72
S1_RpoE cd04460
S1_RpoE: RpoE, S1-like RNA-binding domain. S1-like RNA-binding domains are found in a wide ...
198-250 1.33e-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: 41.12  E-value: 1.33e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2258881609 198 VLDGMIKNVTDYGAFIDLGGVDGLLHVTDISWQRV-----------NHPSQVLKVGETIKVKVI 250
Cdd:cd04460     2 VVEGEVVEVVDFGAFVRIGPVDGLLHISQIMDDYIsydpknkrligEETKRVLKVGDVVRARIV 65
S1_RNase_E cd04453
S1_RNase_E: RNase E and RNase G, S1-like RNA-binding domain. RNase E is an essential ...
275-336 1.37e-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: 40.66  E-value: 1.37e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2258881609 275 ETKFALGSTLKGKVTNVTD--YGAFVEIGGGVEGLIHVSEISWT--RKNVQPSNVLSVGDEINVRV 336
Cdd:cd04453     2 NREPIVGNIYLGRVKKIVPglQAAFVDIGLGKNGFLHLSDILPAyfKKHKKIAKLLKEGQEILVQV 67
S1_Rrp5_repeat_sc12 cd05708
S1_Rrp5_repeat_sc12: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ...
455-525 1.55e-04

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: 40.39  E-value: 1.55e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2258881609 455 GQVVTCEVSAVQSDGIMVTF-GEGMSSFIKRAELSSDRNERRPDRFAVGEKVDAKITTIDPSSRRVSVSIRA 525
Cdd:cd05708     3 GQKIDGTVRRVEDYGVFIDIdGTNVSGLCHKSEISDNRVADASKLFRVGDKVRAKVLKIDAEKKRISLGLKA 74
S1 smart00316
Ribosomal protein S1-like RNA-binding domain;
112-175 2.17e-04

Ribosomal protein S1-like RNA-binding domain;


Pssm-ID: 197648 [Multi-domain]  Cd Length: 72  Bit Score: 39.89  E-value: 2.17e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2258881609  112 VTGVIFSRVKGGFTVDLG-GAIAFLPGSQVDVRPVKDVDA--LMGVAQPFVILKMDRPRGNIVVSRR 175
Cdd:smart00316   6 VEGTVTEITPGGAFVDLGnGVEGLIPISELSDKRVKDPEEvlKVGDEVKVKVLSVDEEKGRIILSLK 72
PRK07400 PRK07400
30S ribosomal protein S1; Reviewed
278-529 2.65e-04

30S ribosomal protein S1; Reviewed


Pssm-ID: 180960 [Multi-domain]  Cd Length: 318  Bit Score: 43.25  E-value: 2.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 278 FALGSTLKGKVTNVTDYGAFVEIGGGVEGLIHVSEISWTRKNvQPSNVLSVGDEINVRVLEIEPVKRRIALGYKQC-LEN 356
Cdd:PRK07400   29 FKPGDIVNGTVFSLEPRGALIDIGAKTAAFMPIQEMSINRVE-GPEEVLQPNETREFFILSDENEDGQLTLSIRRIeYMR 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 357 PWEQLARVYPSGSEAKGEIRNITEFGLFVSLtDDIDGMVHMNDLSWEKNADEAIKEYkkgqvVQVKILEVDSQKERVALG 436
Cdd:PRK07400  108 AWERVRQLQKEDATVRSEVFATNRGGALVRI-EGLRGFIPGSHISTRKPKEELVGEE-----LPLKFLEVDEERNRLVLS 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 437 IKQLQSDPfagAVADLRKGQVVTCEVSAVQSDGIMVTFGeGMSSFIKRAELSSDRNERRPDRFAVGEKVDAKITTIDPSS 516
Cdd:PRK07400  182 HRRALVER---KMNRLEVGEVVVGTVRGIKPYGAFIDIG-GVSGLLHISEISHEHIETPHSVFNVNDEMKVMIIDLDAER 257
                         250
                  ....*....|...
gi 2258881609 517 RRVSVSIRAREQE 529
Cdd:PRK07400  258 GRISLSTKQLEPE 270
S1_Rrp5_repeat_sc11 cd05707
S1_Rrp5_repeat_sc11: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ...
455-522 2.81e-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: 39.20  E-value: 2.81e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2258881609 455 GQVVTCEVSAVQSDGIMVTFGEGMSSFIKRAELSSDRNERRPDRFAVGEKVDAKITTIDPSSRRVSVS 522
Cdd:cd05707     1 GDVVRGFVKNIANNGVFVTLGRGVDARVRVSELSDSYLKDWKKRFKVGQLVKGKIVSIDPDNGRIEMT 68
S1_Rrp5_repeat_hs6_sc5 cd05698
S1_Rrp5_repeat_hs6_sc5: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ...
462-524 3.45e-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: 3.45e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2258881609 462 VSAVQSDGIMVTFGEGMSSFIKRAELSSDRNERRPDRFAVGEKVDAKITTIDPSSRRVSVSIR 524
Cdd:cd05698     8 IVKVKPNGCIVSFYNNVKGFLPKSELSEAFIKDPEEHFRVGQVVKVKVLSCDPEQQRLLLSCK 70
S1_RPS1_repeat_ec1_hs1 cd05687
S1_RPS1_repeat_ec1_hs1: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
196-264 4.11e-04

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: 39.05  E-value: 4.11e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 196 GAVLDGMIKNVTDYGAFIDLGG-VDGLLHVTDISWQRVNHPSQVLKVGETIKVKVIKYNKENHRISLGIK 264
Cdd:cd05687     1 GDIVKGTVVSVDDDEVLVDIGYkSEGIIPISEFSDDPIENGEDEVKVGDEVEVYVLRVEDEEGNVVLSKR 70
S1_Rrp5_repeat_sc10 cd05706
S1_Rrp5_repeat_sc10: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ...
373-435 6.14e-04

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: 38.39  E-value: 6.14e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2258881609 373 GEIRNITEFGLFVSLTDDIDGMVHM----NDLSwEKNAdeaiKEYKKGQVVQVKILEVDSQKERVAL 435
Cdd:cd05706     9 GRVTKVNDRYVLVQLGNKVTGPSFItdalDDYS-EALP----YKFKKNDIVRACVLSVDVPNKKIAL 70
S1_RecJ_like cd04473
S1_RecJ_like: The S1 domain of the archaea-specific RecJ-like exonuclease. The function of ...
193-255 6.78e-04

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: 38.36  E-value: 6.78e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2258881609 193 LEEGAVLDGMIKNVTDYGAFIDLGG-VDGLLHvtdiswqRVNHPSQvLKVGETIKVKV--IKYNKE 255
Cdd:cd04473    14 LEVGKLYKGKVNGVAKYGVFVDLNDhVRGLIH-------RSNLLRD-YEVGDEVIVQVtdIPENGN 71
S1_RPS1_repeat_ec1_hs1 cd05687
S1_RPS1_repeat_ec1_hs1: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
455-524 9.48e-04

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: 37.89  E-value: 9.48e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 455 GQVVTCEVSAVQSDGIMVTFGEGMSSFIKRAELSSDRNERRPDRFAVGEKVDAKITTIDPSSRRVSVSIR 524
Cdd:cd05687     1 GDIVKGTVVSVDDDEVLVDIGYKSEGIIPISEFSDDPIENGEDEVKVGDEVEVYVLRVEDEEGNVVLSKR 70
RpsA COG0539
Ribosomal protein S1 [Translation, ribosomal structure and biogenesis]; Ribosomal protein S1 ...
445-530 1.01e-03

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: 41.57  E-value: 1.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 445 FAGAVADLRKGQVVTCEVSAVQSDGIMVTFGEGMSSFIKRAELSSDRNErrpDRFAVGEKVDAKITTIDPSSRRVSVSIR 524
Cdd:COG0539     9 LEESLKELKEGDIVKGTVVSIDDDEVLVDIGYKSEGIIPLSEFSDEPGE---LEVKVGDEVEVYVEKVEDGEGEIVLSKK 85

                  ....*.
gi 2258881609 525 AREQEE 530
Cdd:COG0539    86 KADREK 91
PLN00207 PLN00207
polyribonucleotide nucleotidyltransferase; Provisional
421-568 1.76e-03

polyribonucleotide nucleotidyltransferase; Provisional


Pssm-ID: 215104 [Multi-domain]  Cd Length: 891  Bit Score: 41.42  E-value: 1.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 421 VKILEVD-SQKERVALGIKQLQSDPfagAVADLRKgqvvTCEVSAVQSDGIMVTFGEGMSSFIKRAELSSDRNERRPDRF 499
Cdd:PLN00207  727 VKITAKDlSSLEKSKAIISSLTMVP---TVGDIYR----NCEIKSIAPYGAFVEIAPGREGLCHISELSSNWLAKPEDAF 799
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2258881609 500 AVGEKVDAKITTI-DPSSRRVSVSIRAREQEEERVAMEKYG--STDSGASLGDILGEALAKADTKTERPASK 568
Cdd:PLN00207  800 KVGDRIDVKLIEVnDKGQLRLSRRALLPEANSEKSSQKQQGgsTKDKAPQKKYVNTSSRPRRAAQAEKNSAE 871
COG1107 COG1107
Archaea-specific RecJ-like exonuclease, contains DnaJ-type Zn finger domain [Replication, ...
193-275 2.06e-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: 40.98  E-value: 2.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258881609 193 LEEGAVLDGMIKNVTDYGAFIDLG-GVDGLLHVTDIswqrvnhpSQVLKVGETIKVKViKYNKENHRISLGIKQLSDDPW 271
Cdd:COG1107    37 LEPGRYYRGTVDGVADFGVFVDLNdHVTGLLHRSEL--------DQDWEVGDEVFVQV-KEVRDNGNVDLGWVSIDSYET 107

                  ....
gi 2258881609 272 KDVE 275
Cdd:COG1107   108 VEVE 111
PRK03987 PRK03987
translation initiation factor IF-2 subunit alpha; Validated
373-438 2.85e-03

translation initiation factor IF-2 subunit alpha; Validated


Pssm-ID: 235188 [Multi-domain]  Cd Length: 262  Bit Score: 39.81  E-value: 2.85e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2258881609 373 GEIRNITEFGLFVSLT--DDIDGMVHMNDLS--WEKNadeaIKEY-KKGQVVQVKILEVDSQKERVALGIK 438
Cdd:PRK03987   14 GTVKEVKDFGAFVTLDeyPGKEGFIHISEVAsgWVKN----IRDHvKEGQKVVCKVIRVDPRKGHIDLSLK 80
PRK08582 PRK08582
RNA-binding protein S1;
368-444 3.37e-03

RNA-binding protein S1;


Pssm-ID: 236305 [Multi-domain]  Cd Length: 139  Bit Score: 38.09  E-value: 3.37e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2258881609 368 GSEAKGEIRNITEFGLFVSLTDDIDGMVHMNDLSweKNADEAIKEY-KKGQVVQVKILEVDsQKERVALGIKQLQSDP 444
Cdd:PRK08582    6 GSKLQGKVTGITNFGAFVELPEGKTGLVHISEVA--DNYVKDINDHlKVGDEVEVKVLNVE-DDGKIGLSIKKAKDRP 80
S1_Rrp5_repeat_hs3 cd05695
S1_Rrp5_repeat_hs3: Rrp5 is a trans-acting factor important for biogenesis of both the 40S and ...
455-522 3.89e-03

S1_Rrp5_repeat_hs3: 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 3 (hs3). Rrp5 is found in eukaryotes but not in prokaryotes or archaea.


Pssm-ID: 240200 [Multi-domain]  Cd Length: 66  Bit Score: 36.10  E-value: 3.89e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2258881609 455 GQVVTCEVSAVQSDGIMVTFgegMSSFIKRA-ELSSDRNERRPDRFAVGEKVDAKITTIDPSSRRVSVS 522
Cdd:cd05695     1 GMLVNARVKKVLSNGLILDF---LSSFTGTVdFLHLDPEKSSKSTYKEGQKVRARILYVDPSTKVVGLS 66
S1_Rrp5_repeat_sc11 cd05707
S1_Rrp5_repeat_sc11: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ...
196-261 5.11e-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: 35.73  E-value: 5.11e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2258881609 196 GAVLDGMIKNVTDYGAFIDLG-GVDGLLHVTDISWQRVNHPSQVLKVGETIKVKVIKYNKENHRISL 261
Cdd:cd05707     1 GDVVRGFVKNIANNGVFVTLGrGVDARVRVSELSDSYLKDWKKRFKVGQLVKGKIVSIDPDNGRIEM 67
S1_Rrp4 cd05789
S1_Rrp4: Rrp4 S1-like RNA-binding domain. S1-like RNA-binding domains are found in a wide ...
286-344 7.75e-03

S1_Rrp4: Rrp4 S1-like RNA-binding domain. S1-like RNA-binding domains are found in a wide variety of RNA-associated proteins. Rrp4 protein is a subunit of the exosome complex. The exosome plays a central role in 3' to 5' RNA processing and degradation in eukarytes and archaea. Its functions include the removal of incorrectly processed RNA and the maintenance of proper levels of mRNA, rRNA and a number of small RNA species. In Saccharomyces cerevisiae, the exosome includes nine core components, six of which are homologous to bacterial RNase PH. These form a hexameric ring structure. The other three subunits (RrP4, Rrp40, and Csl4) contain an S1 RNA binding domain and are part of the "S1 pore structure".


Pssm-ID: 240215 [Multi-domain]  Cd Length: 86  Bit Score: 35.60  E-value: 7.75e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2258881609 286 GKVTNVTDYGAFVEIGGGVEGLIHVSEISWTRKNV---QPSNVLSVGDEINVRVLEIEPVKR 344
Cdd:cd05789    12 GRVTEVGFKRWKVDINSPYDAVLPLSEVNLPRTDEdelNMRSYLDEGDLIVAEVQSVDSDGS 73
S1_Rrp5_repeat_hs11_sc8 cd05702
S1_Rrp5_repeat_hs11_sc8: Rrp5 is a trans-acting factor important for biogenesis of both the ...
368-424 8.14e-03

S1_Rrp5_repeat_hs11_sc8: 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 11 (hs11) and S. cerevisiae S1 repeat 8 (sc8). Rrp5 is found in eukaryotes but not in prokaryotes or archaea.


Pssm-ID: 240207 [Multi-domain]  Cd Length: 70  Bit Score: 35.26  E-value: 8.14e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2258881609 368 GSEAKGEIRNITEFGLFVSLTDDIDGMVHMNDL--SWeKNADEAIKEYKKGQVVQVKIL 424
Cdd:cd05702     1 GDLVKAKVKSVKPTQLNVQLADNVHGRIHVSEVfdEW-PDGKNPLSKFKIGQKIKARVI 58
S1_Rrp5_repeat_hs5 cd05697
S1_Rrp5_repeat_hs5: Rrp5 is a trans-acting factor important for biogenesis of both the 40S and ...
455-521 8.16e-03

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: 35.29  E-value: 8.16e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2258881609 455 GQVVTCEVSAVQSDGIMVTFGEGMSSFIKRAELSsDRNERRPDR-FAVGEKVDAKITTIDPSSRRVSV 521
Cdd:cd05697     1 GQVVKGTIRKLRPSGIFVKLSDHIKGLVPPMHLA-DVRLKHPEKkFKPGLKVKCRVLSVEPERKRLVL 67
CafA COG1530
Ribonuclease G or E [Translation, ribosomal structure and biogenesis];
285-336 8.67e-03

Ribonuclease G or E [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441139 [Multi-domain]  Cd Length: 490  Bit Score: 38.98  E-value: 8.67e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2258881609 285 KGKVTNVTDyG---AFVEIGGGVEGLIHVSEISWTRKNVQP---------SNVLSVGDEINVRV 336
Cdd:COG1530    41 KGKVTRVLP-GlqaAFVDIGLERHGFLHVKDISPEYFSLGKedsgkrpniQDVLKEGQEVLVQV 103
S1_Rrp5_repeat_sc11 cd05707
S1_Rrp5_repeat_sc11: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ...
281-348 8.79e-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: 34.96  E-value: 8.79e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2258881609 281 GSTLKGKVTNVTDYGAFVEIGGGVEGLIHVSEISWTR-KNVQPSnvLSVGDEINVRVLEIEPVKRRIAL 348
Cdd:cd05707     1 GDVVRGFVKNIANNGVFVTLGRGVDARVRVSELSDSYlKDWKKR--FKVGQLVKGKIVSIDPDNGRIEM 67
 
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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