|
Name |
Accession |
Description |
Interval |
E-value |
| VacB |
COG0557 |
Exoribonuclease R [Transcription]; |
17-715 |
0e+00 |
|
Exoribonuclease R [Transcription];
Pssm-ID: 440323 [Multi-domain] Cd Length: 711 Bit Score: 909.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446087495 17 YDNpipSRTLILDTLEQLQ-TPQSHAELVDHFHIQDQKSIEALSHRLSAMVRDGQLMKDGF-KFQLVADQPTYEATVYIN 94
Cdd:COG0557 1 YEN---SRETILAFLKEDAyKPLSKKELAKALGLKDEESREALKRRLRALEREGQLVKTRRgRYRLPEKLDLVEGRVRGH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446087495 95 SKGLGTAHID-GQDDLLLPERELRLVFNGDRVRVRQTSVDRKGKPWGFITEVIQHRVKQLIGKLSVHDGEYFIQPNNPNQ 173
Cdd:COG0557 78 RDGFGFVIPDdGEEDIFIPPRELNGALHGDRVLVRVTKEDRRGRPEGRVVEILERANTRVVGRFEKEKGFGFVVPDDKRL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446087495 174 HQPIPLEKElvEHAKANVGDMLRVAIDTYPTREEFATAHIIQSMADKADTEIIIPQTILEFGLPYEFPDEVIKEAESF-K 252
Cdd:COG0557 158 LQDIFIPPD--DLNGAKDGDLVVVEITRYPERRGPPEGRVVEVLGSPGDPGAEILIAIRKHGLPHEFPEEVLAEAEALpD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446087495 253 EPAEQDREGRVDLRDLALVTIDGEDARDFDDAVYAEKRPGGGYRVVVAIADVSHYVRLDSALNEEAEERGTSVYFPHFVL 332
Cdd:COG0557 236 EVPEADLKGRRDLRDLPLVTIDGEDAKDFDDAVSAEKLDNGGWRLGVHIADVSHYVRPGSALDREARKRGTSVYLPDRVI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446087495 333 PMLPEALSNGLCSLNPHVDRLCMVCDLKLSRTGRVTGYEFYPAVMHSKARLTYTQVGQYFEGATDAIP-KDRDIHKSLNT 411
Cdd:COG0557 316 PMLPERLSNGLCSLNPGEDRLAMSCEMEIDAKGEVVSYEFYRSVIRSDARLTYEEVQAILDGKDEELReEYADLVPMLEE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446087495 412 LFQLYQILKNLRVDRHAMEFETIETYMTFDELGGIKEILPRTRNDAHKLIEECMLLANVAAAEYALEHDIPMLYRVHEAP 491
Cdd:COG0557 396 LYELAKILRKAREKRGAIDFDLPETKIILDEEGKPEDIVPRERNDAHKLIEEFMLLANEAVAEFLEKLKLPFLYRVHEEP 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446087495 492 EFSRIQKVKDFVKLLGLPFP--DQPTQADYQKVIEATKDRIDAPSIHAVLLRSMMQAYYGAKNAGHYGLAYEAYTHFTSP 569
Cdd:COG0557 476 DPEKLEALREFLANLGLKLKggDEPTPKDLQKLLEQVKGRPEEELLNTLLLRSMKQAVYSPENIGHFGLALEAYTHFTSP 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446087495 570 IRRYPDLLLHRAIKAHLKQKP----YPLSGAALDDAGEHFSQTERRADEASRSVTTWLKCHYMQQHLGDEFIGIVSAVTE 645
Cdd:COG0557 556 IRRYPDLLVHRALKAYLEGKRspglQEYLEEELEEIAEHCSETERRADEAERDVVDLKKAEYMKDRVGEEFEGVISGVTS 635
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446087495 646 FGLFVTLKDLYVDGMIHISQLGDDFFIYDQASQNLIGQNRGQVFGLGDEVKIQVAGVNLEERKIDFQLIK 715
Cdd:COG0557 636 FGLFVELDELGVEGLVHVSSLGDDYYEYDERRQALVGERTGKRYRLGDRVEVRVVRVDLDRRQIDFELVE 705
|
|
| RNase_R |
TIGR02063 |
ribonuclease R; This family consists of an exoribonuclease, ribonuclease R, also called VacB. ... |
21-714 |
0e+00 |
|
ribonuclease R; This family consists of an exoribonuclease, ribonuclease R, also called VacB. It is one of the eight exoribonucleases reported in E. coli and is broadly distributed throughout the bacteria. In E. coli, double mutants of this protein and polynucleotide phosphorylase are not viable. Scoring between trusted and noise cutoffs to the model are shorter, divergent forms from the Chlamydiae, and divergent forms from the Campylobacterales (including Helicobacter pylori) and Leptospira interrogans. [Transcription, Degradation of RNA]
Pssm-ID: 273947 [Multi-domain] Cd Length: 709 Bit Score: 767.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446087495 21 IPSRTLILDTLEQL-QTPQSHAELVDHFHIQDQKSIEALSHRLSAMVRDGQLMKD-GFKFQLVADQPTYEATVYINSKGL 98
Cdd:TIGR02063 1 SPLRELILEFLKSKkGKPISLKELAKAFHLKGADEKKALRKRLRALEDDGLVKKNrRGLYALPESLKLVKGTVIAHRDGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446087495 99 GTAHI--DGQDDLLLPERELRLVFNGDRVRVRQT-SVDRKGKPWGFITEVIQHRVKQLIGKLSVHDGEYFIQPNNPNQHQ 175
Cdd:TIGR02063 81 GFLRPedDDEDDIFIPPRQMNGAMHGDRVLVRITgKPDGGDRFEARVIKILERANDQIVGTFYIENGIGFVIPDDKRIYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446087495 176 PIPLEKELVEHAKAnvGDMLRVAIDTYPTREEFATAHIIQSMADKADTEIIIPQTILEFGLPYEFPDEVIKEAESFKEP- 254
Cdd:TIGR02063 161 DIFIPPEQILGAEE--GDKVLVEITKYPDRNRPAIGKVVEILGHADDPGIDILIIIRKHGIPYEFPEEVLDEAAKIPEEv 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446087495 255 AEQDREGRVDLRDLALVTIDGEDARDFDDAVYAEKRPGGGYRVVVAIADVSHYVRLDSALNEEAEERGTSVYFPHFVLPM 334
Cdd:TIGR02063 239 PEEEIKGRKDLRDLPFVTIDGEDAKDFDDAVYVEKLKDGNYKLGVAIADVSHYVREGSALDKEALKRGTSVYLPDRVIPM 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446087495 335 LPEALSNGLCSLNPHVDRLCMVCDLKLSRTGRVTGYEFYPAVMHSKARLTYTQVGQYFEGATDAIPKDRDIHKSLNTLFQ 414
Cdd:TIGR02063 319 LPERLSNGICSLNPNEDRLTLSCEMEIDKKGRVKKYEFYEAVINSHARLTYNQVNDIIEGKDALDKKEPPLKEMLKNLFE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446087495 415 LYQILKNLRVDRHAMEFETIETYMTFDELGGIKEILPRTRNDAHKLIEECMLLANVAAAEYALEHDIPMLYRVHEAPEFS 494
Cdd:TIGR02063 399 LYKILRKKRKKRGAIDFDSKEAKIILDENGKPIDIVPRERGDAHKLIEEFMIAANETVAEHLEKAKLPFIYRVHERPSEE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446087495 495 RIQKVKDFVKLLGL----PFPDQPTQADYQKVIEATKDRIDAPSIHAVLLRSMMQAYYGAKNAGHYGLAYEAYTHFTSPI 570
Cdd:TIGR02063 479 KLQNLREFLKTLGItlkgGTSDKPQPKDFQKLLEKVKGRPEEELINTVLLRSMQQAKYSPENIGHFGLALEYYTHFTSPI 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446087495 571 RRYPDLLLHRAIKAHLKQKPYPL-------SGAALDDAGEHFSQTERRADEASRSVTTWLKCHYMQQHLGDEFIGIVSAV 643
Cdd:TIGR02063 559 RRYPDLIVHRLIKKALFGGENTTtekereyLEAKLEEIAEHSSKTERRADEAERDVNDWKKAEYMSEKIGEEFEGVISGV 638
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446087495 644 TEFGLFVTLKDLYVDGMIHISQLGDDFFIYDQASQNLIGQNRGQVFGLGDEVKIQVAGVNLEERKIDFQLI 714
Cdd:TIGR02063 639 TSFGLFVELENNTIEGLVHISTLKDDYYVFDEKGLALVGERTGKVFRLGDRVKVRVVKADLDTGKIDFELV 709
|
|
| PRK11642 |
PRK11642 |
ribonuclease R; |
7-761 |
0e+00 |
|
ribonuclease R;
Pssm-ID: 236944 [Multi-domain] Cd Length: 813 Bit Score: 651.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446087495 7 DPEAKAEAERYDNPIPSRTLILDTLEQLQTPQSHAELVDHFHIQDQKSIEALSHRLSAMVRDGQLMkdgFK----FQLVA 82
Cdd:PRK11642 4 DPFQEREAEKYANPIPSREFILEHLTKREKPASREELAVELNIEGEEQLEALRRRLRAMERDGQLV---FTrrqcYALPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446087495 83 DQPTYEATVYINSKGLGTAHIDGQ-DDLLLPERELRLVFNGDRVRVRQTSVDRKGKPWGFITEVIQHRVKQLIGKLSVHD 161
Cdd:PRK11642 81 RLDLLKGTVIGHRDGYGFLRVEGRkDDLYLSSEQMKTCIHGDQVLAQPLGADRKGRREARIVRVLVPKTSQIVGRYFTDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446087495 162 GEYFIQPNNPNQHQPIPLEKElvEHAKANVGDMLRVAIDTYPTREEFATAHIIQSMADKADTEIIIPQTILEFGLPYEFP 241
Cdd:PRK11642 161 GVGFVVPDDSRLSFDILIPPE--QIMGARMGFVVVVELTQRPTRRTKAVGKIVEVLGDNMGTGMAVDIALRTHEIPYIWP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446087495 242 DEVIKEAESFKEPA-EQDREGRVDLRDLALVTIDGEDARDFDDAVYAEKRPGGGYRVVVAIADVSHYVRLDSALNEEAEE 320
Cdd:PRK11642 239 QAVEQQVAGLKEEVpEEAKAGRVDLRDLPLVTIDGEDARDFDDAVYCEKKRGGGWRLWVAIADVSYYVRPPTPLDREARN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446087495 321 RGTSVYFPHFVLPMLPEALSNGLCSLNPHVDRLCMVCDLKLSRTGRVTGYEFYPAVMHSKARLTYTQVGQYFEGATDAIP 400
Cdd:PRK11642 319 RGTSVYFPSQVVPMLPEVLSNGLCSLNPQVDRLCMVCEMTISSKGRLTGYKFYEAVMSSHARLTYTKVWHILQGDQDLRE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446087495 401 KDRDIHKSLNTLFQLYQILKNLRVDRHAMEFETIETYMTFDELGGIKEILPRTRNDAHKLIEECMLLANVAAAEYALEHD 480
Cdd:PRK11642 399 QYAPLVKHLEELHNLYKVLDKAREERGGISFESEEAKFIFNAERRIERIEQTQRNDAHKLIEECMILANISAARFVEKAK 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446087495 481 IPMLYRVHEAPEFSRIQKVKDFVKLLGLPFP--DQPTQADYQKVIEATKDRIDAPSIHAVLLRSMMQAYYGAKNAGHYGL 558
Cdd:PRK11642 479 EPALFRIHDKPSTEAITSFRSVLAELGLELPggNKPEPRDYAELLESVADRPDAEMLQTMLLRSMKQAIYDPENRGHFGL 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446087495 559 AYEAYTHFTSPIRRYPDLLLHRAIKAHL------KQKPYPLSGAALD-----DAGEHFSQTERRADEASRSVTTWLKCHY 627
Cdd:PRK11642 559 ALQSYAHFTSPIRRYPDLSLHRAIKYLLakeqghKGNTTETGGYHYSmeemlQLGQHCSMTERRADEATRDVADWLKCDF 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446087495 628 MQQHLGDEFIGIVSAVTEFGLFVTLKDLYVDGMIHISQLGDDFFIYDQASQNLIGQNRGQVFGLGDEVKIQVAGVNLEER 707
Cdd:PRK11642 639 MLDQVGNVFKGVISSVTGFGFFVRLDDLFIDGLVHVSSLDNDYYRFDQVGQRLIGESSGQTYRLGDRVEVRVEAVNMDER 718
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*..
gi 446087495 708 KIDFQLI---KQVTHAGRVVRSRAPRTTKTSTQATEEVFGKPsVSTDGEKPVRKKKE 761
Cdd:PRK11642 719 KIDFSLIsseRAPRNVGKTAREKAKKGDAGKKGGKRRQVGKK-VNFEPDSAFRGEKK 774
|
|
| 3_prime_RNase |
TIGR00358 |
VacB and RNase II family 3'-5' exoribonucleases; This model is defined to identify a pair of ... |
119-714 |
0e+00 |
|
VacB and RNase II family 3'-5' exoribonucleases; This model is defined to identify a pair of paralogous 3-prime exoribonucleases in E. coli, plus the set of proteins apparently orthologous to one or the other in other eubacteria. VacB was characterized originally as required for the expression of virulence genes, but is now recognized as the exoribonuclease RNase R (Rnr). Its paralog in E. coli and H. influenzae is designated exoribonuclease II (Rnb). Both are involved in the degradation of mRNA, and consequently have strong pleiotropic effects that may be difficult to disentangle. Both these proteins share domain-level similarity (RNB, S1) with a considerable number of other proteins, and full-length similarity scoring below the trusted cutoff to proteins associated with various phenotypes but uncertain biochemistry; it may be that these latter proteins are also 3-prime exoribonucleases. [Transcription, Degradation of RNA]
Pssm-ID: 273033 [Multi-domain] Cd Length: 654 Bit Score: 597.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446087495 119 VFNGDRVRVRQTSVDRKGKPWGFITEVIQHRVKQLIGKLSVHDGEYFIQPNNPNQHQPIPLEKELVEHaKANVGDMLRVA 198
Cdd:TIGR00358 51 VMHGDLVEACPLSQPQRGRFEAEVERILEPALTRFVGKFLGENDFGFVVPDDPRIYLDIIVPKASVKN-ELAEGDKVVVE 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446087495 199 IDTYPTREEFATAHIIQSMADKADTEIIIPQTILEFGLPYEFPDEVIKEAESF-KEPAEQDREGRVDLRDLALVTIDGED 277
Cdd:TIGR00358 130 LTEYPLRRNLFYGEITQILGNNDDPLIPWWVTLARHEIPFEFPDGVEQQAAKLqFDVDEQAKKYREDLTDLAFVTIDGAD 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446087495 278 ARDFDDAVYAEKRPGGGYRVVVAIADVSHYVRLDSALNEEAEERGTSVYFPHFVLPMLPEALSNGLCSLNPHVDRLCMVC 357
Cdd:TIGR00358 210 AKDLDDAVYVKKLPDGGWKLYVAIADVSYYVAENSPLDKEAKHRGFSVYLPGFVIPMLPEELSNGLCSLNPNEDRLVLVC 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446087495 358 DLKLSRTGRVTGYEFYPAVMHSKARLTYTQVGQYFEGATDAIPKDRDIHKSLNTLFQLYQILKNLRVDRHAMEFETIETY 437
Cdd:TIGR00358 290 EMTISAQGRITDNEFYPATIESKARLTYDKVNDWLENDDELQPEYETLVEQLKALHQLSQALGEWRHKRGLIDFEHPETK 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446087495 438 MTFDELGGIKEILPRTRNDAHKLIEECMLLANVAAAEYALEHDIPMLYRVHEAPEFSRIQKVKDFVKLLGLPFP----DQ 513
Cdd:TIGR00358 370 FIVDEEGRVIDIVAEVRRIAEKIIEEAMIVANICAARFLHNHKVPGIYRVHPGPSKKKLQSLLEFLAELGLTLPggnaEN 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446087495 514 PTQADYQKVIEATKDRIDAPSIHAVLLRSMMQAYYGAKNAGHYGLAYEAYTHFTSPIRRYPDLLLHRAIKAHL-KQKPY- 591
Cdd:TIGR00358 450 VTTLDGACWLREVKDRPEYEILVTRLLRSLSQAEYSPEPLGHFGLGLEHYAHFTSPIRRYPDLTNHRLIKAVLaKEQTDt 529
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446087495 592 --PLSGAALDDAGEHFSQTERRADEASRSVTTWLKCHYMQQHLGDEFIGIVSAVTEFGLFVTLKDLYVDGMIHISQLGDD 669
Cdd:TIGR00358 530 erYQPQDELLQIAEHCSDTERRARDAERDVADWLKCRYLLDKVGTEFSGEISSVTRFGMFVRLDDNGIDGLIHISTLHND 609
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 446087495 670 FFIYDQASQNLIGQNRGQVFGLGDEVKIQVAGVNLEERKIDFQLI 714
Cdd:TIGR00358 610 YYVFDQEKMALIGKGTGKVYRIGDRVTVKLTEVNMETRSIIFELV 654
|
|
| RNB |
smart00955 |
This domain is the catalytic domain of ribonuclease II; |
262-588 |
1.91e-133 |
|
This domain is the catalytic domain of ribonuclease II;
Pssm-ID: 214935 [Multi-domain] Cd Length: 286 Bit Score: 397.79 E-value: 1.91e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446087495 262 RVDLRDLALVTIDGEDARDFDDAVYAEKRPGGGYRVVVAIADVSHYVRLDSALNEEAEERGTSVYFPHFVLPMLPEALSN 341
Cdd:smart00955 1 RVDLRDLPLFTIDPEDAKDIDDAVSVEKLDNGGYRLGVHIADVSHYVKPGSALDREARKRGTSVYLPDRVIPMLPEELSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446087495 342 GLCSLNPHVDRLCMVCDLKLSR-TGRVTGYEFYPAVMHSKARLTYTQVGQYFEGatdaipkdrdihkslntlfqlyqilk 420
Cdd:smart00955 81 GLCSLNPGEDRLALSVEMTLDAdGGEILDYEFYRSVIRSKARLTYEEVDAILEK-------------------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446087495 421 nlrvdrhamefetietyMTFDELGGIKEILPRTRNDAHKLIEECMLLANVAAAEYALEHDIPMLYRVHEAPEFSRI-QKV 499
Cdd:smart00955 135 -----------------IVLDEEGKIEDIVPRERNDAHSLVEEFMILANEAVARFLAKNGIPGLYRVHEGPDPEKLaELL 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446087495 500 KDFVKLLGLPFPDQPTQADYQKVIEATKDRIDAPSIHAVLLRSMMQAYYGAKNAGHYGLAYEAYTHFTSPIRRYPDLLLH 579
Cdd:smart00955 198 KEFLALLGLLLLGGDGPKALAKLLEKIRDSPEERLLELLLLRSMPHAEYSVDNSGHFGLALDAYTHFTSPIRRYPDLIVH 277
|
....*....
gi 446087495 580 RAIKAHLKQ 588
Cdd:smart00955 278 RQLKAALRG 286
|
|
| RNB |
pfam00773 |
RNB domain; This domain is the catalytic domain of ribonuclease II. |
262-586 |
1.27e-129 |
|
RNB domain; This domain is the catalytic domain of ribonuclease II.
Pssm-ID: 459934 [Multi-domain] Cd Length: 314 Bit Score: 389.34 E-value: 1.27e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446087495 262 RVDLRDLALVTIDGEDARDFDDAVYAEKRPGGGYRVVVAIADVSHYVRLDSALNEEAEERGTSVYFPHFVLPMLPEALSN 341
Cdd:pfam00773 1 RKDLRDLPFITIDPADAKDLDDAISVEKLPNGGYRLGVHIADVSHYVPPGSPLDREARKRGTSVYLPDRVIPMLPEKLSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446087495 342 GLCSLNPHVDRLCMVCDLKLSRTGRVTGYEFYPAVMHSKARLTYTQVGQYFEGATDAIPKDrDIHKSLNTLFQLYQILKN 421
Cdd:pfam00773 81 DLCSLNPGEDRLALSVEITIDADGEVTSYEIYPSVIRSKARLTYEEVDDLLEGKDAEKDKP-DLAEDLRLLYELAKILRA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446087495 422 LRVDRHAMEFETIETYMTFDElGGIKEILPRTRNDAHKLIEECMLLANVAAAEYALEHDIPMLYRVHEAPEfsrIQKVKD 501
Cdd:pfam00773 160 KRLQRGALDLDTPENKLILDE-EGVIDILIQERTDAHSLIEEFMLLANEAVARHLQELGIPALYRVHPEPD---LEKLNS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446087495 502 FVKLLGLpfpdQPTQADYQKVIEATKDriDAPSIHAVLLRSMMQAYYGAKNAGHYGLAYEAYTHFTSPIRRYPDLLLHRA 581
Cdd:pfam00773 236 LIKLLQL----LPDDKGLSKSLEKIKD--DERLLSILLLRTMPRAEYSPEPLGHFGLGLDIYTHFTSPIRRYPDLIVHRQ 309
|
....*
gi 446087495 582 IKAHL 586
Cdd:pfam00773 310 LKALL 314
|
|
| Rnb |
COG4776 |
Exoribonuclease II [Transcription]; |
77-709 |
1.73e-83 |
|
Exoribonuclease II [Transcription];
Pssm-ID: 443808 [Multi-domain] Cd Length: 644 Bit Score: 279.43 E-value: 1.73e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446087495 77 KFQLVADQPTYEATVYINSKGLGTAHIDGQDDLLLPERELRLVFNGDRVR-VRQTSVDRK-GKPwgfiTEVIQHRVKQLI 154
Cdd:COG4776 12 KQQLHEQTPRVEGVVKATDKGFGFLEVDDQKSYFIPPPQMKKVMHGDRIKaVIRTEKDKEsAEP----ETLIEPFLTRFV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446087495 155 GKLSVHDGEYFIQPNNPNQHQPIP------LEKELVEhakanvGDMLRVAIDTYPTREE-FATAHIIQSMADKADteIII 227
Cdd:COG4776 88 GRVQKKDGRLFVVPDHPLIKDAIKarpkkgLEEGLKE------GDWVVAELKRHPLKGDrGFFAEITEFIADADD--PFA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446087495 228 PQ--TILEFGLPYEFPdevikEAESFKEPAEQDREgRVDLRDLALVTIDGEDARDFDDAVYAEKRPGGGYRVVVAIADVS 305
Cdd:COG4776 160 PWwvTLARHNLEREAP-----EGDDEWELLDEGLE-REDLTALPFVTIDSESTEDMDDALYIEKLENGGWKLTVAIADPT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446087495 306 HYVRLDSALNEEAEERGTSVYFPHFVLPMLPEALSNGLCSLNPHVDRLCMVCDLKLSRTGRVTG-YEFYPAVMHSKARLT 384
Cdd:COG4776 234 AYIPEGSELDKEARQRAFTNYLPGFNIPMLPRELSDDLCSLKENEKRPALVCRVTIDADGSIGDdIEFFAAWIRSKAKLA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446087495 385 YTQVGQYFEGATDAIPKDRDIHKSLNTLFQLYQILKNLRvDRHAMEFETIETY-MTFDELGGIKEILPRTRNDAHKLIEE 463
Cdd:COG4776 314 YDNVSDWLEGKGEWQPENEEIAEQIRLLHQFALARSQWR-QQHALVFKDRPDYrFELDEKGNVLDIHAEPRRIANRIVEE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446087495 464 CMLLANVAAAEYALEHDIPMLYRVHE--APEfsriqKVKDFVKLL---GLPF-PDQPTQADYQKVIEATKDRIDAPSIHA 537
Cdd:COG4776 393 AMIAANICAARVLREHLGFGIFNVHSgfDPE-----KLEQAVELLaehGIEFdPEQLLTLEGFCALRRELDAQPTSYLDS 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446087495 538 VLLRsmMQAY--YGAKNAGHYGLAYEAYTHFTSPIRRYPDLLLHRAIKAHLKQKPYPlsgAALDDAGEHFSQTERRADEA 615
Cdd:COG4776 468 RLRR--FQTFaeISTEPGPHFGLGLDAYATWTSPIRKYGDMVNHRLIKAVILGQPAE---KPDEELTERLAERRRLNRMA 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446087495 616 SRSVTTWLKCHYMQQHLGDE--FIGIVSAVTEFGLFVTLKDLYVDGMIHISQLGDD----FFIYDQASQNLIGQNRGQvf 689
Cdd:COG4776 543 ERDVADWLYARYLKPKVGSGqvFTAEIIDINRGGLRVRLLENGAVAFIPASFIHSVrdelVCSQEEGTVYIKGEVRYK-- 620
|
650 660
....*....|....*....|
gi 446087495 690 gLGDEVKIQVAGVNLEERKI 709
Cdd:COG4776 621 -LGDTIQVTLAEVREETRSI 639
|
|
| PRK05054 |
PRK05054 |
exoribonuclease II; Provisional |
77-709 |
5.04e-66 |
|
exoribonuclease II; Provisional
Pssm-ID: 179920 [Multi-domain] Cd Length: 644 Bit Score: 231.69 E-value: 5.04e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446087495 77 KFQLVADQPTYEATVYINSKGLGTAHIDGQDDLLLPERELRLVFNGDRVR-VRQTSVDRK-GKPwgfiTEVIQHRVKQLI 154
Cdd:PRK05054 12 KQQLHSQTPRVEGVVKATEKGFGFLEVDAQKSYFIPPPQMKKVMHGDRIIaVIHTEKDREiAEP----EELIEPFLTRFV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446087495 155 GKLSVHDGEYFIQPNNPNQHQPIP--LEKELVEHAKAnvGDMLRVAIDTYPTR-EEFATAHIIQSMADKADTeiIIPQ-- 229
Cdd:PRK05054 88 GRVQKKDDRLSIVPDHPLLKDAIPcrAAKGLNHEFKE--GDWVVAELRRHPLKgDRGFYAEITQFITDADDH--FAPWwv 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446087495 230 TILEFGLPYEFPDevikeaesFKEPAEQDREG--RVDLRDLALVTIDGEDARDFDDAVYAEKRPGGGYRVVVAIADVSHY 307
Cdd:PRK05054 164 TLARHNLEREAPA--------GGVAWEMLDEGleREDLTALDFVTIDSASTEDMDDALYVEKLPDGGLQLTVAIADPTAY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446087495 308 VRLDSALNEEAEERGTSVYFPHFVLPMLPEALSNGLCSLNPHVDRLCMVCDLKLSRTGRVTG-YEFYPAVMHSKARLTYT 386
Cdd:PRK05054 236 IAEGSKLDKAARQRAFTNYLPGFNIPMLPRELSDDLCSLRPNERRPALACRVTIDADGTIEDdIRFFAAWIESKAKLAYD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446087495 387 QVGQYFEGATDAIPKDRDIHKSLNTLFQLYQILKNLRVDrHAMEF-ETIETYMTFDELGGIKEILPRTRNDAHKLIEECM 465
Cdd:PRK05054 316 NVSDWLENGGDWQPESEAIAEQIRLLHQFCLARSEWRKQ-HALVFkDRPDYRFELGEKGEVLDIVAEPRRIANRIVEESM 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446087495 466 LLANVAAAEYALEHDIPMLYRVHEAPEFSRIQKVKDFVKLLGLPFPDQP--TQADYQKVieatkdRIDAPSIHAVLLRSM 543
Cdd:PRK05054 395 IAANICAARVLRDKLGFGIYNVHSGFDPANAEQAVALLKEHGLHFDAEEllTLEGFCKL------RRELDAQPTGYLDSR 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446087495 544 M---QAYYGAKN--AGHYGLAYEAYTHFTSPIRRYPDLLLHRAIKAHLKQKPYPlsgAALDDAGEHFSQTERRADEASRS 618
Cdd:PRK05054 469 IrrfQSFAEISTepGPHFGLGLEAYATWTSPIRKYGDMINHRLLKAVIKGETAE---RPQDEITVQLAERRRLNRMAERD 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446087495 619 VTTWLKCHYMQQHLGDE--FIGIVSAVTEFGLFVTLKDLYVDGMIHISqlgddfFIYDQASQNLIGQNRGQV-------F 689
Cdd:PRK05054 546 VGDWLYARYLKDKAGTDtrFAAEIIDISRGGMRVRLLENGAVAFIPAS------FLHAVRDELVCNQENGTVqikgetvY 619
|
650 660
....*....|....*....|
gi 446087495 690 GLGDEVKIQVAGVNLEERKI 709
Cdd:PRK05054 620 KLGDVIDVTLAEVRMETRSI 639
|
|
| S1_RNase_R |
cd04471 |
S1_RNase_R: RNase R C-terminal S1 domain. RNase R is a processive 3' to 5' exoribonuclease, ... |
632-714 |
1.89e-36 |
|
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: 131.75 E-value: 1.89e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446087495 632 LGDEFIGIVSAVTEFGLFVTLKDLYVDGMIHISQLGDDFFIYDQASQNLIGQNRGQVFGLGDEVKIQVAGVNLEERKIDF 711
Cdd:cd04471 1 VGEEFDGVISGVTSFGLFVELDNLTVEGLVHVSTLGDDYYEFDEENHALVGERTGKVFRLGDKVKVRVVRVDLDRRKIDF 80
|
...
gi 446087495 712 QLI 714
Cdd:cd04471 81 ELV 83
|
|
| PRK08563 |
PRK08563 |
DNA-directed RNA polymerase subunit E'; Provisional |
638-709 |
1.32e-14 |
|
DNA-directed RNA polymerase subunit E'; Provisional
Pssm-ID: 236289 [Multi-domain] Cd Length: 187 Bit Score: 72.94 E-value: 1.32e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446087495 638 GIVSAVTEFGLFVTLKDlyVDGMIHISQLGDDFFIYDQASQNLIGQNRGQVFGLGDEVKIQVAGVNLEERKI 709
Cdd:PRK08563 87 GEVVEVVEFGAFVRIGP--VDGLLHISQIMDDYISYDPKNGRLIGKESKRVLKVGDVVRARIVAVSLKERRP 156
|
|
| S1_RpoE |
cd04460 |
S1_RpoE: RpoE, S1-like RNA-binding domain. S1-like RNA-binding domains are found in a wide ... |
638-709 |
5.20e-13 |
|
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: 65.39 E-value: 5.20e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446087495 638 GIVSAVTEFGLFVTLKDlyVDGMIHISQLGDDFFIYDQASQNLIGQNRGQVFGLGDEVKIQVAGVNLEERKI 709
Cdd:cd04460 5 GEVVEVVDFGAFVRIGP--VDGLLHISQIMDDYISYDPKNKRLIGEETKRVLKVGDVVRARIVAVSLKERRP 74
|
|
| S1 |
smart00316 |
Ribosomal protein S1-like RNA-binding domain; |
633-711 |
1.11e-09 |
|
Ribosomal protein S1-like RNA-binding domain;
Pssm-ID: 197648 [Multi-domain] Cd Length: 72 Bit Score: 55.30 E-value: 1.11e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446087495 633 GDEFIGIVSAVTEFGLFVTLkDLYVDGMIHISQLGDDFfiydqasqnliGQNRGQVFGLGDEVKIQVAGVNLEERKIDF 711
Cdd:smart00316 3 GDVVEGTVTEITPGGAFVDL-GNGVEGLIPISELSDKR-----------VKDPEEVLKVGDEVKVKVLSVDEEKGRIIL 69
|
|
| S1_Tex |
cd05685 |
S1_Tex: The C-terminal S1 domain of a transcription accessory factor called Tex, which has ... |
633-709 |
1.83e-08 |
|
S1_Tex: The C-terminal S1 domain of a transcription accessory factor called Tex, which has been characterized in Bordetella pertussis and Pseudomonas aeruginosa. The tex gene is essential in Bortella pertusis and is named for its role in toxin expression. Tex has two functional domains, an N-terminal domain homologous to the Escherichia coli maltose repression protein, which is a poorly defined transcriptional factor, and a C-terminal S1 RNA-binding domain. Tex is found in prokaryotes, eukaryotes, and archaea.
Pssm-ID: 240190 [Multi-domain] Cd Length: 68 Bit Score: 51.46 E-value: 1.83e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446087495 633 GDEFIGIVSAVTEFGLFVtlkDLYV--DGMIHISQLGDDFFiydqasqnligQNRGQVFGLGDEVKIQVAGVNLEERKI 709
Cdd:cd05685 1 GMVLEGVVTNVTDFGAFV---DIGVkqDGLIHISKMADRFV-----------SHPSDVVSVGDIVEVKVISIDEERGRI 65
|
|
| S1 |
pfam00575 |
S1 RNA binding domain; The S1 domain occurs in a wide range of RNA associated proteins. It is ... |
633-711 |
3.20e-08 |
|
S1 RNA binding domain; The S1 domain occurs in a wide range of RNA associated proteins. It is structurally similar to cold shock protein which binds nucleic acids. The S1 domain has an OB-fold structure.
Pssm-ID: 425760 [Multi-domain] Cd Length: 72 Bit Score: 51.13 E-value: 3.20e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446087495 633 GDEFIGIVSAVTEFGLFVTLkDLYVDGMIHISQLGDDFfiydqasqnliGQNRGQVFGLGDEVKIQVAGVNLEERKIDF 711
Cdd:pfam00575 4 GDVVEGEVTRVTKGGAFVDL-GNGVEGFIPISELSDDH-----------VEDPDEVIKVGDEVKVKVLKVDKDRRRIIL 70
|
|
| S1_Rrp5_repeat_sc12 |
cd05708 |
S1_Rrp5_repeat_sc12: Rrp5 is a trans-acting factor important for biogenesis of both the 40S ... |
631-713 |
1.61e-07 |
|
S1_Rrp5_repeat_sc12: Rrp5 is a trans-acting factor important for biogenesis of both the 40S and 60S eukaryotic ribosomal subunits. Rrp5 has two distinct regions, an N-terminal region containing tandemly repeated S1 RNA-binding domains (12 S1 repeats in Saccharomyces cerevisiae Rrp5 and 14 S1 repeats in Homo sapiens Rrp5) and a C-terminal region containing tetratricopeptide repeat (TPR) motifs thought to be involved in protein-protein interactions. Mutational studies have shown that each region represents a specific functional domain. Deletions within the S1-containing region inhibit pre-rRNA processing at either site A3 or A2, whereas deletions within the TPR region confer an inability to support cleavage of A0-A2. This CD includes S. cerevisiae S1 repeat 12 (sc12). Rrp5 is found in eukaryotes but not in prokaryotes or archaea.
Pssm-ID: 240213 [Multi-domain] Cd Length: 77 Bit Score: 49.25 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446087495 631 HLGDEFIGIVSAVTEFGLFVTLKDLYVDGMIHISQLGDDffiydqASQNLIGQnrgqvFGLGDEVKIQVAGVNLEERKID 710
Cdd:cd05708 1 KVGQKIDGTVRRVEDYGVFIDIDGTNVSGLCHKSEISDN------RVADASKL-----FRVGDKVRAKVLKIDAEKKRIS 69
|
...
gi 446087495 711 FQL 713
Cdd:cd05708 70 LGL 72
|
|
| S1_RPS1_repeat_ec3 |
cd05688 |
S1_RPS1_repeat_ec3: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ... |
633-709 |
1.66e-07 |
|
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: 48.78 E-value: 1.66e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446087495 633 GDEFIGIVSAVTEFGLFVTLKDlyVDGMIHISQLgddffiydqaSQNLIgQNRGQVFGLGDEVKIQVAGVNLEERKI 709
Cdd:cd05688 2 GDVVEGTVKSITDFGAFVDLGG--VDGLLHISDM----------SWGRV-KHPSEVVNVGDEVEVKVLKIDKERKRI 65
|
|
| RpsA |
COG0539 |
Ribosomal protein S1 [Translation, ribosomal structure and biogenesis]; Ribosomal protein S1 ... |
633-709 |
8.83e-07 |
|
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: 51.97 E-value: 8.83e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446087495 633 GDEFIGIVSAVTEFGLFVTLKDlYVDGMIHISQLGDDFFIydqasqnligQNRGQVFGLGDEVKIQVAGVNLEERKI 709
Cdd:COG0539 275 GDVVKGKVTRLTDFGAFVELEP-GVEGLVHISEMSWTKRV----------AHPSDVVKVGDEVEVKVLDIDPEERRI 340
|
|
| CSD2 |
pfam17876 |
Cold shock domain; Crystallographic structure analysis of E. coli wild-type RNase II revealed ... |
165-241 |
1.08e-06 |
|
Cold shock domain; Crystallographic structure analysis of E. coli wild-type RNase II revealed that the amino-terminal region starts with an alpha-helix followed by two consecutive five-stranded anti-parallel beta-barrels, identified as cold-shock domains (CSD1 and CSD2). This entry relates to CSD2 which lacks the typical sequence motifs RNPI and RNPII but contributes to RNA binding.
Pssm-ID: 465546 [Multi-domain] Cd Length: 74 Bit Score: 46.61 E-value: 1.08e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446087495 165 FIQPNNPNQHQPIPLEKElvEHAKANVGDMLRVAIDTYPTREEfATAHIIQSMADKADTEIIIPQTILEFGLPYEFP 241
Cdd:pfam17876 1 FVVPDDKRIPQDIFIPKE--DLKGAKDGDKVVVEITEYPDGKN-PEGKIVEVLGDPGDPGVEILSIIRKHGLPHEFP 74
|
|
| PRK00087 |
PRK00087 |
bifunctional 4-hydroxy-3-methylbut-2-enyl diphosphate reductase/30S ribosomal protein S1; |
631-717 |
2.72e-06 |
|
bifunctional 4-hydroxy-3-methylbut-2-enyl diphosphate reductase/30S ribosomal protein S1;
Pssm-ID: 234623 [Multi-domain] Cd Length: 647 Bit Score: 51.10 E-value: 2.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446087495 631 HLGDEFIGIVSAVTEFGLFVTLKDlYVDGMIHISQLgddffiydqaSQNLIGqNRGQVFGLGDEVKIQVAGVNLEERKID 710
Cdd:PRK00087 561 PVGSIVLGKVVRIAPFGAFVELEP-GVDGLVHISQI----------SWKRID-KPEDVLSEGEEVKAKILEVDPEEKRIR 628
|
....*..
gi 446087495 711 FQlIKQV 717
Cdd:PRK00087 629 LS-IKEV 634
|
|
| rpsA |
PRK06299 |
30S ribosomal protein S1; Reviewed |
633-716 |
3.61e-06 |
|
30S ribosomal protein S1; Reviewed
Pssm-ID: 235775 [Multi-domain] Cd Length: 565 Bit Score: 50.55 E-value: 3.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446087495 633 GDEFIGIVSAVTEFGLFVTLKDlYVDGMIHISQLgddffiydqaSQNLIGQNRGQVFGLGDEVKIQVAGVNLEERKIDfq 712
Cdd:PRK06299 374 GDVVEGKVKNITDFGAFVGLEG-GIDGLVHLSDI----------SWDKKGEEAVELYKKGDEVEAVVLKVDVEKERIS-- 440
|
....*
gi 446087495 713 L-IKQ 716
Cdd:PRK06299 441 LgIKQ 445
|
|
| S1_DHX8_helicase |
cd05684 |
S1_DHX8_helicase: The N-terminal S1 domain of human ATP-dependent RNA helicase DHX8, a DEAH ... |
638-702 |
4.62e-06 |
|
S1_DHX8_helicase: The N-terminal S1 domain of human ATP-dependent RNA helicase DHX8, a DEAH (Asp-Glu-Ala-His) box polypeptide. The DEAH-box RNA helicases are thought to play key roles in pre-mRNA splicing and DHX8 facilitates nuclear export of spliced mRNA by releasing the RNA from the spliceosome. DHX8 is also known as HRH1 (human RNA helicase 1) in Homo sapiens and PRP22 in Saccharomyces cerevisiae.
Pssm-ID: 240189 [Multi-domain] Cd Length: 79 Bit Score: 45.31 E-value: 4.62e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446087495 638 GIVSAVTEFGLFVTLKDL--YVDGMIHISQLgddffiydqaSQNLIGQNRGQVFGLGDEVKIQVAGV 702
Cdd:cd05684 6 GKVTSIMDFGCFVQLEGLkgRKEGLVHISQL----------SFEGRVANPSDVVKRGQKVKVKVISI 62
|
|
| S1_like |
cd00164 |
S1_like: Ribosomal protein S1-like RNA-binding domain. Found in a wide variety of ... |
636-709 |
4.81e-06 |
|
S1_like: Ribosomal protein S1-like RNA-binding domain. Found in a wide variety of RNA-associated proteins. Originally identified in S1 ribosomal protein. This superfamily also contains the Cold Shock Domain (CSD), which is a homolog of the S1 domain. Both domains are members of the Oligonucleotide/oligosaccharide Binding (OB) fold.
Pssm-ID: 238094 [Multi-domain] Cd Length: 65 Bit Score: 44.68 E-value: 4.81e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446087495 636 FIGIVSAVTEFGLFVTLKDlYVDGMIHISQLGDDFFiydqasqnligQNRGQVFGLGDEVKIQVAGVNLEERKI 709
Cdd:cd00164 1 VTGKVVSITKFGVFVELED-GVEGLVHISELSDKFV-----------KDPSEVFKVGDEVEVKVLEVDPEKGRI 62
|
|
| rpsA |
PRK06676 |
30S ribosomal protein S1; Reviewed |
633-709 |
9.32e-06 |
|
30S ribosomal protein S1; Reviewed
Pssm-ID: 235851 [Multi-domain] Cd Length: 390 Bit Score: 48.72 E-value: 9.32e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446087495 633 GDEFIGIVSAVTEFGLFVTLKDlYVDGMIHISQLGDDFfiydqasqnlIGqNRGQVFGLGDEVKIQVAGVNLEERKI 709
Cdd:PRK06676 278 GDVIEGTVKRLTDFGAFVEVLP-GVEGLVHISQISHKH----------IA-TPSEVLEEGQEVKVKVLEVNEEEKRI 342
|
|
| RpsA |
COG0539 |
Ribosomal protein S1 [Translation, ribosomal structure and biogenesis]; Ribosomal protein S1 ... |
633-718 |
1.57e-05 |
|
Ribosomal protein S1 [Translation, ribosomal structure and biogenesis]; Ribosomal protein S1 is part of the Pathway/BioSystem: Ribosome 30S subunit
Pssm-ID: 440305 [Multi-domain] Cd Length: 348 Bit Score: 47.73 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446087495 633 GDEFIGIVSAVTEFGLFVtlkDLY-VDGMIHISQLgddffiydqaSQNLIgQNRGQVFGLGDEVKIQVAGVNLEERKIdf 711
Cdd:COG0539 190 GDVVEGTVKNITDFGAFV---DLGgVDGLLHISEI----------SWGRV-KHPSEVLKVGDEVEVKVLKIDREKERI-- 253
|
....*...
gi 446087495 712 QL-IKQVT 718
Cdd:COG0539 254 SLsLKQLQ 261
|
|
| S1_RPS1_repeat_ec5 |
cd05690 |
S1_RPS1_repeat_ec5: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ... |
633-709 |
2.51e-05 |
|
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: 42.87 E-value: 2.51e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446087495 633 GDEFIGIVSAVTEFGLFVTLKDlYVDGMIHISQLgddffiydqaSQNLIGQNRGQVFGLGDEVKIQVAGVNLEERKI 709
Cdd:cd05690 1 GTVVSGKIKSITDFGIFVGLDG-GIDGLVHISDI----------SWTQRVRHPSEIYKKGQEVEAVVLNIDVERERI 66
|
|
| S1_PNPase |
cd04472 |
S1_PNPase: Polynucleotide phosphorylase (PNPase), ), S1-like RNA-binding domain. PNPase is a ... |
633-703 |
2.92e-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: 42.53 E-value: 2.92e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446087495 633 GDEFIGIVSAVTEFGLFVTL---KDlyvdGMIHISQLGDDFFiydqasqnligQNRGQVFGLGDEVKIQVAGVN 703
Cdd:cd04472 1 GKIYEGKVVKIKDFGAFVEIlpgKD----GLVHISELSDERV-----------EKVEDVLKVGDEVKVKVIEVD 59
|
|
| rpsA |
PRK06299 |
30S ribosomal protein S1; Reviewed |
633-709 |
3.37e-05 |
|
30S ribosomal protein S1; Reviewed
Pssm-ID: 235775 [Multi-domain] Cd Length: 565 Bit Score: 47.47 E-value: 3.37e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446087495 633 GDEFIGIVSAVTEFGLFVTLKDlYVDGMIHISQLGDDFfiydqasqnliGQNRGQVFGLGDEVKIQVAGVNLEERKI 709
Cdd:PRK06299 461 GSIVTGTVTEVKDKGAFVELED-GVEGLIRASELSRDR-----------VEDATEVLKVGDEVEAKVINIDRKNRRI 525
|
|
| YabR |
COG1098 |
Predicted RNA-binding protein, contains ribosomal protein S1 (RPS1) domain [General function ... |
638-735 |
1.53e-04 |
|
Predicted RNA-binding protein, contains ribosomal protein S1 (RPS1) domain [General function prediction only];
Pssm-ID: 440715 [Multi-domain] Cd Length: 130 Bit Score: 42.09 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446087495 638 GIVSAVTEFGLFVTLKDlYVDGMIHISQLGDDFFiydqasqnligQNRGQVFGLGDEVKIQVAGVNlEERKIDFQlIKQV 717
Cdd:COG1098 11 GKVTGITPFGAFVELPE-GTTGLVHISEIADGYV-----------KDINDYLKVGDEVKVKVLSID-EDGKISLS-IKQA 76
|
90 100
....*....|....*....|..
gi 446087495 718 T----HAGRVVRSRAPRTTKTS 735
Cdd:COG1098 77 EekpkRPPRPRRNSRPKAGFES 98
|
|
| rpsA |
TIGR00717 |
ribosomal protein S1; This model describes ribosomal protein S1, RpsA. This protein is found ... |
633-719 |
1.94e-04 |
|
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: 44.72 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446087495 633 GDEFIGIVSAVTEFGLFVTLKDlYVDGMIHISQLgddffiyDQASQNligQNRGQVFGLGDEVKIQVAGVNLEERKIDFQ 712
Cdd:TIGR00717 273 GDKITGRVTNLTDYGVFVEIEE-GIEGLVHVSEM-------SWVKKN---SHPSKVVKKGDEVEVMILDIDPERRRLSLG 341
|
....*..
gi 446087495 713 LiKQVTH 719
Cdd:TIGR00717 342 L-KQCKA 347
|
|
| Tex |
COG2183 |
Transcriptional accessory protein Tex/SPT6 [Transcription]; |
638-709 |
2.38e-04 |
|
Transcriptional accessory protein Tex/SPT6 [Transcription];
Pssm-ID: 441786 [Multi-domain] Cd Length: 719 Bit Score: 44.63 E-value: 2.38e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446087495 638 GIVSAVTEFGLFVtlkDLYV--DGMIHISQLGDDFFiydqasqnligQNRGQVFGLGDEVKIQVAGVNLEERKI 709
Cdd:COG2183 647 GTVTNVTDFGAFV---DIGVhqDGLVHISQLSDRFV-----------KDPREVVKVGDIVKVKVLEVDLKRKRI 706
|
|
| PRK00087 |
PRK00087 |
bifunctional 4-hydroxy-3-methylbut-2-enyl diphosphate reductase/30S ribosomal protein S1; |
633-718 |
2.63e-04 |
|
bifunctional 4-hydroxy-3-methylbut-2-enyl diphosphate reductase/30S ribosomal protein S1;
Pssm-ID: 234623 [Multi-domain] Cd Length: 647 Bit Score: 44.55 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446087495 633 GDEFIGIVSAVTEFGLFVTLKDlyVDGMIHISQLgddffiydqaSQNLIGQNRgQVFGLGDEVKIQVAGVNLEERKIDFQ 712
Cdd:PRK00087 478 GDVVEGEVKRLTDFGAFVDIGG--VDGLLHVSEI----------SWGRVEKPS-DVLKVGDEIKVYILDIDKENKKLSLS 544
|
....*.
gi 446087495 713 LiKQVT 718
Cdd:PRK00087 545 L-KKLL 549
|
|
| PRK11824 |
PRK11824 |
polynucleotide phosphorylase/polyadenylase; Provisional |
633-703 |
4.02e-04 |
|
polynucleotide phosphorylase/polyadenylase; Provisional
Pssm-ID: 236995 [Multi-domain] Cd Length: 693 Bit Score: 43.88 E-value: 4.02e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446087495 633 GDEFIGIVSAVTEFGLFVTLKDlYVDGMIHISQLGDDFFiydqasqnligQNRGQVFGLGDEVKIQVAGVN 703
Cdd:PRK11824 622 GEIYEGKVVRIVDFGAFVEILP-GKDGLVHISEIADERV-----------EKVEDVLKEGDEVKVKVLEID 680
|
|
| S1_RPS1_repeat_ec4 |
cd05689 |
S1_RPS1_repeat_ec4: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ... |
633-709 |
7.50e-04 |
|
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: 38.71 E-value: 7.50e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446087495 633 GDEFIGIVSAVTEFGLFVTLKDlYVDGMIHISQLgddffiyDQASQNLigqNRGQVFGLGDEVKIQVAGVNLEERKI 709
Cdd:cd05689 4 GTRLFGKVTNLTDYGCFVELEE-GVEGLVHVSEM-------DWTNKNI---HPSKVVSLGDEVEVMVLDIDEERRRI 69
|
|
| S1_RPS1_repeat_hs4 |
cd05692 |
S1_RPS1_repeat_hs4: Ribosomal protein S1 (RPS1) domain. RPS1 is a component of the small ... |
633-707 |
1.19e-03 |
|
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: 38.04 E-value: 1.19e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446087495 633 GDEFIGIVSAVTEFGLFVTLKDlYVDGMIHISQLGDDFFiydqasqnligQNRGQVFGLGDEVKIQVAGVNLEER 707
Cdd:cd05692 1 GSVVEGTVTRLKPFGAFVELGG-GISGLVHISQIAHKRV-----------KDVKDVLKEGDKVKVKVLSIDARGR 63
|
|
| rpsA |
TIGR00717 |
ribosomal protein S1; This model describes ribosomal protein S1, RpsA. This protein is found ... |
633-718 |
2.01e-03 |
|
ribosomal protein S1; This model describes ribosomal protein S1, RpsA. This protein is found in most bacterial genomes in a single copy, but is not present in the Mycoplasmas. It is heterogeneous with respect to the number of repeats of the S1 RNA binding domain described by pfam00575: six repeats in E. coli and most other bacteria, four in Bacillus subtilis and some other species. rpsA is an essential gene in E. coli but not in B. subtilis. It is associated with the cytidylate kinase gene cmk in many species, and fused to it in Treponema pallidum. RpsA is proposed (Medline:97323001) to assist in mRNA degradation. This model provides trusted hits to most long form (6 repeat) examples of RpsA. Among homologs with only four repeats are some to which other (perhaps secondary) functions have been assigned. [Protein synthesis, Ribosomal proteins: synthesis and modification]
Pssm-ID: 273232 [Multi-domain] Cd Length: 516 Bit Score: 41.64 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446087495 633 GDEFIGIVSAVTEFGLFVTLKDlYVDGMIHISQLgddffiydqaSQNLIGQNRGQVFGLGDEVKIQVAGVNLEERKIDFQ 712
Cdd:TIGR00717 360 GDRVTGKIKKITDFGAFVELEG-GIDGLIHLSDI----------SWDKDGREADHLYKKGDEIEAVVLAVDKEKKRISLG 428
|
....*.
gi 446087495 713 lIKQVT 718
Cdd:TIGR00717 429 -VKQLT 433
|
|
| rpsA |
TIGR00717 |
ribosomal protein S1; This model describes ribosomal protein S1, RpsA. This protein is found ... |
633-711 |
3.00e-03 |
|
ribosomal protein S1; This model describes ribosomal protein S1, RpsA. This protein is found in most bacterial genomes in a single copy, but is not present in the Mycoplasmas. It is heterogeneous with respect to the number of repeats of the S1 RNA binding domain described by pfam00575: six repeats in E. coli and most other bacteria, four in Bacillus subtilis and some other species. rpsA is an essential gene in E. coli but not in B. subtilis. It is associated with the cytidylate kinase gene cmk in many species, and fused to it in Treponema pallidum. RpsA is proposed (Medline:97323001) to assist in mRNA degradation. This model provides trusted hits to most long form (6 repeat) examples of RpsA. Among homologs with only four repeats are some to which other (perhaps secondary) functions have been assigned. [Protein synthesis, Ribosomal proteins: synthesis and modification]
Pssm-ID: 273232 [Multi-domain] Cd Length: 516 Bit Score: 40.87 E-value: 3.00e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446087495 633 GDEFIGIVSAVTEFGLFVTLKDlYVDGMIHISQLGDDFFiydqasqnligQNRGQVFGLGDEVKIQVAGVNLEERKIDF 711
Cdd:TIGR00717 447 GSVVKGKVTEIKDFGAFVELPG-GVEGLIRNSELSENRD-----------EDKTDEIKVGDEVEAKVVDIDKKNRKVSL 513
|
|
| rpsA |
PRK06299 |
30S ribosomal protein S1; Reviewed |
633-718 |
4.44e-03 |
|
30S ribosomal protein S1; Reviewed
Pssm-ID: 235775 [Multi-domain] Cd Length: 565 Bit Score: 40.53 E-value: 4.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446087495 633 GDEFIGIVSAVTEFGLFVTLKDlYVDGMIHISQLgdDFfiydqaSQNLIgqNRGQVFGLGDEVKIQVAGVNLEERKIdfQ 712
Cdd:PRK06299 287 GSKVKGKVTNITDYGAFVELEE-GIEGLVHVSEM--SW------TKKNK--HPSKVVSVGQEVEVMVLEIDEEKRRI--S 353
|
....*..
gi 446087495 713 L-IKQVT 718
Cdd:PRK06299 354 LgLKQCK 360
|
|
| rpsA |
PRK07899 |
30S ribosomal protein S1; Reviewed |
638-718 |
5.35e-03 |
|
30S ribosomal protein S1; Reviewed
Pssm-ID: 236126 [Multi-domain] Cd Length: 486 Bit Score: 40.03 E-value: 5.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446087495 638 GIVSAVTEFGLFVTLKDlYVDGMIHISQLgddffiydqASQNLigQNRGQVFGLGDEVKIQVAGVNLEERKIDFQLiKQV 717
Cdd:PRK07899 299 GKVTKLVPFGAFVRVEE-GIEGLVHISEL---------AERHV--EVPEQVVQVGDEVFVKVIDIDLERRRISLSL-KQA 365
|
.
gi 446087495 718 T 718
Cdd:PRK07899 366 N 366
|
|
| S1_RecJ_like |
cd04473 |
S1_RecJ_like: The S1 domain of the archaea-specific RecJ-like exonuclease. The function of ... |
636-711 |
7.36e-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: 7.36e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446087495 636 FIGIVSAVTEFGLFVTLKDlYVDGMIHISQLGDDFFIydqasqnligqnrgqvfglGDEVKIQVAGVnLEERKIDF 711
Cdd:cd04473 20 YKGKVNGVAKYGVFVDLND-HVRGLIHRSNLLRDYEV-------------------GDEVIVQVTDI-PENGNIDL 74
|
|
| |
