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Conserved domains on  [gi|489056936|ref|WP_002967062|]
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MULTISPECIES: 30S ribosomal protein S1 [Brucella]

Protein Classification

30S ribosomal protein S1( domain architecture ID 11482186)

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

Gene Ontology:  GO:0000028|GO:0006412

Graphical summary

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List of domain hits

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

30S ribosomal protein S1; Reviewed


:

Pssm-ID: 235775 [Multi-domain]  Cd Length: 565  Bit Score: 892.21  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936   1 MSQSNPTRADFESLLAESFAEHDLAEGYVVKGRIVAIEKDMAIIDAGLKVEGRVPLKEFGAKGKDGTLKPGDEVEVYVER 80
Cdd:PRK06299   5 AQNQNDMEESFAELFEESLKESETREGSIVKGTVVAIDKDYVLVDVGLKSEGRIPLEEFKNEQGELEVKVGDEVEVYVER 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936  81 IENALGEAVLSREKARREESWVKLEQKFANGERVDGVIFNQVKGGFTVDLDGAVAFLPRSQVDIRPIRDVTPLMHVPQPF 160
Cdd:PRK06299  85 IEDGFGETVLSREKAKRLEAWDKLEKAFENGEIVEGVINGKVKGGFTVDLNGVEAFLPGSQVDVRPVRDTDPLEGKELEF 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936 161 EILKMDKRRGNIVVSRRTVLEESRAEQRSEIVQNLEEGQVVEGVVKNITDYGAFVDLGGIDGLLHVTDMAWRRVNHPSEI 240
Cdd:PRK06299 165 KVIKLDKKRNNIVVSRRAVLEEERAEEREELLENLEEGQVVEGVVKNITDYGAFVDLGGVDGLLHITDISWKRVNHPSEV 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936 241 LTIGQTVKVQIIRINQETHRISLGMKQLESDPWDGIGAKYPIGKKITGTVTNITDYGAFVEIEPGIEGLIHVSEMSWTKK 320
Cdd:PRK06299 245 VNVGDEVKVKVLKFDKEKKRVSLGLKQLGEDPWEAIEKKYPVGSKVKGKVTNITDYGAFVELEEGIEGLVHVSEMSWTKK 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936 321 NVHPGKILSTTQEVEVVVLEVDPVKRRISLGLKQTLDNPWTTFAQKYPVGTVVEGEVKNKTEFGLFIGLDGDVDGMVHLS 400
Cdd:PRK06299 325 NKHPSKVVSVGQEVEVMVLEIDEEKRRISLGLKQCKENPWEEFAEKYPVGDVVEGKVKNITDFGAFVGLEGGIDGLVHLS 404
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936 401 DLDWNRPGEQVIEEYNKGEVVKAVVLDVDVEKERISLGIKQLSGDKVGEAAASgeLRKNAIVTCEVTAVTDGGLEVRLVD 480
Cdd:PRK06299 405 DISWDKKGEEAVELYKKGDEVEAVVLKVDVEKERISLGIKQLEEDPFEEFAKK--HKKGSIVTGTVTEVKDKGAFVELED 482
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936 481 hDLDSFIRRSDLSRDRDEQRPERFTVGQKVDARVIAFDKKTSKLQVSIKALEIAEEKEAVAQYGS-SDSGASLGDILGAA 559
Cdd:PRK06299 483 -GVEGLIRASELSRDRVEDATEVLKVGDEVEAKVINIDRKNRRISLSIKALDEAEEKEAIAEYNSaSDSKTTLGDLLKAA 561

                 ....
gi 489056936 560 LKKQ 563
Cdd:PRK06299 562 LKGK 565
 
Name Accession Description Interval E-value
rpsA PRK06299
30S ribosomal protein S1; Reviewed
1-563 0e+00

30S ribosomal protein S1; Reviewed


Pssm-ID: 235775 [Multi-domain]  Cd Length: 565  Bit Score: 892.21  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936   1 MSQSNPTRADFESLLAESFAEHDLAEGYVVKGRIVAIEKDMAIIDAGLKVEGRVPLKEFGAKGKDGTLKPGDEVEVYVER 80
Cdd:PRK06299   5 AQNQNDMEESFAELFEESLKESETREGSIVKGTVVAIDKDYVLVDVGLKSEGRIPLEEFKNEQGELEVKVGDEVEVYVER 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936  81 IENALGEAVLSREKARREESWVKLEQKFANGERVDGVIFNQVKGGFTVDLDGAVAFLPRSQVDIRPIRDVTPLMHVPQPF 160
Cdd:PRK06299  85 IEDGFGETVLSREKAKRLEAWDKLEKAFENGEIVEGVINGKVKGGFTVDLNGVEAFLPGSQVDVRPVRDTDPLEGKELEF 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936 161 EILKMDKRRGNIVVSRRTVLEESRAEQRSEIVQNLEEGQVVEGVVKNITDYGAFVDLGGIDGLLHVTDMAWRRVNHPSEI 240
Cdd:PRK06299 165 KVIKLDKKRNNIVVSRRAVLEEERAEEREELLENLEEGQVVEGVVKNITDYGAFVDLGGVDGLLHITDISWKRVNHPSEV 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936 241 LTIGQTVKVQIIRINQETHRISLGMKQLESDPWDGIGAKYPIGKKITGTVTNITDYGAFVEIEPGIEGLIHVSEMSWTKK 320
Cdd:PRK06299 245 VNVGDEVKVKVLKFDKEKKRVSLGLKQLGEDPWEAIEKKYPVGSKVKGKVTNITDYGAFVELEEGIEGLVHVSEMSWTKK 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936 321 NVHPGKILSTTQEVEVVVLEVDPVKRRISLGLKQTLDNPWTTFAQKYPVGTVVEGEVKNKTEFGLFIGLDGDVDGMVHLS 400
Cdd:PRK06299 325 NKHPSKVVSVGQEVEVMVLEIDEEKRRISLGLKQCKENPWEEFAEKYPVGDVVEGKVKNITDFGAFVGLEGGIDGLVHLS 404
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936 401 DLDWNRPGEQVIEEYNKGEVVKAVVLDVDVEKERISLGIKQLSGDKVGEAAASgeLRKNAIVTCEVTAVTDGGLEVRLVD 480
Cdd:PRK06299 405 DISWDKKGEEAVELYKKGDEVEAVVLKVDVEKERISLGIKQLEEDPFEEFAKK--HKKGSIVTGTVTEVKDKGAFVELED 482
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936 481 hDLDSFIRRSDLSRDRDEQRPERFTVGQKVDARVIAFDKKTSKLQVSIKALEIAEEKEAVAQYGS-SDSGASLGDILGAA 559
Cdd:PRK06299 483 -GVEGLIRASELSRDRVEDATEVLKVGDEVEAKVINIDRKNRRISLSIKALDEAEEKEAIAEYNSaSDSKTTLGDLLKAA 561

                 ....
gi 489056936 560 LKKQ 563
Cdd:PRK06299 562 LKGK 565
rpsA TIGR00717
ribosomal protein S1; This model describes ribosomal protein S1, RpsA. This protein is found ...
9-529 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: 577.84  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936    9 ADFESLLAESFAEHDLAEGYVVKGRIVAIEKDMAIIDAGLKVEGRVPLKEFgaKGKDGTLKPGDEVEVYVERIENALGEA 88
Cdd:TIGR00717   1 ESFAQLLEESLKTEETRPGSIVKGTVVAINKDTVFVDVGLKSEGRIPKEEF--LDAPLEIQVGDEVEVYLDRVEDRFGET 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936   89 VLSREKARREESWVKLEQKFANGERVDGVIFNQVKGGFTVDLDGAVAFLPRSQVDIRPIRDVTPLMHVPQPFEILKMDKR 168
Cdd:TIGR00717  79 VLSREKAQRHELWIKLEKAYEEGSIVEGKIVGKVKGGFIVDLNGVEAFLPGSQVDVKPIKDLDSLIGKTLKFKIIKLDQK 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936  169 RGNIVVSRRTVLEESRAEQRSEIVQNLEEGQVVEGVVKNITDYGAFVDLGGIDGLLHVTDMAWRRVNHPSEILTIGQTVK 248
Cdd:TIGR00717 159 RNNIVVSRRAYLEEERSQAREELLENLKEGDVVKGVVKNITDFGAFVDLGGVDGLLHITDMSWKRVKHPSEYVKVGQEVK 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936  249 VQIIRINQETHRISLGMKQLESDPWDGIGAKYPIGKKITGTVTNITDYGAFVEIEPGIEGLIHVSEMSWTKKNVHPGKIL 328
Cdd:TIGR00717 239 VKVIKFDKEKGRISLSLKQLGEDPWEAIEKKFPVGDKITGRVTNLTDYGVFVEIEEGIEGLVHVSEMSWVKKNSHPSKVV 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936  329 STTQEVEVVVLEVDPVKRRISLGLKQTLDNPWTTFAQKYPVGTVVEGEVKNKTEFGLFIGLDGDVDGMVHLSDLDWNRPG 408
Cdd:TIGR00717 319 KKGDEVEVMILDIDPERRRLSLGLKQCKANPWEQFEEKHPVGDRVTGKIKKITDFGAFVELEGGIDGLIHLSDISWDKDG 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936  409 EQVIEEYNKGEVVKAVVLDVDVEKERISLGIKQLSGDKVGEAAAsgELRKNAIVTCEVTAVTDGGLEVRLvDHDLDSFIR 488
Cdd:TIGR00717 399 READHLYKKGDEIEAVVLAVDKEKKRISLGVKQLTENPWEKFAA--KYKVGSVVKGKVTEIKDFGAFVEL-PGGVEGLIR 475
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|.
gi 489056936  489 RSDLSRDRDEQRPERFTVGQKVDARVIAFDKKTSKLQVSIK 529
Cdd:TIGR00717 476 NSELSENRDEDKTDEIKVGDEVEAKVVDIDKKNRKVSLSVK 516
RpsA COG0539
Ribosomal protein S1 [Translation, ribosomal structure and biogenesis]; Ribosomal protein S1 ...
7-355 0e+00

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


Pssm-ID: 440305 [Multi-domain]  Cd Length: 348  Bit Score: 522.68  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936   7 TRADFESLLAESFAEhdLAEGYVVKGRIVAIEKDMAIIDAGLKVEGRVPLKEFGAKGKDGTLKPGDEVEVYVERIENALG 86
Cdd:COG0539    1 MSESFAELLEESLKE--LKEGDIVKGTVVSIDDDEVLVDIGYKSEGIIPLSEFSDEPGELEVKVGDEVEVYVEKVEDGEG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936  87 EAVLSREKARREESWVKLEQKFANGERVDGVIFNQVKGGFTVDLDGAVAFLPRSQVDIRPIRDVTPLMHVPQPFEILKMD 166
Cdd:COG0539   79 EIVLSKKKADREKAWEELEEAFENGEPVEGKVKGVVKGGLIVDIGGVRAFLPASQVDVRPVRDLDEYVGKTLEFKIIKLD 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936 167 KRRGNIVVSRRTVLEESRAEQRSEIVQNLEEGQVVEGVVKNITDYGAFVDLGGIDGLLHVTDMAWRRVNHPSEILTIGQT 246
Cdd:COG0539  159 RKRNNVVVSRRAVLEEEREEKREELLEKLEEGDVVEGTVKNITDFGAFVDLGGVDGLLHISEISWGRVKHPSEVLKVGDE 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936 247 VKVQIIRINQETHRISLGMKQLESDPWDGIGAKYPIGKKITGTVTNITDYGAFVEIEPGIEGLIHVSEMSWTKKNVHPGK 326
Cdd:COG0539  239 VEVKVLKIDREKERISLSLKQLQPDPWENIAEKYPVGDVVKGKVTRLTDFGAFVELEPGVEGLVHISEMSWTKRVAHPSD 318
                        330       340
                 ....*....|....*....|....*....
gi 489056936 327 ILSTTQEVEVVVLEVDPVKRRISLGLKQT 355
Cdd:COG0539  319 VVKVGDEVEVKVLDIDPEERRISLSIKQL 347
S1_RPS1_repeat_ec3 cd05688
S1_RPS1_repeat_ec3: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
197-264 1.32e-35

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: 127.75  E-value: 1.32e-35
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489056936 197 EGQVVEGVVKNITDYGAFVDLGGIDGLLHVTDMAWRRVNHPSEILTIGQTVKVQIIRINQETHRISLG 264
Cdd:cd05688    1 EGDVVEGTVKSITDFGAFVDLGGVDGLLHISDMSWGRVKHPSEVVNVGDEVEVKVLKIDKERKRISLG 68
S1 smart00316
Ribosomal protein S1-like RNA-binding domain;
196-266 4.06e-20

Ribosomal protein S1-like RNA-binding domain;


Pssm-ID: 197648 [Multi-domain]  Cd Length: 72  Bit Score: 84.58  E-value: 4.06e-20
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489056936   196 EEGQVVEGVVKNITDYGAFVDLG-GIDGLLHVTDMAWRRVNHPSEILTIGQTVKVQIIRINQETHRISLGMK 266
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 ...
195-265 4.41e-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: 70.01  E-value: 4.41e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489056936  195 LEEGQVVEGVVKNITDYGAFVDLG-GIDGLLHVTDMAWRRVNHPSEILTIGQTVKVQIIRINQETHRISLGM 265
Cdd:pfam00575   1 PEKGDVVEGEVTRVTKGGAFVDLGnGVEGFIPISELSDDHVEDPDEVIKVGDEVKVKVLKVDKDRRRIILSI 72
S1_dom_CvfD NF040579
CvfD/Ygs/GSP13 family RNA-binding post-transcriptional regulator; CvfD, Ygs, and GSP13 form a ...
280-314 1.49e-09

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: 55.51  E-value: 1.49e-09
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 489056936 280 YPIGKKITGTVTNITDYGAFVEIEPGIEGLIHVSE 314
Cdd:NF040579   1 YKIGDIVEGKVTGIQPYGAFVALDEHTQGLIHISE 35
 
Name Accession Description Interval E-value
rpsA PRK06299
30S ribosomal protein S1; Reviewed
1-563 0e+00

30S ribosomal protein S1; Reviewed


Pssm-ID: 235775 [Multi-domain]  Cd Length: 565  Bit Score: 892.21  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936   1 MSQSNPTRADFESLLAESFAEHDLAEGYVVKGRIVAIEKDMAIIDAGLKVEGRVPLKEFGAKGKDGTLKPGDEVEVYVER 80
Cdd:PRK06299   5 AQNQNDMEESFAELFEESLKESETREGSIVKGTVVAIDKDYVLVDVGLKSEGRIPLEEFKNEQGELEVKVGDEVEVYVER 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936  81 IENALGEAVLSREKARREESWVKLEQKFANGERVDGVIFNQVKGGFTVDLDGAVAFLPRSQVDIRPIRDVTPLMHVPQPF 160
Cdd:PRK06299  85 IEDGFGETVLSREKAKRLEAWDKLEKAFENGEIVEGVINGKVKGGFTVDLNGVEAFLPGSQVDVRPVRDTDPLEGKELEF 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936 161 EILKMDKRRGNIVVSRRTVLEESRAEQRSEIVQNLEEGQVVEGVVKNITDYGAFVDLGGIDGLLHVTDMAWRRVNHPSEI 240
Cdd:PRK06299 165 KVIKLDKKRNNIVVSRRAVLEEERAEEREELLENLEEGQVVEGVVKNITDYGAFVDLGGVDGLLHITDISWKRVNHPSEV 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936 241 LTIGQTVKVQIIRINQETHRISLGMKQLESDPWDGIGAKYPIGKKITGTVTNITDYGAFVEIEPGIEGLIHVSEMSWTKK 320
Cdd:PRK06299 245 VNVGDEVKVKVLKFDKEKKRVSLGLKQLGEDPWEAIEKKYPVGSKVKGKVTNITDYGAFVELEEGIEGLVHVSEMSWTKK 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936 321 NVHPGKILSTTQEVEVVVLEVDPVKRRISLGLKQTLDNPWTTFAQKYPVGTVVEGEVKNKTEFGLFIGLDGDVDGMVHLS 400
Cdd:PRK06299 325 NKHPSKVVSVGQEVEVMVLEIDEEKRRISLGLKQCKENPWEEFAEKYPVGDVVEGKVKNITDFGAFVGLEGGIDGLVHLS 404
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936 401 DLDWNRPGEQVIEEYNKGEVVKAVVLDVDVEKERISLGIKQLSGDKVGEAAASgeLRKNAIVTCEVTAVTDGGLEVRLVD 480
Cdd:PRK06299 405 DISWDKKGEEAVELYKKGDEVEAVVLKVDVEKERISLGIKQLEEDPFEEFAKK--HKKGSIVTGTVTEVKDKGAFVELED 482
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936 481 hDLDSFIRRSDLSRDRDEQRPERFTVGQKVDARVIAFDKKTSKLQVSIKALEIAEEKEAVAQYGS-SDSGASLGDILGAA 559
Cdd:PRK06299 483 -GVEGLIRASELSRDRVEDATEVLKVGDEVEAKVINIDRKNRRISLSIKALDEAEEKEAIAEYNSaSDSKTTLGDLLKAA 561

                 ....
gi 489056936 560 LKKQ 563
Cdd:PRK06299 562 LKGK 565
rpsA TIGR00717
ribosomal protein S1; This model describes ribosomal protein S1, RpsA. This protein is found ...
9-529 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: 577.84  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936    9 ADFESLLAESFAEHDLAEGYVVKGRIVAIEKDMAIIDAGLKVEGRVPLKEFgaKGKDGTLKPGDEVEVYVERIENALGEA 88
Cdd:TIGR00717   1 ESFAQLLEESLKTEETRPGSIVKGTVVAINKDTVFVDVGLKSEGRIPKEEF--LDAPLEIQVGDEVEVYLDRVEDRFGET 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936   89 VLSREKARREESWVKLEQKFANGERVDGVIFNQVKGGFTVDLDGAVAFLPRSQVDIRPIRDVTPLMHVPQPFEILKMDKR 168
Cdd:TIGR00717  79 VLSREKAQRHELWIKLEKAYEEGSIVEGKIVGKVKGGFIVDLNGVEAFLPGSQVDVKPIKDLDSLIGKTLKFKIIKLDQK 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936  169 RGNIVVSRRTVLEESRAEQRSEIVQNLEEGQVVEGVVKNITDYGAFVDLGGIDGLLHVTDMAWRRVNHPSEILTIGQTVK 248
Cdd:TIGR00717 159 RNNIVVSRRAYLEEERSQAREELLENLKEGDVVKGVVKNITDFGAFVDLGGVDGLLHITDMSWKRVKHPSEYVKVGQEVK 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936  249 VQIIRINQETHRISLGMKQLESDPWDGIGAKYPIGKKITGTVTNITDYGAFVEIEPGIEGLIHVSEMSWTKKNVHPGKIL 328
Cdd:TIGR00717 239 VKVIKFDKEKGRISLSLKQLGEDPWEAIEKKFPVGDKITGRVTNLTDYGVFVEIEEGIEGLVHVSEMSWVKKNSHPSKVV 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936  329 STTQEVEVVVLEVDPVKRRISLGLKQTLDNPWTTFAQKYPVGTVVEGEVKNKTEFGLFIGLDGDVDGMVHLSDLDWNRPG 408
Cdd:TIGR00717 319 KKGDEVEVMILDIDPERRRLSLGLKQCKANPWEQFEEKHPVGDRVTGKIKKITDFGAFVELEGGIDGLIHLSDISWDKDG 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936  409 EQVIEEYNKGEVVKAVVLDVDVEKERISLGIKQLSGDKVGEAAAsgELRKNAIVTCEVTAVTDGGLEVRLvDHDLDSFIR 488
Cdd:TIGR00717 399 READHLYKKGDEIEAVVLAVDKEKKRISLGVKQLTENPWEKFAA--KYKVGSVVKGKVTEIKDFGAFVEL-PGGVEGLIR 475
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|.
gi 489056936  489 RSDLSRDRDEQRPERFTVGQKVDARVIAFDKKTSKLQVSIK 529
Cdd:TIGR00717 476 NSELSENRDEDKTDEIKVGDEVEAKVVDIDKKNRKVSLSVK 516
RpsA COG0539
Ribosomal protein S1 [Translation, ribosomal structure and biogenesis]; Ribosomal protein S1 ...
7-355 0e+00

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


Pssm-ID: 440305 [Multi-domain]  Cd Length: 348  Bit Score: 522.68  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936   7 TRADFESLLAESFAEhdLAEGYVVKGRIVAIEKDMAIIDAGLKVEGRVPLKEFGAKGKDGTLKPGDEVEVYVERIENALG 86
Cdd:COG0539    1 MSESFAELLEESLKE--LKEGDIVKGTVVSIDDDEVLVDIGYKSEGIIPLSEFSDEPGELEVKVGDEVEVYVEKVEDGEG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936  87 EAVLSREKARREESWVKLEQKFANGERVDGVIFNQVKGGFTVDLDGAVAFLPRSQVDIRPIRDVTPLMHVPQPFEILKMD 166
Cdd:COG0539   79 EIVLSKKKADREKAWEELEEAFENGEPVEGKVKGVVKGGLIVDIGGVRAFLPASQVDVRPVRDLDEYVGKTLEFKIIKLD 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936 167 KRRGNIVVSRRTVLEESRAEQRSEIVQNLEEGQVVEGVVKNITDYGAFVDLGGIDGLLHVTDMAWRRVNHPSEILTIGQT 246
Cdd:COG0539  159 RKRNNVVVSRRAVLEEEREEKREELLEKLEEGDVVEGTVKNITDFGAFVDLGGVDGLLHISEISWGRVKHPSEVLKVGDE 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936 247 VKVQIIRINQETHRISLGMKQLESDPWDGIGAKYPIGKKITGTVTNITDYGAFVEIEPGIEGLIHVSEMSWTKKNVHPGK 326
Cdd:COG0539  239 VEVKVLKIDREKERISLSLKQLQPDPWENIAEKYPVGDVVKGKVTRLTDFGAFVELEPGVEGLVHISEMSWTKRVAHPSD 318
                        330       340
                 ....*....|....*....|....*....
gi 489056936 327 ILSTTQEVEVVVLEVDPVKRRISLGLKQT 355
Cdd:COG0539  319 VVKVGDEVEVKVLDIDPEERRISLSIKQL 347
PRK00087 PRK00087
bifunctional 4-hydroxy-3-methylbut-2-enyl diphosphate reductase/30S ribosomal protein S1;
11-368 5.25e-110

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


Pssm-ID: 234623 [Multi-domain]  Cd Length: 647  Bit Score: 342.31  E-value: 5.25e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936  11 FESLLAESFAEHDLAEGYVVKGRIVAIEKDMAIIDAGLKVEGRVPLKEFGAKGKDGTL---KPGDEVEVYVERIENALGE 87
Cdd:PRK00087 287 NEQLEYMNELEKQIRRGDIVKGTVVSVNENEVFVDVGYKSEGVIPLRELTLDEISSLKesvKVGDEIEVKVLKLEDEDGY 366
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936  88 AVLSREKARREESWVKLEQKFANGERVDGVIFNQVKGGFTVDLDGAVAFLPRSQVDIRPIRDVTPLMHVPQPFEILKMD- 166
Cdd:PRK00087 367 VVLSKKEADREKAWKELEEAFENGEPVKGKVKEVVKGGLLVDYGGVRAFLPASHVELGYVEDLSEYKGQELEVKIIEFNr 446
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936 167 KRRGNIVVSRRTVLEESRAEQRSEIVQNLEEGQVVEGVVKNITDYGAFVDLGGIDGLLHVTDMAWRRVNHPSEILTIGQT 246
Cdd:PRK00087 447 KRRKKVVLSRKAILEEEKEKKKEETWNSLEEGDVVEGEVKRLTDFGAFVDIGGVDGLLHVSEISWGRVEKPSDVLKVGDE 526
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936 247 VKVQIIRINQETHRISLGMKQLESDPWDGIGAKYPIGKKITGTVTNITDYGAFVEIEPGIEGLIHVSEMSWtKKNVHPGK 326
Cdd:PRK00087 527 IKVYILDIDKENKKLSLSLKKLLPDPWENVEEKYPVGSIVLGKVVRIAPFGAFVELEPGVDGLVHISQISW-KRIDKPED 605
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 489056936 327 ILSTTQEVEVVVLEVDPVKRRISLGLKQTLDNPWTTFAQKYP 368
Cdd:PRK00087 606 VLSEGEEVKAKILEVDPEEKRIRLSIKEVEEEPGDIEKVELE 647
rpsA PRK13806
30S ribosomal protein S1; Provisional
4-460 4.99e-109

30S ribosomal protein S1; Provisional


Pssm-ID: 237516 [Multi-domain]  Cd Length: 491  Bit Score: 335.16  E-value: 4.99e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936   4 SNPTRADFESLLA--ESFAEHDLAEGYVVKGRIVAIEKDMAIIDAGLKVEGRVPLKEFGAKGKDGTLKPGDEVEVYVERI 81
Cdd:PRK13806  10 ELDESESFAELLEayEGERKTELRVGDKITGTVIAITEDSVFVDTGSKVDGVVDRAELLDADGELTVAVGDEVELYVVSV 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936  82 ENalGEAVLSReKARREESWVKLEQKFANGERVDGVIFNQVKGGFTVDLDGAVAFLPRSQVDIRPIRDvtPLMHVPQ--P 159
Cdd:PRK13806  90 NG--QEIRLSK-ALSGQGGAAMLEEAYENGVPVEGKVTGTCKGGFNVEVLGRRAFCPVSQIDLRYVED--PESYVGQtfQ 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936 160 FEILKMDKRRGNIVVSRRTVLEESRAEQRSEIVQNLEEGQVVEGVVKNITDYGAFVDLG-GIDGLLHVTDMAWRRVNHPS 238
Cdd:PRK13806 165 FLITRVEENGRNIVVSRRALLEREQKEALEAFMETVKEGDVVEGTVTRLAPFGAFVELApGVEGMVHISELSWSRVQKAD 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936 239 EILTIGQTVKVQIIRINQETH----RISLGMKQLESDPWDGIGAKYPIGKKITGTVTNITDYGAFVEIEPGIEGLIHVSE 314
Cdd:PRK13806 245 EAVSVGDTVRVKVLGIERAKKgkglRISLSIKQAGGDPWDTVGDRLKAGDKVTGKVVRLAPFGAFVEILPGIEGLVHVSE 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936 315 MSWTKKNVHPGKILSTTQEVEVVVLEVDPVKRRISLGLKQTLDNPWTTFAQKYPVGTVVEGEVKNKTEFGLFIGLDGDVD 394
Cdd:PRK13806 325 MSWTRRVNKPEDVVAPGDAVAVKIKDIDPAKRRISLSLRDAEGDPWADVAERFAPGTTVTGTVEKRAQFGLFVNLAPGVT 404
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489056936 395 GMVHLSDLDwNRPGEQVIEEYNKGEVVKAVVLDVDVEKERISLGikqlSGDKVGEAAASGELRKNA 460
Cdd:PRK13806 405 GLLPASVIS-RAGKPATYEKLKPGDSVTLVVEEIDTAKRKISLA----PAGAAGSGADDDDWKQFA 465
rpsA PRK06676
30S ribosomal protein S1; Reviewed
11-359 7.97e-102

30S ribosomal protein S1; Reviewed


Pssm-ID: 235851 [Multi-domain]  Cd Length: 390  Bit Score: 312.96  E-value: 7.97e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936  11 FESLLAESFAE-HDLAEGYVVKGRIVAIEKDMAIID-AGLKVEGRVPLKEF----GAKGKDgTLKPGDEVEVYVERIENA 84
Cdd:PRK06676   1 MMEEFEESLNSvKEVEVGDVVTGEVLKVEDKQVFVNiEGYKVEGVIPISELsndhIEDIND-VVKVGDELEVYVLKVEDG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936  85 LGEAVLSREKARREESWVKLEQKFANGERVDGVIFNQVKGGFTVDLDGAVAFLPRSQVDIRPIRDVTPLMHVPQPFEILK 164
Cdd:PRK06676  80 EGNLLLSKRRLEAEKAWDKLEEKFEEGEVVEVKVTEVVKGGLVVDVEGVRGFIPASLISTRFVEDFSDFKGKTLEVKIIE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936 165 MDKRRGNIVVSRRTVLEESRAEQRSEIVQNLEEGQVVEGVVKNITDYGAFVDLGGIDGLLHVTDMAWRRVNHPSEILTIG 244
Cdd:PRK06676 160 LDPEKNRVILSRRAVVEEERAAKKEELLSSLKEGDVVEGTVARLTDFGAFVDIGGVDGLVHISELSHERVEKPSEVVSVG 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936 245 QTVKVQIIRINQETHRISLGMKQLESDPWDGIGAKYPIGKKITGTVTNITDYGAFVEIEPGIEGLIHVSEMSWtkKNV-H 323
Cdd:PRK06676 240 QEVEVKVLSIDWETERISLSLKDTLPGPWEGVEEKLPEGDVIEGTVKRLTDFGAFVEVLPGVEGLVHISQISH--KHIaT 317
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 489056936 324 PGKILSTTQEVEVVVLEVDPVKRRISLGLKQTLDNP 359
Cdd:PRK06676 318 PSEVLEEGQEVKVKVLEVNEEEKRISLSIKALEEAP 353
PRK12269 PRK12269
bifunctional cytidylate kinase/ribosomal protein S1; Provisional
15-563 1.21e-95

bifunctional cytidylate kinase/ribosomal protein S1; Provisional


Pssm-ID: 105491 [Multi-domain]  Cd Length: 863  Bit Score: 310.49  E-value: 1.21e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936  15 LAESFAEHDLAEGYVVKGRIVAIEKDMAIIDAGLKVEGRVPLKEFGAKGKdgtlkPGDEVEVYVERIENALGEavLSREK 94
Cdd:PRK12269 310 LQERYSFEAPEPGSVRMGTVVQVNAGTVFVDIGGKSEGRVPVEEFEAPPK-----AGDGVRVYVERVTPYGPE--LSKTK 382
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936  95 ARREESWVKLEQKFANGERVDGVI--FNQVKGGFTVDLD-GAVAFLPRSQVDIRPIRDVTPLMHVPQPFEILKMDK---R 168
Cdd:PRK12269 383 ADRLGLKVKLRDAERDGTPVEGRIvrLTEKKSGFEVDLGaGMMAFLPISQSDCQKVDAPESLIGLTSKFYIERISQskqH 462
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936 169 RGN--IVVSRRTVLEESRAEQRSEIVQNLEEGQVVEGVVKNITDYGAFVDLGGIDGLLHVTDMAWRRVNHPSEILTIGQT 246
Cdd:PRK12269 463 RGNdnIVINRRRYLEERARQAREEFFNSVHIEDSVSGVVKSFTSFGAFIDLGGFDGLLHVNDMSWGHVARPREFVKKGQT 542
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936 247 VKVQIIRINQETHRISLGMKQLESDPWDGIGAKYPIGKKITGTVTNITDYGAFVEIEPGIEGLIHVSEMSWTKKNVHPGK 326
Cdd:PRK12269 543 IELKVIRLDQAEKRINLSLKHFQPDPWLEFENKFGVNDVVKGRVTKIADFGAFIELAEGIEGLAHISEFSWVKKTSKPSD 622
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936 327 ILSTTQEVEVVVLEVDPVKRRISLGLKQTLDNPWTTFAQKYPVGTVVEGEVKNKTEFGLFIGLDGDVDGMVHLSDLDWNR 406
Cdd:PRK12269 623 MVKIGDEVECMILGYDIQAGRVSLGLKQVTANPWEEIEARYPVGARFTRRIVKVTNAGAFIEMEEGIDGFLHVDDLSWVK 702
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936 407 PGEQVIEEYNKGEVVKAVVLDVDVEKERISLGIKQLSgDKVGEAAASGeLRKNAIVTCEVTAVTDGGLEVRlVDHDLDSF 486
Cdd:PRK12269 703 RTRPADHELEVGKEIECMVIECDPQARRIRLGVKQLS-DNPWQVFANA-YGVGSTVEGEVSSVTDFGIFVR-VPGGVEGL 779
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936 487 IRRSDLSRDRDEQRPE---RFTVGQKVDARVIAFDKKTSKLQVSIKALEIAEEKEAVAQYGSSDSGASLGDILGAALKKQ 563
Cdd:PRK12269 780 VRKQHLVENRDGDPGEalrKYAVGDRVKAVIVDMNVKDRKVAFSVRDYQRKVQRDELSRYMSAPRGEDEGSFTLGDLMRQ 859
rpsA PRK07899
30S ribosomal protein S1; Reviewed
26-354 2.30e-76

30S ribosomal protein S1; Reviewed


Pssm-ID: 236126 [Multi-domain]  Cd Length: 486  Bit Score: 249.96  E-value: 2.30e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936  26 EGYVVKGRIVAIEKDMAIIDAGLKVEGRVPLKEFGAK---GKDGTLKPGDEVEVYVERIENALGEAVLSREKARREESWV 102
Cdd:PRK07899  35 DGDIVEGTVVKVDRDEVLLDIGYKTEGVIPSRELSIKhdvDPNEVVEVGDEVEALVLQKEDKEGRLILSKKRAQYERAWG 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936 103 KLEQKFANGERVDGVIFNQVKGGFTVDLdGAVAFLPRSQVDIRPIRDVTPlmHVPQPFE--ILKMDKRRGNIVVSRRTVL 180
Cdd:PRK07899 115 TIEKIKEKDGVVTGTVIEVVKGGLILDI-GLRGFLPASLVEMRRVRDLQP--YIGQEIEakIIELDKNRNNVVLSRRAWL 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936 181 EESRAEQRSEIVQNLEEGQVVEGVVKNITDYGAFVDLGGIDGLLHVTDMAWRRVNHPSEILTIGQTVKVQIIRINQETHR 260
Cdd:PRK07899 192 EQTQSEVRSEFLNQLQKGQVRKGVVSSIVNFGAFVDLGGVDGLVHVSELSWKHIDHPSEVVEVGQEVTVEVLDVDMDRER 271
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936 261 ISLGMKQLESDPWDGIGAKYPIGKKITGTVTNITDYGAFVEIEPGIEGLIHVSEMSwtKKNVH-PGKILSTTQEVEVVVL 339
Cdd:PRK07899 272 VSLSLKATQEDPWQQFARTHAIGQIVPGKVTKLVPFGAFVRVEEGIEGLVHISELA--ERHVEvPEQVVQVGDEVFVKVI 349
                        330
                 ....*....|....*
gi 489056936 340 EVDPVKRRISLGLKQ 354
Cdd:PRK07899 350 DIDLERRRISLSLKQ 364
S1_RPS1_repeat_ec3 cd05688
S1_RPS1_repeat_ec3: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
197-264 1.32e-35

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: 127.75  E-value: 1.32e-35
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489056936 197 EGQVVEGVVKNITDYGAFVDLGGIDGLLHVTDMAWRRVNHPSEILTIGQTVKVQIIRINQETHRISLG 264
Cdd:cd05688    1 EGDVVEGTVKSITDFGAFVDLGGVDGLLHISDMSWGRVKHPSEVVNVGDEVEVKVLKIDKERKRISLG 68
PRK07400 PRK07400
30S ribosomal protein S1; Reviewed
7-274 1.97e-34

30S ribosomal protein S1; Reviewed


Pssm-ID: 180960 [Multi-domain]  Cd Length: 318  Bit Score: 132.62  E-value: 1.97e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936   7 TRADFESLLAESfaEHDLAEGYVVKGRIVAIEKDMAIIDAGLKVEGRVPLKEFG---AKGKDGTLKPGDEVEVYVERIEN 83
Cdd:PRK07400  14 THEDFAALLDKY--DYHFKPGDIVNGTVFSLEPRGALIDIGAKTAAFMPIQEMSinrVEGPEEVLQPNETREFFILSDEN 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936  84 ALGEAVLSREKARREESWVKLEQKFANGERVDGVIFNQVKGGFTVDLDGAVAFLPRSQVDIRPIRDvtPLMHVPQPFEIL 163
Cdd:PRK07400  92 EDGQLTLSIRRIEYMRAWERVRQLQKEDATVRSEVFATNRGGALVRIEGLRGFIPGSHISTRKPKE--ELVGEELPLKFL 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936 164 KMDKRRGNIVVSRRTVLEESRaeqrseiVQNLEEGQVVEGVVKNITDYGAFVDLGGIDGLLHVTDMAWRRVNHPSEILTI 243
Cdd:PRK07400 170 EVDEERNRLVLSHRRALVERK-------MNRLEVGEVVVGTVRGIKPYGAFIDIGGVSGLLHISEISHEHIETPHSVFNV 242
                        250       260       270
                 ....*....|....*....|....*....|.
gi 489056936 244 GQTVKVQIIRINQETHRISLGMKQLESDPWD 274
Cdd:PRK07400 243 NDEMKVMIIDLDAERGRISLSTKQLEPEPGD 273
S1_RPS1_repeat_ec5 cd05690
S1_RPS1_repeat_ec5: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
370-438 3.47e-24

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: 96.02  E-value: 3.47e-24
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489056936 370 GTVVEGEVKNKTEFGLFIGLDGDVDGMVHLSDLDWNRPGEQVIEEYNKGEVVKAVVLDVDVEKERISLG 438
Cdd:cd05690    1 GTVVSGKIKSITDFGIFVGLDGGIDGLVHISDISWTQRVRHPSEIYKKGQEVEAVVLNIDVERERISLG 69
S1_RPS1_repeat_ec4 cd05689
S1_RPS1_repeat_ec4: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
280-351 5.64e-24

S1_RPS1_repeat_ec4: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ribosomal subunit thought to be involved in the recognition and binding of mRNA's during translation initiation. The bacterial RPS1 domain architecture consists of 4-6 tandem S1 domains. In some bacteria, the tandem S1 array is located C-terminal to a 4-hydroxy-3-methylbut-2-enyl diphosphate reductase (HMBPP reductase) domain. While RPS1 is found primarily in bacteria, proteins with tandem RPS1-like domains have been identified in plants and humans, however these lack the N-terminal HMBPP reductase domain. This CD includes S1 repeat 4 (ec4) of the Escherichia coli RPS1. Autoantibodies to double-stranded DNA from patients with systemic lupus erythematosus cross-react with the human RPS1 homolog.


Pssm-ID: 240194 [Multi-domain]  Cd Length: 72  Bit Score: 95.34  E-value: 5.64e-24
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489056936 280 YPIGKKITGTVTNITDYGAFVEIEPGIEGLIHVSEMSWTKKNVHPGKILSTTQEVEVVVLEVDPVKRRISLG 351
Cdd:cd05689    1 YPEGTRLFGKVTNLTDYGCFVELEEGVEGLVHVSEMDWTNKNIHPSKVVSLGDEVEVMVLDIDEERRRISLG 72
S1_RPS1_repeat_ec6 cd05691
S1_RPS1_repeat_ec6: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
459-532 2.39e-23

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


Pssm-ID: 240196 [Multi-domain]  Cd Length: 73  Bit Score: 93.49  E-value: 2.39e-23
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489056936 459 NAIVTCEVTAVTDGGLEVRLVDhDLDSFIRRSDLSRDRDEQRPERFTVGQKVDARVIAFDKKTSKLQVSIKALE 532
Cdd:cd05691    1 GSIVTGKVTEVDAKGATVKLGD-GVEGFLRAAELSRDRVEDATERFKVGDEVEAKITNVDRKNRKISLSIKAKE 73
S1_RPS1_repeat_ec2_hs2 cd04465
S1_RPS1_repeat_ec2_hs2: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
111-177 4.23e-21

S1_RPS1_repeat_ec2_hs2: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ribosomal subunit thought to be involved in the recognition and binding of mRNA's during translation initiation. The bacterial RPS1 domain architecture consists of 4-6 tandem S1 domains. In some bacteria, the tandem S1 array is located C-terminal to a 4-hydroxy-3-methylbut-2-enyl diphosphate reductase (HMBPP reductase) domain.While RPS1 is found primarily in bacteria, proteins with tandem RPS1-like domains have been identified in plants and humans, however these lack the N-terminal HMBPP reductase domain. This CD includes S1 repeat 2 of the Escherichia coli and Homo sapiens RPS1 (ec2 and hs2, respectively). Autoantibodies to double-stranded DNA from patients with systemic lupus erythematosus cross-react with the human RPS1 homolog.


Pssm-ID: 239911 [Multi-domain]  Cd Length: 67  Bit Score: 87.13  E-value: 4.23e-21
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489056936 111 GERVDGVIFNQVKGGFTVDLDGAVAFLPRSQVDIRPIRDVTPLMHVPQPFEILKMDKRRGNIVVSRR 177
Cdd:cd04465    1 GEIVEGKVTEKVKGGLIVDIEGVRAFLPASQVDLRPVEDLDEYVGKELKFKIIEIDRERNNIVLSRR 67
S1 smart00316
Ribosomal protein S1-like RNA-binding domain;
196-266 4.06e-20

Ribosomal protein S1-like RNA-binding domain;


Pssm-ID: 197648 [Multi-domain]  Cd Length: 72  Bit Score: 84.58  E-value: 4.06e-20
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489056936   196 EEGQVVEGVVKNITDYGAFVDLG-GIDGLLHVTDMAWRRVNHPSEILTIGQTVKVQIIRINQETHRISLGMK 266
Cdd:smart00316   1 EVGDVVEGTVTEITPGGAFVDLGnGVEGLIPISELSDKRVKDPEEVLKVGDEVKVKVLSVDEEKGRIILSLK 72
Tex COG2183
Transcriptional accessory protein Tex/SPT6 [Transcription];
195-272 2.62e-19

Transcriptional accessory protein Tex/SPT6 [Transcription];


Pssm-ID: 441786 [Multi-domain]  Cd Length: 719  Bit Score: 91.63  E-value: 2.62e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936 195 LEEGQVVEGVVKNITDYGAFVDLGgI--DGLLHVTDMAWRRVNHPSEILTIGQTVKVQIIRINQETHRISLGMKQLESDP 272
Cdd:COG2183  639 LKPGMILEGTVTNVTDFGAFVDIG-VhqDGLVHISQLSDRFVKDPREVVKVGDIVKVKVLEVDLKRKRISLSMKLDDEAG 717
PRK11824 PRK11824
polynucleotide phosphorylase/polyadenylase; Provisional
190-269 5.92e-19

polynucleotide phosphorylase/polyadenylase; Provisional


Pssm-ID: 236995 [Multi-domain]  Cd Length: 693  Bit Score: 90.49  E-value: 5.92e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936 190 EIVQNLEEGQVVEGVVKNITDYGAFVD-LGGIDGLLHVTDMAWRRVNHPSEILTIGQTVKVQIIRINqETHRISLGMKQL 268
Cdd:PRK11824 614 GITAEPEVGEIYEGKVVRIVDFGAFVEiLPGKDGLVHISEIADERVEKVEDVLKEGDEVKVKVLEID-KRGRIRLSRKAV 692

                 .
gi 489056936 269 E 269
Cdd:PRK11824 693 L 693
S1_Tex cd05685
S1_Tex: The C-terminal S1 domain of a transcription accessory factor called Tex, which has ...
198-263 1.05e-18

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


Pssm-ID: 240190 [Multi-domain]  Cd Length: 68  Bit Score: 80.35  E-value: 1.05e-18
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489056936 198 GQVVEGVVKNITDYGAFVDLG-GIDGLLHVTDMAWRRVNHPSEILTIGQTVKVQIIRINQETHRISL 263
Cdd:cd05685    1 GMVLEGVVTNVTDFGAFVDIGvKQDGLIHISKMADRFVSHPSDVVSVGDIVEVKVISIDEERGRISL 67
S1_RPS1_repeat_ec5 cd05690
S1_RPS1_repeat_ec5: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
198-264 1.65e-18

S1_RPS1_repeat_ec5: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ribosomal subunit thought to be involved in the recognition and binding of mRNA's during translation initiation. The bacterial RPS1 domain architecture consists of 4-6 tandem S1 domains. In some bacteria, the tandem S1 array is located C-terminal to a 4-hydroxy-3-methylbut-2-enyl diphosphate reductase (HMBPP reductase) domain. While RPS1 is found primarily in bacteria, proteins with tandem RPS1-like domains have been identified in plants and humans, however these lack the N-terminal HMBPP reductase domain. This CD includes S1 repeat 5 (ec5) of the Escherichia coli RPS1. Autoantibodies to double-stranded DNA from patients with systemic lupus erythematosus cross-react with the human RPS1 homolog.


Pssm-ID: 240195 [Multi-domain]  Cd Length: 69  Bit Score: 79.85  E-value: 1.65e-18
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489056936 198 GQVVEGVVKNITDYGAFVDL-GGIDGLLHVTDMAW-RRVNHPSEILTIGQTVKVQIIRINQETHRISLG 264
Cdd:cd05690    1 GTVVSGKIKSITDFGIFVGLdGGIDGLVHISDISWtQRVRHPSEIYKKGQEVEAVVLNIDVERERISLG 69
S1_DHX8_helicase cd05684
S1_DHX8_helicase: The N-terminal S1 domain of human ATP-dependent RNA helicase DHX8, a DEAH ...
198-266 2.41e-16

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: 73.81  E-value: 2.41e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489056936 198 GQVVEGVVKNITDYGAFVDL----GGIDGLLHVTDMAW-RRVNHPSEILTIGQTVKVQIIRINQEthRISLGMK 266
Cdd:cd05684    1 GKIYKGKVTSIMDFGCFVQLeglkGRKEGLVHISQLSFeGRVANPSDVVKRGQKVKVKVISIQNG--KISLSMK 72
YabR COG1098
Predicted RNA-binding protein, contains ribosomal protein S1 (RPS1) domain [General function ...
194-272 7.76e-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: 74.06  E-value: 7.76e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936 194 NLEEGQVVEGVVKNITDYGAFVDL-GGIDGLLHVTDMAWRRVNHPSEILTIGQTVKVQIIRINqETHRISLGMKQLESDP 272
Cdd:COG1098    2 SIEVGDIVEGKVTGITPFGAFVELpEGTTGLVHISEIADGYVKDINDYLKVGDEVKVKVLSID-EDGKISLSIKQAEEKP 80
S1_RPS1_repeat_ec3 cd05688
S1_RPS1_repeat_ec3: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
369-438 8.49e-16

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: 71.89  E-value: 8.49e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489056936 369 VGTVVEGEVKNKTEFGLFIGLdGDVDGMVHLSDLDWNR---PGEQVieeyNKGEVVKAVVLDVDVEKERISLG 438
Cdd:cd05688    1 EGDVVEGTVKSITDFGAFVDL-GGVDGLLHISDMSWGRvkhPSEVV----NVGDEVEVKVLKIDKERKRISLG 68
S1_RPS1_repeat_ec1_hs1 cd05687
S1_RPS1_repeat_ec1_hs1: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
27-93 1.19e-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: 71.79  E-value: 1.19e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489056936  27 GYVVKGRIVAIEKDMAIIDAGLKVEGRVPLKEFG----AKGKDgTLKPGDEVEVYVERIENALGEAVLSRE 93
Cdd:cd05687    1 GDIVKGTVVSVDDDEVLVDIGYKSEGIIPISEFSddpiENGED-EVKVGDEVEVYVLRVEDEEGNVVLSKR 70
S1 pfam00575
S1 RNA binding domain; The S1 domain occurs in a wide range of RNA associated proteins. It is ...
195-265 4.41e-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: 70.01  E-value: 4.41e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489056936  195 LEEGQVVEGVVKNITDYGAFVDLG-GIDGLLHVTDMAWRRVNHPSEILTIGQTVKVQIIRINQETHRISLGM 265
Cdd:pfam00575   1 PEKGDVVEGEVTRVTKGGAFVDLGnGVEGFIPISELSDDHVEDPDEVIKVGDEVKVKVLKVDKDRRRIILSI 72
S1_Rrp5_repeat_sc12 cd05708
S1_Rrp5_repeat_sc12: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ...
196-266 5.56e-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: 70.05  E-value: 5.56e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489056936 196 EEGQVVEGVVKNITDYGAFVDLGGID--GLLHVTDMAWRRVNHPSEILTIGQTVKVQIIRINQETHRISLGMK 266
Cdd:cd05708    1 KVGQKIDGTVRRVEDYGVFIDIDGTNvsGLCHKSEISDNRVADASKLFRVGDKVRAKVLKIDAEKKRISLGLK 73
S1_Rrp5_repeat_sc12 cd05708
S1_Rrp5_repeat_sc12: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ...
369-440 7.98e-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: 7.98e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489056936 369 VGTVVEGEVKNKTEFGLFIGLDG-DVDGMVHLSDLDWNRPGEqVIEEYNKGEVVKAVVLDVDVEKERISLGIK 440
Cdd:cd05708    2 VGQKIDGTVRRVEDYGVFIDIDGtNVSGLCHKSEISDNRVAD-ASKLFRVGDKVRAKVLKIDAEKKRISLGLK 73
S1_RPS1_repeat_ec5 cd05690
S1_RPS1_repeat_ec5: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
283-351 9.44e-15

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: 69.06  E-value: 9.44e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489056936 283 GKKITGTVTNITDYGAFVEIEPGIEGLIHVSEMSWTKKNVHPGKILSTTQEVEVVVLEVDPVKRRISLG 351
Cdd:cd05690    1 GTVVSGKIKSITDFGIFVGLDGGIDGLVHISDISWTQRVRHPSEIYKKGQEVEAVVLNIDVERERISLG 69
S1 pfam00575
S1 RNA binding domain; The S1 domain occurs in a wide range of RNA associated proteins. It is ...
367-439 1.10e-14

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


Pssm-ID: 425760 [Multi-domain]  Cd Length: 72  Bit Score: 68.85  E-value: 1.10e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489056936  367 YPVGTVVEGEVKNKTEFGLFIGLDGDVDGMVHLSDLDWNRpGEQVIEEYNKGEVVKAVVLDVDVEKERISLGI 439
Cdd:pfam00575   1 PEKGDVVEGEVTRVTKGGAFVDLGNGVEGFIPISELSDDH-VEDPDEVIKVGDEVKVKVLKVDKDRRRIILSI 72
S1_like cd00164
S1_like: Ribosomal protein S1-like RNA-binding domain. Found in a wide variety of ...
201-264 1.48e-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: 68.56  E-value: 1.48e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489056936 201 VEGVVKNITDYGAFVDLG-GIDGLLHVTDMAWRRVNHPSEILTIGQTVKVQIIRINQETHRISLG 264
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 ...
198-266 1.74e-14

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


Pssm-ID: 240197 [Multi-domain]  Cd Length: 69  Bit Score: 68.47  E-value: 1.74e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936 198 GQVVEGVVKNITDYGAFVDLG-GIDGLLHVTDMAWRRVNHPSEILTIGQTVKVQIIRINQEThRISLGMK 266
Cdd:cd05692    1 GSVVEGTVTRLKPFGAFVELGgGISGLVHISQIAHKRVKDVKDVLKEGDKVKVKVLSIDARG-RISLSIK 69
S1 smart00316
Ribosomal protein S1-like RNA-binding domain;
369-440 2.65e-14

Ribosomal protein S1-like RNA-binding domain;


Pssm-ID: 197648 [Multi-domain]  Cd Length: 72  Bit Score: 68.01  E-value: 2.65e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489056936   369 VGTVVEGEVKNKTEFGLFIGLDGDVDGMVHLSDLDWNRpGEQVIEEYNKGEVVKAVVLDVDVEKERISLGIK 440
Cdd:smart00316   2 VGDVVEGTVTEITPGGAFVDLGNGVEGLIPISELSDKR-VKDPEEVLKVGDEVKVKVLSVDEEKGRIILSLK 72
S1_RPS1_repeat_ec4 cd05689
S1_RPS1_repeat_ec4: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
197-264 1.12e-13

S1_RPS1_repeat_ec4: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ribosomal subunit thought to be involved in the recognition and binding of mRNA's during translation initiation. The bacterial RPS1 domain architecture consists of 4-6 tandem S1 domains. In some bacteria, the tandem S1 array is located C-terminal to a 4-hydroxy-3-methylbut-2-enyl diphosphate reductase (HMBPP reductase) domain. While RPS1 is found primarily in bacteria, proteins with tandem RPS1-like domains have been identified in plants and humans, however these lack the N-terminal HMBPP reductase domain. This CD includes S1 repeat 4 (ec4) of the Escherichia coli RPS1. Autoantibodies to double-stranded DNA from patients with systemic lupus erythematosus cross-react with the human RPS1 homolog.


Pssm-ID: 240194 [Multi-domain]  Cd Length: 72  Bit Score: 66.06  E-value: 1.12e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936 197 EGQVVEGVVKNITDYGAFVDLG-GIDGLLHVTDMAWRRVN-HPSEILTIGQTVKVQIIRINQETHRISLG 264
Cdd:cd05689    3 EGTRLFGKVTNLTDYGCFVELEeGVEGLVHVSEMDWTNKNiHPSKVVSLGDEVEVMVLDIDEERRRISLG 72
S1_RPS1_repeat_ec4 cd05689
S1_RPS1_repeat_ec4: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
367-438 5.12e-13

S1_RPS1_repeat_ec4: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ribosomal subunit thought to be involved in the recognition and binding of mRNA's during translation initiation. The bacterial RPS1 domain architecture consists of 4-6 tandem S1 domains. In some bacteria, the tandem S1 array is located C-terminal to a 4-hydroxy-3-methylbut-2-enyl diphosphate reductase (HMBPP reductase) domain. While RPS1 is found primarily in bacteria, proteins with tandem RPS1-like domains have been identified in plants and humans, however these lack the N-terminal HMBPP reductase domain. This CD includes S1 repeat 4 (ec4) of the Escherichia coli RPS1. Autoantibodies to double-stranded DNA from patients with systemic lupus erythematosus cross-react with the human RPS1 homolog.


Pssm-ID: 240194 [Multi-domain]  Cd Length: 72  Bit Score: 64.14  E-value: 5.12e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489056936 367 YPVGTVVEGEVKNKTEFGLFIGLDGDVDGMVHLSDLDWNRPGEQVIEEYNKGEVVKAVVLDVDVEKERISLG 438
Cdd:cd05689    1 YPEGTRLFGKVTNLTDYGCFVELEEGVEGLVHVSEMDWTNKNIHPSKVVSLGDEVEVMVLDIDEERRRISLG 72
PRK08059 PRK08059
general stress protein 13; Validated
194-272 2.66e-12

general stress protein 13; Validated


Pssm-ID: 181215 [Multi-domain]  Cd Length: 123  Bit Score: 63.91  E-value: 2.66e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936 194 NLEEGQVVEGVVKNITDYGAFVDL-GGIDGLLHVTDMAWRRVNHPSEILTIGQTVKVQIIRINQETHRISLGMKQLESDP 272
Cdd:PRK08059   4 QYEVGSVVTGKVTGIQPYGAFVALdEETQGLVHISEITHGFVKDIHDFLSVGDEVKVKVLSVDEEKGKISLSIRATEEAP 83
S1_PNPase cd04472
S1_PNPase: Polynucleotide phosphorylase (PNPase), ), S1-like RNA-binding domain. PNPase is a ...
198-263 5.76e-12

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


Pssm-ID: 239918 [Multi-domain]  Cd Length: 68  Bit Score: 61.02  E-value: 5.76e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489056936 198 GQVVEGVVKNITDYGAFVD-LGGIDGLLHVTDMAWRRVNHPSEILTIGQTVKVQIIRINqETHRISL 263
Cdd:cd04472    1 GKIYEGKVVKIKDFGAFVEiLPGKDGLVHISELSDERVEKVEDVLKVGDEVKVKVIEVD-DRGRISL 66
RpsA COG0539
Ribosomal protein S1 [Translation, ribosomal structure and biogenesis]; Ribosomal protein S1 ...
369-540 6.01e-12

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: 66.99  E-value: 6.01e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936 369 VGTVVEGEVKNKTEFGLFIGLDGDVDGMVHLSDLDwNRPGEqviEEYNKGEVVKAVVLDVDVEKERISLGIKQLSG---- 444
Cdd:COG0539   18 EGDIVKGTVVSIDDDEVLVDIGYKSEGIIPLSEFS-DEPGE---LEVKVGDEVEVYVEKVEDGEGEIVLSKKKADRekaw 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936 445 DKVGEAAASGElrknaIVTCEVTAVTDGGLEVRLvdHDLDSFIRRS--DLSRDRDeqrPERFtVGQKVDARVIAFDKKTS 522
Cdd:COG0539   94 EELEEAFENGE-----PVEGKVKGVVKGGLIVDI--GGVRAFLPASqvDVRPVRD---LDEY-VGKTLEFKIIKLDRKRN 162
                        170       180
                 ....*....|....*....|.
gi 489056936 523 KLQVSIKAL---EIAEEKEAV 540
Cdd:COG0539  163 NVVVSRRAVleeEREEKREEL 183
S1 smart00316
Ribosomal protein S1-like RNA-binding domain;
282-353 7.39e-12

Ribosomal protein S1-like RNA-binding domain;


Pssm-ID: 197648 [Multi-domain]  Cd Length: 72  Bit Score: 61.08  E-value: 7.39e-12
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489056936   282 IGKKITGTVTNITDYGAFVEIEPGIEGLIHVSEMSWtKKNVHPGKILSTTQEVEVVVLEVDPVKRRISLGLK 353
Cdd:smart00316   2 VGDVVEGTVTEITPGGAFVDLGNGVEGLIPISELSD-KRVKDPEEVLKVGDEVKVKVLSVDEEKGRIILSLK 72
PRK05807 PRK05807
RNA-binding protein S1;
195-267 1.56e-11

RNA-binding protein S1;


Pssm-ID: 235614 [Multi-domain]  Cd Length: 136  Bit Score: 62.07  E-value: 1.56e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489056936 195 LEEGQVVEGVVKNITDYGAFVDLGGIDGLLHVTDMAWRRVNHPSEILTIGQTVKVQIIRINqETHRISLGMKQ 267
Cdd:PRK05807   3 LKAGSILEGTVVNITNFGAFVEVEGKTGLVHISEVADTYVKDIREHLKEQDKVKVKVISID-DNGKISLSIKQ 74
S1_like cd00164
S1_like: Ribosomal protein S1-like RNA-binding domain. Found in a wide variety of ...
286-351 2.50e-11

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


Pssm-ID: 238094 [Multi-domain]  Cd Length: 65  Bit Score: 59.32  E-value: 2.50e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489056936 286 ITGTVTNITDYGAFVEIEPGIEGLIHVSEMSWTKKnVHPGKILSTTQEVEVVVLEVDPVKRRISLG 351
Cdd:cd00164    1 VTGKVVSITKFGVFVELEDGVEGLVHISELSDKFV-KDPSEVFKVGDEVEVKVLEVDPEKGRISLS 65
S1_Rrp5_repeat_hs8_sc7 cd04461
S1_Rrp5_repeat_hs8_sc7: Rrp5 Homo sapiens S1 repeat 8 (hs8) and Saccharomyces cerevisiae S1 ...
187-265 2.76e-11

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: 59.52  E-value: 2.76e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936 187 QRSEIVQNLEE---GQVVEGVVKNITDYGAFVD-LGGIDGLLHVTDMAWRRVNHPSEILTIGQTVKVQIIRINQETHRIS 262
Cdd:cd04461    1 KEGTLPTNFSDlkpGMVVHGYVRNITPYGVFVEfLGGLTGLAPKSYISDEFVTDPSFGFKKGQSVTAKVTSVDEEKQRFL 80

                 ...
gi 489056936 263 LGM 265
Cdd:cd04461   81 LSL 83
YabR COG1098
Predicted RNA-binding protein, contains ribosomal protein S1 (RPS1) domain [General function ...
366-460 4.81e-11

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


Pssm-ID: 440715 [Multi-domain]  Cd Length: 130  Bit Score: 60.58  E-value: 4.81e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936 366 KYPVGTVVEGEVKNKTEFGLFIGLDGDVDGMVHLSDL--DWNRPGEQVIEEynkGEVVKAVVLDVDvEKERISLGIKQLS 443
Cdd:COG1098    2 SIEVGDIVEGKVTGITPFGAFVELPEGTTGLVHISEIadGYVKDINDYLKV---GDEVKVKVLSID-EDGKISLSIKQAE 77
                         90
                 ....*....|....*..
gi 489056936 444 GDKVGEAAASGELRKNA 460
Cdd:COG1098   78 EKPKRPPRPRRNSRPKA 94
Pnp COG1185
Polyribonucleotide nucleotidyltransferase (polynucleotide phosphorylase) [Translation, ...
274-317 8.42e-11

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


Pssm-ID: 440798 [Multi-domain]  Cd Length: 686  Bit Score: 64.64  E-value: 8.42e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 489056936 274 DGIGAKYPIGKKITGTVTNITDYGAFVEIEPGIEGLIHVSEMSW 317
Cdd:COG1185  608 EGITAEPEVGEIYEGKVVRIMDFGAFVEILPGKDGLVHISELAD 651
S1 smart00316
Ribosomal protein S1-like RNA-binding domain;
457-529 1.59e-10

Ribosomal protein S1-like RNA-binding domain;


Pssm-ID: 197648 [Multi-domain]  Cd Length: 72  Bit Score: 57.23  E-value: 1.59e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489056936   457 RKNAIVTCEVTAVTDGGLEVRLvDHDLDSFIRRSDLSRDRDEQRPERFTVGQKVDARVIAFDKKTSKLQVSIK 529
Cdd:smart00316   1 EVGDVVEGTVTEITPGGAFVDL-GNGVEGLIPISELSDKRVKDPEEVLKVGDEVKVKVLSVDEEKGRIILSLK 72
PRK11824 PRK11824
polynucleotide phosphorylase/polyadenylase; Provisional
274-317 1.67e-10

polynucleotide phosphorylase/polyadenylase; Provisional


Pssm-ID: 236995 [Multi-domain]  Cd Length: 693  Bit Score: 63.92  E-value: 1.67e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 489056936 274 DGIGAKYPIGKKITGTVTNITDYGAFVEIEPGIEGLIHVSEMSW 317
Cdd:PRK11824 613 EGITAEPEVGEIYEGKVVRIVDFGAFVEILPGKDGLVHISEIAD 656
YabR COG1098
Predicted RNA-binding protein, contains ribosomal protein S1 (RPS1) domain [General function ...
279-359 1.83e-10

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


Pssm-ID: 440715 [Multi-domain]  Cd Length: 130  Bit Score: 58.65  E-value: 1.83e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936 279 KYPIGKKITGTVTNITDYGAFVEIEPGIEGLIHVSEMSWTK-KNVH---------PGKILSTTQevevvvlevdpvKRRI 348
Cdd:COG1098    2 SIEVGDIVEGKVTGITPFGAFVELPEGTTGLVHISEIADGYvKDINdylkvgdevKVKVLSIDE------------DGKI 69
                         90
                 ....*....|.
gi 489056936 349 SLGLKQTLDNP 359
Cdd:COG1098   70 SLSIKQAEEKP 80
S1_Tex cd05685
S1_Tex: The C-terminal S1 domain of a transcription accessory factor called Tex, which has ...
283-350 2.33e-10

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: 56.47  E-value: 2.33e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489056936 283 GKKITGTVTNITDYGAFVEIEPGIEGLIHVSEMSwTKKNVHPGKILSTTQEVEVVVLEVDPVKRRISL 350
Cdd:cd05685    1 GMVLEGVVTNVTDFGAFVDIGVKQDGLIHISKMA-DRFVSHPSDVVSVGDIVEVKVISIDEERGRISL 67
S1_IF2_alpha cd04452
S1_IF2_alpha: The alpha subunit of translation Initiation Factor 2, S1-like RNA-binding domain. ...
196-267 3.41e-10

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: 56.44  E-value: 3.41e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489056936 196 EEGQVVEGVVKNITDYGAFVDL---GGIDGLLHVTDMAWRRVNHPSEILTIGQTVKVQIIRINQETHRISLGMKQ 267
Cdd:cd04452    2 EEGELVVVTVKSIADMGAYVSLleyGNIEGMILLSELSRRRIRSIRKLVKVGRKEVVKVIRVDKEKGYIDLSKKR 76
S1_like cd00164
S1_like: Ribosomal protein S1-like RNA-binding domain. Found in a wide variety of ...
373-438 5.71e-10

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


Pssm-ID: 238094 [Multi-domain]  Cd Length: 65  Bit Score: 55.46  E-value: 5.71e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489056936 373 VEGEVKNKTEFGLFIGLDGDVDGMVHLSDLDWNRPgEQVIEEYNKGEVVKAVVLDVDVEKERISLG 438
Cdd:cd00164    1 VTGKVVSITKFGVFVELEDGVEGLVHISELSDKFV-KDPSEVFKVGDEVEVKVLEVDPEKGRISLS 65
S1 pfam00575
S1 RNA binding domain; The S1 domain occurs in a wide range of RNA associated proteins. It is ...
456-528 1.11e-09

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


Pssm-ID: 425760 [Multi-domain]  Cd Length: 72  Bit Score: 54.60  E-value: 1.11e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489056936  456 LRKNAIVTCEVTAVTDGGLEVRLvDHDLDSFIRRSDLSRDRDEQRPERFTVGQKVDARVIAFDKKTSKLQVSI 528
Cdd:pfam00575   1 PEKGDVVEGEVTRVTKGGAFVDL-GNGVEGFIPISELSDDHVEDPDEVIKVGDEVKVKVLKVDKDRRRIILSI 72
S1_RPS1_repeat_ec6 cd05691
S1_RPS1_repeat_ec6: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
198-269 1.25e-09

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


Pssm-ID: 240196 [Multi-domain]  Cd Length: 73  Bit Score: 54.58  E-value: 1.25e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489056936 198 GQVVEGVVKNITDYGAFVDLG-GIDGLLHVTDMAWRRVNHPSEILTIGQTVKVQIIRINQETHRISLGMKQLE 269
Cdd:cd05691    1 GSIVTGKVTEVDAKGATVKLGdGVEGFLRAAELSRDRVEDATERFKVGDEVEAKITNVDRKNRKISLSIKAKE 73
S1_dom_CvfD NF040579
CvfD/Ygs/GSP13 family RNA-binding post-transcriptional regulator; CvfD, Ygs, and GSP13 form a ...
280-314 1.49e-09

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: 55.51  E-value: 1.49e-09
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 489056936 280 YPIGKKITGTVTNITDYGAFVEIEPGIEGLIHVSE 314
Cdd:NF040579   1 YKIGDIVEGKVTGIQPYGAFVALDEHTQGLIHISE 35
S1 pfam00575
S1 RNA binding domain; The S1 domain occurs in a wide range of RNA associated proteins. It is ...
280-352 5.53e-09

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


Pssm-ID: 425760 [Multi-domain]  Cd Length: 72  Bit Score: 52.67  E-value: 5.53e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489056936  280 YPIGKKITGTVTNITDYGAFVEIEPGIEGLIHVSEMSWtKKNVHPGKILSTTQEVEVVVLEVDPVKRRISLGL 352
Cdd:pfam00575   1 PEKGDVVEGEVTRVTKGGAFVDLGNGVEGFIPISELSD-DHVEDPDEVIKVGDEVKVKVLKVDKDRRRIILSI 72
S1 smart00316
Ribosomal protein S1-like RNA-binding domain;
26-92 6.15e-09

Ribosomal protein S1-like RNA-binding domain;


Pssm-ID: 197648 [Multi-domain]  Cd Length: 72  Bit Score: 52.61  E-value: 6.15e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936    26 EGYVVKGRIVAIEKDMAIIDAGLKVEGRVPLKEF---GAKGKDGTLKPGDEVEVYVERIENALGEAVLSR 92
Cdd:smart00316   2 VGDVVEGTVTEITPGGAFVDLGNGVEGLIPISELsdkRVKDPEEVLKVGDEVKVKVLSVDEEKGRIILSL 71
S1 pfam00575
S1 RNA binding domain; The S1 domain occurs in a wide range of RNA associated proteins. It is ...
24-92 1.30e-08

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


Pssm-ID: 425760 [Multi-domain]  Cd Length: 72  Bit Score: 51.90  E-value: 1.30e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489056936   24 LAEGYVVKGRIVAIEKDMAIIDAGLKVEGRVPLKEFGAKG---KDGTLKPGDEVEVYVERIENALGEAVLSR 92
Cdd:pfam00575   1 PEKGDVVEGEVTRVTKGGAFVDLGNGVEGFIPISELSDDHvedPDEVIKVGDEVKVKVLKVDKDRRRIILSI 72
PRK11824 PRK11824
polynucleotide phosphorylase/polyadenylase; Provisional
369-442 1.36e-08

polynucleotide phosphorylase/polyadenylase; Provisional


Pssm-ID: 236995 [Multi-domain]  Cd Length: 693  Bit Score: 57.75  E-value: 1.36e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489056936 369 VGTVVEGEVKNKTEFGLFIGLDGDVDGMVHLSDLDWNRpGEQVIEEYNKGEVVKAVVLDVDvEKERISLGIKQL 442
Cdd:PRK11824 621 VGEIYEGKVVRIVDFGAFVEILPGKDGLVHISEIADER-VEKVEDVLKEGDEVKVKVLEID-KRGRIRLSRKAV 692
PRK08059 PRK08059
general stress protein 13; Validated
366-463 1.44e-08

general stress protein 13; Validated


Pssm-ID: 181215 [Multi-domain]  Cd Length: 123  Bit Score: 53.13  E-value: 1.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936 366 KYPVGTVVEGEVKNKTEFGLFIGLDGDVDGMVHLSDLDwNRPGEQVIEEYNKGEVVKAVVLDVDVEKERISLGIKQLsgd 445
Cdd:PRK08059   4 QYEVGSVVTGKVTGIQPYGAFVALDEETQGLVHISEIT-HGFVKDIHDFLSVGDEVKVKVLSVDEEKGKISLSIRAT--- 79
                         90
                 ....*....|....*...
gi 489056936 446 kvgEAAASGELRKNAIVT 463
Cdd:PRK08059  80 ---EEAPEAKRKKGKILI 94
S1_Tex cd05685
S1_Tex: The C-terminal S1 domain of a transcription accessory factor called Tex, which has ...
370-437 1.50e-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: 51.46  E-value: 1.50e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489056936 370 GTVVEGEVKNKTEFGLFIGLDGDVDGMVHLSDLD---WNRPGEQVieeyNKGEVVKAVVLDVDVEKERISL 437
Cdd:cd05685    1 GMVLEGVVTNVTDFGAFVDIGVKQDGLIHISKMAdrfVSHPSDVV----SVGDIVEVKVISIDEERGRISL 67
S1_Rrp5_repeat_hs5 cd05697
S1_Rrp5_repeat_hs5: Rrp5 is a trans-acting factor important for biogenesis of both the 40S and ...
198-263 1.65e-08

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


Pssm-ID: 240202 [Multi-domain]  Cd Length: 69  Bit Score: 51.47  E-value: 1.65e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489056936 198 GQVVEGVVKNITDYGAFVDL-GGIDGLLHVTDMAWRRVNHPSEILTIGQTVKVQIIRINQETHRISL 263
Cdd:cd05697    1 GQVVKGTIRKLRPSGIFVKLsDHIKGLVPPMHLADVRLKHPEKKFKPGLKVKCRVLSVEPERKRLVL 67
S1_PNPase cd04472
S1_PNPase: Polynucleotide phosphorylase (PNPase), ), S1-like RNA-binding domain. PNPase is a ...
283-316 1.82e-08

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: 51.00  E-value: 1.82e-08
                         10        20        30
                 ....*....|....*....|....*....|....
gi 489056936 283 GKKITGTVTNITDYGAFVEIEPGIEGLIHVSEMS 316
Cdd:cd04472    1 GKIYEGKVVKIKDFGAFVEILPGKDGLVHISELS 34
PRK07252 PRK07252
S1 RNA-binding domain-containing protein;
282-315 2.50e-08

S1 RNA-binding domain-containing protein;


Pssm-ID: 180908 [Multi-domain]  Cd Length: 120  Bit Score: 52.40  E-value: 2.50e-08
                         10        20        30
                 ....*....|....*....|....*....|....
gi 489056936 282 IGKKITGTVTNITDYGAFVEIEPGIEGLIHVSEM 315
Cdd:PRK07252   3 IGDKLKGTITGIKPYGAFVALENGTTGLIHISEI 36
PRK07252 PRK07252
S1 RNA-binding domain-containing protein;
198-271 2.63e-08

S1 RNA-binding domain-containing protein;


Pssm-ID: 180908 [Multi-domain]  Cd Length: 120  Bit Score: 52.40  E-value: 2.63e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489056936 198 GQVVEGVVKNITDYGAFVDL-GGIDGLLHVTDMAWRRVNHPSEILTIGQTVKVQIIRINQETHRISLGMKQLESD 271
Cdd:PRK07252   4 GDKLKGTITGIKPYGAFVALeNGTTGLIHISEIKTGFIDNIHQLLKVGEEVLVQVVDFDEYTGKASLSLRTLEEE 78
PRK08059 PRK08059
general stress protein 13; Validated
278-359 2.68e-08

general stress protein 13; Validated


Pssm-ID: 181215 [Multi-domain]  Cd Length: 123  Bit Score: 52.36  E-value: 2.68e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936 278 AKYPIGKKITGTVTNITDYGAFVEIEPGIEGLIHVSEMSWT-KKNVHpgKILSTTQEVEVVVLEVDPVKRRISLGLKQTL 356
Cdd:PRK08059   3 SQYEVGSVVTGKVTGIQPYGAFVALDEETQGLVHISEITHGfVKDIH--DFLSVGDEVKVKVLSVDEEKGKISLSIRATE 80

                 ...
gi 489056936 357 DNP 359
Cdd:PRK08059  81 EAP 83
Tex COG2183
Transcriptional accessory protein Tex/SPT6 [Transcription];
282-354 3.52e-08

Transcriptional accessory protein Tex/SPT6 [Transcription];


Pssm-ID: 441786 [Multi-domain]  Cd Length: 719  Bit Score: 56.19  E-value: 3.52e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489056936 282 IGKKITGTVTNITDYGAFVEIepGI--EGLIHVSEMSwtKKNV-HPGKILSTTQEVEVVVLEVDPVKRRISLGLKQ 354
Cdd:COG2183  641 PGMILEGTVTNVTDFGAFVDI--GVhqDGLVHISQLS--DRFVkDPREVVKVGDIVKVKVLEVDLKRKRISLSMKL 712
S1 pfam00575
S1 RNA binding domain; The S1 domain occurs in a wide range of RNA associated proteins. It is ...
111-176 4.19e-08

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


Pssm-ID: 425760 [Multi-domain]  Cd Length: 72  Bit Score: 50.36  E-value: 4.19e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489056936  111 GERVDGVIFNQVKGGFTVDLD-GAVAFLPRSQVDIR--PIRDVTPLMHVPQPFEILKMDKRRGNIVVSR 176
Cdd:pfam00575   4 GDVVEGEVTRVTKGGAFVDLGnGVEGFIPISELSDDhvEDPDEVIKVGDEVKVKVLKVDKDRRRIILSI 72
S1_RPS1_repeat_hs4 cd05692
S1_RPS1_repeat_hs4: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
283-316 4.45e-08

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: 49.98  E-value: 4.45e-08
                         10        20        30
                 ....*....|....*....|....*....|....
gi 489056936 283 GKKITGTVTNITDYGAFVEIEPGIEGLIHVSEMS 316
Cdd:cd05692    1 GSVVEGTVTRLKPFGAFVELGGGISGLVHISQIA 34
S1_pNO40 cd05686
S1_pNO40: pNO40 , S1-like RNA-binding domain. pNO40 is a nucleolar protein of unknown function ...
199-266 9.16e-08

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: 49.40  E-value: 9.16e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936 199 QVVEGVVKNITDYGAFVDLGGI--DGLLHVTDMAWRRVNHPSEILTIGQTVKVQIIRInQETHRISLGMK 266
Cdd:cd05686    5 QIFKGEVASVTEYGAFVKIPGCrkQGLVHKSHMSSCRVDDPSEVVDVGEKVWVKVIGR-EMKDKMKLSLS 73
S1_DHX8_helicase cd05684
S1_DHX8_helicase: The N-terminal S1 domain of human ATP-dependent RNA helicase DHX8, a DEAH ...
283-332 1.19e-07

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


Pssm-ID: 240189 [Multi-domain]  Cd Length: 79  Bit Score: 49.16  E-value: 1.19e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489056936 283 GKKITGTVTNITDYGAFVEIE---PGIEGLIHVSEMSWTKKNVHPGKILSTTQ 332
Cdd:cd05684    1 GKIYKGKVTSIMDFGCFVQLEglkGRKEGLVHISQLSFEGRVANPSDVVKRGQ 53
S1_RPS1_repeat_hs4 cd05692
S1_RPS1_repeat_hs4: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
370-440 1.31e-07

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: 48.82  E-value: 1.31e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489056936 370 GTVVEGEVKNKTEFGLFIGLDGDVDGMVHLSDLDWNRPgEQVIEEYNKGEVVKAVVLDVDvEKERISLGIK 440
Cdd:cd05692    1 GSVVEGTVTRLKPFGAFVELGGGISGLVHISQIAHKRV-KDVKDVLKEGDKVKVKVLSID-ARGRISLSIK 69
PRK08563 PRK08563
DNA-directed RNA polymerase subunit E'; Provisional
196-267 2.94e-07

DNA-directed RNA polymerase subunit E'; Provisional


Pssm-ID: 236289 [Multi-domain]  Cd Length: 187  Bit Score: 50.98  E-value: 2.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936 196 EEGQVVEGVVKNITDYGAFVDLGGIDGLLHVTDMAWRRVNHPSE-----------ILTIGQTVKVQIIRI-----NQETH 259
Cdd:PRK08563  80 ELQEVVEGEVVEVVEFGAFVRIGPVDGLLHISQIMDDYISYDPKngrligkeskrVLKVGDVVRARIVAVslkerRPRGS 159

                 ....*...
gi 489056936 260 RISLGMKQ 267
Cdd:PRK08563 160 KIGLTMRQ 167
S1_Rrp5_repeat_sc12 cd05708
S1_Rrp5_repeat_sc12: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ...
283-353 3.24e-07

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: 48.09  E-value: 3.24e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489056936 283 GKKITGTVTNITDYGAFVEIE-PGIEGLIHVSEMSWTKKNvHPGKILSTTQEVEVVVLEVDPVKRRISLGLK 353
Cdd:cd05708    3 GQKIDGTVRRVEDYGVFIDIDgTNVSGLCHKSEISDNRVA-DASKLFRVGDKVRAKVLKIDAEKKRISLGLK 73
S1_Rrp5_repeat_hs6_sc5 cd05698
S1_Rrp5_repeat_hs6_sc5: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ...
203-266 7.69e-07

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


Pssm-ID: 240203 [Multi-domain]  Cd Length: 70  Bit Score: 46.45  E-value: 7.69e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489056936 203 GVVKNITDYGAFVD-LGGIDGLLHVTDMAWRRVNHPSEILTIGQTVKVQIIRINQETHRISLGMK 266
Cdd:cd05698    6 GTIVKVKPNGCIVSfYNNVKGFLPKSELSEAFIKDPEEHFRVGQVVKVKVLSCDPEQQRLLLSCK 70
PRK05807 PRK05807
RNA-binding protein S1;
369-446 9.99e-07

RNA-binding protein S1;


Pssm-ID: 235614 [Multi-domain]  Cd Length: 136  Bit Score: 48.20  E-value: 9.99e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489056936 369 VGTVVEGEVKNKTEFGLFIGLDGDVdGMVHLSDLDWNRPGEqvIEEYNK-GEVVKAVVLDVDvEKERISLGIKQLSGDK 446
Cdd:PRK05807   5 AGSILEGTVVNITNFGAFVEVEGKT-GLVHISEVADTYVKD--IREHLKeQDKVKVKVISID-DNGKISLSIKQAMKQK 79
Tex COG2183
Transcriptional accessory protein Tex/SPT6 [Transcription];
369-441 1.19e-06

Transcriptional accessory protein Tex/SPT6 [Transcription];


Pssm-ID: 441786 [Multi-domain]  Cd Length: 719  Bit Score: 51.56  E-value: 1.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936 369 VGTVVEGEVKNKTEFGLFIgldgDV----DGMVHLSDLDwNR----PGEQVieeynK-GEVVKAVVLDVDVEKERISLGI 439
Cdd:COG2183  641 PGMILEGTVTNVTDFGAFV----DIgvhqDGLVHISQLS-DRfvkdPREVV-----KvGDIVKVKVLEVDLKRKRISLSM 710

                 ..
gi 489056936 440 KQ 441
Cdd:COG2183  711 KL 712
PRK05807 PRK05807
RNA-binding protein S1;
283-358 1.23e-06

RNA-binding protein S1;


Pssm-ID: 235614 [Multi-domain]  Cd Length: 136  Bit Score: 47.82  E-value: 1.23e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489056936 283 GKKITGTVTNITDYGAFVEIEpGIEGLIHVSEMSWTK-KNVHpgKILSTTQEVEVVVLEVDPvKRRISLGLKQTLDN 358
Cdd:PRK05807   6 GSILEGTVVNITNFGAFVEVE-GKTGLVHISEVADTYvKDIR--EHLKEQDKVKVKVISIDD-NGKISLSIKQAMKQ 78
S1_RPS1_repeat_ec2_hs2 cd04465
S1_RPS1_repeat_ec2_hs2: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
198-261 1.51e-06

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: 45.53  E-value: 1.51e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489056936 198 GQVVEGVVKNITDYGAFVDLGGIDGLLHVTDMAWRRVNHPSEIltIGQTVKVQIIRINQETHRI 261
Cdd:cd04465    1 GEIVEGKVTEKVKGGLIVDIEGVRAFLPASQVDLRPVEDLDEY--VGKELKFKIIEIDRERNNI 62
PRK03987 PRK03987
translation initiation factor IF-2 subunit alpha; Validated
196-266 1.86e-06

translation initiation factor IF-2 subunit alpha; Validated


Pssm-ID: 235188 [Multi-domain]  Cd Length: 262  Bit Score: 49.44  E-value: 1.86e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489056936 196 EEGQVVEGVVKNITDYGAFVDL---GGIDGLLHVTDMAWRRVNHPSEILTIGQTVKVQIIRINQETHRISLGMK 266
Cdd:PRK03987   7 EEGELVVGTVKEVKDFGAFVTLdeyPGKEGFIHISEVASGWVKNIRDHVKEGQKVVCKVIRVDPRKGHIDLSLK 80
PRK08582 PRK08582
RNA-binding protein S1;
282-316 2.36e-06

RNA-binding protein S1;


Pssm-ID: 236305 [Multi-domain]  Cd Length: 139  Bit Score: 47.33  E-value: 2.36e-06
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 489056936 282 IGKKITGTVTNITDYGAFVEIEPGIEGLIHVSEMS 316
Cdd:PRK08582   5 VGSKLQGKVTGITNFGAFVELPEGKTGLVHISEVA 39
S1_PNPase cd04472
S1_PNPase: Polynucleotide phosphorylase (PNPase), ), S1-like RNA-binding domain. PNPase is a ...
370-437 2.36e-06

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


Pssm-ID: 239918 [Multi-domain]  Cd Length: 68  Bit Score: 45.23  E-value: 2.36e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489056936 370 GTVVEGEVKNKTEFGLFIGLDGDVDGMVHLSDLDWNRPgEQVIEEYNKGEVVKAVVLDVDvEKERISL 437
Cdd:cd04472    1 GKIYEGKVVKIKDFGAFVEILPGKDGLVHISELSDERV-EKVEDVLKVGDEVKVKVIEVD-DRGRISL 66
S1_like cd00164
S1_like: Ribosomal protein S1-like RNA-binding domain. Found in a wide variety of ...
462-527 2.95e-06

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


Pssm-ID: 238094 [Multi-domain]  Cd Length: 65  Bit Score: 44.68  E-value: 2.95e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489056936 462 VTCEVTAVTDGGLEVRLvDHDLDSFIRRSDLSRDRDEQRPERFTVGQKVDARVIAFDKKTSKLQVS 527
Cdd:cd00164    1 VTGKVVSITKFGVFVEL-EDGVEGLVHISELSDKFVKDPSEVFKVGDEVEVKVLEVDPEKGRISLS 65
PRK08582 PRK08582
RNA-binding protein S1;
195-267 3.63e-06

RNA-binding protein S1;


Pssm-ID: 236305 [Multi-domain]  Cd Length: 139  Bit Score: 46.56  E-value: 3.63e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489056936 195 LEEGQVVEGVVKNITDYGAFVDL-GGIDGLLHVTDMAWRRVNHPSEILTIGQTVKVQIIRINQEThRISLGMKQ 267
Cdd:PRK08582   3 IEVGSKLQGKVTGITNFGAFVELpEGKTGLVHISEVADNYVKDINDHLKVGDEVEVKVLNVEDDG-KIGLSIKK 75
S1_RNase_R cd04471
S1_RNase_R: RNase R C-terminal S1 domain. RNase R is a processive 3' to 5' exoribonuclease, ...
282-315 4.68e-06

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: 44.70  E-value: 4.68e-06
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 489056936 282 IGKKITGTVTNITDYGAFVEI-EPGIEGLIHVSEM 315
Cdd:cd04471    1 VGEEFDGVISGVTSFGLFVELdNLTVEGLVHVSTL 35
S1_DHX8_helicase cd05684
S1_DHX8_helicase: The N-terminal S1 domain of human ATP-dependent RNA helicase DHX8, a DEAH ...
370-444 8.66e-06

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: 43.77  E-value: 8.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936 370 GTVVEGEVKNKTEFGLFI---GLDGDVDGMVHLSDLDWNRPGEQVIEEYNKGEVVKAVVLdvDVEKERISL---GIKQLS 443
Cdd:cd05684    1 GKIYKGKVTSIMDFGCFVqleGLKGRKEGLVHISQLSFEGRVANPSDVVKRGQKVKVKVI--SIQNGKISLsmkDVDQDT 78

                 .
gi 489056936 444 G 444
Cdd:cd05684   79 G 79
S1_Rrp5_repeat_sc11 cd05707
S1_Rrp5_repeat_sc11: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ...
198-263 9.36e-06

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


Pssm-ID: 240212 [Multi-domain]  Cd Length: 68  Bit Score: 43.44  E-value: 9.36e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489056936 198 GQVVEGVVKNITDYGAFVDLG-GIDGLLHVTDMAWRRVNHPSEILTIGQTVKVQIIRINQETHRISL 263
Cdd:cd05707    1 GDVVRGFVKNIANNGVFVTLGrGVDARVRVSELSDSYLKDWKKRFKVGQLVKGKIVSIDPDNGRIEM 67
S1_RpoE cd04460
S1_RpoE: RpoE, S1-like RNA-binding domain. S1-like RNA-binding domains are found in a wide ...
199-267 1.00e-05

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


Pssm-ID: 239907 [Multi-domain]  Cd Length: 99  Bit Score: 44.20  E-value: 1.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936 199 QVVEGVVKNITDYGAFVDLGGIDGLLHVTDMAWRRVNHPSE-----------ILTIGQTVKVQIIRINQETH-----RIS 262
Cdd:cd04460    1 EVVEGEVVEVVDFGAFVRIGPVDGLLHISQIMDDYISYDPKnkrligeetkrVLKVGDVVRARIVAVSLKERrpresKIG 80

                 ....*
gi 489056936 263 LGMKQ 267
Cdd:cd04460   81 LTMRQ 85
S1 smart00316
Ribosomal protein S1-like RNA-binding domain;
111-177 1.25e-05

Ribosomal protein S1-like RNA-binding domain;


Pssm-ID: 197648 [Multi-domain]  Cd Length: 72  Bit Score: 43.36  E-value: 1.25e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936   111 GERVDGVIFNQVKGGFTVDL-DGAVAFLPRSQVDIRPIRDVTPLMHVPQ--PFEILKMDKRRGNIVVSRR 177
Cdd:smart00316   3 GDVVEGTVTEITPGGAFVDLgNGVEGLIPISELSDKRVKDPEEVLKVGDevKVKVLSVDEEKGRIILSLK 72
S1_Rrp5_repeat_hs5 cd05697
S1_Rrp5_repeat_hs5: Rrp5 is a trans-acting factor important for biogenesis of both the 40S and ...
370-437 1.45e-05

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: 43.00  E-value: 1.45e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489056936 370 GTVVEGEVKNKTEFGLFIGLDGDVDGMV---HLSDLDWNRPGEQvieeYNKGEVVKAVVLDVDVEKERISL 437
Cdd:cd05697    1 GQVVKGTIRKLRPSGIFVKLSDHIKGLVppmHLADVRLKHPEKK----FKPGLKVKCRVLSVEPERKRLVL 67
VacB COG0557
Exoribonuclease R [Transcription];
282-315 3.56e-05

Exoribonuclease R [Transcription];


Pssm-ID: 440323 [Multi-domain]  Cd Length: 711  Bit Score: 46.64  E-value: 3.56e-05
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 489056936 282 IGKKITGTVTNITDYGAFVEI-EPGIEGLIHVSEM 315
Cdd:COG0557  622 VGEEFEGVISGVTSFGLFVELdELGVEGLVHVSSL 656
S1_RPS1_repeat_ec6 cd05691
S1_RPS1_repeat_ec6: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
370-442 3.90e-05

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


Pssm-ID: 240196 [Multi-domain]  Cd Length: 73  Bit Score: 41.87  E-value: 3.90e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489056936 370 GTVVEGEVKNKTEFGLFIGLDGDVDGMVHLSDLDWNRPgEQVIEEYNKGEVVKAVVLDVDVEKERISLGIKQL 442
Cdd:cd05691    1 GSIVTGKVTEVDAKGATVKLGDGVEGFLRAAELSRDRV-EDATERFKVGDEVEAKITNVDRKNRKISLSIKAK 72
S1_IF2_alpha cd04452
S1_IF2_alpha: The alpha subunit of translation Initiation Factor 2, S1-like RNA-binding domain. ...
369-441 1.08e-04

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: 40.65  E-value: 1.08e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489056936 369 VGTVVEGEVKNKTEFGLFIGLD--GDVDGMVHLSDLD--WNRPGEQVIEEYNKgEVVKavVLDVDVEKERISLGIKQ 441
Cdd:cd04452    3 EGELVVVTVKSIADMGAYVSLLeyGNIEGMILLSELSrrRIRSIRKLVKVGRK-EVVK--VIRVDKEKGYIDLSKKR 76
PRK03987 PRK03987
translation initiation factor IF-2 subunit alpha; Validated
288-319 1.51e-04

translation initiation factor IF-2 subunit alpha; Validated


Pssm-ID: 235188 [Multi-domain]  Cd Length: 262  Bit Score: 43.66  E-value: 1.51e-04
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 489056936 288 GTVTNITDYGAFVEIE--PGIEGLIHVSEMS--WTK 319
Cdd:PRK03987  14 GTVKEVKDFGAFVTLDeyPGKEGFIHISEVAsgWVK 49
S1_IF2_alpha cd04452
S1_IF2_alpha: The alpha subunit of translation Initiation Factor 2, S1-like RNA-binding domain. ...
288-354 1.58e-04

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: 40.26  E-value: 1.58e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936 288 GTVTNITDYGAFVEIE--PGIEGLIHVSEMSWTK-KNVHpgKILSTTQEVEVVVLEVDPVKRRISLGLKQ 354
Cdd:cd04452    9 VTVKSIADMGAYVSLLeyGNIEGMILLSELSRRRiRSIR--KLVKVGRKEVVKVIRVDKEKGYIDLSKKR 76
S1_Rrp5_repeat_sc10 cd05706
S1_Rrp5_repeat_sc10: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ...
369-437 2.38e-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: 2.38e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489056936 369 VGTVVEGEVKNKTEFGLFIGLDGDVDGMVHLSDL--DWNRPGEQvieEYNKGEVVKAVVLDVDVEKERISL 437
Cdd:cd05706    3 VGDILPGRVTKVNDRYVLVQLGNKVTGPSFITDAldDYSEALPY---KFKKNDIVRACVLSVDVPNKKIAL 70
PLN00207 PLN00207
polyribonucleotide nucleotidyltransferase; Provisional
290-320 2.59e-04

polyribonucleotide nucleotidyltransferase; Provisional


Pssm-ID: 215104 [Multi-domain]  Cd Length: 891  Bit Score: 44.11  E-value: 2.59e-04
                         10        20        30
                 ....*....|....*....|....*....|...
gi 489056936 290 VTNITDYGAFVEIEPGIEGLIHVSEMS--WTKK 320
Cdd:PLN00207 762 IKSIAPYGAFVEIAPGREGLCHISELSsnWLAK 794
S1_RPS1_repeat_ec2_hs2 cd04465
S1_RPS1_repeat_ec2_hs2: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
459-529 3.00e-04

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: 39.36  E-value: 3.00e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489056936 459 NAIVTCEVTAVTDGGLEVRLvdHDLDSFIRRSDLSrDRDEQRPERFtVGQKVDARVIAFDKKTSKLQVSIK 529
Cdd:cd04465    1 GEIVEGKVTEKVKGGLIVDI--EGVRAFLPASQVD-LRPVEDLDEY-VGKELKFKIIEIDRERNNIVLSRR 67
PLN00207 PLN00207
polyribonucleotide nucleotidyltransferase; Provisional
172-272 3.87e-04

polyribonucleotide nucleotidyltransferase; Provisional


Pssm-ID: 215104 [Multi-domain]  Cd Length: 891  Bit Score: 43.34  E-value: 3.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936 172 IVVSRRTVLEESRAEQRS--------EIVQNLEegqvvegvVKNITDYGAFVDLG-GIDGLLHVTDMAWRRVNHPSEILT 242
Cdd:PLN00207 729 ITAKDLSSLEKSKAIISSltmvptvgDIYRNCE--------IKSIAPYGAFVEIApGREGLCHISELSSNWLAKPEDAFK 800
                         90       100       110
                 ....*....|....*....|....*....|
gi 489056936 243 IGQTVKVQIIRINQETHrISLGMKQLESDP 272
Cdd:PLN00207 801 VGDRIDVKLIEVNDKGQ-LRLSRRALLPEA 829
S1_NusA cd04455
S1_NusA: N-utilizing substance A protein (NusA), S1-like RNA-binding domain. S1-like ...
197-258 5.63e-04

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: 38.58  E-value: 5.63e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489056936 197 EGQVVEGVVKNITDYGAFVDLGGIDGLLHVTDMAwrrvnhPSEILTIGQTVKVQIIRINQET 258
Cdd:cd04455    3 EGEIVTGIVKRVDRGNVIVDLGKVEAILPKKEQI------PGESYRPGDRIKAYVLEVRKTS 58
S1_RNase_E cd04453
S1_RNase_E: RNase E and RNase G, S1-like RNA-binding domain. RNase E is an essential ...
200-253 5.85e-04

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


Pssm-ID: 239900 [Multi-domain]  Cd Length: 88  Bit Score: 39.11  E-value: 5.85e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 489056936 200 VVEGVVKNITdyGAFVDLG-GIDGLLHVTDMAW---RRVNHPSEILTIGQTVKVQIIR 253
Cdd:cd04453   14 RVKKIVPGLQ--AAFVDIGlGKNGFLHLSDILPayfKKHKKIAKLLKEGQEILVQVVK 69
nusA PRK09202
transcription elongation factor NusA; Validated
197-258 9.18e-04

transcription elongation factor NusA; Validated


Pssm-ID: 236410 [Multi-domain]  Cd Length: 470  Bit Score: 41.78  E-value: 9.18e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489056936 197 EGQVVEGVVKNITDYGAFVDLGGIDGLLHVTDMAwrrvnhPSEILTIGQTVKVQIIRINQET 258
Cdd:PRK09202 134 VGEIITGVVKRVERGNIIVDLGRAEAILPRKEQI------PRENFRPGDRVRAYVYEVRKEA 189
PRK08563 PRK08563
DNA-directed RNA polymerase subunit E'; Provisional
372-415 9.56e-04

DNA-directed RNA polymerase subunit E'; Provisional


Pssm-ID: 236289 [Multi-domain]  Cd Length: 187  Bit Score: 40.58  E-value: 9.56e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 489056936 372 VVEGEVKNKTEFGLFIGLdGDVDGMVHLSdldwnrpgeQVIEEY 415
Cdd:PRK08563  84 VVEGEVVEVVEFGAFVRI-GPVDGLLHIS---------QIMDDY 117
S1_RpoE cd04460
S1_RpoE: RpoE, S1-like RNA-binding domain. S1-like RNA-binding domains are found in a wide ...
372-438 1.09e-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: 38.42  E-value: 1.09e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489056936 372 VVEGEVKNKTEFGLFIGLdGDVDGMVHLSD-----LDWNRPGEQVIEEYNK-----GEVVKAVVLDVDVEKERISLG 438
Cdd:cd04460    2 VVEGEVVEVVDFGAFVRI-GPVDGLLHISQimddyISYDPKNKRLIGEETKrvlkvGDVVRARIVAVSLKERRPRES 77
S1_RPS1_repeat_ec1_hs1 cd05687
S1_RPS1_repeat_ec1_hs1: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
198-257 1.18e-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: 37.51  E-value: 1.18e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489056936 198 GQVVEGVVKNITDYGAFVDLGG-IDGLLHVTDMAWRRVNHPSEILTIGQTVKVQIIRINQE 257
Cdd:cd05687    1 GDIVKGTVVSVDDDEVLVDIGYkSEGIIPISEFSDDPIENGEDEVKVGDEVEVYVLRVEDE 61
S1_Rrp5_repeat_hs8_sc7 cd04461
S1_Rrp5_repeat_hs8_sc7: Rrp5 Homo sapiens S1 repeat 8 (hs8) and Saccharomyces cerevisiae S1 ...
369-437 1.21e-03

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: 37.95  E-value: 1.21e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489056936 369 VGTVVEGEVKNKTEFGLFIGLDGDVDGMVHLSDLDwNRPGEQVIEEYNKGEVVKAVVLDVDVEKERISL 437
Cdd:cd04461   14 PGMVVHGYVRNITPYGVFVEFLGGLTGLAPKSYIS-DEFVTDPSFGFKKGQSVTAKVTSVDEEKQRFLL 81
rpoE TIGR00448
DNA-directed RNA polymerase (rpoE), archaeal and eukaryotic form; This family seems to be ...
196-275 1.41e-03

DNA-directed RNA polymerase (rpoE), archaeal and eukaryotic form; This family seems to be confined to the archea and eukaryotic taxa and are quite dissimilar to E.coli rpoE. [Transcription, DNA-dependent RNA polymerase]


Pssm-ID: 129540 [Multi-domain]  Cd Length: 179  Bit Score: 39.77  E-value: 1.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936  196 EEGQVVEGVVKNITDYGAFVDLGGIDGLLHVTDMAWRRVNHPSE-----------ILTIGQTVKVQIIRIN-----QETH 259
Cdd:TIGR00448  80 ELGEIVEGEVIEIVEFGAFVSLGPFDGLFHVSQVTDDYCYYDPKesaligketkkVLDEGDKVRARIVALSlkdrrPEGS 159
                          90
                  ....*....|....*.
gi 489056936  260 RISLGMKQlesdPWDG 275
Cdd:TIGR00448 160 KIGLTMRQ----PLLG 171
S1_like cd00164
S1_like: Ribosomal protein S1-like RNA-binding domain. Found in a wide variety of ...
30-91 1.89e-03

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: 36.97  E-value: 1.89e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489056936  30 VKGRIVAIEKDMAIIDAGLKVEGRVPLKEF---GAKGKDGTLKPGDEVEVYVERIENALGEAVLS 91
Cdd:cd00164    1 VTGKVVSITKFGVFVELEDGVEGLVHISELsdkFVKDPSEVFKVGDEVEVKVLEVDPEKGRISLS 65
S1_RecJ_like cd04473
S1_RecJ_like: The S1 domain of the archaea-specific RecJ-like exonuclease. The function of ...
282-316 1.93e-03

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


Pssm-ID: 239919 [Multi-domain]  Cd Length: 77  Bit Score: 37.20  E-value: 1.93e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 489056936 282 IGKKITGTVTNITDYGAFVEIEPGIEGLIHVSEMS 316
Cdd:cd04473   16 VGKLYKGKVNGVAKYGVFVDLNDHVRGLIHRSNLL 50
S1_RecJ_like cd04473
S1_RecJ_like: The S1 domain of the archaea-specific RecJ-like exonuclease. The function of ...
192-225 2.56e-03

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


Pssm-ID: 239919 [Multi-domain]  Cd Length: 77  Bit Score: 36.82  E-value: 2.56e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 489056936 192 VQNLEEGQVVEGVVKNITDYGAFVDLGG-IDGLLH 225
Cdd:cd04473   11 MEDLEVGKLYKGKVNGVAKYGVFVDLNDhVRGLIH 45
S1_pNO40 cd05686
S1_pNO40: pNO40 , S1-like RNA-binding domain. pNO40 is a nucleolar protein of unknown function ...
288-329 3.54e-03

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: 36.30  E-value: 3.54e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 489056936 288 GTVTNITDYGAFVEIePGI--EGLIHVSEMSwTKKNVHPGKILS 329
Cdd:cd05686    9 GEVASVTEYGAFVKI-PGCrkQGLVHKSHMS-SCRVDDPSEVVD 50
COG1107 COG1107
Archaea-specific RecJ-like exonuclease, contains DnaJ-type Zn finger domain [Replication, ...
195-303 3.58e-03

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


Pssm-ID: 440724 [Multi-domain]  Cd Length: 626  Bit Score: 40.20  E-value: 3.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936 195 LEEGQVVEGVVKNITDYGAFVDLG-GIDGLLHVTDMawrrvnhpSEILTIGQTVKVQI--IRINQEthrISLGMKQLESD 271
Cdd:COG1107   37 LEPGRYYRGTVDGVADFGVFVDLNdHVTGLLHRSEL--------DQDWEVGDEVFVQVkeVRDNGN---VDLGWVSIDSY 105
                         90       100       110
                 ....*....|....*....|....*....|...
gi 489056936 272 PWDGIGAKYPIgkkitGTVTNITDY-GAFVEIE 303
Cdd:COG1107  106 ETVEVEKELPR-----TTIGDLEDRvGETVRIE 133
S1_Rrp5_repeat_sc11 cd05707
S1_Rrp5_repeat_sc11: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ...
283-350 4.22e-03

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


Pssm-ID: 240212 [Multi-domain]  Cd Length: 68  Bit Score: 36.12  E-value: 4.22e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489056936 283 GKKITGTVTNITDYGAFVEIEPGIEGLIHVSEMS------WtKKNVHP-----GKILSTtqevevvvlevDPVKRRISL 350
Cdd:cd05707    1 GDVVRGFVKNIANNGVFVTLGRGVDARVRVSELSdsylkdW-KKRFKVgqlvkGKIVSI-----------DPDNGRIEM 67
S1_Rrp5_repeat_hs6_sc5 cd05698
S1_Rrp5_repeat_hs6_sc5: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ...
466-529 6.06e-03

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


Pssm-ID: 240203 [Multi-domain]  Cd Length: 70  Bit Score: 35.66  E-value: 6.06e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489056936 466 VTAVTDGGLEVRLVDhDLDSFIRRSDLSRDRDEQRPERFTVGQKVDARVIAFDKKTSKLQVSIK 529
Cdd:cd05698    8 IVKVKPNGCIVSFYN-NVKGFLPKSELSEAFIKDPEEHFRVGQVVKVKVLSCDPEQQRLLLSCK 70
COG1107 COG1107
Archaea-specific RecJ-like exonuclease, contains DnaJ-type Zn finger domain [Replication, ...
282-315 6.20e-03

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


Pssm-ID: 440724 [Multi-domain]  Cd Length: 626  Bit Score: 39.43  E-value: 6.20e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 489056936 282 IGKKITGTVTNITDYGAFVEIEPGIEGLIHVSEM 315
Cdd:COG1107   39 PGRYYRGTVDGVADFGVFVDLNDHVTGLLHRSEL 72
NusA COG0195
Transcription antitermination factor NusA, contains S1 and KH domains [Transcription];
72-258 6.69e-03

Transcription antitermination factor NusA, contains S1 and KH domains [Transcription];


Pssm-ID: 439965 [Multi-domain]  Cd Length: 353  Bit Score: 39.08  E-value: 6.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936  72 DEVEVYVERIENALGEAVLSREKARREEswvklEQKFANGERVDGVIFNQVKGGFTVDLDGAVAFLPRSQVDIRPIRDVT 151
Cdd:COG0195   13 EELEKEKGIDKEILIEALEAALKKAYKK-----NYGNEVVVRVIIDGDTGEIRVYVVKEVVEEVEDPREEILLEAAKEDD 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056936 152 PLMHVPQPFEILKMDKRRGNIVV-SRRTVLEESRAEQRSEIVQN---LEEGQVVEGVVKNITDYGAFVDLGGIDGLLHVT 227
Cdd:COG0195   88 PDEEGGDIIEEEVPPDFFGRIAAqAAKQVIQQKRREAEREIIYEefkDRGGEIVGGVVQRVERGNVIVDLGKVEAILPRR 167
                        170       180       190
                 ....*....|....*....|....*....|.
gi 489056936 228 DMAwrrvnhPSEILTIGQTVKVQIIRINQET 258
Cdd:COG0195  168 EQI------PGENYRVGDRIRAYVLEVRKET 192
PRK08563 PRK08563
DNA-directed RNA polymerase subunit E'; Provisional
286-316 8.76e-03

DNA-directed RNA polymerase subunit E'; Provisional


Pssm-ID: 236289 [Multi-domain]  Cd Length: 187  Bit Score: 37.50  E-value: 8.76e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 489056936 286 ITGTVTNITDYGAFVEIEPgIEGLIHVSEMS 316
Cdd:PRK08563  85 VEGEVVEVVEFGAFVRIGP-VDGLLHISQIM 114
 
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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