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Conserved domains on  [gi|1015655940|gb|KZA06265|]
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ribosomal protein S1 [Akkermansia sp. KLE1605]

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
2-522 0e+00

30S ribosomal protein S1; Reviewed


:

Pssm-ID: 235775 [Multi-domain]  Cd Length: 565  Bit Score: 681.50  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940   2 STTELAELIDSKF--RELREGSIVTGTIQEIRPQVVLVDIGYKSEGAISISEFEDE----EIEVGDQIEVLLERLENDEG 75
Cdd:PRK06299   11 MEESFAELFEESLkeSETREGSIVKGTVVAIDKDYVLVDVGLKSEGRIPLEEFKNEqgelEVKVGDEVEVYVERIEDGFG 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940  76 IVVLSKEKAAHKQNWDKIVGVYRDGGLVKGKVKSVVKGGLMVNV-GVEAFLPGSQVDIIPPRDLNEYVGKVYEFKIVKVN 154
Cdd:PRK06299   91 ETVLSREKAKRLEAWDKLEKAFENGEIVEGVINGKVKGGFTVDLnGVEAFLPGSQVDVRPVRDTDPLEGKELEFKVIKLD 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 155 DDRKNIVLSRREVIEAERADQRQRFLETVKEGDKVEGLVKNITDFGAFVDLRGMDGLLHITDMSWGRVNHPSEMLHIGQS 234
Cdd:PRK06299  171 KKRNNIVVSRRAVLEEERAEEREELLENLEEGQVVEGVVKNITDYGAFVDLGGVDGLLHITDISWKRVNHPSEVVNVGDE 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 235 LEVVILEVDRDKERVSLGLKQMTDNPWADIERKYPINSQVKGRVTKLLPYGAFVELEKGVEGLVHVSELSWVKRITRPSD 314
Cdd:PRK06299  251 VKVKVLKFDKEKKRVSLGLKQLGEDPWEAIEKKYPVGSKVKGKVTNITDYGAFVELEEGIEGLVHVSEMSWTKKNKHPSK 330
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 315 VLKLDQEIEAVVLSISVKEQKISLGVRQLEDNPWADIESRFPIGTVIKGQVRNLTPYGAFVGLEEGIDGMIHVSDMSWTR 394
Cdd:PRK06299  331 VVSVGQEVEVMVLEIDEEKRRISLGLKQCKENPWEEFAEKYPVGDVVEGKVKNITDFGAFVGLEGGIDGLVHLSDISWDK 410
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 395 KINHPSEVLKKGDEVEAIVLEIKKEDQRVSLGIKQLESDPWESINDRFKVGDMVSGQVAKIASFGAFVNLDGDIDGLIHI 474
Cdd:PRK06299  411 KGEEAVELYKKGDEVEAVVLKVDVEKERISLGIKQLEEDPFEEFAKKHKKGSIVTGTVTEVKDKGAFVELEDGVEGLIRA 490
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 1015655940 475 SQLSEDHVERVKDVIKVGDEITARVIKVDSIERRIGLSIKAVNYDTEQ 522
Cdd:PRK06299  491 SELSRDRVEDATEVLKVGDEVEAKVINIDRKNRRISLSIKALDEAEEK 538
 
Name Accession Description Interval E-value
rpsA PRK06299
30S ribosomal protein S1; Reviewed
2-522 0e+00

30S ribosomal protein S1; Reviewed


Pssm-ID: 235775 [Multi-domain]  Cd Length: 565  Bit Score: 681.50  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940   2 STTELAELIDSKF--RELREGSIVTGTIQEIRPQVVLVDIGYKSEGAISISEFEDE----EIEVGDQIEVLLERLENDEG 75
Cdd:PRK06299   11 MEESFAELFEESLkeSETREGSIVKGTVVAIDKDYVLVDVGLKSEGRIPLEEFKNEqgelEVKVGDEVEVYVERIEDGFG 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940  76 IVVLSKEKAAHKQNWDKIVGVYRDGGLVKGKVKSVVKGGLMVNV-GVEAFLPGSQVDIIPPRDLNEYVGKVYEFKIVKVN 154
Cdd:PRK06299   91 ETVLSREKAKRLEAWDKLEKAFENGEIVEGVINGKVKGGFTVDLnGVEAFLPGSQVDVRPVRDTDPLEGKELEFKVIKLD 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 155 DDRKNIVLSRREVIEAERADQRQRFLETVKEGDKVEGLVKNITDFGAFVDLRGMDGLLHITDMSWGRVNHPSEMLHIGQS 234
Cdd:PRK06299  171 KKRNNIVVSRRAVLEEERAEEREELLENLEEGQVVEGVVKNITDYGAFVDLGGVDGLLHITDISWKRVNHPSEVVNVGDE 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 235 LEVVILEVDRDKERVSLGLKQMTDNPWADIERKYPINSQVKGRVTKLLPYGAFVELEKGVEGLVHVSELSWVKRITRPSD 314
Cdd:PRK06299  251 VKVKVLKFDKEKKRVSLGLKQLGEDPWEAIEKKYPVGSKVKGKVTNITDYGAFVELEEGIEGLVHVSEMSWTKKNKHPSK 330
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 315 VLKLDQEIEAVVLSISVKEQKISLGVRQLEDNPWADIESRFPIGTVIKGQVRNLTPYGAFVGLEEGIDGMIHVSDMSWTR 394
Cdd:PRK06299  331 VVSVGQEVEVMVLEIDEEKRRISLGLKQCKENPWEEFAEKYPVGDVVEGKVKNITDFGAFVGLEGGIDGLVHLSDISWDK 410
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 395 KINHPSEVLKKGDEVEAIVLEIKKEDQRVSLGIKQLESDPWESINDRFKVGDMVSGQVAKIASFGAFVNLDGDIDGLIHI 474
Cdd:PRK06299  411 KGEEAVELYKKGDEVEAVVLKVDVEKERISLGIKQLEEDPFEEFAKKHKKGSIVTGTVTEVKDKGAFVELEDGVEGLIRA 490
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 1015655940 475 SQLSEDHVERVKDVIKVGDEITARVIKVDSIERRIGLSIKAVNYDTEQ 522
Cdd:PRK06299  491 SELSRDRVEDATEVLKVGDEVEAKVINIDRKNRRISLSIKALDEAEEK 538
rpsA TIGR00717
ribosomal protein S1; This model describes ribosomal protein S1, RpsA. This protein is found ...
13-514 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: 563.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940  13 KFRELREGSIVTGTIQEIRPQVVLVDIGYKSEGAISISEFEDE--EIEVGDQIEVLLERLENDEGIVVLSKEKAAHKQNW 90
Cdd:TIGR00717  12 KTEETRPGSIVKGTVVAINKDTVFVDVGLKSEGRIPKEEFLDAplEIQVGDEVEVYLDRVEDRFGETVLSREKAQRHELW 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940  91 DKIVGVYRDGGLVKGKVKSVVKGGLMVNV-GVEAFLPGSQVDIIPPRDLNEYVGKVYEFKIVKVNDDRKNIVLSRREVIE 169
Cdd:TIGR00717  92 IKLEKAYEEGSIVEGKIVGKVKGGFIVDLnGVEAFLPGSQVDVKPIKDLDSLIGKTLKFKIIKLDQKRNNIVVSRRAYLE 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 170 AERADQRQRFLETVKEGDKVEGLVKNITDFGAFVDLRGMDGLLHITDMSWGRVNHPSEMLHIGQSLEVVILEVDRDKERV 249
Cdd:TIGR00717 172 EERSQAREELLENLKEGDVVKGVVKNITDFGAFVDLGGVDGLLHITDMSWKRVKHPSEYVKVGQEVKVKVIKFDKEKGRI 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 250 SLGLKQMTDNPWADIERKYPINSQVKGRVTKLLPYGAFVELEKGVEGLVHVSELSWVKRITRPSDVLKLDQEIEAVVLSI 329
Cdd:TIGR00717 252 SLSLKQLGEDPWEAIEKKFPVGDKITGRVTNLTDYGVFVEIEEGIEGLVHVSEMSWVKKNSHPSKVVKKGDEVEVMILDI 331
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 330 SVKEQKISLGVRQLEDNPWADIESRFPIGTVIKGQVRNLTPYGAFVGLEEGIDGMIHVSDMSWTRKINHPSEVLKKGDEV 409
Cdd:TIGR00717 332 DPERRRLSLGLKQCKANPWEQFEEKHPVGDRVTGKIKKITDFGAFVELEGGIDGLIHLSDISWDKDGREADHLYKKGDEI 411
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 410 EAIVLEIKKEDQRVSLGIKQLESDPWESINDRFKVGDMVSGQVAKIASFGAFVNLDGDIDGLIHISQLSEDHVERVKDVI 489
Cdd:TIGR00717 412 EAVVLAVDKEKKRISLGVKQLTENPWEKFAAKYKVGSVVKGKVTEIKDFGAFVELPGGVEGLIRNSELSENRDEDKTDEI 491
                         490       500
                  ....*....|....*....|....*
gi 1015655940 490 KVGDEITARVIKVDSIERRIGLSIK 514
Cdd:TIGR00717 492 KVGDEVEAKVVDIDKKNRKVSLSVK 516
RpsA COG0539
Ribosomal protein S1 [Translation, ribosomal structure and biogenesis]; Ribosomal protein S1 ...
2-343 5.12e-163

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: 467.60  E-value: 5.12e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940   2 STTELAELIDSKFRELREGSIVTGTIQEIRPQVVLVDIGYKSEGAISISEFEDE----EIEVGDQIEVLLERLENDEGIV 77
Cdd:COG0539     1 MSESFAELLEESLKELKEGDIVKGTVVSIDDDEVLVDIGYKSEGIIPLSEFSDEpgelEVKVGDEVEVYVEKVEDGEGEI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940  78 VLSKEKAAHKQNWDKIVGVYRDGGLVKGKVKSVVKGGLMVNV-GVEAFLPGSQVDIIPPRDLNEYVGKVYEFKIVKVNDD 156
Cdd:COG0539    81 VLSKKKADREKAWEELEEAFENGEPVEGKVKGVVKGGLIVDIgGVRAFLPASQVDVRPVRDLDEYVGKTLEFKIIKLDRK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 157 RKNIVLSRREVIEAERADQRQRFLETVKEGDKVEGLVKNITDFGAFVDLRGMDGLLHITDMSWGRVNHPSEMLHIGQSLE 236
Cdd:COG0539   161 RNNVVVSRRAVLEEEREEKREELLEKLEEGDVVEGTVKNITDFGAFVDLGGVDGLLHISEISWGRVKHPSEVLKVGDEVE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 237 VVILEVDRDKERVSLGLKQMTDNPWADIERKYPINSQVKGRVTKLLPYGAFVELEKGVEGLVHVSELSWVKRITRPSDVL 316
Cdd:COG0539   241 VKVLKIDREKERISLSLKQLQPDPWENIAEKYPVGDVVKGKVTRLTDFGAFVELEPGVEGLVHISEMSWTKRVAHPSDVV 320
                         330       340
                  ....*....|....*....|....*..
gi 1015655940 317 KLDQEIEAVVLSISVKEQKISLGVRQL 343
Cdd:COG0539   321 KVGDEVEVKVLDIDPEERRISLSIKQL 347
S1_RPS1_repeat_ec3 cd05688
S1_RPS1_repeat_ec3: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
185-252 6.99e-31

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: 114.65  E-value: 6.99e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1015655940 185 EGDKVEGLVKNITDFGAFVDLRGMDGLLHITDMSWGRVNHPSEMLHIGQSLEVVILEVDRDKERVSLG 252
Cdd:cd05688     1 EGDVVEGTVKSITDFGAFVDLGGVDGLLHISDMSWGRVKHPSEVVNVGDEVEVKVLKIDKERKRISLG 68
S1_dom_CvfD NF040579
CvfD/Ygs/GSP13 family RNA-binding post-transcriptional regulator; CvfD, Ygs, and GSP13 form a ...
442-525 1.79e-18

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: 80.93  E-value: 1.79e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 442 FKVGDMVSGQVAKIASFGAFVNLDGDIDGLIHISQLSEDHVERVKDVIKVGDEITARVIKVDSIERRIGLSIKAVNYDTE 521
Cdd:NF040579    1 YKIGDIVEGKVTGIQPYGAFVALDEHTQGLIHISEIKHGYVKDINDFLKVGQEVKVKVLDIDEYTGKISLSLRALEEAPE 80

                  ....
gi 1015655940 522 QLRR 525
Cdd:NF040579   81 KHRK 84
S1_dom_CvfD NF040579
CvfD/Ygs/GSP13 family RNA-binding post-transcriptional regulator; CvfD, Ygs, and GSP13 form a ...
268-347 5.26e-18

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: 79.78  E-value: 5.26e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 268 YPINSQVKGRVTKLLPYGAFVELEKGVEGLVHVSELS--WVKRItrpSDVLKLDQEIEAVVLSISVKEQKISLGVRQLED 345
Cdd:NF040579    1 YKIGDIVEGKVTGIQPYGAFVALDEHTQGLIHISEIKhgYVKDI---NDFLKVGQEVKVKVLDIDEYTGKISLSLRALEE 77

                  ..
gi 1015655940 346 NP 347
Cdd:NF040579   78 AP 79
S1 smart00316
Ribosomal protein S1-like RNA-binding domain;
443-514 7.57e-18

Ribosomal protein S1-like RNA-binding domain;


Pssm-ID: 197648 [Multi-domain]  Cd Length: 72  Bit Score: 78.03  E-value: 7.57e-18
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1015655940  443 KVGDMVSGQVAKIASFGAFVNLDGDIDGLIHISQLSEDHVERVKDVIKVGDEITARVIKVDSIERRIGLSIK 514
Cdd:smart00316   1 EVGDVVEGTVTEITPGGAFVDLGNGVEGLIPISELSDKRVKDPEEVLKVGDEVKVKVLSVDEEKGRIILSLK 72
S1 pfam00575
S1 RNA binding domain; The S1 domain occurs in a wide range of RNA associated proteins. It is ...
442-513 2.21e-15

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


Pssm-ID: 425760 [Multi-domain]  Cd Length: 72  Bit Score: 70.78  E-value: 2.21e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1015655940 442 FKVGDMVSGQVAKIASFGAFVNLDGDIDGLIHISQLSEDHVERVKDVIKVGDEITARVIKVDSIERRIGLSI 513
Cdd:pfam00575   1 PEKGDVVEGEVTRVTKGGAFVDLGNGVEGFIPISELSDDHVEDPDEVIKVGDEVKVKVLKVDKDRRRIILSI 72
S1_dom_CvfD NF040579
CvfD/Ygs/GSP13 family RNA-binding post-transcriptional regulator; CvfD, Ygs, and GSP13 form a ...
357-434 4.79e-13

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: 65.53  E-value: 4.79e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 357 IGTVIKGQVRNLTPYGAFVGLEEGIDGMIHVSDMS--WTRKINhpsEVLKKGDEVEAIVLEIKKEDQRVSLGIKQLESDP 434
Cdd:NF040579    3 IGDIVEGKVTGIQPYGAFVALDEHTQGLIHISEIKhgYVKDIN---DFLKVGQEVKVKVLDIDEYTGKISLSLRALEEAP 79
 
Name Accession Description Interval E-value
rpsA PRK06299
30S ribosomal protein S1; Reviewed
2-522 0e+00

30S ribosomal protein S1; Reviewed


Pssm-ID: 235775 [Multi-domain]  Cd Length: 565  Bit Score: 681.50  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940   2 STTELAELIDSKF--RELREGSIVTGTIQEIRPQVVLVDIGYKSEGAISISEFEDE----EIEVGDQIEVLLERLENDEG 75
Cdd:PRK06299   11 MEESFAELFEESLkeSETREGSIVKGTVVAIDKDYVLVDVGLKSEGRIPLEEFKNEqgelEVKVGDEVEVYVERIEDGFG 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940  76 IVVLSKEKAAHKQNWDKIVGVYRDGGLVKGKVKSVVKGGLMVNV-GVEAFLPGSQVDIIPPRDLNEYVGKVYEFKIVKVN 154
Cdd:PRK06299   91 ETVLSREKAKRLEAWDKLEKAFENGEIVEGVINGKVKGGFTVDLnGVEAFLPGSQVDVRPVRDTDPLEGKELEFKVIKLD 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 155 DDRKNIVLSRREVIEAERADQRQRFLETVKEGDKVEGLVKNITDFGAFVDLRGMDGLLHITDMSWGRVNHPSEMLHIGQS 234
Cdd:PRK06299  171 KKRNNIVVSRRAVLEEERAEEREELLENLEEGQVVEGVVKNITDYGAFVDLGGVDGLLHITDISWKRVNHPSEVVNVGDE 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 235 LEVVILEVDRDKERVSLGLKQMTDNPWADIERKYPINSQVKGRVTKLLPYGAFVELEKGVEGLVHVSELSWVKRITRPSD 314
Cdd:PRK06299  251 VKVKVLKFDKEKKRVSLGLKQLGEDPWEAIEKKYPVGSKVKGKVTNITDYGAFVELEEGIEGLVHVSEMSWTKKNKHPSK 330
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 315 VLKLDQEIEAVVLSISVKEQKISLGVRQLEDNPWADIESRFPIGTVIKGQVRNLTPYGAFVGLEEGIDGMIHVSDMSWTR 394
Cdd:PRK06299  331 VVSVGQEVEVMVLEIDEEKRRISLGLKQCKENPWEEFAEKYPVGDVVEGKVKNITDFGAFVGLEGGIDGLVHLSDISWDK 410
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 395 KINHPSEVLKKGDEVEAIVLEIKKEDQRVSLGIKQLESDPWESINDRFKVGDMVSGQVAKIASFGAFVNLDGDIDGLIHI 474
Cdd:PRK06299  411 KGEEAVELYKKGDEVEAVVLKVDVEKERISLGIKQLEEDPFEEFAKKHKKGSIVTGTVTEVKDKGAFVELEDGVEGLIRA 490
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 1015655940 475 SQLSEDHVERVKDVIKVGDEITARVIKVDSIERRIGLSIKAVNYDTEQ 522
Cdd:PRK06299  491 SELSRDRVEDATEVLKVGDEVEAKVINIDRKNRRISLSIKALDEAEEK 538
rpsA TIGR00717
ribosomal protein S1; This model describes ribosomal protein S1, RpsA. This protein is found ...
13-514 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: 563.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940  13 KFRELREGSIVTGTIQEIRPQVVLVDIGYKSEGAISISEFEDE--EIEVGDQIEVLLERLENDEGIVVLSKEKAAHKQNW 90
Cdd:TIGR00717  12 KTEETRPGSIVKGTVVAINKDTVFVDVGLKSEGRIPKEEFLDAplEIQVGDEVEVYLDRVEDRFGETVLSREKAQRHELW 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940  91 DKIVGVYRDGGLVKGKVKSVVKGGLMVNV-GVEAFLPGSQVDIIPPRDLNEYVGKVYEFKIVKVNDDRKNIVLSRREVIE 169
Cdd:TIGR00717  92 IKLEKAYEEGSIVEGKIVGKVKGGFIVDLnGVEAFLPGSQVDVKPIKDLDSLIGKTLKFKIIKLDQKRNNIVVSRRAYLE 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 170 AERADQRQRFLETVKEGDKVEGLVKNITDFGAFVDLRGMDGLLHITDMSWGRVNHPSEMLHIGQSLEVVILEVDRDKERV 249
Cdd:TIGR00717 172 EERSQAREELLENLKEGDVVKGVVKNITDFGAFVDLGGVDGLLHITDMSWKRVKHPSEYVKVGQEVKVKVIKFDKEKGRI 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 250 SLGLKQMTDNPWADIERKYPINSQVKGRVTKLLPYGAFVELEKGVEGLVHVSELSWVKRITRPSDVLKLDQEIEAVVLSI 329
Cdd:TIGR00717 252 SLSLKQLGEDPWEAIEKKFPVGDKITGRVTNLTDYGVFVEIEEGIEGLVHVSEMSWVKKNSHPSKVVKKGDEVEVMILDI 331
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 330 SVKEQKISLGVRQLEDNPWADIESRFPIGTVIKGQVRNLTPYGAFVGLEEGIDGMIHVSDMSWTRKINHPSEVLKKGDEV 409
Cdd:TIGR00717 332 DPERRRLSLGLKQCKANPWEQFEEKHPVGDRVTGKIKKITDFGAFVELEGGIDGLIHLSDISWDKDGREADHLYKKGDEI 411
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 410 EAIVLEIKKEDQRVSLGIKQLESDPWESINDRFKVGDMVSGQVAKIASFGAFVNLDGDIDGLIHISQLSEDHVERVKDVI 489
Cdd:TIGR00717 412 EAVVLAVDKEKKRISLGVKQLTENPWEKFAAKYKVGSVVKGKVTEIKDFGAFVELPGGVEGLIRNSELSENRDEDKTDEI 491
                         490       500
                  ....*....|....*....|....*
gi 1015655940 490 KVGDEITARVIKVDSIERRIGLSIK 514
Cdd:TIGR00717 492 KVGDEVEAKVVDIDKKNRKVSLSVK 516
RpsA COG0539
Ribosomal protein S1 [Translation, ribosomal structure and biogenesis]; Ribosomal protein S1 ...
2-343 5.12e-163

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: 467.60  E-value: 5.12e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940   2 STTELAELIDSKFRELREGSIVTGTIQEIRPQVVLVDIGYKSEGAISISEFEDE----EIEVGDQIEVLLERLENDEGIV 77
Cdd:COG0539     1 MSESFAELLEESLKELKEGDIVKGTVVSIDDDEVLVDIGYKSEGIIPLSEFSDEpgelEVKVGDEVEVYVEKVEDGEGEI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940  78 VLSKEKAAHKQNWDKIVGVYRDGGLVKGKVKSVVKGGLMVNV-GVEAFLPGSQVDIIPPRDLNEYVGKVYEFKIVKVNDD 156
Cdd:COG0539    81 VLSKKKADREKAWEELEEAFENGEPVEGKVKGVVKGGLIVDIgGVRAFLPASQVDVRPVRDLDEYVGKTLEFKIIKLDRK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 157 RKNIVLSRREVIEAERADQRQRFLETVKEGDKVEGLVKNITDFGAFVDLRGMDGLLHITDMSWGRVNHPSEMLHIGQSLE 236
Cdd:COG0539   161 RNNVVVSRRAVLEEEREEKREELLEKLEEGDVVEGTVKNITDFGAFVDLGGVDGLLHISEISWGRVKHPSEVLKVGDEVE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 237 VVILEVDRDKERVSLGLKQMTDNPWADIERKYPINSQVKGRVTKLLPYGAFVELEKGVEGLVHVSELSWVKRITRPSDVL 316
Cdd:COG0539   241 VKVLKIDREKERISLSLKQLQPDPWENIAEKYPVGDVVKGKVTRLTDFGAFVELEPGVEGLVHISEMSWTKRVAHPSDVV 320
                         330       340
                  ....*....|....*....|....*..
gi 1015655940 317 KLDQEIEAVVLSISVKEQKISLGVRQL 343
Cdd:COG0539   321 KVGDEVEVKVLDIDPEERRISLSIKQL 347
PRK00087 PRK00087
bifunctional 4-hydroxy-3-methylbut-2-enyl diphosphate reductase/30S ribosomal protein S1;
1-347 6.67e-122

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


Pssm-ID: 234623 [Multi-domain]  Cd Length: 647  Bit Score: 373.13  E-value: 6.67e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940   1 MSTTELAELIDSKFRELREGSIVTGTIQEIRPQVVLVDIGYKSEGAISISEF-------EDEEIEVGDQIEVLLERLEND 73
Cdd:PRK00087  284 VEENEQLEYMNELEKQIRRGDIVKGTVVSVNENEVFVDVGYKSEGVIPLRELtldeissLKESVKVGDEIEVKVLKLEDE 363
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940  74 EGIVVLSKEKAAHKQNWDKIVGVYRDGGLVKGKVKSVVKGGLMVNVG-VEAFLPGSQVDIIPPRDLNEYVGKVYEFKIVK 152
Cdd:PRK00087  364 DGYVVLSKKEADREKAWKELEEAFENGEPVKGKVKEVVKGGLLVDYGgVRAFLPASHVELGYVEDLSEYKGQELEVKIIE 443
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 153 VN-DDRKNIVLSRREVIEAERADQRQRFLETVKEGDKVEGLVKNITDFGAFVDLRGMDGLLHITDMSWGRVNHPSEMLHI 231
Cdd:PRK00087  444 FNrKRRKKVVLSRKAILEEEKEKKKEETWNSLEEGDVVEGEVKRLTDFGAFVDIGGVDGLLHVSEISWGRVEKPSDVLKV 523
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 232 GQSLEVVILEVDRDKERVSLGLKQMTDNPWADIERKYPINSQVKGRVTKLLPYGAFVELEKGVEGLVHVSELSWvKRITR 311
Cdd:PRK00087  524 GDEIKVYILDIDKENKKLSLSLKKLLPDPWENVEEKYPVGSIVLGKVVRIAPFGAFVELEPGVDGLVHISQISW-KRIDK 602
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 1015655940 312 PSDVLKLDQEIEAVVLSISVKEQKISLGVRQLEDNP 347
Cdd:PRK00087  603 PEDVLSEGEEVKAKILEVDPEEKRIRLSIKEVEEEP 638
PRK12269 PRK12269
bifunctional cytidylate kinase/ribosomal protein S1; Provisional
14-530 1.06e-114

bifunctional cytidylate kinase/ribosomal protein S1; Provisional


Pssm-ID: 105491 [Multi-domain]  Cd Length: 863  Bit Score: 360.57  E-value: 1.06e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940  14 FRELREGSIVTGTIQEIRPQVVLVDIGYKSEGAISISEFEDEEiEVGDQIEVLLERLE--NDEgivvLSKEKAAHKQNWD 91
Cdd:PRK12269  316 FEAPEPGSVRMGTVVQVNAGTVFVDIGGKSEGRVPVEEFEAPP-KAGDGVRVYVERVTpyGPE----LSKTKADRLGLKV 390
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940  92 KIVGVYRDG----GLVKGKVKSVVKGGLMVNVGVEAFLPGSQVD---IIPPRDLNEYVGKVYEFKIVKVNDDR--KNIVL 162
Cdd:PRK12269  391 KLRDAERDGtpveGRIVRLTEKKSGFEVDLGAGMMAFLPISQSDcqkVDAPESLIGLTSKFYIERISQSKQHRgnDNIVI 470
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 163 SRREVIEaERADQ-RQRFLETVKEGDKVEGLVKNITDFGAFVDLRGMDGLLHITDMSWGRVNHPSEMLHIGQSLEVVILE 241
Cdd:PRK12269  471 NRRRYLE-ERARQaREEFFNSVHIEDSVSGVVKSFTSFGAFIDLGGFDGLLHVNDMSWGHVARPREFVKKGQTIELKVIR 549
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 242 VDRDKERVSLGLKQMTDNPWADIERKYPINSQVKGRVTKLLPYGAFVELEKGVEGLVHVSELSWVKRITRPSDVLKLDQE 321
Cdd:PRK12269  550 LDQAEKRINLSLKHFQPDPWLEFENKFGVNDVVKGRVTKIADFGAFIELAEGIEGLAHISEFSWVKKTSKPSDMVKIGDE 629
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 322 IEAVVLSISVKEQKISLGVRQLEDNPWADIESRFPIGTVIKGQVRNLTPYGAFVGLEEGIDGMIHVSDMSWTRKINHPSE 401
Cdd:PRK12269  630 VECMILGYDIQAGRVSLGLKQVTANPWEEIEARYPVGARFTRRIVKVTNAGAFIEMEEGIDGFLHVDDLSWVKRTRPADH 709
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 402 VLKKGDEVEAIVLEIKKEDQRVSLGIKQLESDPWESINDRFKVGDMVSGQVAKIASFGAFVNLDGDIDGLIHISQLSEDH 481
Cdd:PRK12269  710 ELEVGKEIECMVIECDPQARRIRLGVKQLSDNPWQVFANAYGVGSTVEGEVSSVTDFGIFVRVPGGVEGLVRKQHLVENR 789
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1015655940 482 VERVKDVIK---VGDEITARVIKVDSIERRIGLSIKavNYDTEQLRRETASF 530
Cdd:PRK12269  790 DGDPGEALRkyaVGDRVKAVIVDMNVKDRKVAFSVR--DYQRKVQRDELSRY 839
rpsA PRK06676
30S ribosomal protein S1; Reviewed
3-347 6.23e-103

30S ribosomal protein S1; Reviewed


Pssm-ID: 235851 [Multi-domain]  Cd Length: 390  Bit Score: 315.66  E-value: 6.23e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940   3 TTELAELIDSKFRELREGSIVTGTIQEIRPQVVLVDI-GYKSEGAISISEFEDEEIE-------VGDQIEVLLERLENDE 74
Cdd:PRK06676    1 MMEEFEESLNSVKEVEVGDVVTGEVLKVEDKQVFVNIeGYKVEGVIPISELSNDHIEdindvvkVGDELEVYVLKVEDGE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940  75 GIVVLSKEKAAHKQNWDKIVGVYRDGGLVKGKVKSVVKGGLMVNV-GVEAFLPGSQVDIIPPRDLNEYVGKVYEFKIVKV 153
Cdd:PRK06676   81 GNLLLSKRRLEAEKAWDKLEEKFEEGEVVEVKVTEVVKGGLVVDVeGVRGFIPASLISTRFVEDFSDFKGKTLEVKIIEL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 154 NDDRKNIVLSRREVIEAERADQRQRFLETVKEGDKVEGLVKNITDFGAFVDLRGMDGLLHITDMSWGRVNHPSEMLHIGQ 233
Cdd:PRK06676  161 DPEKNRVILSRRAVVEEERAAKKEELLSSLKEGDVVEGTVARLTDFGAFVDIGGVDGLVHISELSHERVEKPSEVVSVGQ 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 234 SLEVVILEVDRDKERVSLGLKQMTDNPWADIERKYPINSQVKGRVTKLLPYGAFVELEKGVEGLVHVSELSWvKRITRPS 313
Cdd:PRK06676  241 EVEVKVLSIDWETERISLSLKDTLPGPWEGVEEKLPEGDVIEGTVKRLTDFGAFVEVLPGVEGLVHISQISH-KHIATPS 319
                         330       340       350
                  ....*....|....*....|....*....|....
gi 1015655940 314 DVLKLDQEIEAVVLSISVKEQKISLGVRQLEDNP 347
Cdd:PRK06676  320 EVLEEGQEVKVKVLEVNEEEKRISLSIKALEEAP 353
rpsA PRK13806
30S ribosomal protein S1; Provisional
5-426 1.73e-94

30S ribosomal protein S1; Provisional


Pssm-ID: 237516 [Multi-domain]  Cd Length: 491  Bit Score: 297.41  E-value: 1.73e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940   5 ELAELIDS----KFRELREGSIVTGTIQEIRPQVVLVDIGYKSEGAISISEFEDEEIE----VGDQIEVLLERLENDEgi 76
Cdd:PRK13806   16 SFAELLEAyegeRKTELRVGDKITGTVIAITEDSVFVDTGSKVDGVVDRAELLDADGEltvaVGDEVELYVVSVNGQE-- 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940  77 VVLSKE----------KAAHKQNW---DKIVGVyRDGGLVKGKvksvvkgglmvnVGVEAFLPGSQVDIIPPRDLNEYVG 143
Cdd:PRK13806   94 IRLSKAlsgqggaamlEEAYENGVpveGKVTGT-CKGGFNVEV------------LGRRAFCPVSQIDLRYVEDPESYVG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 144 KVYEFKIVKVNDDRKNIVLSRREVIEAERADQRQRFLETVKEGDKVEGLVKNITDFGAFVDLR-GMDGLLHITDMSWGRV 222
Cdd:PRK13806  161 QTFQFLITRVEENGRNIVVSRRALLEREQKEALEAFMETVKEGDVVEGTVTRLAPFGAFVELApGVEGMVHISELSWSRV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 223 NHPSEMLHIGQSLEVVILEVDRDKE----RVSLGLKQMTDNPWADIERKYPINSQVKGRVTKLLPYGAFVELEKGVEGLV 298
Cdd:PRK13806  241 QKADEAVSVGDTVRVKVLGIERAKKgkglRISLSIKQAGGDPWDTVGDRLKAGDKVTGKVVRLAPFGAFVEILPGIEGLV 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 299 HVSELSWVKRITRPSDVLKLDQEIEAVVLSISVKEQKISLGVRQLEDNPWADIESRFPIGTVIKGQVRNLTPYGAFVGLE 378
Cdd:PRK13806  321 HVSEMSWTRRVNKPEDVVAPGDAVAVKIKDIDPAKRRISLSLRDAEGDPWADVAERFAPGTTVTGTVEKRAQFGLFVNLA 400
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 1015655940 379 EGIDGMIHVSDMSWTRKiNHPSEVLKKGDEVEAIVLEIKKEDQRVSLG 426
Cdd:PRK13806  401 PGVTGLLPASVISRAGK-PATYEKLKPGDSVTLVVEEIDTAKRKISLA 447
rpsA PRK07899
30S ribosomal protein S1; Reviewed
2-342 2.90e-82

30S ribosomal protein S1; Reviewed


Pssm-ID: 236126 [Multi-domain]  Cd Length: 486  Bit Score: 265.37  E-value: 2.90e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940   2 STTELAELIDSKFRELREGSIVTGTIQEIRPQVVLVDIGYKSEGAISISEFE-------DEEIEVGDQIEVLLERLENDE 74
Cdd:PRK07899   18 SAEDFLAAIDKTIKYFNDGDIVEGTVVKVDRDEVLLDIGYKTEGVIPSRELSikhdvdpNEVVEVGDEVEALVLQKEDKE 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940  75 GIVVLSKEKAAHKQNWDKIVGVYRDGGLVKGKVKSVVKGGLMVNVGVEAFLPGSQVDIIPPRDLNEYVGKVYEFKIVKVN 154
Cdd:PRK07899   98 GRLILSKKRAQYERAWGTIEKIKEKDGVVTGTVIEVVKGGLILDIGLRGFLPASLVEMRRVRDLQPYIGQEIEAKIIELD 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 155 DDRKNIVLSRREVIEAERADQRQRFLETVKEGDKVEGLVKNITDFGAFVDLRGMDGLLHITDMSWGRVNHPSEMLHIGQS 234
Cdd:PRK07899  178 KNRNNVVLSRRAWLEQTQSEVRSEFLNQLQKGQVRKGVVSSIVNFGAFVDLGGVDGLVHVSELSWKHIDHPSEVVEVGQE 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 235 LEVVILEVDRDKERVSLGLKQMTDNPWADIERKYPINSQVKGRVTKLLPYGAFVELEKGVEGLVHVSELSwVKRITRPSD 314
Cdd:PRK07899  258 VTVEVLDVDMDRERVSLSLKATQEDPWQQFARTHAIGQIVPGKVTKLVPFGAFVRVEEGIEGLVHISELA-ERHVEVPEQ 336
                         330       340
                  ....*....|....*....|....*...
gi 1015655940 315 VLKLDQEIEAVVLSISVKEQKISLGVRQ 342
Cdd:PRK07899  337 VVQVGDEVFVKVIDIDLERRRISLSLKQ 364
S1_RPS1_repeat_ec3 cd05688
S1_RPS1_repeat_ec3: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
185-252 6.99e-31

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: 114.65  E-value: 6.99e-31
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1015655940 185 EGDKVEGLVKNITDFGAFVDLRGMDGLLHITDMSWGRVNHPSEMLHIGQSLEVVILEVDRDKERVSLG 252
Cdd:cd05688     1 EGDVVEGTVKSITDFGAFVDLGGVDGLLHISDMSWGRVKHPSEVVNVGDEVEVKVLKIDKERKRISLG 68
S1_RPS1_repeat_ec5 cd05690
S1_RPS1_repeat_ec5: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
358-426 2.64e-27

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: 104.50  E-value: 2.64e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1015655940 358 GTVIKGQVRNLTPYGAFVGLEEGIDGMIHVSDMSWTRKINHPSEVLKKGDEVEAIVLEIKKEDQRVSLG 426
Cdd:cd05690     1 GTVVSGKIKSITDFGIFVGLDGGIDGLVHISDISWTQRVRHPSEIYKKGQEVEAVVLNIDVERERISLG 69
S1_RPS1_repeat_ec3 cd05688
S1_RPS1_repeat_ec3: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
357-426 3.27e-23

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: 93.08  E-value: 3.27e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 357 IGTVIKGQVRNLTPYGAFVGLEeGIDGMIHVSDMSWTRkINHPSEVLKKGDEVEAIVLEIKKEDQRVSLG 426
Cdd:cd05688     1 EGDVVEGTVKSITDFGAFVDLG-GVDGLLHISDMSWGR-VKHPSEVVNVGDEVEVKVLKIDKERKRISLG 68
PRK07400 PRK07400
30S ribosomal protein S1; Reviewed
5-260 7.13e-23

30S ribosomal protein S1; Reviewed


Pssm-ID: 180960 [Multi-domain]  Cd Length: 318  Bit Score: 99.49  E-value: 7.13e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940   5 ELAELIDSKFRELREGSIVTGTIQEIRPQVVLVDIGYKSEGAISISEFE-------DEEIEVGDQIEVLLERLENDEGIV 77
Cdd:PRK07400   17 DFAALLDKYDYHFKPGDIVNGTVFSLEPRGALIDIGAKTAAFMPIQEMSinrvegpEEVLQPNETREFFILSDENEDGQL 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940  78 VLSKEKAAHKQNWDKIVGVYRDGGLVKGKVKSVVKGGLMVNV-GVEAFLPGSQVDIIPPRDlnEYVGKVYEFKIVKVNDD 156
Cdd:PRK07400   97 TLSIRRIEYMRAWERVRQLQKEDATVRSEVFATNRGGALVRIeGLRGFIPGSHISTRKPKE--ELVGEELPLKFLEVDEE 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 157 RKNIVLS-RREVIEaeradqrqRFLETVKEGDKVEGLVKNITDFGAFVDLRGMDGLLHITDMSWGRVNHPSEMLHIGQSL 235
Cdd:PRK07400  175 RNRLVLShRRALVE--------RKMNRLEVGEVVVGTVRGIKPYGAFIDIGGVSGLLHISEISHEHIETPHSVFNVNDEM 246
                         250       260
                  ....*....|....*....|....*
gi 1015655940 236 EVVILEVDRDKERVSLGLKQMTDNP 260
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 ...
355-426 4.28e-21

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: 87.25  E-value: 4.28e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1015655940 355 FPIGTVIKGQVRNLTPYGAFVGLEEGIDGMIHVSDMSWTRKINHPSEVLKKGDEVEAIVLEIKKEDQRVSLG 426
Cdd:cd05689     1 YPEGTRLFGKVTNLTDYGCFVELEEGVEGLVHVSEMDWTNKNIHPSKVVSLGDEVEVMVLDIDEERRRISLG 72
YabR COG1098
Predicted RNA-binding protein, contains ribosomal protein S1 (RPS1) domain [General function ...
442-538 1.08e-20

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


Pssm-ID: 440715 [Multi-domain]  Cd Length: 130  Bit Score: 87.93  E-value: 1.08e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 442 FKVGDMVSGQVAKIASFGAFVNLDGDIDGLIHISQLSEDHVERVKDVIKVGDEITARVIKVDSiERRIGLSIKAVNYDTE 521
Cdd:COG1098     3 IEVGDIVEGKVTGITPFGAFVELPEGTTGLVHISEIADGYVKDINDYLKVGDEVKVKVLSIDE-DGKISLSIKQAEEKPK 81
                          90
                  ....*....|....*..
gi 1015655940 522 QLRRETASFEALRPSSD 538
Cdd:COG1098    82 RPPRPRRNSRPKAGFES 98
PRK11824 PRK11824
polynucleotide phosphorylase/polyadenylase; Provisional
436-516 1.25e-20

polynucleotide phosphorylase/polyadenylase; Provisional


Pssm-ID: 236995 [Multi-domain]  Cd Length: 693  Bit Score: 95.89  E-value: 1.25e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 436 ESINDRFKVGDMVSGQVAKIASFGAFVNLDGDIDGLIHISQLSEDHVERVKDVIKVGDEITARVIKVDSiERRIGLSIKA 515
Cdd:PRK11824  613 EGITAEPEVGEIYEGKVVRIVDFGAFVEILPGKDGLVHISEIADERVEKVEDVLKEGDEVKVKVLEIDK-RGRIRLSRKA 691

                  .
gi 1015655940 516 V 516
Cdd:PRK11824  692 V 692
S1_RPS1_repeat_ec5 cd05690
S1_RPS1_repeat_ec5: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
186-252 8.37e-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: 8.37e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1015655940 186 GDKVEGLVKNITDFGAFVDLR-GMDGLLHITDMSWG-RVNHPSEMLHIGQSLEVVILEVDRDKERVSLG 252
Cdd:cd05690     1 GTVVSGKIKSITDFGIFVGLDgGIDGLVHISDISWTqRVRHPSEIYKKGQEVEAVVLNIDVERERISLG 69
YabR COG1098
Predicted RNA-binding protein, contains ribosomal protein S1 (RPS1) domain [General function ...
267-347 1.69e-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: 84.46  E-value: 1.69e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 267 KYPINSQVKGRVTKLLPYGAFVELEKGVEGLVHVSELS--WVKRItrpSDVLKLDQEIEAVVLSISvKEQKISLGVRQLE 344
Cdd:COG1098     2 SIEVGDIVEGKVTGITPFGAFVELPEGTTGLVHISEIAdgYVKDI---NDYLKVGDEVKVKVLSID-EDGKISLSIKQAE 77

                  ...
gi 1015655940 345 DNP 347
Cdd:COG1098    78 EKP 80
Pnp COG1185
Polyribonucleotide nucleotidyltransferase (polynucleotide phosphorylase) [Translation, ...
443-515 1.98e-19

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


Pssm-ID: 440798 [Multi-domain]  Cd Length: 686  Bit Score: 91.99  E-value: 1.98e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1015655940 443 KVGDMVSGQVAKIASFGAFVNLDGDIDGLIHISQLSEDHVERVKDVIKVGDEITARVIKVDSiERRIGLSIKA 515
Cdd:COG1185   615 EVGEIYEGKVVRIMDFGAFVEILPGKDGLVHISELADERVEKVEDVLKEGDEVKVKVLEIDD-QGRIKLSRKA 686
rpsA PRK07899
30S ribosomal protein S1; Reviewed
295-523 7.84e-19

30S ribosomal protein S1; Reviewed


Pssm-ID: 236126 [Multi-domain]  Cd Length: 486  Bit Score: 89.33  E-value: 7.84e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 295 EGLVHVSELSwVKRITRPSDVLKLDQEIEAVVLSISVKEQKISLGVR--QLEdNPWADIESRFPIGTVIKGQVRNLTPYG 372
Cdd:PRK07899   60 EGVIPSRELS-IKHDVDPNEVVEVGDEVEALVLQKEDKEGRLILSKKraQYE-RAWGTIEKIKEKDGVVTGTVIEVVKGG 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 373 AFVGLeeGIDGMIHVS--DMswtRKINHPSEVLkkGDEVEAIVLEIKKEDQRVSLG----IKQLESDPWESINDRFKVGD 446
Cdd:PRK07899  138 LILDI--GLRGFLPASlvEM---RRVRDLQPYI--GQEIEAKIIELDKNRNNVVLSrrawLEQTQSEVRSEFLNQLQKGQ 210
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1015655940 447 MVSGQVAKIASFGAFVNLDGdIDGLIHISQLSEDHVERVKDVIKVGDEITARVIKVDSIERRIGLSIKAVNYDTEQL 523
Cdd:PRK07899  211 VRKGVVSSIVNFGAFVDLGG-VDGLVHVSELSWKHIDHPSEVVEVGQEVTVEVLDVDMDRERVSLSLKATQEDPWQQ 286
PRK08059 PRK08059
general stress protein 13; Validated
442-516 1.07e-18

general stress protein 13; Validated


Pssm-ID: 181215 [Multi-domain]  Cd Length: 123  Bit Score: 82.02  E-value: 1.07e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1015655940 442 FKVGDMVSGQVAKIASFGAFVNLDGDIDGLIHISQLSEDHVERVKDVIKVGDEITARVIKVDSIERRIGLSIKAV 516
Cdd:PRK08059    5 YEVGSVVTGKVTGIQPYGAFVALDEETQGLVHISEITHGFVKDIHDFLSVGDEVKVKVLSVDEEKGKISLSIRAT 79
S1_dom_CvfD NF040579
CvfD/Ygs/GSP13 family RNA-binding post-transcriptional regulator; CvfD, Ygs, and GSP13 form a ...
442-525 1.79e-18

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: 80.93  E-value: 1.79e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 442 FKVGDMVSGQVAKIASFGAFVNLDGDIDGLIHISQLSEDHVERVKDVIKVGDEITARVIKVDSIERRIGLSIKAVNYDTE 521
Cdd:NF040579    1 YKIGDIVEGKVTGIQPYGAFVALDEHTQGLIHISEIKHGYVKDINDFLKVGQEVKVKVLDIDEYTGKISLSLRALEEAPE 80

                  ....
gi 1015655940 522 QLRR 525
Cdd:NF040579   81 KHRK 84
S1_dom_CvfD NF040579
CvfD/Ygs/GSP13 family RNA-binding post-transcriptional regulator; CvfD, Ygs, and GSP13 form a ...
268-347 5.26e-18

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: 79.78  E-value: 5.26e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 268 YPINSQVKGRVTKLLPYGAFVELEKGVEGLVHVSELS--WVKRItrpSDVLKLDQEIEAVVLSISVKEQKISLGVRQLED 345
Cdd:NF040579    1 YKIGDIVEGKVTGIQPYGAFVALDEHTQGLIHISEIKhgYVKDI---NDFLKVGQEVKVKVLDIDEYTGKISLSLRALEE 77

                  ..
gi 1015655940 346 NP 347
Cdd:NF040579   78 AP 79
S1 smart00316
Ribosomal protein S1-like RNA-binding domain;
443-514 7.57e-18

Ribosomal protein S1-like RNA-binding domain;


Pssm-ID: 197648 [Multi-domain]  Cd Length: 72  Bit Score: 78.03  E-value: 7.57e-18
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1015655940  443 KVGDMVSGQVAKIASFGAFVNLDGDIDGLIHISQLSEDHVERVKDVIKVGDEITARVIKVDSIERRIGLSIK 514
Cdd:smart00316   1 EVGDVVEGTVTEITPGGAFVDLGNGVEGLIPISELSDKRVKDPEEVLKVGDEVKVKVLSVDEEKGRIILSLK 72
S1 smart00316
Ribosomal protein S1-like RNA-binding domain;
184-254 7.72e-18

Ribosomal protein S1-like RNA-binding domain;


Pssm-ID: 197648 [Multi-domain]  Cd Length: 72  Bit Score: 78.03  E-value: 7.72e-18
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1015655940  184 KEGDKVEGLVKNITDFGAFVDL-RGMDGLLHITDMSWGRVNHPSEMLHIGQSLEVVILEVDRDKERVSLGLK 254
Cdd:smart00316   1 EVGDVVEGTVTEITPGGAFVDLgNGVEGLIPISELSDKRVKDPEEVLKVGDEVKVKVLSVDEEKGRIILSLK 72
PRK07400 PRK07400
30S ribosomal protein S1; Reviewed
274-516 8.09e-18

30S ribosomal protein S1; Reviewed


Pssm-ID: 180960 [Multi-domain]  Cd Length: 318  Bit Score: 84.47  E-value: 8.09e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 274 VKGRVTKLLPYGAFVELEKGVEGLVHVSELSwVKRITRPSDVLKLDQEIEAVVLSISVKEQKISLGVRQLE-DNPWADIE 352
Cdd:PRK07400   35 VNGTVFSLEPRGALIDIGAKTAAFMPIQEMS-INRVEGPEEVLQPNETREFFILSDENEDGQLTLSIRRIEyMRAWERVR 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 353 SRFPIGTVIKGQVRNLTPYGAFVGLEeGIDGMIHVSDMSwTRKinhPSEVLKkGDEVEAIVLEIKKEDQRVSLGIKQLES 432
Cdd:PRK07400  114 QLQKEDATVRSEVFATNRGGALVRIE-GLRGFIPGSHIS-TRK---PKEELV-GEELPLKFLEVDEERNRLVLSHRRALV 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 433 dpwESINDRFKVGDMVSGQVAKIASFGAFVNLDGdIDGLIHISQLSEDHVERVKDVIKVGDEITARVIKVDSIERRIGLS 512
Cdd:PRK07400  188 ---ERKMNRLEVGEVVVGTVRGIKPYGAFIDIGG-VSGLLHISEISHEHIETPHSVFNVNDEMKVMIIDLDAERGRISLS 263

                  ....
gi 1015655940 513 IKAV 516
Cdd:PRK07400  264 TKQL 267
S1_RPS1_repeat_ec5 cd05690
S1_RPS1_repeat_ec5: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
274-339 1.55e-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: 77.15  E-value: 1.55e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1015655940 274 VKGRVTKLLPYGAFVELEKGVEGLVHVSELSWVKRITRPSDVLKLDQEIEAVVLSISVKEQKISLG 339
Cdd:cd05690     4 VSGKIKSITDFGIFVGLDGGIDGLVHISDISWTQRVRHPSEIYKKGQEVEAVVLNIDVERERISLG 69
S1_RPS1_repeat_ec4 cd05689
S1_RPS1_repeat_ec4: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
268-339 1.80e-17

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: 76.85  E-value: 1.80e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1015655940 268 YPINSQVKGRVTKLLPYGAFVELEKGVEGLVHVSELSWVKRITRPSDVLKLDQEIEAVVLSISVKEQKISLG 339
Cdd:cd05689     1 YPEGTRLFGKVTNLTDYGCFVELEEGVEGLVHVSEMDWTNKNIHPSKVVSLGDEVEVMVLDIDEERRRISLG 72
S1_RPS1_repeat_ec3 cd05688
S1_RPS1_repeat_ec3: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
444-512 5.03e-17

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: 75.36  E-value: 5.03e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1015655940 444 VGDMVSGQVAKIASFGAFVNLdGDIDGLIHISQLSEDHVERVKDVIKVGDEITARVIKVDSIERRIGLS 512
Cdd:cd05688     1 EGDVVEGTVKSITDFGAFVDL-GGVDGLLHISDMSWGRVKHPSEVVNVGDEVEVKVLKIDKERKRISLG 68
Tex COG2183
Transcriptional accessory protein Tex/SPT6 [Transcription];
180-255 5.71e-17

Transcriptional accessory protein Tex/SPT6 [Transcription];


Pssm-ID: 441786 [Multi-domain]  Cd Length: 719  Bit Score: 84.31  E-value: 5.71e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1015655940 180 LETVKEGDKVEGLVKNITDFGAFVDLrGM--DGLLHITDMSWGRVNHPSEMLHIGQSLEVVILEVDRDKERVSLGLKQ 255
Cdd:COG2183   636 IEDLKPGMILEGTVTNVTDFGAFVDI-GVhqDGLVHISQLSDRFVKDPREVVKVGDIVKVKVLEVDLKRKRISLSMKL 712
S1_PNPase cd04472
S1_PNPase: Polynucleotide phosphorylase (PNPase), ), S1-like RNA-binding domain. PNPase is a ...
445-513 6.30e-17

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: 75.27  E-value: 6.30e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1015655940 445 GDMVSGQVAKIASFGAFVNLDGDIDGLIHISQLSEDHVERVKDVIKVGDEITARVIKVDSiERRIGLSI 513
Cdd:cd04472     1 GKIYEGKVVKIKDFGAFVEILPGKDGLVHISELSDERVEKVEDVLKVGDEVKVKVIEVDD-RGRISLSR 68
PRK07400 PRK07400
30S ribosomal protein S1; Reviewed
184-454 6.54e-17

30S ribosomal protein S1; Reviewed


Pssm-ID: 180960 [Multi-domain]  Cd Length: 318  Bit Score: 81.77  E-value: 6.54e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 184 KEGDKVEGLVKNITDFGAFVDLRGMDG-LLHITDMSWGRVNHPSEMLHIGQSLEVVILEVDRDKERVSLGLKQMT-DNPW 261
Cdd:PRK07400   30 KPGDIVNGTVFSLEPRGALIDIGAKTAaFMPIQEMSINRVEGPEEVLQPNETREFFILSDENEDGQLTLSIRRIEyMRAW 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 262 ADIERKYPINSQVKGRVTKLLPYGAFVELEkGVEGLVHVSELSwvkriTR-----------PSDVLKLDQEIEAVVLSis 330
Cdd:PRK07400  110 ERVRQLQKEDATVRSEVFATNRGGALVRIE-GLRGFIPGSHIS-----TRkpkeelvgeelPLKFLEVDEERNRLVLS-- 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 331 vkeQKISLGVRQLednpwadieSRFPIGTVIKGQVRNLTPYGAFVGLEeGIDGMIHVSDMSwTRKINHPSEVLKKGDEVE 410
Cdd:PRK07400  182 ---HRRALVERKM---------NRLEVGEVVVGTVRGIKPYGAFIDIG-GVSGLLHISEIS-HEHIETPHSVFNVNDEMK 247
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1015655940 411 AIVLEIKKEDQRVSLGIKQLESDPWESINDRFKVGDMVSGQVAK 454
Cdd:PRK07400  248 VMIIDLDAERGRISLSTKQLEPEPGDMLKDPQKVFDKAEEMAAK 291
S1_RPS1_repeat_hs4 cd05692
S1_RPS1_repeat_hs4: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
445-514 7.27e-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: 75.01  E-value: 7.27e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 445 GDMVSGQVAKIASFGAFVNLDGDIDGLIHISQLSEDHVERVKDVIKVGDEITARVIKVDSiERRIGLSIK 514
Cdd:cd05692     1 GSVVEGTVTRLKPFGAFVELGGGISGLVHISQIAHKRVKDVKDVLKEGDKVKVKVLSIDA-RGRISLSIK 69
S1 smart00316
Ribosomal protein S1-like RNA-binding domain;
357-428 2.01e-16

Ribosomal protein S1-like RNA-binding domain;


Pssm-ID: 197648 [Multi-domain]  Cd Length: 72  Bit Score: 73.79  E-value: 2.01e-16
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1015655940  357 IGTVIKGQVRNLTPYGAFVGLEEGIDGMIHVSDMSWtRKINHPSEVLKKGDEVEAIVLEIKKEDQRVSLGIK 428
Cdd:smart00316   2 VGDVVEGTVTEITPGGAFVDLGNGVEGLIPISELSD-KRVKDPEEVLKVGDEVKVKVLSVDEEKGRIILSLK 72
S1_Tex cd05685
S1_Tex: The C-terminal S1 domain of a transcription accessory factor called Tex, which has ...
186-251 5.42e-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: 72.65  E-value: 5.42e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1015655940 186 GDKVEGLVKNITDFGAFVDLR-GMDGLLHITDMSWGRVNHPSEMLHIGQSLEVVILEVDRDKERVSL 251
Cdd:cd05685     1 GMVLEGVVTNVTDFGAFVDIGvKQDGLIHISKMADRFVSHPSDVVSVGDIVEVKVISIDEERGRISL 67
YabR COG1098
Predicted RNA-binding protein, contains ribosomal protein S1 (RPS1) domain [General function ...
357-434 6.65e-16

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


Pssm-ID: 440715 [Multi-domain]  Cd Length: 130  Bit Score: 74.45  E-value: 6.65e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 357 IGTVIKGQVRNLTPYGAFVGLEEGIDGMIHVSDMS--WTRKINhpsEVLKKGDEVEAIVLEIkKEDQRVSLGIKQLESDP 434
Cdd:COG1098     5 VGDIVEGKVTGITPFGAFVELPEGTTGLVHISEIAdgYVKDIN---DYLKVGDEVKVKVLSI-DEDGKISLSIKQAEEKP 80
rpsA TIGR00717
ribosomal protein S1; This model describes ribosomal protein S1, RpsA. This protein is found ...
274-519 1.16e-15

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: 79.78  E-value: 1.16e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 274 VKGRVTKLLPYGAFVELEKGVEGLVHVSElswvkrITRPSDVLKLDQEIEAVVLSISVKEQKISLGV-RQLEDNPWADIE 352
Cdd:TIGR00717  22 VKGTVVAINKDTVFVDVGLKSEGRIPKEE------FLDAPLEIQVGDEVEVYLDRVEDRFGETVLSReKAQRHELWIKLE 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 353 SRFPIGTVIKGQVRNLTPYGAFVGLEeGIDGMIHVSDMSwTRKINHPSEVLkkGDEVEAIVLEIKKEDQRVSLGIKQL-- 430
Cdd:TIGR00717  96 KAYEEGSIVEGKIVGKVKGGFIVDLN-GVEAFLPGSQVD-VKPIKDLDSLI--GKTLKFKIIKLDQKRNNIVVSRRAYle 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 431 --ESDPWESINDRFKVGDMVSGQVAKIASFGAFVNLDGdIDGLIHISQLSEDHVERVKDVIKVGDEITARVIKVDSIERR 508
Cdd:TIGR00717 172 eeRSQAREELLENLKEGDVVKGVVKNITDFGAFVDLGG-VDGLLHITDMSWKRVKHPSEYVKVGQEVKVKVIKFDKEKGR 250
                         250
                  ....*....|.
gi 1015655940 509 IGLSIKAVNYD 519
Cdd:TIGR00717 251 ISLSLKQLGED 261
S1_RPS1_repeat_ec3 cd05688
S1_RPS1_repeat_ec3: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
274-339 1.64e-15

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: 71.12  E-value: 1.64e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1015655940 274 VKGRVTKLLPYGAFVELeKGVEGLVHVSELSWvKRITRPSDVLKLDQEIEAVVLSISVKEQKISLG 339
Cdd:cd05688     5 VEGTVKSITDFGAFVDL-GGVDGLLHISDMSW-GRVKHPSEVVNVGDEVEVKVLKIDKERKRISLG 68
S1_RPS1_repeat_ec1_hs1 cd05687
S1_RPS1_repeat_ec1_hs1: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
20-82 1.71e-15

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: 71.02  E-value: 1.71e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940  20 GSIVTGTIQEIRPQVVLVDIGYKSEGAISISEFEDEEIE-------VGDQIEVLLERLENDEGIVVLSKE 82
Cdd:cd05687     1 GDIVKGTVVSVDDDEVLVDIGYKSEGIIPISEFSDDPIEngedevkVGDEVEVYVLRVEDEEGNVVLSKR 70
S1_RPS1_repeat_ec2_hs2 cd04465
S1_RPS1_repeat_ec2_hs2: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
120-165 2.11e-15

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: 70.95  E-value: 2.11e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1015655940 120 GVEAFLPGSQVDIIPPRDLNEYVGKVYEFKIVKVNDDRKNIVLSRR 165
Cdd:cd04465    22 GVRAFLPASQVDLRPVEDLDEYVGKELKFKIIEIDRERNNIVLSRR 67
S1 pfam00575
S1 RNA binding domain; The S1 domain occurs in a wide range of RNA associated proteins. It is ...
442-513 2.21e-15

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


Pssm-ID: 425760 [Multi-domain]  Cd Length: 72  Bit Score: 70.78  E-value: 2.21e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1015655940 442 FKVGDMVSGQVAKIASFGAFVNLDGDIDGLIHISQLSEDHVERVKDVIKVGDEITARVIKVDSIERRIGLSI 513
Cdd:pfam00575   1 PEKGDVVEGEVTRVTKGGAFVDLGNGVEGFIPISELSDDHVEDPDEVIKVGDEVKVKVLKVDKDRRRIILSI 72
S1 smart00316
Ribosomal protein S1-like RNA-binding domain;
270-341 2.87e-15

Ribosomal protein S1-like RNA-binding domain;


Pssm-ID: 197648 [Multi-domain]  Cd Length: 72  Bit Score: 70.71  E-value: 2.87e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1015655940  270 INSQVKGRVTKLLPYGAFVELEKGVEGLVHVSELSWvKRITRPSDVLKLDQEIEAVVLSISVKEQKISLGVR 341
Cdd:smart00316   2 VGDVVEGTVTEITPGGAFVDLGNGVEGLIPISELSD-KRVKDPEEVLKVGDEVKVKVLSVDEEKGRIILSLK 72
Pnp COG1185
Polyribonucleotide nucleotidyltransferase (polynucleotide phosphorylase) [Translation, ...
181-254 3.27e-15

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


Pssm-ID: 440798 [Multi-domain]  Cd Length: 686  Bit Score: 78.89  E-value: 3.27e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1015655940 181 ETVKEGDKVEGLVKNITDFGAFVD-LRGMDGLLHITDMSWGRVNHPSEMLHIGQSLEVVILEVDrDKERVSLGLK 254
Cdd:COG1185   612 AEPEVGEIYEGKVVRIMDFGAFVEiLPGKDGLVHISELADERVEKVEDVLKEGDEVKVKVLEID-DQGRIKLSRK 685
PRK08582 PRK08582
RNA-binding protein S1;
444-514 3.47e-15

RNA-binding protein S1;


Pssm-ID: 236305 [Multi-domain]  Cd Length: 139  Bit Score: 72.76  E-value: 3.47e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1015655940 444 VGDMVSGQVAKIASFGAFVNLDGDIDGLIHISQLSEDHVERVKDVIKVGDEITARVIKVDSiERRIGLSIK 514
Cdd:PRK08582    5 VGSKLQGKVTGITNFGAFVELPEGKTGLVHISEVADNYVKDINDHLKVGDEVEVKVLNVED-DGKIGLSIK 74
Tex COG2183
Transcriptional accessory protein Tex/SPT6 [Transcription];
436-516 5.75e-15

Transcriptional accessory protein Tex/SPT6 [Transcription];


Pssm-ID: 441786 [Multi-domain]  Cd Length: 719  Bit Score: 78.14  E-value: 5.75e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 436 ESINDrFKVGDMVSGQVAKIASFGAFVnldgDI----DGLIHISQLSEDHVERVKDVIKVGDEITARVIKVDsIER-RIG 510
Cdd:COG2183   634 LKIED-LKPGMILEGTVTNVTDFGAFV----DIgvhqDGLVHISQLSDRFVKDPREVVKVGDIVKVKVLEVD-LKRkRIS 707

                  ....*.
gi 1015655940 511 LSIKAV 516
Cdd:COG2183   708 LSMKLD 713
S1_Rrp5_repeat_sc12 cd05708
S1_Rrp5_repeat_sc12: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ...
443-515 7.25e-15

S1_Rrp5_repeat_sc12: Rrp5 is a trans-acting factor important for biogenesis of both the 40S and 60S eukaryotic ribosomal subunits. Rrp5 has two distinct regions, an N-terminal region containing tandemly repeated S1 RNA-binding domains (12 S1 repeats in Saccharomyces cerevisiae Rrp5 and 14 S1 repeats in Homo sapiens Rrp5) and a C-terminal region containing tetratricopeptide repeat (TPR) motifs thought to be involved in protein-protein interactions. Mutational studies have shown that each region represents a specific functional domain. Deletions within the S1-containing region inhibit pre-rRNA processing at either site A3 or A2, whereas deletions within the TPR region confer an inability to support cleavage of A0-A2. This CD includes S. cerevisiae S1 repeat 12 (sc12). Rrp5 is found in eukaryotes but not in prokaryotes or archaea.


Pssm-ID: 240213 [Multi-domain]  Cd Length: 77  Bit Score: 69.67  E-value: 7.25e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1015655940 443 KVGDMVSGQVAKIASFGAFVNLDG-DIDGLIHISQLSEDHVERVKDVIKVGDEITARVIKVDSIERRIGLSIKA 515
Cdd:cd05708     1 KVGQKIDGTVRRVEDYGVFIDIDGtNVSGLCHKSEISDNRVADASKLFRVGDKVRAKVLKIDAEKKRISLGLKA 74
S1_like cd00164
S1_like: Ribosomal protein S1-like RNA-binding domain. Found in a wide variety of ...
361-426 7.88e-15

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: 69.33  E-value: 7.88e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1015655940 361 IKGQVRNLTPYGAFVGLEEGIDGMIHVSDMSWTRKiNHPSEVLKKGDEVEAIVLEIKKEDQRVSLG 426
Cdd:cd00164     1 VTGKVVSITKFGVFVELEDGVEGLVHISELSDKFV-KDPSEVFKVGDEVEVKVLEVDPEKGRISLS 65
S1_DHX8_helicase cd05684
S1_DHX8_helicase: The N-terminal S1 domain of human ATP-dependent RNA helicase DHX8, a DEAH ...
275-341 8.31e-15

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: 69.58  E-value: 8.31e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 275 KGRVTKLLPYGAFVELE---KGVEGLVHVSELSWVKRITRPSDVLKLDQEIEAVVlsISVKEQKISLGVR 341
Cdd:cd05684     5 KGKVTSIMDFGCFVQLEglkGRKEGLVHISQLSFEGRVANPSDVVKRGQKVKVKV--ISIQNGKISLSMK 72
PRK08059 PRK08059
general stress protein 13; Validated
267-349 9.89e-15

general stress protein 13; Validated


Pssm-ID: 181215 [Multi-domain]  Cd Length: 123  Bit Score: 70.85  E-value: 9.89e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 267 KYPINSQVKGRVTKLLPYGAFVELEKGVEGLVHVSELS--WVKRItrpSDVLKLDQEIEAVVLSISVKEQKISLGVRQLE 344
Cdd:PRK08059    4 QYEVGSVVTGKVTGIQPYGAFVALDEETQGLVHISEIThgFVKDI---HDFLSVGDEVKVKVLSVDEEKGKISLSIRATE 80

                  ....*
gi 1015655940 345 DNPWA 349
Cdd:PRK08059   81 EAPEA 85
PRK11824 PRK11824
polynucleotide phosphorylase/polyadenylase; Provisional
183-254 1.27e-14

polynucleotide phosphorylase/polyadenylase; Provisional


Pssm-ID: 236995 [Multi-domain]  Cd Length: 693  Bit Score: 77.01  E-value: 1.27e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1015655940 183 VKEGDKVEGLVKNITDFGAFVD-LRGMDGLLHITDMSWGRVNHPSEMLHIGQSLEVVILEVDrDKERVSLGLK 254
Cdd:PRK11824  619 PEVGEIYEGKVVRIVDFGAFVEiLPGKDGLVHISEIADERVEKVEDVLKEGDEVKVKVLEID-KRGRIRLSRK 690
YabR COG1098
Predicted RNA-binding protein, contains ribosomal protein S1 (RPS1) domain [General function ...
181-260 1.54e-14

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


Pssm-ID: 440715 [Multi-domain]  Cd Length: 130  Bit Score: 70.59  E-value: 1.54e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 181 ETVKEGDKVEGLVKNITDFGAFVDLR-GMDGLLHITDMSWGRVNHPSEMLHIGQSLEVVILEVDRDKeRVSLGLKQMTDN 259
Cdd:COG1098     1 MSIEVGDIVEGKVTGITPFGAFVELPeGTTGLVHISEIADGYVKDINDYLKVGDEVKVKVLSIDEDG-KISLSIKQAEEK 79

                  .
gi 1015655940 260 P 260
Cdd:COG1098    80 P 80
S1_Tex cd05685
S1_Tex: The C-terminal S1 domain of a transcription accessory factor called Tex, which has ...
358-425 1.58e-14

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: 68.41  E-value: 1.58e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1015655940 358 GTVIKGQVRNLTPYGAFVGLEEGIDGMIHVSDMSwTRKINHPSEVLKKGDEVEAIVLEIKKEDQRVSL 425
Cdd:cd05685     1 GMVLEGVVTNVTDFGAFVDIGVKQDGLIHISKMA-DRFVSHPSDVVSVGDIVEVKVISIDEERGRISL 67
S1_Rrp5_repeat_sc12 cd05708
S1_Rrp5_repeat_sc12: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ...
184-254 1.92e-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: 1.92e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1015655940 184 KEGDKVEGLVKNITDFGAFVDLRGMD--GLLHITDMSWGRVNHPSEMLHIGQSLEVVILEVDRDKERVSLGLK 254
Cdd:cd05708     1 KVGQKIDGTVRRVEDYGVFIDIDGTNvsGLCHKSEISDNRVADASKLFRVGDKVRAKVLKIDAEKKRISLGLK 73
S1_RPS1_repeat_ec4 cd05689
S1_RPS1_repeat_ec4: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
185-252 2.07e-14

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: 68.37  E-value: 2.07e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 185 EGDKVEGLVKNITDFGAFVDLR-GMDGLLHITDMSWGRVN-HPSEMLHIGQSLEVVILEVDRDKERVSLG 252
Cdd:cd05689     3 EGTRLFGKVTNLTDYGCFVELEeGVEGLVHVSEMDWTNKNiHPSKVVSLGDEVEVMVLDIDEERRRISLG 72
S1_like cd00164
S1_like: Ribosomal protein S1-like RNA-binding domain. Found in a wide variety of ...
189-252 2.44e-14

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: 67.79  E-value: 2.44e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1015655940 189 VEGLVKNITDFGAFVDL-RGMDGLLHITDMSWGRVNHPSEMLHIGQSLEVVILEVDRDKERVSLG 252
Cdd:cd00164     1 VTGKVVSITKFGVFVELeDGVEGLVHISELSDKFVKDPSEVFKVGDEVEVKVLEVDPEKGRISLS 65
Pnp COG1185
Polyribonucleotide nucleotidyltransferase (polynucleotide phosphorylase) [Translation, ...
275-338 3.42e-14

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


Pssm-ID: 440798 [Multi-domain]  Cd Length: 686  Bit Score: 75.43  E-value: 3.42e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1015655940 275 KGRVTKLLPYGAFVELEKGVEGLVHVSELSWvKRITRPSDVLKLDQEIEAVVLSISvKEQKISL 338
Cdd:COG1185   621 EGKVVRIMDFGAFVEILPGKDGLVHISELAD-ERVEKVEDVLKEGDEVKVKVLEID-DQGRIKL 682
S1_RPS1_repeat_hs4 cd05692
S1_RPS1_repeat_hs4: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
358-428 3.67e-14

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


Pssm-ID: 240197 [Multi-domain]  Cd Length: 69  Bit Score: 67.31  E-value: 3.67e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1015655940 358 GTVIKGQVRNLTPYGAFVGLEEGIDGMIHVSDMSWTRkINHPSEVLKKGDEVEAIVLEIkKEDQRVSLGIK 428
Cdd:cd05692     1 GSVVEGTVTRLKPFGAFVELGGGISGLVHISQIAHKR-VKDVKDVLKEGDKVKVKVLSI-DARGRISLSIK 69
rpsA PRK13806
30S ribosomal protein S1; Provisional
443-519 4.17e-14

30S ribosomal protein S1; Provisional


Pssm-ID: 237516 [Multi-domain]  Cd Length: 491  Bit Score: 74.76  E-value: 4.17e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 443 KVGDMVSGQVAKIASFGAFVNLDGDIDGLIHISQLSEDHVERVKDVIKVGDEITARVIKVDSIER----RIGLSIKAVNY 518
Cdd:PRK13806  201 KEGDVVEGTVTRLAPFGAFVELAPGVEGMVHISELSWSRVQKADEAVSVGDTVRVKVLGIERAKKgkglRISLSIKQAGG 280

                  .
gi 1015655940 519 D 519
Cdd:PRK13806  281 D 281
PRK11824 PRK11824
polynucleotide phosphorylase/polyadenylase; Provisional
275-344 4.34e-14

polynucleotide phosphorylase/polyadenylase; Provisional


Pssm-ID: 236995 [Multi-domain]  Cd Length: 693  Bit Score: 75.09  E-value: 4.34e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 275 KGRVTKLLPYGAFVELEKGVEGLVHVSELSWvKRITRPSDVLKLDQEIEAVVLSISvKEQKISLGVRQLE 344
Cdd:PRK11824  626 EGKVVRIVDFGAFVEILPGKDGLVHISEIAD-ERVEKVEDVLKEGDEVKVKVLEID-KRGRIRLSRKAVL 693
S1_like cd00164
S1_like: Ribosomal protein S1-like RNA-binding domain. Found in a wide variety of ...
274-339 6.00e-14

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: 66.64  E-value: 6.00e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1015655940 274 VKGRVTKLLPYGAFVELEKGVEGLVHVSELSWvKRITRPSDVLKLDQEIEAVVLSISVKEQKISLG 339
Cdd:cd00164     1 VTGKVVSITKFGVFVELEDGVEGLVHISELSD-KFVKDPSEVFKVGDEVEVKVLEVDPEKGRISLS 65
S1_Tex cd05685
S1_Tex: The C-terminal S1 domain of a transcription accessory factor called Tex, which has ...
445-512 6.33e-14

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: 66.49  E-value: 6.33e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1015655940 445 GDMVSGQVAKIASFGAFVNLDGDIDGLIHISQLSEDHVERVKDVIKVGDEITARVIKVDSIERRIGLS 512
Cdd:cd05685     1 GMVLEGVVTNVTDFGAFVDIGVKQDGLIHISKMADRFVSHPSDVVSVGDIVEVKVISIDEERGRISLS 68
S1_DHX8_helicase cd05684
S1_DHX8_helicase: The N-terminal S1 domain of human ATP-dependent RNA helicase DHX8, a DEAH ...
358-428 9.70e-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: 66.49  E-value: 9.70e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1015655940 358 GTVIKGQVRNLTPYGAFV---GLEEGIDGMIHVSDMSWTRKINHPSEVLKKGDEVEAIVLEIKKedQRVSLGIK 428
Cdd:cd05684     1 GKIYKGKVTSIMDFGCFVqleGLKGRKEGLVHISQLSFEGRVANPSDVVKRGQKVKVKVISIQN--GKISLSMK 72
S1 pfam00575
S1 RNA binding domain; The S1 domain occurs in a wide range of RNA associated proteins. It is ...
183-253 1.55e-13

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: 65.77  E-value: 1.55e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1015655940 183 VKEGDKVEGLVKNITDFGAFVDL-RGMDGLLHITDMSWGRVNHPSEMLHIGQSLEVVILEVDRDKERVSLGL 253
Cdd:pfam00575   1 PEKGDVVEGEVTRVTKGGAFVDLgNGVEGFIPISELSDDHVEDPDEVIKVGDEVKVKVLKVDKDRRRIILSI 72
S1_RPS1_repeat_hs4 cd05692
S1_RPS1_repeat_hs4: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
272-341 2.14e-13

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: 65.00  E-value: 2.14e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 272 SQVKGRVTKLLPYGAFVELEKGVEGLVHVSELSWvKRITRPSDVLKLDQEIEAVVLSISvKEQKISLGVR 341
Cdd:cd05692     2 SVVEGTVTRLKPFGAFVELGGGISGLVHISQIAH-KRVKDVKDVLKEGDKVKVKVLSID-ARGRISLSIK 69
S1_RPS1_repeat_ec5 cd05690
S1_RPS1_repeat_ec5: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
445-511 2.44e-13

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: 65.21  E-value: 2.44e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1015655940 445 GDMVSGQVAKIASFGAFVNLDGDIDGLIHISQLS-EDHVERVKDVIKVGDEITARVIKVDSIERRIGL 511
Cdd:cd05690     1 GTVVSGKIKSITDFGIFVGLDGGIDGLVHISDISwTQRVRHPSEIYKKGQEVEAVVLNIDVERERISL 68
PRK08059 PRK08059
general stress protein 13; Validated
353-436 3.04e-13

general stress protein 13; Validated


Pssm-ID: 181215 [Multi-domain]  Cd Length: 123  Bit Score: 66.61  E-value: 3.04e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 353 SRFPIGTVIKGQVRNLTPYGAFVGLEEGIDGMIHVSDMS--WTRKINhpsEVLKKGDEVEAIVLEIKKEDQRVSLGIKQL 430
Cdd:PRK08059    3 SQYEVGSVVTGKVTGIQPYGAFVALDEETQGLVHISEIThgFVKDIH---DFLSVGDEVKVKVLSVDEEKGKISLSIRAT 79

                  ....*.
gi 1015655940 431 ESDPWE 436
Cdd:PRK08059   80 EEAPEA 85
S1 pfam00575
S1 RNA binding domain; The S1 domain occurs in a wide range of RNA associated proteins. It is ...
355-427 4.17e-13

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: 64.62  E-value: 4.17e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1015655940 355 FPIGTVIKGQVRNLTPYGAFVGLEEGIDGMIHVSDMSWtRKINHPSEVLKKGDEVEAIVLEIKKEDQRVSLGI 427
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 ...
357-434 4.79e-13

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: 65.53  E-value: 4.79e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 357 IGTVIKGQVRNLTPYGAFVGLEEGIDGMIHVSDMS--WTRKINhpsEVLKKGDEVEAIVLEIKKEDQRVSLGIKQLESDP 434
Cdd:NF040579    3 IGDIVEGKVTGIQPYGAFVALDEHTQGLIHISEIKhgYVKDIN---DFLKVGQEVKVKVLDIDEYTGKISLSLRALEEAP 79
S1_like cd00164
S1_like: Ribosomal protein S1-like RNA-binding domain. Found in a wide variety of ...
448-512 5.66e-13

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: 63.94  E-value: 5.66e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1015655940 448 VSGQVAKIASFGAFVNLDGDIDGLIHISQLSEDHVERVKDVIKVGDEITARVIKVDSIERRIGLS 512
Cdd:cd00164     1 VTGKVVSITKFGVFVELEDGVEGLVHISELSDKFVKDPSEVFKVGDEVEVKVLEVDPEKGRISLS 65
S1_RPS1_repeat_hs4 cd05692
S1_RPS1_repeat_hs4: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
186-254 6.15e-13

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: 63.84  E-value: 6.15e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 186 GDKVEGLVKNITDFGAFVDL-RGMDGLLHITDMSWGRVNHPSEMLHIGQSLEVVILEVDrDKERVSLGLK 254
Cdd:cd05692     1 GSVVEGTVTRLKPFGAFVELgGGISGLVHISQIAHKRVKDVKDVLKEGDKVKVKVLSID-ARGRISLSIK 69
S1_IF2_alpha cd04452
S1_IF2_alpha: The alpha subunit of translation Initiation Factor 2, S1-like RNA-binding domain. ...
443-514 7.50e-13

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: 63.76  E-value: 7.50e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1015655940 443 KVGDMVSGQVAKIASFGAFVNLD--GDIDGLIHISQLSEDHVERVKDVIKVGDEITARVIKVDSIERRIGLSIK 514
Cdd:cd04452     2 EEGELVVVTVKSIADMGAYVSLLeyGNIEGMILLSELSRRRIRSIRKLVKVGRKEVVKVIRVDKEKGYIDLSKK 75
S1_DHX8_helicase cd05684
S1_DHX8_helicase: The N-terminal S1 domain of human ATP-dependent RNA helicase DHX8, a DEAH ...
445-520 1.04e-12

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: 63.41  E-value: 1.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 445 GDMVSGQVAKIASFGAFVNLDG---DIDGLIHISQLSEDHVER-VKDVIKVGDEITARVIKVDSieRRIGLSIKAVNYDT 520
Cdd:cd05684     1 GKIYKGKVTSIMDFGCFVQLEGlkgRKEGLVHISQLSFEGRVAnPSDVVKRGQKVKVKVISIQN--GKISLSMKDVDQDT 78
PRK03987 PRK03987
translation initiation factor IF-2 subunit alpha; Validated
444-527 1.41e-12

translation initiation factor IF-2 subunit alpha; Validated


Pssm-ID: 235188 [Multi-domain]  Cd Length: 262  Bit Score: 67.93  E-value: 1.41e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 444 VGDMVSGQVAKIASFGAFVNLD--GDIDGLIHISQLSEDHVERVKDVIKVGDEITARVIKVDSIERRIGLSIKAVNydtE 521
Cdd:PRK03987    8 EGELVVGTVKEVKDFGAFVTLDeyPGKEGFIHISEVASGWVKNIRDHVKEGQKVVCKVIRVDPRKGHIDLSLKRVN---E 84

                  ....*.
gi 1015655940 522 QLRRET 527
Cdd:PRK03987   85 HQRREK 90
PRK11824 PRK11824
polynucleotide phosphorylase/polyadenylase; Provisional
357-431 1.52e-12

polynucleotide phosphorylase/polyadenylase; Provisional


Pssm-ID: 236995 [Multi-domain]  Cd Length: 693  Bit Score: 70.46  E-value: 1.52e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1015655940 357 IGTVIKGQVRNLTPYGAFVGLEEGIDGMIHVSDMSWTRkINHPSEVLKKGDEVEAIVLEIKKEDqRVSLGIKQLE 431
Cdd:PRK11824  621 VGEIYEGKVVRIVDFGAFVEILPGKDGLVHISEIADER-VEKVEDVLKEGDEVKVKVLEIDKRG-RIRLSRKAVL 693
S1_Rrp5_repeat_hs8_sc7 cd04461
S1_Rrp5_repeat_hs8_sc7: Rrp5 Homo sapiens S1 repeat 8 (hs8) and Saccharomyces cerevisiae S1 ...
180-253 1.89e-12

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: 62.99  E-value: 1.89e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1015655940 180 LETVKEGDKVEGLVKNITDFGAFVD-LRGMDGLLHITDMSWGRVNHPSEMLHIGQSLEVVILEVDRDKERVSLGL 253
Cdd:cd04461     9 FSDLKPGMVVHGYVRNITPYGVFVEfLGGLTGLAPKSYISDEFVTDPSFGFKKGQSVTAKVTSVDEEKQRFLLSL 83
PRK05807 PRK05807
RNA-binding protein S1;
442-524 1.91e-12

RNA-binding protein S1;


Pssm-ID: 235614 [Multi-domain]  Cd Length: 136  Bit Score: 64.77  E-value: 1.91e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 442 FKVGDMVSGQVAKIASFGAFVNLDGDIdGLIHISQLSEDHVERVKDVIKVGDEITARVIKVDSiERRIGLSIKAVNYDTE 521
Cdd:PRK05807    3 LKAGSILEGTVVNITNFGAFVEVEGKT-GLVHISEVADTYVKDIREHLKEQDKVKVKVISIDD-NGKISLSIKQAMKQKK 80

                  ...
gi 1015655940 522 QLR 524
Cdd:PRK05807   81 SVK 83
S1_PNPase cd04472
S1_PNPase: Polynucleotide phosphorylase (PNPase), ), S1-like RNA-binding domain. PNPase is a ...
275-338 2.95e-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: 61.79  E-value: 2.95e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1015655940 275 KGRVTKLLPYGAFVELEKGVEGLVHVSELSwVKRITRPSDVLKLDQEIEAVVLSISvKEQKISL 338
Cdd:cd04472     5 EGKVVKIKDFGAFVEILPGKDGLVHISELS-DERVEKVEDVLKVGDEVKVKVIEVD-DRGRISL 66
Pnp COG1185
Polyribonucleotide nucleotidyltransferase (polynucleotide phosphorylase) [Translation, ...
349-428 3.02e-12

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


Pssm-ID: 440798 [Multi-domain]  Cd Length: 686  Bit Score: 69.26  E-value: 3.02e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 349 ADIEsrfpIGTVIKGQVRNLTPYGAFVGLEEGIDGMIHVSDMSWTRkINHPSEVLKKGDEVEAIVLEIKKEDqRVSLGIK 428
Cdd:COG1185   612 AEPE----VGEIYEGKVVRIMDFGAFVEILPGKDGLVHISELADER-VEKVEDVLKEGDEVKVKVLEIDDQG-RIKLSRK 685
S1_RPS1_repeat_ec6 cd05691
S1_RPS1_repeat_ec6: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
445-517 4.17e-12

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: 61.52  E-value: 4.17e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1015655940 445 GDMVSGQVAKIASFGAFVNLDGDIDGLIHISQLSEDHVERVKDVIKVGDEITARVIKVDSIERRIGLSIKAVN 517
Cdd:cd05691     1 GSIVTGKVTEVDAKGATVKLGDGVEGFLRAAELSRDRVEDATERFKVGDEVEAKITNVDRKNRKISLSIKAKE 73
PRK08582 PRK08582
RNA-binding protein S1;
272-347 4.20e-12

RNA-binding protein S1;


Pssm-ID: 236305 [Multi-domain]  Cd Length: 139  Bit Score: 63.90  E-value: 4.20e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1015655940 272 SQVKGRVTKLLPYGAFVELEKGVEGLVHVSELS--WVKRItrpSDVLKLDQEIEAVVLSISvKEQKISLGVRQLEDNP 347
Cdd:PRK08582    7 SKLQGKVTGITNFGAFVELPEGKTGLVHISEVAdnYVKDI---NDHLKVGDEVEVKVLNVE-DDGKIGLSIKKAKDRP 80
S1_PNPase cd04472
S1_PNPase: Polynucleotide phosphorylase (PNPase), ), S1-like RNA-binding domain. PNPase is a ...
186-251 6.69e-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: 6.69e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1015655940 186 GDKVEGLVKNITDFGAFVD-LRGMDGLLHITDMSWGRVNHPSEMLHIGQSLEVVILEVDrDKERVSL 251
Cdd:cd04472     1 GKIYEGKVVKIKDFGAFVEiLPGKDGLVHISELSDERVEKVEDVLKVGDEVKVKVIEVD-DRGRISL 66
PRK08059 PRK08059
general stress protein 13; Validated
180-262 2.10e-11

general stress protein 13; Validated


Pssm-ID: 181215 [Multi-domain]  Cd Length: 123  Bit Score: 61.22  E-value: 2.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 180 LETVKEGDKVEGLVKNITDFGAFVDL-RGMDGLLHITDMSWGRVNHPSEMLHIGQSLEVVILEVDRDKERVSLGLKQMTD 258
Cdd:PRK08059    2 MSQYEVGSVVTGKVTGIQPYGAFVALdEETQGLVHISEITHGFVKDIHDFLSVGDEVKVKVLSVDEEKGKISLSIRATEE 81

                  ....
gi 1015655940 259 NPWA 262
Cdd:PRK08059   82 APEA 85
PRK07252 PRK07252
S1 RNA-binding domain-containing protein;
443-525 3.24e-11

S1 RNA-binding domain-containing protein;


Pssm-ID: 180908 [Multi-domain]  Cd Length: 120  Bit Score: 60.49  E-value: 3.24e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 443 KVGDMVSGQVAKIASFGAFVNLDGDIDGLIHISQLSEDHVERVKDVIKVGDEITARVIKVDSIERRIGLSIKAVNYDTEQ 522
Cdd:PRK07252    2 KIGDKLKGTITGIKPYGAFVALENGTTGLIHISEIKTGFIDNIHQLLKVGEEVLVQVVDFDEYTGKASLSLRTLEEEKQH 81

                  ...
gi 1015655940 523 LRR 525
Cdd:PRK07252   82 FPH 84
PRK07252 PRK07252
S1 RNA-binding domain-containing protein;
270-345 3.82e-11

S1 RNA-binding domain-containing protein;


Pssm-ID: 180908 [Multi-domain]  Cd Length: 120  Bit Score: 60.49  E-value: 3.82e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1015655940 270 INSQVKGRVTKLLPYGAFVELEKGVEGLVHVSEL--SWVKRItrpSDVLKLDQEIEAVVLSISVKEQKISLGVRQLED 345
Cdd:PRK07252    3 IGDKLKGTITGIKPYGAFVALENGTTGLIHISEIktGFIDNI---HQLLKVGEEVLVQVVDFDEYTGKASLSLRTLEE 77
PRK05807 PRK05807
RNA-binding protein S1;
182-255 4.69e-11

RNA-binding protein S1;


Pssm-ID: 235614 [Multi-domain]  Cd Length: 136  Bit Score: 60.53  E-value: 4.69e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1015655940 182 TVKEGDKVEGLVKNITDFGAFVDLRGMDGLLHITDMSWGRVNHPSEMLHIGQSLEVVILEVDrDKERVSLGLKQ 255
Cdd:PRK05807    2 TLKAGSILEGTVVNITNFGAFVEVEGKTGLVHISEVADTYVKDIREHLKEQDKVKVKVISID-DNGKISLSIKQ 74
Tex COG2183
Transcriptional accessory protein Tex/SPT6 [Transcription];
357-434 5.37e-11

Transcriptional accessory protein Tex/SPT6 [Transcription];


Pssm-ID: 441786 [Multi-domain]  Cd Length: 719  Bit Score: 65.43  E-value: 5.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 357 IGTVIKGQVRNLTPYGAFV--GLEEgiDGMIHVSDMSwTRKINHPSEVLKKGDEVEAIVLEIKKEDQRVSLGIKQLESDP 434
Cdd:COG2183   641 PGMILEGTVTNVTDFGAFVdiGVHQ--DGLVHISQLS-DRFVKDPREVVKVGDIVKVKVLEVDLKRKRISLSMKLDDEAG 717
S1_RpoE cd04460
S1_RpoE: RpoE, S1-like RNA-binding domain. S1-like RNA-binding domains are found in a wide ...
448-512 5.87e-11

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: 59.22  E-value: 5.87e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1015655940 448 VSGQVAKIASFGAFVNLdGDIDGLIHISQLSEDHV-----------ERVKDVIKVGDEITARVIKVDSIERRIGLS 512
Cdd:cd04460     3 VEGEVVEVVDFGAFVRI-GPVDGLLHISQIMDDYIsydpknkrligEETKRVLKVGDVVRARIVAVSLKERRPRES 77
PRK07252 PRK07252
S1 RNA-binding domain-containing protein;
357-445 6.14e-11

S1 RNA-binding domain-containing protein;


Pssm-ID: 180908 [Multi-domain]  Cd Length: 120  Bit Score: 59.72  E-value: 6.14e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 357 IGTVIKGQVRNLTPYGAFVGLEEGIDGMIHVSDMSwTRKINHPSEVLKKGDEVEAIVLEIKKEDQRVSLGIKQLESDPWE 436
Cdd:PRK07252    3 IGDKLKGTITGIKPYGAFVALENGTTGLIHISEIK-TGFIDNIHQLLKVGEEVLVQVVDFDEYTGKASLSLRTLEEEKQH 81
                          90
                  ....*....|....*
gi 1015655940 437 S------INDRFKVG 445
Cdd:PRK07252   82 FphrhrfSNSRHKIG 96
S1_Rrp5_repeat_sc12 cd05708
S1_Rrp5_repeat_sc12: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ...
358-428 1.01e-10

S1_Rrp5_repeat_sc12: Rrp5 is a trans-acting factor important for biogenesis of both the 40S and 60S eukaryotic ribosomal subunits. Rrp5 has two distinct regions, an N-terminal region containing tandemly repeated S1 RNA-binding domains (12 S1 repeats in Saccharomyces cerevisiae Rrp5 and 14 S1 repeats in Homo sapiens Rrp5) and a C-terminal region containing tetratricopeptide repeat (TPR) motifs thought to be involved in protein-protein interactions. Mutational studies have shown that each region represents a specific functional domain. Deletions within the S1-containing region inhibit pre-rRNA processing at either site A3 or A2, whereas deletions within the TPR region confer an inability to support cleavage of A0-A2. This CD includes S. cerevisiae S1 repeat 12 (sc12). Rrp5 is found in eukaryotes but not in prokaryotes or archaea.


Pssm-ID: 240213 [Multi-domain]  Cd Length: 77  Bit Score: 57.72  E-value: 1.01e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1015655940 358 GTVIKGQVRNLTPYGAFVGLE-EGIDGMIHVSDMSWTRKINhPSEVLKKGDEVEAIVLEIKKEDQRVSLGIK 428
Cdd:cd05708     3 GQKIDGTVRRVEDYGVFIDIDgTNVSGLCHKSEISDNRVAD-ASKLFRVGDKVRAKVLKIDAEKKRISLGLK 73
PRK08563 PRK08563
DNA-directed RNA polymerase subunit E'; Provisional
448-512 2.53e-10

DNA-directed RNA polymerase subunit E'; Provisional


Pssm-ID: 236289 [Multi-domain]  Cd Length: 187  Bit Score: 59.84  E-value: 2.53e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1015655940 448 VSGQVAKIASFGAFVNLdGDIDGLIHISQLSEDHV-----------ERVKDVIKVGDEITARVIKVDSIERRIGLS 512
Cdd:PRK08563   85 VEGEVVEVVEFGAFVRI-GPVDGLLHISQIMDDYIsydpkngrligKESKRVLKVGDVVRARIVAVSLKERRPRGS 159
S1 pfam00575
S1 RNA binding domain; The S1 domain occurs in a wide range of RNA associated proteins. It is ...
274-340 4.32e-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: 55.76  E-value: 4.32e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1015655940 274 VKGRVTKLLPYGAFVELEKGVEGLVHVSELSWvKRITRPSDVLKLDQEIEAVVLSISVKEQKISLGV 340
Cdd:pfam00575   7 VEGEVTRVTKGGAFVDLGNGVEGFIPISELSD-DHVEDPDEVIKVGDEVKVKVLKVDKDRRRIILSI 72
S1_DHX8_helicase cd05684
S1_DHX8_helicase: The N-terminal S1 domain of human ATP-dependent RNA helicase DHX8, a DEAH ...
190-254 5.86e-10

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: 55.71  E-value: 5.86e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 190 EGLVKNITDFGAFVDLRGM----DGLLHITDMSW-GRVNHPSEMLHIGQSLEVVILEVDRDKerVSLGLK 254
Cdd:cd05684     5 KGKVTSIMDFGCFVQLEGLkgrkEGLVHISQLSFeGRVANPSDVVKRGQKVKVKVISIQNGK--ISLSMK 72
S1_RPS1_repeat_ec1_hs1 cd05687
S1_RPS1_repeat_ec1_hs1: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
445-514 1.51e-09

S1_RPS1_repeat_ec1_hs1: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ribosomal subunit thought to be involved in the recognition and binding of mRNA's during translation initiation. The bacterial RPS1 domain architecture consists of 4-6 tandem S1 domains. In some bacteria, the tandem S1 array is located C-terminal to a 4-hydroxy-3-methylbut-2-enyl diphosphate reductase (HMBPP reductase) domain. While RPS1 is found primarily in bacteria, proteins with tandem RPS1-like domains have been identified in plants and humans, however these lack the N-terminal HMBPP reductase domain. This CD includes S1 repeat 1 of the Escherichia coli and Homo sapiens RPS1 (ec1 and hs1, respectively). Autoantibodies to double-stranded DNA from patients with systemic lupus erythematosus cross-react with the human RPS1 homolog.


Pssm-ID: 240192 [Multi-domain]  Cd Length: 70  Bit Score: 54.46  E-value: 1.51e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 445 GDMVSGQVAKIASFGAFVNLDGDIDGLIHISQLSEDHVERVKDVIKVGDEITARVIKVDSIERRIGLSIK 514
Cdd:cd05687     1 GDIVKGTVVSVDDDEVLVDIGYKSEGIIPISEFSDDPIENGEDEVKVGDEVEVYVLRVEDEEGNVVLSKR 70
S1_RNase_R cd04471
S1_RNase_R: RNase R C-terminal S1 domain. RNase R is a processive 3' to 5' exoribonuclease, ...
444-509 2.10e-09

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: 54.33  E-value: 2.10e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1015655940 444 VGDMVSGQVAKIASFGAFVNLDGD-IDGLIHISQLSEDHV-----------ERVKDVIKVGDEITARVIKVDSIERRI 509
Cdd:cd04471     1 VGEEFDGVISGVTSFGLFVELDNLtVEGLVHVSTLGDDYYefdeenhalvgERTGKVFRLGDKVKVRVVRVDLDRRKI 78
S1_PNPase cd04472
S1_PNPase: Polynucleotide phosphorylase (PNPase), ), S1-like RNA-binding domain. PNPase is a ...
358-425 6.21e-09

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: 52.54  E-value: 6.21e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1015655940 358 GTVIKGQVRNLTPYGAFVGLEEGIDGMIHVSDMSWTRkINHPSEVLKKGDEVEAIVLEIKKEDqRVSL 425
Cdd:cd04472     1 GKIYEGKVVKIKDFGAFVEILPGKDGLVHISELSDER-VEKVEDVLKVGDEVKVKVIEVDDRG-RISL 66
S1_pNO40 cd05686
S1_pNO40: pNO40 , S1-like RNA-binding domain. pNO40 is a nucleolar protein of unknown function ...
450-514 8.60e-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: 52.10  E-value: 8.60e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1015655940 450 GQVAKIASFGAFVNLDG-DIDGLIHISQLSEDHVERVKDVIKVGDEITARVIKVDsIERRIGLSIK 514
Cdd:cd05686     9 GEVASVTEYGAFVKIPGcRKQGLVHKSHMSSCRVDDPSEVVDVGEKVWVKVIGRE-MKDKMKLSLS 73
PRK08582 PRK08582
RNA-binding protein S1;
357-429 1.52e-08

RNA-binding protein S1;


Pssm-ID: 236305 [Multi-domain]  Cd Length: 139  Bit Score: 53.50  E-value: 1.52e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1015655940 357 IGTVIKGQVRNLTPYGAFVGLEEGIDGMIHVSDMS--WTRKINhpsEVLKKGDEVEAIVLEIKKeDQRVSLGIKQ 429
Cdd:PRK08582    5 VGSKLQGKVTGITNFGAFVELPEGKTGLVHISEVAdnYVKDIN---DHLKVGDEVEVKVLNVED-DGKIGLSIKK 75
S1_IF2_alpha cd04452
S1_IF2_alpha: The alpha subunit of translation Initiation Factor 2, S1-like RNA-binding domain. ...
184-255 1.70e-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: 51.43  E-value: 1.70e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1015655940 184 KEGDKVEGLVKNITDFGAFVDLR---GMDGLLHITDMSWGRVNHPSEMLHIGQSLEVVILEVDRDKERVSLGLKQ 255
Cdd:cd04452     2 EEGELVVVTVKSIADMGAYVSLLeygNIEGMILLSELSRRRIRSIRKLVKVGRKEVVKVIRVDKEKGYIDLSKKR 76
S1_RPS1_repeat_ec6 cd05691
S1_RPS1_repeat_ec6: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
358-431 2.18e-08

S1_RPS1_repeat_ec6: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ribosomal subunit thought to be involved in the recognition and binding of mRNA's during translation initiation. The bacterial RPS1 domain architecture consists of 4-6 tandem S1 domains. In some bacteria, the tandem S1 array is located C-terminal to a 4-hydroxy-3-methylbut-2-enyl diphosphate reductase (HMBPP reductase) domain. While RPS1 is found primarily in bacteria, proteins with tandem RPS1-like domains have been identified in plants and humans, however these lack the N-terminal HMBPP reductase domain. This CD includes S1 repeat 6 (ec6) of the Escherichia coli RPS1. Autoantibodies to double-stranded DNA from patients with systemic lupus erythematosus cross-react with the human RPS1 homolog.


Pssm-ID: 240196 [Multi-domain]  Cd Length: 73  Bit Score: 51.12  E-value: 2.18e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1015655940 358 GTVIKGQVRNLTPYGAFVGLEEGIDGMIHVSDMSWTRKINHPsEVLKKGDEVEAIVLEIKKEDQRVSLGIKQLE 431
Cdd:cd05691     1 GSIVTGKVTEVDAKGATVKLGDGVEGFLRAAELSRDRVEDAT-ERFKVGDEVEAKITNVDRKNRKISLSIKAKE 73
S1_Tex cd05685
S1_Tex: The C-terminal S1 domain of a transcription accessory factor called Tex, which has ...
273-338 2.36e-08

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: 50.69  E-value: 2.36e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1015655940 273 QVKGRVTKLLPYGAFVELEKGVEGLVHVSELSwVKRITRPSDVLKLDQEIEAVVLSISVKEQKISL 338
Cdd:cd05685     3 VLEGVVTNVTDFGAFVDIGVKQDGLIHISKMA-DRFVSHPSDVVSVGDIVEVKVISIDEERGRISL 67
PRK08582 PRK08582
RNA-binding protein S1;
186-260 2.99e-08

RNA-binding protein S1;


Pssm-ID: 236305 [Multi-domain]  Cd Length: 139  Bit Score: 52.73  E-value: 2.99e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1015655940 186 GDKVEGLVKNITDFGAFVDL-RGMDGLLHITDMSWGRVNHPSEMLHIGQSLEVVILEVDRDKeRVSLGLKQMTDNP 260
Cdd:PRK08582    6 GSKLQGKVTGITNFGAFVELpEGKTGLVHISEVADNYVKDINDHLKVGDEVEVKVLNVEDDG-KIGLSIKKAKDRP 80
PRK00087 PRK00087
bifunctional 4-hydroxy-3-methylbut-2-enyl diphosphate reductase/30S ribosomal protein S1;
408-517 3.13e-08

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


Pssm-ID: 234623 [Multi-domain]  Cd Length: 647  Bit Score: 56.49  E-value: 3.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 408 EVEAIVLEIKKEDQRVSlgIKQLESdpWESINDRFKVGDMVSGQVAKIASFGAFVNLDGDIDGLIHISQLSEDHVERVKD 487
Cdd:PRK00087  270 EVIKKMSELDNMEEVEE--NEQLEY--MNELEKQIRRGDIVKGTVVSVNENEVFVDVGYKSEGVIPLRELTLDEISSLKE 345
                          90       100       110
                  ....*....|....*....|....*....|
gi 1015655940 488 VIKVGDEITARVIKVDSIERRIGLSIKAVN 517
Cdd:PRK00087  346 SVKVGDEIEVKVLKLEDEDGYVVLSKKEAD 375
S1_Rrp5_repeat_hs8_sc7 cd04461
S1_Rrp5_repeat_hs8_sc7: Rrp5 Homo sapiens S1 repeat 8 (hs8) and Saccharomyces cerevisiae S1 ...
443-513 6.58e-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: 49.89  E-value: 6.58e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1015655940 443 KVGDMVSGQVAKIASFGAFVNLDGDIDGLIHISQLSEDHVERVKDVIKVGDEITARVIKVDSIERRIGLSI 513
Cdd:cd04461    13 KPGMVVHGYVRNITPYGVFVEFLGGLTGLAPKSYISDEFVTDPSFGFKKGQSVTAKVTSVDEEKQRFLLSL 83
S1_RPS1_repeat_ec6 cd05691
S1_RPS1_repeat_ec6: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
271-344 1.01e-07

S1_RPS1_repeat_ec6: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ribosomal subunit thought to be involved in the recognition and binding of mRNA's during translation initiation. The bacterial RPS1 domain architecture consists of 4-6 tandem S1 domains. In some bacteria, the tandem S1 array is located C-terminal to a 4-hydroxy-3-methylbut-2-enyl diphosphate reductase (HMBPP reductase) domain. While RPS1 is found primarily in bacteria, proteins with tandem RPS1-like domains have been identified in plants and humans, however these lack the N-terminal HMBPP reductase domain. This CD includes S1 repeat 6 (ec6) of the Escherichia coli RPS1. Autoantibodies to double-stranded DNA from patients with systemic lupus erythematosus cross-react with the human RPS1 homolog.


Pssm-ID: 240196 [Multi-domain]  Cd Length: 73  Bit Score: 49.19  E-value: 1.01e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1015655940 271 NSQVKGRVTKLLPYGAFVELEKGVEGLVHVSELSwVKRITRPSDVLKLDQEIEAVVLSISVKEQKISLGVRQLE 344
Cdd:cd05691     1 GSIVTGKVTEVDAKGATVKLGDGVEGFLRAAELS-RDRVEDATERFKVGDEVEAKITNVDRKNRKISLSIKAKE 73
VacB COG0557
Exoribonuclease R [Transcription];
443-513 1.62e-07

Exoribonuclease R [Transcription];


Pssm-ID: 440323 [Multi-domain]  Cd Length: 711  Bit Score: 54.34  E-value: 1.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 443 KVGDMVSGQVAKIASFGAFVNLDGD-IDGLIHISQLSEDHV-----------ERVKDVIKVGDEITARVIKVDSIERRIG 510
Cdd:COG0557   621 RVGEEFEGVISGVTSFGLFVELDELgVEGLVHVSSLGDDYYeyderrqalvgERTGKRYRLGDRVEVRVVRVDLDRRQID 700

                  ...
gi 1015655940 511 LSI 513
Cdd:COG0557   701 FEL 703
PRK09521 PRK09521
exosome complex RNA-binding protein Csl4; Provisional
443-518 1.75e-07

exosome complex RNA-binding protein Csl4; Provisional


Pssm-ID: 236547 [Multi-domain]  Cd Length: 189  Bit Score: 51.51  E-value: 1.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 443 KVGDMVSGQVAKIASFGAFVNLDG----------DIDGLIHISQLSEDHVERVKDVIKVGDEITARVIkvdSIERRIGLS 512
Cdd:PRK09521   63 KKGDIVYGRVVDVKEQRALVRIVSiegserelatSKLAYIHISQVSDGYVESLTDAFKIGDIVRAKVI---SYTDPLQLS 139

                  ....*.
gi 1015655940 513 IKAVNY 518
Cdd:PRK09521  140 TKGKDL 145
S1_Rrp5_repeat_hs6_sc5 cd05698
S1_Rrp5_repeat_hs6_sc5: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ...
445-514 2.73e-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: 47.99  E-value: 2.73e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 445 GDMVSGQVAKIASFGAFVNLDGDIDGLIHISQLSEDHVERVKDVIKVGDEITARVIKVDSIERRIGLSIK 514
Cdd:cd05698     1 GLKTHGTIVKVKPNGCIVSFYNNVKGFLPKSELSEAFIKDPEEHFRVGQVVKVKVLSCDPEQQRLLLSCK 70
S1 smart00316
Ribosomal protein S1-like RNA-binding domain;
18-80 2.75e-07

Ribosomal protein S1-like RNA-binding domain;


Pssm-ID: 197648 [Multi-domain]  Cd Length: 72  Bit Score: 47.98  E-value: 2.75e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940   18 REGSIVTGTIQEIRPQVVLVDIGYKSEGAISISEFED-------EEIEVGDQIEVLLERLENDEGIVVLS 80
Cdd:smart00316   1 EVGDVVEGTVTEITPGGAFVDLGNGVEGLIPISELSDkrvkdpeEVLKVGDEVKVKVLSVDEEKGRIILS 70
PLN00207 PLN00207
polyribonucleotide nucleotidyltransferase; Provisional
237-353 6.25e-07

polyribonucleotide nucleotidyltransferase; Provisional


Pssm-ID: 215104 [Multi-domain]  Cd Length: 891  Bit Score: 52.59  E-value: 6.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 237 VVILEVDRDK-ERVSLGLKQMTDNPW-ADIERKYPINSqvkgrvtkLLPYGAFVELEKGVEGLVHVSELSwVKRITRPSD 314
Cdd:PLN00207  727 VKITAKDLSSlEKSKAIISSLTMVPTvGDIYRNCEIKS--------IAPYGAFVEIAPGREGLCHISELS-SNWLAKPED 797
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1015655940 315 VLKLDQEIEAVVLSISVKEQkISLGVRQLEdnPWADIES 353
Cdd:PLN00207  798 AFKVGDRIDVKLIEVNDKGQ-LRLSRRALL--PEANSEK 833
PRK07252 PRK07252
S1 RNA-binding domain-containing protein;
184-254 9.04e-07

S1 RNA-binding domain-containing protein;


Pssm-ID: 180908 [Multi-domain]  Cd Length: 120  Bit Score: 47.77  E-value: 9.04e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1015655940 184 KEGDKVEGLVKNITDFGAFVDLR-GMDGLLHITDMSWGRVNHPSEMLHIGQSLEVVILEVDRDKERVSLGLK 254
Cdd:PRK07252    2 KIGDKLKGTITGIKPYGAFVALEnGTTGLIHISEIKTGFIDNIHQLLKVGEEVLVQVVDFDEYTGKASLSLR 73
PRK05807 PRK05807
RNA-binding protein S1;
355-429 1.09e-06

RNA-binding protein S1;


Pssm-ID: 235614 [Multi-domain]  Cd Length: 136  Bit Score: 48.20  E-value: 1.09e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1015655940 355 FPIGTVIKGQVRNLTPYGAFVGLeEGIDGMIHVSDM--SWTRKINhpsEVLKKGDEVEAIVLEIkKEDQRVSLGIKQ 429
Cdd:PRK05807    3 LKAGSILEGTVVNITNFGAFVEV-EGKTGLVHISEVadTYVKDIR---EHLKEQDKVKVKVISI-DDNGKISLSIKQ 74
S1_Rrp5_repeat_hs5 cd05697
S1_Rrp5_repeat_hs5: Rrp5 is a trans-acting factor important for biogenesis of both the 40S and ...
358-425 1.38e-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: 45.69  E-value: 1.38e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1015655940 358 GTVIKGQVRNLTPYGAFVGLEEGIDGMI---HVSDMswtrKINHPSEVLKKGDEVEAIVLEIKKEDQRVSL 425
Cdd:cd05697     1 GQVVKGTIRKLRPSGIFVKLSDHIKGLVppmHLADV----RLKHPEKKFKPGLKVKCRVLSVEPERKRLVL 67
PLN00207 PLN00207
polyribonucleotide nucleotidyltransferase; Provisional
427-503 1.83e-06

polyribonucleotide nucleotidyltransferase; Provisional


Pssm-ID: 215104 [Multi-domain]  Cd Length: 891  Bit Score: 51.05  E-value: 1.83e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1015655940 427 IKQLESDPwesindrfKVGDMVSG-QVAKIASFGAFVNLDGDIDGLIHISQLSEDHVERVKDVIKVGDEITARVIKVD 503
Cdd:PLN00207  744 ISSLTMVP--------TVGDIYRNcEIKSIAPYGAFVEIAPGREGLCHISELSSNWLAKPEDAFKVGDRIDVKLIEVN 813
S1_Rrp5_repeat_hs6_sc5 cd05698
S1_Rrp5_repeat_hs6_sc5: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ...
186-254 2.45e-06

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


Pssm-ID: 240203 [Multi-domain]  Cd Length: 70  Bit Score: 45.29  E-value: 2.45e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 186 GDKVEGLVKNITDFGAFVDLRG-MDGLLHITDMSWGRVNHPSEMLHIGQSLEVVILEVDRDKERVSLGLK 254
Cdd:cd05698     1 GLKTHGTIVKVKPNGCIVSFYNnVKGFLPKSELSEAFIKDPEEHFRVGQVVKVKVLSCDPEQQRLLLSCK 70
S1_IF2_alpha cd04452
S1_IF2_alpha: The alpha subunit of translation Initiation Factor 2, S1-like RNA-binding domain. ...
274-342 2.74e-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: 45.27  E-value: 2.74e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1015655940 274 VKGRVTKLLPYGAFVELE--KGVEGLVHVSELS--WVKRItrpSDVLKLDQEIEAVVLSISVKEQKISLGVRQ 342
Cdd:cd04452     7 VVVTVKSIADMGAYVSLLeyGNIEGMILLSELSrrRIRSI---RKLVKVGRKEVVKVIRVDKEKGYIDLSKKR 76
S1_Rrp5_repeat_sc12 cd05708
S1_Rrp5_repeat_sc12: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ...
272-341 2.91e-06

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: 45.40  E-value: 2.91e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1015655940 272 SQVKGRVTKLLPYGAFVELE-KGVEGLVHVSELSwvkrITRPSDVLKLDQE---IEAVVLSISVKEQKISLGVR 341
Cdd:cd05708     4 QKIDGTVRRVEDYGVFIDIDgTNVSGLCHKSEIS----DNRVADASKLFRVgdkVRAKVLKIDAEKKRISLGLK 73
RpsA COG0539
Ribosomal protein S1 [Translation, ribosomal structure and biogenesis]; Ribosomal protein S1 ...
436-519 2.98e-06

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


Pssm-ID: 440305 [Multi-domain]  Cd Length: 348  Bit Score: 49.66  E-value: 2.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 436 ESINDrFKVGDMVSGQVAKIASFGAFVNLDGDIDGLIHISQLSEDHVErvkDVIKVGDEITARVIKVDSIERRIGLSIKA 515
Cdd:COG0539    11 ESLKE-LKEGDIVKGTVVSIDDDEVLVDIGYKSEGIIPLSEFSDEPGE---LEVKVGDEVEVYVEKVEDGEGEIVLSKKK 86

                  ....
gi 1015655940 516 VNYD 519
Cdd:COG0539    87 ADRE 90
PRK05807 PRK05807
RNA-binding protein S1;
274-346 3.18e-06

RNA-binding protein S1;


Pssm-ID: 235614 [Multi-domain]  Cd Length: 136  Bit Score: 46.66  E-value: 3.18e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1015655940 274 VKGRVTKLLPYGAFVELEkGVEGLVHVSEL--SWVKRItrpSDVLKLDQEIEAVVLSISvKEQKISLGVRQLEDN 346
Cdd:PRK05807    9 LEGTVVNITNFGAFVEVE-GKTGLVHISEVadTYVKDI---REHLKEQDKVKVKVISID-DNGKISLSIKQAMKQ 78
PRK03987 PRK03987
translation initiation factor IF-2 subunit alpha; Validated
185-259 3.41e-06

translation initiation factor IF-2 subunit alpha; Validated


Pssm-ID: 235188 [Multi-domain]  Cd Length: 262  Bit Score: 48.67  E-value: 3.41e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1015655940 185 EGDKVEGLVKNITDFGAFVDL---RGMDGLLHITDMSWGRVNHPSEMLHIGQSLEVVILEVDRDKERVSLGLKQMTDN 259
Cdd:PRK03987    8 EGELVVGTVKEVKDFGAFVTLdeyPGKEGFIHISEVASGWVKNIRDHVKEGQKVVCKVIRVDPRKGHIDLSLKRVNEH 85
S1_Rrp5_repeat_hs5 cd05697
S1_Rrp5_repeat_hs5: Rrp5 is a trans-acting factor important for biogenesis of both the 40S and ...
445-511 4.14e-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: 4.14e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 445 GDMVSGQVAKIASFGAFVNLDGDIDGLI---HISQLSEDHVERvkdVIKVGDEITARVIKVDSIERRIGL 511
Cdd:cd05697     1 GQVVKGTIRKLRPSGIFVKLSDHIKGLVppmHLADVRLKHPEK---KFKPGLKVKCRVLSVEPERKRLVL 67
S1_RPS1_repeat_ec6 cd05691
S1_RPS1_repeat_ec6: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
186-256 5.45e-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: 5.45e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1015655940 186 GDKVEGLVKNITDFGAFVDL-RGMDGLLHITDMSWGRVNHPSEMLHIGQSLEVVILEVDRDKERVSLGLKQM 256
Cdd:cd05691     1 GSIVTGKVTEVDAKGATVKLgDGVEGFLRAAELSRDRVEDATERFKVGDEVEAKITNVDRKNRKISLSIKAK 72
S1_RPS1_repeat_ec4 cd05689
S1_RPS1_repeat_ec4: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
445-511 5.94e-06

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: 44.10  E-value: 5.94e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1015655940 445 GDMVSGQVAKIASFGAFVNLDGDIDGLIHISQL--SEDHVERVKdVIKVGDEITARVIKVDSIERRIGL 511
Cdd:cd05689     4 GTRLFGKVTNLTDYGCFVELEEGVEGLVHVSEMdwTNKNIHPSK-VVSLGDEVEVMVLDIDEERRRISL 71
S1_IF2_alpha cd04452
S1_IF2_alpha: The alpha subunit of translation Initiation Factor 2, S1-like RNA-binding domain. ...
357-429 6.12e-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: 44.11  E-value: 6.12e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1015655940 357 IGTVIKGQVRNLTPYGAFVGLEE--GIDGMIHVSDMSwTRKINHPSEVLKKGDEVEAIVLEIKKEDQRVSLGIKQ 429
Cdd:cd04452     3 EGELVVVTVKSIADMGAYVSLLEygNIEGMILLSELS-RRRIRSIRKLVKVGRKEVVKVIRVDKEKGYIDLSKKR 76
S1_Rrp5_repeat_hs6_sc5 cd05698
S1_Rrp5_repeat_hs6_sc5: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ...
276-341 7.42e-06

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


Pssm-ID: 240203 [Multi-domain]  Cd Length: 70  Bit Score: 43.75  E-value: 7.42e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1015655940 276 GRVTKLLPYGAFVELEKGVEGLVHVSELSwVKRITRPSDVLKLDQEIEAVVLSISVKEQKISLGVR 341
Cdd:cd05698     6 GTIVKVKPNGCIVSFYNNVKGFLPKSELS-EAFIKDPEEHFRVGQVVKVKVLSCDPEQQRLLLSCK 70
S1 pfam00575
S1 RNA binding domain; The S1 domain occurs in a wide range of RNA associated proteins. It is ...
17-81 1.07e-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: 43.43  E-value: 1.07e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1015655940  17 LREGSIVTGTIQEIRPQVVLVDIGYKSEGAISISEF-------EDEEIEVGDQIEVLLERLENDEGIVVLSK 81
Cdd:pfam00575   1 PEKGDVVEGEVTRVTKGGAFVDLGNGVEGFIPISELsddhvedPDEVIKVGDEVKVKVLKVDKDRRRIILSI 72
S1_Rrp5_repeat_hs8_sc7 cd04461
S1_Rrp5_repeat_hs8_sc7: Rrp5 Homo sapiens S1 repeat 8 (hs8) and Saccharomyces cerevisiae S1 ...
271-338 1.14e-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: 1.14e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1015655940 271 NSQVKGRVTKLLPYGAFVELEKGVEGLVHVSELSwVKRITRPSDVLKLDQEIEAVVLSISVKEQKISL 338
Cdd:cd04461    15 GMVVHGYVRNITPYGVFVEFLGGLTGLAPKSYIS-DEFVTDPSFGFKKGQSVTAKVTSVDEEKQRFLL 81
PRK03987 PRK03987
translation initiation factor IF-2 subunit alpha; Validated
274-338 1.21e-05

translation initiation factor IF-2 subunit alpha; Validated


Pssm-ID: 235188 [Multi-domain]  Cd Length: 262  Bit Score: 47.13  E-value: 1.21e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1015655940 274 VKGRVTKLLPYGAFVELEK--GVEGLVHVSELS--WVKRItrpSDVLKLDQEIEAVVLSISVKEQKISL 338
Cdd:PRK03987   12 VVGTVKEVKDFGAFVTLDEypGKEGFIHISEVAsgWVKNI---RDHVKEGQKVVCKVIRVDPRKGHIDL 77
S1_RecJ_like cd04473
S1_RecJ_like: The S1 domain of the archaea-specific RecJ-like exonuclease. The function of ...
444-502 1.26e-05

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: 43.36  E-value: 1.26e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1015655940 444 VGDMVSGQVAKIASFGAFVNLDGDIDGLIHISQLSEDHvervkdviKVGDEITARVIKV 502
Cdd:cd04473    16 VGKLYKGKVNGVAKYGVFVDLNDHVRGLIHRSNLLRDY--------EVGDEVIVQVTDI 66
Tex COG2183
Transcriptional accessory protein Tex/SPT6 [Transcription];
285-347 1.54e-05

Transcriptional accessory protein Tex/SPT6 [Transcription];


Pssm-ID: 441786 [Multi-domain]  Cd Length: 719  Bit Score: 47.71  E-value: 1.54e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1015655940 285 GAFVELekGV--EGLVHVSELSwVKRITRPSDVLKLDQEIEAVVLSISVKEQKISLGVRQLEDNP 347
Cdd:COG2183   656 GAFVDI--GVhqDGLVHISQLS-DRFVKDPREVVKVGDIVKVKVLEVDLKRKRISLSMKLDDEAG 717
S1_Rrp5_repeat_sc11 cd05707
S1_Rrp5_repeat_sc11: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ...
445-512 3.02e-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: 41.90  E-value: 3.02e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1015655940 445 GDMVSGQVAKIASFGAFVNLDGDIDGLIHISQLSEDHVERVKDVIKVGDEITARVIKVDSIERRIGLS 512
Cdd:cd05707     1 GDVVRGFVKNIANNGVFVTLGRGVDARVRVSELSDSYLKDWKKRFKVGQLVKGKIVSIDPDNGRIEMT 68
S1_Rrp5_repeat_hs8_sc7 cd04461
S1_Rrp5_repeat_hs8_sc7: Rrp5 Homo sapiens S1 repeat 8 (hs8) and Saccharomyces cerevisiae S1 ...
358-425 3.91e-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: 42.19  E-value: 3.91e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1015655940 358 GTVIKGQVRNLTPYGAFVGLEEGIDGMIHVSDMSwTRKINHPSEVLKKGDEVEAIVLEIKKEDQRVSL 425
Cdd:cd04461    15 GMVVHGYVRNITPYGVFVEFLGGLTGLAPKSYIS-DEFVTDPSFGFKKGQSVTAKVTSVDEEKQRFLL 81
S1_Rrp5_repeat_hs11_sc8 cd05702
S1_Rrp5_repeat_hs11_sc8: Rrp5 is a trans-acting factor important for biogenesis of both the ...
445-500 6.77e-05

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: 41.04  E-value: 6.77e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1015655940 445 GDMVSGQVAKIASFGAFVNLDGDIDGLIHISQLSEDHVERVK--DVIKVGDEITARVI 500
Cdd:cd05702     1 GDLVKAKVKSVKPTQLNVQLADNVHGRIHVSEVFDEWPDGKNplSKFKIGQKIKARVI 58
PLN00207 PLN00207
polyribonucleotide nucleotidyltransferase; Provisional
357-434 7.64e-05

polyribonucleotide nucleotidyltransferase; Provisional


Pssm-ID: 215104 [Multi-domain]  Cd Length: 891  Bit Score: 45.66  E-value: 7.64e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1015655940 357 IGTVIKG-QVRNLTPYGAFVGLEEGIDGMIHVSDMSwTRKINHPSEVLKKGDEVEAIVLEIKKEDQrVSLGIKQLESDP 434
Cdd:PLN00207  753 VGDIYRNcEIKSIAPYGAFVEIAPGREGLCHISELS-SNWLAKPEDAFKVGDRIDVKLIEVNDKGQ-LRLSRRALLPEA 829
S1_pNO40 cd05686
S1_pNO40: pNO40 , S1-like RNA-binding domain. pNO40 is a nucleolar protein of unknown function ...
190-251 9.47e-05

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: 40.93  E-value: 9.47e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1015655940 190 EGLVKNITDFGAFVDLRG--MDGLLHITDMSWGRVNHPSEMLHIGQSL--EVVILEVDrDKERVSL 251
Cdd:cd05686     8 KGEVASVTEYGAFVKIPGcrKQGLVHKSHMSSCRVDDPSEVVDVGEKVwvKVIGREMK-DKMKLSL 72
S1_pNO40 cd05686
S1_pNO40: pNO40 , S1-like RNA-binding domain. pNO40 is a nucleolar protein of unknown function ...
356-428 1.02e-04

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: 40.93  E-value: 1.02e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1015655940 356 PIGTVIKGQVRNLTPYGAFVGLeEGI--DGMIHVSDMSwTRKINHPSEVLKKGDEVEAIVLEiKKEDQRVSLGIK 428
Cdd:cd05686     2 ALYQIFKGEVASVTEYGAFVKI-PGCrkQGLVHKSHMS-SCRVDDPSEVVDVGEKVWVKVIG-REMKDKMKLSLS 73
S1_Rrp5_repeat_hs5 cd05697
S1_Rrp5_repeat_hs5: Rrp5 is a trans-acting factor important for biogenesis of both the 40S and ...
186-253 1.98e-04

S1_Rrp5_repeat_hs5: Rrp5 is a trans-acting factor important for biogenesis of both the 40S and 60S eukaryotic ribosomal subunits. Rrp5 has two distinct regions, an N-terminal region containing tandemly repeated S1 RNA-binding domains (12 S1 repeats in Saccharomyces cerevisiae Rrp5 and 14 S1 repeats in Homo sapiens Rrp5) and a C-terminal region containing tetratricopeptide repeat (TPR) motifs thought to be involved in protein-protein interactions. Mutational studies have shown that each region represents a specific functional domain. Deletions within the S1-containing region inhibit pre-rRNA processing at either site A3 or A2, whereas deletions within the TPR region confer an inability to support cleavage of A0-A2. This CD includes H. sapiens S1 repeat 5 (hs5) and S. cerevisiae S1 repeat 5 (sc5). Rrp5 is found in eukaryotes but not in prokaryotes or archaea.


Pssm-ID: 240202 [Multi-domain]  Cd Length: 69  Bit Score: 39.91  E-value: 1.98e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1015655940 186 GDKVEGLVKNITDFGAFVDLRG-MDGLLHITDMSWGRVNHPSEMLHIGQSLEVVILEVDRDKERVSLGL 253
Cdd:cd05697     1 GQVVKGTIRKLRPSGIFVKLSDhIKGLVPPMHLADVRLKHPEKKFKPGLKVKCRVLSVEPERKRLVLTL 69
S1_Rrp5_repeat_sc10 cd05706
S1_Rrp5_repeat_sc10: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ...
443-512 3.05e-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: 39.54  E-value: 3.05e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 443 KVGDMVSGQVAKIASFGAFVNLDGDIDGLIHISQLSEDHVERVKDVIKVGDEITARVIKVDSIERRIGLS 512
Cdd:cd05706     2 KVGDILPGRVTKVNDRYVLVQLGNKVTGPSFITDALDDYSEALPYKFKKNDIVRACVLSVDVPNKKIALS 71
PTZ00248 PTZ00248
eukaryotic translation initiation factor 2 subunit 1; Provisional
443-517 3.19e-04

eukaryotic translation initiation factor 2 subunit 1; Provisional


Pssm-ID: 240329 [Multi-domain]  Cd Length: 319  Bit Score: 43.11  E-value: 3.19e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1015655940 443 KVGDMVSGQVAKIASFGAFVNL--DGDIDGLIHISQLSEDHVERVKDVIKVGDEITARVIKVDSIERRIGLSIKAVN 517
Cdd:PTZ00248   16 EEDDLVMVKVVRITEMGAYVSLleYDDIEGMILMSELSKRRIRSINKLIRVGRHEVVVVLRVDKEKGYIDLSKKRVS 92
PLN00207 PLN00207
polyribonucleotide nucleotidyltransferase; Provisional
193-260 3.31e-04

polyribonucleotide nucleotidyltransferase; Provisional


Pssm-ID: 215104 [Multi-domain]  Cd Length: 891  Bit Score: 43.73  E-value: 3.31e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1015655940 193 VKNITDFGAFVDLR-GMDGLLHITDMSWGRVNHPSEMLHIGQSLEVVILEVDrDKERVSLGLKQMTDNP 260
Cdd:PLN00207  762 IKSIAPYGAFVEIApGREGLCHISELSSNWLAKPEDAFKVGDRIDVKLIEVN-DKGQLRLSRRALLPEA 829
PRK11642 PRK11642
ribonuclease R;
443-513 4.38e-04

ribonuclease R;


Pssm-ID: 236944 [Multi-domain]  Cd Length: 813  Bit Score: 43.19  E-value: 4.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 443 KVGDMVSGQVAKIASFGAFVNL-DGDIDGLIHISQLSEDHV-----------ERVKDVIKVGDEITARVIKVDSIERRIG 510
Cdd:PRK11642  642 QVGNVFKGVISSVTGFGFFVRLdDLFIDGLVHVSSLDNDYYrfdqvgqrligESSGQTYRLGDRVEVRVEAVNMDERKID 721

                  ...
gi 1015655940 511 LSI 513
Cdd:PRK11642  722 FSL 724
S1_Rrp5_repeat_hs11_sc8 cd05702
S1_Rrp5_repeat_hs11_sc8: Rrp5 is a trans-acting factor important for biogenesis of both the ...
274-327 4.97e-04

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: 38.73  E-value: 4.97e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1015655940 274 VKGRVTKLLPYGAFVELEKGVEGLVHVSEL--SWvKRITRPSDVLKLDQEIEAVVL 327
Cdd:cd05702     4 VKAKVKSVKPTQLNVQLADNVHGRIHVSEVfdEW-PDGKNPLSKFKIGQKIKARVI 58
S1_Rrp5_repeat_hs6_sc5 cd05698
S1_Rrp5_repeat_hs6_sc5: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ...
358-428 5.46e-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: 38.75  E-value: 5.46e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1015655940 358 GTVIKGQVRNLTPYGAFVGLEEGIDGMIHVSDMSwTRKINHPSEVLKKGDEVEAIVLEIKKEDQRVSLGIK 428
Cdd:cd05698     1 GLKTHGTIVKVKPNGCIVSFYNNVKGFLPKSELS-EAFIKDPEEHFRVGQVVKVKVLSCDPEQQRLLLSCK 70
S1_Rrp5_repeat_hs4 cd05696
S1_Rrp5_repeat_hs4: Rrp5 is a trans-acting factor important for biogenesis of both the 40S and ...
458-512 5.62e-04

S1_Rrp5_repeat_hs4: 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 4 (hs4). Rrp5 is found in eukaryotes but not in prokaryotes or archaea.


Pssm-ID: 240201 [Multi-domain]  Cd Length: 71  Bit Score: 38.40  E-value: 5.62e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1015655940 458 FGAFVNLDGDIDGLIHISQLSEDHVERVKDVIKVGDEITARVIKVDSIERRIGLS 512
Cdd:cd05696    16 LGAVFELKDGLLGFVHISHLSDDKVPSDTGPFKAGTTHKARIIGYSPMDGLLQLS 70
S1_Rrp5_repeat_sc11 cd05707
S1_Rrp5_repeat_sc11: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ...
186-251 6.46e-04

S1_Rrp5_repeat_sc11: Rrp5 is a trans-acting factor important for biogenesis of both the 40S and 60S eukaryotic ribosomal subunits. Rrp5 has two distinct regions, an N-terminal region containing tandemly repeated S1 RNA-binding domains (12 S1 repeats in Saccharomyces cerevisiae Rrp5 and 14 S1 repeats in Homo sapiens Rrp5) and a C-terminal region containing tetratricopeptide repeat (TPR) motifs thought to be involved in protein-protein interactions. Mutational studies have shown that each region represents a specific functional domain. Deletions within the S1-containing region inhibit pre-rRNA processing at either site A3 or A2, whereas deletions within the TPR region confer an inability to support cleavage of A0-A2. This CD includes S. cerevisiae S1 repeat 11 (sc11). Rrp5 is found in eukaryotes but not in prokaryotes or archaea.


Pssm-ID: 240212 [Multi-domain]  Cd Length: 68  Bit Score: 38.43  E-value: 6.46e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1015655940 186 GDKVEGLVKNITDFGAFVDL-RGMDGLLHITDMSWGRVNHPSEMLHIGQSLEVVILEVDRDKERVSL 251
Cdd:cd05707     1 GDVVRGFVKNIANNGVFVTLgRGVDARVRVSELSDSYLKDWKKRFKVGQLVKGKIVSIDPDNGRIEM 67
nusA PRK09202
transcription elongation factor NusA; Validated
142-245 1.19e-03

transcription elongation factor NusA; Validated


Pssm-ID: 236410 [Multi-domain]  Cd Length: 470  Bit Score: 41.39  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1015655940 142 VGKVYEFKIVKVNDDR------KNIVLSRreVIEAERADQRQRFLEtvKEGDKVEGLVKNITDFGAFVDLRGMDGLLHIT 215
Cdd:PRK09202   89 VGDYIEEEIESVDFGRiaaqtaKQVIVQK--IREAERERVYEEYKD--RVGEIITGVVKRVERGNIIVDLGRAEAILPRK 164
                          90       100       110
                  ....*....|....*....|....*....|
gi 1015655940 216 DMSwgrvnhPSEMLHIGQSLEVVILEVDRD 245
Cdd:PRK09202  165 EQI------PRENFRPGDRVRAYVYEVRKE 188
S1_Rrp5_repeat_hs5 cd05697
S1_Rrp5_repeat_hs5: Rrp5 is a trans-acting factor important for biogenesis of both the 40S and ...
273-338 1.33e-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: 37.60  E-value: 1.33e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1015655940 273 QVKGRVTKLLPYGAFVELEKGVEGLVHVSELSWVkRITRPSDVLKLDQEIEAVVLSISVKEQKISL 338
Cdd:cd05697     3 VVKGTIRKLRPSGIFVKLSDHIKGLVPPMHLADV-RLKHPEKKFKPGLKVKCRVLSVEPERKRLVL 67
S1_RNase_E cd04453
S1_RNase_E: RNase E and RNase G, S1-like RNA-binding domain. RNase E is an essential ...
444-501 1.59e-03

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: 37.96  E-value: 1.59e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1015655940 444 VGDMVSGQVAKIASF--GAFVNLDGDIDGLIHISQLSEDHVERVK---DVIKVGDEITARVIK 501
Cdd:cd04453     7 VGNIYLGRVKKIVPGlqAAFVDIGLGKNGFLHLSDILPAYFKKHKkiaKLLKEGQEILVQVVK 69
S1_RNase_R cd04471
S1_RNase_R: RNase R C-terminal S1 domain. RNase R is a processive 3' to 5' exoribonuclease, ...
276-303 1.65e-03

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: 37.38  E-value: 1.65e-03
                          10        20
                  ....*....|....*....|....*....
gi 1015655940 276 GRVTKLLPYGAFVEL-EKGVEGLVHVSEL 303
Cdd:cd04471     7 GVISGVTSFGLFVELdNLTVEGLVHVSTL 35
PRK08563 PRK08563
DNA-directed RNA polymerase subunit E'; Provisional
189-214 1.70e-03

DNA-directed RNA polymerase subunit E'; Provisional


Pssm-ID: 236289 [Multi-domain]  Cd Length: 187  Bit Score: 39.81  E-value: 1.70e-03
                          10        20
                  ....*....|....*....|....*.
gi 1015655940 189 VEGLVKNITDFGAFVDLRGMDGLLHI 214
Cdd:PRK08563   85 VEGEVVEVVEFGAFVRIGPVDGLLHI 110
S1_RPS1_repeat_ec1_hs1 cd05687
S1_RPS1_repeat_ec1_hs1: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
272-338 1.83e-03

S1_RPS1_repeat_ec1_hs1: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ribosomal subunit thought to be involved in the recognition and binding of mRNA's during translation initiation. The bacterial RPS1 domain architecture consists of 4-6 tandem S1 domains. In some bacteria, the tandem S1 array is located C-terminal to a 4-hydroxy-3-methylbut-2-enyl diphosphate reductase (HMBPP reductase) domain. While RPS1 is found primarily in bacteria, proteins with tandem RPS1-like domains have been identified in plants and humans, however these lack the N-terminal HMBPP reductase domain. This CD includes S1 repeat 1 of the Escherichia coli and Homo sapiens RPS1 (ec1 and hs1, respectively). Autoantibodies to double-stranded DNA from patients with systemic lupus erythematosus cross-react with the human RPS1 homolog.


Pssm-ID: 240192 [Multi-domain]  Cd Length: 70  Bit Score: 37.12  E-value: 1.83e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1015655940 272 SQVKGRVTKLLPYGAFVELEKGVEGLVHVSELSWvKRITRPSDVLKLDQEIEAVVLSISVKEQKISL 338
Cdd:cd05687     2 DIVKGTVVSVDDDEVLVDIGYKSEGIIPISEFSD-DPIENGEDEVKVGDEVEVYVLRVEDEEGNVVL 67
S1_RpoE cd04460
S1_RpoE: RpoE, S1-like RNA-binding domain. S1-like RNA-binding domains are found in a wide ...
189-214 1.96e-03

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


Pssm-ID: 239907 [Multi-domain]  Cd Length: 99  Bit Score: 37.65  E-value: 1.96e-03
                          10        20
                  ....*....|....*....|....*.
gi 1015655940 189 VEGLVKNITDFGAFVDLRGMDGLLHI 214
Cdd:cd04460     3 VEGEVVEVVDFGAFVRIGPVDGLLHI 28
S1_RPS1_repeat_ec2_hs2 cd04465
S1_RPS1_repeat_ec2_hs2: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
186-249 2.04e-03

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: 36.67  E-value: 2.04e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1015655940 186 GDKVEGLVKNITDFGAFVDLRGMDGLLHITDMSWGRVNHPSEMlhIGQSLEVVILEVDRDKERV 249
Cdd:cd04465     1 GEIVEGKVTEKVKGGLIVDIEGVRAFLPASQVDLRPVEDLDEY--VGKELKFKIIEIDRERNNI 62
VacB COG0557
Exoribonuclease R [Transcription];
276-303 2.31e-03

Exoribonuclease R [Transcription];


Pssm-ID: 440323 [Multi-domain]  Cd Length: 711  Bit Score: 40.86  E-value: 2.31e-03
                          10        20
                  ....*....|....*....|....*....
gi 1015655940 276 GRVTKLLPYGAFVELEK-GVEGLVHVSEL 303
Cdd:COG0557   628 GVISGVTSFGLFVELDElGVEGLVHVSSL 656
S1_Rrp5_repeat_hs11_sc8 cd05702
S1_Rrp5_repeat_hs11_sc8: Rrp5 is a trans-acting factor important for biogenesis of both the ...
358-414 2.92e-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: 36.41  E-value: 2.92e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1015655940 358 GTVIKGQVRNLTPYGAFVGLEEGIDGMIHVSDMSWTRK-INHPSEVLKKGDEVEAIVL 414
Cdd:cd05702     1 GDLVKAKVKSVKPTQLNVQLADNVHGRIHVSEVFDEWPdGKNPLSKFKIGQKIKARVI 58
S1 smart00316
Ribosomal protein S1-like RNA-binding domain;
117-165 3.45e-03

Ribosomal protein S1-like RNA-binding domain;


Pssm-ID: 197648 [Multi-domain]  Cd Length: 72  Bit Score: 36.43  E-value: 3.45e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1015655940  117 VNVGVEAFLPGSQVDIIPPRDLNEY--VGKVYEFKIVKVNDDRKNIVLSRR 165
Cdd:smart00316  22 LGNGVEGLIPISELSDKRVKDPEEVlkVGDEVKVKVLSVDEEKGRIILSLK 72
S1_RPS1_repeat_ec1_hs1 cd05687
S1_RPS1_repeat_ec1_hs1: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
358-428 4.88e-03

S1_RPS1_repeat_ec1_hs1: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ribosomal subunit thought to be involved in the recognition and binding of mRNA's during translation initiation. The bacterial RPS1 domain architecture consists of 4-6 tandem S1 domains. In some bacteria, the tandem S1 array is located C-terminal to a 4-hydroxy-3-methylbut-2-enyl diphosphate reductase (HMBPP reductase) domain. While RPS1 is found primarily in bacteria, proteins with tandem RPS1-like domains have been identified in plants and humans, however these lack the N-terminal HMBPP reductase domain. This CD includes S1 repeat 1 of the Escherichia coli and Homo sapiens RPS1 (ec1 and hs1, respectively). Autoantibodies to double-stranded DNA from patients with systemic lupus erythematosus cross-react with the human RPS1 homolog.


Pssm-ID: 240192 [Multi-domain]  Cd Length: 70  Bit Score: 35.97  E-value: 4.88e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1015655940 358 GTVIKGQVRNLTPYGAFVGLEEGIDGMIHVSDMSWTRKINhPSEVLKKGDEVEAIVLEIKKEDQRVSLGIK 428
Cdd:cd05687     1 GDIVKGTVVSVDDDEVLVDIGYKSEGIIPISEFSDDPIEN-GEDEVKVGDEVEVYVLRVEDEEGNVVLSKR 70
S1_NusA cd04455
S1_NusA: N-utilizing substance A protein (NusA), S1-like RNA-binding domain. S1-like ...
18-73 4.96e-03

S1_NusA: N-utilizing substance A protein (NusA), S1-like RNA-binding domain. S1-like RNA-binding domains are found in a wide variety of RNA-associated proteins. NusA is a transcription elongation factor containing an N-terminal catalytic domain and three RNA binding domains (RBD's). The RBD's include one S1 domain and two KH domains that form an RNA binding surface. DNA transcription by RNA polymerase (RNAP) includes three phases - initiation, elongation, and termination. During initiation, sigma factors bind RNAP and target RNAP to specific promoters. During elongation, N-utilization substances (NusA, B, E, and G) replace sigma factors and regulate pausing, termination, and antitermination. NusA is cold-shock-inducible.


Pssm-ID: 239902 [Multi-domain]  Cd Length: 67  Bit Score: 35.88  E-value: 4.96e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1015655940  18 REGSIVTGTIQEIRPQVVLVDIGyKSEGAISISE-FEDEEIEVGDQIEVLLERLEND 73
Cdd:cd04455     2 REGEIVTGIVKRVDRGNVIVDLG-KVEAILPKKEqIPGESYRPGDRIKAYVLEVRKT 57
PRK03987 PRK03987
translation initiation factor IF-2 subunit alpha; Validated
358-428 7.50e-03

translation initiation factor IF-2 subunit alpha; Validated


Pssm-ID: 235188 [Multi-domain]  Cd Length: 262  Bit Score: 38.27  E-value: 7.50e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1015655940 358 GTVIKGQVRNLTPYGAFVGLEE--GIDGMIHVSDMS--WTRKINhpsEVLKKGDEVEAIVLEIKKEDQRVSLGIK 428
Cdd:PRK03987    9 GELVVGTVKEVKDFGAFVTLDEypGKEGFIHISEVAsgWVKNIR---DHVKEGQKVVCKVIRVDPRKGHIDLSLK 80
 
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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