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Conserved domains on  [gi|15604817|ref|NP_219601|]
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30S ribosomal protein S1 [Chlamydia trachomatis D/UW-3/CX]

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
14-550 0e+00

30S ribosomal protein S1; Reviewed


:

Pssm-ID: 235775 [Multi-domain]  Cd Length: 565  Bit Score: 746.22  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817   14 NLDTIACLPEDVKQFKDLLyamygftaTEEEPTSEVHPGAILKGTVVDISKDFVVVDVGLKSEGVIPMSEFIDSSEGLT- 92
Cdd:PRK06299   1 KEQDAQNQNDMEESFAELF--------EESLKESETREGSIVKGTVVAIDKDYVLVDVGLKSEGRIPLEEFKNEQGELEv 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817   93 -VGAEVEVYLDQTEDDEGKVVLSREKATRQRQWEYILAHCEEGSIVKGQITRKVKGGLIVDI-GMEAFLPGSQIDNKKIK 170
Cdd:PRK06299  73 kVGDEVEVYVERIEDGFGETVLSREKAKRLEAWDKLEKAFENGEIVEGVINGKVKGGFTVDLnGVEAFLPGSQVDVRPVR 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817  171 NLDDYVGKVCEFKILKINVDRRNVVVSRRELLEAERISKKAELIEQITIGERRKGIVKNITDFGVFLDLDGIDGLLHITD 250
Cdd:PRK06299 153 DTDPLEGKELEFKVIKLDKKRNNIVVSRRAVLEEERAEEREELLENLEEGQVVEGVVKNITDYGAFVDLGGVDGLLHITD 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817  251 MTWKRIRHPSEMVELNQELEVIILSVDKEKGRVALGLKQKEHNPWEDIEKKYPPGKRVRGKIVKLLPYGAFIEIEEGIEG 330
Cdd:PRK06299 233 ISWKRVNHPSEVVNVGDEVKVKVLKFDKEKKRVSLGLKQLGEDPWEAIEKKYPVGSKVKGKVTNITDYGAFVELEEGIEG 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817  331 LIHVSEMSWVKNIVDPNEVVNKGDEVEVVVLSIQKDEGKISLGLKQTKHNPWDNIEEKYPIGLRVTAEIKNLTNYGAFVE 410
Cdd:PRK06299 313 LVHVSEMSWTKKNKHPSKVVSVGQEVEVMVLEIDEEKRRISLGLKQCKENPWEEFAEKYPVGDVVEGKVKNITDFGAFVG 392
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817  411 LEPGIEGLIHISDMSWIKKVSHPSELFKKGNTVEAVILSVDKESKKITLGVKQLTPNPWDEIEVMFPVGSDISGVVTKIT 490
Cdd:PRK06299 393 LEGGIDGLVHLSDISWDKKGEEAVELYKKGDEVEAVVLKVDVEKERISLGIKQLEEDPFEEFAKKHKKGSIVTGTVTEVK 472
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817  491 AFGAFVELQNGIEGLIHVSELSEKPFAKIEDVLSIGDKVSAKVIKLDPDHKKVSLSIKEF 550
Cdd:PRK06299 473 DKGAFVELEDGVEGLIRASELSRDRVEDATEVLKVGDEVEAKVINIDRKNRRISLSIKAL 532
 
Name Accession Description Interval E-value
rpsA PRK06299
30S ribosomal protein S1; Reviewed
14-550 0e+00

30S ribosomal protein S1; Reviewed


Pssm-ID: 235775 [Multi-domain]  Cd Length: 565  Bit Score: 746.22  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817   14 NLDTIACLPEDVKQFKDLLyamygftaTEEEPTSEVHPGAILKGTVVDISKDFVVVDVGLKSEGVIPMSEFIDSSEGLT- 92
Cdd:PRK06299   1 KEQDAQNQNDMEESFAELF--------EESLKESETREGSIVKGTVVAIDKDYVLVDVGLKSEGRIPLEEFKNEQGELEv 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817   93 -VGAEVEVYLDQTEDDEGKVVLSREKATRQRQWEYILAHCEEGSIVKGQITRKVKGGLIVDI-GMEAFLPGSQIDNKKIK 170
Cdd:PRK06299  73 kVGDEVEVYVERIEDGFGETVLSREKAKRLEAWDKLEKAFENGEIVEGVINGKVKGGFTVDLnGVEAFLPGSQVDVRPVR 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817  171 NLDDYVGKVCEFKILKINVDRRNVVVSRRELLEAERISKKAELIEQITIGERRKGIVKNITDFGVFLDLDGIDGLLHITD 250
Cdd:PRK06299 153 DTDPLEGKELEFKVIKLDKKRNNIVVSRRAVLEEERAEEREELLENLEEGQVVEGVVKNITDYGAFVDLGGVDGLLHITD 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817  251 MTWKRIRHPSEMVELNQELEVIILSVDKEKGRVALGLKQKEHNPWEDIEKKYPPGKRVRGKIVKLLPYGAFIEIEEGIEG 330
Cdd:PRK06299 233 ISWKRVNHPSEVVNVGDEVKVKVLKFDKEKKRVSLGLKQLGEDPWEAIEKKYPVGSKVKGKVTNITDYGAFVELEEGIEG 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817  331 LIHVSEMSWVKNIVDPNEVVNKGDEVEVVVLSIQKDEGKISLGLKQTKHNPWDNIEEKYPIGLRVTAEIKNLTNYGAFVE 410
Cdd:PRK06299 313 LVHVSEMSWTKKNKHPSKVVSVGQEVEVMVLEIDEEKRRISLGLKQCKENPWEEFAEKYPVGDVVEGKVKNITDFGAFVG 392
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817  411 LEPGIEGLIHISDMSWIKKVSHPSELFKKGNTVEAVILSVDKESKKITLGVKQLTPNPWDEIEVMFPVGSDISGVVTKIT 490
Cdd:PRK06299 393 LEGGIDGLVHLSDISWDKKGEEAVELYKKGDEVEAVVLKVDVEKERISLGIKQLEEDPFEEFAKKHKKGSIVTGTVTEVK 472
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817  491 AFGAFVELQNGIEGLIHVSELSEKPFAKIEDVLSIGDKVSAKVIKLDPDHKKVSLSIKEF 550
Cdd:PRK06299 473 DKGAFVELEDGVEGLIRASELSRDRVEDATEVLKVGDEVEAKVINIDRKNRRISLSIKAL 532
rpsA TIGR00717
ribosomal protein S1; This model describes ribosomal protein S1, RpsA. This protein is found ...
34-548 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: 743.48  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817    34 AMYGFTATEEEPTSEVHPGAILKGTVVDISKDFVVVDVGLKSEGVIPMSEFIDSSEGLTVGAEVEVYLDQTEDDEGKVVL 113
Cdd:TIGR00717   1 ESFAQLLEESLKTEETRPGSIVKGTVVAINKDTVFVDVGLKSEGRIPKEEFLDAPLEIQVGDEVEVYLDRVEDRFGETVL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817   114 SREKATRQRQWEYILAHCEEGSIVKGQITRKVKGGLIVDI-GMEAFLPGSQIDNKKIKNLDDYVGKVCEFKILKINVDRR 192
Cdd:TIGR00717  81 SREKAQRHELWIKLEKAYEEGSIVEGKIVGKVKGGFIVDLnGVEAFLPGSQVDVKPIKDLDSLIGKTLKFKIIKLDQKRN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817   193 NVVVSRRELLEAERISKKAELIEQITIGERRKGIVKNITDFGVFLDLDGIDGLLHITDMTWKRIRHPSEMVELNQELEVI 272
Cdd:TIGR00717 161 NIVVSRRAYLEEERSQAREELLENLKEGDVVKGVVKNITDFGAFVDLGGVDGLLHITDMSWKRVKHPSEYVKVGQEVKVK 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817   273 ILSVDKEKGRVALGLKQKEHNPWEDIEKKYPPGKRVRGKIVKLLPYGAFIEIEEGIEGLIHVSEMSWVKNIVDPNEVVNK 352
Cdd:TIGR00717 241 VIKFDKEKGRISLSLKQLGEDPWEAIEKKFPVGDKITGRVTNLTDYGVFVEIEEGIEGLVHVSEMSWVKKNSHPSKVVKK 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817   353 GDEVEVVVLSIQKDEGKISLGLKQTKHNPWDNIEEKYPIGLRVTAEIKNLTNYGAFVELEPGIEGLIHISDMSWIKKVSH 432
Cdd:TIGR00717 321 GDEVEVMILDIDPERRRLSLGLKQCKANPWEQFEEKHPVGDRVTGKIKKITDFGAFVELEGGIDGLIHLSDISWDKDGRE 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817   433 PSELFKKGNTVEAVILSVDKESKKITLGVKQLTPNPWDEIEVMFPVGSDISGVVTKITAFGAFVELQNGIEGLIHVSELS 512
Cdd:TIGR00717 401 ADHLYKKGDEIEAVVLAVDKEKKRISLGVKQLTENPWEKFAAKYKVGSVVKGKVTEIKDFGAFVELPGGVEGLIRNSELS 480
                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 15604817   513 EKPFAKIEDVLSIGDKVSAKVIKLDPDHKKVSLSIK 548
Cdd:TIGR00717 481 ENRDEDKTDEIKVGDEVEAKVVDIDKKNRKVSLSVK 516
RpsA COG0539
Ribosomal protein S1 [Translation, ribosomal structure and biogenesis]; Ribosomal protein S1 ...
43-378 2.34e-172

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: 491.48  E-value: 2.34e-172
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817  43 EEPTSEVHPGAILKGTVVDISKDFVVVDVGLKSEGVIPMSEFIDSSEGLT--VGAEVEVYLDQTEDDEGKVVLSREKATR 120
Cdd:COG0539  10 EESLKELKEGDIVKGTVVSIDDDEVLVDIGYKSEGIIPLSEFSDEPGELEvkVGDEVEVYVEKVEDGEGEIVLSKKKADR 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817 121 QRQWEYILAHCEEGSIVKGQITRKVKGGLIVDI-GMEAFLPGSQIDNKKIKNLDDYVGKVCEFKILKINVDRRNVVVSRR 199
Cdd:COG0539  90 EKAWEELEEAFENGEPVEGKVKGVVKGGLIVDIgGVRAFLPASQVDVRPVRDLDEYVGKTLEFKIIKLDRKRNNVVVSRR 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817 200 ELLEAERISKKAELIEQITIGERRKGIVKNITDFGVFLDLDGIDGLLHITDMTWKRIRHPSEMVELNQELEVIILSVDKE 279
Cdd:COG0539 170 AVLEEEREEKREELLEKLEEGDVVEGTVKNITDFGAFVDLGGVDGLLHISEISWGRVKHPSEVLKVGDEVEVKVLKIDRE 249
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817 280 KGRVALGLKQKEHNPWEDIEKKYPPGKRVRGKIVKLLPYGAFIEIEEGIEGLIHVSEMSWVKNIVDPNEVVNKGDEVEVV 359
Cdd:COG0539 250 KERISLSLKQLQPDPWENIAEKYPVGDVVKGKVTRLTDFGAFVELEPGVEGLVHISEMSWTKRVAHPSDVVKVGDEVEVK 329
                       330
                ....*....|....*....
gi 15604817 360 VLSIQKDEGKISLGLKQTK 378
Cdd:COG0539 330 VLDIDPEERRISLSIKQLA 348
S1_RPS1_repeat_ec3 cd05688
S1_RPS1_repeat_ec3: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
219-286 1.03e-26

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: 103.09  E-value: 1.03e-26
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15604817 219 IGERRKGIVKNITDFGVFLDLDGIDGLLHITDMTWKRIRHPSEMVELNQELEVIILSVDKEKGRVALG 286
Cdd:cd05688   1 EGDVVEGTVKSITDFGAFVDLGGVDGLLHISDMSWGRVKHPSEVVNVGDEVEVKVLKIDKERKRISLG 68
S1_dom_CvfD NF040579
CvfD/Ygs/GSP13 family RNA-binding post-transcriptional regulator; CvfD, Ygs, and GSP13 form a ...
478-549 1.78e-18

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


Pssm-ID: 468553 [Multi-domain]  Cd Length: 113  Bit Score: 80.93  E-value: 1.78e-18
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15604817  478 VGSDISGVVTKITAFGAFVELQNGIEGLIHVSELSEKpFAK-IEDVLSIGDKVSAKVIKLDPDHKKVSLSIKE 549
Cdd:NF040579   3 IGDIVEGKVTGIQPYGAFVALDEHTQGLIHISEIKHG-YVKdINDFLKVGQEVKVKVLDIDEYTGKISLSLRA 74
S1_dom_CvfD NF040579
CvfD/Ygs/GSP13 family RNA-binding post-transcriptional regulator; CvfD, Ygs, and GSP13 form a ...
302-389 5.83e-18

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


Pssm-ID: 468553 [Multi-domain]  Cd Length: 113  Bit Score: 79.78  E-value: 5.83e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817  302 YPPGKRVRGKIVKLLPYGAFIEIEEGIEGLIHVSEMS--WVKNIvdpNEVVNKGDEVEVVVLSIQKDEGKISLGLKQT-- 377
Cdd:NF040579   1 YKIGDIVEGKVTGIQPYGAFVALDEHTQGLIHISEIKhgYVKDI---NDFLKVGQEVKVKVLDIDEYTGKISLSLRALee 77
                         90       100
                 ....*....|....*....|
gi 15604817  378 --------KHNPWDNIEEKY 389
Cdd:NF040579  78 apekhrkrRKHRWTNKRLKI 97
S1 smart00316
Ribosomal protein S1-like RNA-binding domain;
478-548 1.18e-17

Ribosomal protein S1-like RNA-binding domain;


Pssm-ID: 197648 [Multi-domain]  Cd Length: 72  Bit Score: 77.26  E-value: 1.18e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15604817    478 VGSDISGVVTKITAFGAFVELQNGIEGLIHVSELSEKPFAKIEDVLSIGDKVSAKVIKLDPDHKKVSLSIK 548
Cdd:smart00316   2 VGDVVEGTVTEITPGGAFVDLGNGVEGLIPISELSDKRVKDPEEVLKVGDEVKVKVLSVDEEKGRIILSLK 72
S1 pfam00575
S1 RNA binding domain; The S1 domain occurs in a wide range of RNA associated proteins. It is ...
476-547 4.22e-14

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


Pssm-ID: 425760 [Multi-domain]  Cd Length: 72  Bit Score: 67.31  E-value: 4.22e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15604817   476 FPVGSDISGVVTKITAFGAFVELQNGIEGLIHVSELSEKPFAKIEDVLSIGDKVSAKVIKLDPDHKKVSLSI 547
Cdd:pfam00575   1 PEKGDVVEGEVTRVTKGGAFVDLGNGVEGFIPISELSDDHVEDPDEVIKVGDEVKVKVLKVDKDRRRIILSI 72
S1_dom_CvfD NF040579
CvfD/Ygs/GSP13 family RNA-binding post-transcriptional regulator; CvfD, Ygs, and GSP13 form a ...
389-468 5.20e-13

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


Pssm-ID: 468553 [Multi-domain]  Cd Length: 113  Bit Score: 65.53  E-value: 5.20e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817  389 YPIGLRVTAEIKNLTNYGAFVELEPGIEGLIHISDMS--WIKKVshpSELFKKGNTVEAVILSVDKESKKITLGVKQLTP 466
Cdd:NF040579   1 YKIGDIVEGKVTGIQPYGAFVALDEHTQGLIHISEIKhgYVKDI---NDFLKVGQEVKVKVLDIDEYTGKISLSLRALEE 77

                 ..
gi 15604817  467 NP 468
Cdd:NF040579  78 AP 79
 
Name Accession Description Interval E-value
rpsA PRK06299
30S ribosomal protein S1; Reviewed
14-550 0e+00

30S ribosomal protein S1; Reviewed


Pssm-ID: 235775 [Multi-domain]  Cd Length: 565  Bit Score: 746.22  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817   14 NLDTIACLPEDVKQFKDLLyamygftaTEEEPTSEVHPGAILKGTVVDISKDFVVVDVGLKSEGVIPMSEFIDSSEGLT- 92
Cdd:PRK06299   1 KEQDAQNQNDMEESFAELF--------EESLKESETREGSIVKGTVVAIDKDYVLVDVGLKSEGRIPLEEFKNEQGELEv 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817   93 -VGAEVEVYLDQTEDDEGKVVLSREKATRQRQWEYILAHCEEGSIVKGQITRKVKGGLIVDI-GMEAFLPGSQIDNKKIK 170
Cdd:PRK06299  73 kVGDEVEVYVERIEDGFGETVLSREKAKRLEAWDKLEKAFENGEIVEGVINGKVKGGFTVDLnGVEAFLPGSQVDVRPVR 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817  171 NLDDYVGKVCEFKILKINVDRRNVVVSRRELLEAERISKKAELIEQITIGERRKGIVKNITDFGVFLDLDGIDGLLHITD 250
Cdd:PRK06299 153 DTDPLEGKELEFKVIKLDKKRNNIVVSRRAVLEEERAEEREELLENLEEGQVVEGVVKNITDYGAFVDLGGVDGLLHITD 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817  251 MTWKRIRHPSEMVELNQELEVIILSVDKEKGRVALGLKQKEHNPWEDIEKKYPPGKRVRGKIVKLLPYGAFIEIEEGIEG 330
Cdd:PRK06299 233 ISWKRVNHPSEVVNVGDEVKVKVLKFDKEKKRVSLGLKQLGEDPWEAIEKKYPVGSKVKGKVTNITDYGAFVELEEGIEG 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817  331 LIHVSEMSWVKNIVDPNEVVNKGDEVEVVVLSIQKDEGKISLGLKQTKHNPWDNIEEKYPIGLRVTAEIKNLTNYGAFVE 410
Cdd:PRK06299 313 LVHVSEMSWTKKNKHPSKVVSVGQEVEVMVLEIDEEKRRISLGLKQCKENPWEEFAEKYPVGDVVEGKVKNITDFGAFVG 392
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817  411 LEPGIEGLIHISDMSWIKKVSHPSELFKKGNTVEAVILSVDKESKKITLGVKQLTPNPWDEIEVMFPVGSDISGVVTKIT 490
Cdd:PRK06299 393 LEGGIDGLVHLSDISWDKKGEEAVELYKKGDEVEAVVLKVDVEKERISLGIKQLEEDPFEEFAKKHKKGSIVTGTVTEVK 472
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817  491 AFGAFVELQNGIEGLIHVSELSEKPFAKIEDVLSIGDKVSAKVIKLDPDHKKVSLSIKEF 550
Cdd:PRK06299 473 DKGAFVELEDGVEGLIRASELSRDRVEDATEVLKVGDEVEAKVINIDRKNRRISLSIKAL 532
rpsA TIGR00717
ribosomal protein S1; This model describes ribosomal protein S1, RpsA. This protein is found ...
34-548 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: 743.48  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817    34 AMYGFTATEEEPTSEVHPGAILKGTVVDISKDFVVVDVGLKSEGVIPMSEFIDSSEGLTVGAEVEVYLDQTEDDEGKVVL 113
Cdd:TIGR00717   1 ESFAQLLEESLKTEETRPGSIVKGTVVAINKDTVFVDVGLKSEGRIPKEEFLDAPLEIQVGDEVEVYLDRVEDRFGETVL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817   114 SREKATRQRQWEYILAHCEEGSIVKGQITRKVKGGLIVDI-GMEAFLPGSQIDNKKIKNLDDYVGKVCEFKILKINVDRR 192
Cdd:TIGR00717  81 SREKAQRHELWIKLEKAYEEGSIVEGKIVGKVKGGFIVDLnGVEAFLPGSQVDVKPIKDLDSLIGKTLKFKIIKLDQKRN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817   193 NVVVSRRELLEAERISKKAELIEQITIGERRKGIVKNITDFGVFLDLDGIDGLLHITDMTWKRIRHPSEMVELNQELEVI 272
Cdd:TIGR00717 161 NIVVSRRAYLEEERSQAREELLENLKEGDVVKGVVKNITDFGAFVDLGGVDGLLHITDMSWKRVKHPSEYVKVGQEVKVK 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817   273 ILSVDKEKGRVALGLKQKEHNPWEDIEKKYPPGKRVRGKIVKLLPYGAFIEIEEGIEGLIHVSEMSWVKNIVDPNEVVNK 352
Cdd:TIGR00717 241 VIKFDKEKGRISLSLKQLGEDPWEAIEKKFPVGDKITGRVTNLTDYGVFVEIEEGIEGLVHVSEMSWVKKNSHPSKVVKK 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817   353 GDEVEVVVLSIQKDEGKISLGLKQTKHNPWDNIEEKYPIGLRVTAEIKNLTNYGAFVELEPGIEGLIHISDMSWIKKVSH 432
Cdd:TIGR00717 321 GDEVEVMILDIDPERRRLSLGLKQCKANPWEQFEEKHPVGDRVTGKIKKITDFGAFVELEGGIDGLIHLSDISWDKDGRE 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817   433 PSELFKKGNTVEAVILSVDKESKKITLGVKQLTPNPWDEIEVMFPVGSDISGVVTKITAFGAFVELQNGIEGLIHVSELS 512
Cdd:TIGR00717 401 ADHLYKKGDEIEAVVLAVDKEKKRISLGVKQLTENPWEKFAAKYKVGSVVKGKVTEIKDFGAFVELPGGVEGLIRNSELS 480
                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 15604817   513 EKPFAKIEDVLSIGDKVSAKVIKLDPDHKKVSLSIK 548
Cdd:TIGR00717 481 ENRDEDKTDEIKVGDEVEAKVVDIDKKNRKVSLSVK 516
RpsA COG0539
Ribosomal protein S1 [Translation, ribosomal structure and biogenesis]; Ribosomal protein S1 ...
43-378 2.34e-172

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: 491.48  E-value: 2.34e-172
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817  43 EEPTSEVHPGAILKGTVVDISKDFVVVDVGLKSEGVIPMSEFIDSSEGLT--VGAEVEVYLDQTEDDEGKVVLSREKATR 120
Cdd:COG0539  10 EESLKELKEGDIVKGTVVSIDDDEVLVDIGYKSEGIIPLSEFSDEPGELEvkVGDEVEVYVEKVEDGEGEIVLSKKKADR 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817 121 QRQWEYILAHCEEGSIVKGQITRKVKGGLIVDI-GMEAFLPGSQIDNKKIKNLDDYVGKVCEFKILKINVDRRNVVVSRR 199
Cdd:COG0539  90 EKAWEELEEAFENGEPVEGKVKGVVKGGLIVDIgGVRAFLPASQVDVRPVRDLDEYVGKTLEFKIIKLDRKRNNVVVSRR 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817 200 ELLEAERISKKAELIEQITIGERRKGIVKNITDFGVFLDLDGIDGLLHITDMTWKRIRHPSEMVELNQELEVIILSVDKE 279
Cdd:COG0539 170 AVLEEEREEKREELLEKLEEGDVVEGTVKNITDFGAFVDLGGVDGLLHISEISWGRVKHPSEVLKVGDEVEVKVLKIDRE 249
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817 280 KGRVALGLKQKEHNPWEDIEKKYPPGKRVRGKIVKLLPYGAFIEIEEGIEGLIHVSEMSWVKNIVDPNEVVNKGDEVEVV 359
Cdd:COG0539 250 KERISLSLKQLQPDPWENIAEKYPVGDVVKGKVTRLTDFGAFVELEPGVEGLVHISEMSWTKRVAHPSDVVKVGDEVEVK 329
                       330
                ....*....|....*....
gi 15604817 360 VLSIQKDEGKISLGLKQTK 378
Cdd:COG0539 330 VLDIDPEERRISLSIKQLA 348
PRK12269 PRK12269
bifunctional cytidylate kinase/ribosomal protein S1; Provisional
32-550 4.27e-115

bifunctional cytidylate kinase/ribosomal protein S1; Provisional


Pssm-ID: 105491 [Multi-domain]  Cd Length: 863  Bit Score: 362.11  E-value: 4.27e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817   32 LYAMYGFTATEeeptsevhPGAILKGTVVDISKDFVVVDVGLKSEGVIPMSEFIDSSEGltvGAEVEVYLDQTEDDEGKv 111
Cdd:PRK12269 310 LQERYSFEAPE--------PGSVRMGTVVQVNAGTVFVDIGGKSEGRVPVEEFEAPPKA---GDGVRVYVERVTPYGPE- 377
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817  112 vLSREKATRQRQWEYILAHCEEGSIVKGQITR--KVKGGLIVDIG--MEAFLPGSQIDNKKIKNLDDYVGKVCEFKILKI 187
Cdd:PRK12269 378 -LSKTKADRLGLKVKLRDAERDGTPVEGRIVRltEKKSGFEVDLGagMMAFLPISQSDCQKVDAPESLIGLTSKFYIERI 456
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817  188 NVDRR-----NVVVSRRELLEAERISKKAELIEQITIGERRKGIVKNITDFGVFLDLDGIDGLLHITDMTWKRIRHPSEM 262
Cdd:PRK12269 457 SQSKQhrgndNIVINRRRYLEERARQAREEFFNSVHIEDSVSGVVKSFTSFGAFIDLGGFDGLLHVNDMSWGHVARPREF 536
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817  263 VELNQELEVIILSVDKEKGRVALGLKQKEHNPWEDIEKKYPPGKRVRGKIVKLLPYGAFIEIEEGIEGLIHVSEMSWVKN 342
Cdd:PRK12269 537 VKKGQTIELKVIRLDQAEKRINLSLKHFQPDPWLEFENKFGVNDVVKGRVTKIADFGAFIELAEGIEGLAHISEFSWVKK 616
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817  343 IVDPNEVVNKGDEVEVVVLSIQKDEGKISLGLKQTKHNPWDNIEEKYPIGLRVTAEIKNLTNYGAFVELEPGIEGLIHIS 422
Cdd:PRK12269 617 TSKPSDMVKIGDEVECMILGYDIQAGRVSLGLKQVTANPWEEIEARYPVGARFTRRIVKVTNAGAFIEMEEGIDGFLHVD 696
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817  423 DMSWIKKVSHPSELFKKGNTVEAVILSVDKESKKITLGVKQLTPNPWDEIEVMFPVGSDISGVVTKITAFGAFVELQNGI 502
Cdd:PRK12269 697 DLSWVKRTRPADHELEVGKEIECMVIECDPQARRIRLGVKQLSDNPWQVFANAYGVGSTVEGEVSSVTDFGIFVRVPGGV 776
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|.
gi 15604817  503 EGLIHVSELSEKPFAKIEDVL---SIGDKVSAKVIKLDPDHKKVSLSIKEF 550
Cdd:PRK12269 777 EGLVRKQHLVENRDGDPGEALrkyAVGDRVKAVIVDMNVKDRKVAFSVRDY 827
PRK00087 PRK00087
bifunctional 4-hydroxy-3-methylbut-2-enyl diphosphate reductase/30S ribosomal protein S1;
23-390 4.70e-112

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


Pssm-ID: 234623 [Multi-domain]  Cd Length: 647  Bit Score: 348.09  E-value: 4.70e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817   23 EDVKQFKDLLYAMYGFTAteeeptseVHPGAILKGTVVDISKDFVVVDVGLKSEGVIPMSEF-----IDSSEGLTVGAEV 97
Cdd:PRK00087 282 EEVEENEQLEYMNELEKQ--------IRRGDIVKGTVVSVNENEVFVDVGYKSEGVIPLRELtldeiSSLKESVKVGDEI 353
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817   98 EVYLDQTEDDEGKVVLSREKATRQRQWEYILAHCEEGSIVKGQITRKVKGGLIVDIG-MEAFLPGSQIDNKKIKNLDDYV 176
Cdd:PRK00087 354 EVKVLKLEDEDGYVVLSKKEADREKAWKELEEAFENGEPVKGKVKEVVKGGLLVDYGgVRAFLPASHVELGYVEDLSEYK 433
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817  177 GKVCEFKILKINVDRR-NVVVSRRELLEAERISKKAELIEQITIGERRKGIVKNITDFGVFLDLDGIDGLLHITDMTWKR 255
Cdd:PRK00087 434 GQELEVKIIEFNRKRRkKVVLSRKAILEEEKEKKKEETWNSLEEGDVVEGEVKRLTDFGAFVDIGGVDGLLHVSEISWGR 513
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817  256 IRHPSEMVELNQELEVIILSVDKEKGRVALGLKQKEHNPWEDIEKKYPPGKRVRGKIVKLLPYGAFIEIEEGIEGLIHVS 335
Cdd:PRK00087 514 VEKPSDVLKVGDEIKVYILDIDKENKKLSLSLKKLLPDPWENVEEKYPVGSIVLGKVVRIAPFGAFVELEPGVDGLVHIS 593
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 15604817  336 EMSWvKNIVDPNEVVNKGDEVEVVVLSIQKDEGKISLGLKQTKHNPWDNIEEKYP 390
Cdd:PRK00087 594 QISW-KRIDKPEDVLSEGEEVKAKILEVDPEEKRIRLSIKEVEEEPGDIEKVELE 647
rpsA PRK06676
30S ribosomal protein S1; Reviewed
47-381 4.80e-105

30S ribosomal protein S1; Reviewed


Pssm-ID: 235851 [Multi-domain]  Cd Length: 390  Bit Score: 321.44  E-value: 4.80e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817   47 SEVHPGAILKGTVVDISKDFVVVDV-GLKSEGVIPMSEFIDS-----SEGLTVGAEVEVYLDQTEDDEGKVVLSREKATR 120
Cdd:PRK06676  13 KEVEVGDVVTGEVLKVEDKQVFVNIeGYKVEGVIPISELSNDhiediNDVVKVGDELEVYVLKVEDGEGNLLLSKRRLEA 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817  121 QRQWEYILAHCEEGSIVKGQITRKVKGGLIVDI-GMEAFLPGSQIDNKKIKNLDDYVGKVCEFKILKINVDRRNVVVSRR 199
Cdd:PRK06676  93 EKAWDKLEEKFEEGEVVEVKVTEVVKGGLVVDVeGVRGFIPASLISTRFVEDFSDFKGKTLEVKIIELDPEKNRVILSRR 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817  200 ELLEAERISKKAELIEQITIGERRKGIVKNITDFGVFLDLDGIDGLLHITDMTWKRIRHPSEMVELNQELEVIILSVDKE 279
Cdd:PRK06676 173 AVVEEERAAKKEELLSSLKEGDVVEGTVARLTDFGAFVDIGGVDGLVHISELSHERVEKPSEVVSVGQEVEVKVLSIDWE 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817  280 KGRVALGLKQKEHNPWEDIEKKYPPGKRVRGKIVKLLPYGAFIEIEEGIEGLIHVSEMSWvKNIVDPNEVVNKGDEVEVV 359
Cdd:PRK06676 253 TERISLSLKDTLPGPWEGVEEKLPEGDVIEGTVKRLTDFGAFVEVLPGVEGLVHISQISH-KHIATPSEVLEEGQEVKVK 331
                        330       340
                 ....*....|....*....|..
gi 15604817  360 VLSIQKDEGKISLGLKQTKHNP 381
Cdd:PRK06676 332 VLEVNEEEKRISLSIKALEEAP 353
rpsA PRK13806
30S ribosomal protein S1; Provisional
38-460 4.99e-104

30S ribosomal protein S1; Provisional


Pssm-ID: 237516 [Multi-domain]  Cd Length: 491  Bit Score: 322.06  E-value: 4.99e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817   38 FTATEEEPTSEVHPGAILKGTVVDISKDFVVVDVGLKSEGVIPMSEFIDSSEGLT--VGAEVEVYLDQTEDDEgkVVLSR 115
Cdd:PRK13806  21 LEAYEGERKTELRVGDKITGTVIAITEDSVFVDTGSKVDGVVDRAELLDADGELTvaVGDEVELYVVSVNGQE--IRLSK 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817  116 eKATRQRQWEYILAHCEEGSIVKGQITRKVKGGLIVDI-GMEAFLPGSQIDNKKIKNLDDYVGKVCEFKILKINVDRRNV 194
Cdd:PRK13806  99 -ALSGQGGAAMLEEAYENGVPVEGKVTGTCKGGFNVEVlGRRAFCPVSQIDLRYVEDPESYVGQTFQFLITRVEENGRNI 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817  195 VVSRRELLEAERISKKAELIEQITIGERRKGIVKNITDFGVFLDLD-GIDGLLHITDMTWKRIRHPSEMVELNQELEVII 273
Cdd:PRK13806 178 VVSRRALLEREQKEALEAFMETVKEGDVVEGTVTRLAPFGAFVELApGVEGMVHISELSWSRVQKADEAVSVGDTVRVKV 257
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817  274 LSVDKEKG----RVALGLKQKEHNPWEDIEKKYPPGKRVRGKIVKLLPYGAFIEIEEGIEGLIHVSEMSWVKNIVDPNEV 349
Cdd:PRK13806 258 LGIERAKKgkglRISLSIKQAGGDPWDTVGDRLKAGDKVTGKVVRLAPFGAFVEILPGIEGLVHVSEMSWTRRVNKPEDV 337
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817  350 VNKGDEVEVVVLSIQKDEGKISLGLKQTKHNPWDNIEEKYPIGLRVTAEIKNLTNYGAFVELEPGIEGLIhisDMSWIKK 429
Cdd:PRK13806 338 VAPGDAVAVKIKDIDPAKRRISLSLRDAEGDPWADVAERFAPGTTVTGTVEKRAQFGLFVNLAPGVTGLL---PASVISR 414
                        410       420       430
                 ....*....|....*....|....*....|...
gi 15604817  430 VSHPSEL--FKKGNTVEAVILSVDKESKKITLG 460
Cdd:PRK13806 415 AGKPATYekLKPGDSVTLVVEEIDTAKRKISLA 447
rpsA PRK07899
30S ribosomal protein S1; Reviewed
52-376 8.96e-97

30S ribosomal protein S1; Reviewed


Pssm-ID: 236126 [Multi-domain]  Cd Length: 486  Bit Score: 303.12  E-value: 8.96e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817   52 GAILKGTVVDISKDFVVVDVGLKSEGVIPMSEF-----IDSSEGLTVGAEVEVYLDQTEDDEGKVVLSREKATRQRQWEY 126
Cdd:PRK07899  36 GDIVEGTVVKVDRDEVLLDIGYKTEGVIPSRELsikhdVDPNEVVEVGDEVEALVLQKEDKEGRLILSKKRAQYERAWGT 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817  127 ILAHCEEGSIVKGQITRKVKGGLIVDIGMEAFLPGSQIDNKKIKNLDDYVGKVCEFKILKINVDRRNVVVSRRELLEAER 206
Cdd:PRK07899 116 IEKIKEKDGVVTGTVIEVVKGGLILDIGLRGFLPASLVEMRRVRDLQPYIGQEIEAKIIELDKNRNNVVLSRRAWLEQTQ 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817  207 ISKKAELIEQITIGERRKGIVKNITDFGVFLDLDGIDGLLHITDMTWKRIRHPSEMVELNQELEVIILSVDKEKGRVALG 286
Cdd:PRK07899 196 SEVRSEFLNQLQKGQVRKGVVSSIVNFGAFVDLGGVDGLVHVSELSWKHIDHPSEVVEVGQEVTVEVLDVDMDRERVSLS 275
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817  287 LKQKEHNPWEDIEKKYPPGKRVRGKIVKLLPYGAFIEIEEGIEGLIHVSEMSwVKNIVDPNEVVNKGDEVEVVVLSIQKD 366
Cdd:PRK07899 276 LKATQEDPWQQFARTHAIGQIVPGKVTKLVPFGAFVRVEEGIEGLVHISELA-ERHVEVPEQVVQVGDEVFVKVIDIDLE 354
                        330
                 ....*....|
gi 15604817  367 EGKISLGLKQ 376
Cdd:PRK07899 355 RRRISLSLKQ 364
PRK00087 PRK00087
bifunctional 4-hydroxy-3-methylbut-2-enyl diphosphate reductase/30S ribosomal protein S1;
305-551 1.64e-33

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


Pssm-ID: 234623 [Multi-domain]  Cd Length: 647  Bit Score: 135.46  E-value: 1.64e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817  305 GKRVRGKIVKLLPYGAFIEIEEGIEGLIHVSEMSWvKNIVDPNEVVNKGDEVEVVVLSIQKDEGKISLGLKQT-KHNPWD 383
Cdd:PRK00087 303 GDIVKGTVVSVNENEVFVDVGYKSEGVIPLRELTL-DEISSLKESVKVGDEIEVKVLKLEDEDGYVVLSKKEAdREKAWK 381
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817  384 NIEEKYPIGLRVTAEIKNLTNYGAFVELEpGIEGLIHISDMSwIKKVSHPSELfkKGNTVEAVILSVDKESKK-ITLGVK 462
Cdd:PRK00087 382 ELEEAFENGEPVKGKVKEVVKGGLLVDYG-GVRAFLPASHVE-LGYVEDLSEY--KGQELEVKIIEFNRKRRKkVVLSRK 457
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817  463 QLTPNP--------WDEIEVmfpvGSDISGVVTKITAFGAFVELqNGIEGLIHVSELSEKPFAKIEDVLSIGDKVSAKVI 534
Cdd:PRK00087 458 AILEEEkekkkeetWNSLEE----GDVVEGEVKRLTDFGAFVDI-GGVDGLLHVSEISWGRVEKPSDVLKVGDEIKVYIL 532
                        250
                 ....*....|....*..
gi 15604817  535 KLDPDHKKVSLSIKEFL 551
Cdd:PRK00087 533 DIDKENKKLSLSLKKLL 549
PRK07400 PRK07400
30S ribosomal protein S1; Reviewed
51-294 9.91e-32

30S ribosomal protein S1; Reviewed


Pssm-ID: 180960 [Multi-domain]  Cd Length: 318  Bit Score: 124.91  E-value: 9.91e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817   51 PGAILKGTVVDISKDFVVVDVGLKSEGVIPMSEF----IDS-SEGLTVGAEVEVYLDQTEDDEGKVVLSREKATRQRQWE 125
Cdd:PRK07400  31 PGDIVNGTVFSLEPRGALIDIGAKTAAFMPIQEMsinrVEGpEEVLQPNETREFFILSDENEDGQLTLSIRRIEYMRAWE 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817  126 YILAHCEEGSIVKGQITRKVKGGLIVDI-GMEAFLPGSQIDNKKIKnlDDYVGKVCEFKILKINVDRRNVVVSRRELLeA 204
Cdd:PRK07400 111 RVRQLQKEDATVRSEVFATNRGGALVRIeGLRGFIPGSHISTRKPK--EELVGEELPLKFLEVDEERNRLVLSHRRAL-V 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817  205 ERISKKAElieqitIGERRKGIVKNITDFGVFLDLDGIDGLLHITDMTWKRIRHPSEMVELNQELEVIILSVDKEKGRVA 284
Cdd:PRK07400 188 ERKMNRLE------VGEVVVGTVRGIKPYGAFIDIGGVSGLLHISEISHEHIETPHSVFNVNDEMKVMIIDLDAERGRIS 261
                        250
                 ....*....|
gi 15604817  285 LGLKQKEHNP 294
Cdd:PRK07400 262 LSTKQLEPEP 271
S1_RPS1_repeat_ec3 cd05688
S1_RPS1_repeat_ec3: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
219-286 1.03e-26

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: 103.09  E-value: 1.03e-26
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15604817 219 IGERRKGIVKNITDFGVFLDLDGIDGLLHITDMTWKRIRHPSEMVELNQELEVIILSVDKEKGRVALG 286
Cdd:cd05688   1 EGDVVEGTVKSITDFGAFVDLGGVDGLLHISDMSWGRVKHPSEVVNVGDEVEVKVLKIDKERKRISLG 68
S1_RPS1_repeat_ec5 cd05690
S1_RPS1_repeat_ec5: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
392-460 8.53e-25

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: 97.56  E-value: 8.53e-25
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15604817 392 GLRVTAEIKNLTNYGAFVELEPGIEGLIHISDMSWIKKVSHPSELFKKGNTVEAVILSVDKESKKITLG 460
Cdd:cd05690   1 GTVVSGKIKSITDFGIFVGLDGGIDGLVHISDISWTQRVRHPSEIYKKGQEVEAVVLNIDVERERISLG 69
S1_RPS1_repeat_ec2_hs2 cd04465
S1_RPS1_repeat_ec2_hs2: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
134-199 1.73e-24

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: 96.76  E-value: 1.73e-24
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15604817 134 GSIVKGQITRKVKGGLIVDI-GMEAFLPGSQIDNKKIKNLDDYVGKVCEFKILKINVDRRNVVVSRR 199
Cdd:cd04465   1 GEIVEGKVTEKVKGGLIVDIeGVRAFLPASQVDLRPVEDLDEYVGKELKFKIIEIDRERNNIVLSRR 67
rpsA TIGR00717
ribosomal protein S1; This model describes ribosomal protein S1, RpsA. This protein is found ...
304-550 3.09e-22

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: 100.19  E-value: 3.09e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817   304 PGKRVRGKIVKLLPYGAFIEIEEGIEGLIHVSEmswvknIVDPNEVVNKGDEVEVVVLSIQKDEGKISLG-LKQTKHNPW 382
Cdd:TIGR00717  18 PGSIVKGTVVAINKDTVFVDVGLKSEGRIPKEE------FLDAPLEIQVGDEVEVYLDRVEDRFGETVLSrEKAQRHELW 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817   383 DNIEEKYPIGLRVTAEIKNLTNYGAFVELEpGIEGLIHISDMSwIKKVSHPSELFkkGNTVEAVILSVDKESKKITLGVK 462
Cdd:TIGR00717  92 IKLEKAYEEGSIVEGKIVGKVKGGFIVDLN-GVEAFLPGSQVD-VKPIKDLDSLI--GKTLKFKIIKLDQKRNNIVVSRR 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817   463 Q-LTPNPWDEIEVMFP---VGSDISGVVTKITAFGAFVELqNGIEGLIHVSELSEKPFAKIEDVLSIGDKVSAKVIKLDP 538
Cdd:TIGR00717 168 AyLEEERSQAREELLEnlkEGDVVKGVVKNITDFGAFVDL-GGVDGLLHITDMSWKRVKHPSEYVKVGQEVKVKVIKFDK 246
                         250
                  ....*....|..
gi 15604817   539 DHKKVSLSIKEF 550
Cdd:TIGR00717 247 EKGRISLSLKQL 258
S1_RPS1_repeat_ec4 cd05689
S1_RPS1_repeat_ec4: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
302-373 1.97e-21

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


Pssm-ID: 240194 [Multi-domain]  Cd Length: 72  Bit Score: 88.02  E-value: 1.97e-21
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15604817 302 YPPGKRVRGKIVKLLPYGAFIEIEEGIEGLIHVSEMSWVKNIVDPNEVVNKGDEVEVVVLSIQKDEGKISLG 373
Cdd:cd05689   1 YPEGTRLFGKVTNLTDYGCFVELEEGVEGLVHVSEMDWTNKNIHPSKVVSLGDEVEVMVLDIDEERRRISLG 72
S1_RPS1_repeat_ec4 cd05689
S1_RPS1_repeat_ec4: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
389-460 6.88e-21

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


Pssm-ID: 240194 [Multi-domain]  Cd Length: 72  Bit Score: 86.48  E-value: 6.88e-21
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15604817 389 YPIGLRVTAEIKNLTNYGAFVELEPGIEGLIHISDMSWIKKVSHPSELFKKGNTVEAVILSVDKESKKITLG 460
Cdd:cd05689   1 YPEGTRLFGKVTNLTDYGCFVELEEGVEGLVHVSEMDWTNKNIHPSKVVSLGDEVEVMVLDIDEERRRISLG 72
rpsA PRK06299
30S ribosomal protein S1; Reviewed
43-291 1.29e-20

30S ribosomal protein S1; Reviewed


Pssm-ID: 235775 [Multi-domain]  Cd Length: 565  Bit Score: 95.62  E-value: 1.29e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817   43 EEPTSEVHPGAILKGTVVDIsKDF-VVVDVGLKSEGVIPMSEF------IDSSEGLTVGAEVEVYLDQTEDDEGKVVLSR 115
Cdd:PRK06299 278 EAIEKKYPVGSKVKGKVTNI-TDYgAFVELEEGIEGLVHVSEMswtkknKHPSKVVSVGQEVEVMVLEIDEEKRRISLGL 356
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817  116 eKATRQRQWEYILAHCEEGSIVKGQITRKVKGGLIVDI--GMEAFLPGSQID-NKKIKNLDDY--VGKVCEFKILKINVD 190
Cdd:PRK06299 357 -KQCKENPWEEFAEKYPVGDVVEGKVKNITDFGAFVGLegGIDGLVHLSDISwDKKGEEAVELykKGDEVEAVVLKVDVE 435
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817  191 RRNVVVSRRELLEaeriSKKAELIEQITIGERRKGIVKNITDFGVFLDL-DGIDGLLHITDMTWKRIRHPSEMVELNQEL 269
Cdd:PRK06299 436 KERISLGIKQLEE----DPFEEFAKKHKKGSIVTGTVTEVKDKGAFVELeDGVEGLIRASELSRDRVEDATEVLKVGDEV 511
                        250       260
                 ....*....|....*....|..
gi 15604817  270 EVIILSVDKEKGRVALGLKQKE 291
Cdd:PRK06299 512 EAKVINIDRKNRRISLSIKALD 533
Pnp COG1185
Polyribonucleotide nucleotidyltransferase (polynucleotide phosphorylase) [Translation, ...
447-549 1.34e-20

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


Pssm-ID: 440798 [Multi-domain]  Cd Length: 686  Bit Score: 95.84  E-value: 1.34e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817 447 ILSVDKES----KKItlgVKQLTpnpwDEIEVmfpvGSDISGVVTKITAFGAFVELQNGIEGLIHVSELSEKPFAKIEDV 522
Cdd:COG1185 592 IAATDGEAaekaIER---IEGIT----AEPEV----GEIYEGKVVRIMDFGAFVEILPGKDGLVHISELADERVEKVEDV 660
                        90       100
                ....*....|....*....|....*..
gi 15604817 523 LSIGDKVSAKVIKLDpDHKKVSLSIKE 549
Cdd:COG1185 661 LKEGDEVKVKVLEID-DQGRIKLSRKA 686
YabR COG1098
Predicted RNA-binding protein, contains ribosomal protein S1 (RPS1) domain [General function ...
478-549 2.37e-20

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


Pssm-ID: 440715 [Multi-domain]  Cd Length: 130  Bit Score: 87.16  E-value: 2.37e-20
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15604817 478 VGSDISGVVTKITAFGAFVELQNGIEGLIHVSELSEKPFAKIEDVLSIGDKVSAKVIKLDPDHkKVSLSIKE 549
Cdd:COG1098   5 VGDIVEGKVTGITPFGAFVELPEGTTGLVHISEIADGYVKDINDYLKVGDEVKVKVLSIDEDG-KISLSIKQ 75
PRK11824 PRK11824
polynucleotide phosphorylase/polyadenylase; Provisional
447-551 2.66e-20

polynucleotide phosphorylase/polyadenylase; Provisional


Pssm-ID: 236995 [Multi-domain]  Cd Length: 693  Bit Score: 94.73  E-value: 2.66e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817  447 ILSVDKESKKITLG-VKQLTpnpwDEIEVmfpvGSDISGVVTKITAFGAFVELQNGIEGLIHVSELSEKPFAKIEDVLSI 525
Cdd:PRK11824 597 IAATDGEAAEAAKErIEGIT----AEPEV----GEIYEGKVVRIVDFGAFVEILPGKDGLVHISEIADERVEKVEDVLKE 668
                         90       100
                 ....*....|....*....|....*.
gi 15604817  526 GDKVSAKVIKLDpDHKKVSLSIKEFL 551
Cdd:PRK11824 669 GDEVKVKVLEID-KRGRIRLSRKAVL 693
YabR COG1098
Predicted RNA-binding protein, contains ribosomal protein S1 (RPS1) domain [General function ...
300-381 3.70e-20

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


Pssm-ID: 440715 [Multi-domain]  Cd Length: 130  Bit Score: 86.39  E-value: 3.70e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817 300 KKYPPGKRVRGKIVKLLPYGAFIEIEEGIEGLIHVSEMS--WVKNIvdpNEVVNKGDEVEVVVLSIQKDeGKISLGLKQT 377
Cdd:COG1098   1 MSIEVGDIVEGKVTGITPFGAFVELPEGTTGLVHISEIAdgYVKDI---NDYLKVGDEVKVKVLSIDED-GKISLSIKQA 76

                ....
gi 15604817 378 KHNP 381
Cdd:COG1098  77 EEKP 80
S1_RPS1_repeat_ec3 cd05688
S1_RPS1_repeat_ec3: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
391-460 4.33e-20

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


Pssm-ID: 240193 [Multi-domain]  Cd Length: 68  Bit Score: 84.22  E-value: 4.33e-20
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817 391 IGLRVTAEIKNLTNYGAFVELEpGIEGLIHISDMSWiKKVSHPSELFKKGNTVEAVILSVDKESKKITLG 460
Cdd:cd05688   1 EGDVVEGTVKSITDFGAFVDLG-GVDGLLHISDMSW-GRVKHPSEVVNVGDEVEVKVLKIDKERKRISLG 68
S1_RPS1_repeat_ec5 cd05690
S1_RPS1_repeat_ec5: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
220-286 5.91e-19

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


Pssm-ID: 240195 [Multi-domain]  Cd Length: 69  Bit Score: 81.00  E-value: 5.91e-19
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15604817 220 GERRKGIVKNITDFGVFLDLD-GIDGLLHITDMTW-KRIRHPSEMVELNQELEVIILSVDKEKGRVALG 286
Cdd:cd05690   1 GTVVSGKIKSITDFGIFVGLDgGIDGLVHISDISWtQRVRHPSEIYKKGQEVEAVVLNIDVERERISLG 69
S1_dom_CvfD NF040579
CvfD/Ygs/GSP13 family RNA-binding post-transcriptional regulator; CvfD, Ygs, and GSP13 form a ...
478-549 1.78e-18

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


Pssm-ID: 468553 [Multi-domain]  Cd Length: 113  Bit Score: 80.93  E-value: 1.78e-18
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15604817  478 VGSDISGVVTKITAFGAFVELQNGIEGLIHVSELSEKpFAK-IEDVLSIGDKVSAKVIKLDPDHKKVSLSIKE 549
Cdd:NF040579   3 IGDIVEGKVTGIQPYGAFVALDEHTQGLIHISEIKHG-YVKdINDFLKVGQEVKVKVLDIDEYTGKISLSLRA 74
S1_dom_CvfD NF040579
CvfD/Ygs/GSP13 family RNA-binding post-transcriptional regulator; CvfD, Ygs, and GSP13 form a ...
302-389 5.83e-18

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


Pssm-ID: 468553 [Multi-domain]  Cd Length: 113  Bit Score: 79.78  E-value: 5.83e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817  302 YPPGKRVRGKIVKLLPYGAFIEIEEGIEGLIHVSEMS--WVKNIvdpNEVVNKGDEVEVVVLSIQKDEGKISLGLKQT-- 377
Cdd:NF040579   1 YKIGDIVEGKVTGIQPYGAFVALDEHTQGLIHISEIKhgYVKDI---NDFLKVGQEVKVKVLDIDEYTGKISLSLRALee 77
                         90       100
                 ....*....|....*....|
gi 15604817  378 --------KHNPWDNIEEKY 389
Cdd:NF040579  78 apekhrkrRKHRWTNKRLKI 97
S1_RPS1_repeat_ec5 cd05690
S1_RPS1_repeat_ec5: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
305-373 5.85e-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: 78.30  E-value: 5.85e-18
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15604817 305 GKRVRGKIVKLLPYGAFIEIEEGIEGLIHVSEMSWVKNIVDPNEVVNKGDEVEVVVLSIQKDEGKISLG 373
Cdd:cd05690   1 GTVVSGKIKSITDFGIFVGLDGGIDGLVHISDISWTQRVRHPSEIYKKGQEVEAVVLNIDVERERISLG 69
S1 smart00316
Ribosomal protein S1-like RNA-binding domain;
478-548 1.18e-17

Ribosomal protein S1-like RNA-binding domain;


Pssm-ID: 197648 [Multi-domain]  Cd Length: 72  Bit Score: 77.26  E-value: 1.18e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15604817    478 VGSDISGVVTKITAFGAFVELQNGIEGLIHVSELSEKPFAKIEDVLSIGDKVSAKVIKLDPDHKKVSLSIK 548
Cdd:smart00316   2 VGDVVEGTVTEITPGGAFVDLGNGVEGLIPISELSDKRVKDPEEVLKVGDEVKVKVLSVDEEKGRIILSLK 72
S1_RPS1_repeat_ec3 cd05688
S1_RPS1_repeat_ec3: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
304-373 1.39e-17

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


Pssm-ID: 240193 [Multi-domain]  Cd Length: 68  Bit Score: 76.90  E-value: 1.39e-17
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817 304 PGKRVRGKIVKLLPYGAFIEIEeGIEGLIHVSEMSWvKNIVDPNEVVNKGDEVEVVVLSIQKDEGKISLG 373
Cdd:cd05688   1 EGDVVEGTVKSITDFGAFVDLG-GVDGLLHISDMSW-GRVKHPSEVVNVGDEVEVKVLKIDKERKRISLG 68
S1 smart00316
Ribosomal protein S1-like RNA-binding domain;
304-375 2.06e-17

Ribosomal protein S1-like RNA-binding domain;


Pssm-ID: 197648 [Multi-domain]  Cd Length: 72  Bit Score: 76.87  E-value: 2.06e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15604817    304 PGKRVRGKIVKLLPYGAFIEIEEGIEGLIHVSEMSWvKNIVDPNEVVNKGDEVEVVVLSIQKDEGKISLGLK 375
Cdd:smart00316   2 VGDVVEGTVTEITPGGAFVDLGNGVEGLIPISELSD-KRVKDPEEVLKVGDEVKVKVLSVDEEKGRIILSLK 72
S1_RPS1_repeat_ec1_hs1 cd05687
S1_RPS1_repeat_ec1_hs1: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
52-116 8.51e-17

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: 74.87  E-value: 8.51e-17
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817  52 GAILKGTVVDISKDFVVVDVGLKSEGVIPMSEFIDS-----SEGLTVGAEVEVYLDQTEDDEGKVVLSRE 116
Cdd:cd05687   1 GDIVKGTVVSVDDDEVLVDIGYKSEGIIPISEFSDDpiengEDEVKVGDEVEVYVLRVEDEEGNVVLSKR 70
S1_PNPase cd04472
S1_PNPase: Polynucleotide phosphorylase (PNPase), ), S1-like RNA-binding domain. PNPase is a ...
479-547 8.90e-17

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


Pssm-ID: 239918 [Multi-domain]  Cd Length: 68  Bit Score: 74.89  E-value: 8.90e-17
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15604817 479 GSDISGVVTKITAFGAFVELQNGIEGLIHVSELSEKPFAKIEDVLSIGDKVSAKVIKLDpDHKKVSLSI 547
Cdd:cd04472   1 GKIYEGKVVKIKDFGAFVEILPGKDGLVHISELSDERVEKVEDVLKVGDEVKVKVIEVD-DRGRISLSR 68
PRK08059 PRK08059
general stress protein 13; Validated
476-549 1.03e-16

general stress protein 13; Validated


Pssm-ID: 181215 [Multi-domain]  Cd Length: 123  Bit Score: 76.62  E-value: 1.03e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15604817  476 FPVGSDISGVVTKITAFGAFVELQNGIEGLIHVSELSEKPFAKIEDVLSIGDKVSAKVIKLDPDHKKVSLSIKE 549
Cdd:PRK08059   5 YEVGSVVTGKVTGIQPYGAFVALDEETQGLVHISEITHGFVKDIHDFLSVGDEVKVKVLSVDEEKGKISLSIRA 78
PRK08582 PRK08582
RNA-binding protein S1;
478-548 1.25e-16

RNA-binding protein S1;


Pssm-ID: 236305 [Multi-domain]  Cd Length: 139  Bit Score: 76.61  E-value: 1.25e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15604817  478 VGSDISGVVTKITAFGAFVELQNGIEGLIHVSELSEKPFAKIEDVLSIGDKVSAKVIKLDPDhKKVSLSIK 548
Cdd:PRK08582   5 VGSKLQGKVTGITNFGAFVELPEGKTGLVHISEVADNYVKDINDHLKVGDEVEVKVLNVEDD-GKIGLSIK 74
S1 smart00316
Ribosomal protein S1-like RNA-binding domain;
391-462 2.28e-16

Ribosomal protein S1-like RNA-binding domain;


Pssm-ID: 197648 [Multi-domain]  Cd Length: 72  Bit Score: 73.79  E-value: 2.28e-16
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15604817    391 IGLRVTAEIKNLTNYGAFVELEPGIEGLIHISDMSWiKKVSHPSELFKKGNTVEAVILSVDKESKKITLGVK 462
Cdd:smart00316   2 VGDVVEGTVTEITPGGAFVDLGNGVEGLIPISELSD-KRVKDPEEVLKVGDEVKVKVLSVDEEKGRIILSLK 72
Pnp COG1185
Polyribonucleotide nucleotidyltransferase (polynucleotide phosphorylase) [Translation, ...
271-375 2.60e-16

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


Pssm-ID: 440798 [Multi-domain]  Cd Length: 686  Bit Score: 82.36  E-value: 2.60e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817 271 VIILSVDKEKGRVALGlkqkehnpW-EDIEKKYPPGKRVRGKIVKLLPYGAFIEIEEGIEGLIHVSEMSW--VKNIvdpN 347
Cdd:COG1185 590 VKIAATDGEAAEKAIE--------RiEGITAEPEVGEIYEGKVVRIMDFGAFVEILPGKDGLVHISELADerVEKV---E 658
                        90       100
                ....*....|....*....|....*...
gi 15604817 348 EVVNKGDEVEVVVLSIqKDEGKISLGLK 375
Cdd:COG1185 659 DVLKEGDEVKVKVLEI-DDQGRIKLSRK 685
PRK08059 PRK08059
general stress protein 13; Validated
301-381 2.64e-16

general stress protein 13; Validated


Pssm-ID: 181215 [Multi-domain]  Cd Length: 123  Bit Score: 75.47  E-value: 2.64e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817  301 KYPPGKRVRGKIVKLLPYGAFIEIEEGIEGLIHVSEMS--WVKNIvdpNEVVNKGDEVEVVVLSIQKDEGKISLGLKQTK 378
Cdd:PRK08059   4 QYEVGSVVTGKVTGIQPYGAFVALDEETQGLVHISEIThgFVKDI---HDFLSVGDEVKVKVLSVDEEKGKISLSIRATE 80

                 ...
gi 15604817  379 HNP 381
Cdd:PRK08059  81 EAP 83
S1_RPS1_repeat_hs4 cd05692
S1_RPS1_repeat_hs4: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
479-548 3.27e-16

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


Pssm-ID: 240197 [Multi-domain]  Cd Length: 69  Bit Score: 73.09  E-value: 3.27e-16
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817 479 GSDISGVVTKITAFGAFVELQNGIEGLIHVSELSEKPFAKIEDVLSIGDKVSAKVIKLDPDhKKVSLSIK 548
Cdd:cd05692   1 GSVVEGTVTRLKPFGAFVELGGGISGLVHISQIAHKRVKDVKDVLKEGDKVKVKVLSIDAR-GRISLSIK 69
PRK11824 PRK11824
polynucleotide phosphorylase/polyadenylase; Provisional
270-375 4.70e-16

polynucleotide phosphorylase/polyadenylase; Provisional


Pssm-ID: 236995 [Multi-domain]  Cd Length: 693  Bit Score: 81.63  E-value: 4.70e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817  270 EVIILSVDKEKGRVAlglkqKEHnpWEDIEKKYPPGKRVRGKIVKLLPYGAFIEIEEGIEGLIHVSEMSWvKNIVDPNEV 349
Cdd:PRK11824 594 TVKIAATDGEAAEAA-----KER--IEGITAEPEVGEIYEGKVVRIVDFGAFVEILPGKDGLVHISEIAD-ERVEKVEDV 665
                         90       100
                 ....*....|....*....|....*.
gi 15604817  350 VNKGDEVEVVVLSIQKDeGKISLGLK 375
Cdd:PRK11824 666 LKEGDEVKVKVLEIDKR-GRIRLSRK 690
PRK07400 PRK07400
30S ribosomal protein S1; Reviewed
302-556 7.07e-16

30S ribosomal protein S1; Reviewed


Pssm-ID: 180960 [Multi-domain]  Cd Length: 318  Bit Score: 78.69  E-value: 7.07e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817  302 YPPGKRVRGKIVKLLPYGAFIEIEEGIEGLIHVSEMSwVKNIVDPNEVVNKGDEVEVVVLSIQKDEGKISLGLKQTKH-N 380
Cdd:PRK07400  29 FKPGDIVNGTVFSLEPRGALIDIGAKTAAFMPIQEMS-INRVEGPEEVLQPNETREFFILSDENEDGQLTLSIRRIEYmR 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817  381 PWDNIEEKYPIGLRVTAEIKNLTNYGAFVELEpGIEGLI---HISDMSwIKKVSHPSELFKKgntveavILSVDKESKKI 457
Cdd:PRK07400 108 AWERVRQLQKEDATVRSEVFATNRGGALVRIE-GLRGFIpgsHISTRK-PKEELVGEELPLK-------FLEVDEERNRL 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817  458 TLGVKQ-LTPNPWDEIEVmfpvGSDISGVVTKITAFGAFVELqNGIEGLIHVSELSEKPFAKIEDVLSIGDKVSAKVIKL 536
Cdd:PRK07400 179 VLSHRRaLVERKMNRLEV----GEVVVGTVRGIKPYGAFIDI-GGVSGLLHISEISHEHIETPHSVFNVNDEMKVMIIDL 253
                        250       260
                 ....*....|....*....|
gi 15604817  537 DPDHKKVSLSIKEFLVHGGD 556
Cdd:PRK07400 254 DAERGRISLSTKQLEPEPGD 273
S1_RPS1_repeat_hs4 cd05692
S1_RPS1_repeat_hs4: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
305-375 7.36e-16

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


Pssm-ID: 240197 [Multi-domain]  Cd Length: 69  Bit Score: 72.32  E-value: 7.36e-16
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15604817 305 GKRVRGKIVKLLPYGAFIEIEEGIEGLIHVSEMSWvKNIVDPNEVVNKGDEVEVVVLSIqKDEGKISLGLK 375
Cdd:cd05692   1 GSVVEGTVTRLKPFGAFVELGGGISGLVHISQIAH-KRVKDVKDVLKEGDKVKVKVLSI-DARGRISLSIK 69
S1_RPS1_repeat_ec3 cd05688
S1_RPS1_repeat_ec3: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
478-546 1.07e-15

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


Pssm-ID: 240193 [Multi-domain]  Cd Length: 68  Bit Score: 71.89  E-value: 1.07e-15
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15604817 478 VGSDISGVVTKITAFGAFVELqNGIEGLIHVSELSEKPFAKIEDVLSIGDKVSAKVIKLDPDHKKVSLS 546
Cdd:cd05688   1 EGDVVEGTVKSITDFGAFVDL-GGVDGLLHISDMSWGRVKHPSEVVNVGDEVEVKVLKIDKERKRISLG 68
S1 smart00316
Ribosomal protein S1-like RNA-binding domain;
219-288 2.85e-15

Ribosomal protein S1-like RNA-binding domain;


Pssm-ID: 197648 [Multi-domain]  Cd Length: 72  Bit Score: 70.71  E-value: 2.85e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15604817    219 IGERRKGIVKNITDFGVFLDL-DGIDGLLHITDMTWKRIRHPSEMVELNQELEVIILSVDKEKGRVALGLK 288
Cdd:smart00316   2 VGDVVEGTVTEITPGGAFVDLgNGVEGLIPISELSDKRVKDPEEVLKVGDEVKVKVLSVDEEKGRIILSLK 72
Tex COG2183
Transcriptional accessory protein Tex/SPT6 [Transcription];
214-291 3.93e-15

Transcriptional accessory protein Tex/SPT6 [Transcription];


Pssm-ID: 441786 [Multi-domain]  Cd Length: 719  Bit Score: 78.53  E-value: 3.93e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817 214 IEQITIGERRKGIVKNITDFGVFLDLdGI--DGLLHITDMTWKRIRHPSEMVELNQELEVIILSVDKEKGRVALGLKQKE 291
Cdd:COG2183 636 IEDLKPGMILEGTVTNVTDFGAFVDI-GVhqDGLVHISQLSDRFVKDPREVVKVGDIVKVKVLEVDLKRKRISLSMKLDD 714
S1_like cd00164
S1_like: Ribosomal protein S1-like RNA-binding domain. Found in a wide variety of ...
395-460 4.03e-15

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


Pssm-ID: 238094 [Multi-domain]  Cd Length: 65  Bit Score: 70.10  E-value: 4.03e-15
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15604817 395 VTAEIKNLTNYGAFVELEPGIEGLIHISDMSWiKKVSHPSELFKKGNTVEAVILSVDKESKKITLG 460
Cdd:cd00164   1 VTGKVVSITKFGVFVELEDGVEGLVHISELSD-KFVKDPSEVFKVGDEVEVKVLEVDPEKGRISLS 65
S1_Tex cd05685
S1_Tex: The C-terminal S1 domain of a transcription accessory factor called Tex, which has ...
479-546 4.34e-15

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


Pssm-ID: 240190 [Multi-domain]  Cd Length: 68  Bit Score: 69.95  E-value: 4.34e-15
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15604817 479 GSDISGVVTKITAFGAFVELQNGIEGLIHVSELSEKPFAKIEDVLSIGDKVSAKVIKLDPDHKKVSLS 546
Cdd:cd05685   1 GMVLEGVVTNVTDFGAFVDIGVKQDGLIHISKMADRFVSHPSDVVSVGDIVEVKVISIDEERGRISLS 68
S1_like cd00164
S1_like: Ribosomal protein S1-like RNA-binding domain. Found in a wide variety of ...
308-373 5.45e-15

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


Pssm-ID: 238094 [Multi-domain]  Cd Length: 65  Bit Score: 69.72  E-value: 5.45e-15
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15604817 308 VRGKIVKLLPYGAFIEIEEGIEGLIHVSEMSWvKNIVDPNEVVNKGDEVEVVVLSIQKDEGKISLG 373
Cdd:cd00164   1 VTGKVVSITKFGVFVELEDGVEGLVHISELSD-KFVKDPSEVFKVGDEVEVKVLEVDPEKGRISLS 65
YabR COG1098
Predicted RNA-binding protein, contains ribosomal protein S1 (RPS1) domain [General function ...
387-468 8.64e-15

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


Pssm-ID: 440715 [Multi-domain]  Cd Length: 130  Bit Score: 70.98  E-value: 8.64e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817 387 EKYPIGLRVTAEIKNLTNYGAFVELEPGIEGLIHISDMS--WIKKVshpSELFKKGNTVEAVILSVDkESKKITLGVKQL 464
Cdd:COG1098   1 MSIEVGDIVEGKVTGITPFGAFVELPEGTTGLVHISEIAdgYVKDI---NDYLKVGDEVKVKVLSID-EDGKISLSIKQA 76

                ....
gi 15604817 465 TPNP 468
Cdd:COG1098  77 EEKP 80
PRK08582 PRK08582
RNA-binding protein S1;
305-381 1.17e-14

RNA-binding protein S1;


Pssm-ID: 236305 [Multi-domain]  Cd Length: 139  Bit Score: 71.22  E-value: 1.17e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15604817  305 GKRVRGKIVKLLPYGAFIEIEEGIEGLIHVSEMS--WVKNIvdpNEVVNKGDEVEVVVLSIQKDeGKISLGLKQTKHNP 381
Cdd:PRK08582   6 GSKLQGKVTGITNFGAFVELPEGKTGLVHISEVAdnYVKDI---NDHLKVGDEVEVKVLNVEDD-GKIGLSIKKAKDRP 80
S1_Rrp5_repeat_sc12 cd05708
S1_Rrp5_repeat_sc12: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ...
478-548 1.29e-14

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


Pssm-ID: 240213 [Multi-domain]  Cd Length: 77  Bit Score: 68.90  E-value: 1.29e-14
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15604817 478 VGSDISGVVTKITAFGAFVELQN-GIEGLIHVSELSEKPFAKIEDVLSIGDKVSAKVIKLDPDHKKVSLSIK 548
Cdd:cd05708   2 VGQKIDGTVRRVEDYGVFIDIDGtNVSGLCHKSEISDNRVADASKLFRVGDKVRAKVLKIDAEKKRISLGLK 73
S1_Tex cd05685
S1_Tex: The C-terminal S1 domain of a transcription accessory factor called Tex, which has ...
220-285 3.11e-14

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


Pssm-ID: 240190 [Multi-domain]  Cd Length: 68  Bit Score: 67.64  E-value: 3.11e-14
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15604817 220 GERRKGIVKNITDFGVFLDLdGI--DGLLHITDMTWKRIRHPSEMVELNQELEVIILSVDKEKGRVAL 285
Cdd:cd05685   1 GMVLEGVVTNVTDFGAFVDI-GVkqDGLIHISKMADRFVSHPSDVVSVGDIVEVKVISIDEERGRISL 67
S1 pfam00575
S1 RNA binding domain; The S1 domain occurs in a wide range of RNA associated proteins. It is ...
476-547 4.22e-14

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


Pssm-ID: 425760 [Multi-domain]  Cd Length: 72  Bit Score: 67.31  E-value: 4.22e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15604817   476 FPVGSDISGVVTKITAFGAFVELQNGIEGLIHVSELSEKPFAKIEDVLSIGDKVSAKVIKLDPDHKKVSLSI 547
Cdd:pfam00575   1 PEKGDVVEGEVTRVTKGGAFVDLGNGVEGFIPISELSDDHVEDPDEVIKVGDEVKVKVLKVDKDRRRIILSI 72
S1_like cd00164
S1_like: Ribosomal protein S1-like RNA-binding domain. Found in a wide variety of ...
482-546 4.32e-14

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


Pssm-ID: 238094 [Multi-domain]  Cd Length: 65  Bit Score: 67.02  E-value: 4.32e-14
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15604817 482 ISGVVTKITAFGAFVELQNGIEGLIHVSELSEKPFAKIEDVLSIGDKVSAKVIKLDPDHKKVSLS 546
Cdd:cd00164   1 VTGKVVSITKFGVFVELEDGVEGLVHISELSDKFVKDPSEVFKVGDEVEVKVLEVDPEKGRISLS 65
PRK11824 PRK11824
polynucleotide phosphorylase/polyadenylase; Provisional
209-288 6.49e-14

polynucleotide phosphorylase/polyadenylase; Provisional


Pssm-ID: 236995 [Multi-domain]  Cd Length: 693  Bit Score: 74.70  E-value: 6.49e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817  209 KKA-ELIEQIT----IGERRKGIVKNITDFGVFLD-LDGIDGLLHITDMTWKRIRHPSEMVELNQELEVIILSVDKeKGR 282
Cdd:PRK11824 606 EAAkERIEGITaepeVGEIYEGKVVRIVDFGAFVEiLPGKDGLVHISEIADERVEKVEDVLKEGDEVKVKVLEIDK-RGR 684

                 ....*.
gi 15604817  283 VALGLK 288
Cdd:PRK11824 685 IRLSRK 690
S1_like cd00164
S1_like: Ribosomal protein S1-like RNA-binding domain. Found in a wide variety of ...
224-286 1.21e-13

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


Pssm-ID: 238094 [Multi-domain]  Cd Length: 65  Bit Score: 65.86  E-value: 1.21e-13
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15604817 224 KGIVKNITDFGVFLDL-DGIDGLLHITDMTWKRIRHPSEMVELNQELEVIILSVDKEKGRVALG 286
Cdd:cd00164   2 TGKVVSITKFGVFVELeDGVEGLVHISELSDKFVKDPSEVFKVGDEVEVKVLEVDPEKGRISLS 65
S1_DHX8_helicase cd05684
S1_DHX8_helicase: The N-terminal S1 domain of human ATP-dependent RNA helicase DHX8, a DEAH ...
305-375 1.66e-13

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


Pssm-ID: 240189 [Multi-domain]  Cd Length: 79  Bit Score: 65.72  E-value: 1.66e-13
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15604817 305 GKRVRGKIVKLLPYGAFIEIE---EGIEGLIHVSEMSWVKNIVDPNEVVNKGDEVEVVVLSIQKdeGKISLGLK 375
Cdd:cd05684   1 GKIYKGKVTSIMDFGCFVQLEglkGRKEGLVHISQLSFEGRVANPSDVVKRGQKVKVKVISIQN--GKISLSMK 72
PRK07252 PRK07252
S1 RNA-binding domain-containing protein;
478-548 1.79e-13

S1 RNA-binding domain-containing protein;


Pssm-ID: 180908 [Multi-domain]  Cd Length: 120  Bit Score: 67.03  E-value: 1.79e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15604817  478 VGSDISGVVTKITAFGAFVELQNGIEGLIHVSELSEKPFAKIEDVLSIGDKVSAKVIKLDPDHKKVSLSIK 548
Cdd:PRK07252   3 IGDKLKGTITGIKPYGAFVALENGTTGLIHISEIKTGFIDNIHQLLKVGEEVLVQVVDFDEYTGKASLSLR 73
S1 pfam00575
S1 RNA binding domain; The S1 domain occurs in a wide range of RNA associated proteins. It is ...
302-374 3.98e-13

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


Pssm-ID: 425760 [Multi-domain]  Cd Length: 72  Bit Score: 64.62  E-value: 3.98e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15604817   302 YPPGKRVRGKIVKLLPYGAFIEIEEGIEGLIHVSEMSWvKNIVDPNEVVNKGDEVEVVVLSIQKDEGKISLGL 374
Cdd:pfam00575   1 PEKGDVVEGEVTRVTKGGAFVDLGNGVEGFIPISELSD-DHVEDPDEVIKVGDEVKVKVLKVDKDRRRIILSI 72
S1_RPS1_repeat_ec4 cd05689
S1_RPS1_repeat_ec4: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
220-286 4.58e-13

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


Pssm-ID: 240194 [Multi-domain]  Cd Length: 72  Bit Score: 64.52  E-value: 4.58e-13
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817 220 GERRKGIVKNITDFGVFLDLD-GIDGLLHITDMTW--KRIrHPSEMVELNQELEVIILSVDKEKGRVALG 286
Cdd:cd05689   4 GTRLFGKVTNLTDYGCFVELEeGVEGLVHVSEMDWtnKNI-HPSKVVSLGDEVEVMVLDIDEERRRISLG 72
S1_Tex cd05685
S1_Tex: The C-terminal S1 domain of a transcription accessory factor called Tex, which has ...
392-459 4.88e-13

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: 64.18  E-value: 4.88e-13
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15604817 392 GLRVTAEIKNLTNYGAFVELEPGIEGLIHISDMSwIKKVSHPSELFKKGNTVEAVILSVDKESKKITL 459
Cdd:cd05685   1 GMVLEGVVTNVTDFGAFVDIGVKQDGLIHISKMA-DRFVSHPSDVVSVGDIVEVKVISIDEERGRISL 67
S1_dom_CvfD NF040579
CvfD/Ygs/GSP13 family RNA-binding post-transcriptional regulator; CvfD, Ygs, and GSP13 form a ...
389-468 5.20e-13

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


Pssm-ID: 468553 [Multi-domain]  Cd Length: 113  Bit Score: 65.53  E-value: 5.20e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817  389 YPIGLRVTAEIKNLTNYGAFVELEPGIEGLIHISDMS--WIKKVshpSELFKKGNTVEAVILSVDKESKKITLGVKQLTP 466
Cdd:NF040579   1 YKIGDIVEGKVTGIQPYGAFVALDEHTQGLIHISEIKhgYVKDI---NDFLKVGQEVKVKVLDIDEYTGKISLSLRALEE 77

                 ..
gi 15604817  467 NP 468
Cdd:NF040579  78 AP 79
S1 pfam00575
S1 RNA binding domain; The S1 domain occurs in a wide range of RNA associated proteins. It is ...
389-461 6.81e-13

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


Pssm-ID: 425760 [Multi-domain]  Cd Length: 72  Bit Score: 63.85  E-value: 6.81e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15604817   389 YPIGLRVTAEIKNLTNYGAFVELEPGIEGLIHISDMSWiKKVSHPSELFKKGNTVEAVILSVDKESKKITLGV 461
Cdd:pfam00575   1 PEKGDVVEGEVTRVTKGGAFVDLGNGVEGFIPISELSD-DHVEDPDEVIKVGDEVKVKVLKVDKDRRRIILSI 72
PRK05807 PRK05807
RNA-binding protein S1;
476-553 1.32e-12

RNA-binding protein S1;


Pssm-ID: 235614 [Multi-domain]  Cd Length: 136  Bit Score: 65.15  E-value: 1.32e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15604817  476 FPVGSDISGVVTKITAFGAFVELqNGIEGLIHVSELSEKPFAKIEDVLSIGDKVSAKVIKLDpDHKKVSLSIKEFLVH 553
Cdd:PRK05807   3 LKAGSILEGTVVNITNFGAFVEV-EGKTGLVHISEVADTYVKDIREHLKEQDKVKVKVISID-DNGKISLSIKQAMKQ 78
S1_PNPase cd04472
S1_PNPase: Polynucleotide phosphorylase (PNPase), ), S1-like RNA-binding domain. PNPase is a ...
305-372 2.04e-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: 62.56  E-value: 2.04e-12
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817 305 GKRVRGKIVKLLPYGAFIEIEEGIEGLIHVSEMS--WVKNIVDpneVVNKGDEVEVVVLSIQKDeGKISL 372
Cdd:cd04472   1 GKIYEGKVVKIKDFGAFVEILPGKDGLVHISELSdeRVEKVED---VLKVGDEVKVKVIEVDDR-GRISL 66
Tex COG2183
Transcriptional accessory protein Tex/SPT6 [Transcription];
484-548 2.72e-12

Transcriptional accessory protein Tex/SPT6 [Transcription];


Pssm-ID: 441786 [Multi-domain]  Cd Length: 719  Bit Score: 69.67  E-value: 2.72e-12
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15604817 484 GVVTKITAFGAFVEL---QNgieGLIHVSELSEKPFAKIEDVLSIGDKVSAKVIKLDPDHKKVSLSIK 548
Cdd:COG2183 647 GTVTNVTDFGAFVDIgvhQD---GLVHISQLSDRFVKDPREVVKVGDIVKVKVLEVDLKRKRISLSMK 711
S1_Rrp5_repeat_sc12 cd05708
S1_Rrp5_repeat_sc12: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ...
218-288 3.46e-12

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


Pssm-ID: 240213 [Multi-domain]  Cd Length: 77  Bit Score: 61.96  E-value: 3.46e-12
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15604817 218 TIGERRKGIVKNITDFGVFLDLDGID--GLLHITDMTWKRIRHPSEMVELNQELEVIILSVDKEKGRVALGLK 288
Cdd:cd05708   1 KVGQKIDGTVRRVEDYGVFIDIDGTNvsGLCHKSEISDNRVADASKLFRVGDKVRAKVLKIDAEKKRISLGLK 73
S1_DHX8_helicase cd05684
S1_DHX8_helicase: The N-terminal S1 domain of human ATP-dependent RNA helicase DHX8, a DEAH ...
483-549 1.91e-11

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


Pssm-ID: 240189 [Multi-domain]  Cd Length: 79  Bit Score: 59.95  E-value: 1.91e-11
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15604817 483 SGVVTKITAFGAFVELQN---GIEGLIHVSELS-EKPFAKIEDVLSIGDKVSAKVIKLDPDhkKVSLSIKE 549
Cdd:cd05684   5 KGKVTSIMDFGCFVQLEGlkgRKEGLVHISQLSfEGRVANPSDVVKRGQKVKVKVISIQNG--KISLSMKD 73
S1 pfam00575
S1 RNA binding domain; The S1 domain occurs in a wide range of RNA associated proteins. It is ...
219-287 1.94e-11

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


Pssm-ID: 425760 [Multi-domain]  Cd Length: 72  Bit Score: 59.61  E-value: 1.94e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817   219 IGERRKGIVKNITDFGVFLDLD-GIDGLLHITDMTWKRIRHPSEMVELNQELEVIILSVDKEKGRVALGL 287
Cdd:pfam00575   3 KGDVVEGEVTRVTKGGAFVDLGnGVEGFIPISELSDDHVEDPDEVIKVGDEVKVKVLKVDKDRRRIILSI 72
S1_IF2_alpha cd04452
S1_IF2_alpha: The alpha subunit of translation Initiation Factor 2, S1-like RNA-binding domain. ...
478-548 2.92e-11

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: 59.52  E-value: 2.92e-11
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15604817 478 VGSDISGVVTKITAFGAFVELQ--NGIEGLIHVSELSEKPFAKIEDVLSIGDKVSAKVIKLDPDHKKVSLSIK 548
Cdd:cd04452   3 EGELVVVTVKSIADMGAYVSLLeyGNIEGMILLSELSRRRIRSIRKLVKVGRKEVVKVIRVDKEKGYIDLSKK 75
S1_RPS1_repeat_ec6 cd05691
S1_RPS1_repeat_ec6: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
479-548 3.41e-11

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: 59.21  E-value: 3.41e-11
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817 479 GSDISGVVTKITAFGAFVELQNGIEGLIHVSELSEKPFAKIEDVLSIGDKVSAKVIKLDPDHKKVSLSIK 548
Cdd:cd05691   1 GSIVTGKVTEVDAKGATVKLGDGVEGFLRAAELSRDRVEDATERFKVGDEVEAKITNVDRKNRKISLSIK 70
S1_Tex cd05685
S1_Tex: The C-terminal S1 domain of a transcription accessory factor called Tex, which has ...
305-372 4.81e-11

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: 58.40  E-value: 4.81e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15604817 305 GKRVRGKIVKLLPYGAFIEIEEGIEGLIHVSEMSwVKNIVDPNEVVNKGDEVEVVVLSIQKDEGKISL 372
Cdd:cd05685   1 GMVLEGVVTNVTDFGAFVDIGVKQDGLIHISKMA-DRFVSHPSDVVSVGDIVEVKVISIDEERGRISL 67
S1_RPS1_repeat_hs4 cd05692
S1_RPS1_repeat_hs4: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
392-462 5.96e-11

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


Pssm-ID: 240197 [Multi-domain]  Cd Length: 69  Bit Score: 58.45  E-value: 5.96e-11
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15604817 392 GLRVTAEIKNLTNYGAFVELEPGIEGLIHISDMSWiKKVSHPSELFKKGNTVEAVILSVDKEsKKITLGVK 462
Cdd:cd05692   1 GSVVEGTVTRLKPFGAFVELGGGISGLVHISQIAH-KRVKDVKDVLKEGDKVKVKVLSIDAR-GRISLSIK 69
S1 smart00316
Ribosomal protein S1-like RNA-binding domain;
132-199 6.13e-11

Ribosomal protein S1-like RNA-binding domain;


Pssm-ID: 197648 [Multi-domain]  Cd Length: 72  Bit Score: 58.38  E-value: 6.13e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15604817    132 EEGSIVKGQITRKVKGGLIVDI--GMEAFLPGSQIDNKKIKNLDDY--VGKVCEFKILKINVDRRNVVVSRR 199
Cdd:smart00316   1 EVGDVVEGTVTEITPGGAFVDLgnGVEGLIPISELSDKRVKDPEEVlkVGDEVKVKVLSVDEEKGRIILSLK 72
S1_RPS1_repeat_ec4 cd05689
S1_RPS1_repeat_ec4: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
476-545 1.02e-10

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: 57.59  E-value: 1.02e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15604817 476 FPVGSDISGVVTKITAFGAFVELQNGIEGLIHVSEL--SEKPFAKIEdVLSIGDKVSAKVIKLDPDHKKVSL 545
Cdd:cd05689   1 YPEGTRLFGKVTNLTDYGCFVELEEGVEGLVHVSEMdwTNKNIHPSK-VVSLGDEVEVMVLDIDEERRRISL 71
S1_RPS1_repeat_ec5 cd05690
S1_RPS1_repeat_ec5: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
479-545 3.79e-10

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: 55.96  E-value: 3.79e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15604817 479 GSDISGVVTKITAFGAFVELQNGIEGLIHVSELSEKPFAK-IEDVLSIGDKVSAKVIKLDPDHKKVSL 545
Cdd:cd05690   1 GTVVSGKIKSITDFGIFVGLDGGIDGLVHISDISWTQRVRhPSEIYKKGQEVEAVVLNIDVERERISL 68
S1_Rrp5_repeat_sc12 cd05708
S1_Rrp5_repeat_sc12: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ...
392-462 6.50e-10

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


Pssm-ID: 240213 [Multi-domain]  Cd Length: 77  Bit Score: 55.41  E-value: 6.50e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15604817 392 GLRVTAEIKNLTNYGAFVELE-PGIEGLIHISDMSwIKKVSHPSELFKKGNTVEAVILSVDKESKKITLGVK 462
Cdd:cd05708   3 GQKIDGTVRRVEDYGVFIDIDgTNVSGLCHKSEIS-DNRVADASKLFRVGDKVRAKVLKIDAEKKRISLGLK 73
S1_Rrp5_repeat_sc12 cd05708
S1_Rrp5_repeat_sc12: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ...
305-375 6.82e-10

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


Pssm-ID: 240213 [Multi-domain]  Cd Length: 77  Bit Score: 55.41  E-value: 6.82e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15604817 305 GKRVRGKIVKLLPYGAFIEIE-EGIEGLIHVSEMSwVKNIVDPNEVVNKGDEVEVVVLSIQKDEGKISLGLK 375
Cdd:cd05708   3 GQKIDGTVRRVEDYGVFIDIDgTNVSGLCHKSEIS-DNRVADASKLFRVGDKVRAKVLKIDAEKKRISLGLK 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 ...
479-548 7.00e-10

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: 55.31  E-value: 7.00e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817 479 GSDISGVVTKITAFGAFVELQNGIEGLIHVSELSEKPFAKIEDVLSIGDKVSAKVIKLDPDHKKVSLSIK 548
Cdd:cd05698   1 GLKTHGTIVKVKPNGCIVSFYNNVKGFLPKSELSEAFIKDPEEHFRVGQVVKVKVLSCDPEQQRLLLSCK 70
PRK08059 PRK08059
general stress protein 13; Validated
387-468 7.26e-10

general stress protein 13; Validated


Pssm-ID: 181215 [Multi-domain]  Cd Length: 123  Bit Score: 56.98  E-value: 7.26e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817  387 EKYPIGLRVTAEIKNLTNYGAFVELEPGIEGLIHISDMS--WIKKVshpSELFKKGNTVEAVILSVDKESKKITLGVKQL 464
Cdd:PRK08059   3 SQYEVGSVVTGKVTGIQPYGAFVALDEETQGLVHISEIThgFVKDI---HDFLSVGDEVKVKVLSVDEEKGKISLSIRAT 79

                 ....
gi 15604817  465 TPNP 468
Cdd:PRK08059  80 EEAP 83
S1_Rrp5_repeat_hs8_sc7 cd04461
S1_Rrp5_repeat_hs8_sc7: Rrp5 Homo sapiens S1 repeat 8 (hs8) and Saccharomyces cerevisiae S1 ...
392-459 8.89e-10

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: 55.29  E-value: 8.89e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15604817 392 GLRVTAEIKNLTNYGAFVELEPGIEGLIHISDMSwIKKVSHPSELFKKGNTVEAVILSVDKESKKITL 459
Cdd:cd04461  15 GMVVHGYVRNITPYGVFVEFLGGLTGLAPKSYIS-DEFVTDPSFGFKKGQSVTAKVTSVDEEKQRFLL 81
PRK05807 PRK05807
RNA-binding protein S1;
305-376 8.89e-10

RNA-binding protein S1;


Pssm-ID: 235614 [Multi-domain]  Cd Length: 136  Bit Score: 57.06  E-value: 8.89e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15604817  305 GKRVRGKIVKLLPYGAFIEIeEGIEGLIHVSEM--SWVKNIvdpNEVVNKGDEVEVVVLSIQkDEGKISLGLKQ 376
Cdd:PRK05807   6 GSILEGTVVNITNFGAFVEV-EGKTGLVHISEVadTYVKDI---REHLKEQDKVKVKVISID-DNGKISLSIKQ 74
PRK07252 PRK07252
S1 RNA-binding domain-containing protein;
305-375 1.26e-09

S1 RNA-binding domain-containing protein;


Pssm-ID: 180908 [Multi-domain]  Cd Length: 120  Bit Score: 56.25  E-value: 1.26e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15604817  305 GKRVRGKIVKLLPYGAFIEIEEGIEGLIHVSEM--SWVKNIvdpNEVVNKGDEVEVVVLSIQKDEGKISLGLK 375
Cdd:PRK07252   4 GDKLKGTITGIKPYGAFVALENGTTGLIHISEIktGFIDNI---HQLLKVGEEVLVQVVDFDEYTGKASLSLR 73
S1_RNase_R cd04471
S1_RNase_R: RNase R C-terminal S1 domain. RNase R is a processive 3' to 5' exoribonuclease, ...
478-547 1.45e-09

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


Pssm-ID: 239917 [Multi-domain]  Cd Length: 83  Bit Score: 54.71  E-value: 1.45e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817 478 VGSDISGVVTKITAFGAFVELQN-GIEGLIHVSELSEKPFAKIED-----------VLSIGDKVSAKVIKLDPDHKKVSL 545
Cdd:cd04471   1 VGEEFDGVISGVTSFGLFVELDNlTVEGLVHVSTLGDDYYEFDEEnhalvgertgkVFRLGDKVKVRVVRVDLDRRKIDF 80

                ..
gi 15604817 546 SI 547
Cdd:cd04471  81 EL 82
S1_IF2_alpha cd04452
S1_IF2_alpha: The alpha subunit of translation Initiation Factor 2, S1-like RNA-binding domain. ...
308-376 1.59e-09

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


Pssm-ID: 239899 [Multi-domain]  Cd Length: 76  Bit Score: 54.51  E-value: 1.59e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15604817 308 VRGKIVKLLPYGAFIEIEE--GIEGLIHVSEMS--WVKNIvdpNEVVNKGDEVEVVVLSIQKDEGKISLGLKQ 376
Cdd:cd04452   7 VVVTVKSIADMGAYVSLLEygNIEGMILLSELSrrRIRSI---RKLVKVGRKEVVKVIRVDKEKGYIDLSKKR 76
S1_DHX8_helicase cd05684
S1_DHX8_helicase: The N-terminal S1 domain of human ATP-dependent RNA helicase DHX8, a DEAH ...
224-280 2.22e-09

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: 54.17  E-value: 2.22e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15604817 224 KGIVKNITDFGVFLDLDGI----DGLLHITDMTWK-RIRHPSEMVELNQELEVIILSVDKEK 280
Cdd:cd05684   5 KGKVTSIMDFGCFVQLEGLkgrkEGLVHISQLSFEgRVANPSDVVKRGQKVKVKVISIQNGK 66
S1 pfam00575
S1 RNA binding domain; The S1 domain occurs in a wide range of RNA associated proteins. It is ...
132-198 2.83e-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: 53.45  E-value: 2.83e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15604817   132 EEGSIVKGQITRKVKGGLIVDIG--MEAFLPGSQIDNKKIKNLDD--YVGKVCEFKILKINVDRRNVVVSR 198
Cdd:pfam00575   2 EKGDVVEGEVTRVTKGGAFVDLGngVEGFIPISELSDDHVEDPDEviKVGDEVKVKVLKVDKDRRRIILSI 72
PLN00207 PLN00207
polyribonucleotide nucleotidyltransferase; Provisional
486-568 4.87e-09

polyribonucleotide nucleotidyltransferase; Provisional


Pssm-ID: 215104 [Multi-domain]  Cd Length: 891  Bit Score: 59.14  E-value: 4.87e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817  486 VTKITAFGAFVELQNGIEGLIHVSELSEKPFAKIEDVLSIGDKVSAKVIKLDpDHKKVSLSIKEFLVhggdaghDAEEES 565
Cdd:PLN00207 762 IKSIAPYGAFVEIAPGREGLCHISELSSNWLAKPEDAFKVGDRIDVKLIEVN-DKGQLRLSRRALLP-------EANSEK 833

                 ...
gi 15604817  566 SDR 568
Cdd:PLN00207 834 SSQ 836
S1_Rrp5_repeat_hs8_sc7 cd04461
S1_Rrp5_repeat_hs8_sc7: Rrp5 Homo sapiens S1 repeat 8 (hs8) and Saccharomyces cerevisiae S1 ...
478-547 4.96e-09

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: 53.36  E-value: 4.96e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817 478 VGSDISGVVTKITAFGAFVELQNGIEGLIHVSELSEKPFAKIEDVLSIGDKVSAKVIKLDPDHKKVSLSI 547
Cdd:cd04461  14 PGMVVHGYVRNITPYGVFVEFLGGLTGLAPKSYISDEFVTDPSFGFKKGQSVTAKVTSVDEEKQRFLLSL 83
PRK03987 PRK03987
translation initiation factor IF-2 subunit alpha; Validated
484-548 5.28e-09

translation initiation factor IF-2 subunit alpha; Validated


Pssm-ID: 235188 [Multi-domain]  Cd Length: 262  Bit Score: 57.14  E-value: 5.28e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15604817  484 GVVTKITAFGAFVELQ--NGIEGLIHVSELSEKPFAKIEDVLSIGDKVSAKVIKLDPDHKKVSLSIK 548
Cdd:PRK03987  14 GTVKEVKDFGAFVTLDeyPGKEGFIHISEVASGWVKNIRDHVKEGQKVVCKVIRVDPRKGHIDLSLK 80
S1_RPS1_repeat_hs4 cd05692
S1_RPS1_repeat_hs4: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
225-288 5.36e-09

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: 52.67  E-value: 5.36e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15604817 225 GIVKNITDFGVFLDL-DGIDGLLHITDMTWKRIRHPSEMVELNQELEVIILSVDkEKGRVALGLK 288
Cdd:cd05692   6 GTVTRLKPFGAFVELgGGISGLVHISQIAHKRVKDVKDVLKEGDKVKVKVLSID-ARGRISLSIK 69
PRK11824 PRK11824
polynucleotide phosphorylase/polyadenylase; Provisional
383-452 8.06e-09

polynucleotide phosphorylase/polyadenylase; Provisional


Pssm-ID: 236995 [Multi-domain]  Cd Length: 693  Bit Score: 58.52  E-value: 8.06e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817  383 DNIEEKYPIGLRVTAEIKNLTNYGAFVELEPGIEGLIHISDMSWiKKVSHPSELFKKGNTVEAVILSVDK 452
Cdd:PRK11824 613 EGITAEPEVGEIYEGKVVRIVDFGAFVEILPGKDGLVHISEIAD-ERVEKVEDVLKEGDEVKVKVLEIDK 681
S1_IF2_alpha cd04452
S1_IF2_alpha: The alpha subunit of translation Initiation Factor 2, S1-like RNA-binding domain. ...
395-463 8.63e-09

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


Pssm-ID: 239899 [Multi-domain]  Cd Length: 76  Bit Score: 52.20  E-value: 8.63e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15604817 395 VTAEIKNLTNYGAFVELE--PGIEGLIHISDMS--WIKKVshpSELFKKGNTVEAVILSVDKESKKITLGVKQ 463
Cdd:cd04452   7 VVVTVKSIADMGAYVSLLeyGNIEGMILLSELSrrRIRSI---RKLVKVGRKEVVKVIRVDKEKGYIDLSKKR 76
Tex COG2183
Transcriptional accessory protein Tex/SPT6 [Transcription];
319-378 9.33e-09

Transcriptional accessory protein Tex/SPT6 [Transcription];


Pssm-ID: 441786 [Multi-domain]  Cd Length: 719  Bit Score: 58.11  E-value: 9.33e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15604817 319 GAFIEIeeGI--EGLIHVSEMS--WVKnivDPNEVVNKGDEVEVVVLSIQKDEGKISLGLKQTK 378
Cdd:COG2183 656 GAFVDI--GVhqDGLVHISQLSdrFVK---DPREVVKVGDIVKVKVLEVDLKRKRISLSMKLDD 714
S1_DHX8_helicase cd05684
S1_DHX8_helicase: The N-terminal S1 domain of human ATP-dependent RNA helicase DHX8, a DEAH ...
399-462 1.07e-08

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: 52.24  E-value: 1.07e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15604817 399 IKNLTNYGAFVELE---PGIEGLIHISDMSWIKKVSHPSELFKKGNTVEAVILSVdkESKKITLGVK 462
Cdd:cd05684   8 VTSIMDFGCFVQLEglkGRKEGLVHISQLSFEGRVANPSDVVKRGQKVKVKVISI--QNGKISLSMK 72
S1_RPS1_repeat_ec6 cd05691
S1_RPS1_repeat_ec6: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
392-464 1.10e-08

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


Pssm-ID: 240196 [Multi-domain]  Cd Length: 73  Bit Score: 51.89  E-value: 1.10e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15604817 392 GLRVTAEIKNLTNYGAFVELEPGIEGLIHISDMSwIKKVSHPSELFKKGNTVEAVILSVDKESKKITLGVKQL 464
Cdd:cd05691   1 GSIVTGKVTEVDAKGATVKLGDGVEGFLRAAELS-RDRVEDATERFKVGDEVEAKITNVDRKNRKISLSIKAK 72
S1 smart00316
Ribosomal protein S1-like RNA-binding domain;
51-115 1.12e-08

Ribosomal protein S1-like RNA-binding domain;


Pssm-ID: 197648 [Multi-domain]  Cd Length: 72  Bit Score: 51.84  E-value: 1.12e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817     51 PGAILKGTVVDISKDFVVVDVGLKSEGVIPMSEFID-----SSEGLTVGAEVEVYLDQTEDDEGKVVLSR 115
Cdd:smart00316   2 VGDVVEGTVTEITPGGAFVDLGNGVEGLIPISELSDkrvkdPEEVLKVGDEVKVKVLSVDEEKGRIILSL 71
PLN00207 PLN00207
polyribonucleotide nucleotidyltransferase; Provisional
398-471 1.15e-08

polyribonucleotide nucleotidyltransferase; Provisional


Pssm-ID: 215104 [Multi-domain]  Cd Length: 891  Bit Score: 57.98  E-value: 1.15e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15604817  398 EIKNLTNYGAFVELEPGIEGLIHISDMS--WIKKvshPSELFKKGNTVEAVILSVDKESkKITLGVKQLTPNPWDE 471
Cdd:PLN00207 761 EIKSIAPYGAFVEIAPGREGLCHISELSsnWLAK---PEDAFKVGDRIDVKLIEVNDKG-QLRLSRRALLPEANSE 832
PRK05807 PRK05807
RNA-binding protein S1;
220-316 1.37e-08

RNA-binding protein S1;


Pssm-ID: 235614 [Multi-domain]  Cd Length: 136  Bit Score: 53.60  E-value: 1.37e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817  220 GERRKGIVKNITDFGVFLDLDGIDGLLHITDMTWKRIRHPSEMVELNQELEVIILSVDkEKGRVALGLKQ-----KEHNP 294
Cdd:PRK05807   6 GSILEGTVVNITNFGAFVEVEGKTGLVHISEVADTYVKDIREHLKEQDKVKVKVISID-DNGKISLSIKQamkqkKSVKP 84
                         90       100
                 ....*....|....*....|....*.
gi 15604817  295 ----WEDiEKKYPPGKRVRGKIVKLL 316
Cdd:PRK05807  85 aeidWQK-EKNKNNNGNFEDRLSKFL 109
PRK08059 PRK08059
general stress protein 13; Validated
215-306 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 15604817  215 EQITIGERRKGIVKNITDFGVFLDLD-GIDGLLHITDMTWKRIRHPSEMVELNQELEVIILSVDKEKGRVALGLKQKEHN 293
Cdd:PRK08059   3 SQYEVGSVVTGKVTGIQPYGAFVALDeETQGLVHISEITHGFVKDIHDFLSVGDEVKVKVLSVDEEKGKISLSIRATEEA 82
                         90
                 ....*....|...
gi 15604817  294 PWEDIEKKYPPGK 306
Cdd:PRK08059  83 PEAKRKKGKILIP 95
Pnp COG1185
Polyribonucleotide nucleotidyltransferase (polynucleotide phosphorylase) [Translation, ...
391-452 2.03e-08

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


Pssm-ID: 440798 [Multi-domain]  Cd Length: 686  Bit Score: 56.94  E-value: 2.03e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15604817 391 IGLRVTAEIKNLTNYGAFVELEPGIEGLIHISDMSWiKKVSHPSELFKKGNTVEAVILSVDK 452
Cdd:COG1185 616 VGEIYEGKVVRIMDFGAFVEILPGKDGLVHISELAD-ERVEKVEDVLKEGDEVKVKVLEIDD 676
VacB COG0557
Exoribonuclease R [Transcription];
478-547 2.08e-08

Exoribonuclease R [Transcription];


Pssm-ID: 440323 [Multi-domain]  Cd Length: 711  Bit Score: 57.04  E-value: 2.08e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817 478 VGSDISGVVTKITAFGAFVELQN-GIEGLIHVSELSEKPFAKIED-----------VLSIGDKVSAKVIKLDPDHKKVSL 545
Cdd:COG0557 622 VGEEFEGVISGVTSFGLFVELDElGVEGLVHVSSLGDDYYEYDERrqalvgertgkRYRLGDRVEVRVVRVDLDRRQIDF 701

                ..
gi 15604817 546 SI 547
Cdd:COG0557 702 EL 703
PRK03987 PRK03987
translation initiation factor IF-2 subunit alpha; Validated
299-375 3.05e-08

translation initiation factor IF-2 subunit alpha; Validated


Pssm-ID: 235188 [Multi-domain]  Cd Length: 262  Bit Score: 54.83  E-value: 3.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817  299 EKKYP-PGKRVRGKIVKLLPYGAFIEIEE--GIEGLIHVSEMS--WVKNIVDpneVVNKGDEVEVVVLSIQKDEGKISLG 373
Cdd:PRK03987   2 RKEWPeEGELVVGTVKEVKDFGAFVTLDEypGKEGFIHISEVAsgWVKNIRD---HVKEGQKVVCKVIRVDPRKGHIDLS 78

                 ..
gi 15604817  374 LK 375
Cdd:PRK03987  79 LK 80
S1_Rrp5_repeat_hs8_sc7 cd04461
S1_Rrp5_repeat_hs8_sc7: Rrp5 Homo sapiens S1 repeat 8 (hs8) and Saccharomyces cerevisiae S1 ...
214-287 4.21e-08

S1_Rrp5_repeat_hs8_sc7: Rrp5 Homo sapiens S1 repeat 8 (hs8) and Saccharomyces cerevisiae S1 repeat 7 (sc7)-like domains. Rrp5 is a trans-acting factor important for biogenesis of both the 40S and 60S eukaryotic ribosomal subunits. Rrp5 has two distinct regions, an N-terminal region containing tandemly repeated S1 RNA-binding domains (12 S1 repeats in S. cerevisiae Rrp5 and 14 S1 repeats in H. sapiens Rrp5) and a C-terminal region containing tetratricopeptide repeat (TPR) motifs thought to be involved in protein-protein interactions. Mutational studies have shown that each region represents a specific functional domain. Deletions within the S1-containing region inhibit pre-rRNA processing at either site A3 or A2, whereas deletions within the TPR region confer an inability to support cleavage of A0-A2. This CD includes H. sapiens S1 repeat 8 and S. cerevisiae S1 repeat 7. Rrp5 is found in eukaryotes but not in prokaryotes or archaea.


Pssm-ID: 239908 [Multi-domain]  Cd Length: 83  Bit Score: 50.66  E-value: 4.21e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15604817 214 IEQITIGERRKGIVKNITDFGVFLD-LDGIDGLLHITDMTWKRIRHPSEMVELNQELEVIILSVDKEKGRVALGL 287
Cdd:cd04461   9 FSDLKPGMVVHGYVRNITPYGVFVEfLGGLTGLAPKSYISDEFVTDPSFGFKKGQSVTAKVTSVDEEKQRFLLSL 83
RpsA COG0539
Ribosomal protein S1 [Translation, ribosomal structure and biogenesis]; Ribosomal protein S1 ...
350-551 7.94e-08

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


Pssm-ID: 440305 [Multi-domain]  Cd Length: 348  Bit Score: 54.28  E-value: 7.94e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817 350 VNKGDEVEVVVLSIQKDEGKISLGLKQtkhnpwdnieekypiglrvtaeiknltnygafvelepgiEGLIHISDMSWikk 429
Cdd:COG0539  16 LKEGDIVKGTVVSIDDDEVLVDIGYKS---------------------------------------EGIIPLSEFSD--- 53
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817 430 vSHPSELFKKGNTVEAVILSVDKESKKITLGVKQL-TPNPWDEIEVMFPVGSDISGVVTKITAFGAFVELqNGIEGLIHV 508
Cdd:COG0539  54 -EPGELEVKVGDEVEVYVEKVEDGEGEIVLSKKKAdREKAWEELEEAFENGEPVEGKVKGVVKGGLIVDI-GGVRAFLPA 131
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 15604817 509 SELSEKPFAKIEDVlsIGDKVSAKVIKLDPDHKKVSLSIKEFL 551
Cdd:COG0539 132 SQVDVRPVRDLDEY--VGKTLEFKIIKLDRKRNNVVVSRRAVL 172
S1_RPS1_repeat_ec1_hs1 cd05687
S1_RPS1_repeat_ec1_hs1: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
305-372 7.95e-08

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


Pssm-ID: 240192 [Multi-domain]  Cd Length: 70  Bit Score: 49.45  E-value: 7.95e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15604817 305 GKRVRGKIVKLLPYGAFIEIEEGIEGLIHVSEMSWvKNIVDPNEVVNKGDEVEVVVLSIQKDEGKISL 372
Cdd:cd05687   1 GDIVKGTVVSVDDDEVLVDIGYKSEGIIPISEFSD-DPIENGEDEVKVGDEVEVYVLRVEDEEGNVVL 67
S1_PNPase cd04472
S1_PNPase: Polynucleotide phosphorylase (PNPase), ), S1-like RNA-binding domain. PNPase is a ...
220-285 1.17e-07

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


Pssm-ID: 239918 [Multi-domain]  Cd Length: 68  Bit Score: 48.69  E-value: 1.17e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15604817 220 GERRKGIVKNITDFGVFLD-LDGIDGLLHITDMTWKRIRHPSEMVELNQELEVIILSVDKeKGRVAL 285
Cdd:cd04472   1 GKIYEGKVVKIKDFGAFVEiLPGKDGLVHISELSDERVEKVEDVLKVGDEVKVKVIEVDD-RGRISL 66
S1_IF2_alpha cd04452
S1_IF2_alpha: The alpha subunit of translation Initiation Factor 2, S1-like RNA-binding domain. ...
225-289 1.17e-07

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


Pssm-ID: 239899 [Multi-domain]  Cd Length: 76  Bit Score: 49.12  E-value: 1.17e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15604817 225 GIVKNITDFGVFLDLD---GIDGLLHITDMTWKRIRHPSEMVELNQELEVIILSVDKEKGRVALGLKQ 289
Cdd:cd04452   9 VTVKSIADMGAYVSLLeygNIEGMILLSELSRRRIRSIRKLVKVGRKEVVKVIRVDKEKGYIDLSKKR 76
Tex COG2183
Transcriptional accessory protein Tex/SPT6 [Transcription];
401-459 3.18e-07

Transcriptional accessory protein Tex/SPT6 [Transcription];


Pssm-ID: 441786 [Multi-domain]  Cd Length: 719  Bit Score: 53.49  E-value: 3.18e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15604817 401 NLTNYGAFVELepGI--EGLIHISDMSwiKK-VSHPSELFKKGNTVEAVILSVDKESKKITL 459
Cdd:COG2183 651 NVTDFGAFVDI--GVhqDGLVHISQLS--DRfVKDPREVVKVGDIVKVKVLEVDLKRKRISL 708
S1 pfam00575
S1 RNA binding domain; The S1 domain occurs in a wide range of RNA associated proteins. It is ...
52-115 4.68e-07

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: 47.28  E-value: 4.68e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15604817    52 GAILKGTVVDISKDFVVVDVGLKSEGVIPMSEF-----IDSSEGLTVGAEVEVYLDQTEDDEGKVVLSR 115
Cdd:pfam00575   4 GDVVEGEVTRVTKGGAFVDLGNGVEGFIPISELsddhvEDPDEVIKVGDEVKVKVLKVDKDRRRIILSI 72
PRK05807 PRK05807
RNA-binding protein S1;
395-467 1.09e-06

RNA-binding protein S1;


Pssm-ID: 235614 [Multi-domain]  Cd Length: 136  Bit Score: 48.20  E-value: 1.09e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15604817  395 VTAEIKNLTNYGAFVELEpGIEGLIHISDM--SWIKKVshpSELFKKGNTVEAVILSVDkESKKITLGVKQLTPN 467
Cdd:PRK05807   9 LEGTVVNITNFGAFVEVE-GKTGLVHISEVadTYVKDI---REHLKEQDKVKVKVISID-DNGKISLSIKQAMKQ 78
PRK08582 PRK08582
RNA-binding protein S1;
391-468 1.51e-06

RNA-binding protein S1;


Pssm-ID: 236305 [Multi-domain]  Cd Length: 139  Bit Score: 47.72  E-value: 1.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817  391 IGLRVTAEIKNLTNYGAFVELEPGIEGLIHISDMS--WIKKVshpSELFKKGNTVEAVILSVDKESkKITLGVKQLTPNP 468
Cdd:PRK08582   5 VGSKLQGKVTGITNFGAFVELPEGKTGLVHISEVAdnYVKDI---NDHLKVGDEVEVKVLNVEDDG-KIGLSIKKAKDRP 80
S1_RPS1_repeat_ec1_hs1 cd05687
S1_RPS1_repeat_ec1_hs1: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
479-548 2.20e-06

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: 45.21  E-value: 2.20e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817 479 GSDISGVVTKITAFGAFVELQNGIEGLIHVSELSEKPFAKIEDVLSIGDKVSAKVIKLDPDHKKVSLSIK 548
Cdd:cd05687   1 GDIVKGTVVSVDDDEVLVDIGYKSEGIIPISEFSDDPIENGEDEVKVGDEVEVYVLRVEDEEGNVVLSKR 70
PRK07252 PRK07252
S1 RNA-binding domain-containing protein;
391-464 2.79e-06

S1 RNA-binding domain-containing protein;


Pssm-ID: 180908 [Multi-domain]  Cd Length: 120  Bit Score: 46.62  E-value: 2.79e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15604817  391 IGLRVTAEIKNLTNYGAFVELEPGIEGLIHISDmswIKK--VSHPSELFKKGNTVEAVILSVDKESKKITLGVKQL 464
Cdd:PRK07252   3 IGDKLKGTITGIKPYGAFVALENGTTGLIHISE---IKTgfIDNIHQLLKVGEEVLVQVVDFDEYTGKASLSLRTL 75
PRK03987 PRK03987
translation initiation factor IF-2 subunit alpha; Validated
395-462 3.08e-06

translation initiation factor IF-2 subunit alpha; Validated


Pssm-ID: 235188 [Multi-domain]  Cd Length: 262  Bit Score: 49.05  E-value: 3.08e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15604817  395 VTAEIKNLTNYGAFVELE--PGIEGLIHISDMS--WIKKVshpSELFKKGNTVEAVILSVDKESKKITLGVK 462
Cdd:PRK03987  12 VVGTVKEVKDFGAFVTLDeyPGKEGFIHISEVAsgWVKNI---RDHVKEGQKVVCKVIRVDPRKGHIDLSLK 80
S1_pNO40 cd05686
S1_pNO40: pNO40 , S1-like RNA-binding domain. pNO40 is a nucleolar protein of unknown function ...
484-546 4.54e-06

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: 44.78  E-value: 4.54e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15604817 484 GVVTKITAFGAFVELQN-GIEGLIHVSELSEKPFAKIEDVLSIGDKVSAKVIKLDPDHK-KVSLS 546
Cdd:cd05686   9 GEVASVTEYGAFVKIPGcRKQGLVHKSHMSSCRVDDPSEVVDVGEKVWVKVIGREMKDKmKLSLS 73
S1_Rrp5_repeat_hs5 cd05697
S1_Rrp5_repeat_hs5: Rrp5 is a trans-acting factor important for biogenesis of both the 40S and ...
395-459 4.72e-06

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


Pssm-ID: 240202 [Multi-domain]  Cd Length: 69  Bit Score: 44.54  E-value: 4.72e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15604817 395 VTAEIKNLTNYGAFVELEPGIEGLI---HISDMswikKVSHPSELFKKGNTVEAVILSVDKESKKITL 459
Cdd:cd05697   4 VKGTIRKLRPSGIFVKLSDHIKGLVppmHLADV----RLKHPEKKFKPGLKVKCRVLSVEPERKRLVL 67
S1_PNPase cd04472
S1_PNPase: Polynucleotide phosphorylase (PNPase), ), S1-like RNA-binding domain. PNPase is a ...
402-455 7.34e-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: 43.69  E-value: 7.34e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 15604817 402 LTNYGAFVELEPGIEGLIHISDMSwIKKVSHPSELFKKGNTVEAVILSVDKESK 455
Cdd:cd04472  11 IKDFGAFVEILPGKDGLVHISELS-DERVEKVEDVLKVGDEVKVKVIEVDDRGR 63
S1_RPS1_repeat_ec6 cd05691
S1_RPS1_repeat_ec6: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
305-376 7.41e-06

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


Pssm-ID: 240196 [Multi-domain]  Cd Length: 73  Bit Score: 43.80  E-value: 7.41e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15604817 305 GKRVRGKIVKLLPYGAFIEIEEGIEGLIHVSEMSwVKNIVDPNEVVNKGDEVEVVVLSIQKDEGKISLGLKQ 376
Cdd:cd05691   1 GSIVTGKVTEVDAKGATVKLGDGVEGFLRAAELS-RDRVEDATERFKVGDEVEAKITNVDRKNRKISLSIKA 71
S1_Rrp5_repeat_hs5 cd05697
S1_Rrp5_repeat_hs5: Rrp5 is a trans-acting factor important for biogenesis of both the 40S and ...
479-545 1.04e-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: 43.38  E-value: 1.04e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15604817 479 GSDISGVVTKITAFGAFVELQNGIEGLIHVSELSEKPFAKIEDVLSIGDKVSAKVIKLDPDHKKVSL 545
Cdd:cd05697   1 GQVVKGTIRKLRPSGIFVKLSDHIKGLVPPMHLADVRLKHPEKKFKPGLKVKCRVLSVEPERKRLVL 67
S1_RNase_R cd04471
S1_RNase_R: RNase R C-terminal S1 domain. RNase R is a processive 3' to 5' exoribonuclease, ...
391-457 1.58e-05

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: 43.16  E-value: 1.58e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817 391 IGLRVTAEIKNLTNYGAFVEL-EPGIEGLIHISDM------------SWIKKVSHPSelFKKGNTVEAVILSVDKESKKI 457
Cdd:cd04471   1 VGEEFDGVISGVTSFGLFVELdNLTVEGLVHVSTLgddyyefdeenhALVGERTGKV--FRLGDKVKVRVVRVDLDRRKI 78
S1_Rrp5_repeat_hs6_sc5 cd05698
S1_Rrp5_repeat_hs6_sc5: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ...
310-375 1.85e-05

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


Pssm-ID: 240203 [Multi-domain]  Cd Length: 70  Bit Score: 42.60  E-value: 1.85e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15604817 310 GKIVKLLPYGAFIEIEEGIEGLIHVSEMSwVKNIVDPNEVVNKGDEVEVVVLSIQKDEGKISLGLK 375
Cdd:cd05698   6 GTIVKVKPNGCIVSFYNNVKGFLPKSELS-EAFIKDPEEHFRVGQVVKVKVLSCDPEQQRLLLSCK 70
S1_RPS1_repeat_ec6 cd05691
S1_RPS1_repeat_ec6: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
220-291 1.94e-05

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


Pssm-ID: 240196 [Multi-domain]  Cd Length: 73  Bit Score: 42.64  E-value: 1.94e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15604817 220 GERRKGIVKNITDFGVFLDL-DGIDGLLHITDMTWKRIRHPSEMVELNQELEVIILSVDKEKGRVALGLKQKE 291
Cdd:cd05691   1 GSIVTGKVTEVDAKGATVKLgDGVEGFLRAAELSRDRVEDATERFKVGDEVEAKITNVDRKNRKISLSIKAKE 73
S1_Rrp5_repeat_hs5 cd05697
S1_Rrp5_repeat_hs5: Rrp5 is a trans-acting factor important for biogenesis of both the 40S and ...
305-374 2.20e-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: 42.61  E-value: 2.20e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817 305 GKRVRGKIVKLLPYGAFIEIEEGIEGLIHVSEMSWVKnIVDPNEVVNKGDEVEVVVLSIQKDEGKISLGL 374
Cdd:cd05697   1 GQVVKGTIRKLRPSGIFVKLSDHIKGLVPPMHLADVR-LKHPEKKFKPGLKVKCRVLSVEPERKRLVLTL 69
PLN00207 PLN00207
polyribonucleotide nucleotidyltransferase; Provisional
312-375 3.14e-05

polyribonucleotide nucleotidyltransferase; Provisional


Pssm-ID: 215104 [Multi-domain]  Cd Length: 891  Bit Score: 46.81  E-value: 3.14e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15604817  312 IVKLLPYGAFIEIEEGIEGLIHVSEMS--WvknIVDPNEVVNKGDEVEVVVLSIQkDEGKISLGLK 375
Cdd:PLN00207 762 IKSIAPYGAFVEIAPGREGLCHISELSsnW---LAKPEDAFKVGDRIDVKLIEVN-DKGQLRLSRR 823
S1_RNase_R cd04471
S1_RNase_R: RNase R C-terminal S1 domain. RNase R is a processive 3' to 5' exoribonuclease, ...
219-287 3.71e-05

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: 42.39  E-value: 3.71e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817 219 IGERRKGIVKNITDFGVFLDLD--GIDGLLHITDM------------------TWKRIRhpsemveLNQELEVIILSVDK 278
Cdd:cd04471   1 VGEEFDGVISGVTSFGLFVELDnlTVEGLVHVSTLgddyyefdeenhalvgerTGKVFR-------LGDKVKVRVVRVDL 73

                ....*....
gi 15604817 279 EKGRVALGL 287
Cdd:cd04471  74 DRRKIDFEL 82
Csl4 COG1096
Exosome complex RNA-binding protein Csl4, contains S1 and Zn-ribbon domains [Intracellular ...
448-549 4.76e-05

Exosome complex RNA-binding protein Csl4, contains S1 and Zn-ribbon domains [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 440713 [Multi-domain]  Cd Length: 191  Bit Score: 44.51  E-value: 4.76e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817 448 LSVDKESKKITlgVKQLTPNPwdeieVMFPVGSDISGVVTKITAFGAFV----------ELQNGIEGLIHVSELSEKPFA 517
Cdd:COG1096  42 VVIDDKNRVIS--VKPKKKPP-----PVPKKGDIVIGEVVDVRESMALVkiyaiegnerELPSSFSGIIHISQVSDSYVK 114
                        90       100       110
                ....*....|....*....|....*....|..
gi 15604817 518 KIEDVLSIGDKVSAKVIKLDPdhkKVSLSIKE 549
Cdd:COG1096 115 DLSDEFRVGDIVRAKVISTLP---PIQLSIKE 143
S1_RNase_R cd04471
S1_RNase_R: RNase R C-terminal S1 domain. RNase R is a processive 3' to 5' exoribonuclease, ...
305-374 7.36e-05

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: 41.23  E-value: 7.36e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817 305 GKRVRGKIVKLLPYGAFIEIEE-GIEGLIHVSEMS--WVKNIVDPNEVVNK--------GDEVEVVVLSIQKDEGKISLG 373
Cdd:cd04471   2 GEEFDGVISGVTSFGLFVELDNlTVEGLVHVSTLGddYYEFDEENHALVGErtgkvfrlGDKVKVRVVRVDLDRRKIDFE 81

                .
gi 15604817 374 L 374
Cdd:cd04471  82 L 82
S1_Rrp5_repeat_hs6_sc5 cd05698
S1_Rrp5_repeat_hs6_sc5: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ...
392-462 7.69e-05

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


Pssm-ID: 240203 [Multi-domain]  Cd Length: 70  Bit Score: 41.06  E-value: 7.69e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15604817 392 GLRVTAEIKNLTNYGAFVELEPGIEGLIHISDMSwIKKVSHPSELFKKGNTVEAVILSVDKESKKITLGVK 462
Cdd:cd05698   1 GLKTHGTIVKVKPNGCIVSFYNNVKGFLPKSELS-EAFIKDPEEHFRVGQVVKVKVLSCDPEQQRLLLSCK 70
S1_Rrp5_repeat_hs11_sc8 cd05702
S1_Rrp5_repeat_hs11_sc8: Rrp5 is a trans-acting factor important for biogenesis of both the ...
479-534 9.03e-05

S1_Rrp5_repeat_hs11_sc8: Rrp5 is a trans-acting factor important for biogenesis of both the 40S and 60S eukaryotic ribosomal subunits. Rrp5 has two distinct regions, an N-terminal region containing tandemly repeated S1 RNA-binding domains (12 S1 repeats in Saccharomyces cerevisiae Rrp5 and 14 S1 repeats in Homo sapiens Rrp5) and a C-terminal region containing tetratricopeptide repeat (TPR) motifs thought to be involved in protein-protein interactions. Mutational studies have shown that each region represents a specific functional domain. Deletions within the S1-containing region inhibit pre-rRNA processing at either site A3 or A2, whereas deletions within the TPR region confer an inability to support cleavage of A0-A2. This CD includes H. sapiens S1 repeat 11 (hs11) and S. cerevisiae S1 repeat 8 (sc8). Rrp5 is found in eukaryotes but not in prokaryotes or archaea.


Pssm-ID: 240207 [Multi-domain]  Cd Length: 70  Bit Score: 40.65  E-value: 9.03e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15604817 479 GSDISGVVTKITAFGAFVELQNGIEGLIHVSEL------SEKPFAKiedvLSIGDKVSAKVI 534
Cdd:cd05702   1 GDLVKAKVKSVKPTQLNVQLADNVHGRIHVSEVfdewpdGKNPLSK----FKIGQKIKARVI 58
S1_Rrp5_repeat_hs12_sc9 cd05703
S1_Rrp5_repeat_hs12_sc9: Rrp5 is a trans-acting factor important for biogenesis of both the ...
392-459 1.36e-04

S1_Rrp5_repeat_hs12_sc9: 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 12 (hs12) and S. cerevisiae S1 repeat 9 (sc9). Rrp5 is found in eukaryotes but not in prokaryotes or archaea.


Pssm-ID: 240208 [Multi-domain]  Cd Length: 73  Bit Score: 40.25  E-value: 1.36e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15604817 392 GLRVTAEIKNLTNYGAFVELEPGIEGLIHISDMSW-IKKVSHPSELFKKGNTVEAVILSVDKESKKITL 459
Cdd:cd05703   1 GQEVTGFVNNVSKEFVWLTISPDVKGRIPLLDLSDdVSVLEHPEKKFPIGQALKAKVVGVDKEHKLLRL 69
PRK11824 PRK11824
polynucleotide phosphorylase/polyadenylase; Provisional
94-202 1.55e-04

polynucleotide phosphorylase/polyadenylase; Provisional


Pssm-ID: 236995 [Multi-domain]  Cd Length: 693  Bit Score: 44.66  E-value: 1.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817   94 GAEVEVyldqteDDEGKVVLS---REKATRQRQW-EYILAHCEEGSIVKGQITRkvkgglIVDIGmeAF---LPG----- 161
Cdd:PRK11824 584 GAKIDI------EDDGTVKIAatdGEAAEAAKERiEGITAEPEVGEIYEGKVVR------IVDFG--AFveiLPGkdglv 649
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 15604817  162 --SQIDNKKIKNLDDYV--GKVCEFKILKINvDRRNVVVSRRELL 202
Cdd:PRK11824 650 hiSEIADERVEKVEDVLkeGDEVKVKVLEID-KRGRIRLSRKAVL 693
S1_Rrp5_repeat_sc10 cd05706
S1_Rrp5_repeat_sc10: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ...
478-546 1.78e-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: 39.93  E-value: 1.78e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15604817 478 VGSDISGVVTKITAFGAFVELQNGIEGLIHVSELSEKPFAKIEDVLSIGDKVSAKVIKLDPDHKKVSLS 546
Cdd:cd05706   3 VGDILPGRVTKVNDRYVLVQLGNKVTGPSFITDALDDYSEALPYKFKKNDIVRACVLSVDVPNKKIALS 71
S1_pNO40 cd05686
S1_pNO40: pNO40 , S1-like RNA-binding domain. pNO40 is a nucleolar protein of unknown function ...
224-288 2.49e-04

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


Pssm-ID: 240191 [Multi-domain]  Cd Length: 73  Bit Score: 39.77  E-value: 2.49e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15604817 224 KGIVKNITDFGVFLDLDGI--DGLLHITDMTWKRIRHPSEMVELNQELEVIILSVDkEKGRVALGLK 288
Cdd:cd05686   8 KGEVASVTEYGAFVKIPGCrkQGLVHKSHMSSCRVDDPSEVVDVGEKVWVKVIGRE-MKDKMKLSLS 73
PRK03987 PRK03987
translation initiation factor IF-2 subunit alpha; Validated
225-288 2.93e-04

translation initiation factor IF-2 subunit alpha; Validated


Pssm-ID: 235188 [Multi-domain]  Cd Length: 262  Bit Score: 42.89  E-value: 2.93e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15604817  225 GIVKNITDFGVFLDLD---GIDGLLHITDMTWKRIRHPSEMVELNQELEVIILSVDKEKGRVALGLK 288
Cdd:PRK03987  14 GTVKEVKDFGAFVTLDeypGKEGFIHISEVASGWVKNIRDHVKEGQKVVCKVIRVDPRKGHIDLSLK 80
S1_Rrp4_like cd04454
S1_Rrp4_like: Rrp4-like, S1-like RNA-binding domain. S1-like RNA-binding domains are found in ...
478-549 3.22e-04

S1_Rrp4_like: Rrp4-like, S1-like RNA-binding domain. S1-like RNA-binding domains are found in a wide variety of RNA-associated proteins. Rrp4 protein, and Rrp40 and Csl4 proteins, also represented in this group, are subunits of the exosome complex. The exosome plays a central role in 3' to 5' RNA processing and degradation in eukarytes and archaea. Its functions include the removal of incorrectly processed RNA and the maintenance of proper levels of mRNA, rRNA and a number of small RNA species. In Saccharomyces cerevisiae, the exosome includes nine core components, six of which are homologous to bacterial RNase PH. These form a hexameric ring structure. The other three subunits (RrP4, Rrp40, and Csl4) contain an S1 RNA binding domain and are part of the "S1 pore structure".


Pssm-ID: 239901 [Multi-domain]  Cd Length: 82  Bit Score: 39.46  E-value: 3.22e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15604817 478 VGSDISGVVTKITAFGAFVELQNGIEGLIHVSELSEKPFAKIEDVLSIGDKVSAKVIKLDPDhKKVSLSIKE 549
Cdd:cd04454   6 VGDIVIGIVTEVNSRFWKVDILSRGTARLEDSSATEKDKKEIRKSLQPGDLILAKVISLGDD-MNVLLTTAD 76
S1_Rrp5_repeat_hs12_sc9 cd05703
S1_Rrp5_repeat_hs12_sc9: Rrp5 is a trans-acting factor important for biogenesis of both the ...
479-546 3.78e-04

S1_Rrp5_repeat_hs12_sc9: 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 12 (hs12) and S. cerevisiae S1 repeat 9 (sc9). Rrp5 is found in eukaryotes but not in prokaryotes or archaea.


Pssm-ID: 240208 [Multi-domain]  Cd Length: 73  Bit Score: 39.09  E-value: 3.78e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817 479 GSDISGVVTKITAFGAFVELQNGIEGLIHVSELSEKP--FAKIEDVLSIGDKVSAKVIKLDPDHKKVSLS 546
Cdd:cd05703   1 GQEVTGFVNNVSKEFVWLTISPDVKGRIPLLDLSDDVsvLEHPEKKFPIGQALKAKVVGVDKEHKLLRLS 70
S1_Rrp5_repeat_sc11 cd05707
S1_Rrp5_repeat_sc11: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ...
479-546 4.00e-04

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


Pssm-ID: 240212 [Multi-domain]  Cd Length: 68  Bit Score: 38.82  E-value: 4.00e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15604817 479 GSDISGVVTKITAFGAFVELQNGIEGLIHVSELSEKPFAKIEDVLSIGDKVSAKVIKLDPDHKKVSLS 546
Cdd:cd05707   1 GDVVRGFVKNIANNGVFVTLGRGVDARVRVSELSDSYLKDWKKRFKVGQLVKGKIVSIDPDNGRIEMT 68
PTZ00248 PTZ00248
eukaryotic translation initiation factor 2 subunit 1; Provisional
227-326 9.20e-04

eukaryotic translation initiation factor 2 subunit 1; Provisional


Pssm-ID: 240329 [Multi-domain]  Cd Length: 319  Bit Score: 41.57  E-value: 9.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817  227 VKNITDFGVFLDL---DGIDGLLHITDMTWKRIRHPSEMVELNQELEVIILSVDKEKGRVALGLKQKEHNPWEDIEKKYP 303
Cdd:PTZ00248  25 VVRITEMGAYVSLleyDDIEGMILMSELSKRRIRSINKLIRVGRHEVVVVLRVDKEKGYIDLSKKRVSPEDIEACEEKFS 104
                         90       100
                 ....*....|....*....|...
gi 15604817  304 PGKRVRGkIVKLLPYGAFIEIEE 326
Cdd:PTZ00248 105 KSKKVHS-IMRHIAQKHGMSVEE 126
S1_like cd00164
S1_like: Ribosomal protein S1-like RNA-binding domain. Found in a wide variety of ...
55-114 1.00e-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: 37.75  E-value: 1.00e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15604817  55 LKGTVVDISKDFVVVDVGLKSEGVIPMSEFIDS-----SEGLTVGAEVEVYLDQTEDDEGKVVLS 114
Cdd:cd00164   1 VTGKVVSITKFGVFVELEDGVEGLVHISELSDKfvkdpSEVFKVGDEVEVKVLEVDPEKGRISLS 65
RuvA_N pfam01330
RuvA N terminal domain; The N terminal domain of RuvA has an OB-fold structure. This domain ...
55-100 1.60e-03

RuvA N terminal domain; The N terminal domain of RuvA has an OB-fold structure. This domain forms the RuvA tetramer contacts.


Pssm-ID: 460162 [Multi-domain]  Cd Length: 61  Bit Score: 37.01  E-value: 1.60e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 15604817    55 LKGTVVDISKDFVVVDVGlkseGV-----IPMSEFidssEGLTVGAEVEVY 100
Cdd:pfam01330   5 LKGTVVEKGPDYVVIDVG----GVgyevfISLSTL----SKLAVGEEVKLY 47
S1_Rrp5_repeat_hs5 cd05697
S1_Rrp5_repeat_hs5: Rrp5 is a trans-acting factor important for biogenesis of both the 40S and ...
220-287 1.71e-03

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


Pssm-ID: 240202 [Multi-domain]  Cd Length: 69  Bit Score: 37.22  E-value: 1.71e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15604817 220 GERRKGIVKNITDFGVFLDL-DGIDGLLHITDMTWKRIRHPSEMVELNQELEVIILSVDKEKGRVALGL 287
Cdd:cd05697   1 GQVVKGTIRKLRPSGIFVKLsDHIKGLVPPMHLADVRLKHPEKKFKPGLKVKCRVLSVEPERKRLVLTL 69
VacB COG0557
Exoribonuclease R [Transcription];
305-374 1.77e-03

Exoribonuclease R [Transcription];


Pssm-ID: 440323 [Multi-domain]  Cd Length: 711  Bit Score: 41.25  E-value: 1.77e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817 305 GKRVRGKIVKLLPYGAFIEIEE-GIEGLIHVSEMswvKN---IVDP--NEVVNK--------GDEVEVVVLSIQKDEGKI 370
Cdd:COG0557 623 GEEFEGVISGVTSFGLFVELDElGVEGLVHVSSL---GDdyyEYDErrQALVGErtgkryrlGDRVEVRVVRVDLDRRQI 699

                ....
gi 15604817 371 SLGL 374
Cdd:COG0557 700 DFEL 703
PTZ00248 PTZ00248
eukaryotic translation initiation factor 2 subunit 1; Provisional
486-548 2.01e-03

eukaryotic translation initiation factor 2 subunit 1; Provisional


Pssm-ID: 240329 [Multi-domain]  Cd Length: 319  Bit Score: 40.42  E-value: 2.01e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15604817  486 VTKITAFGAFVEL--QNGIEGLIHVSELSEKPFAKIEDVLSIGDKVSAKVIKLDPDHKKVSLSIK 548
Cdd:PTZ00248  25 VVRITEMGAYVSLleYDDIEGMILMSELSKRRIRSINKLIRVGRHEVVVVLRVDKEKGYIDLSKK 89
S1_Rrp5_repeat_hs1_sc1 cd05693
S1_Rrp5_repeat_hs1_sc1: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ...
478-553 2.09e-03

S1_Rrp5_repeat_hs1_sc1: 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 1 (hs1) and S. cerevisiae S1 repeat 1 (sc1). Rrp5 is found in eukaryotes but not in prokaryotes or archaea.


Pssm-ID: 240198 [Multi-domain]  Cd Length: 100  Bit Score: 37.97  E-value: 2.09e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817 478 VGSDISGVVTKITAFGAFVELQNGIEGLIHVSELSEKPFAKIE-------------------DVLSIGDKVSAKVIKLDP 538
Cdd:cd05693   3 EGMLVLGQVKEITKLDLVISLPNGLTGYVPITNISDAYTERLEeldeeseeeddeeelpdleDLFSVGQLVRCKVVSLDK 82
                        90
                ....*....|....*...
gi 15604817 539 D---HKKVSLSIKEFLVH 553
Cdd:cd05693  83 SksgKKRIELSLEPELVN 100
S1_RecJ_like cd04473
S1_RecJ_like: The S1 domain of the archaea-specific RecJ-like exonuclease. The function of ...
296-373 2.20e-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: 2.20e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15604817 296 EDIEkkypPGKRVRGKIVKLLPYGAFIEIEEGIEGLIHVSEMswvknIVDPNEvvnkGDEVEVVVLSIqKDEGKISLG 373
Cdd:cd04473  12 EDLE----VGKLYKGKVNGVAKYGVFVDLNDHVRGLIHRSNL-----LRDYEV----GDEVIVQVTDI-PENGNIDLI 75
S1_Rrp5_repeat_sc10 cd05706
S1_Rrp5_repeat_sc10: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ...
391-459 3.17e-03

S1_Rrp5_repeat_sc10: Rrp5 is a trans-acting factor important for biogenesis of both the 40S and 60S eukaryotic ribosomal subunits. Rrp5 has two distinct regions, an N-terminal region containing tandemly repeated S1 RNA-binding domains (12 S1 repeats in Saccharomyces cerevisiae Rrp5 and 14 S1 repeats in Homo sapiens Rrp5) and a C-terminal region containing tetratricopeptide repeat (TPR) motifs thought to be involved in protein-protein interactions. Mutational studies have shown that each region represents a specific functional domain. Deletions within the S1-containing region inhibit pre-rRNA processing at either site A3 or A2, whereas deletions within the TPR region confer an inability to support cleavage of A0-A2. This CD includes S. cerevisiae S1 repeat 10 (sc10). Rrp5 is found in eukaryotes but not in prokaryotes or archaea.


Pssm-ID: 240211 [Multi-domain]  Cd Length: 73  Bit Score: 36.46  E-value: 3.17e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817 391 IGLRVTAEIKNLTNYGAFVELEPGIEGLIHISDMswIKKVSHPSEL-FKKGNTVEAVILSVDKESKKITL 459
Cdd:cd05706   3 VGDILPGRVTKVNDRYVLVQLGNKVTGPSFITDA--LDDYSEALPYkFKKNDIVRACVLSVDVPNKKIAL 70
S1_pNO40 cd05686
S1_pNO40: pNO40 , S1-like RNA-binding domain. pNO40 is a nucleolar protein of unknown function ...
398-455 3.49e-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: 3.49e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15604817 398 EIKNLTNYGAFVELePGI--EGLIHISDMSwIKKVSHPSELFKKGNTVEAVILSVDKESK 455
Cdd:cd05686  10 EVASVTEYGAFVKI-PGCrkQGLVHKSHMS-SCRVDDPSEVVDVGEKVWVKVIGREMKDK 67
S1_Tex cd05685
S1_Tex: The C-terminal S1 domain of a transcription accessory factor called Tex, which has ...
52-114 4.01e-03

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


Pssm-ID: 240190 [Multi-domain]  Cd Length: 68  Bit Score: 36.06  E-value: 4.01e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15604817  52 GAILKGTVVDISKDFVVVDVGLKSEGVIPMSEFIDS-----SEGLTVGAEVEVYLDQTEDDEGKVVLS 114
Cdd:cd05685   1 GMVLEGVVTNVTDFGAFVDIGVKQDGLIHISKMADRfvshpSDVVSVGDIVEVKVISIDEERGRISLS 68
S1_RpoE cd04460
S1_RpoE: RpoE, S1-like RNA-binding domain. S1-like RNA-binding domains are found in a wide ...
482-549 4.24e-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: 36.88  E-value: 4.24e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15604817 482 ISGVVTKITAFGAFVELqNGIEGLIHVSELSEKPFAKIED-----------VLSIGDKVSAKVikldpdhkkVSLSIKE 549
Cdd:cd04460   3 VEGEVVEVVDFGAFVRI-GPVDGLLHISQIMDDYISYDPKnkrligeetkrVLKVGDVVRARI---------VAVSLKE 71
S1_Rrp5_repeat_hs14 cd05705
S1_Rrp5_repeat_hs14: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ...
479-546 4.39e-03

S1_Rrp5_repeat_hs14: Rrp5 is a trans-acting factor important for biogenesis of both the 40S and 60S eukaryotic ribosomal subunits. Rrp5 has two distinct regions, an N-terminal region containing tandemly repeated S1 RNA-binding domains (12 S1 repeats in Saccharomyces cerevisiae Rrp5 and 14 S1 repeats in Homo sapiens Rrp5) and a C-terminal region containing tetratricopeptide repeat (TPR) motifs thought to be involved in protein-protein interactions. Mutational studies have shown that each region represents a specific functional domain. Deletions within the S1-containing region inhibit pre-rRNA processing at either site A3 or A2, whereas deletions within the TPR region confer an inability to support cleavage of A0-A2. This CD includes H. sapiens S1 repeat 14 (hs14). Rrp5 is found in eukaryotes but not in prokaryotes or archaea.


Pssm-ID: 240210 [Multi-domain]  Cd Length: 74  Bit Score: 36.22  E-value: 4.39e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15604817 479 GSDISGVVTKITAFGAFVELQNGIEGLI---HVSELSEKPFAKIEDVLSIGDKVSAKVIKLDPDHKKVSLS 546
Cdd:cd05705   4 GQLLRGYVSSVTKQGVFFRLSSSIVGRVlfqNVTKYFVSDPSLYNKYLPEGKLLTAKVLSVNSEKNLVELS 74
VacB COG0557
Exoribonuclease R [Transcription];
403-424 4.76e-03

Exoribonuclease R [Transcription];


Pssm-ID: 440323 [Multi-domain]  Cd Length: 711  Bit Score: 39.70  E-value: 4.76e-03
                        10        20
                ....*....|....*....|...
gi 15604817 403 TNYGAFVEL-EPGIEGLIHISDM 424
Cdd:COG0557 634 TSFGLFVELdELGVEGLVHVSSL 656
S1_like cd00164
S1_like: Ribosomal protein S1-like RNA-binding domain. Found in a wide variety of ...
137-197 6.58e-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: 35.43  E-value: 6.58e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15604817 137 VKGQITRKVKGGLIVDI--GMEAFLPGSQIDNKKIKNLDD--YVGKVCEFKILKINVDRRNVVVS 197
Cdd:cd00164   1 VTGKVVSITKFGVFVELedGVEGLVHISELSDKFVKDPSEvfKVGDEVEVKVLEVDPEKGRISLS 65
PRK08582 PRK08582
RNA-binding protein S1;
52-123 8.18e-03

RNA-binding protein S1;


Pssm-ID: 236305 [Multi-domain]  Cd Length: 139  Bit Score: 36.93  E-value: 8.18e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15604817   52 GAILKGTVVDISKDFVVVDVGLKSEGVIPMSEFIDS-----SEGLTVGAEVEVYLDQTEDDeGKVVLSREKATRQRQ 123
Cdd:PRK08582   6 GSKLQGKVTGITNFGAFVELPEGKTGLVHISEVADNyvkdiNDHLKVGDEVEVKVLNVEDD-GKIGLSIKKAKDRPK 81
PRK07252 PRK07252
S1 RNA-binding domain-containing protein;
219-291 9.78e-03

S1 RNA-binding domain-containing protein;


Pssm-ID: 180908 [Multi-domain]  Cd Length: 120  Bit Score: 36.22  E-value: 9.78e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15604817  219 IGERRKGIVKNITDFGVFLDLD-GIDGLLHITDMTWKRIRHPSEMVELNQELEVIILSVDKEKGRVALGLKQKE 291
Cdd:PRK07252   3 IGDKLKGTITGIKPYGAFVALEnGTTGLIHISEIKTGFIDNIHQLLKVGEEVLVQVVDFDEYTGKASLSLRTLE 76
 
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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