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Conserved domains on  [gi|1276677562|gb|ATV39116|]
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30S ribosomal protein S1 [Prevotella intermedia]

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

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
rpsA PRK06299
30S ribosomal protein S1; Reviewed
27-589 0e+00

30S ribosomal protein S1; Reviewed


:

Pssm-ID: 235775 [Multi-domain]  Cd Length: 565  Bit Score: 755.85  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562  27 DKEELTKAYDNTL--NKIQEHQVVEGEVISIDKKEVVVNIGYKSDGIIPASEFRY---NPELKVGDKVEVYVENQEDKSG 101
Cdd:PRK06299   11 MEESFAELFEESLkeSETREGSIVKGTVVAIDKDYVLVDVGLKSEGRIPLEEFKNeqgELEVKVGDEVEVYVERIEDGFG 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 102 QLILSHKKARLQKSWVNINEALEADAVIQGYIKSRTKGGMIVDVFGIEAFLPGSQIDVHPIRDYDVFVGKTMEFKVVKIN 181
Cdd:PRK06299   91 ETVLSREKAKRLEAWDKLEKAFENGEIVEGVINGKVKGGFTVDLNGVEAFLPGSQVDVRPVRDTDPLEGKELEFKVIKLD 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 182 QEFRNVVVSHKALIEAELEAQRKEIISHLEKGQILEGVVKNITSYGVFVDLGGVDGLIHITDLSWGRINDPHEVVELDQK 261
Cdd:PRK06299  171 KKRNNIVVSRRAVLEEERAEEREELLENLEEGQVVEGVVKNITDYGAFVDLGGVDGLLHITDISWKRVNHPSEVVNVGDE 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 262 INVVILDFDEEKKRIALGLKQLAPHPWDALDPNLKVGDHVKGKVVVMADYGAFVEIQPGVEGLIHVSEMSWSQHLRSAQE 341
Cdd:PRK06299  251 VKVKVLKFDKEKKRVSLGLKQLGEDPWEAIEKKYPVGSKVKGKVTNITDYGAFVELEEGIEGLVHVSEMSWTKKNKHPSK 330
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 342 FMKAGDEVEAVVLTLDRDERKMSLGIKQLKEDPWEAIEAKYPVGSKHVAKVRNFTNFGIFVELEEGVDGLIHISDLSWTK 421
Cdd:PRK06299  331 VVSVGQEVEVMVLEIDEEKRRISLGLKQCKENPWEEFAEKYPVGDVVEGKVKNITDFGAFVGLEGGIDGLVHLSDISWDK 410
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 422 KVKHPSEFTQVGADMDVIVLEIDKENRRLSLGHKQLETNPWDTYESIYTPGSTHVGKITESMDKGAVITLNEGGEGFATP 501
Cdd:PRK06299  411 KGEEAVELYKKGDEVEAVVLKVDVEKERISLGIKQLEEDPFEEFAKKHKKGSIVTGTVTEVKDKGAFVELEDGVEGLIRA 490
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 502 KHL----VKEDGSQAQLGEELPFVVIEFVKDTKRIILSHSRTFEEvkeeqarrqrtaskKHSEPASQINNVA-AGTSLGD 576
Cdd:PRK06299  491 SELsrdrVEDATEVLKVGDEVEAKVINIDRKNRRISLSIKALDEA--------------EEKEAIAEYNSASdSKTTLGD 556
                         570
                  ....*....|...
gi 1276677562 577 LdvladLKKKMEE 589
Cdd:PRK06299  557 L-----LKAALKG 564
 
Name Accession Description Interval E-value
rpsA PRK06299
30S ribosomal protein S1; Reviewed
27-589 0e+00

30S ribosomal protein S1; Reviewed


Pssm-ID: 235775 [Multi-domain]  Cd Length: 565  Bit Score: 755.85  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562  27 DKEELTKAYDNTL--NKIQEHQVVEGEVISIDKKEVVVNIGYKSDGIIPASEFRY---NPELKVGDKVEVYVENQEDKSG 101
Cdd:PRK06299   11 MEESFAELFEESLkeSETREGSIVKGTVVAIDKDYVLVDVGLKSEGRIPLEEFKNeqgELEVKVGDEVEVYVERIEDGFG 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 102 QLILSHKKARLQKSWVNINEALEADAVIQGYIKSRTKGGMIVDVFGIEAFLPGSQIDVHPIRDYDVFVGKTMEFKVVKIN 181
Cdd:PRK06299   91 ETVLSREKAKRLEAWDKLEKAFENGEIVEGVINGKVKGGFTVDLNGVEAFLPGSQVDVRPVRDTDPLEGKELEFKVIKLD 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 182 QEFRNVVVSHKALIEAELEAQRKEIISHLEKGQILEGVVKNITSYGVFVDLGGVDGLIHITDLSWGRINDPHEVVELDQK 261
Cdd:PRK06299  171 KKRNNIVVSRRAVLEEERAEEREELLENLEEGQVVEGVVKNITDYGAFVDLGGVDGLLHITDISWKRVNHPSEVVNVGDE 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 262 INVVILDFDEEKKRIALGLKQLAPHPWDALDPNLKVGDHVKGKVVVMADYGAFVEIQPGVEGLIHVSEMSWSQHLRSAQE 341
Cdd:PRK06299  251 VKVKVLKFDKEKKRVSLGLKQLGEDPWEAIEKKYPVGSKVKGKVTNITDYGAFVELEEGIEGLVHVSEMSWTKKNKHPSK 330
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 342 FMKAGDEVEAVVLTLDRDERKMSLGIKQLKEDPWEAIEAKYPVGSKHVAKVRNFTNFGIFVELEEGVDGLIHISDLSWTK 421
Cdd:PRK06299  331 VVSVGQEVEVMVLEIDEEKRRISLGLKQCKENPWEEFAEKYPVGDVVEGKVKNITDFGAFVGLEGGIDGLVHLSDISWDK 410
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 422 KVKHPSEFTQVGADMDVIVLEIDKENRRLSLGHKQLETNPWDTYESIYTPGSTHVGKITESMDKGAVITLNEGGEGFATP 501
Cdd:PRK06299  411 KGEEAVELYKKGDEVEAVVLKVDVEKERISLGIKQLEEDPFEEFAKKHKKGSIVTGTVTEVKDKGAFVELEDGVEGLIRA 490
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 502 KHL----VKEDGSQAQLGEELPFVVIEFVKDTKRIILSHSRTFEEvkeeqarrqrtaskKHSEPASQINNVA-AGTSLGD 576
Cdd:PRK06299  491 SELsrdrVEDATEVLKVGDEVEAKVINIDRKNRRISLSIKALDEA--------------EEKEAIAEYNSASdSKTTLGD 556
                         570
                  ....*....|...
gi 1276677562 577 LdvladLKKKMEE 589
Cdd:PRK06299  557 L-----LKAALKG 564
RpsA COG0539
Ribosomal protein S1 [Translation, ribosomal structure and biogenesis]; Ribosomal protein S1 ...
27-371 0e+00

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


Pssm-ID: 440305 [Multi-domain]  Cd Length: 348  Bit Score: 540.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562  27 DKEELTKAYDNTLNKIQEHQVVEGEVISIDKKEVVVNIGYKSDGIIPASEFRY---NPELKVGDKVEVYVENQEDKSGQL 103
Cdd:COG0539     1 MSESFAELLEESLKELKEGDIVKGTVVSIDDDEVLVDIGYKSEGIIPLSEFSDepgELEVKVGDEVEVYVEKVEDGEGEI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 104 ILSHKKARLQKSWVNINEALEADAVIQGYIKSRTKGGMIVDVFGIEAFLPGSQIDVHPIRDYDVFVGKTMEFKVVKINQE 183
Cdd:COG0539    81 VLSKKKADREKAWEELEEAFENGEPVEGKVKGVVKGGLIVDIGGVRAFLPASQVDVRPVRDLDEYVGKTLEFKIIKLDRK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 184 FRNVVVSHKALIEAELEAQRKEIISHLEKGQILEGVVKNITSYGVFVDLGGVDGLIHITDLSWGRINDPHEVVELDQKIN 263
Cdd:COG0539   161 RNNVVVSRRAVLEEEREEKREELLEKLEEGDVVEGTVKNITDFGAFVDLGGVDGLLHISEISWGRVKHPSEVLKVGDEVE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 264 VVILDFDEEKKRIALGLKQLAPHPWDALDPNLKVGDHVKGKVVVMADYGAFVEIQPGVEGLIHVSEMSWSQHLRSAQEFM 343
Cdd:COG0539   241 VKVLKIDREKERISLSLKQLQPDPWENIAEKYPVGDVVKGKVTRLTDFGAFVELEPGVEGLVHISEMSWTKRVAHPSDVV 320
                         330       340
                  ....*....|....*....|....*...
gi 1276677562 344 KAGDEVEAVVLTLDRDERKMSLGIKQLK 371
Cdd:COG0539   321 KVGDEVEVKVLDIDPEERRISLSIKQLA 348
rpsA TIGR00717
ribosomal protein S1; This model describes ribosomal protein S1, RpsA. This protein is found ...
29-535 4.93e-173

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: 500.80  E-value: 4.93e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562  29 EELTKAYDNTLNKIQEH--QVVEGEVISIDKKEVVVNIGYKSDGIIPASEFRYNP-ELKVGDKVEVYVENQEDKSGQLIL 105
Cdd:TIGR00717   1 ESFAQLLEESLKTEETRpgSIVKGTVVAINKDTVFVDVGLKSEGRIPKEEFLDAPlEIQVGDEVEVYLDRVEDRFGETVL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 106 SHKKARLQKSWVNINEALEADAVIQGYIKSRTKGGMIVDVFGIEAFLPGSQIDVHPIRDYDVFVGKTMEFKVVKINQEFR 185
Cdd:TIGR00717  81 SREKAQRHELWIKLEKAYEEGSIVEGKIVGKVKGGFIVDLNGVEAFLPGSQVDVKPIKDLDSLIGKTLKFKIIKLDQKRN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 186 NVVVSHKALIEAELEAQRKEIISHLEKGQILEGVVKNITSYGVFVDLGGVDGLIHITDLSWGRINDPHEVVELDQKINVV 265
Cdd:TIGR00717 161 NIVVSRRAYLEEERSQAREELLENLKEGDVVKGVVKNITDFGAFVDLGGVDGLLHITDMSWKRVKHPSEYVKVGQEVKVK 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 266 ILDFDEEKKRIALGLKQLAPHPWDALDPNLKVGDHVKGKVVVMADYGAFVEIQPGVEGLIHVSEMSWSQHLRSAQEFMKA 345
Cdd:TIGR00717 241 VIKFDKEKGRISLSLKQLGEDPWEAIEKKFPVGDKITGRVTNLTDYGVFVEIEEGIEGLVHVSEMSWVKKNSHPSKVVKK 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 346 GDEVEAVVLTLDRDERKMSLGIKQLKEDPWEAIEAKYPVGSKHVAKVRNFTNFGIFVELEEGVDGLIHISDLSWTKKVKH 425
Cdd:TIGR00717 321 GDEVEVMILDIDPERRRLSLGLKQCKANPWEQFEEKHPVGDRVTGKIKKITDFGAFVELEGGIDGLIHLSDISWDKDGRE 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 426 PSEFTQVGADMDVIVLEIDKENRRLSLGHKQLETNPWDTYESIYTPGSTHVGKITESMDKGAVITLNEGGEGFATPKHLV 505
Cdd:TIGR00717 401 ADHLYKKGDEIEAVVLAVDKEKKRISLGVKQLTENPWEKFAAKYKVGSVVKGKVTEIKDFGAFVELPGGVEGLIRNSELS 480
                         490       500       510
                  ....*....|....*....|....*....|....
gi 1276677562 506 KEDGSQAQL----GEELPFVVIEFVKDTKRIILS 535
Cdd:TIGR00717 481 ENRDEDKTDeikvGDEVEAKVVDIDKKNRKVSLS 514
S1_RPS1_repeat_ec3 cd05688
S1_RPS1_repeat_ec3: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
212-279 3.48e-30

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: 112.72  E-value: 3.48e-30
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1276677562 212 KGQILEGVVKNITSYGVFVDLGGVDGLIHITDLSWGRINDPHEVVELDQKINVVILDFDEEKKRIALG 279
Cdd:cd05688     1 EGDVVEGTVKSITDFGAFVDLGGVDGLLHISDMSWGRVKHPSEVVNVGDEVEVKVLKIDKERKRISLG 68
S1 smart00316
Ribosomal protein S1-like RNA-binding domain;
211-281 4.41e-18

Ribosomal protein S1-like RNA-binding domain;


Pssm-ID: 197648 [Multi-domain]  Cd Length: 72  Bit Score: 78.80  E-value: 4.41e-18
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1276677562  211 EKGQILEGVVKNITSYGVFVDLG-GVDGLIHITDLSWGRINDPHEVVELDQKINVVILDFDEEKKRIALGLK 281
Cdd:smart00316   1 EVGDVVEGTVTEITPGGAFVDLGnGVEGLIPISELSDKRVKDPEEVLKVGDEVKVKVLSVDEEKGRIILSLK 72
S1 pfam00575
S1 RNA binding domain; The S1 domain occurs in a wide range of RNA associated proteins. It is ...
210-280 5.71e-14

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


Pssm-ID: 425760 [Multi-domain]  Cd Length: 72  Bit Score: 66.93  E-value: 5.71e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1276677562 210 LEKGQILEGVVKNITSYGVFVDLG-GVDGLIHITDLSWGRINDPHEVVELDQKINVVILDFDEEKKRIALGL 280
Cdd:pfam00575   1 PEKGDVVEGEVTRVTKGGAFVDLGnGVEGFIPISELSDDHVEDPDEVIKVGDEVKVKVLKVDKDRRRIILSI 72
S1_dom_CvfD NF040579
CvfD/Ygs/GSP13 family RNA-binding post-transcriptional regulator; CvfD, Ygs, and GSP13 form a ...
296-374 2.83e-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: 66.30  E-value: 2.83e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1276677562 296 KVGDHVKGKVVVMADYGAFVEIQPGVEGLIHVSEMSwSQHLRSAQEFMKAGDEVEAVVLTLDRDERKMSLGIKQLKEDP 374
Cdd:NF040579    2 KIGDIVEGKVTGIQPYGAFVALDEHTQGLIHISEIK-HGYVKDINDFLKVGQEVKVKVLDIDEYTGKISLSLRALEEAP 79
 
Name Accession Description Interval E-value
rpsA PRK06299
30S ribosomal protein S1; Reviewed
27-589 0e+00

30S ribosomal protein S1; Reviewed


Pssm-ID: 235775 [Multi-domain]  Cd Length: 565  Bit Score: 755.85  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562  27 DKEELTKAYDNTL--NKIQEHQVVEGEVISIDKKEVVVNIGYKSDGIIPASEFRY---NPELKVGDKVEVYVENQEDKSG 101
Cdd:PRK06299   11 MEESFAELFEESLkeSETREGSIVKGTVVAIDKDYVLVDVGLKSEGRIPLEEFKNeqgELEVKVGDEVEVYVERIEDGFG 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 102 QLILSHKKARLQKSWVNINEALEADAVIQGYIKSRTKGGMIVDVFGIEAFLPGSQIDVHPIRDYDVFVGKTMEFKVVKIN 181
Cdd:PRK06299   91 ETVLSREKAKRLEAWDKLEKAFENGEIVEGVINGKVKGGFTVDLNGVEAFLPGSQVDVRPVRDTDPLEGKELEFKVIKLD 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 182 QEFRNVVVSHKALIEAELEAQRKEIISHLEKGQILEGVVKNITSYGVFVDLGGVDGLIHITDLSWGRINDPHEVVELDQK 261
Cdd:PRK06299  171 KKRNNIVVSRRAVLEEERAEEREELLENLEEGQVVEGVVKNITDYGAFVDLGGVDGLLHITDISWKRVNHPSEVVNVGDE 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 262 INVVILDFDEEKKRIALGLKQLAPHPWDALDPNLKVGDHVKGKVVVMADYGAFVEIQPGVEGLIHVSEMSWSQHLRSAQE 341
Cdd:PRK06299  251 VKVKVLKFDKEKKRVSLGLKQLGEDPWEAIEKKYPVGSKVKGKVTNITDYGAFVELEEGIEGLVHVSEMSWTKKNKHPSK 330
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 342 FMKAGDEVEAVVLTLDRDERKMSLGIKQLKEDPWEAIEAKYPVGSKHVAKVRNFTNFGIFVELEEGVDGLIHISDLSWTK 421
Cdd:PRK06299  331 VVSVGQEVEVMVLEIDEEKRRISLGLKQCKENPWEEFAEKYPVGDVVEGKVKNITDFGAFVGLEGGIDGLVHLSDISWDK 410
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 422 KVKHPSEFTQVGADMDVIVLEIDKENRRLSLGHKQLETNPWDTYESIYTPGSTHVGKITESMDKGAVITLNEGGEGFATP 501
Cdd:PRK06299  411 KGEEAVELYKKGDEVEAVVLKVDVEKERISLGIKQLEEDPFEEFAKKHKKGSIVTGTVTEVKDKGAFVELEDGVEGLIRA 490
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 502 KHL----VKEDGSQAQLGEELPFVVIEFVKDTKRIILSHSRTFEEvkeeqarrqrtaskKHSEPASQINNVA-AGTSLGD 576
Cdd:PRK06299  491 SELsrdrVEDATEVLKVGDEVEAKVINIDRKNRRISLSIKALDEA--------------EEKEAIAEYNSASdSKTTLGD 556
                         570
                  ....*....|...
gi 1276677562 577 LdvladLKKKMEE 589
Cdd:PRK06299  557 L-----LKAALKG 564
RpsA COG0539
Ribosomal protein S1 [Translation, ribosomal structure and biogenesis]; Ribosomal protein S1 ...
27-371 0e+00

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


Pssm-ID: 440305 [Multi-domain]  Cd Length: 348  Bit Score: 540.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562  27 DKEELTKAYDNTLNKIQEHQVVEGEVISIDKKEVVVNIGYKSDGIIPASEFRY---NPELKVGDKVEVYVENQEDKSGQL 103
Cdd:COG0539     1 MSESFAELLEESLKELKEGDIVKGTVVSIDDDEVLVDIGYKSEGIIPLSEFSDepgELEVKVGDEVEVYVEKVEDGEGEI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 104 ILSHKKARLQKSWVNINEALEADAVIQGYIKSRTKGGMIVDVFGIEAFLPGSQIDVHPIRDYDVFVGKTMEFKVVKINQE 183
Cdd:COG0539    81 VLSKKKADREKAWEELEEAFENGEPVEGKVKGVVKGGLIVDIGGVRAFLPASQVDVRPVRDLDEYVGKTLEFKIIKLDRK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 184 FRNVVVSHKALIEAELEAQRKEIISHLEKGQILEGVVKNITSYGVFVDLGGVDGLIHITDLSWGRINDPHEVVELDQKIN 263
Cdd:COG0539   161 RNNVVVSRRAVLEEEREEKREELLEKLEEGDVVEGTVKNITDFGAFVDLGGVDGLLHISEISWGRVKHPSEVLKVGDEVE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 264 VVILDFDEEKKRIALGLKQLAPHPWDALDPNLKVGDHVKGKVVVMADYGAFVEIQPGVEGLIHVSEMSWSQHLRSAQEFM 343
Cdd:COG0539   241 VKVLKIDREKERISLSLKQLQPDPWENIAEKYPVGDVVKGKVTRLTDFGAFVELEPGVEGLVHISEMSWTKRVAHPSDVV 320
                         330       340
                  ....*....|....*....|....*...
gi 1276677562 344 KAGDEVEAVVLTLDRDERKMSLGIKQLK 371
Cdd:COG0539   321 KVGDEVEVKVLDIDPEERRISLSIKQLA 348
rpsA TIGR00717
ribosomal protein S1; This model describes ribosomal protein S1, RpsA. This protein is found ...
29-535 4.93e-173

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: 500.80  E-value: 4.93e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562  29 EELTKAYDNTLNKIQEH--QVVEGEVISIDKKEVVVNIGYKSDGIIPASEFRYNP-ELKVGDKVEVYVENQEDKSGQLIL 105
Cdd:TIGR00717   1 ESFAQLLEESLKTEETRpgSIVKGTVVAINKDTVFVDVGLKSEGRIPKEEFLDAPlEIQVGDEVEVYLDRVEDRFGETVL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 106 SHKKARLQKSWVNINEALEADAVIQGYIKSRTKGGMIVDVFGIEAFLPGSQIDVHPIRDYDVFVGKTMEFKVVKINQEFR 185
Cdd:TIGR00717  81 SREKAQRHELWIKLEKAYEEGSIVEGKIVGKVKGGFIVDLNGVEAFLPGSQVDVKPIKDLDSLIGKTLKFKIIKLDQKRN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 186 NVVVSHKALIEAELEAQRKEIISHLEKGQILEGVVKNITSYGVFVDLGGVDGLIHITDLSWGRINDPHEVVELDQKINVV 265
Cdd:TIGR00717 161 NIVVSRRAYLEEERSQAREELLENLKEGDVVKGVVKNITDFGAFVDLGGVDGLLHITDMSWKRVKHPSEYVKVGQEVKVK 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 266 ILDFDEEKKRIALGLKQLAPHPWDALDPNLKVGDHVKGKVVVMADYGAFVEIQPGVEGLIHVSEMSWSQHLRSAQEFMKA 345
Cdd:TIGR00717 241 VIKFDKEKGRISLSLKQLGEDPWEAIEKKFPVGDKITGRVTNLTDYGVFVEIEEGIEGLVHVSEMSWVKKNSHPSKVVKK 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 346 GDEVEAVVLTLDRDERKMSLGIKQLKEDPWEAIEAKYPVGSKHVAKVRNFTNFGIFVELEEGVDGLIHISDLSWTKKVKH 425
Cdd:TIGR00717 321 GDEVEVMILDIDPERRRLSLGLKQCKANPWEQFEEKHPVGDRVTGKIKKITDFGAFVELEGGIDGLIHLSDISWDKDGRE 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 426 PSEFTQVGADMDVIVLEIDKENRRLSLGHKQLETNPWDTYESIYTPGSTHVGKITESMDKGAVITLNEGGEGFATPKHLV 505
Cdd:TIGR00717 401 ADHLYKKGDEIEAVVLAVDKEKKRISLGVKQLTENPWEKFAAKYKVGSVVKGKVTEIKDFGAFVELPGGVEGLIRNSELS 480
                         490       500       510
                  ....*....|....*....|....*....|....
gi 1276677562 506 KEDGSQAQL----GEELPFVVIEFVKDTKRIILS 535
Cdd:TIGR00717 481 ENRDEDKTDeikvGDEVEAKVVDIDKKNRKVSLS 514
rpsA PRK06676
30S ribosomal protein S1; Reviewed
30-383 1.52e-117

30S ribosomal protein S1; Reviewed


Pssm-ID: 235851 [Multi-domain]  Cd Length: 390  Bit Score: 354.18  E-value: 1.52e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562  30 ELTKAYDNTLNKIQEHQVVEGEVISIDKKEVVVNI-GYKSDGIIPASEF------RYNPELKVGDKVEVYVENQEDKSGQ 102
Cdd:PRK06676    3 EEFEESLNSVKEVEVGDVVTGEVLKVEDKQVFVNIeGYKVEGVIPISELsndhieDINDVVKVGDELEVYVLKVEDGEGN 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 103 LILSHKKARLQKSWVNINEALEADAVIQGYIKSRTKGGMIVDVFGIEAFLPGSQIDVHPIRDYDVFVGKTMEFKVVKINQ 182
Cdd:PRK06676   83 LLLSKRRLEAEKAWDKLEEKFEEGEVVEVKVTEVVKGGLVVDVEGVRGFIPASLISTRFVEDFSDFKGKTLEVKIIELDP 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 183 EFRNVVVSHKALIEAELEAQRKEIISHLEKGQILEGVVKNITSYGVFVDLGGVDGLIHITDLSWGRINDPHEVVELDQKI 262
Cdd:PRK06676  163 EKNRVILSRRAVVEEERAAKKEELLSSLKEGDVVEGTVARLTDFGAFVDIGGVDGLVHISELSHERVEKPSEVVSVGQEV 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 263 NVVILDFDEEKKRIALGLKQLAPHPWDALDPNLKVGDHVKGKVVVMADYGAFVEIQPGVEGLIHVSEMSWsQHLRSAQEF 342
Cdd:PRK06676  243 EVKVLSIDWETERISLSLKDTLPGPWEGVEEKLPEGDVIEGTVKRLTDFGAFVEVLPGVEGLVHISQISH-KHIATPSEV 321
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1276677562 343 MKAGDEVEAVVLTLDRDERKMSLGIKQLKEDPWEAIEAKYP 383
Cdd:PRK06676  322 LEEGQEVKVKVLEVNEEEKRISLSIKALEEAPAEEEDRREE 362
PRK00087 PRK00087
bifunctional 4-hydroxy-3-methylbut-2-enyl diphosphate reductase/30S ribosomal protein S1;
19-383 2.02e-113

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


Pssm-ID: 234623 [Multi-domain]  Cd Length: 647  Bit Score: 352.33  E-value: 2.02e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562  19 ENGVTVGGDKEELTKAYDNTLNKIQEHQVVEGEVISIDKKEVVVNIGYKSDGIIPASEFRYNP------ELKVGDKVEVY 92
Cdd:PRK00087  277 ELDNMEEVEENEQLEYMNELEKQIRRGDIVKGTVVSVNENEVFVDVGYKSEGVIPLRELTLDEisslkeSVKVGDEIEVK 356
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562  93 VENQEDKSGQLILSHKKARLQKSWVNINEALEADAVIQGYIKSRTKGGMIVDVFGIEAFLPGSQIDVHPIRDYDVFVGKT 172
Cdd:PRK00087  357 VLKLEDEDGYVVLSKKEADREKAWKELEEAFENGEPVKGKVKEVVKGGLLVDYGGVRAFLPASHVELGYVEDLSEYKGQE 436
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 173 MEFKVVKINQEFR-NVVVSHKALIEAELEAQRKEIISHLEKGQILEGVVKNITSYGVFVDLGGVDGLIHITDLSWGRIND 251
Cdd:PRK00087  437 LEVKIIEFNRKRRkKVVLSRKAILEEEKEKKKEETWNSLEEGDVVEGEVKRLTDFGAFVDIGGVDGLLHVSEISWGRVEK 516
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 252 PHEVVELDQKINVVILDFDEEKKRIALGLKQLAPHPWDALDPNLKVGDHVKGKVVVMADYGAFVEIQPGVEGLIHVSEMS 331
Cdd:PRK00087  517 PSDVLKVGDEIKVYILDIDKENKKLSLSLKKLLPDPWENVEEKYPVGSIVLGKVVRIAPFGAFVELEPGVDGLVHISQIS 596
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1276677562 332 WsQHLRSAQEFMKAGDEVEAVVLTLDRDERKMSLGIKQLKEDPWEAIEAKYP 383
Cdd:PRK00087  597 W-KRIDKPEDVLSEGEEVKAKILEVDPEEKRIRLSIKEVEEEPGDIEKVELE 647
PRK12269 PRK12269
bifunctional cytidylate kinase/ribosomal protein S1; Provisional
50-573 4.76e-106

bifunctional cytidylate kinase/ribosomal protein S1; Provisional


Pssm-ID: 105491 [Multi-domain]  Cd Length: 863  Bit Score: 339.00  E-value: 4.76e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562  50 GEVISIDKKEVVVNIGYKSDGIIPASEFRYNPelKVGDKVEVYVENQEDKSGQLilSHKKARLQKSWVNINEALEADAVI 129
Cdd:PRK12269  327 GTVVQVNAGTVFVDIGGKSEGRVPVEEFEAPP--KAGDGVRVYVERVTPYGPEL--SKTKADRLGLKVKLRDAERDGTPV 402
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 130 QGYIKSRT--KGGMIVDV-FGIEAFLPGSQIDVHPIRDYDVFVGKTMEFKVVKINQEFR-----NVVVSHKALIEAELEA 201
Cdd:PRK12269  403 EGRIVRLTekKSGFEVDLgAGMMAFLPISQSDCQKVDAPESLIGLTSKFYIERISQSKQhrgndNIVINRRRYLEERARQ 482
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 202 QRKEIISHLEKGQILEGVVKNITSYGVFVDLGGVDGLIHITDLSWGRINDPHEVVELDQKINVVILDFDEEKKRIALGLK 281
Cdd:PRK12269  483 AREEFFNSVHIEDSVSGVVKSFTSFGAFIDLGGFDGLLHVNDMSWGHVARPREFVKKGQTIELKVIRLDQAEKRINLSLK 562
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 282 QLAPHPWDALDPNLKVGDHVKGKVVVMADYGAFVEIQPGVEGLIHVSEMSWSQHLRSAQEFMKAGDEVEAVVLTLDRDER 361
Cdd:PRK12269  563 HFQPDPWLEFENKFGVNDVVKGRVTKIADFGAFIELAEGIEGLAHISEFSWVKKTSKPSDMVKIGDEVECMILGYDIQAG 642
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 362 KMSLGIKQLKEDPWEAIEAKYPVGSKHVAKVRNFTNFGIFVELEEGVDGLIHISDLSWTKKVKHPSEFTQVGADMDVIVL 441
Cdd:PRK12269  643 RVSLGLKQVTANPWEEIEARYPVGARFTRRIVKVTNAGAFIEMEEGIDGFLHVDDLSWVKRTRPADHELEVGKEIECMVI 722
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 442 EIDKENRRLSLGHKQLETNPWDTYESIYTPGSTHVGKITESMDKGAVITLNEGGEGFATPKHLVK-EDGSQAQ------L 514
Cdd:PRK12269  723 ECDPQARRIRLGVKQLSDNPWQVFANAYGVGSTVEGEVSSVTDFGIFVRVPGGVEGLVRKQHLVEnRDGDPGEalrkyaV 802
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1276677562 515 GEELPFVVIEFVKDTKRIILSHSRTFEEVKEEQARRQRTASKKHSEPASQINNVAAGTS 573
Cdd:PRK12269  803 GDRVKAVIVDMNVKDRKVAFSVRDYQRKVQRDELSRYMSAPRGEDEGSFTLGDLMRQTS 861
rpsA PRK13806
30S ribosomal protein S1; Provisional
30-453 2.56e-102

30S ribosomal protein S1; Provisional


Pssm-ID: 237516 [Multi-domain]  Cd Length: 491  Bit Score: 318.59  E-value: 2.56e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562  30 ELTKAYDNTLN-KIQEHQVVEGEVISIDKKEVVVNIGYKSDGIIPASEFR-YNPEL--KVGDKVEVYVENQEDksGQLIL 105
Cdd:PRK13806   19 ELLEAYEGERKtELRVGDKITGTVIAITEDSVFVDTGSKVDGVVDRAELLdADGELtvAVGDEVELYVVSVNG--QEIRL 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 106 ShKKARLQKSWVNINEALEADAVIQGYIKSRTKGGMIVDVFGIEAFLPGSQIDVHPIRDYDVFVGKTMEFKVVKINQEFR 185
Cdd:PRK13806   97 S-KALSGQGGAAMLEEAYENGVPVEGKVTGTCKGGFNVEVLGRRAFCPVSQIDLRYVEDPESYVGQTFQFLITRVEENGR 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 186 NVVVSHKALIEAELEAQRKEIISHLEKGQILEGVVKNITSYGVFVDLG-GVDGLIHITDLSWGRINDPHEVVELDQKINV 264
Cdd:PRK13806  176 NIVVSRRALLEREQKEALEAFMETVKEGDVVEGTVTRLAPFGAFVELApGVEGMVHISELSWSRVQKADEAVSVGDTVRV 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 265 VILDFDEEKK----RIALGLKQLAPHPWDALDPNLKVGDHVKGKVVVMADYGAFVEIQPGVEGLIHVSEMSWSQHLRSAQ 340
Cdd:PRK13806  256 KVLGIERAKKgkglRISLSIKQAGGDPWDTVGDRLKAGDKVTGKVVRLAPFGAFVEILPGIEGLVHVSEMSWTRRVNKPE 335
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 341 EFMKAGDEVEAVVLTLDRDERKMSLGIKQLKEDPWEAIEAKYPVGSKHVAKVRNFTNFGIFVELEEGVDGLIHISDLSWT 420
Cdd:PRK13806  336 DVVAPGDAVAVKIKDIDPAKRRISLSLRDAEGDPWADVAERFAPGTTVTGTVEKRAQFGLFVNLAPGVTGLLPASVISRA 415
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 1276677562 421 KKvkhPSEFTQV--GADMDVIVLEIDKENRRLSLG 453
Cdd:PRK13806  416 GK---PATYEKLkpGDSVTLVVEEIDTAKRKISLA 447
rpsA PRK07899
30S ribosomal protein S1; Reviewed
26-373 5.67e-88

30S ribosomal protein S1; Reviewed


Pssm-ID: 236126 [Multi-domain]  Cd Length: 486  Bit Score: 281.16  E-value: 5.67e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562  26 GDKEELTKAYDNTLNKIQEHQVVEGEVISIDKKEVVVNIGYKSDGIIPASEFRY------NPELKVGDKVEVYVENQEDK 99
Cdd:PRK07899   17 GSAEDFLAAIDKTIKYFNDGDIVEGTVVKVDRDEVLLDIGYKTEGVIPSRELSIkhdvdpNEVVEVGDEVEALVLQKEDK 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 100 SGQLILSHKKARLQKSWVNINEALEADAVIQGYIKSRTKGGMIVDVfGIEAFLPGSQIDVHPIRDYDVFVGKTMEFKVVK 179
Cdd:PRK07899   97 EGRLILSKKRAQYERAWGTIEKIKEKDGVVTGTVIEVVKGGLILDI-GLRGFLPASLVEMRRVRDLQPYIGQEIEAKIIE 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 180 INQEFRNVVVSHKALIEAELEAQRKEIISHLEKGQILEGVVKNITSYGVFVDLGGVDGLIHITDLSWGRINDPHEVVELD 259
Cdd:PRK07899  176 LDKNRNNVVLSRRAWLEQTQSEVRSEFLNQLQKGQVRKGVVSSIVNFGAFVDLGGVDGLVHVSELSWKHIDHPSEVVEVG 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 260 QKINVVILDFDEEKKRIALGLKQLAPHPWDALDPNLKVGDHVKGKVVVMADYGAFVEIQPGVEGLIHVSEMSwSQHLRSA 339
Cdd:PRK07899  256 QEVTVEVLDVDMDRERVSLSLKATQEDPWQQFARTHAIGQIVPGKVTKLVPFGAFVRVEEGIEGLVHISELA-ERHVEVP 334
                         330       340       350
                  ....*....|....*....|....*....|....
gi 1276677562 340 QEFMKAGDEVEAVVLTLDRDERKMSLGIKQLKED 373
Cdd:PRK07899  335 EQVVQVGDEVFVKVIDIDLERRRISLSLKQANEG 368
rpsA TIGR00717
ribosomal protein S1; This model describes ribosomal protein S1, RpsA. This protein is found ...
29-368 2.29e-49

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: 179.16  E-value: 2.29e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562  29 EELTKAYDNTLNKIQEHQVVEGEVISIDKKEVVVNIGyKSDGIIPASEFRY----NPE--LKVGDKVEVYVENQEDKSGQ 102
Cdd:TIGR00717 172 EERSQAREELLENLKEGDVVKGVVKNITDFGAFVDLG-GVDGLLHITDMSWkrvkHPSeyVKVGQEVKVKVIKFDKEKGR 250
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 103 LILShKKARLQKSWVNINEALEADAVIQGYIKSRTKGGMIVDVF-GIEAFLPGSQID-----VHPiRDYdVFVGKTMEFK 176
Cdd:TIGR00717 251 ISLS-LKQLGEDPWEAIEKKFPVGDKITGRVTNLTDYGVFVEIEeGIEGLVHVSEMSwvkknSHP-SKV-VKKGDEVEVM 327
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 177 VVKINQEFRNVVVSHKALIEAELEaqrkEIISHLEKGQILEGVVKNITSYGVFVDLG-GVDGLIHITDLSWGR-INDPHE 254
Cdd:TIGR00717 328 ILDIDPERRRLSLGLKQCKANPWE----QFEEKHPVGDRVTGKIKKITDFGAFVELEgGIDGLIHLSDISWDKdGREADH 403
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 255 VVELDQKINVVILDFDEEKKRIALGLKQLAPHPWDALDPNLKVGDHVKGKVVVMADYGAFVEIQPGVEGLIHVSEMSWSQ 334
Cdd:TIGR00717 404 LYKKGDEIEAVVLAVDKEKKRISLGVKQLTENPWEKFAAKYKVGSVVKGKVTEIKDFGAFVELPGGVEGLIRNSELSENR 483
                         330       340       350
                  ....*....|....*....|....*....|....
gi 1276677562 335 HLRSAQEFmKAGDEVEAVVLTLDRDERKMSLGIK 368
Cdd:TIGR00717 484 DEDKTDEI-KVGDEVEAKVVDIDKKNRKVSLSVK 516
PRK07400 PRK07400
30S ribosomal protein S1; Reviewed
47-295 5.47e-39

30S ribosomal protein S1; Reviewed


Pssm-ID: 180960 [Multi-domain]  Cd Length: 318  Bit Score: 145.71  E-value: 5.47e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562  47 VVEGEVISIDKKEVVVNIGYKSDGIIPASEFRYN----PE--LKVGDKVEVYVENQEDKSGQLILSHKKARLQKSWVNIN 120
Cdd:PRK07400   34 IVNGTVFSLEPRGALIDIGAKTAAFMPIQEMSINrvegPEevLQPNETREFFILSDENEDGQLTLSIRRIEYMRAWERVR 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 121 EALEADAVIQGYIKSRTKGGMIVDVFGIEAFLPGSQIDVHPIRDYdvFVGKTMEFKVVKINQEFRNVVVSHK-ALIEael 199
Cdd:PRK07400  114 QLQKEDATVRSEVFATNRGGALVRIEGLRGFIPGSHISTRKPKEE--LVGEELPLKFLEVDEERNRLVLSHRrALVE--- 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 200 eaqRKeiISHLEKGQILEGVVKNITSYGVFVDLGGVDGLIHITDLSWGRINDPHEVVELDQKINVVILDFDEEKKRIALG 279
Cdd:PRK07400  189 ---RK--MNRLEVGEVVVGTVRGIKPYGAFIDIGGVSGLLHISEISHEHIETPHSVFNVNDEMKVMIIDLDAERGRISLS 263
                         250
                  ....*....|....*..
gi 1276677562 280 LKQLAPHPWDAL-DPNL 295
Cdd:PRK07400  264 TKQLEPEPGDMLkDPQK 280
S1_RPS1_repeat_ec3 cd05688
S1_RPS1_repeat_ec3: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
212-279 3.48e-30

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: 112.72  E-value: 3.48e-30
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1276677562 212 KGQILEGVVKNITSYGVFVDLGGVDGLIHITDLSWGRINDPHEVVELDQKINVVILDFDEEKKRIALG 279
Cdd:cd05688     1 EGDVVEGTVKSITDFGAFVDLGGVDGLLHISDMSWGRVKHPSEVVNVGDEVEVKVLKIDKERKRISLG 68
S1_RPS1_repeat_ec2_hs2 cd04465
S1_RPS1_repeat_ec2_hs2: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
126-192 3.16e-23

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: 92.91  E-value: 3.16e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1276677562 126 DAVIQGYIKSRTKGGMIVDVFGIEAFLPGSQIDVHPIRDYDVFVGKTMEFKVVKINQEFRNVVVSHK 192
Cdd:cd04465     1 GEIVEGKVTEKVKGGLIVDIEGVRAFLPASQVDLRPVEDLDEYVGKELKFKIIEIDRERNNIVLSRR 67
S1_RPS1_repeat_ec5 cd05690
S1_RPS1_repeat_ec5: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
385-453 2.29e-22

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: 90.63  E-value: 2.29e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1276677562 385 GSKHVAKVRNFTNFGIFVELEEGVDGLIHISDLSWTKKVKHPSEFTQVGADMDVIVLEIDKENRRLSLG 453
Cdd:cd05690     1 GTVVSGKIKSITDFGIFVGLDGGIDGLVHISDISWTQRVRHPSEIYKKGQEVEAVVLNIDVERERISLG 69
S1_RPS1_repeat_ec4 cd05689
S1_RPS1_repeat_ec4: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
382-453 4.83e-22

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: 89.94  E-value: 4.83e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1276677562 382 YPVGSKHVAKVRNFTNFGIFVELEEGVDGLIHISDLSWTKKVKHPSEFTQVGADMDVIVLEIDKENRRLSLG 453
Cdd:cd05689     1 YPEGTRLFGKVTNLTDYGCFVELEEGVEGLVHVSEMDWTNKNIHPSKVVSLGDEVEVMVLDIDEERRRISLG 72
S1_RPS1_repeat_ec1_hs1 cd05687
S1_RPS1_repeat_ec1_hs1: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
46-108 8.93e-21

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: 86.43  E-value: 8.93e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1276677562  46 QVVEGEVISIDKKEVVVNIGYKSDGIIPASEFRYNP------ELKVGDKVEVYVENQEDKSGQLILSHK 108
Cdd:cd05687     2 DIVKGTVVSVDDDEVLVDIGYKSEGIIPISEFSDDPiengedEVKVGDEVEVYVLRVEDEEGNVVLSKR 70
S1_RPS1_repeat_ec3 cd05688
S1_RPS1_repeat_ec3: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
384-453 2.62e-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: 84.99  E-value: 2.62e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 384 VGSKHVAKVRNFTNFGIFVELEeGVDGLIHISDLSWtKKVKHPSEFTQVGADMDVIVLEIDKENRRLSLG 453
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 ...
298-366 1.37e-19

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


Pssm-ID: 240195 [Multi-domain]  Cd Length: 69  Bit Score: 82.93  E-value: 1.37e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1276677562 298 GDHVKGKVVVMADYGAFVEIQPGVEGLIHVSEMSWSQHLRSAQEFMKAGDEVEAVVLTLDRDERKMSLG 366
Cdd:cd05690     1 GTVVSGKIKSITDFGIFVGLDGGIDGLVHISDISWTQRVRHPSEIYKKGQEVEAVVLNIDVERERISLG 69
Tex COG2183
Transcriptional accessory protein Tex/SPT6 [Transcription];
207-282 1.78e-19

Transcriptional accessory protein Tex/SPT6 [Transcription];


Pssm-ID: 441786 [Multi-domain]  Cd Length: 719  Bit Score: 92.40  E-value: 1.78e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1276677562 207 ISHLEKGQILEGVVKNITSYGVFVDLGgV--DGLIHITDLSWGRINDPHEVVELDQKINVVILDFDEEKKRIALGLKQ 282
Cdd:COG2183   636 IEDLKPGMILEGTVTNVTDFGAFVDIG-VhqDGLVHISQLSDRFVKDPREVVKVGDIVKVKVLEVDLKRKRISLSMKL 712
S1 smart00316
Ribosomal protein S1-like RNA-binding domain;
211-281 4.41e-18

Ribosomal protein S1-like RNA-binding domain;


Pssm-ID: 197648 [Multi-domain]  Cd Length: 72  Bit Score: 78.80  E-value: 4.41e-18
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1276677562  211 EKGQILEGVVKNITSYGVFVDLG-GVDGLIHITDLSWGRINDPHEVVELDQKINVVILDFDEEKKRIALGLK 281
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 ...
298-366 4.97e-17

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


Pssm-ID: 240194 [Multi-domain]  Cd Length: 72  Bit Score: 75.69  E-value: 4.97e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1276677562 298 GDHVKGKVVVMADYGAFVEIQPGVEGLIHVSEMSWSQHLRSAQEFMKAGDEVEAVVLTLDRDERKMSLG 366
Cdd:cd05689     4 GTRLFGKVTNLTDYGCFVELEEGVEGLVHVSEMDWTNKNIHPSKVVSLGDEVEVMVLDIDEERRRISLG 72
S1_Tex cd05685
S1_Tex: The C-terminal S1 domain of a transcription accessory factor called Tex, which has ...
213-278 1.92e-16

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


Pssm-ID: 240190 [Multi-domain]  Cd Length: 68  Bit Score: 73.81  E-value: 1.92e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1276677562 213 GQILEGVVKNITSYGVFVDLG-GVDGLIHITDLSWGRINDPHEVVELDQKINVVILDFDEEKKRIAL 278
Cdd:cd05685     1 GMVLEGVVTNVTDFGAFVDIGvKQDGLIHISKMADRFVSHPSDVVSVGDIVEVKVISIDEERGRISL 67
YabR COG1098
Predicted RNA-binding protein, contains ribosomal protein S1 (RPS1) domain [General function ...
210-294 3.01e-16

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


Pssm-ID: 440715 [Multi-domain]  Cd Length: 130  Bit Score: 75.22  E-value: 3.01e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 210 LEKGQILEGVVKNITSYGVFVDL-GGVDGLIHITDLSWGRINDPHEVVELDQKINVVILDFDeEKKRIALGLKQLAPHPW 288
Cdd:COG1098     3 IEVGDIVEGKVTGITPFGAFVELpEGTTGLVHISEIADGYVKDINDYLKVGDEVKVKVLSID-EDGKISLSIKQAEEKPK 81

                  ....*.
gi 1276677562 289 DALDPN 294
Cdd:COG1098    82 RPPRPR 87
S1_RPS1_repeat_ec5 cd05690
S1_RPS1_repeat_ec5: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
213-279 7.23e-16

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: 72.14  E-value: 7.23e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1276677562 213 GQILEGVVKNITSYGVFVDL-GGVDGLIHITDLSWG-RINDPHEVVELDQKINVVILDFDEEKKRIALG 279
Cdd:cd05690     1 GTVVSGKIKSITDFGIFVGLdGGIDGLVHISDISWTqRVRHPSEIYKKGQEVEAVVLNIDVERERISLG 69
PRK11824 PRK11824
polynucleotide phosphorylase/polyadenylase; Provisional
204-283 1.21e-15

polynucleotide phosphorylase/polyadenylase; Provisional


Pssm-ID: 236995 [Multi-domain]  Cd Length: 693  Bit Score: 80.48  E-value: 1.21e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 204 KEIISHLEKGQILEGVVKNITSYGVFVD-LGGVDGLIHITDLSWGRINDPHEVVELDQKINVVILDFDeEKKRIALGLKQ 282
Cdd:PRK11824  613 EGITAEPEVGEIYEGKVVRIVDFGAFVEiLPGKDGLVHISEIADERVEKVEDVLKEGDEVKVKVLEID-KRGRIRLSRKA 691

                  .
gi 1276677562 283 L 283
Cdd:PRK11824  692 V 692
S1 smart00316
Ribosomal protein S1-like RNA-binding domain;
296-368 5.23e-15

Ribosomal protein S1-like RNA-binding domain;


Pssm-ID: 197648 [Multi-domain]  Cd Length: 72  Bit Score: 69.94  E-value: 5.23e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1276677562  296 KVGDHVKGKVVVMADYGAFVEIQPGVEGLIHVSEMSWSQHLRSAQEFmKAGDEVEAVVLTLDRDERKMSLGIK 368
Cdd:smart00316   1 EVGDVVEGTVTEITPGGAFVDLGNGVEGLIPISELSDKRVKDPEEVL-KVGDEVKVKVLSVDEEKGRIILSLK 72
S1_Rrp5_repeat_sc12 cd05708
S1_Rrp5_repeat_sc12: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ...
213-281 1.08e-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: 69.28  E-value: 1.08e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1276677562 213 GQILEGVVKNITSYGVFVDLGGVD--GLIHITDLSWGRINDPHEVVELDQKINVVILDFDEEKKRIALGLK 281
Cdd:cd05708     3 GQKIDGTVRRVEDYGVFIDIDGTNvsGLCHKSEISDNRVADASKLFRVGDKVRAKVLKIDAEKKRISLGLK 73
PRK07400 PRK07400
30S ribosomal protein S1; Reviewed
209-463 1.28e-14

30S ribosomal protein S1; Reviewed


Pssm-ID: 180960 [Multi-domain]  Cd Length: 318  Bit Score: 75.22  E-value: 1.28e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 209 HLEKGQILEGVVKNITSYGVFVDLGG-VDGLIHITDLSWGRINDPHEVVELDQKINVVILDFDEEKKRIALGLKQLA-PH 286
Cdd:PRK07400   28 HFKPGDIVNGTVFSLEPRGALIDIGAkTAAFMPIQEMSINRVEGPEEVLQPNETREFFILSDENEDGQLTLSIRRIEyMR 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 287 PWDALDPNLKVGDHVKGKVVVMADYGAFVEIQpGVEGLIHVSEMSwsqhLRSAQEFMkAGDEVEAVVLTLDRDERKMSLG 366
Cdd:PRK07400  108 AWERVRQLQKEDATVRSEVFATNRGGALVRIE-GLRGFIPGSHIS----TRKPKEEL-VGEELPLKFLEVDEERNRLVLS 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 367 IKQ-LKEDPWEAIEakypVGSKHVAKVRNFTNFGIFVELEeGVDGLIHISDLSwTKKVKHPSEFTQVGADMDVIVLEIDK 445
Cdd:PRK07400  182 HRRaLVERKMNRLE----VGEVVVGTVRGIKPYGAFIDIG-GVSGLLHISEIS-HEHIETPHSVFNVNDEMKVMIIDLDA 255
                         250
                  ....*....|....*...
gi 1276677562 446 ENRRLSLGHKQLETNPWD 463
Cdd:PRK07400  256 ERGRISLSTKQLEPEPGD 273
S1 smart00316
Ribosomal protein S1-like RNA-binding domain;
384-455 1.79e-14

Ribosomal protein S1-like RNA-binding domain;


Pssm-ID: 197648 [Multi-domain]  Cd Length: 72  Bit Score: 68.40  E-value: 1.79e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1276677562  384 VGSKHVAKVRNFTNFGIFVELEEGVDGLIHISDLSWtKKVKHPSEFTQVGADMDVIVLEIDKENRRLSLGHK 455
Cdd:smart00316   2 VGDVVEGTVTEITPGGAFVDLGNGVEGLIPISELSD-KRVKDPEEVLKVGDEVKVKVLSVDEEKGRIILSLK 72
YabR COG1098
Predicted RNA-binding protein, contains ribosomal protein S1 (RPS1) domain [General function ...
294-374 2.54e-14

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


Pssm-ID: 440715 [Multi-domain]  Cd Length: 130  Bit Score: 69.82  E-value: 2.54e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 294 NLKVGDHVKGKVVVMADYGAFVEIQPGVEGLIHVSEMSwSQHLRSAQEFMKAGDEVEAVVLTLDRDErKMSLGIKQLKED 373
Cdd:COG1098     2 SIEVGDIVEGKVTGITPFGAFVELPEGTTGLVHISEIA-DGYVKDINDYLKVGDEVKVKVLSIDEDG-KISLSIKQAEEK 79

                  .
gi 1276677562 374 P 374
Cdd:COG1098    80 P 80
PRK08059 PRK08059
general stress protein 13; Validated
293-376 4.57e-14

general stress protein 13; Validated


Pssm-ID: 181215 [Multi-domain]  Cd Length: 123  Bit Score: 68.92  E-value: 4.57e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 293 PNLKVGDHVKGKVVVMADYGAFVEIQPGVEGLIHVSEMSwSQHLRSAQEFMKAGDEVEAVVLTLDRDERKMSLGIKQLKE 372
Cdd:PRK08059    3 SQYEVGSVVTGKVTGIQPYGAFVALDEETQGLVHISEIT-HGFVKDIHDFLSVGDEVKVKVLSVDEEKGKISLSIRATEE 81

                  ....
gi 1276677562 373 DPWE 376
Cdd:PRK08059   82 APEA 85
S1 pfam00575
S1 RNA binding domain; The S1 domain occurs in a wide range of RNA associated proteins. It is ...
210-280 5.71e-14

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


Pssm-ID: 425760 [Multi-domain]  Cd Length: 72  Bit Score: 66.93  E-value: 5.71e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1276677562 210 LEKGQILEGVVKNITSYGVFVDLG-GVDGLIHITDLSWGRINDPHEVVELDQKINVVILDFDEEKKRIALGL 280
Cdd:pfam00575   1 PEKGDVVEGEVTRVTKGGAFVDLGnGVEGFIPISELSDDHVEDPDEVIKVGDEVKVKVLKVDKDRRRIILSI 72
S1_like cd00164
S1_like: Ribosomal protein S1-like RNA-binding domain. Found in a wide variety of ...
301-366 1.45e-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: 65.48  E-value: 1.45e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1276677562 301 VKGKVVVMADYGAFVEIQPGVEGLIHVSEMSWSqHLRSAQEFMKAGDEVEAVVLTLDRDERKMSLG 366
Cdd:cd00164     1 VTGKVVSITKFGVFVELEDGVEGLVHISELSDK-FVKDPSEVFKVGDEVEVKVLEVDPEKGRISLS 65
S1_like cd00164
S1_like: Ribosomal protein S1-like RNA-binding domain. Found in a wide variety of ...
390-453 1.51e-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: 65.48  E-value: 1.51e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1276677562 390 AKVRNFTNFGIFVELEEGVDGLIHISDLSWtKKVKHPSEFTQVGADMDVIVLEIDKENRRLSLG 453
Cdd:cd00164     3 GKVVSITKFGVFVELEDGVEGLVHISELSD-KFVKDPSEVFKVGDEVEVKVLEVDPEKGRISLS 65
S1_dom_CvfD NF040579
CvfD/Ygs/GSP13 family RNA-binding post-transcriptional regulator; CvfD, Ygs, and GSP13 form a ...
296-374 2.83e-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: 66.30  E-value: 2.83e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1276677562 296 KVGDHVKGKVVVMADYGAFVEIQPGVEGLIHVSEMSwSQHLRSAQEFMKAGDEVEAVVLTLDRDERKMSLGIKQLKEDP 374
Cdd:NF040579    2 KIGDIVEGKVTGIQPYGAFVALDEHTQGLIHISEIK-HGYVKDINDFLKVGQEVKVKVLDIDEYTGKISLSLRALEEAP 79
S1_like cd00164
S1_like: Ribosomal protein S1-like RNA-binding domain. Found in a wide variety of ...
216-279 2.95e-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: 64.71  E-value: 2.95e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1276677562 216 LEGVVKNITSYGVFVDLG-GVDGLIHITDLSWGRINDPHEVVELDQKINVVILDFDEEKKRIALG 279
Cdd:cd00164     1 VTGKVVSITKFGVFVELEdGVEGLVHISELSDKFVKDPSEVFKVGDEVEVKVLEVDPEKGRISLS 65
PRK08059 PRK08059
general stress protein 13; Validated
208-287 3.09e-13

general stress protein 13; Validated


Pssm-ID: 181215 [Multi-domain]  Cd Length: 123  Bit Score: 66.61  E-value: 3.09e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 208 SHLEKGQILEGVVKNITSYGVFVDL-GGVDGLIHITDLSWGRINDPHEVVELDQKINVVILDFDEEKKRIALGLKQLAPH 286
Cdd:PRK08059    3 SQYEVGSVVTGKVTGIQPYGAFVALdEETQGLVHISEITHGFVKDIHDFLSVGDEVKVKVLSVDEEKGKISLSIRATEEA 82

                  .
gi 1276677562 287 P 287
Cdd:PRK08059   83 P 83
PRK11824 PRK11824
polynucleotide phosphorylase/polyadenylase; Provisional
376-458 7.08e-13

polynucleotide phosphorylase/polyadenylase; Provisional


Pssm-ID: 236995 [Multi-domain]  Cd Length: 693  Bit Score: 71.62  E-value: 7.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 376 EAIEAKYPVGSKHVAKVRNFTNFGIFVELEEGVDGLIHISDLSWtKKVKHPSEFTQVGADMDVIVLEIDKENrRLSLGHK 455
Cdd:PRK11824  613 EGITAEPEVGEIYEGKVVRIVDFGAFVEILPGKDGLVHISEIAD-ERVEKVEDVLKEGDEVKVKVLEIDKRG-RIRLSRK 690

                  ...
gi 1276677562 456 QLE 458
Cdd:PRK11824  691 AVL 693
S1_RPS1_repeat_hs4 cd05692
S1_RPS1_repeat_hs4: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
298-368 1.20e-12

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


Pssm-ID: 240197 [Multi-domain]  Cd Length: 69  Bit Score: 63.07  E-value: 1.20e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1276677562 298 GDHVKGKVVVMADYGAFVEIQPGVEGLIHVSEMSWSqHLRSAQEFMKAGDEVEavVLTLDRDER-KMSLGIK 368
Cdd:cd05692     1 GSVVEGTVTRLKPFGAFVELGGGISGLVHISQIAHK-RVKDVKDVLKEGDKVK--VKVLSIDARgRISLSIK 69
S1_RPS1_repeat_ec4 cd05689
S1_RPS1_repeat_ec4: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
213-279 1.32e-12

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


Pssm-ID: 240194 [Multi-domain]  Cd Length: 72  Bit Score: 62.98  E-value: 1.32e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1276677562 213 GQILEGVVKNITSYGVFVDLG-GVDGLIHITDLSWGRIN-DPHEVVELDQKINVVILDFDEEKKRIALG 279
Cdd:cd05689     4 GTRLFGKVTNLTDYGCFVELEeGVEGLVHVSEMDWTNKNiHPSKVVSLGDEVEVMVLDIDEERRRISLG 72
Pnp COG1185
Polyribonucleotide nucleotidyltransferase (polynucleotide phosphorylase) [Translation, ...
296-368 1.61e-12

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


Pssm-ID: 440798 [Multi-domain]  Cd Length: 686  Bit Score: 70.42  E-value: 1.61e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1276677562 296 KVGDHVKGKVVVMADYGAFVEIQPGVEGLIHVSEMSWsQHLRSAQEFMKAGDEVEAVVLTLDrDERKMSLGIK 368
Cdd:COG1185   615 EVGEIYEGKVVRIMDFGAFVEILPGKDGLVHISELAD-ERVEKVEDVLKEGDEVKVKVLEID-DQGRIKLSRK 685
S1_DHX8_helicase cd05684
S1_DHX8_helicase: The N-terminal S1 domain of human ATP-dependent RNA helicase DHX8, a DEAH ...
213-281 2.08e-12

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


Pssm-ID: 240189 [Multi-domain]  Cd Length: 79  Bit Score: 62.64  E-value: 2.08e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1276677562 213 GQILEGVVKNITSYGVFVDL----GGVDGLIHITDLSW-GRINDPHEVVELDQKINVVILDFDEEKkrIALGLK 281
Cdd:cd05684     1 GKIYKGKVTSIMDFGCFVQLeglkGRKEGLVHISQLSFeGRVANPSDVVKRGQKVKVKVISIQNGK--ISLSMK 72
S1_Tex cd05685
S1_Tex: The C-terminal S1 domain of a transcription accessory factor called Tex, which has ...
391-452 2.38e-12

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: 62.25  E-value: 2.38e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1276677562 391 KVRNFTNFGIFVELEEGVDGLIHISDLSwTKKVKHPSEFTQVGADMDVIVLEIDKENRRLSL 452
Cdd:cd05685     7 VVTNVTDFGAFVDIGVKQDGLIHISKMA-DRFVSHPSDVVSVGDIVEVKVISIDEERGRISL 67
PRK11824 PRK11824
polynucleotide phosphorylase/polyadenylase; Provisional
296-370 5.72e-12

polynucleotide phosphorylase/polyadenylase; Provisional


Pssm-ID: 236995 [Multi-domain]  Cd Length: 693  Bit Score: 68.54  E-value: 5.72e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1276677562 296 KVGDHVKGKVVVMADYGAFVEIQPGVEGLIHVSEMSWsQHLRSAQEFMKAGDEVEavVLTLDRDER-KMSLGIKQL 370
Cdd:PRK11824  620 EVGEIYEGKVVRIVDFGAFVEILPGKDGLVHISEIAD-ERVEKVEDVLKEGDEVK--VKVLEIDKRgRIRLSRKAV 692
Pnp COG1185
Polyribonucleotide nucleotidyltransferase (polynucleotide phosphorylase) [Translation, ...
376-451 1.02e-11

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


Pssm-ID: 440798 [Multi-domain]  Cd Length: 686  Bit Score: 67.72  E-value: 1.02e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1276677562 376 EAIEAKYPVGSKHVAKVRNFTNFGIFVELEEGVDGLIHISDLSWtKKVKHPSEFTQVGADMDVIVLEIDKENR-RLS 451
Cdd:COG1185   608 EGITAEPEVGEIYEGKVVRIMDFGAFVEILPGKDGLVHISELAD-ERVEKVEDVLKEGDEVKVKVLEIDDQGRiKLS 683
S1_RPS1_repeat_hs4 cd05692
S1_RPS1_repeat_hs4: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
213-281 1.52e-11

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


Pssm-ID: 240197 [Multi-domain]  Cd Length: 69  Bit Score: 59.99  E-value: 1.52e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 213 GQILEGVVKNITSYGVFVDLG-GVDGLIHITDLSWGRINDPHEVVELDQKINVVILDFDeEKKRIALGLK 281
Cdd:cd05692     1 GSVVEGTVTRLKPFGAFVELGgGISGLVHISQIAHKRVKDVKDVLKEGDKVKVKVLSID-ARGRISLSIK 69
S1 pfam00575
S1 RNA binding domain; The S1 domain occurs in a wide range of RNA associated proteins. It is ...
295-367 1.71e-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: 59.99  E-value: 1.71e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1276677562 295 LKVGDHVKGKVVVMADYGAFVEIQPGVEGLIHVSEMSWSqHLRSAQEFMKAGDEVEAVVLTLDRDERKMSLGI 367
Cdd:pfam00575   1 PEKGDVVEGEVTRVTKGGAFVDLGNGVEGFIPISELSDD-HVEDPDEVIKVGDEVKVKVLKVDKDRRRIILSI 72
YabR COG1098
Predicted RNA-binding protein, contains ribosomal protein S1 (RPS1) domain [General function ...
381-461 1.95e-11

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


Pssm-ID: 440715 [Multi-domain]  Cd Length: 130  Bit Score: 61.73  E-value: 1.95e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 381 KYPVGSKHVAKVRNFTNFGIFVELEEGVDGLIHISDLSwTKKVKHPSEFTQVGADMDVIVLEIDKENR-RLSLghKQLET 459
Cdd:COG1098     2 SIEVGDIVEGKVTGITPFGAFVELPEGTTGLVHISEIA-DGYVKDINDYLKVGDEVKVKVLSIDEDGKiSLSI--KQAEE 78

                  ..
gi 1276677562 460 NP 461
Cdd:COG1098    79 KP 80
Tex COG2183
Transcriptional accessory protein Tex/SPT6 [Transcription];
392-452 2.55e-11

Transcriptional accessory protein Tex/SPT6 [Transcription];


Pssm-ID: 441786 [Multi-domain]  Cd Length: 719  Bit Score: 66.59  E-value: 2.55e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1276677562 392 VRNFTNFGIFVELeeGV--DGLIHISDLSwTKKVKHPSEFTQVGADMDVIVLEIDKENRRLSL 452
Cdd:COG2183   649 VTNVTDFGAFVDI--GVhqDGLVHISQLS-DRFVKDPREVVKVGDIVKVKVLEVDLKRKRISL 708
PRK05807 PRK05807
RNA-binding protein S1;
210-286 4.22e-11

RNA-binding protein S1;


Pssm-ID: 235614 [Multi-domain]  Cd Length: 136  Bit Score: 60.91  E-value: 4.22e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1276677562 210 LEKGQILEGVVKNITSYGVFVDLGGVDGLIHITDLSWGRINDPHEVVELDQKINVVILDFDeEKKRIALGLKQLAPH 286
Cdd:PRK05807    3 LKAGSILEGTVVNITNFGAFVEVEGKTGLVHISEVADTYVKDIREHLKEQDKVKVKVISID-DNGKISLSIKQAMKQ 78
S1_Rrp5_repeat_hs8_sc7 cd04461
S1_Rrp5_repeat_hs8_sc7: Rrp5 Homo sapiens S1 repeat 8 (hs8) and Saccharomyces cerevisiae S1 ...
207-280 4.71e-11

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


Pssm-ID: 239908 [Multi-domain]  Cd Length: 83  Bit Score: 59.14  E-value: 4.71e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1276677562 207 ISHLEKGQILEGVVKNITSYGVFVD-LGGVDGLIHITDLSWGRINDPHEVVELDQKINVVILDFDEEKKRIALGL 280
Cdd:cd04461     9 FSDLKPGMVVHGYVRNITPYGVFVEfLGGLTGLAPKSYISDEFVTDPSFGFKKGQSVTAKVTSVDEEKQRFLLSL 83
PRK08582 PRK08582
RNA-binding protein S1;
297-374 6.53e-11

RNA-binding protein S1;


Pssm-ID: 236305 [Multi-domain]  Cd Length: 139  Bit Score: 60.43  E-value: 6.53e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1276677562 297 VGDHVKGKVVVMADYGAFVEIQPGVEGLIHVSEMSwSQHLRSAQEFMKAGDEVEAVVLTLDRDErKMSLGIKQLKEDP 374
Cdd:PRK08582    5 VGSKLQGKVTGITNFGAFVELPEGKTGLVHISEVA-DNYVKDINDHLKVGDEVEVKVLNVEDDG-KIGLSIKKAKDRP 80
S1_Rrp5_repeat_sc12 cd05708
S1_Rrp5_repeat_sc12: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ...
296-368 1.24e-10

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


Pssm-ID: 240213 [Multi-domain]  Cd Length: 77  Bit Score: 57.72  E-value: 1.24e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1276677562 296 KVGDHVKGKVVVMADYGAFVEI-QPGVEGLIHVSEMSwSQHLRSAQEFMKAGDEVEAVVLTLDRDERKMSLGIK 368
Cdd:cd05708     1 KVGQKIDGTVRRVEDYGVFIDIdGTNVSGLCHKSEIS-DNRVADASKLFRVGDKVRAKVLKIDAEKKRISLGLK 73
S1_PNPase cd04472
S1_PNPase: Polynucleotide phosphorylase (PNPase), ), S1-like RNA-binding domain. PNPase is a ...
298-364 1.74e-10

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: 56.78  E-value: 1.74e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1276677562 298 GDHVKGKVVVMADYGAFVEIQPGVEGLIHVSEMSwSQHLRSAQEFMKAGDEVEAVVLTLDRDER-KMS 364
Cdd:cd04472     1 GKIYEGKVVKIKDFGAFVEILPGKDGLVHISELS-DERVEKVEDVLKVGDEVKVKVIEVDDRGRiSLS 67
S1 smart00316
Ribosomal protein S1-like RNA-binding domain;
43-108 2.68e-10

Ribosomal protein S1-like RNA-binding domain;


Pssm-ID: 197648 [Multi-domain]  Cd Length: 72  Bit Score: 56.46  E-value: 2.68e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1276677562   43 QEHQVVEGEVISIDKKEVVVNIGYKSDGIIPASEF------RYNPELKVGDKVEVYVENQEDKSGQLILSHK 108
Cdd:smart00316   1 EVGDVVEGTVTEITPGGAFVDLGNGVEGLIPISELsdkrvkDPEEVLKVGDEVKVKVLSVDEEKGRIILSLK 72
S1_PNPase cd04472
S1_PNPase: Polynucleotide phosphorylase (PNPase), ), S1-like RNA-binding domain. PNPase is a ...
213-278 3.31e-10

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: 56.01  E-value: 3.31e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1276677562 213 GQILEGVVKNITSYGVFVD-LGGVDGLIHITDLSWGRINDPHEVVELDQKINVVILDFDeEKKRIAL 278
Cdd:cd04472     1 GKIYEGKVVKIKDFGAFVEiLPGKDGLVHISELSDERVEKVEDVLKVGDEVKVKVIEVD-DRGRISL 66
PRK07252 PRK07252
S1 RNA-binding domain-containing protein;
295-373 4.66e-10

S1 RNA-binding domain-containing protein;


Pssm-ID: 180908 [Multi-domain]  Cd Length: 120  Bit Score: 57.40  E-value: 4.66e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1276677562 295 LKVGDHVKGKVVVMADYGAFVEIQPGVEGLIHVSEMSwSQHLRSAQEFMKAGDEVEAVVLTLDRDERKMSLGIKQLKED 373
Cdd:PRK07252    1 MKIGDKLKGTITGIKPYGAFVALENGTTGLIHISEIK-TGFIDNIHQLLKVGEEVLVQVVDFDEYTGKASLSLRTLEEE 78
S1 pfam00575
S1 RNA binding domain; The S1 domain occurs in a wide range of RNA associated proteins. It is ...
390-454 6.22e-10

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


Pssm-ID: 425760 [Multi-domain]  Cd Length: 72  Bit Score: 55.37  E-value: 6.22e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1276677562 390 AKVRNFTNFGIFVELEEGVDGLIHISDLSWtKKVKHPSEFTQVGADMDVIVLEIDKENRRLSLGH 454
Cdd:pfam00575   9 GEVTRVTKGGAFVDLGNGVEGFIPISELSD-DHVEDPDEVIKVGDEVKVKVLKVDKDRRRIILSI 72
PRK05807 PRK05807
RNA-binding protein S1;
295-369 6.44e-10

RNA-binding protein S1;


Pssm-ID: 235614 [Multi-domain]  Cd Length: 136  Bit Score: 57.45  E-value: 6.44e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1276677562 295 LKVGDHVKGKVVVMADYGAFVEIQpGVEGLIHVSEMSWSqHLRSAQEFMKAGDEVEAVVLTLDrDERKMSLGIKQ 369
Cdd:PRK05807    3 LKAGSILEGTVVNITNFGAFVEVE-GKTGLVHISEVADT-YVKDIREHLKEQDKVKVKVISID-DNGKISLSIKQ 74
S1_RPS1_repeat_hs4 cd05692
S1_RPS1_repeat_hs4: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
385-455 1.77e-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: 54.21  E-value: 1.77e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1276677562 385 GSKHVAKVRNFTNFGIFVELEEGVDGLIHISDLSwTKKVKHPSEFTQVGADMDVIVLEIDkENRRLSLGHK 455
Cdd:cd05692     1 GSVVEGTVTRLKPFGAFVELGGGISGLVHISQIA-HKRVKDVKDVLKEGDKVKVKVLSID-ARGRISLSIK 69
S1_Tex cd05685
S1_Tex: The C-terminal S1 domain of a transcription accessory factor called Tex, which has ...
298-365 2.40e-09

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: 53.78  E-value: 2.40e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1276677562 298 GDHVKGKVVVMADYGAFVEIQPGVEGLIHVSEMSwSQHLRSAQEFMKAGDEVEAVVLTLDRDERKMSL 365
Cdd:cd05685     1 GMVLEGVVTNVTDFGAFVDIGVKQDGLIHISKMA-DRFVSHPSDVVSVGDIVEVKVISIDEERGRISL 67
S1_Rrp5_repeat_sc12 cd05708
S1_Rrp5_repeat_sc12: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ...
384-455 3.17e-09

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: 53.87  E-value: 3.17e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1276677562 384 VGSKHVAKVRNFTNFGIFVELE-EGVDGLIHISDLSwTKKVKHPSEFTQVGADMDVIVLEIDKENRRLSLGHK 455
Cdd:cd05708     2 VGQKIDGTVRRVEDYGVFIDIDgTNVSGLCHKSEIS-DNRVADASKLFRVGDKVRAKVLKIDAEKKRISLGLK 73
S1_IF2_alpha cd04452
S1_IF2_alpha: The alpha subunit of translation Initiation Factor 2, S1-like RNA-binding domain. ...
211-282 3.99e-09

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


Pssm-ID: 239899 [Multi-domain]  Cd Length: 76  Bit Score: 53.36  E-value: 3.99e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1276677562 211 EKGQILEGVVKNITSYGVFVDL---GGVDGLIHITDLSWGRINDPHEVVELDQKINVVILDFDEEKKRIALGLKQ 282
Cdd:cd04452     2 EEGELVVVTVKSIADMGAYVSLleyGNIEGMILLSELSRRRIRSIRKLVKVGRKEVVKVIRVDKEKGYIDLSKKR 76
S1_RPS1_repeat_ec6 cd05691
S1_RPS1_repeat_ec6: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
298-370 4.94e-09

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


Pssm-ID: 240196 [Multi-domain]  Cd Length: 73  Bit Score: 53.04  E-value: 4.94e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1276677562 298 GDHVKGKVVVMADYGAFVEIQPGVEGLIHVSEMSwSQHLRSAQEFMKAGDEVEAVVLTLDRDERKMSLGIKQL 370
Cdd:cd05691     1 GSIVTGKVTEVDAKGATVKLGDGVEGFLRAAELS-RDRVEDATERFKVGDEVEAKITNVDRKNRKISLSIKAK 72
PRK08582 PRK08582
RNA-binding protein S1;
384-446 5.22e-09

RNA-binding protein S1;


Pssm-ID: 236305 [Multi-domain]  Cd Length: 139  Bit Score: 55.04  E-value: 5.22e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1276677562 384 VGSKHVAKVRNFTNFGIFVELEEGVDGLIHISDLSwTKKVKHPSEFTQVGADMDVIVLEIDKE 446
Cdd:PRK08582    5 VGSKLQGKVTGITNFGAFVELPEGKTGLVHISEVA-DNYVKDINDHLKVGDEVEVKVLNVEDD 66
PRK07252 PRK07252
S1 RNA-binding domain-containing protein;
213-284 6.32e-09

S1 RNA-binding domain-containing protein;


Pssm-ID: 180908 [Multi-domain]  Cd Length: 120  Bit Score: 54.32  E-value: 6.32e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1276677562 213 GQILEGVVKNITSYGVFVDL-GGVDGLIHITDLSWGRINDPHEVVELDQKINVVILDFDEEKKRIALGLKQLA 284
Cdd:PRK07252    4 GDKLKGTITGIKPYGAFVALeNGTTGLIHISEIKTGFIDNIHQLLKVGEEVLVQVVDFDEYTGKASLSLRTLE 76
S1_PNPase cd04472
S1_PNPase: Polynucleotide phosphorylase (PNPase), ), S1-like RNA-binding domain. PNPase is a ...
391-451 8.27e-09

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


Pssm-ID: 239918 [Multi-domain]  Cd Length: 68  Bit Score: 52.16  E-value: 8.27e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1276677562 391 KVRNFTNFGIFVELEEGVDGLIHISDLSwTKKVKHPSEFTQVGADMDVIVLEIDKENR-RLS 451
Cdd:cd04472     7 KVVKIKDFGAFVEILPGKDGLVHISELS-DERVEKVEDVLKVGDEVKVKVIEVDDRGRiSLS 67
S1_IF2_alpha cd04452
S1_IF2_alpha: The alpha subunit of translation Initiation Factor 2, S1-like RNA-binding domain. ...
296-369 1.12e-08

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


Pssm-ID: 239899 [Multi-domain]  Cd Length: 76  Bit Score: 52.20  E-value: 1.12e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1276677562 296 KVGDHVKGKVVVMADYGAFVEIQ--PGVEGLIHVSEMSwSQHLRSAQEFMKAGDEVEAVVLTLDRDERKMSLGIKQ 369
Cdd:cd04452     2 EEGELVVVTVKSIADMGAYVSLLeyGNIEGMILLSELS-RRRIRSIRKLVKVGRKEVVKVIRVDKEKGYIDLSKKR 76
PRK08059 PRK08059
general stress protein 13; Validated
380-461 1.27e-08

general stress protein 13; Validated


Pssm-ID: 181215 [Multi-domain]  Cd Length: 123  Bit Score: 53.51  E-value: 1.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 380 AKYPVGSKHVAKVRNFTNFGIFVELEEGVDGLIHISDLSwTKKVKHPSEFTQVGADMDVIVLEIDKENRRLSLGHKQLET 459
Cdd:PRK08059    3 SQYEVGSVVTGKVTGIQPYGAFVALDEETQGLVHISEIT-HGFVKDIHDFLSVGDEVKVKVLSVDEEKGKISLSIRATEE 81

                  ..
gi 1276677562 460 NP 461
Cdd:PRK08059   82 AP 83
S1 pfam00575
S1 RNA binding domain; The S1 domain occurs in a wide range of RNA associated proteins. It is ...
43-107 4.93e-08

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


Pssm-ID: 425760 [Multi-domain]  Cd Length: 72  Bit Score: 49.98  E-value: 4.93e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1276677562  43 QEHQVVEGEVISIDKKEVVVNIGYKSDGIIPASEF----RYNPE--LKVGDKVEVYVENQEDKSGQLILSH 107
Cdd:pfam00575   2 EKGDVVEGEVTRVTKGGAFVDLGNGVEGFIPISELsddhVEDPDevIKVGDEVKVKVLKVDKDRRRIILSI 72
PRK03987 PRK03987
translation initiation factor IF-2 subunit alpha; Validated
211-286 5.77e-08

translation initiation factor IF-2 subunit alpha; Validated


Pssm-ID: 235188 [Multi-domain]  Cd Length: 262  Bit Score: 54.06  E-value: 5.77e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1276677562 211 EKGQILEGVVKNITSYGVFVDL---GGVDGLIHITDLSWGRINDPHEVVELDQKINVVILDFDEEKKRIALGLKQLAPH 286
Cdd:PRK03987    7 EEGELVVGTVKEVKDFGAFVTLdeyPGKEGFIHISEVASGWVKNIRDHVKEGQKVVCKVIRVDPRKGHIDLSLKRVNEH 85
PLN00207 PLN00207
polyribonucleotide nucleotidyltransferase; Provisional
296-374 6.11e-08

polyribonucleotide nucleotidyltransferase; Provisional


Pssm-ID: 215104 [Multi-domain]  Cd Length: 891  Bit Score: 55.67  E-value: 6.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 296 KVGDHVKG-KVVVMADYGAFVEIQPGVEGLIHVSEMSwSQHLRSAQEFMKAGDEVEAVVLTLDrDERKMSLGIKQLKEDP 374
Cdd:PLN00207  752 TVGDIYRNcEIKSIAPYGAFVEIAPGREGLCHISELS-SNWLAKPEDAFKVGDRIDVKLIEVN-DKGQLRLSRRALLPEA 829
S1_RPS1_repeat_ec6 cd05691
S1_RPS1_repeat_ec6: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
213-283 6.35e-08

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


Pssm-ID: 240196 [Multi-domain]  Cd Length: 73  Bit Score: 49.96  E-value: 6.35e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1276677562 213 GQILEGVVKNITSYGVFVDLG-GVDGLIHITDLSWGRINDPHEVVELDQKINVVILDFDEEKKRIALGLKQL 283
Cdd:cd05691     1 GSIVTGKVTEVDAKGATVKLGdGVEGFLRAAELSRDRVEDATERFKVGDEVEAKITNVDRKNRKISLSIKAK 72
S1_DHX8_helicase cd05684
S1_DHX8_helicase: The N-terminal S1 domain of human ATP-dependent RNA helicase DHX8, a DEAH ...
391-452 1.03e-07

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


Pssm-ID: 240189 [Multi-domain]  Cd Length: 79  Bit Score: 49.54  E-value: 1.03e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1276677562 391 KVRNFTNFGIFVELE---EGVDGLIHISDLSWTKKVKHPSEFTQVGADMDVIVLEIdkENRRLSL 452
Cdd:cd05684     7 KVTSIMDFGCFVQLEglkGRKEGLVHISQLSFEGRVANPSDVVKRGQKVKVKVISI--QNGKISL 69
S1_NusA cd04455
S1_NusA: N-utilizing substance A protein (NusA), S1-like RNA-binding domain. S1-like ...
43-106 1.69e-07

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


Pssm-ID: 239902 [Multi-domain]  Cd Length: 67  Bit Score: 48.59  E-value: 1.69e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1276677562  43 QEHQVVEGEVISIDKKEVVVNIGyKSDGIIPASEFRYNPELKVGDKVEVYVE--NQEDKSGQLILS 106
Cdd:cd04455     2 REGEIVTGIVKRVDRGNVIVDLG-KVEAILPKKEQIPGESYRPGDRIKAYVLevRKTSKGPQIILS 66
S1 smart00316
Ribosomal protein S1-like RNA-binding domain;
124-192 1.79e-07

Ribosomal protein S1-like RNA-binding domain;


Pssm-ID: 197648 [Multi-domain]  Cd Length: 72  Bit Score: 48.37  E-value: 1.79e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1276677562  124 EADAVIQGYIKSRTKGGMIVDVF-GIEAFLPGSQI-DVHPIRDYDVF-VGKTMEFKVVKINQEFRNVVVSHK 192
Cdd:smart00316   1 EVGDVVEGTVTEITPGGAFVDLGnGVEGLIPISELsDKRVKDPEEVLkVGDEVKVKVLSVDEEKGRIILSLK 72
S1_pNO40 cd05686
S1_pNO40: pNO40 , S1-like RNA-binding domain. pNO40 is a nucleolar protein of unknown function ...
214-281 7.95e-07

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: 46.71  E-value: 7.95e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 214 QILEGVVKNITSYGVFVDLGGV--DGLIHITDLSWGRINDPHEVVELDQKINVVILDFdEEKKRIALGLK 281
Cdd:cd05686     5 QIFKGEVASVTEYGAFVKIPGCrkQGLVHKSHMSSCRVDDPSEVVDVGEKVWVKVIGR-EMKDKMKLSLS 73
S1_RPS1_repeat_ec6 cd05691
S1_RPS1_repeat_ec6: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
390-458 8.93e-07

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


Pssm-ID: 240196 [Multi-domain]  Cd Length: 73  Bit Score: 46.49  E-value: 8.93e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1276677562 390 AKVRNFTNFGIFVELEEGVDGLIHISDLSWTKKVKHPSEFTqVGADMDVIVLEIDKENRRLSLGHKQLE 458
Cdd:cd05691     6 GKVTEVDAKGATVKLGDGVEGFLRAAELSRDRVEDATERFK-VGDEVEAKITNVDRKNRKISLSIKAKE 73
S1_RpoE cd04460
S1_RpoE: RpoE, S1-like RNA-binding domain. S1-like RNA-binding domains are found in a wide ...
214-309 9.47e-07

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: 47.28  E-value: 9.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 214 QILEGVVKNITSYGVFVDLGGVDGLIHITdlswgRINDphEVVELDQKINVVIldfDEEKKRIalglkqlaphpwdaldp 293
Cdd:cd04460     1 EVVEGEVVEVVDFGAFVRIGPVDGLLHIS-----QIMD--DYISYDPKNKRLI---GEETKRV----------------- 53
                          90
                  ....*....|....*.
gi 1276677562 294 nLKVGDHVKGKVVVMA 309
Cdd:cd04460    54 -LKVGDVVRARIVAVS 68
PLN00207 PLN00207
polyribonucleotide nucleotidyltransferase; Provisional
392-490 1.91e-06

polyribonucleotide nucleotidyltransferase; Provisional


Pssm-ID: 215104 [Multi-domain]  Cd Length: 891  Bit Score: 51.05  E-value: 1.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 392 VRNFTNFGIFVELEEGVDGLIHISDLS--WTKKvkhPSEFTQVGADMDVIVLEIDKENrRLSLGHKQLETNPWDTYESIY 469
Cdd:PLN00207  762 IKSIAPYGAFVEIAPGREGLCHISELSsnWLAK---PEDAFKVGDRIDVKLIEVNDKG-QLRLSRRALLPEANSEKSSQK 837
                          90       100
                  ....*....|....*....|.
gi 1276677562 470 TPGSTHVGKiteSMDKGAVIT 490
Cdd:PLN00207  838 QQGGSTKDK---APQKKYVNT 855
S1_Rrp5_repeat_sc11 cd05707
S1_Rrp5_repeat_sc11: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ...
213-278 2.10e-06

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


Pssm-ID: 240212 [Multi-domain]  Cd Length: 68  Bit Score: 45.36  E-value: 2.10e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1276677562 213 GQILEGVVKNITSYGVFVDLG-GVDGLIHITDLSWGRINDPHEVVELDQKINVVILDFDEEKKRIAL 278
Cdd:cd05707     1 GDVVRGFVKNIANNGVFVTLGrGVDARVRVSELSDSYLKDWKKRFKVGQLVKGKIVSIDPDNGRIEM 67
PRK08563 PRK08563
DNA-directed RNA polymerase subunit E'; Provisional
209-306 2.86e-06

DNA-directed RNA polymerase subunit E'; Provisional


Pssm-ID: 236289 [Multi-domain]  Cd Length: 187  Bit Score: 47.90  E-value: 2.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 209 HLEKGQILEGVVKNITSYGVFVDLGGVDGLIHITdlswgRINDphEVVELDQKINVVILdfdEEKKRIalglkqlaphpw 288
Cdd:PRK08563   78 KPELQEVVEGEVVEVVEFGAFVRIGPVDGLLHIS-----QIMD--DYISYDPKNGRLIG---KESKRV------------ 135
                          90
                  ....*....|....*...
gi 1276677562 289 daldpnLKVGDHVKGKVV 306
Cdd:PRK08563  136 ------LKVGDVVRARIV 147
COG1107 COG1107
Archaea-specific RecJ-like exonuclease, contains DnaJ-type Zn finger domain [Replication, ...
295-384 4.76e-06

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


Pssm-ID: 440724 [Multi-domain]  Cd Length: 626  Bit Score: 49.45  E-value: 4.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 295 LKVGDHVKGKVVVMADYGAFVEIQPGVEGLIHVSEMSwsqhlrsaQEFmKAGDEVeaVVLTLD-RDERKMSLGIKQLKED 373
Cdd:COG1107    37 LEPGRYYRGTVDGVADFGVFVDLNDHVTGLLHRSELD--------QDW-EVGDEV--FVQVKEvRDNGNVDLGWVSIDSY 105
                          90
                  ....*....|.
gi 1276677562 374 PWEAIEAKYPV 384
Cdd:COG1107   106 ETVEVEKELPR 116
Tex COG2183
Transcriptional accessory protein Tex/SPT6 [Transcription];
295-374 5.33e-06

Transcriptional accessory protein Tex/SPT6 [Transcription];


Pssm-ID: 441786 [Multi-domain]  Cd Length: 719  Bit Score: 49.25  E-value: 5.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 295 LKVGDHVKGKVVVMADYGAFVEIqpGV--EGLIHVSEMSwSQHLRSAQEFMKAGDEVEAVVLTLDRDERKMSLGIKQLKE 372
Cdd:COG2183   639 LKPGMILEGTVTNVTDFGAFVDI--GVhqDGLVHISQLS-DRFVKDPREVVKVGDIVKVKVLEVDLKRKRISLSMKLDDE 715

                  ..
gi 1276677562 373 DP 374
Cdd:COG2183   716 AG 717
S1_Rrp5_repeat_hs6_sc5 cd05698
S1_Rrp5_repeat_hs6_sc5: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ...
213-281 8.37e-06

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


Pssm-ID: 240203 [Multi-domain]  Cd Length: 70  Bit Score: 43.75  E-value: 8.37e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 213 GQILEGVVKNITSYGVFVD-LGGVDGLIHITDLSWGRINDPHEVVELDQKINVVILDFDEEKKRIALGLK 281
Cdd:cd05698     1 GLKTHGTIVKVKPNGCIVSfYNNVKGFLPKSELSEAFIKDPEEHFRVGQVVKVKVLSCDPEQQRLLLSCK 70
S1 smart00316
Ribosomal protein S1-like RNA-binding domain;
471-536 9.11e-06

Ribosomal protein S1-like RNA-binding domain;


Pssm-ID: 197648 [Multi-domain]  Cd Length: 72  Bit Score: 43.75  E-value: 9.11e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562  471 PGSTHVGKITESMDKGAVITLNEGGEGFATPKHL----VKEDGSQAQLGEELPFVVIEFVKDTKRIILSH 536
Cdd:smart00316   2 VGDVVEGTVTEITPGGAFVDLGNGVEGLIPISELsdkrVKDPEEVLKVGDEVKVKVLSVDEEKGRIILSL 71
S1_DHX8_helicase cd05684
S1_DHX8_helicase: The N-terminal S1 domain of human ATP-dependent RNA helicase DHX8, a DEAH ...
302-368 1.32e-05

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


Pssm-ID: 240189 [Multi-domain]  Cd Length: 79  Bit Score: 43.38  E-value: 1.32e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 302 KGKVVVMADYGAFVEIQ---PGVEGLIHVSEMSWSQHLRSAQEFMKAGDEVEAVVLTLDRDerKMSLGIK 368
Cdd:cd05684     5 KGKVTSIMDFGCFVQLEglkGRKEGLVHISQLSFEGRVANPSDVVKRGQKVKVKVISIQNG--KISLSMK 72
S1_IF2_alpha cd04452
S1_IF2_alpha: The alpha subunit of translation Initiation Factor 2, S1-like RNA-binding domain. ...
389-456 1.56e-05

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


Pssm-ID: 239899 [Multi-domain]  Cd Length: 76  Bit Score: 43.34  E-value: 1.56e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 389 VAKVRNFTNFGIFVELEE--GVDGLIHISDLSwTKKVKHPSEFTQVGADMDVIVLEIDKENRRLSLGHKQ 456
Cdd:cd04452     8 VVTVKSIADMGAYVSLLEygNIEGMILLSELS-RRRIRSIRKLVKVGRKEVVKVIRVDKEKGYIDLSKKR 76
S1_pNO40 cd05686
S1_pNO40: pNO40 , S1-like RNA-binding domain. pNO40 is a nucleolar protein of unknown function ...
302-365 2.53e-05

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


Pssm-ID: 240191 [Multi-domain]  Cd Length: 73  Bit Score: 42.47  E-value: 2.53e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1276677562 302 KGKVVVMADYGAFVEIqPGV--EGLIHVSEMSwSQHLRSAQEFMKAGDEVEAVVLTLDRDER-KMSL 365
Cdd:cd05686     8 KGEVASVTEYGAFVKI-PGCrkQGLVHKSHMS-SCRVDDPSEVVDVGEKVWVKVIGREMKDKmKLSL 72
PLN00207 PLN00207
polyribonucleotide nucleotidyltransferase; Provisional
204-287 3.04e-05

polyribonucleotide nucleotidyltransferase; Provisional


Pssm-ID: 215104 [Multi-domain]  Cd Length: 891  Bit Score: 47.20  E-value: 3.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 204 KEIISHLEK----GQILEGV-VKNITSYGVFVDLG-GVDGLIHITDLSWGRINDPHEVVELDQKINVVILDFDeEKKRIA 277
Cdd:PLN00207  741 KAIISSLTMvptvGDIYRNCeIKSIAPYGAFVEIApGREGLCHISELSSNWLAKPEDAFKVGDRIDVKLIEVN-DKGQLR 819
                          90
                  ....*....|
gi 1276677562 278 LGLKQLAPHP 287
Cdd:PLN00207  820 LSRRALLPEA 829
nusA PRK09202
transcription elongation factor NusA; Validated
43-106 3.07e-05

transcription elongation factor NusA; Validated


Pssm-ID: 236410 [Multi-domain]  Cd Length: 470  Bit Score: 46.79  E-value: 3.07e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1276677562  43 QEHQVVEGEVISIDKKEVVVNIGyKSDGIIPASEFRYNPELKVGDKVEVYVE--NQEDKSGQLILS 106
Cdd:PRK09202  133 RVGEIITGVVKRVERGNIIVDLG-RAEAILPRKEQIPRENFRPGDRVRAYVYevRKEARGPQIILS 197
PRK00087 PRK00087
bifunctional 4-hydroxy-3-methylbut-2-enyl diphosphate reductase/30S ribosomal protein S1;
400-550 3.24e-05

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


Pssm-ID: 234623 [Multi-domain]  Cd Length: 647  Bit Score: 46.86  E-value: 3.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 400 IFVELEEGVDGLIHISDLSWtKKVKHPSEFTQVGADMDVIVLEIDKENRRLSLGHKQLET-NPWDTYESIYTPGSTHVGK 478
Cdd:PRK00087  318 VFVDVGYKSEGVIPLRELTL-DEISSLKESVKVGDEIEVKVLKLEDEDGYVVLSKKEADReKAWKELEEAFENGEPVKGK 396
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1276677562 479 ITESMdKGAVITLNEGGEGFaTPKHLVK----EDGSQAqLGEELPFVVIEF-VKDTKRIILSHSRTFEEVKEEQARR 550
Cdd:PRK00087  397 VKEVV-KGGLLVDYGGVRAF-LPASHVElgyvEDLSEY-KGQELEVKIIEFnRKRRKKVVLSRKAILEEEKEKKKEE 470
PRK05807 PRK05807
RNA-binding protein S1;
392-456 3.41e-05

RNA-binding protein S1;


Pssm-ID: 235614 [Multi-domain]  Cd Length: 136  Bit Score: 43.97  E-value: 3.41e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1276677562 392 VRNFTNFGIFVELeEGVDGLIHISDLSWTkKVKHPSEFTQVGADMDVIVLEIDkENRRLSLGHKQ 456
Cdd:PRK05807   13 VVNITNFGAFVEV-EGKTGLVHISEVADT-YVKDIREHLKEQDKVKVKVISID-DNGKISLSIKQ 74
VacB COG0557
Exoribonuclease R [Transcription];
396-450 3.72e-05

Exoribonuclease R [Transcription];


Pssm-ID: 440323 [Multi-domain]  Cd Length: 711  Bit Score: 46.64  E-value: 3.72e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1276677562 396 TNFGIFVELEE-GVDGLIHISDL----------------SWTKKVkhpseFtQVGADMDVIVLEIDKENRRL 450
Cdd:COG0557   634 TSFGLFVELDElGVEGLVHVSSLgddyyeyderrqalvgERTGKR-----Y-RLGDRVEVRVVRVDLDRRQI 699
PRK08582 PRK08582
RNA-binding protein S1;
210-287 5.09e-05

RNA-binding protein S1;


Pssm-ID: 236305 [Multi-domain]  Cd Length: 139  Bit Score: 43.48  E-value: 5.09e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1276677562 210 LEKGQILEGVVKNITSYGVFVDL-GGVDGLIHITDLSWGRINDPHEVVELDQKINVVILDFDEEKKrIALGLKQLAPHP 287
Cdd:PRK08582    3 IEVGSKLQGKVTGITNFGAFVELpEGKTGLVHISEVADNYVKDINDHLKVGDEVEVKVLNVEDDGK-IGLSIKKAKDRP 80
S1_RPS1_repeat_ec6 cd05691
S1_RPS1_repeat_ec6: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
46-108 5.53e-05

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


Pssm-ID: 240196 [Multi-domain]  Cd Length: 73  Bit Score: 41.49  E-value: 5.53e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1276677562  46 QVVEGEVISIDKKEVVVNIGYKSDGIIPASEFRYN------PELKVGDKVEVYVENQEDKSGQLILSHK 108
Cdd:cd05691     2 SIVTGKVTEVDAKGATVKLGDGVEGFLRAAELSRDrvedatERFKVGDEVEAKITNVDRKNRKISLSIK 70
S1_Rrp5_repeat_sc10 cd05706
S1_Rrp5_repeat_sc10: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ...
210-281 5.88e-05

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: 41.47  E-value: 5.88e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1276677562 210 LEKGQILEGVVKNITSYGVFVDLGG-VDGLIHITDLswgrINDPHEVVELDQKIN----VVILDFDEEKKRIALGLK 281
Cdd:cd05706     1 LKVGDILPGRVTKVNDRYVLVQLGNkVTGPSFITDA----LDDYSEALPYKFKKNdivrACVLSVDVPNKKIALSLR 73
S1_RNase_R cd04471
S1_RNase_R: RNase R C-terminal S1 domain. RNase R is a processive 3' to 5' exoribonuclease, ...
396-417 6.11e-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: 41.62  E-value: 6.11e-05
                          10        20
                  ....*....|....*....|...
gi 1276677562 396 TNFGIFVELEE-GVDGLIHISDL 417
Cdd:cd04471    13 TSFGLFVELDNlTVEGLVHVSTL 35
S1_Rrp5_repeat_hs5 cd05697
S1_Rrp5_repeat_hs5: Rrp5 is a trans-acting factor important for biogenesis of both the 40S and ...
213-280 6.54e-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: 41.07  E-value: 6.54e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1276677562 213 GQILEGVVKNITSYGVFVDL-GGVDGLIHITDLSWGRINDPHEVVELDQKINVVILDFDEEKKRIALGL 280
Cdd:cd05697     1 GQVVKGTIRKLRPSGIFVKLsDHIKGLVPPMHLADVRLKHPEKKFKPGLKVKCRVLSVEPERKRLVLTL 69
S1_RNase_R cd04471
S1_RNase_R: RNase R C-terminal S1 domain. RNase R is a processive 3' to 5' exoribonuclease, ...
213-244 6.88e-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: 41.62  E-value: 6.88e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1276677562 213 GQILEGVVKNITSYGVFVDLG--GVDGLIHITDL 244
Cdd:cd04471     2 GEEFDGVISGVTSFGLFVELDnlTVEGLVHVSTL 35
RpsA COG0539
Ribosomal protein S1 [Translation, ribosomal structure and biogenesis]; Ribosomal protein S1 ...
294-547 7.78e-05

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: 45.04  E-value: 7.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 294 NLKVGDHVKGKVVVMADYGAFVEIQPGVEGLIHVSEMSWSQhlrsAQEFMKAGDEVEAVVLTLDRDERKMSLGIKQLKED 373
Cdd:COG0539    15 ELKEGDIVKGTVVSIDDDEVLVDIGYKSEGIIPLSEFSDEP----GELEVKVGDEVEVYVEKVEDGEGEIVLSKKKADRE 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 374 P-WEAIEAKYPVGSKHVAKVRNFTNFGIFVELEeGVDGLIHISDLSwTKKVKHPSEFtqvgadmdvivleidkenrrlsl 452
Cdd:COG0539    91 KaWEELEEAFENGEPVEGKVKGVVKGGLIVDIG-GVRAFLPASQVD-VRPVRDLDEY----------------------- 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 453 ghkqletnpwdtyesiytpgsthvgkitesmdkgavitlneggegfatpkhlvkedgsqaqLGEELPFVVIEFVKDTKRI 532
Cdd:COG0539   146 -------------------------------------------------------------VGKTLEFKIIKLDRKRNNV 164
                         250
                  ....*....|....*
gi 1276677562 533 ILSHSRTFEEVKEEQ 547
Cdd:COG0539   165 VVSRRAVLEEEREEK 179
S1 pfam00575
S1 RNA binding domain; The S1 domain occurs in a wide range of RNA associated proteins. It is ...
123-191 1.05e-04

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


Pssm-ID: 425760 [Multi-domain]  Cd Length: 72  Bit Score: 40.73  E-value: 1.05e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1276677562 123 LEADAVIQGYIKSRTKGGMIVDVF-GIEAFLPGSQIDVHPIRDYD--VFVGKTMEFKVVKINQEFRNVVVSH 191
Cdd:pfam00575   1 PEKGDVVEGEVTRVTKGGAFVDLGnGVEGFIPISELSDDHVEDPDevIKVGDEVKVKVLKVDKDRRRIILSI 72
S1_Rrp5_repeat_hs5 cd05697
S1_Rrp5_repeat_hs5: Rrp5 is a trans-acting factor important for biogenesis of both the 40S and ...
390-452 1.11e-04

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


Pssm-ID: 240202 [Multi-domain]  Cd Length: 69  Bit Score: 40.68  E-value: 1.11e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1276677562 390 AKVRNFTNFGIFVELEEGVDGLI---HISDLswtkKVKHPSEFTQVGADMDVIVLEIDKENRRLSL 452
Cdd:cd05697     6 GTIRKLRPSGIFVKLSDHIKGLVppmHLADV----RLKHPEKKFKPGLKVKCRVLSVEPERKRLVL 67
S1_RPS1_repeat_ec1_hs1 cd05687
S1_RPS1_repeat_ec1_hs1: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
298-368 1.47e-04

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


Pssm-ID: 240192 [Multi-domain]  Cd Length: 70  Bit Score: 40.21  E-value: 1.47e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1276677562 298 GDHVKGKVVVMADYGAFVEIQPGVEGLIHVSEMSwSQHLRSAQEFMKAGDEVEAVVLTLDRDERKMSLGIK 368
Cdd:cd05687     1 GDIVKGTVVSVDDDEVLVDIGYKSEGIIPISEFS-DDPIENGEDEVKVGDEVEVYVLRVEDEEGNVVLSKR 70
VacB COG0557
Exoribonuclease R [Transcription];
213-244 2.00e-04

Exoribonuclease R [Transcription];


Pssm-ID: 440323 [Multi-domain]  Cd Length: 711  Bit Score: 44.33  E-value: 2.00e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1276677562 213 GQILEGVVKNITSYGVFVDL--GGVDGLIHITDL 244
Cdd:COG0557   623 GEEFEGVISGVTSFGLFVELdeLGVEGLVHVSSL 656
S1_RPS1_repeat_ec2_hs2 cd04465
S1_RPS1_repeat_ec2_hs2: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
213-278 3.33e-04

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


Pssm-ID: 239911 [Multi-domain]  Cd Length: 67  Bit Score: 38.98  E-value: 3.33e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1276677562 213 GQILEGVVKNITSYGVFVDLGGVDGLIHITDLSWGRINDPHEVVEldQKINVVILDFDEEKKRIAL 278
Cdd:cd04465     1 GEIVEGKVTEKVKGGLIVDIEGVRAFLPASQVDLRPVEDLDEYVG--KELKFKIIEIDRERNNIVL 64
PRK03987 PRK03987
translation initiation factor IF-2 subunit alpha; Validated
297-373 4.36e-04

translation initiation factor IF-2 subunit alpha; Validated


Pssm-ID: 235188 [Multi-domain]  Cd Length: 262  Bit Score: 42.50  E-value: 4.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 297 VGDHVKGKVVVMADYGAFVEIQ--PGVEGLIHVSEMS--WSQHLRsaqEFMKAGDEVEAVVLTLDRDERKMSLGIKQLKE 372
Cdd:PRK03987    8 EGELVVGTVKEVKDFGAFVTLDeyPGKEGFIHISEVAsgWVKNIR---DHVKEGQKVVCKVIRVDPRKGHIDLSLKRVNE 84

                  .
gi 1276677562 373 D 373
Cdd:PRK03987   85 H 85
S1_RNase_R cd04471
S1_RNase_R: RNase R C-terminal S1 domain. RNase R is a processive 3' to 5' exoribonuclease, ...
297-365 6.05e-04

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: 38.92  E-value: 6.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 297 VGDHVKGKVVVMADYGAFVEI-QPGVEGLIHVSEMS--WSQHLRSAQEFM--------KAGDEVEAVVLTLDRDERKMSL 365
Cdd:cd04471     1 VGEEFDGVISGVTSFGLFVELdNLTVEGLVHVSTLGddYYEFDEENHALVgertgkvfRLGDKVKVRVVRVDLDRRKIDF 80
S1_Rrp5_repeat_hs5 cd05697
S1_Rrp5_repeat_hs5: Rrp5 is a trans-acting factor important for biogenesis of both the 40S and ...
298-365 6.84e-04

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


Pssm-ID: 240202 [Multi-domain]  Cd Length: 69  Bit Score: 38.37  E-value: 6.84e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1276677562 298 GDHVKGKVVVMADYGAFVEIQPGVEGLIHVSEMSWSQhLRSAQEFMKAGDEVEAVVLTLDRDERKMSL 365
Cdd:cd05697     1 GQVVKGTIRKLRPSGIFVKLSDHIKGLVPPMHLADVR-LKHPEKKFKPGLKVKCRVLSVEPERKRLVL 67
PRK07252 PRK07252
S1 RNA-binding domain-containing protein;
384-458 7.06e-04

S1 RNA-binding domain-containing protein;


Pssm-ID: 180908 [Multi-domain]  Cd Length: 120  Bit Score: 39.68  E-value: 7.06e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1276677562 384 VGSKHVAKVRNFTNFGIFVELEEGVDGLIHISDLSwTKKVKHPSEFTQVGADMDVIVLEIDKENRRLSLGHKQLE 458
Cdd:PRK07252    3 IGDKLKGTITGIKPYGAFVALENGTTGLIHISEIK-TGFIDNIHQLLKVGEEVLVQVVDFDEYTGKASLSLRTLE 76
S1_RPS1_repeat_ec1_hs1 cd05687
S1_RPS1_repeat_ec1_hs1: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
213-272 1.05e-03

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


Pssm-ID: 240192 [Multi-domain]  Cd Length: 70  Bit Score: 37.89  E-value: 1.05e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1276677562 213 GQILEGVVKNITSYGVFVDLGG-VDGLIHITDLSWGRINDPHEVVELDQKINVVILDFDEE 272
Cdd:cd05687     1 GDIVKGTVVSVDDDEVLVDIGYkSEGIIPISEFSDDPIENGEDEVKVGDEVEVYVLRVEDE 61
S1_Rrp5_repeat_hs8_sc7 cd04461
S1_Rrp5_repeat_hs8_sc7: Rrp5 Homo sapiens S1 repeat 8 (hs8) and Saccharomyces cerevisiae S1 ...
384-452 1.19e-03

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


Pssm-ID: 239908 [Multi-domain]  Cd Length: 83  Bit Score: 37.95  E-value: 1.19e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1276677562 384 VGSKHVAKVRNFTNFGIFVELEEGVDGLIHISDLSwTKKVKHPSEFTQVGADMDVIVLEIDKENRRLSL 452
Cdd:cd04461    14 PGMVVHGYVRNITPYGVFVEFLGGLTGLAPKSYIS-DEFVTDPSFGFKKGQSVTAKVTSVDEEKQRFLL 81
S1_Rrp5_repeat_sc11 cd05707
S1_Rrp5_repeat_sc11: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ...
298-365 1.30e-03

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


Pssm-ID: 240212 [Multi-domain]  Cd Length: 68  Bit Score: 37.66  E-value: 1.30e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1276677562 298 GDHVKGKVVVMADYGAFVEIQPGVEGLIHVSEMSWSqHLRSAQEFMKAGDEVEAVVLTLDRDERKMSL 365
Cdd:cd05707     1 GDVVRGFVKNIANNGVFVTLGRGVDARVRVSELSDS-YLKDWKKRFKVGQLVKGKIVSIDPDNGRIEM 67
S1_RecJ_like cd04473
S1_RecJ_like: The S1 domain of the archaea-specific RecJ-like exonuclease. The function of ...
384-453 1.47e-03

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


Pssm-ID: 239919 [Multi-domain]  Cd Length: 77  Bit Score: 37.59  E-value: 1.47e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 384 VGSKHVAKVRNFTNFGIFVELEEGVDGLIHISDLSWTKKvkhpseftqVGADMDVIVLEIdKENRRLSLG 453
Cdd:cd04473    16 VGKLYKGKVNGVAKYGVFVDLNDHVRGLIHRSNLLRDYE---------VGDEVIVQVTDI-PENGNIDLI 75
S1_Rrp5_repeat_hs8_sc7 cd04461
S1_Rrp5_repeat_hs8_sc7: Rrp5 Homo sapiens S1 repeat 8 (hs8) and Saccharomyces cerevisiae S1 ...
295-365 1.74e-03

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


Pssm-ID: 239908 [Multi-domain]  Cd Length: 83  Bit Score: 37.57  E-value: 1.74e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1276677562 295 LKVGDHVKGKVVVMADYGAFVEIQPGVEGLIHVSEMSwSQHLRSAQEFMKAGDEVEAVVLTLDRDERKMSL 365
Cdd:cd04461    12 LKPGMVVHGYVRNITPYGVFVEFLGGLTGLAPKSYIS-DEFVTDPSFGFKKGQSVTAKVTSVDEEKQRFLL 81
PRK07400 PRK07400
30S ribosomal protein S1; Reviewed
422-544 1.77e-03

30S ribosomal protein S1; Reviewed


Pssm-ID: 180960 [Multi-domain]  Cd Length: 318  Bit Score: 40.94  E-value: 1.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 422 KVKHPSEFTQVGADMDVIVLEIDKENRRLSLGHKQLE-TNPWDTYESIYTPGSTHVGKITESMDKGAVITLnEGGEGFAT 500
Cdd:PRK07400   68 RVEGPEEVLQPNETREFFILSDENEDGQLTLSIRRIEyMRAWERVRQLQKEDATVRSEVFATNRGGALVRI-EGLRGFIP 146
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1276677562 501 PKHLVKEDGSQAQLGEELPFVVIEFVKDTKRIILSHSRTFEEVK 544
Cdd:PRK07400  147 GSHISTRKPKEELVGEELPLKFLEVDEERNRLVLSHRRALVERK 190
S1_like cd00164
S1_like: Ribosomal protein S1-like RNA-binding domain. Found in a wide variety of ...
48-106 1.81e-03

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


Pssm-ID: 238094 [Multi-domain]  Cd Length: 65  Bit Score: 36.97  E-value: 1.81e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1276677562  48 VEGEVISIDKKEVVVNIGYKSDGIIPASEFRY------NPELKVGDKVEVYVENQEDKSGQLILS 106
Cdd:cd00164     1 VTGKVVSITKFGVFVELEDGVEGLVHISELSDkfvkdpSEVFKVGDEVEVKVLEVDPEKGRISLS 65
S1_RecJ_like cd04473
S1_RecJ_like: The S1 domain of the archaea-specific RecJ-like exonuclease. The function of ...
210-240 2.12e-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: 2.12e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1276677562 210 LEKGQILEGVVKNITSYGVFVDLGG-VDGLIH 240
Cdd:cd04473    14 LEVGKLYKGKVNGVAKYGVFVDLNDhVRGLIH 45
VacB COG0557
Exoribonuclease R [Transcription];
296-363 2.39e-03

Exoribonuclease R [Transcription];


Pssm-ID: 440323 [Multi-domain]  Cd Length: 711  Bit Score: 40.86  E-value: 2.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562 296 KVGDHVKGKVVVMADYGAFVEI-QPGVEGLIHVSEM--------SWSQHL---RSAQEFmKAGDEVEAVVLTLDRDERKM 363
Cdd:COG0557   621 RVGEEFEGVISGVTSFGLFVELdELGVEGLVHVSSLgddyyeydERRQALvgeRTGKRY-RLGDRVEVRVVRVDLDRRQI 699
S1_Rrp5_repeat_sc10 cd05706
S1_Rrp5_repeat_sc10: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ...
384-452 4.74e-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: 36.08  E-value: 4.74e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1276677562 384 VGSKHVAKVRNFTNFGIFVELEEGVDGLIHISDLSWTKKVKHPSEFTQvGADMDVIVLEIDKENRRLSL 452
Cdd:cd05706     3 VGDILPGRVTKVNDRYVLVQLGNKVTGPSFITDALDDYSEALPYKFKK-NDIVRACVLSVDVPNKKIAL 70
rpsA TIGR00717
ribosomal protein S1; This model describes ribosomal protein S1, RpsA. This protein is found ...
26-106 4.80e-03

ribosomal protein S1; This model describes ribosomal protein S1, RpsA. This protein is found in most bacterial genomes in a single copy, but is not present in the Mycoplasmas. It is heterogeneous with respect to the number of repeats of the S1 RNA binding domain described by pfam00575: six repeats in E. coli and most other bacteria, four in Bacillus subtilis and some other species. rpsA is an essential gene in E. coli but not in B. subtilis. It is associated with the cytidylate kinase gene cmk in many species, and fused to it in Treponema pallidum. RpsA is proposed (Medline:97323001) to assist in mRNA degradation. This model provides trusted hits to most long form (6 repeat) examples of RpsA. Among homologs with only four repeats are some to which other (perhaps secondary) functions have been assigned. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 273232 [Multi-domain]  Cd Length: 516  Bit Score: 39.72  E-value: 4.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276677562  26 GDKEELTKAYDNTLNKIQEHQVVEGEVISIDKKEVVVNIGYKSDGIIPASEFRYNP------ELKVGDKVEVYVENQEDK 99
Cdd:TIGR00717 428 GVKQLTENPWEKFAAKYKVGSVVKGKVTEIKDFGAFVELPGGVEGLIRNSELSENRdedktdEIKVGDEVEAKVVDIDKK 507

                  ....*..
gi 1276677562 100 SGQLILS 106
Cdd:TIGR00717 508 NRKVSLS 514
S1_Rrp5_repeat_hs12_sc9 cd05703
S1_Rrp5_repeat_hs12_sc9: Rrp5 is a trans-acting factor important for biogenesis of both the ...
385-452 6.47e-03

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: 35.63  E-value: 6.47e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1276677562 385 GSKHVAKVRNFTNFGIFVELEEGVDGLIHISDLSWTKKV-KHPSEFTQVGADMDVIVLEIDKENRRLSL 452
Cdd:cd05703     1 GQEVTGFVNNVSKEFVWLTISPDVKGRIPLLDLSDDVSVlEHPEKKFPIGQALKAKVVGVDKEHKLLRL 69
S1_RPS1_repeat_ec2_hs2 cd04465
S1_RPS1_repeat_ec2_hs2: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
390-455 8.46e-03

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


Pssm-ID: 239911 [Multi-domain]  Cd Length: 67  Bit Score: 35.13  E-value: 8.46e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1276677562 390 AKVRNFTNFGIFVELEeGVDGLIHISDLSwTKKVKHPSEFtqVGADMDVIVLEIDKENRRLSLGHK 455
Cdd:cd04465     6 GKVTEKVKGGLIVDIE-GVRAFLPASQVD-LRPVEDLDEY--VGKELKFKIIEIDRERNNIVLSRR 67
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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