NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|374680314|gb|AEZ60604|]
View 

bifunctional cytidylate kinase/ribosomal protein S1 [Treponema pallidum subsp. pallidum DAL-1]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PRK12269 super family cl30919
bifunctional cytidylate kinase/ribosomal protein S1; Provisional
1-863 0e+00

bifunctional cytidylate kinase/ribosomal protein S1; Provisional


The actual alignment was detected with superfamily member PRK12269:

Pssm-ID: 105491 [Multi-domain]  Cd Length: 863  Bit Score: 1820.09  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314   1 MHGGGERERSFVHPRTRCVAVRARTVLQCRPMGTVIIALDGPAGSGKSSVCRLLASRLGAQCLNTGSFYRAFTLAALRRV 80
Cdd:PRK12269   1 MHGGGERERSFVHPRTRCVAVRARTVLQCRPMGTVIIALDGPAGSGKSSVCRLLASRLGAQCLNTGSFYRAFTLAALRRV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314  81 SELAVQACSPSPDPDAAVGCAAVPHATNLDTSYAPLTAQKKVALFDEAYWVSFARTVALSYRAGVMYVGEENVESLLRSD 160
Cdd:PRK12269  81 SELAVQACSPSPDPDAAVGCAAVPHATNLDTSYAPLTAQKKVALFDEAYWVSFARTVALSYRAGVMYVGEENVESLLRSD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 161 EVESAVSYFAAMPAIRAIMTGKIRSAVCGARVVCEGRDLTTVVFVDADLKCYLDASIEARVARRWAQGTSRLSKQELEQR 240
Cdd:PRK12269 161 EVESAVSYFAAMPAIRAIMTGKIRSAVCGARVVCEGRDLTTVVFVDADLKCYLDASIEARVARRWAQGTSRLSKQELEQR 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 241 MRARDAHDRARTVGGLRCAPDALYVDTSCLTIEEVCERIAREAHRRALWGGERSVENQEGKGTPLVPRQLQERYSFEAPE 320
Cdd:PRK12269 241 MRARDAHDRARTVGGLRCAPDALYVDTSCLTIEEVCERIAREAHRRALWGGERSVENQEGKGTPLVPRQLQERYSFEAPE 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 321 PGSVRMGTVVQVNAGTVFVDIGGKSEGRVPVEEFEAPPKAGDGVRVYVERVTPYGPELSKTKADRLGLKVKLRDAERDGT 400
Cdd:PRK12269 321 PGSVRMGTVVQVNAGTVFVDIGGKSEGRVPVEEFEAPPKAGDGVRVYVERVTPYGPELSKTKADRLGLKVKLRDAERDGT 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 401 PVEGRIVRLTEKKSGFEVDLGAGMMAFLPISQSDCQKVDAPESLIGLTSKFYIERISQSKQHRGNDNIVINRRRYLEERA 480
Cdd:PRK12269 401 PVEGRIVRLTEKKSGFEVDLGAGMMAFLPISQSDCQKVDAPESLIGLTSKFYIERISQSKQHRGNDNIVINRRRYLEERA 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 481 RQAREEFFNSVHIEDSVSGVVKSFTSFGAFIDLGGFDGLLHVNDMSWGHVARPREFVKKGQTIELKVIRLDQAEKRINLS 560
Cdd:PRK12269 481 RQAREEFFNSVHIEDSVSGVVKSFTSFGAFIDLGGFDGLLHVNDMSWGHVARPREFVKKGQTIELKVIRLDQAEKRINLS 560
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 561 LKHFQPDPWLEFENKFGVNDVVKGRVTKIADFGAFIELAEGIEGLAHISEFSWVKKTSKPSDMVKIGDEVECMILGYDIQ 640
Cdd:PRK12269 561 LKHFQPDPWLEFENKFGVNDVVKGRVTKIADFGAFIELAEGIEGLAHISEFSWVKKTSKPSDMVKIGDEVECMILGYDIQ 640
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 641 AGRVSLGLKQVTANPWEEIEARYPVGARFTRRIVKVTNAGAFIEMEEGIDGFLHVDDLSWVKRTRPADHELEVGKEIECM 720
Cdd:PRK12269 641 AGRVSLGLKQVTANPWEEIEARYPVGARFTRRIVKVTNAGAFIEMEEGIDGFLHVDDLSWVKRTRPADHELEVGKEIECM 720
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 721 VIECDPQARRIRLGVKQLSDNPWQVFANAYGVGSTVEGEVSSVTDFGIFVRVPGGVEGLVRKQHLVENRDGDPGEALRKY 800
Cdd:PRK12269 721 VIECDPQARRIRLGVKQLSDNPWQVFANAYGVGSTVEGEVSSVTDFGIFVRVPGGVEGLVRKQHLVENRDGDPGEALRKY 800
                        810       820       830       840       850       860
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 374680314 801 AVGDRVKAVIVDMNVKDRKVAFSVRDYQRKVQRDELSRYMSAPRGEDEGSFTLGDLMRQTSGK 863
Cdd:PRK12269 801 AVGDRVKAVIVDMNVKDRKVAFSVRDYQRKVQRDELSRYMSAPRGEDEGSFTLGDLMRQTSGK 863
 
Name Accession Description Interval E-value
PRK12269 PRK12269
bifunctional cytidylate kinase/ribosomal protein S1; Provisional
1-863 0e+00

bifunctional cytidylate kinase/ribosomal protein S1; Provisional


Pssm-ID: 105491 [Multi-domain]  Cd Length: 863  Bit Score: 1820.09  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314   1 MHGGGERERSFVHPRTRCVAVRARTVLQCRPMGTVIIALDGPAGSGKSSVCRLLASRLGAQCLNTGSFYRAFTLAALRRV 80
Cdd:PRK12269   1 MHGGGERERSFVHPRTRCVAVRARTVLQCRPMGTVIIALDGPAGSGKSSVCRLLASRLGAQCLNTGSFYRAFTLAALRRV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314  81 SELAVQACSPSPDPDAAVGCAAVPHATNLDTSYAPLTAQKKVALFDEAYWVSFARTVALSYRAGVMYVGEENVESLLRSD 160
Cdd:PRK12269  81 SELAVQACSPSPDPDAAVGCAAVPHATNLDTSYAPLTAQKKVALFDEAYWVSFARTVALSYRAGVMYVGEENVESLLRSD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 161 EVESAVSYFAAMPAIRAIMTGKIRSAVCGARVVCEGRDLTTVVFVDADLKCYLDASIEARVARRWAQGTSRLSKQELEQR 240
Cdd:PRK12269 161 EVESAVSYFAAMPAIRAIMTGKIRSAVCGARVVCEGRDLTTVVFVDADLKCYLDASIEARVARRWAQGTSRLSKQELEQR 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 241 MRARDAHDRARTVGGLRCAPDALYVDTSCLTIEEVCERIAREAHRRALWGGERSVENQEGKGTPLVPRQLQERYSFEAPE 320
Cdd:PRK12269 241 MRARDAHDRARTVGGLRCAPDALYVDTSCLTIEEVCERIAREAHRRALWGGERSVENQEGKGTPLVPRQLQERYSFEAPE 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 321 PGSVRMGTVVQVNAGTVFVDIGGKSEGRVPVEEFEAPPKAGDGVRVYVERVTPYGPELSKTKADRLGLKVKLRDAERDGT 400
Cdd:PRK12269 321 PGSVRMGTVVQVNAGTVFVDIGGKSEGRVPVEEFEAPPKAGDGVRVYVERVTPYGPELSKTKADRLGLKVKLRDAERDGT 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 401 PVEGRIVRLTEKKSGFEVDLGAGMMAFLPISQSDCQKVDAPESLIGLTSKFYIERISQSKQHRGNDNIVINRRRYLEERA 480
Cdd:PRK12269 401 PVEGRIVRLTEKKSGFEVDLGAGMMAFLPISQSDCQKVDAPESLIGLTSKFYIERISQSKQHRGNDNIVINRRRYLEERA 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 481 RQAREEFFNSVHIEDSVSGVVKSFTSFGAFIDLGGFDGLLHVNDMSWGHVARPREFVKKGQTIELKVIRLDQAEKRINLS 560
Cdd:PRK12269 481 RQAREEFFNSVHIEDSVSGVVKSFTSFGAFIDLGGFDGLLHVNDMSWGHVARPREFVKKGQTIELKVIRLDQAEKRINLS 560
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 561 LKHFQPDPWLEFENKFGVNDVVKGRVTKIADFGAFIELAEGIEGLAHISEFSWVKKTSKPSDMVKIGDEVECMILGYDIQ 640
Cdd:PRK12269 561 LKHFQPDPWLEFENKFGVNDVVKGRVTKIADFGAFIELAEGIEGLAHISEFSWVKKTSKPSDMVKIGDEVECMILGYDIQ 640
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 641 AGRVSLGLKQVTANPWEEIEARYPVGARFTRRIVKVTNAGAFIEMEEGIDGFLHVDDLSWVKRTRPADHELEVGKEIECM 720
Cdd:PRK12269 641 AGRVSLGLKQVTANPWEEIEARYPVGARFTRRIVKVTNAGAFIEMEEGIDGFLHVDDLSWVKRTRPADHELEVGKEIECM 720
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 721 VIECDPQARRIRLGVKQLSDNPWQVFANAYGVGSTVEGEVSSVTDFGIFVRVPGGVEGLVRKQHLVENRDGDPGEALRKY 800
Cdd:PRK12269 721 VIECDPQARRIRLGVKQLSDNPWQVFANAYGVGSTVEGEVSSVTDFGIFVRVPGGVEGLVRKQHLVENRDGDPGEALRKY 800
                        810       820       830       840       850       860
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 374680314 801 AVGDRVKAVIVDMNVKDRKVAFSVRDYQRKVQRDELSRYMSAPRGEDEGSFTLGDLMRQTSGK 863
Cdd:PRK12269 801 AVGDRVKAVIVDMNVKDRKVAFSVRDYQRKVQRDELSRYMSAPRGEDEGSFTLGDLMRQTSGK 863
rpsA TIGR00717
ribosomal protein S1; This model describes ribosomal protein S1, RpsA. This protein is found ...
304-825 0e+00

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


Pssm-ID: 273232 [Multi-domain]  Cd Length: 516  Bit Score: 773.91  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314  304 PLVPRQLQERYSFEAPEPGSVRMGTVVQVNAGTVFVDIGGKSEGRVPVEEFEAPP---KAGDGVRVYVERVTP-YG-PEL 378
Cdd:TIGR00717   1 ESFAQLLEESLKTEETRPGSIVKGTVVAINKDTVFVDVGLKSEGRIPKEEFLDAPleiQVGDEVEVYLDRVEDrFGeTVL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314  379 SKTKADRLGLKVKLRDAERDGTPVEGRIVRLTekKSGFEVDLGaGMMAFLPISQSDCQKVDAPESLIGLTSKFYIERISQ 458
Cdd:TIGR00717  81 SREKAQRHELWIKLEKAYEEGSIVEGKIVGKV--KGGFIVDLN-GVEAFLPGSQVDVKPIKDLDSLIGKTLKFKIIKLDQ 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314  459 SkqhrgNDNIVINRRRYLEERARQAREEFFNSVHIEDSVSGVVKSFTSFGAFIDLGGFDGLLHVNDMSWGHVARPREFVK 538
Cdd:TIGR00717 158 K-----RNNIVVSRRAYLEEERSQAREELLENLKEGDVVKGVVKNITDFGAFVDLGGVDGLLHITDMSWKRVKHPSEYVK 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314  539 KGQTIELKVIRLDQAEKRINLSLKHFQPDPWLEFENKFGVNDVVKGRVTKIADFGAFIELAEGIEGLAHISEFSWVKKTS 618
Cdd:TIGR00717 233 VGQEVKVKVIKFDKEKGRISLSLKQLGEDPWEAIEKKFPVGDKITGRVTNLTDYGVFVEIEEGIEGLVHVSEMSWVKKNS 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314  619 KPSDMVKIGDEVECMILGYDIQAGRVSLGLKQVTANPWEEIEARYPVGARFTRRIVKVTNAGAFIEMEEGIDGFLHVDDL 698
Cdd:TIGR00717 313 HPSKVVKKGDEVEVMILDIDPERRRLSLGLKQCKANPWEQFEEKHPVGDRVTGKIKKITDFGAFVELEGGIDGLIHLSDI 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314  699 SWVKRTRPADHELEVGKEIECMVIECDPQARRIRLGVKQLSDNPWQVFANAYGVGSTVEGEVSSVTDFGIFVRVPGGVEG 778
Cdd:TIGR00717 393 SWDKDGREADHLYKKGDEIEAVVLAVDKEKKRISLGVKQLTENPWEKFAAKYKVGSVVKGKVTEIKDFGAFVELPGGVEG 472
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*..
gi 374680314  779 LVRKQHLVENRDGDpgeALRKYAVGDRVKAVIVDMNVKDRKVAFSVR 825
Cdd:TIGR00717 473 LIRNSELSENRDED---KTDEIKVGDEVEAKVVDIDKKNRKVSLSVK 516
RpsA COG0539
Ribosomal protein S1 [Translation, ribosomal structure and biogenesis]; Ribosomal protein S1 ...
315-651 5.27e-138

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: 413.67  E-value: 5.27e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 315 SFEAPEPGSVRMGTVVQVNAGTVFVDIGGKSEGRVPVEEF-----EAPPKAGDGVRVYVERVTPYGPE--LSKTKADRLG 387
Cdd:COG0539   12 SLKELKEGDIVKGTVVSIDDDEVLVDIGYKSEGIIPLSEFsdepgELEVKVGDEVEVYVEKVEDGEGEivLSKKKADREK 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 388 LKVKLRDAERDGTPVEGRIVRLTekKSGFEVDLGaGMMAFLPISQSDCQKVDAPESLIGLTSKFYIERISQSKQhrgndN 467
Cdd:COG0539   92 AWEELEEAFENGEPVEGKVKGVV--KGGLIVDIG-GVRAFLPASQVDVRPVRDLDEYVGKTLEFKIIKLDRKRN-----N 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 468 IVINRRRYLEERARQAREEFFNSVHIEDSVSGVVKSFTSFGAFIDLGGFDGLLHVNDMSWGHVARPREFVKKGQTIELKV 547
Cdd:COG0539  164 VVVSRRAVLEEEREEKREELLEKLEEGDVVEGTVKNITDFGAFVDLGGVDGLLHISEISWGRVKHPSEVLKVGDEVEVKV 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 548 IRLDQAEKRINLSLKHFQPDPWLEFENKFGVNDVVKGRVTKIADFGAFIELAEGIEGLAHISEFSWVKKTSKPSDMVKIG 627
Cdd:COG0539  244 LKIDREKERISLSLKQLQPDPWENIAEKYPVGDVVKGKVTRLTDFGAFVELEPGVEGLVHISEMSWTKRVAHPSDVVKVG 323
                        330       340
                 ....*....|....*....|....
gi 374680314 628 DEVECMILGYDIQAGRVSLGLKQV 651
Cdd:COG0539  324 DEVEVKVLDIDPEERRISLSIKQL 347
Cytidylate_kin pfam02224
Cytidylate kinase; Cytidylate kinase EC:2.7.4.14 catalyzes the phosphorylation of cytidine 5 ...
37-285 3.89e-92

Cytidylate kinase; Cytidylate kinase EC:2.7.4.14 catalyzes the phosphorylation of cytidine 5'-monophosphate (dCMP) to cytidine 5'-diphosphate (dCDP) in the presence of ATP or GTP.


Pssm-ID: 280401 [Multi-domain]  Cd Length: 211  Bit Score: 289.20  E-value: 3.89e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314   37 IALDGPAGSGKSSVCRLLASRLGAQCLNTGSFYRAFTLAALRRvselavqacspspdpdaavgcaavphatnldtsyapl 116
Cdd:pfam02224   1 IAIDGPSGSGKSTVARILARKLGYKYLDTGAMYRALALAALRQ------------------------------------- 43
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314  117 taqkKVALFDEAYWVSFARTVALSYRAGVMYVGEENVESLLRSDEVESAVSYFAAMPAIRAIMTGKIRSAVCGARVVCEG 196
Cdd:pfam02224  44 ----KVDLTDEDALAELASEVDISFGHTEVFLNGEDVSSEIRTDEVAQAASQVAAIPAVRARLNKLQRQLAKNGNIVMEG 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314  197 RDLTTVVFVDADLKCYLDASIEARVARRWAQ----GTSrLSKQELEQRMRARDAHDRARTVGGLRCAPDALYVDTSCLTI 272
Cdd:pfam02224 120 RDIGTVVFPDAEVKIFLTASPEERAKRRYKQlqakGLS-VDFEELLAEIKRRDKRDSERAVGPLKPAPDALIIDTSKLTI 198
                         250
                  ....*....|...
gi 374680314  273 EEVCERIAREAHR 285
Cdd:pfam02224 199 EEVVEKILELIKQ 211
CMPK cd02020
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ...
36-268 1.77e-42

Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine monophosphate (CMP) to produce cytidine diphosphate (CDP), using ATP as the preferred phosphoryl donor.


Pssm-ID: 238978 [Multi-domain]  Cd Length: 147  Bit Score: 151.49  E-value: 1.77e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314  36 IIALDGPAGSGKSSVCRLLASRLGAQCLNTGsfyraftlaalrrvselavqacspspdpdaavgcaavphatnldtsyap 115
Cdd:cd02020    1 IIAIDGPAGSGKSTVAKLLAKKLGLPYLDTG------------------------------------------------- 31
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 116 ltaqkkvalfdeaywvsfartvalsyragvmyvgeenvesLLRSDEVESAVSYFAAMPAIRAIMTGKIRSAVCGARVVCE 195
Cdd:cd02020   32 ----------------------------------------GIRTEEVGKLASEVAAIPEVRKALDERQRELAKKPGIVLE 71
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 374680314 196 GRDLTTVVFVDADLKCYLDASIEARVARRWAQ---GTSRLSKQELEQRMRARDAHDRARTVGGLRCAPDALYVDTS 268
Cdd:cd02020   72 GRDIGTVVFPDADLKIFLTASPEVRAKRRAKQlqaKGEGVDLEEILAEIIERDERDSTRYVAPLKLAEDAIVIDTS 147
S1 smart00316
Ribosomal protein S1-like RNA-binding domain;
578-649 2.21e-20

Ribosomal protein S1-like RNA-binding domain;


Pssm-ID: 197648 [Multi-domain]  Cd Length: 72  Bit Score: 85.73  E-value: 2.21e-20
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 374680314   578 VNDVVKGRVTKIADFGAFIELAEGIEGLAHISEFSWvKKTSKPSDMVKIGDEVECMILGYDIQAGRVSLGLK 649
Cdd:smart00316   2 VGDVVEGTVTEITPGGAFVDLGNGVEGLIPISELSD-KRVKDPEEVLKVGDEVKVKVLSVDEEKGRIILSLK 72
S1_dom_CvfD NF040579
CvfD/Ygs/GSP13 family RNA-binding post-transcriptional regulator; CvfD, Ygs, and GSP13 form a ...
580-675 7.28e-15

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


Pssm-ID: 468553 [Multi-domain]  Cd Length: 113  Bit Score: 71.30  E-value: 7.28e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 580 DVVKGRVTKIADFGAFIELAEGIEGLAHISEFS--WVKKTskpSDMVKIGDEVECMILGYDIQAGRVSLGLKQVTANPwe 657
Cdd:NF040579   5 DIVEGKVTGIQPYGAFVALDEHTQGLIHISEIKhgYVKDI---NDFLKVGQEVKVKVLDIDEYTGKISLSLRALEEAP-- 79
                         90
                 ....*....|....*...
gi 374680314 658 eIEARYPVGARFTRRIVK 675
Cdd:NF040579  80 -EKHRKRRKHRWTNKRLK 96
 
Name Accession Description Interval E-value
PRK12269 PRK12269
bifunctional cytidylate kinase/ribosomal protein S1; Provisional
1-863 0e+00

bifunctional cytidylate kinase/ribosomal protein S1; Provisional


Pssm-ID: 105491 [Multi-domain]  Cd Length: 863  Bit Score: 1820.09  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314   1 MHGGGERERSFVHPRTRCVAVRARTVLQCRPMGTVIIALDGPAGSGKSSVCRLLASRLGAQCLNTGSFYRAFTLAALRRV 80
Cdd:PRK12269   1 MHGGGERERSFVHPRTRCVAVRARTVLQCRPMGTVIIALDGPAGSGKSSVCRLLASRLGAQCLNTGSFYRAFTLAALRRV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314  81 SELAVQACSPSPDPDAAVGCAAVPHATNLDTSYAPLTAQKKVALFDEAYWVSFARTVALSYRAGVMYVGEENVESLLRSD 160
Cdd:PRK12269  81 SELAVQACSPSPDPDAAVGCAAVPHATNLDTSYAPLTAQKKVALFDEAYWVSFARTVALSYRAGVMYVGEENVESLLRSD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 161 EVESAVSYFAAMPAIRAIMTGKIRSAVCGARVVCEGRDLTTVVFVDADLKCYLDASIEARVARRWAQGTSRLSKQELEQR 240
Cdd:PRK12269 161 EVESAVSYFAAMPAIRAIMTGKIRSAVCGARVVCEGRDLTTVVFVDADLKCYLDASIEARVARRWAQGTSRLSKQELEQR 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 241 MRARDAHDRARTVGGLRCAPDALYVDTSCLTIEEVCERIAREAHRRALWGGERSVENQEGKGTPLVPRQLQERYSFEAPE 320
Cdd:PRK12269 241 MRARDAHDRARTVGGLRCAPDALYVDTSCLTIEEVCERIAREAHRRALWGGERSVENQEGKGTPLVPRQLQERYSFEAPE 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 321 PGSVRMGTVVQVNAGTVFVDIGGKSEGRVPVEEFEAPPKAGDGVRVYVERVTPYGPELSKTKADRLGLKVKLRDAERDGT 400
Cdd:PRK12269 321 PGSVRMGTVVQVNAGTVFVDIGGKSEGRVPVEEFEAPPKAGDGVRVYVERVTPYGPELSKTKADRLGLKVKLRDAERDGT 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 401 PVEGRIVRLTEKKSGFEVDLGAGMMAFLPISQSDCQKVDAPESLIGLTSKFYIERISQSKQHRGNDNIVINRRRYLEERA 480
Cdd:PRK12269 401 PVEGRIVRLTEKKSGFEVDLGAGMMAFLPISQSDCQKVDAPESLIGLTSKFYIERISQSKQHRGNDNIVINRRRYLEERA 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 481 RQAREEFFNSVHIEDSVSGVVKSFTSFGAFIDLGGFDGLLHVNDMSWGHVARPREFVKKGQTIELKVIRLDQAEKRINLS 560
Cdd:PRK12269 481 RQAREEFFNSVHIEDSVSGVVKSFTSFGAFIDLGGFDGLLHVNDMSWGHVARPREFVKKGQTIELKVIRLDQAEKRINLS 560
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 561 LKHFQPDPWLEFENKFGVNDVVKGRVTKIADFGAFIELAEGIEGLAHISEFSWVKKTSKPSDMVKIGDEVECMILGYDIQ 640
Cdd:PRK12269 561 LKHFQPDPWLEFENKFGVNDVVKGRVTKIADFGAFIELAEGIEGLAHISEFSWVKKTSKPSDMVKIGDEVECMILGYDIQ 640
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 641 AGRVSLGLKQVTANPWEEIEARYPVGARFTRRIVKVTNAGAFIEMEEGIDGFLHVDDLSWVKRTRPADHELEVGKEIECM 720
Cdd:PRK12269 641 AGRVSLGLKQVTANPWEEIEARYPVGARFTRRIVKVTNAGAFIEMEEGIDGFLHVDDLSWVKRTRPADHELEVGKEIECM 720
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 721 VIECDPQARRIRLGVKQLSDNPWQVFANAYGVGSTVEGEVSSVTDFGIFVRVPGGVEGLVRKQHLVENRDGDPGEALRKY 800
Cdd:PRK12269 721 VIECDPQARRIRLGVKQLSDNPWQVFANAYGVGSTVEGEVSSVTDFGIFVRVPGGVEGLVRKQHLVENRDGDPGEALRKY 800
                        810       820       830       840       850       860
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 374680314 801 AVGDRVKAVIVDMNVKDRKVAFSVRDYQRKVQRDELSRYMSAPRGEDEGSFTLGDLMRQTSGK 863
Cdd:PRK12269 801 AVGDRVKAVIVDMNVKDRKVAFSVRDYQRKVQRDELSRYMSAPRGEDEGSFTLGDLMRQTSGK 863
rpsA TIGR00717
ribosomal protein S1; This model describes ribosomal protein S1, RpsA. This protein is found ...
304-825 0e+00

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


Pssm-ID: 273232 [Multi-domain]  Cd Length: 516  Bit Score: 773.91  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314  304 PLVPRQLQERYSFEAPEPGSVRMGTVVQVNAGTVFVDIGGKSEGRVPVEEFEAPP---KAGDGVRVYVERVTP-YG-PEL 378
Cdd:TIGR00717   1 ESFAQLLEESLKTEETRPGSIVKGTVVAINKDTVFVDVGLKSEGRIPKEEFLDAPleiQVGDEVEVYLDRVEDrFGeTVL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314  379 SKTKADRLGLKVKLRDAERDGTPVEGRIVRLTekKSGFEVDLGaGMMAFLPISQSDCQKVDAPESLIGLTSKFYIERISQ 458
Cdd:TIGR00717  81 SREKAQRHELWIKLEKAYEEGSIVEGKIVGKV--KGGFIVDLN-GVEAFLPGSQVDVKPIKDLDSLIGKTLKFKIIKLDQ 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314  459 SkqhrgNDNIVINRRRYLEERARQAREEFFNSVHIEDSVSGVVKSFTSFGAFIDLGGFDGLLHVNDMSWGHVARPREFVK 538
Cdd:TIGR00717 158 K-----RNNIVVSRRAYLEEERSQAREELLENLKEGDVVKGVVKNITDFGAFVDLGGVDGLLHITDMSWKRVKHPSEYVK 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314  539 KGQTIELKVIRLDQAEKRINLSLKHFQPDPWLEFENKFGVNDVVKGRVTKIADFGAFIELAEGIEGLAHISEFSWVKKTS 618
Cdd:TIGR00717 233 VGQEVKVKVIKFDKEKGRISLSLKQLGEDPWEAIEKKFPVGDKITGRVTNLTDYGVFVEIEEGIEGLVHVSEMSWVKKNS 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314  619 KPSDMVKIGDEVECMILGYDIQAGRVSLGLKQVTANPWEEIEARYPVGARFTRRIVKVTNAGAFIEMEEGIDGFLHVDDL 698
Cdd:TIGR00717 313 HPSKVVKKGDEVEVMILDIDPERRRLSLGLKQCKANPWEQFEEKHPVGDRVTGKIKKITDFGAFVELEGGIDGLIHLSDI 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314  699 SWVKRTRPADHELEVGKEIECMVIECDPQARRIRLGVKQLSDNPWQVFANAYGVGSTVEGEVSSVTDFGIFVRVPGGVEG 778
Cdd:TIGR00717 393 SWDKDGREADHLYKKGDEIEAVVLAVDKEKKRISLGVKQLTENPWEKFAAKYKVGSVVKGKVTEIKDFGAFVELPGGVEG 472
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*..
gi 374680314  779 LVRKQHLVENRDGDpgeALRKYAVGDRVKAVIVDMNVKDRKVAFSVR 825
Cdd:TIGR00717 473 LIRNSELSENRDED---KTDEIKVGDEVEAKVVDIDKKNRKVSLSVK 516
rpsA PRK06299
30S ribosomal protein S1; Reviewed
310-859 0e+00

30S ribosomal protein S1; Reviewed


Pssm-ID: 235775 [Multi-domain]  Cd Length: 565  Bit Score: 580.20  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 310 LQERYSFEAPEPGSVRMGTVVQVNAGTVFVDIGGKSEGRVPVEEFEAP-----PKAGDGVRVYVERV-TPYG-PELSKTK 382
Cdd:PRK06299  19 FEESLKESETREGSIVKGTVVAIDKDYVLVDVGLKSEGRIPLEEFKNEqgeleVKVGDEVEVYVERIeDGFGeTVLSREK 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 383 ADRLGLKVKLRDAERDGTPVEGRIVRltEKKSGFEVDLGaGMMAFLPISQSDCQKVDAPESLIGLTSKFYIERISQSKQh 462
Cdd:PRK06299  99 AKRLEAWDKLEKAFENGEIVEGVING--KVKGGFTVDLN-GVEAFLPGSQVDVRPVRDTDPLEGKELEFKVIKLDKKRN- 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 463 rgndNIVINRRRYLEERARQAREEFFNSVHIEDSVSGVVKSFTSFGAFIDLGGFDGLLHVNDMSWGHVARPREFVKKGQT 542
Cdd:PRK06299 175 ----NIVVSRRAVLEEERAEEREELLENLEEGQVVEGVVKNITDYGAFVDLGGVDGLLHITDISWKRVNHPSEVVNVGDE 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 543 IELKVIRLDQAEKRINLSLKHFQPDPWLEFENKFGVNDVVKGRVTKIADFGAFIELAEGIEGLAHISEFSWVKKTSKPSD 622
Cdd:PRK06299 251 VKVKVLKFDKEKKRVSLGLKQLGEDPWEAIEKKYPVGSKVKGKVTNITDYGAFVELEEGIEGLVHVSEMSWTKKNKHPSK 330
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 623 MVKIGDEVECMILGYDIQAGRVSLGLKQVTANPWEEIEARYPVGARFTRRIVKVTNAGAFIEMEEGIDGFLHVDDLSWVK 702
Cdd:PRK06299 331 VVSVGQEVEVMVLEIDEEKRRISLGLKQCKENPWEEFAEKYPVGDVVEGKVKNITDFGAFVGLEGGIDGLVHLSDISWDK 410
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 703 RTRPADHELEVGKEIECMVIECDPQARRIRLGVKQLSDNPWQVFANAYGVGSTVEGEVSSVTDFGIFVRVPGGVEGLVRK 782
Cdd:PRK06299 411 KGEEAVELYKKGDEVEAVVLKVDVEKERISLGIKQLEEDPFEEFAKKHKKGSIVTGTVTEVKDKGAFVELEDGVEGLIRA 490
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 374680314 783 QHLVENRDGDPGEalrKYAVGDRVKAVIVDMNVKDRKVAFSVRDYQRKVQRDELSRYMSAprgEDEGSfTLGDLMRQ 859
Cdd:PRK06299 491 SELSRDRVEDATE---VLKVGDEVEAKVINIDRKNRRISLSIKALDEAEEKEAIAEYNSA---SDSKT-TLGDLLKA 560
RpsA COG0539
Ribosomal protein S1 [Translation, ribosomal structure and biogenesis]; Ribosomal protein S1 ...
315-651 5.27e-138

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: 413.67  E-value: 5.27e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 315 SFEAPEPGSVRMGTVVQVNAGTVFVDIGGKSEGRVPVEEF-----EAPPKAGDGVRVYVERVTPYGPE--LSKTKADRLG 387
Cdd:COG0539   12 SLKELKEGDIVKGTVVSIDDDEVLVDIGYKSEGIIPLSEFsdepgELEVKVGDEVEVYVEKVEDGEGEivLSKKKADREK 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 388 LKVKLRDAERDGTPVEGRIVRLTekKSGFEVDLGaGMMAFLPISQSDCQKVDAPESLIGLTSKFYIERISQSKQhrgndN 467
Cdd:COG0539   92 AWEELEEAFENGEPVEGKVKGVV--KGGLIVDIG-GVRAFLPASQVDVRPVRDLDEYVGKTLEFKIIKLDRKRN-----N 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 468 IVINRRRYLEERARQAREEFFNSVHIEDSVSGVVKSFTSFGAFIDLGGFDGLLHVNDMSWGHVARPREFVKKGQTIELKV 547
Cdd:COG0539  164 VVVSRRAVLEEEREEKREELLEKLEEGDVVEGTVKNITDFGAFVDLGGVDGLLHISEISWGRVKHPSEVLKVGDEVEVKV 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 548 IRLDQAEKRINLSLKHFQPDPWLEFENKFGVNDVVKGRVTKIADFGAFIELAEGIEGLAHISEFSWVKKTSKPSDMVKIG 627
Cdd:COG0539  244 LKIDREKERISLSLKQLQPDPWENIAEKYPVGDVVKGKVTRLTDFGAFVELEPGVEGLVHISEMSWTKRVAHPSDVVKVG 323
                        330       340
                 ....*....|....*....|....
gi 374680314 628 DEVECMILGYDIQAGRVSLGLKQV 651
Cdd:COG0539  324 DEVEVKVLDIDPEERRISLSIKQL 347
PRK00087 PRK00087
bifunctional 4-hydroxy-3-methylbut-2-enyl diphosphate reductase/30S ribosomal protein S1;
309-664 7.66e-94

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


Pssm-ID: 234623 [Multi-domain]  Cd Length: 647  Bit Score: 308.80  E-value: 7.66e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 309 QLQERYSFEAPEPGSVRMGTVVQVNAGTVFVDIGGKSEGRVPVEEFEAPP--------KAGDGVRVYVERV-----TPYg 375
Cdd:PRK00087 290 LEYMNELEKQIRRGDIVKGTVVSVNENEVFVDVGYKSEGVIPLRELTLDEisslkesvKVGDEIEVKVLKLededgYVV- 368
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 376 peLSKTKADRLGLKVKLRDAERDGTPVEGRIvrlTEK-KSGFEVDLGaGMMAFLPISQSDCQKVDAPESLIGLTSKFYIe 454
Cdd:PRK00087 369 --LSKKEADREKAWKELEEAFENGEPVKGKV---KEVvKGGLLVDYG-GVRAFLPASHVELGYVEDLSEYKGQELEVKI- 441
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 455 rISQSKQHRGNdnIVINRRRYLEERARQAREEFFNSVHIEDSVSGVVKSFTSFGAFIDLGGFDGLLHVNDMSWGHVARPR 534
Cdd:PRK00087 442 -IEFNRKRRKK--VVLSRKAILEEEKEKKKEETWNSLEEGDVVEGEVKRLTDFGAFVDIGGVDGLLHVSEISWGRVEKPS 518
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 535 EFVKKGQTIELKVIRLDQAEKRINLSLKHFQPDPWLEFENKFGVNDVVKGRVTKIADFGAFIELAEGIEGLAHISEFSWv 614
Cdd:PRK00087 519 DVLKVGDEIKVYILDIDKENKKLSLSLKKLLPDPWENVEEKYPVGSIVLGKVVRIAPFGAFVELEPGVDGLVHISQISW- 597
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 374680314 615 KKTSKPSDMVKIGDEVECMILGYDIQAGRVSLGLKQVTANPWEEIEARYP 664
Cdd:PRK00087 598 KRIDKPEDVLSEGEEVKAKILEVDPEEKRIRLSIKEVEEEPGDIEKVELE 647
Cytidylate_kin pfam02224
Cytidylate kinase; Cytidylate kinase EC:2.7.4.14 catalyzes the phosphorylation of cytidine 5 ...
37-285 3.89e-92

Cytidylate kinase; Cytidylate kinase EC:2.7.4.14 catalyzes the phosphorylation of cytidine 5'-monophosphate (dCMP) to cytidine 5'-diphosphate (dCDP) in the presence of ATP or GTP.


Pssm-ID: 280401 [Multi-domain]  Cd Length: 211  Bit Score: 289.20  E-value: 3.89e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314   37 IALDGPAGSGKSSVCRLLASRLGAQCLNTGSFYRAFTLAALRRvselavqacspspdpdaavgcaavphatnldtsyapl 116
Cdd:pfam02224   1 IAIDGPSGSGKSTVARILARKLGYKYLDTGAMYRALALAALRQ------------------------------------- 43
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314  117 taqkKVALFDEAYWVSFARTVALSYRAGVMYVGEENVESLLRSDEVESAVSYFAAMPAIRAIMTGKIRSAVCGARVVCEG 196
Cdd:pfam02224  44 ----KVDLTDEDALAELASEVDISFGHTEVFLNGEDVSSEIRTDEVAQAASQVAAIPAVRARLNKLQRQLAKNGNIVMEG 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314  197 RDLTTVVFVDADLKCYLDASIEARVARRWAQ----GTSrLSKQELEQRMRARDAHDRARTVGGLRCAPDALYVDTSCLTI 272
Cdd:pfam02224 120 RDIGTVVFPDAEVKIFLTASPEERAKRRYKQlqakGLS-VDFEELLAEIKRRDKRDSERAVGPLKPAPDALIIDTSKLTI 198
                         250
                  ....*....|...
gi 374680314  273 EEVCERIAREAHR 285
Cdd:pfam02224 199 EEVVEKILELIKQ 211
rpsA PRK13806
30S ribosomal protein S1; Provisional
327-747 7.53e-87

30S ribosomal protein S1; Provisional


Pssm-ID: 237516 [Multi-domain]  Cd Length: 491  Bit Score: 285.08  E-value: 7.53e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 327 GTVVQVNAGTVFVDIGGKSEGRVPVEEF-----EAPPKAGDGVRVYVERVTPYGPELSKTKADRLGLKVkLRDAERDGTP 401
Cdd:PRK13806  40 GTVIAITEDSVFVDTGSKVDGVVDRAELldadgELTVAVGDEVELYVVSVNGQEIRLSKALSGQGGAAM-LEEAYENGVP 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 402 VEGRIvrlTEK-KSGFEVDLgAGMMAFLPISQSDCQKVDAPESLIGLTSKFYIERISQskqhRGNdNIVINRRRYLEERA 480
Cdd:PRK13806 119 VEGKV---TGTcKGGFNVEV-LGRRAFCPVSQIDLRYVEDPESYVGQTFQFLITRVEE----NGR-NIVVSRRALLEREQ 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 481 RQAREEFFNSVHIEDSVSGVVKSFTSFGAFIDLG-GFDGLLHVNDMSWGHVARPREFVKKGQTIELKVIRLDQAEK---- 555
Cdd:PRK13806 190 KEALEAFMETVKEGDVVEGTVTRLAPFGAFVELApGVEGMVHISELSWSRVQKADEAVSVGDTVRVKVLGIERAKKgkgl 269
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 556 RINLSLKHFQPDPWLEFENKFGVNDVVKGRVTKIADFGAFIELAEGIEGLAHISEFSWVKKTSKPSDMVKIGDEVECMIL 635
Cdd:PRK13806 270 RISLSIKQAGGDPWDTVGDRLKAGDKVTGKVVRLAPFGAFVEILPGIEGLVHVSEMSWTRRVNKPEDVVAPGDAVAVKIK 349
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 636 GYDIQAGRVSLGLKQVTANPWEEIEARYPVGARFTRRIVKVTNAGAFIEMEEGIDGFLHVDDLSwvKRTRPADHE-LEVG 714
Cdd:PRK13806 350 DIDPAKRRISLSLRDAEGDPWADVAERFAPGTTVTGTVEKRAQFGLFVNLAPGVTGLLPASVIS--RAGKPATYEkLKPG 427
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 374680314 715 KEIECMVIECDPQARRIRLGV-----KQLSDNPWQVFA 747
Cdd:PRK13806 428 DSVTLVVEEIDTAKRKISLAPagaagSGADDDDWKQFA 465
rpsA PRK06676
30S ribosomal protein S1; Reviewed
310-664 4.53e-84

30S ribosomal protein S1; Reviewed


Pssm-ID: 235851 [Multi-domain]  Cd Length: 390  Bit Score: 274.45  E-value: 4.53e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 310 LQERYSFEAPEPGSVRMGTVVQVNAGTVFVDI-GGKSEGRVPVEEFEAPP--------KAGDGVRVYVERVT--PYGPEL 378
Cdd:PRK06676   6 EESLNSVKEVEVGDVVTGEVLKVEDKQVFVNIeGYKVEGVIPISELSNDHiedindvvKVGDELEVYVLKVEdgEGNLLL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 379 SKTKADRLGLKVKLRDAERDGTPVEGRIVRltEKKSGFEVDLGaGMMAFLPISQSDCQKVDAPESLIGLTSKFYIERISQ 458
Cdd:PRK06676  86 SKRRLEAEKAWDKLEEKFEEGEVVEVKVTE--VVKGGLVVDVE-GVRGFIPASLISTRFVEDFSDFKGKTLEVKIIELDP 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 459 SKqhrgnDNIVINRRRYLEERARQAREEFFNSVHIEDSVSGVVKSFTSFGAFIDLGGFDGLLHVNDMSWGHVARPREFVK 538
Cdd:PRK06676 163 EK-----NRVILSRRAVVEEERAAKKEELLSSLKEGDVVEGTVARLTDFGAFVDIGGVDGLVHISELSHERVEKPSEVVS 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 539 KGQTIELKVIRLDQAEKRINLSLKHFQPDPWLEFENKFGVNDVVKGRVTKIADFGAFIELAEGIEGLAHISEFSWvKKTS 618
Cdd:PRK06676 238 VGQEVEVKVLSIDWETERISLSLKDTLPGPWEGVEEKLPEGDVIEGTVKRLTDFGAFVEVLPGVEGLVHISQISH-KHIA 316
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 374680314 619 KPSDMVKIGDEVECMILGYDIQAGRVSLGLKQVTANPWEEIEARYP 664
Cdd:PRK06676 317 TPSEVLEEGQEVKVKVLEVNEEEKRISLSIKALEEAPAEEEDRREE 362
Cmk COG0283
Cytidylate kinase [Nucleotide transport and metabolism];
36-286 1.34e-68

Cytidylate kinase [Nucleotide transport and metabolism];


Pssm-ID: 440052 [Multi-domain]  Cd Length: 220  Bit Score: 226.44  E-value: 1.34e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314  36 IIALDGPAGSGKSSVCRLLASRLGAQCLNTGSFYRAFTLAALRRvselavqacspspdpdaavgcaavphatnldtsyap 115
Cdd:COG0283    2 VIAIDGPAGSGKSTVAKALAKRLGYHYLDTGAMYRAVALAALRN------------------------------------ 45
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 116 ltaqkKVALFDEAYWVSFARTVALSYR----AGVMYVGEENVESLLRSDEVESAVSYFAAMPAIRAIMTGKIRSAVCGAR 191
Cdd:COG0283   46 -----GIDLDDEEALAALARNLDIEFEtdpgGQRVFLNGEDVTDEIRTEEVSNAVSKVAAIPEVREALVALQRAFAKAPG 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 192 VVCEGRDLTTVVFVDADLKCYLDASIEARVARRWAQGTSR---LSKQELEQRMRARDAHDRARTVGGLRCAPDALYVDTS 268
Cdd:COG0283  121 LVADGRDIGTVVFPDAELKIFLTASAEERARRRYKELKEKgisVSLEELLADIKERDERDSTRAVAPLKPAEDAIVIDTT 200
                        250
                 ....*....|....*...
gi 374680314 269 CLTIEEVCERIAREAHRR 286
Cdd:COG0283  201 DLSIEEVVEKILALVRER 218
rpsA PRK07899
30S ribosomal protein S1; Reviewed
327-653 1.28e-56

30S ribosomal protein S1; Reviewed


Pssm-ID: 236126 [Multi-domain]  Cd Length: 486  Bit Score: 202.58  E-value: 1.28e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 327 GTVVQVNAGTVFVDIGGKSEGRVPVEEF----EAPP----KAGDGVRVYVervtpygpeLSKT-KADRLGLKVKLRDAER 397
Cdd:PRK07899  41 GTVVKVDRDEVLLDIGYKTEGVIPSRELsikhDVDPnevvEVGDEVEALV---------LQKEdKEGRLILSKKRAQYER 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 398 -----------DGtPVEGRIVRLTekKSGFEVDLgaGMMAFLPISQSDCQKVDAPESLIGLTskfyIE-RISQSKQHRgn 465
Cdd:PRK07899 112 awgtiekikekDG-VVTGTVIEVV--KGGLILDI--GLRGFLPASLVEMRRVRDLQPYIGQE----IEaKIIELDKNR-- 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 466 DNIVINRRRYLEERARQAREEFFNSVHIEDSVSGVVKSFTSFGAFIDLGGFDGLLHVNDMSWGHVARPREFVKKGQTIEL 545
Cdd:PRK07899 181 NNVVLSRRAWLEQTQSEVRSEFLNQLQKGQVRKGVVSSIVNFGAFVDLGGVDGLVHVSELSWKHIDHPSEVVEVGQEVTV 260
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 546 KVIRLDQAEKRINLSLKHFQPDPWLEFENKFGVNDVVKGRVTKIADFGAFIELAEGIEGLAHISEFSwVKKTSKPSDMVK 625
Cdd:PRK07899 261 EVLDVDMDRERVSLSLKATQEDPWQQFARTHAIGQIVPGKVTKLVPFGAFVRVEEGIEGLVHISELA-ERHVEVPEQVVQ 339
                        330       340
                 ....*....|....*....|....*...
gi 374680314 626 IGDEVECMILGYDIQAGRVSLGLKQVTA 653
Cdd:PRK07899 340 VGDEVFVKVIDIDLERRRISLSLKQANE 367
cmk TIGR00017
cytidylate kinase; This family consists of cytidylate kinase, which catalyzes the ...
36-283 6.34e-47

cytidylate kinase; This family consists of cytidylate kinase, which catalyzes the phosphorylation of cytidine 5-monophosphate (dCMP) to cytidine 5 -diphosphate (dCDP) in the presence of ATP or GTP. UMP and dCMP can also act as acceptors. [Purines, pyrimidines, nucleosides, and nucleotides, Nucleotide and nucleoside interconversions]


Pssm-ID: 129128 [Multi-domain]  Cd Length: 217  Bit Score: 166.83  E-value: 6.34e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314   36 IIALDGPAGSGKSSVCRLLASRLGAQCLNTGSFYRAFTLAALrrvselaVQACSPSPDPDaavgcaavphatnldtsYAP 115
Cdd:TIGR00017   4 IIAIDGPSGAGKSTVAKAVAEKLGYAYLDSGAMYRAIALAAL-------QNRVDLTSEDA-----------------LAE 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314  116 LTAQKKVALFDEAYWVSFartvalsyragvmYVGEENVESLLRSDEVESAVSYFAAMPAIRAIMTGKIRSAVCGARVVCE 195
Cdd:TIGR00017  60 LISHLDIRFIPTNGEVEV-------------FLNGEDVSEAIRTQEVANAASKVAVFPKVREALLKRQQALAKNDGIIAD 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314  196 GRDLTTVVFVDADLKCYLDASIEARVARRWAQGTSRLSK---QELEQRMRARDAHDRARTVGGLRCAPDALYVDTSCLTI 272
Cdd:TIGR00017 127 GRDIGTVVFPNAEVKIFLDASVEERAKRRYKQLQIKGNEvnfEELLAEIKERDDRDSNREVAPLKKADDALYLDTSNLSI 206
                         250
                  ....*....|.
gi 374680314  273 EEVCERIAREA 283
Cdd:TIGR00017 207 DEVVEKILEYA 217
CMPK cd02020
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ...
36-268 1.77e-42

Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine monophosphate (CMP) to produce cytidine diphosphate (CDP), using ATP as the preferred phosphoryl donor.


Pssm-ID: 238978 [Multi-domain]  Cd Length: 147  Bit Score: 151.49  E-value: 1.77e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314  36 IIALDGPAGSGKSSVCRLLASRLGAQCLNTGsfyraftlaalrrvselavqacspspdpdaavgcaavphatnldtsyap 115
Cdd:cd02020    1 IIAIDGPAGSGKSTVAKLLAKKLGLPYLDTG------------------------------------------------- 31
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 116 ltaqkkvalfdeaywvsfartvalsyragvmyvgeenvesLLRSDEVESAVSYFAAMPAIRAIMTGKIRSAVCGARVVCE 195
Cdd:cd02020   32 ----------------------------------------GIRTEEVGKLASEVAAIPEVRKALDERQRELAKKPGIVLE 71
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 374680314 196 GRDLTTVVFVDADLKCYLDASIEARVARRWAQ---GTSRLSKQELEQRMRARDAHDRARTVGGLRCAPDALYVDTS 268
Cdd:cd02020   72 GRDIGTVVFPDADLKIFLTASPEVRAKRRAKQlqaKGEGVDLEEILAEIIERDERDSTRYVAPLKLAEDAIVIDTS 147
PRK13477 PRK13477
bifunctional pantoate--beta-alanine ligase/(d)CMP kinase;
36-279 2.88e-37

bifunctional pantoate--beta-alanine ligase/(d)CMP kinase;


Pssm-ID: 237393 [Multi-domain]  Cd Length: 512  Bit Score: 147.33  E-value: 2.88e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314  36 IIALDGPAGSGKSSVCRLLASRLGAQCLNTGSFYRAftlaalrrVSELAVQAcspSPDPDAAVGCAAVPHATNLDTSYAP 115
Cdd:PRK13477 286 IIAIDGPAGAGKSTVTRAVAKKLGLLYLDTGAMYRA--------VTWLVLQE---GIDPQDEEALAELLSDLKIELKPSS 354
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 116 LTAQKkvalfdeaywvsfartvalsyragvMYVGEENVESLLRSDEVESAVSYFAAMPAIRAIMTGKIRSAvcGAR--VV 193
Cdd:PRK13477 355 GSPQR-------------------------VWINGEDVTEAIRSPEVTSSVSAIAAQPAVRQALVKQQQRI--GEKggLV 407
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 194 CEGRDLTTVVFVDADLKCYLDASIEARVARRW----AQGTSRLSKQELEQRMRARDAHDRARTVGGLRCAPDALYVDTSC 269
Cdd:PRK13477 408 AEGRDIGTHVFPDAELKIFLTASVEERARRRAldlqAQGFPVIDLEQLEAQIAERDRLDSTREIAPLRKADDAIELITDG 487
                        250
                 ....*....|
gi 374680314 270 LTIEEVCERI 279
Cdd:PRK13477 488 LSIEEVVDKI 497
PRK11860 PRK11860
bifunctional 3-phosphoshikimate 1-carboxyvinyltransferase/cytidylate kinase;
36-279 3.33e-35

bifunctional 3-phosphoshikimate 1-carboxyvinyltransferase/cytidylate kinase;


Pssm-ID: 237003 [Multi-domain]  Cd Length: 661  Bit Score: 142.88  E-value: 3.33e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314  36 IIALDGPAGSGKSSVCRLLASRLGAQCLNTGSFYRAFTLAALRRvselavqacspspdpdaavgcaavphatnldtsyap 115
Cdd:PRK11860 444 VICIDGPTASGKGTVAARVAEALGYHYLDSGALYRLTALAALRA------------------------------------ 487
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 116 ltaqkKVALFDEAYWVSFARTVALSYRAGVMYVGEENVESLLRSDEVESAVSYFAAMPAIRAIMTGKIRSAVCGARVVCE 195
Cdd:PRK11860 488 -----GVALDDEAAIAALARGLPVRFEGDRIWLGGEDVTDAIRTEAAGMGASRVSALPAVRAALLALQRSFRRLPGLVAD 562
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 196 GRDLTTVVFVDADLKCYLDASIEARVARRWAQGTSR---LSKQELEQRMRARDAHDRARTVGGLRCAPDALYVDTSCLTI 272
Cdd:PRK11860 563 GRDMGTVIFPDAALKVFLTASAEARAERRYKQLISKgisANIADLLADLEARDARDTQRSVAPLKPAQDALLLDNSDLTI 642

                 ....*..
gi 374680314 273 EEVCERI 279
Cdd:PRK11860 643 EQAVAQV 649
PRK09518 PRK09518
bifunctional cytidylate kinase/GTPase Der; Reviewed
34-281 3.28e-32

bifunctional cytidylate kinase/GTPase Der; Reviewed


Pssm-ID: 236546 [Multi-domain]  Cd Length: 712  Bit Score: 134.15  E-value: 3.28e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314  34 TVIIALDGPAGSGKSSVCRLLASRLGAQCLNTGSFYRAFTLAALRRVSELAVQACSPSPDPDAAvgcaavphatnldtsy 113
Cdd:PRK09518   1 MIIVAIDGPAGVGKSSVSRALAQYLGYAYLDTGAMYRACAWWCLKQGIDLDAELVDEQVVTEAV---------------- 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 114 APLTAQKKVALFDEAywvsfartvalsyRAGVMYVGEENVESLLRSDEVESAVSYFAAMPAIRAIM----------TGKI 183
Cdd:PRK09518  65 GEFFTGLHFDISVDP-------------DSPGVFADGEDISEEIRSPEVSSHVSAVAAIPPVRNVLiaaqrayiarEASA 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 184 RSAVCGARVVCEGRDLTTVVFVDADLKCYLDASIEARVARRWAQGTSRLSKQELEQrMRARDAHDrARTVGGLRCAPDAL 263
Cdd:PRK09518 132 DSFSGGLGIVAEGRDITTVVAPDAEVRILLTAREEVRQARRSGQDRSETPGVVLED-VAARDEAD-SKVTSFLSAADGVT 209
                        250
                 ....*....|....*...
gi 374680314 264 YVDTSCLTIEEVCERIAR 281
Cdd:PRK09518 210 TLDNSDLDFDETLDLLIG 227
S1_RPS1_repeat_ec3 cd05688
S1_RPS1_repeat_ec3: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
493-560 2.59e-31

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


Pssm-ID: 240193 [Multi-domain]  Cd Length: 68  Bit Score: 116.57  E-value: 2.59e-31
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 374680314 493 IEDSVSGVVKSFTSFGAFIDLGGFDGLLHVNDMSWGHVARPREFVKKGQTIELKVIRLDQAEKRINLS 560
Cdd:cd05688    1 EGDVVEGTVKSITDFGAFVDLGGVDGLLHISDMSWGRVKHPSEVVNVGDEVEVKVLKIDKERKRISLG 68
S1 smart00316
Ribosomal protein S1-like RNA-binding domain;
578-649 2.21e-20

Ribosomal protein S1-like RNA-binding domain;


Pssm-ID: 197648 [Multi-domain]  Cd Length: 72  Bit Score: 85.73  E-value: 2.21e-20
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 374680314   578 VNDVVKGRVTKIADFGAFIELAEGIEGLAHISEFSWvKKTSKPSDMVKIGDEVECMILGYDIQAGRVSLGLK 649
Cdd:smart00316   2 VGDVVEGTVTEITPGGAFVDLGNGVEGLIPISELSD-KRVKDPEEVLKVGDEVKVKVLSVDEEKGRIILSLK 72
YabR COG1098
Predicted RNA-binding protein, contains ribosomal protein S1 (RPS1) domain [General function ...
575-655 8.95e-20

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


Pssm-ID: 440715 [Multi-domain]  Cd Length: 130  Bit Score: 86.00  E-value: 8.95e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 575 KFGVNDVVKGRVTKIADFGAFIELAEGIEGLAHISEFS--WVKKTskpSDMVKIGDEVECMILGYDiQAGRVSLGLKQVT 652
Cdd:COG1098    2 SIEVGDIVEGKVTGITPFGAFVELPEGTTGLVHISEIAdgYVKDI---NDYLKVGDEVKVKVLSID-EDGKISLSIKQAE 77

                 ...
gi 374680314 653 ANP 655
Cdd:COG1098   78 EKP 80
S1_RPS1_repeat_ec3 cd05688
S1_RPS1_repeat_ec3: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
580-647 1.06e-18

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: 80.75  E-value: 1.06e-18
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 374680314 580 DVVKGRVTKIADFGAFIELAeGIEGLAHISEFSWvKKTSKPSDMVKIGDEVECMILGYDIQAGRVSLG 647
Cdd:cd05688    3 DVVEGTVKSITDFGAFVDLG-GVDGLLHISDMSW-GRVKHPSEVVNVGDEVEVKVLKIDKERKRISLG 68
S1_RPS1_repeat_ec4 cd05689
S1_RPS1_repeat_ec4: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
584-647 2.14e-18

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: 79.93  E-value: 2.14e-18
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 374680314 584 GRVTKIADFGAFIELAEGIEGLAHISEFSWVKKTSKPSDMVKIGDEVECMILGYDIQAGRVSLG 647
Cdd:cd05689    9 GKVTNLTDYGCFVELEEGVEGLVHVSEMDWTNKNIHPSKVVSLGDEVEVMVLDIDEERRRISLG 72
S1_RPS1_repeat_ec5 cd05690
S1_RPS1_repeat_ec5: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
580-647 2.71e-18

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


Pssm-ID: 240195 [Multi-domain]  Cd Length: 69  Bit Score: 79.85  E-value: 2.71e-18
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 374680314 580 DVVKGRVTKIADFGAFIELAEGIEGLAHISEFSWVKKTSKPSDMVKIGDEVECMILGYDIQAGRVSLG 647
Cdd:cd05690    2 TVVSGKIKSITDFGIFVGLDGGIDGLVHISDISWTQRVRHPSEIYKKGQEVEAVVLNIDVERERISLG 69
S1_like cd00164
S1_like: Ribosomal protein S1-like RNA-binding domain. Found in a wide variety of ...
582-647 7.39e-18

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: 78.19  E-value: 7.39e-18
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 374680314 582 VKGRVTKIADFGAFIELAEGIEGLAHISEFSWvKKTSKPSDMVKIGDEVECMILGYDIQAGRVSLG 647
Cdd:cd00164    1 VTGKVVSITKFGVFVELEDGVEGLVHISELSD-KFVKDPSEVFKVGDEVEVKVLEVDPEKGRISLS 65
PRK11824 PRK11824
polynucleotide phosphorylase/polyadenylase; Provisional
578-651 7.95e-18

polynucleotide phosphorylase/polyadenylase; Provisional


Pssm-ID: 236995 [Multi-domain]  Cd Length: 693  Bit Score: 88.18  E-value: 7.95e-18
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 374680314 578 VNDVVKGRVTKIADFGAFIELAEGIEGLAHISEFSWvKKTSKPSDMVKIGDEVECMILGYDIQaGRVSLGLKQV 651
Cdd:PRK11824 621 VGEIYEGKVVRIVDFGAFVEILPGKDGLVHISEIAD-ERVEKVEDVLKEGDEVKVKVLEIDKR-GRIRLSRKAV 692
Pnp COG1185
Polyribonucleotide nucleotidyltransferase (polynucleotide phosphorylase) [Translation, ...
578-649 1.86e-17

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


Pssm-ID: 440798 [Multi-domain]  Cd Length: 686  Bit Score: 86.98  E-value: 1.86e-17
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 374680314 578 VNDVVKGRVTKIADFGAFIELAEGIEGLAHISEFSWvKKTSKPSDMVKIGDEVECMILGYDIQaGRVSLGLK 649
Cdd:COG1185  616 VGEIYEGKVVRIMDFGAFVEILPGKDGLVHISELAD-ERVEKVEDVLKEGDEVKVKVLEIDDQ-GRIKLSRK 685
S1 smart00316
Ribosomal protein S1-like RNA-binding domain;
493-562 6.01e-17

Ribosomal protein S1-like RNA-binding domain;


Pssm-ID: 197648 [Multi-domain]  Cd Length: 72  Bit Score: 76.10  E-value: 6.01e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 374680314   493 IEDSVSGVVKSFTSFGAFIDLG-GFDGLLHVNDMSWGHVARPREFVKKGQTIELKVIRLDQAEKRINLSLK 562
Cdd:smart00316   2 VGDVVEGTVTEITPGGAFVDLGnGVEGLIPISELSDKRVKDPEEVLKVGDEVKVKVLSVDEEKGRIILSLK 72
S1_RPS1_repeat_hs4 cd05692
S1_RPS1_repeat_hs4: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
580-649 7.66e-17

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


Pssm-ID: 240197 [Multi-domain]  Cd Length: 69  Bit Score: 75.40  E-value: 7.66e-17
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 580 DVVKGRVTKIADFGAFIELAEGIEGLAHISEFSWvKKTSKPSDMVKIGDEVECMILGYDiQAGRVSLGLK 649
Cdd:cd05692    2 SVVEGTVTRLKPFGAFVELGGGISGLVHISQIAH-KRVKDVKDVLKEGDKVKVKVLSID-ARGRISLSIK 69
PRK08059 PRK08059
general stress protein 13; Validated
574-665 2.04e-16

general stress protein 13; Validated


Pssm-ID: 181215 [Multi-domain]  Cd Length: 123  Bit Score: 76.24  E-value: 2.04e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 574 NKFGVNDVVKGRVTKIADFGAFIELAEGIEGLAHISEFS--WVKKTskpSDMVKIGDEVECMILGYDIQAGRVSLGLKQV 651
Cdd:PRK08059   3 SQYEVGSVVTGKVTGIQPYGAFVALDEETQGLVHISEIThgFVKDI---HDFLSVGDEVKVKVLSVDEEKGKISLSIRAT 79
                         90
                 ....*....|....
gi 374680314 652 TANPWEEIEARYPV 665
Cdd:PRK08059  80 EEAPEAKRKKGKIL 93
PRK07400 PRK07400
30S ribosomal protein S1; Reviewed
399-655 2.86e-16

30S ribosomal protein S1; Reviewed


Pssm-ID: 180960 [Multi-domain]  Cd Length: 318  Bit Score: 80.61  E-value: 2.86e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 399 GTPVEGRIVRLTEKksGFEVDLGAGMMAFLPISQSDCQKVDAPESLI--GLTSKFYIeriSQSKQHRGNDNIVINRRRYL 476
Cdd:PRK07400  32 GDIVNGTVFSLEPR--GALIDIGAKTAAFMPIQEMSINRVEGPEEVLqpNETREFFI---LSDENEDGQLTLSIRRIEYM 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 477 E--ERARQAREEffnsvhiEDSVSGVVKSFTSFGAFIDLGGFDGLLHVNDMSwghVARPREFVKkGQTIELKVIRLDQAE 554
Cdd:PRK07400 107 RawERVRQLQKE-------DATVRSEVFATNRGGALVRIEGLRGFIPGSHIS---TRKPKEELV-GEELPLKFLEVDEER 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 555 KRINLSLKHFQPDPWLefeNKFGVNDVVKGRVTKIADFGAFIELAeGIEGLAHISEFSWvKKTSKPSDMVKIGDEVECMI 634
Cdd:PRK07400 176 NRLVLSHRRALVERKM---NRLEVGEVVVGTVRGIKPYGAFIDIG-GVSGLLHISEISH-EHIETPHSVFNVNDEMKVMI 250
                        250       260
                 ....*....|....*....|.
gi 374680314 635 LGYDIQAGRVSLGLKQVTANP 655
Cdd:PRK07400 251 IDLDAERGRISLSTKQLEPEP 271
S1_PNPase cd04472
S1_PNPase: Polynucleotide phosphorylase (PNPase), ), S1-like RNA-binding domain. PNPase is a ...
579-646 2.26e-15

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: 71.42  E-value: 2.26e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 374680314 579 NDVVKGRVTKIADFGAFIELAEGIEGLAHISEFSwVKKTSKPSDMVKIGDEVECMILGYDIQaGRVSL 646
Cdd:cd04472    1 GKIYEGKVVKIKDFGAFVEILPGKDGLVHISELS-DERVEKVEDVLKVGDEVKVKVIEVDDR-GRISL 66
S1 smart00316
Ribosomal protein S1-like RNA-binding domain;
752-825 3.24e-15

Ribosomal protein S1-like RNA-binding domain;


Pssm-ID: 197648 [Multi-domain]  Cd Length: 72  Bit Score: 71.10  E-value: 3.24e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 374680314   752 VGSTVEGEVSSVTDFGIFVRVPGGVEGLVRKQHLVENRDGDPGEalrKYAVGDRVKAVIVDMNVKDRKVAFSVR 825
Cdd:smart00316   2 VGDVVEGTVTEITPGGAFVDLGNGVEGLIPISELSDKRVKDPEE---VLKVGDEVKVKVLSVDEEKGRIILSLK 72
S1_RPS1_repeat_ec5 cd05690
S1_RPS1_repeat_ec5: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
495-559 4.22e-15

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


Pssm-ID: 240195 [Multi-domain]  Cd Length: 69  Bit Score: 70.60  E-value: 4.22e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 374680314 495 DSVSGVVKSFTSFGAFIDL-GGFDGLLHVNDMSWG-HVARPREFVKKGQTIELKVIRLDQAEKRINL 559
Cdd:cd05690    2 TVVSGKIKSITDFGIFVGLdGGIDGLVHISDISWTqRVRHPSEIYKKGQEVEAVVLNIDVERERISL 68
S1_dom_CvfD NF040579
CvfD/Ygs/GSP13 family RNA-binding post-transcriptional regulator; CvfD, Ygs, and GSP13 form a ...
580-675 7.28e-15

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


Pssm-ID: 468553 [Multi-domain]  Cd Length: 113  Bit Score: 71.30  E-value: 7.28e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 580 DVVKGRVTKIADFGAFIELAEGIEGLAHISEFS--WVKKTskpSDMVKIGDEVECMILGYDIQAGRVSLGLKQVTANPwe 657
Cdd:NF040579   5 DIVEGKVTGIQPYGAFVALDEHTQGLIHISEIKhgYVKDI---NDFLKVGQEVKVKVLDIDEYTGKISLSLRALEEAP-- 79
                         90
                 ....*....|....*...
gi 374680314 658 eIEARYPVGARFTRRIVK 675
Cdd:NF040579  80 -EKHRKRRKHRWTNKRLK 96
S1_Tex cd05685
S1_Tex: The C-terminal S1 domain of a transcription accessory factor called Tex, which has ...
581-646 9.64e-15

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


Pssm-ID: 240190 [Multi-domain]  Cd Length: 68  Bit Score: 69.57  E-value: 9.64e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 374680314 581 VVKGRVTKIADFGAFIELAEGIEGLAHISEFSwVKKTSKPSDMVKIGDEVECMILGYDIQAGRVSL 646
Cdd:cd05685    3 VLEGVVTNVTDFGAFVDIGVKQDGLIHISKMA-DRFVSHPSDVVSVGDIVEVKVISIDEERGRISL 67
S1 smart00316
Ribosomal protein S1-like RNA-binding domain;
665-736 1.36e-14

Ribosomal protein S1-like RNA-binding domain;


Pssm-ID: 197648 [Multi-domain]  Cd Length: 72  Bit Score: 69.17  E-value: 1.36e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 374680314   665 VGARFTRRIVKVTNAGAFIEMEEGIDGFLHVDDLSWVKRTRPADHeLEVGKEIECMVIECDPQARRIRLGVK 736
Cdd:smart00316   2 VGDVVEGTVTEITPGGAFVDLGNGVEGLIPISELSDKRVKDPEEV-LKVGDEVKVKVLSVDEEKGRIILSLK 72
S1_RPS1_repeat_ec4 cd05689
S1_RPS1_repeat_ec4: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
663-734 2.73e-14

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


Pssm-ID: 240194 [Multi-domain]  Cd Length: 72  Bit Score: 68.37  E-value: 2.73e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 374680314 663 YPVGARFTRRIVKVTNAGAFIEMEEGIDGFLHVDDLSWVKRTRPADHELEVGKEIECMVIECDPQARRIRLG 734
Cdd:cd05689    1 YPEGTRLFGKVTNLTDYGCFVELEEGVEGLVHVSEMDWTNKNIHPSKVVSLGDEVEVMVLDIDEERRRISLG 72
S1_like cd00164
S1_like: Ribosomal protein S1-like RNA-binding domain. Found in a wide variety of ...
497-560 6.17e-14

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


Pssm-ID: 238094 [Multi-domain]  Cd Length: 65  Bit Score: 67.02  E-value: 6.17e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 374680314 497 VSGVVKSFTSFGAFIDLG-GFDGLLHVNDMSWGHVARPREFVKKGQTIELKVIRLDQAEKRINLS 560
Cdd:cd00164    1 VTGKVVSITKFGVFVELEdGVEGLVHISELSDKFVKDPSEVFKVGDEVEVKVLEVDPEKGRISLS 65
S1_Tex cd05685
S1_Tex: The C-terminal S1 domain of a transcription accessory factor called Tex, which has ...
497-560 8.33e-14

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


Pssm-ID: 240190 [Multi-domain]  Cd Length: 68  Bit Score: 66.87  E-value: 8.33e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 374680314 497 VSGVVKSFTSFGAFIDLG-GFDGLLHVNDMSWGHVARPREFVKKGQTIELKVIRLDQAEKRINLS 560
Cdd:cd05685    4 LEGVVTNVTDFGAFVDIGvKQDGLIHISKMADRFVSHPSDVVSVGDIVEVKVISIDEERGRISLS 68
S1 pfam00575
S1 RNA binding domain; The S1 domain occurs in a wide range of RNA associated proteins. It is ...
576-648 1.19e-13

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


Pssm-ID: 425760 [Multi-domain]  Cd Length: 72  Bit Score: 66.54  E-value: 1.19e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 374680314  576 FGVNDVVKGRVTKIADFGAFIELAEGIEGLAHISEFSWvKKTSKPSDMVKIGDEVECMILGYDIQAGRVSLGL 648
Cdd:pfam00575   1 PEKGDVVEGEVTRVTKGGAFVDLGNGVEGFIPISELSD-DHVEDPDEVIKVGDEVKVKVLKVDKDRRRIILSI 72
S1_RPS1_repeat_ec5 cd05690
S1_RPS1_repeat_ec5: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
666-734 1.25e-13

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


Pssm-ID: 240195 [Multi-domain]  Cd Length: 69  Bit Score: 66.36  E-value: 1.25e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 374680314 666 GARFTRRIVKVTNAGAFIEMEEGIDGFLHVDDLSWVKRTRPADHELEVGKEIECMVIECDPQARRIRLG 734
Cdd:cd05690    1 GTVVSGKIKSITDFGIFVGLDGGIDGLVHISDISWTQRVRHPSEIYKKGQEVEAVVLNIDVERERISLG 69
S1_like cd00164
S1_like: Ribosomal protein S1-like RNA-binding domain. Found in a wide variety of ...
672-734 1.70e-13

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


Pssm-ID: 238094 [Multi-domain]  Cd Length: 65  Bit Score: 65.86  E-value: 1.70e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 374680314 672 RIVKVTNAGAFIEMEEGIDGFLHVDDLSWvKRTRPADHELEVGKEIECMVIECDPQARRIRLG 734
Cdd:cd00164    4 KVVSITKFGVFVELEDGVEGLVHISELSD-KFVKDPSEVFKVGDEVEVKVLEVDPEKGRISLS 65
S1_Rrp5_repeat_sc12 cd05708
S1_Rrp5_repeat_sc12: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ...
752-825 6.55e-13

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: 64.66  E-value: 6.55e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 374680314 752 VGSTVEGEVSSVTDFGIFVRVPG-GVEGLVRKQHLVENRDGDpgeALRKYAVGDRVKAVIVDMNVKDRKVAFSVR 825
Cdd:cd05708    2 VGQKIDGTVRRVEDYGVFIDIDGtNVSGLCHKSEISDNRVAD---ASKLFRVGDKVRAKVLKIDAEKKRISLGLK 73
S1_DHX8_helicase cd05684
S1_DHX8_helicase: The N-terminal S1 domain of human ATP-dependent RNA helicase DHX8, a DEAH ...
579-651 8.45e-13

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


Pssm-ID: 240189 [Multi-domain]  Cd Length: 79  Bit Score: 64.18  E-value: 8.45e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 374680314 579 NDVVKGRVTKIADFGAFIEL---AEGIEGLAHISEFSWVKKTSKPSDMVKIGDEVECMILgyDIQAGRVSLGLKQV 651
Cdd:cd05684    1 GKIYKGKVTSIMDFGCFVQLeglKGRKEGLVHISQLSFEGRVANPSDVVKRGQKVKVKVI--SIQNGKISLSMKDV 74
S1_RPS1_repeat_hs4 cd05692
S1_RPS1_repeat_hs4: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
497-562 1.93e-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: 1.93e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 374680314 497 VSGVVKSFTSFGAFIDLG-GFDGLLHVNDMSWGHVARPREFVKKGQTIELKVIRLDQaEKRINLSLK 562
Cdd:cd05692    4 VEGTVTRLKPFGAFVELGgGISGLVHISQIAHKRVKDVKDVLKEGDKVKVKVLSIDA-RGRISLSIK 69
PRK07400 PRK07400
30S ribosomal protein S1; Reviewed
321-568 3.64e-12

30S ribosomal protein S1; Reviewed


Pssm-ID: 180960 [Multi-domain]  Cd Length: 318  Bit Score: 68.29  E-value: 3.64e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 321 PGSVRMGTVVQVNAGTVFVDIGGKSEGRVPVEEfeappkagdgvrVYVERVTpyGPE-------------LSKTKAD-RL 386
Cdd:PRK07400  31 PGDIVNGTVFSLEPRGALIDIGAKTAAFMPIQE------------MSINRVE--GPEevlqpnetreffiLSDENEDgQL 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 387 GLKVK----LRDAERdgtpvegriVRLTEKKSG------FEVDLGA------GMMAFLPISQSDCQKvdAPESLIG--LT 448
Cdd:PRK07400  97 TLSIRrieyMRAWER---------VRQLQKEDAtvrsevFATNRGGalvrieGLRGFIPGSHISTRK--PKEELVGeeLP 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 449 SKFYierisQSKQHRgnDNIVINRRRYLEERArqareefFNSVHIEDSVSGVVKSFTSFGAFIDLGGFDGLLHVNDMSWG 528
Cdd:PRK07400 166 LKFL-----EVDEER--NRLVLSHRRALVERK-------MNRLEVGEVVVGTVRGIKPYGAFIDIGGVSGLLHISEISHE 231
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 374680314 529 HVARPREFVKKGQTIELKVIRLDQAEKRINLSLKHFQPDP 568
Cdd:PRK07400 232 HIETPHSVFNVNDEMKVMIIDLDAERGRISLSTKQLEPEP 271
PRK11824 PRK11824
polynucleotide phosphorylase/polyadenylase; Provisional
478-562 5.07e-12

polynucleotide phosphorylase/polyadenylase; Provisional


Pssm-ID: 236995 [Multi-domain]  Cd Length: 693  Bit Score: 69.69  E-value: 5.07e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 478 ERARQAREEFFNSVHIEDSVSGVVKSFTSFGAFID-LGGFDGLLHVNDMSWGHVARPREFVKKGQTIELKVIRLDQaEKR 556
Cdd:PRK11824 606 EAAKERIEGITAEPEVGEIYEGKVVRIVDFGAFVEiLPGKDGLVHISEIADERVEKVEDVLKEGDEVKVKVLEIDK-RGR 684

                 ....*.
gi 374680314 557 INLSLK 562
Cdd:PRK11824 685 IRLSRK 690
S1 pfam00575
S1 RNA binding domain; The S1 domain occurs in a wide range of RNA associated proteins. It is ...
493-561 5.95e-12

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: 61.92  E-value: 5.95e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314  493 IEDSVSGVVKSFTSFGAFIDLG-GFDGLLHVNDMSWGHVARPREFVKKGQTIELKVIRLDQAEKRINLSL 561
Cdd:pfam00575   3 KGDVVEGEVTRVTKGGAFVDLGnGVEGFIPISELSDDHVEDPDEVIKVGDEVKVKVLKVDKDRRRIILSI 72
S1 pfam00575
S1 RNA binding domain; The S1 domain occurs in a wide range of RNA associated proteins. It is ...
752-824 7.67e-12

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: 61.53  E-value: 7.67e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 374680314  752 VGSTVEGEVSSVTDFGIFVRVPGGVEGLVRKQHLVENRDGDPGEalrKYAVGDRVKAVIVDMNVKDRKVAFSV 824
Cdd:pfam00575   3 KGDVVEGEVTRVTKGGAFVDLGNGVEGFIPISELSDDHVEDPDE---VIKVGDEVKVKVLKVDKDRRRIILSI 72
rpsA PRK07899
30S ribosomal protein S1; Reviewed
576-828 1.46e-11

30S ribosomal protein S1; Reviewed


Pssm-ID: 236126 [Multi-domain]  Cd Length: 486  Bit Score: 67.76  E-value: 1.46e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 576 FGVNDVVKGRVTKIADFGAFIELAEGIEGLAHISEFSwVKKTSKPSDMVKIGDEVECMILGYDIQAGRVSLGLKQVT-AN 654
Cdd:PRK07899  33 FNDGDIVEGTVVKVDRDEVLLDIGYKTEGVIPSRELS-IKHDVDPNEVVEVGDEVEALVLQKEDKEGRLILSKKRAQyER 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 655 PWEEIEARYPVGARFTRRIVKVTNAGAFIEMeeGIDGFLHVddlSWVKRTRPADHELEVGKEIECMVIECDPQ------A 728
Cdd:PRK07899 112 AWGTIEKIKEKDGVVTGTVIEVVKGGLILDI--GLRGFLPA---SLVEMRRVRDLQPYIGQEIEAKIIELDKNrnnvvlS 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 729 RRIRLgvKQLSDNPWQVFANAYGVGSTVEGEVSSVTDFGIFVRVpGGVEGLVRKQHLVENRDGDPGEALrkyAVGDRVKA 808
Cdd:PRK07899 187 RRAWL--EQTQSEVRSEFLNQLQKGQVRKGVVSSIVNFGAFVDL-GGVDGLVHVSELSWKHIDHPSEVV---EVGQEVTV 260
                        250       260
                 ....*....|....*....|
gi 374680314 809 VIVDMNVKDRKVAFSVRDYQ 828
Cdd:PRK07899 261 EVLDVDMDRERVSLSLKATQ 280
S1_IF2_alpha cd04452
S1_IF2_alpha: The alpha subunit of translation Initiation Factor 2, S1-like RNA-binding domain. ...
578-650 3.05e-11

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


Pssm-ID: 239899 [Multi-domain]  Cd Length: 76  Bit Score: 59.91  E-value: 3.05e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 374680314 578 VNDVVKGRVTKIADFGAFIELAE--GIEGLAHISEFS--WVKKTSKpsdMVKIGDEVECMILGYDIQAGRVSLGLKQ 650
Cdd:cd04452    3 EGELVVVTVKSIADMGAYVSLLEygNIEGMILLSELSrrRIRSIRK---LVKVGRKEVVKVIRVDKEKGYIDLSKKR 76
S1_Rrp5_repeat_sc12 cd05708
S1_Rrp5_repeat_sc12: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ...
578-649 7.60e-11

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


Pssm-ID: 240213 [Multi-domain]  Cd Length: 77  Bit Score: 58.88  E-value: 7.60e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 374680314 578 VNDVVKGRVTKIADFGAFIEL-AEGIEGLAHISEFSwVKKTSKPSDMVKIGDEVECMILGYDIQAGRVSLGLK 649
Cdd:cd05708    2 VGQKIDGTVRRVEDYGVFIDIdGTNVSGLCHKSEIS-DNRVADASKLFRVGDKVRAKVLKIDAEKKRISLGLK 73
S1_like cd00164
S1_like: Ribosomal protein S1-like RNA-binding domain. Found in a wide variety of ...
756-823 2.03e-10

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


Pssm-ID: 238094 [Multi-domain]  Cd Length: 65  Bit Score: 57.01  E-value: 2.03e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 374680314 756 VEGEVSSVTDFGIFVRVPGGVEGLVRKQHLVENRDGDPGEALRkyaVGDRVKAVIVDMNVKDRKVAFS 823
Cdd:cd00164    1 VTGKVVSITKFGVFVELEDGVEGLVHISELSDKFVKDPSEVFK---VGDEVEVKVLEVDPEKGRISLS 65
PRK08582 PRK08582
RNA-binding protein S1;
582-655 2.14e-10

RNA-binding protein S1;


Pssm-ID: 236305 [Multi-domain]  Cd Length: 139  Bit Score: 59.28  E-value: 2.14e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 374680314 582 VKGRVTKIADFGAFIELAEGIEGLAHISEFS--WVKKTskpSDMVKIGDEVECMILGYDiQAGRVSLGLKQVTANP 655
Cdd:PRK08582   9 LQGKVTGITNFGAFVELPEGKTGLVHISEVAdnYVKDI---NDHLKVGDEVEVKVLNVE-DDGKIGLSIKKAKDRP 80
Tex COG2183
Transcriptional accessory protein Tex/SPT6 [Transcription];
484-562 2.48e-10

Transcriptional accessory protein Tex/SPT6 [Transcription];


Pssm-ID: 441786 [Multi-domain]  Cd Length: 719  Bit Score: 64.28  E-value: 2.48e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 484 REEF----FNS-VH-IED-----SVSGVVKSFTSFGAFIDLG-GFDGLLHVNDMSWGHVARPREFVKKGQTIELKVIRLD 551
Cdd:COG2183  621 RPEFktptFREgVLkIEDlkpgmILEGTVTNVTDFGAFVDIGvHQDGLVHISQLSDRFVKDPREVVKVGDIVKVKVLEVD 700
                         90
                 ....*....|.
gi 374680314 552 QAEKRINLSLK 562
Cdd:COG2183  701 LKRKRISLSMK 711
S1 pfam00575
S1 RNA binding domain; The S1 domain occurs in a wide range of RNA associated proteins. It is ...
663-735 2.79e-10

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


Pssm-ID: 425760 [Multi-domain]  Cd Length: 72  Bit Score: 56.91  E-value: 2.79e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 374680314  663 YPVGARFTRRIVKVTNAGAFIEMEEGIDGFLHVDDLSWVKRTRPADhELEVGKEIECMVIECDPQARRIRLGV 735
Cdd:pfam00575   1 PEKGDVVEGEVTRVTKGGAFVDLGNGVEGFIPISELSDDHVEDPDE-VIKVGDEVKVKVLKVDKDRRRIILSI 72
PRK05807 PRK05807
RNA-binding protein S1;
576-655 2.94e-10

RNA-binding protein S1;


Pssm-ID: 235614 [Multi-domain]  Cd Length: 136  Bit Score: 58.99  E-value: 2.94e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 576 FGVNDVVKGRVTKIADFGAFIELaEGIEGLAHISEF--SWVKKTskpSDMVKIGDEVECMILGYDiQAGRVSLGLKQvtA 653
Cdd:PRK05807   3 LKAGSILEGTVVNITNFGAFVEV-EGKTGLVHISEVadTYVKDI---REHLKEQDKVKVKVISID-DNGKISLSIKQ--A 75

                 ..
gi 374680314 654 NP 655
Cdd:PRK05807  76 MK 77
SUI2 COG1093
Translation initiation factor 2, alpha subunit (eIF-2alpha) [Translation, ribosomal structure ...
497-562 4.68e-10

Translation initiation factor 2, alpha subunit (eIF-2alpha) [Translation, ribosomal structure and biogenesis]; Translation initiation factor 2, alpha subunit (eIF-2alpha) is part of the Pathway/BioSystem: Translation factors


Pssm-ID: 440710 [Multi-domain]  Cd Length: 259  Bit Score: 60.98  E-value: 4.68e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 374680314 497 VSGVVKSFTSFGAFIDL---GGFDGLLHVNDMSWGHVARPREFVKKGQTIELKVIRLDQAEKRINLSLK 562
Cdd:COG1093   14 VVGTVKEVKDFGAYVTLdeyEGKEGFIHISEVASGWIKNIRDYVREGQKVVCKVLRVDPKRGHIDLSLK 82
S1_RPS1_repeat_ec5 cd05690
S1_RPS1_repeat_ec5: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
753-821 8.61e-10

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


Pssm-ID: 240195 [Multi-domain]  Cd Length: 69  Bit Score: 55.58  E-value: 8.61e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 374680314 753 GSTVEGEVSSVTDFGIFVRVPGGVEGLVRKQHLVENRDGDpgEALRKYAVGDRVKAVIVDMNVKDRKVA 821
Cdd:cd05690    1 GTVVSGKIKSITDFGIFVGLDGGIDGLVHISDISWTQRVR--HPSEIYKKGQEVEAVVLNIDVERERIS 67
YabR COG1098
Predicted RNA-binding protein, contains ribosomal protein S1 (RPS1) domain [General function ...
749-826 1.13e-09

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


Pssm-ID: 440715 [Multi-domain]  Cd Length: 130  Bit Score: 57.11  E-value: 1.13e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 749 AYGVGSTVEGEVSSVTDFGIFVRVPGGVEGLVrkqHLVENRDG---DPGEALrkyAVGDRVKAVIVDMNvKDRKVAFSVR 825
Cdd:COG1098    2 SIEVGDIVEGKVTGITPFGAFVELPEGTTGLV---HISEIADGyvkDINDYL---KVGDEVKVKVLSID-EDGKISLSIK 74

                 .
gi 374680314 826 D 826
Cdd:COG1098   75 Q 75
S1_RPS1_repeat_ec3 cd05688
S1_RPS1_repeat_ec3: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
673-734 1.15e-09

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: 54.94  E-value: 1.15e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 374680314 673 IVK-VTNAGAFIEMEeGIDGFLHVDDLSWVKRTRPADHeLEVGKEIECMVIECDPQARRIRLG 734
Cdd:cd05688    8 TVKsITDFGAFVDLG-GVDGLLHISDMSWGRVKHPSEV-VNVGDEVEVKVLKIDKERKRISLG 68
S1_DHX8_helicase cd05684
S1_DHX8_helicase: The N-terminal S1 domain of human ATP-dependent RNA helicase DHX8, a DEAH ...
498-562 1.17e-09

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


Pssm-ID: 240189 [Multi-domain]  Cd Length: 79  Bit Score: 55.32  E-value: 1.17e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 498 SGVVKSFTSFGAFIDLGGF----DGLLHVNDMSWGHVAR-PREFVKKGQTIELKVIRLdQAEKrINLSLK 562
Cdd:cd05684    5 KGKVTSIMDFGCFVQLEGLkgrkEGLVHISQLSFEGRVAnPSDVVKRGQKVKVKVISI-QNGK-ISLSMK 72
S1_RPS1_repeat_ec1_hs1 cd05687
S1_RPS1_repeat_ec1_hs1: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
322-371 1.29e-09

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


Pssm-ID: 240192 [Multi-domain]  Cd Length: 70  Bit Score: 54.84  E-value: 1.29e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 374680314 322 GSVRMGTVVQVNAGTVFVDIGGKSEGRVPVEEF--------EAPPKAGDGVRVYVERV 371
Cdd:cd05687    1 GDIVKGTVVSVDDDEVLVDIGYKSEGIIPISEFsddpiengEDEVKVGDEVEVYVLRV 58
S1_RPS1_repeat_ec6 cd05691
S1_RPS1_repeat_ec6: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
753-825 1.64e-09

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


Pssm-ID: 240196 [Multi-domain]  Cd Length: 73  Bit Score: 54.97  E-value: 1.64e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 374680314 753 GSTVEGEVSSVTDFGIFVRVPGGVEGLVRKQHLVENRDGDPGEALrkyAVGDRVKAVIVDMNVKDRKVAFSVR 825
Cdd:cd05691    1 GSIVTGKVTEVDAKGATVKLGDGVEGFLRAAELSRDRVEDATERF---KVGDEVEAKITNVDRKNRKISLSIK 70
S1_Tex cd05685
S1_Tex: The C-terminal S1 domain of a transcription accessory factor called Tex, which has ...
753-823 1.86e-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: 54.55  E-value: 1.86e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 374680314 753 GSTVEGEVSSVTDFGIFVRVPGGVEGLVRKQHLVENRDGDPGEALRkyaVGDRVKAVIVDMNVKDRKVAFS 823
Cdd:cd05685    1 GMVLEGVVTNVTDFGAFVDIGVKQDGLIHISKMADRFVSHPSDVVS---VGDIVEVKVISIDEERGRISLS 68
PRK07252 PRK07252
S1 RNA-binding domain-containing protein;
578-670 2.64e-09

S1 RNA-binding domain-containing protein;


Pssm-ID: 180908 [Multi-domain]  Cd Length: 120  Bit Score: 55.86  E-value: 2.64e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 578 VNDVVKGRVTKIADFGAFIELAEGIEGLAHISEFswvkKT---SKPSDMVKIGDEVECMILGYDIQAGRVSLGLKQVtan 654
Cdd:PRK07252   3 IGDKLKGTITGIKPYGAFVALENGTTGLIHISEI----KTgfiDNIHQLLKVGEEVLVQVVDFDEYTGKASLSLRTL--- 75
                         90
                 ....*....|....*.
gi 374680314 655 pwEEIEARYPVGARFT 670
Cdd:PRK07252  76 --EEEKQHFPHRHRFS 89
S1_RPS1_repeat_hs4 cd05692
S1_RPS1_repeat_hs4: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
753-825 4.27e-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: 53.44  E-value: 4.27e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 374680314 753 GSTVEGEVSSVTDFGIFVRVPGGVEGLVRKQHLVENRDGDPGEALRkyaVGDRVKAVIvdMNVKDR-KVAFSVR 825
Cdd:cd05692    1 GSVVEGTVTRLKPFGAFVELGGGISGLVHISQIAHKRVKDVKDVLK---EGDKVKVKV--LSIDARgRISLSIK 69
PRK03987 PRK03987
translation initiation factor IF-2 subunit alpha; Validated
578-652 5.33e-09

translation initiation factor IF-2 subunit alpha; Validated


Pssm-ID: 235188 [Multi-domain]  Cd Length: 262  Bit Score: 57.91  E-value: 5.33e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 374680314 578 VNDVVKGRVTKIADFGAFIELAE--GIEGLAHISEFS--WVKKTskpSDMVKIGDEVECMILGYDIQAGRVSLGLKQVT 652
Cdd:PRK03987   8 EGELVVGTVKEVKDFGAFVTLDEypGKEGFIHISEVAsgWVKNI---RDHVKEGQKVVCKVIRVDPRKGHIDLSLKRVN 83
PRK05807 PRK05807
RNA-binding protein S1;
497-567 5.70e-09

RNA-binding protein S1;


Pssm-ID: 235614 [Multi-domain]  Cd Length: 136  Bit Score: 55.14  E-value: 5.70e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 374680314 497 VSGVVKSFTSFGAFIDLGGFDGLLHVNDMSWGHVARPREFVKKGQTIELKVIRLDqAEKRINLSLKHFQPD 567
Cdd:PRK05807   9 LEGTVVNITNFGAFVEVEGKTGLVHISEVADTYVKDIREHLKEQDKVKVKVISID-DNGKISLSIKQAMKQ 78
S1_RPS1_repeat_ec2_hs2 cd04465
S1_RPS1_repeat_ec2_hs2: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
399-473 6.94e-09

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: 52.85  E-value: 6.94e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 374680314 399 GTPVEGRIVRLTekKSGFEVDLGaGMMAFLPISQSDCQKVDAPESLIGLTSKFYIERISQSKQhrgndNIVINRR 473
Cdd:cd04465    1 GEIVEGKVTEKV--KGGLIVDIE-GVRAFLPASQVDLRPVEDLDEYVGKELKFKIIEIDRERN-----NIVLSRR 67
S1_Rrp5_repeat_hs8_sc7 cd04461
S1_Rrp5_repeat_hs8_sc7: Rrp5 Homo sapiens S1 repeat 8 (hs8) and Saccharomyces cerevisiae S1 ...
488-561 7.24e-09

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


Pssm-ID: 239908 [Multi-domain]  Cd Length: 83  Bit Score: 53.36  E-value: 7.24e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 374680314 488 FNSVHIEDSVSGVVKSFTSFGAFID-LGGFDGLLHVNDMSWGHVARPREFVKKGQTIELKVIRLDQAEKRINLSL 561
Cdd:cd04461    9 FSDLKPGMVVHGYVRNITPYGVFVEfLGGLTGLAPKSYISDEFVTDPSFGFKKGQSVTAKVTSVDEEKQRFLLSL 83
S1_Rrp5_repeat_sc12 cd05708
S1_Rrp5_repeat_sc12: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ...
492-562 7.51e-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: 53.10  E-value: 7.51e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 374680314 492 HIEDSVSGVVKSFTSFGAFIDLGGFD--GLLHVNDMSWGHVARPREFVKKGQTIELKVIRLDQAEKRINLSLK 562
Cdd:cd05708    1 KVGQKIDGTVRRVEDYGVFIDIDGTNvsGLCHKSEISDNRVADASKLFRVGDKVRAKVLKIDAEKKRISLGLK 73
PRK03987 PRK03987
translation initiation factor IF-2 subunit alpha; Validated
497-562 1.06e-08

translation initiation factor IF-2 subunit alpha; Validated


Pssm-ID: 235188 [Multi-domain]  Cd Length: 262  Bit Score: 57.14  E-value: 1.06e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 374680314 497 VSGVVKSFTSFGAFIDL---GGFDGLLHVNDMSWGHVARPREFVKKGQTIELKVIRLDQAEKRINLSLK 562
Cdd:PRK03987  12 VVGTVKEVKDFGAFVTLdeyPGKEGFIHISEVASGWVKNIRDHVKEGQKVVCKVIRVDPRKGHIDLSLK 80
PRK08059 PRK08059
general stress protein 13; Validated
497-568 1.07e-08

general stress protein 13; Validated


Pssm-ID: 181215 [Multi-domain]  Cd Length: 123  Bit Score: 54.28  E-value: 1.07e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 374680314 497 VSGVVKSFTSFGAFIDL-GGFDGLLHVNDMSWGHVARPREFVKKGQTIELKVIRLDQAEKRINLSLKHFQPDP 568
Cdd:PRK08059  11 VTGKVTGIQPYGAFVALdEETQGLVHISEITHGFVKDIHDFLSVGDEVKVKVLSVDEEKGKISLSIRATEEAP 83
PRK11824 PRK11824
polynucleotide phosphorylase/polyadenylase; Provisional
657-738 1.28e-08

polynucleotide phosphorylase/polyadenylase; Provisional


Pssm-ID: 236995 [Multi-domain]  Cd Length: 693  Bit Score: 58.52  E-value: 1.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 657 EEIEARYPVGARFTRRIVKVTNAGAFIEMEEGIDGFLHVDDLSWvKRTRPADHELEVGKEIECMVIECDPQaRRIRLGVK 736
Cdd:PRK11824 613 EGITAEPEVGEIYEGKVVRIVDFGAFVEILPGKDGLVHISEIAD-ERVEKVEDVLKEGDEVKVKVLEIDKR-GRIRLSRK 690

                 ..
gi 374680314 737 QL 738
Cdd:PRK11824 691 AV 692
Tex COG2183
Transcriptional accessory protein Tex/SPT6 [Transcription];
581-655 1.38e-08

Transcriptional accessory protein Tex/SPT6 [Transcription];


Pssm-ID: 441786 [Multi-domain]  Cd Length: 719  Bit Score: 58.50  E-value: 1.38e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 374680314 581 VVKGRVTKIADFGAFIELaeGI--EGLAHISEFS--WVKktsKPSDMVKIGDEVECMILGYDIQAGRVSLGLKQVTANP 655
Cdd:COG2183  644 ILEGTVTNVTDFGAFVDI--GVhqDGLVHISQLSdrFVK---DPREVVKVGDIVKVKVLEVDLKRKRISLSMKLDDEAG 717
S1_IF2_alpha cd04452
S1_IF2_alpha: The alpha subunit of translation Initiation Factor 2, S1-like RNA-binding domain. ...
493-562 1.77e-08

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


Pssm-ID: 239899 [Multi-domain]  Cd Length: 76  Bit Score: 51.82  E-value: 1.77e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 374680314 493 IEDSVSGVVKSFTSFGAFIDL---GGFDGLLHVNDMSWGHVARPREFVKKGQTIELKVIRLDQAEKRINLSLK 562
Cdd:cd04452    3 EGELVVVTVKSIADMGAYVSLleyGNIEGMILLSELSRRRIRSIRKLVKVGRKEVVKVIRVDKEKGYIDLSKK 75
S1_RPS1_repeat_ec3 cd05688
S1_RPS1_repeat_ec3: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
752-823 2.26e-08

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: 51.48  E-value: 2.26e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 374680314 752 VGSTVEGEVSSVTDFGIFVRVpGGVEGLVRKQHLVENRDGDPGEALRkyaVGDRVKAVIVDMNVKDRKVAFS 823
Cdd:cd05688    1 EGDVVEGTVKSITDFGAFVDL-GGVDGLLHISDMSWGRVKHPSEVVN---VGDEVEVKVLKIDKERKRISLG 68
S1_RPS1_repeat_ec1_hs1 cd05687
S1_RPS1_repeat_ec1_hs1: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
580-646 3.05e-08

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


Pssm-ID: 240192 [Multi-domain]  Cd Length: 70  Bit Score: 50.99  E-value: 3.05e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 374680314 580 DVVKGRVTKIADFGAFIELAEGIEGLAHISEFSWvKKTSKPSDMVKIGDEVECMILGYDIQAGRVSL 646
Cdd:cd05687    2 DIVKGTVVSVDDDEVLVDIGYKSEGIIPISEFSD-DPIENGEDEVKVGDEVEVYVLRVEDEEGNVVL 67
S1_Rrp5_repeat_hs5 cd05697
S1_Rrp5_repeat_hs5: Rrp5 is a trans-acting factor important for biogenesis of both the 40S and ...
753-820 1.08e-07

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


Pssm-ID: 240202 [Multi-domain]  Cd Length: 69  Bit Score: 49.54  E-value: 1.08e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 374680314 753 GSTVEGEVSSVTDFGIFVRVPGGVEGLVRKQHLVENRDGDPgeaLRKYAVGDRVKAVIVDMNVKDRKV 820
Cdd:cd05697    1 GQVVKGTIRKLRPSGIFVKLSDHIKGLVPPMHLADVRLKHP---EKKFKPGLKVKCRVLSVEPERKRL 65
S1_pNO40 cd05686
S1_pNO40: pNO40 , S1-like RNA-binding domain. pNO40 is a nucleolar protein of unknown function ...
757-823 1.23e-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: 49.40  E-value: 1.23e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 374680314 757 EGEVSSVTDFGIFVRVPG-GVEGLVRKQHLVENRDGDPGEALRkyaVGDRVKAVIVDMNVKDR-KVAFS 823
Cdd:cd05686    8 KGEVASVTEYGAFVKIPGcRKQGLVHKSHMSSCRVDDPSEVVD---VGEKVWVKVIGREMKDKmKLSLS 73
S1_PNPase cd04472
S1_PNPase: Polynucleotide phosphorylase (PNPase), ), S1-like RNA-binding domain. PNPase is a ...
499-560 1.31e-07

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


Pssm-ID: 239918 [Multi-domain]  Cd Length: 68  Bit Score: 49.46  E-value: 1.31e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 374680314 499 GVVKSFTSFGAFID-LGGFDGLLHVNDMSWGHVARPREFVKKGQTIELKVIRLDQaEKRINLS 560
Cdd:cd04472    6 GKVVKIKDFGAFVEiLPGKDGLVHISELSDERVEKVEDVLKVGDEVKVKVIEVDD-RGRISLS 67
S1_RPS1_repeat_ec6 cd05691
S1_RPS1_repeat_ec6: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
579-651 2.06e-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: 48.81  E-value: 2.06e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 374680314 579 NDVVKGRVTKIADFGAFIELAEGIEGLAHISEFSWVKKTSKPSdMVKIGDEVECMILGYDIQAGRVSLGLKQV 651
Cdd:cd05691    1 GSIVTGKVTEVDAKGATVKLGDGVEGFLRAAELSRDRVEDATE-RFKVGDEVEAKITNVDRKNRKISLSIKAK 72
PRK08059 PRK08059
general stress protein 13; Validated
750-859 5.77e-07

general stress protein 13; Validated


Pssm-ID: 181215 [Multi-domain]  Cd Length: 123  Bit Score: 49.27  E-value: 5.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 750 YGVGSTVEGEVSSVTDFGIFVRVPGGVEGLVrkqHLVENRDG---DPGEALrkyAVGDRVKAVIVDMNVKDRKVAFSVRD 826
Cdd:PRK08059   5 YEVGSVVTGKVTGIQPYGAFVALDEETQGLV---HISEITHGfvkDIHDFL---SVGDEVKVKVLSVDEEKGKISLSIRA 78
                         90       100       110
                 ....*....|....*....|....*....|...
gi 374680314 827 YQRKVQRDELSRYMSAPRGEDEGSFTLGDLMRQ 859
Cdd:PRK08059  79 TEEAPEAKRKKGKILIPNPSEQGFNTLRDKLEE 111
VacB COG0557
Exoribonuclease R [Transcription];
752-822 6.79e-07

Exoribonuclease R [Transcription];


Pssm-ID: 440323 [Multi-domain]  Cd Length: 711  Bit Score: 53.19  E-value: 6.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 752 VGSTVEGEVSSVTDFGIFVRVPG-GVEGLV--------------RKQHLVENRDGdpgealRKYAVGDRVKAVIVDMNVK 816
Cdd:COG0557  622 VGEEFEGVISGVTSFGLFVELDElGVEGLVhvsslgddyyeydeRRQALVGERTG------KRYRLGDRVEVRVVRVDLD 695

                 ....*.
gi 374680314 817 DRKVAF 822
Cdd:COG0557  696 RRQIDF 701
S1_pNO40 cd05686
S1_pNO40: pNO40 , S1-like RNA-binding domain. pNO40 is a nucleolar protein of unknown function ...
499-562 7.42e-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: 47.48  E-value: 7.42e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 374680314 499 GVVKSFTSFGAFIDLGGF--DGLLHVNDMSWGHVARPREFVKKGQTIELKVIRLDQAEKrINLSLK 562
Cdd:cd05686    9 GEVASVTEYGAFVKIPGCrkQGLVHKSHMSSCRVDDPSEVVDVGEKVWVKVIGREMKDK-MKLSLS 73
PRK07400 PRK07400
30S ribosomal protein S1; Reviewed
576-825 1.23e-06

30S ribosomal protein S1; Reviewed


Pssm-ID: 180960 [Multi-domain]  Cd Length: 318  Bit Score: 51.34  E-value: 1.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 576 FGVNDVVKGRVTKIADFGAFIELAEGIEGLAHISEFSwVKKTSKPSDMVKIGDEVECMILGYDIQAGRVSLGLKQVT-AN 654
Cdd:PRK07400  29 FKPGDIVNGTVFSLEPRGALIDIGAKTAAFMPIQEMS-INRVEGPEEVLQPNETREFFILSDENEDGQLTLSIRRIEyMR 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 655 PWEEIEARYPVGARfTRRIVKVTNAGAFIEMEEGIDGFLHVDDLSwvkrTRPADHELeVGKEIECMVIECDPQARRIRLG 734
Cdd:PRK07400 108 AWERVRQLQKEDAT-VRSEVFATNRGGALVRIEGLRGFIPGSHIS----TRKPKEEL-VGEELPLKFLEVDEERNRLVLS 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 735 VKQ-LSDNPwqvfANAYGVGSTVEGEVSSVTDFGIFVRVpGGVEGLVRKQHLVENRDGDPGEALRkyaVGDRVKAVIVDM 813
Cdd:PRK07400 182 HRRaLVERK----MNRLEVGEVVVGTVRGIKPYGAFIDI-GGVSGLLHISEISHEHIETPHSVFN---VNDEMKVMIIDL 253
                        250
                 ....*....|..
gi 374680314 814 NVKDRKVAFSVR 825
Cdd:PRK07400 254 DAERGRISLSTK 265
S1_RPS1_repeat_hs4 cd05692
S1_RPS1_repeat_hs4: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
666-736 1.30e-06

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


Pssm-ID: 240197 [Multi-domain]  Cd Length: 69  Bit Score: 46.51  E-value: 1.30e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 374680314 666 GARFTRRIVKVTNAGAFIEMEEGIDGFLHVDDLSWVKRTRPADHeLEVGKEIECMVIECDPQArRIRLGVK 736
Cdd:cd05692    1 GSVVEGTVTRLKPFGAFVELGGGISGLVHISQIAHKRVKDVKDV-LKEGDKVKVKVLSIDARG-RISLSIK 69
S1_Rrp5_repeat_hs8_sc7 cd04461
S1_Rrp5_repeat_hs8_sc7: Rrp5 Homo sapiens S1 repeat 8 (hs8) and Saccharomyces cerevisiae S1 ...
752-823 1.55e-06

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


Pssm-ID: 239908 [Multi-domain]  Cd Length: 83  Bit Score: 46.81  E-value: 1.55e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 374680314 752 VGSTVEGEVSSVTDFGIFVRVPGGVEGLVRKQHLVENRDGDPGEAlrkYAVGDRVKAVIVDMNVKDRKVAFS 823
Cdd:cd04461   14 PGMVVHGYVRNITPYGVFVEFLGGLTGLAPKSYISDEFVTDPSFG---FKKGQSVTAKVTSVDEEKQRFLLS 82
S1 smart00316
Ribosomal protein S1-like RNA-binding domain;
320-373 1.99e-06

Ribosomal protein S1-like RNA-binding domain;


Pssm-ID: 197648 [Multi-domain]  Cd Length: 72  Bit Score: 46.06  E-value: 1.99e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 374680314   320 EPGSVRMGTVVQVNAGTVFVDIGGKSEGRVPVEEF--------EAPPKAGDGVRVYVERVTP 373
Cdd:smart00316   1 EVGDVVEGTVTEITPGGAFVDLGNGVEGLIPISELsdkrvkdpEEVLKVGDEVKVKVLSVDE 62
S1_RPS1_repeat_ec6 cd05691
S1_RPS1_repeat_ec6: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
666-738 2.14e-06

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


Pssm-ID: 240196 [Multi-domain]  Cd Length: 73  Bit Score: 46.11  E-value: 2.14e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 374680314 666 GARFTRRIVKVTNAGAFIEMEEGIDGFLHVDDLSwVKRTRPADHELEVGKEIECMVIECDPQARRIRLGVKQL 738
Cdd:cd05691    1 GSIVTGKVTEVDAKGATVKLGDGVEGFLRAAELS-RDRVEDATERFKVGDEVEAKITNVDRKNRKISLSIKAK 72
PLN00207 PLN00207
polyribonucleotide nucleotidyltransferase; Provisional
586-631 2.46e-06

polyribonucleotide nucleotidyltransferase; Provisional


Pssm-ID: 215104 [Multi-domain]  Cd Length: 891  Bit Score: 51.43  E-value: 2.46e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 374680314 586 VTKIADFGAFIELAEGIEGLAHISEFS--WVkktSKPSDMVKIGDEVE 631
Cdd:PLN00207 762 IKSIAPYGAFVEIAPGREGLCHISELSsnWL---AKPEDAFKVGDRID 806
S1_RPS1_repeat_ec6 cd05691
S1_RPS1_repeat_ec6: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
497-562 2.57e-06

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


Pssm-ID: 240196 [Multi-domain]  Cd Length: 73  Bit Score: 45.72  E-value: 2.57e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 374680314 497 VSGVVKSFTSFGAFIDLG-GFDGLLHVNDMSWGHVARPREFVKKGQTIELKVIRLDQAEKRINLSLK 562
Cdd:cd05691    4 VTGKVTEVDAKGATVKLGdGVEGFLRAAELSRDRVEDATERFKVGDEVEAKITNVDRKNRKISLSIK 70
PRK08582 PRK08582
RNA-binding protein S1;
752-846 2.76e-06

RNA-binding protein S1;


Pssm-ID: 236305 [Multi-domain]  Cd Length: 139  Bit Score: 47.72  E-value: 2.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 752 VGSTVEGEVSSVTDFGIFVRVPGGVEGLVrkqHLVENRDG---DPGEALRkyaVGDRVKaVIVdMNV-KDRKVAFSVRDY 827
Cdd:PRK08582   5 VGSKLQGKVTGITNFGAFVELPEGKTGLV---HISEVADNyvkDINDHLK---VGDEVE-VKV-LNVeDDGKIGLSIKKA 76
                         90
                 ....*....|....*....
gi 374680314 828 QRKVQRDELSRYMSAPRGE 846
Cdd:PRK08582  77 KDRPKRQHDRPRHEDNRGG 95
S1_Rrp5_repeat_hs6_sc5 cd05698
S1_Rrp5_repeat_hs6_sc5: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ...
673-736 3.20e-06

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


Pssm-ID: 240203 [Multi-domain]  Cd Length: 70  Bit Score: 45.29  E-value: 3.20e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 374680314 673 IVKVTNAGAFIEMEEGIDGFLHVDDLSWVKRTRPADHeLEVGKEIECMVIECDPQARRIRLGVK 736
Cdd:cd05698    8 IVKVKPNGCIVSFYNNVKGFLPKSELSEAFIKDPEEH-FRVGQVVKVKVLSCDPEQQRLLLSCK 70
PRK07400 PRK07400
30S ribosomal protein S1; Reviewed
495-742 4.16e-06

30S ribosomal protein S1; Reviewed


Pssm-ID: 180960 [Multi-domain]  Cd Length: 318  Bit Score: 49.80  E-value: 4.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 495 DSVSGVVKSFTSFGAFIDLGG-FDGLLHVNDMSWGHVARPREFVKKGQTIELKVIRLDQAEKRINLSLKHFQPDPWLEFE 573
Cdd:PRK07400  33 DIVNGTVFSLEPRGALIDIGAkTAAFMPIQEMSINRVEGPEEVLQPNETREFFILSDENEDGQLTLSIRRIEYMRAWERV 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 574 NKFGVND-VVKGRVTKIADFGAFIELaEGIEGL---AHISefswvkkTSKPSDMVkIGDEVECMILGYDIQAGRVSLGLK 649
Cdd:PRK07400 113 RQLQKEDaTVRSEVFATNRGGALVRI-EGLRGFipgSHIS-------TRKPKEEL-VGEELPLKFLEVDEERNRLVLSHR 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 650 QVTAnpwEEIEARYPVGARFTRRIVKVTNAGAFIEMEeGIDGFLHVDDLSWVKRTRPadHE-LEVGKEIECMVIECDPQA 728
Cdd:PRK07400 184 RALV---ERKMNRLEVGEVVVGTVRGIKPYGAFIDIG-GVSGLLHISEISHEHIETP--HSvFNVNDEMKVMIIDLDAER 257
                        250
                 ....*....|....
gi 374680314 729 RRIRLGVKQLSDNP 742
Cdd:PRK07400 258 GRISLSTKQLEPEP 271
S1_RPS1_repeat_ec4 cd05689
S1_RPS1_repeat_ec4: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
497-559 5.09e-06

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


Pssm-ID: 240194 [Multi-domain]  Cd Length: 72  Bit Score: 44.88  E-value: 5.09e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 374680314 497 VSGVVKSFTSFGAFIDLG-GFDGLLHVNDMSWGHV-ARPREFVKKGQTIELKVIRLDQAEKRINL 559
Cdd:cd05689    7 LFGKVTNLTDYGCFVELEeGVEGLVHVSEMDWTNKnIHPSKVVSLGDEVEVMVLDIDEERRRISL 71
PRK08563 PRK08563
DNA-directed RNA polymerase subunit E'; Provisional
756-825 5.93e-06

DNA-directed RNA polymerase subunit E'; Provisional


Pssm-ID: 236289 [Multi-domain]  Cd Length: 187  Bit Score: 47.51  E-value: 5.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 756 VEGEVSSVTDFGIFVRVpGGVEGLVRKQHLV-ENRDGDP------GEALRKY-AVGDRVKAVIVDMNVKDR-----KVAF 822
Cdd:PRK08563  85 VEGEVVEVVEFGAFVRI-GPVDGLLHISQIMdDYISYDPkngrliGKESKRVlKVGDVVRARIVAVSLKERrprgsKIGL 163

                 ...
gi 374680314 823 SVR 825
Cdd:PRK08563 164 TMR 166
PRK11824 PRK11824
polynucleotide phosphorylase/polyadenylase; Provisional
752-826 7.92e-06

polynucleotide phosphorylase/polyadenylase; Provisional


Pssm-ID: 236995 [Multi-domain]  Cd Length: 693  Bit Score: 49.66  E-value: 7.92e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 374680314 752 VGSTVEGEVSSVTDFGIFVRVPGGVEGLVRKQHLVENRDGDPGEALRkyaVGDRVKAVIVDMNvKDRKVAFSVRD 826
Cdd:PRK11824 621 VGEIYEGKVVRIVDFGAFVEILPGKDGLVHISEIADERVEKVEDVLK---EGDEVKVKVLEID-KRGRIRLSRKA 691
S1_RpoE cd04460
S1_RpoE: RpoE, S1-like RNA-binding domain. S1-like RNA-binding domains are found in a wide ...
756-825 8.78e-06

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


Pssm-ID: 239907 [Multi-domain]  Cd Length: 99  Bit Score: 44.97  E-value: 8.78e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 756 VEGEVSSVTDFGIFVRVpGGVEGLVRKQHLVENR-DGDP------GEALRK-YAVGDRVKAVIVDMNVKDR-----KVAF 822
Cdd:cd04460    3 VEGEVVEVVDFGAFVRI-GPVDGLLHISQIMDDYiSYDPknkrliGEETKRvLKVGDVVRARIVAVSLKERrpresKIGL 81

                 ...
gi 374680314 823 SVR 825
Cdd:cd04460   82 TMR 84
PLN00207 PLN00207
polyribonucleotide nucleotidyltransferase; Provisional
501-568 1.37e-05

polyribonucleotide nucleotidyltransferase; Provisional


Pssm-ID: 215104 [Multi-domain]  Cd Length: 891  Bit Score: 49.12  E-value: 1.37e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 374680314 501 VKSFTSFGAFIDLG-GFDGLLHVNDMSWGHVARPREFVKKGQTIELKVIRLDQaEKRINLSLKHFQPDP 568
Cdd:PLN00207 762 IKSIAPYGAFVEIApGREGLCHISELSSNWLAKPEDAFKVGDRIDVKLIEVND-KGQLRLSRRALLPEA 829
S1 pfam00575
S1 RNA binding domain; The S1 domain occurs in a wide range of RNA associated proteins. It is ...
319-371 1.45e-05

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


Pssm-ID: 425760 [Multi-domain]  Cd Length: 72  Bit Score: 43.82  E-value: 1.45e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 374680314  319 PEPGSVRMGTVVQVNAGTVFVDIGGKSEGRVPVEEFEAP--------PKAGDGVRVYVERV 371
Cdd:pfam00575   1 PEKGDVVEGEVTRVTKGGAFVDLGNGVEGFIPISELSDDhvedpdevIKVGDEVKVKVLKV 61
S1_PNPase cd04472
S1_PNPase: Polynucleotide phosphorylase (PNPase), ), S1-like RNA-binding domain. PNPase is a ...
753-818 1.65e-05

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


Pssm-ID: 239918 [Multi-domain]  Cd Length: 68  Bit Score: 43.30  E-value: 1.65e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 374680314 753 GSTVEGEVSSVTDFGIFVRVPGGVEGLVRKQHLVENRDGDPGEALrkyAVGDRVKAVIVDMNVKDR 818
Cdd:cd04472    1 GKIYEGKVVKIKDFGAFVEILPGKDGLVHISELSDERVEKVEDVL---KVGDEVKVKVIEVDDRGR 63
PRK04182 PRK04182
cytidylate kinase; Provisional
35-70 1.78e-05

cytidylate kinase; Provisional


Pssm-ID: 235244 [Multi-domain]  Cd Length: 180  Bit Score: 45.95  E-value: 1.78e-05
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 374680314  35 VIIALDGPAGSGKSSVCRLLASRLGAQCLNTGSFYR 70
Cdd:PRK04182   1 MIITISGPPGSGKTTVARLLAEKLGLKHVSAGEIFR 36
S1_Rrp5_repeat_hs11_sc8 cd05702
S1_Rrp5_repeat_hs11_sc8: Rrp5 is a trans-acting factor important for biogenesis of both the ...
580-636 2.22e-05

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


Pssm-ID: 240207 [Multi-domain]  Cd Length: 70  Bit Score: 42.96  E-value: 2.22e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 374680314 580 DVVKGRVTKIADFGAFIELAEGIEGLAHISE-FSWVKKTSKPSDMVKIGDEVECMILG 636
Cdd:cd05702    2 DLVKAKVKSVKPTQLNVQLADNVHGRIHVSEvFDEWPDGKNPLSKFKIGQKIKARVIG 59
S1_Rrp5_repeat_hs5 cd05697
S1_Rrp5_repeat_hs5: Rrp5 is a trans-acting factor important for biogenesis of both the 40S and ...
580-648 2.98e-05

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


Pssm-ID: 240202 [Multi-domain]  Cd Length: 69  Bit Score: 42.61  E-value: 2.98e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 374680314 580 DVVKGRVTKIADFGAFIELAEGIEGLAHISEFSWVKKTsKPSDMVKIGDEVECMILGYDIQAGRVSLGL 648
Cdd:cd05697    2 QVVKGTIRKLRPSGIFVKLSDHIKGLVPPMHLADVRLK-HPEKKFKPGLKVKCRVLSVEPERKRLVLTL 69
PTZ00248 PTZ00248
eukaryotic translation initiation factor 2 subunit 1; Provisional
572-663 3.00e-05

eukaryotic translation initiation factor 2 subunit 1; Provisional


Pssm-ID: 240329 [Multi-domain]  Cd Length: 319  Bit Score: 46.97  E-value: 3.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 572 FENKF-GVNDVVKGRVTKIADFGAFIELAE--GIEGLAHISEFSWVKKTSKPSdMVKIGDEVECMILGYDIQAGRVSLGL 648
Cdd:PTZ00248  10 YEQKFpEEDDLVMVKVVRITEMGAYVSLLEydDIEGMILMSELSKRRIRSINK-LIRVGRHEVVVVLRVDKEKGYIDLSK 88
                         90
                 ....*....|....*
gi 374680314 649 KQVTANPWEEIEARY 663
Cdd:PTZ00248  89 KRVSPEDIEACEEKF 103
S1_RPS1_repeat_ec4 cd05689
S1_RPS1_repeat_ec4: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
750-822 3.73e-05

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: 42.56  E-value: 3.73e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 374680314 750 YGVGSTVEGEVSSVTDFGIFVRVPGGVEGLVrkqHLVE----NRDGDPGEALrkyAVGDRVKAVIVDMNVKDRKVAF 822
Cdd:cd05689    1 YPEGTRLFGKVTNLTDYGCFVELEEGVEGLV---HVSEmdwtNKNIHPSKVV---SLGDEVEVMVLDIDEERRRISL 71
S1_PNPase cd04472
S1_PNPase: Polynucleotide phosphorylase (PNPase), ), S1-like RNA-binding domain. PNPase is a ...
666-733 4.24e-05

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: 42.14  E-value: 4.24e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 374680314 666 GARFTRRIVKVTNAGAFIEMEEGIDGFLHVDDLSwVKRTRPADHELEVGKEIECMVIECDPQArRIRL 733
Cdd:cd04472    1 GKIYEGKVVKIKDFGAFVEILPGKDGLVHISELS-DERVEKVEDVLKVGDEVKVKVIEVDDRG-RISL 66
S1_NusA cd04455
S1_NusA: N-utilizing substance A protein (NusA), S1-like RNA-binding domain. S1-like ...
322-378 4.57e-05

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: 42.04  E-value: 4.57e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 374680314 322 GSVRMGTVVQVNAGTVFVDIGG------KSEgRVPVEEFeappKAGDGVRVYVERV--TPYGPEL 378
Cdd:cd04455    4 GEIVTGIVKRVDRGNVIVDLGKveailpKKE-QIPGESY----RPGDRIKAYVLEVrkTSKGPQI 63
S1_DHX8_helicase cd05684
S1_DHX8_helicase: The N-terminal S1 domain of human ATP-dependent RNA helicase DHX8, a DEAH ...
753-826 5.10e-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: 42.23  E-value: 5.10e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 374680314 753 GSTVEGEVSSVTDFGIFVR---VPGGVEGLVR-KQHLVENRDGDPGEALRKyavGDRVKaVIVdMNVKDRKVAFSVRD 826
Cdd:cd05684    1 GKIYKGKVTSIMDFGCFVQlegLKGRKEGLVHiSQLSFEGRVANPSDVVKR---GQKVK-VKV-ISIQNGKISLSMKD 73
PRK08582 PRK08582
RNA-binding protein S1;
490-562 6.36e-05

RNA-binding protein S1;


Pssm-ID: 236305 [Multi-domain]  Cd Length: 139  Bit Score: 43.87  E-value: 6.36e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 374680314 490 SVHIEDSVSGVVKSFTSFGAFIDL-GGFDGLLHVNDMSWGHVARPREFVKKGQTIELKVIRLDQAEKrINLSLK 562
Cdd:PRK08582   2 SIEVGSKLQGKVTGITNFGAFVELpEGKTGLVHISEVADNYVKDINDHLKVGDEVEVKVLNVEDDGK-IGLSIK 74
PRK08059 PRK08059
general stress protein 13; Validated
661-742 6.45e-05

general stress protein 13; Validated


Pssm-ID: 181215 [Multi-domain]  Cd Length: 123  Bit Score: 43.11  E-value: 6.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 661 ARYPVGARFTRRIVKVTNAGAFIEMEEGIDGFLHVDDLS--WVKRTRpaDHeLEVGKEIECMVIECDPQARRIRLGVKQL 738
Cdd:PRK08059   3 SQYEVGSVVTGKVTGIQPYGAFVALDEETQGLVHISEIThgFVKDIH--DF-LSVGDEVKVKVLSVDEEKGKISLSIRAT 79

                 ....
gi 374680314 739 SDNP 742
Cdd:PRK08059  80 EEAP 83
S1_Rrp5_repeat_hs6_sc5 cd05698
S1_Rrp5_repeat_hs6_sc5: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ...
499-562 8.14e-05

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


Pssm-ID: 240203 [Multi-domain]  Cd Length: 70  Bit Score: 41.44  E-value: 8.14e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 374680314 499 GVVKSFTSFGAFID-LGGFDGLLHVNDMSWGHVARPREFVKKGQTIELKVIRLDQAEKRINLSLK 562
Cdd:cd05698    6 GTIVKVKPNGCIVSfYNNVKGFLPKSELSEAFIKDPEEHFRVGQVVKVKVLSCDPEQQRLLLSCK 70
S1_RPS1_repeat_ec1_hs1 cd05687
S1_RPS1_repeat_ec1_hs1: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
495-562 9.70e-05

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: 41.36  E-value: 9.70e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 374680314 495 DSVSGVVKSFTSFGAFIDLGG-FDGLLHVNDMSWGHVARPREFVKKGQTIELKVIRLDQAEKRINLSLK 562
Cdd:cd05687    2 DIVKGTVVSVDDDEVLVDIGYkSEGIIPISEFSDDPIENGEDEVKVGDEVEVYVLRVEDEEGNVVLSKR 70
S1_IF2_alpha cd04452
S1_IF2_alpha: The alpha subunit of translation Initiation Factor 2, S1-like RNA-binding domain. ...
672-737 2.79e-04

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


Pssm-ID: 239899 [Multi-domain]  Cd Length: 76  Bit Score: 40.26  E-value: 2.79e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 672 RIVKVTNAGAFIEMEE--GIDGFLHVDDLS--WVKRTRpaDHeLEVGKEIECMVIECDPQARRIRLGVKQ 737
Cdd:cd04452   10 TVKSIADMGAYVSLLEygNIEGMILLSELSrrRIRSIR--KL-VKVGRKEVVKVIRVDKEKGYIDLSKKR 76
S1 smart00316
Ribosomal protein S1-like RNA-binding domain;
397-460 2.82e-04

Ribosomal protein S1-like RNA-binding domain;


Pssm-ID: 197648 [Multi-domain]  Cd Length: 72  Bit Score: 39.89  E-value: 2.82e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 374680314   397 RDGTPVEGRIVRLTekKSGFEVDLGAGMMAFLPISQSDCQKVDAPES--LIGLTSKFYIERISQSK 460
Cdd:smart00316   1 EVGDVVEGTVTEIT--PGGAFVDLGNGVEGLIPISELSDKRVKDPEEvlKVGDEVKVKVLSVDEEK 64
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
30-61 3.72e-04

Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway/BioSystem: Pyrimidine salvage


Pssm-ID: 440337 [Multi-domain]  Cd Length: 206  Bit Score: 42.52  E-value: 3.72e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 374680314  30 RPMGTVIIALDGPAGSGKSSVCRLLASRLGAQ 61
Cdd:COG0572    3 RSGKPRIIGIAGPSGSGKTTFARRLAEQLGAD 34
S1_pNO40 cd05686
S1_pNO40: pNO40 , S1-like RNA-binding domain. pNO40 is a nucleolar protein of unknown function ...
578-649 4.53e-04

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


Pssm-ID: 240191 [Multi-domain]  Cd Length: 73  Bit Score: 39.39  E-value: 4.53e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 374680314 578 VNDVVKGRVTKIADFGAFIELaEGI--EGLAHISEFSwVKKTSKPSDMVKIGDEVECMILGYDIQaGRVSLGLK 649
Cdd:cd05686    3 LYQIFKGEVASVTEYGAFVKI-PGCrkQGLVHKSHMS-SCRVDDPSEVVDVGEKVWVKVIGREMK-DKMKLSLS 73
S1_RecJ_like cd04473
S1_RecJ_like: The S1 domain of the archaea-specific RecJ-like exonuclease. The function of ...
752-806 5.11e-04

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


Pssm-ID: 239919 [Multi-domain]  Cd Length: 77  Bit Score: 39.51  E-value: 5.11e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 374680314 752 VGSTVEGEVSSVTDFGIFVRVPGGVEGLVRKQHLvenrdgdpgeaLRKYAVGDRV 806
Cdd:cd04473   16 VGKLYKGKVNGVAKYGVFVDLNDHVRGLIHRSNL-----------LRDYEVGDEV 59
S1_RPS1_repeat_ec2_hs2 cd04465
S1_RPS1_repeat_ec2_hs2: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
497-560 5.16e-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: 5.16e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 374680314 497 VSGVVKSFTSFGAFIDLGGFDGLLHVNDMSWGHVARPREFVkkGQTIELKVIRLDQAEKRINLS 560
Cdd:cd04465    4 VEGKVTEKVKGGLIVDIEGVRAFLPASQVDLRPVEDLDEYV--GKELKFKIIEIDRERNNIVLS 65
S1_Tex cd05685
S1_Tex: The C-terminal S1 domain of a transcription accessory factor called Tex, which has ...
666-733 5.49e-04

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: 39.14  E-value: 5.49e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 374680314 666 GARFTRRIVKVTNAGAFIEMEEGIDGFLHVDDLSWVKRTRPADhELEVGKEIECMVIECDPQARRIRL 733
Cdd:cd05685    1 GMVLEGVVTNVTDFGAFVDIGVKQDGLIHISKMADRFVSHPSD-VVSVGDIVEVKVISIDEERGRISL 67
PRK03987 PRK03987
translation initiation factor IF-2 subunit alpha; Validated
675-741 5.81e-04

translation initiation factor IF-2 subunit alpha; Validated


Pssm-ID: 235188 [Multi-domain]  Cd Length: 262  Bit Score: 42.50  E-value: 5.81e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 374680314 675 KVTNAGAFIEMEE--GIDGFLHVDDLS--WVKRTRpaDHeLEVGKEIECMVIECDPQARRIRLGVKQLSDN 741
Cdd:PRK03987  18 EVKDFGAFVTLDEypGKEGFIHISEVAsgWVKNIR--DH-VKEGQKVVCKVIRVDPRKGHIDLSLKRVNEH 85
PRK08582 PRK08582
RNA-binding protein S1;
665-742 5.91e-04

RNA-binding protein S1;


Pssm-ID: 236305 [Multi-domain]  Cd Length: 139  Bit Score: 40.79  E-value: 5.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 665 VGARFTRRIVKVTNAGAFIEMEEGIDGFLHVDDLS--WVKRTrpADHeLEVGKEIECMVIECDpQARRIRLGVKQLSDNP 742
Cdd:PRK08582   5 VGSKLQGKVTGITNFGAFVELPEGKTGLVHISEVAdnYVKDI--NDH-LKVGDEVEVKVLNVE-DDGKIGLSIKKAKDRP 80
S1_RPS1_repeat_ec1_hs1 cd05687
S1_RPS1_repeat_ec1_hs1: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
753-825 6.52e-04

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


Pssm-ID: 240192 [Multi-domain]  Cd Length: 70  Bit Score: 39.05  E-value: 6.52e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 374680314 753 GSTVEGEVSSVTDFGIFVRVPGGVEGLVRKQHLVENRDGDPGEALrkyAVGDRVKAVIVDMNVKDRKVAFSVR 825
Cdd:cd05687    1 GDIVKGTVVSVDDDEVLVDIGYKSEGIIPISEFSDDPIENGEDEV---KVGDEVEVYVLRVEDEEGNVVLSKR 70
S1_RNase_E cd04453
S1_RNase_E: RNase E and RNase G, S1-like RNA-binding domain. RNase E is an essential ...
573-630 6.94e-04

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


Pssm-ID: 239900 [Multi-domain]  Cd Length: 88  Bit Score: 39.50  E-value: 6.94e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 374680314 573 ENKFGVNDVVKGRVTKIADF--GAFIELAEGIEGLAHISEFSWV--KKTSKPSDMVKIGDEV 630
Cdd:cd04453    2 NREPIVGNIYLGRVKKIVPGlqAAFVDIGLGKNGFLHLSDILPAyfKKHKKIAKLLKEGQEI 63
rpoE TIGR00448
DNA-directed RNA polymerase (rpoE), archaeal and eukaryotic form; This family seems to be ...
753-819 6.98e-04

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


Pssm-ID: 129540 [Multi-domain]  Cd Length: 179  Bit Score: 41.31  E-value: 6.98e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 374680314  753 GSTVEGEVSSVTDFGIFVRVpGGVEGLVRKQHLVEnrDG---DP------GEALRKY-AVGDRVKAVIVDMNVKDRK 819
Cdd:TIGR00448  82 GEIVEGEVIEIVEFGAFVSL-GPFDGLFHVSQVTD--DYcyyDPkesaliGKETKKVlDEGDKVRARIVALSLKDRR 155
S1_Rrp5_repeat_hs8_sc7 cd04461
S1_Rrp5_repeat_hs8_sc7: Rrp5 Homo sapiens S1 repeat 8 (hs8) and Saccharomyces cerevisiae S1 ...
578-648 1.37e-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: 38.34  E-value: 1.37e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 374680314 578 VNDVVKGRVTKIADFGAFIELAEGIEGLAHISEFSwVKKTSKPSDMVKIGDEVECMILGYDIQAGRVSLGL 648
Cdd:cd04461   14 PGMVVHGYVRNITPYGVFVEFLGGLTGLAPKSYIS-DEFVTDPSFGFKKGQSVTAKVTSVDEEKQRFLLSL 83
S1_Rrp5_repeat_hs5 cd05697
S1_Rrp5_repeat_hs5: Rrp5 is a trans-acting factor important for biogenesis of both the 40S and ...
673-733 1.47e-03

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


Pssm-ID: 240202 [Multi-domain]  Cd Length: 69  Bit Score: 37.99  E-value: 1.47e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 374680314 673 IVKVTNAGAFIEMEEGIDGFLHVDDLSWVKRTRPaDHELEVGKEIECMVIECDPQARRIRL 733
Cdd:cd05697    8 IRKLRPSGIFVKLSDHIKGLVPPMHLADVRLKHP-EKKFKPGLKVKCRVLSVEPERKRLVL 67
S1_RNase_R cd04471
S1_RNase_R: RNase R C-terminal S1 domain. RNase R is a processive 3' to 5' exoribonuclease, ...
578-648 1.88e-03

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


Pssm-ID: 239917 [Multi-domain]  Cd Length: 83  Bit Score: 38.15  E-value: 1.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 374680314 578 VNDVVKGRVTKIADFGAFIELAE-GIEGLAHISEFS---WV----------KKTSKpsdMVKIGDEVECMILGYDIQAGR 643
Cdd:cd04471    1 VGEEFDGVISGVTSFGLFVELDNlTVEGLVHVSTLGddyYEfdeenhalvgERTGK---VFRLGDKVKVRVVRVDLDRRK 77

                 ....*
gi 374680314 644 VSLGL 648
Cdd:cd04471   78 IDFEL 82
S1_Rrp5_repeat_hs6_sc5 cd05698
S1_Rrp5_repeat_hs6_sc5: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ...
753-825 3.51e-03

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


Pssm-ID: 240203 [Multi-domain]  Cd Length: 70  Bit Score: 36.82  E-value: 3.51e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 374680314 753 GSTVEGEVSSVTDFGIFVRVPGGVEGLVRKQHLVENRDGDPGEALRkyaVGDRVKAVIVDMNVKDRKVAFSVR 825
Cdd:cd05698    1 GLKTHGTIVKVKPNGCIVSFYNNVKGFLPKSELSEAFIKDPEEHFR---VGQVVKVKVLSCDPEQQRLLLSCK 70
nusA PRK09202
transcription elongation factor NusA; Validated
752-812 3.57e-03

transcription elongation factor NusA; Validated


Pssm-ID: 236410 [Multi-domain]  Cd Length: 470  Bit Score: 40.62  E-value: 3.57e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 374680314 752 VGSTVEGEVSSVTDFGIFVRVpGGVEGLVRKQHLVenrdgdPGEALRkyaVGDRVKAVIVD 812
Cdd:PRK09202 134 VGEIITGVVKRVERGNIIVDL-GRAEAILPRKEQI------PRENFR---PGDRVRAYVYE 184
S1_RpoE cd04460
S1_RpoE: RpoE, S1-like RNA-binding domain. S1-like RNA-binding domains are found in a wide ...
497-523 4.31e-03

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


Pssm-ID: 239907 [Multi-domain]  Cd Length: 99  Bit Score: 37.27  E-value: 4.31e-03
                         10        20
                 ....*....|....*....|....*..
gi 374680314 497 VSGVVKSFTSFGAFIDLGGFDGLLHVN 523
Cdd:cd04460    3 VEGEVVEVVDFGAFVRIGPVDGLLHIS 29
S1_RPS1_repeat_ec2_hs2 cd04465
S1_RPS1_repeat_ec2_hs2: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ...
672-731 5.26e-03

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


Pssm-ID: 239911 [Multi-domain]  Cd Length: 67  Bit Score: 36.28  E-value: 5.26e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 374680314 672 RIVKVTNAGaFIEMEEGIDGFL---HVDdlswVKRTRPADhELeVGKEIECMVIECDPQARRI 731
Cdd:cd04465    7 KVTEKVKGG-LIVDIEGVRAFLpasQVD----LRPVEDLD-EY-VGKELKFKIIEIDRERNNI 62
S1_RecJ_like cd04473
S1_RecJ_like: The S1 domain of the archaea-specific RecJ-like exonuclease. The function of ...
574-610 6.82e-03

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


Pssm-ID: 239919 [Multi-domain]  Cd Length: 77  Bit Score: 36.05  E-value: 6.82e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 374680314 574 NKFGVNDVV-----KGRVTKIADFGAFIELAEGIEGLAHISE 610
Cdd:cd04473    7 PACTMEDLEvgklyKGKVNGVAKYGVFVDLNDHVRGLIHRSN 48
PRK08563 PRK08563
DNA-directed RNA polymerase subunit E'; Provisional
497-523 7.28e-03

DNA-directed RNA polymerase subunit E'; Provisional


Pssm-ID: 236289 [Multi-domain]  Cd Length: 187  Bit Score: 38.65  E-value: 7.28e-03
                         10        20
                 ....*....|....*....|....*..
gi 374680314 497 VSGVVKSFTSFGAFIDLGGFDGLLHVN 523
Cdd:PRK08563  85 VEGEVVEVVEFGAFVRIGPVDGLLHIS 111
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH