|
Name |
Accession |
Description |
Interval |
E-value |
| glnD |
PRK00275 |
PII uridylyl-transferase; Provisional |
1-894 |
0e+00 |
|
PII uridylyl-transferase; Provisional
Pssm-ID: 234709 [Multi-domain] Cd Length: 895 Bit Score: 1812.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 1 MPQVDPDLFDRGQFQAELALKASPIAAFKKAIRRAKDVLDDRFRSGRDIRRLIEDRAWFVDNILQKAWDQFEWSEDADIA 80
Cdd:PRK00275 1 MPQVDPELFDRGQFQAELALKASPIAAFKKAIRQAREVLDERFRSGRDIRRLIEDRAWFVDQILQQAWHQFDWSDDADIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 81 LLAVGGYGRGELHPYSDIDLLILLDSDDHEIFREPIERFLTLLWDIGLEVGQSVRSVNECAQEGLADLTVITNLMESRTI 160
Cdd:PRK00275 81 LVAVGGYGRGELHPYSDIDLLILLDSADHEEFREPIERFLTLLWDIGLEIGQSVRSVDECAEEARADLTVITNLMESRTI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 161 AGPEHLRQRMLEVTSTQHMWPSKEFFLAKHAEQKKRHHKYNDTEYNLEPNVKGSPGGLRDIQTILWVARRQYGTLNLHAL 240
Cdd:PRK00275 161 AGPESLRQRMLEVTSSEHMWPSKEFFLAKRAEQKARHHKYNDTEYNLEPNVKGSPGGLRDIQTILWVAKRQFGTLNLHAL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 241 AGEGFLLGSENALLASSQEFLWKVRYALHMLAGRSEDRLLFDYQVRIAGLLGYEDSDAKLAIERFMQKYYRVVMSIAELS 320
Cdd:PRK00275 241 VGEGFLTESEYGLLASGQEFLWKVRYALHMLAGRAEDRLLFDHQRSIATLLGYEDSDAKLAVEQFMQKYYRVVMALAELN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 321 DLIIQHFEEVIL-SDDSGTAQPINSRFQLHDGYIEATNPNVFKRTPFAMIEIFVLMAQHPEIKGVRADTIRLLREHRHLI 399
Cdd:PRK00275 321 DLILQHFEEVILaADDSGTIQPLNSRFQLRDGYIEATHPNVFKRTPFALLEIFVLMAQHPEIKGVRADTIRLLREHRHLI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 400 NDDFRNDIRNTSLFIELFKCETGIHRNLRRMNRYGILGLYLPEFGHIVGQMQHDLFHIYTVDAHTLNLIKHLRKLQYTEV 479
Cdd:PRK00275 401 DDAFRNDIRNTSLFIELFKCPIGIHRNLRRMNRYGILGRYLPEFGHIVGQMQHDLFHIYTVDAHTLNLIKNLRKLRYPEV 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 480 SEKFPLASKIMARLPKPELIYLAGLYHDIGKGRGGDHSELGAIDAQAFGTRHHLPDWDTRLIVWLVSNHLVMSTTAQRKD 559
Cdd:PRK00275 481 SEKFPLASKLMGRLPKPELLYIAGLYHDIGKGRGGDHSELGAVDAEAFCQRHQLPAWDTRLVVWLVENHLLMSTTAQRKD 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 560 LSDPQVIHDFAQFVGDEVHLDYLYVLTVADINATNPTLWNSWRASLLRQLYTETKRALRRGLENPVDREEQIRRTQTAAL 639
Cdd:PRK00275 561 LSDPQVIHDFALKVGDQTHLDYLYVLTVADINATNPTLWNSWRASLLRQLYTETKRALRRGLENPVDREEQIRQTQSAAL 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 640 DILVRNGTDPDDVEQLWSALGDDYFLRHTAGDVAWHSDAILQQPADGGPLVLIKETTQREFEGGTQIFIYAPDQHDFFAV 719
Cdd:PRK00275 641 DILVRKGTDPDDAEQLWSQLGDDYFLRHTAGDIAWHTEAILQHPDDGGPLVLIKETTQREFEGGTQIFIYAPDQHDFFAA 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 720 TVAAMDQLNLNIHDARIITSSSKFTLDTYIVLDNEGGSIGDNPERVQEIRNGLTEALRNPDDYPTIIKRRVPRQLKHFAF 799
Cdd:PRK00275 721 TVAAMDQLNLNIHDARIITSSSQFTLDTYIVLDDDGEPIGDNPARIEQIREGLTEALRNPDDYPTIIQRRVPRQLKHFAF 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 800 APQVTIHNDAQRPVTVLELLAPDRPGLLARIGKIFLEFDLSLQNAKIATLGERVEDVFFITDANNHPLSDPQLCSQLQDA 879
Cdd:PRK00275 801 PTQVTISNDAQRPVTVLEIIAPDRPGLLARIGRIFLEFDLSLQNAKIATLGERVEDVFFITDADNQPLSDPQLCSRLQDA 880
|
890
....*....|....*
gi 488617883 880 IVKQLSVNSEPGHDL 894
Cdd:PRK00275 881 ICEQLDARNEKDTSP 895
|
|
| GlnD |
COG2844 |
UTP:GlnB (protein PII) uridylyltransferase [Posttranslational modification, protein turnover, ... |
22-889 |
0e+00 |
|
UTP:GlnB (protein PII) uridylyltransferase [Posttranslational modification, protein turnover, chaperones, Signal transduction mechanisms];
Pssm-ID: 442092 [Multi-domain] Cd Length: 864 Bit Score: 1261.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 22 ASPIAAFKKAIRRAKDVLDDRFRSGRDIRRLIEDRAWFVDNILQKAWDQFEWSEDADIALLAVGGYGRGELHPY------ 95
Cdd:COG2844 1 AAALAALREALAEGRAALRERFRAGADGRELVRARAALVDQLLRALWDLAGLTEPERLALVAVGGYGRGELAPHsdidll 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 96 --SDIDLLilldsddhEIFREPIERFLTLLWDIGLEVGQSVRSVNECAQEGLADLTVITNLMESRTIAGPEHLRQRMLEV 173
Cdd:COG2844 81 flLPDKPT--------PALEEVIEAFLYLLWDLGLEVGHSVRTVDECLREAREDITVRTALLEARLLAGDEALFEELRER 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 174 TSTQHMWPSKEFFLAKHAEQKKRHHKYNDTEYNLEPNVKGSPGGLRDIQTILWVARRQYGTLNLHALAGEGFLLGSENAL 253
Cdd:COG2844 153 FRADVFWDSRAFFEAKLAEQRERHAKYGDTRYNLEPNIKEGPGGLRDLQTLLWIAKRHFGVRSLEELVKKGLLTEEEYRE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 254 LASSQEFLWKVRYALHMLAGRSEDRLLFDYQVRIAGLLGYEDSDAKLAIERFMQKYYRVVMSIAELSDLIIQHFEEVILS 333
Cdd:COG2844 233 LRRAEDFLWRVRFALHLLAGRAEDRLLFDLQREVAERLGYQDTEGNRAVERFMQRYYRTAKAVGRLNEILLQRLEEAILK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 334 DDS-GTAQPINSRFQLHDGYIEATNPNVFKRTPFAMIEIFVLMAQHPEIKGVRADTIRLLREHRHLINDDFRNDIRNTSL 412
Cdd:COG2844 313 PPGlRRPRPINEGFQLRNGRLEVADPDVFERDPVALLRLFLLAAQHPEGLGIHPDTLRLLRRALRLIDDAFRRDPEARRL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 413 FIELFKCETGIHRNLRRMNRYGILGLYLPEFGHIVGQMQHDLFHIYTVDAHTLNLIKHLRKLQYTEVSEKFPLASKIMAR 492
Cdd:COG2844 393 FLEILRQPRGITRALRRMNEYGVLGRYIPEFGRIVGQMQFDLFHVYTVDEHTLRVVRNLRRFERGELAEEFPLASELIAE 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 493 LPKPELIYLAGLYHDIGKGRGGDHSELGAIDAQAFGTRHHLPDWDTRLIVWLVSNHLVMSTTAQRKDLSDPQVIHDFAQF 572
Cdd:COG2844 473 LPKPELLYLAALFHDIAKGRGGDHSELGAEDARRFCPRHGLSPEDTELVAWLVRHHLLMSHTAQRRDISDPEVIRDFARL 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 573 VGDEVHLDYLYVLTVADINATNPTLWNSWRASLLRQLYTETKRALRRGLEnPVDREEQIRRTQTAALDILVRNGTDPDDV 652
Cdd:COG2844 553 VGSEERLDYLYLLTVADIRATGPKVWNSWKASLLRELYRATLRALRGGLE-PPDREERIEERKEEALALLADQGWDEEEI 631
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 653 EQLWSALGDDYFLRHTAGDVAWHSDAILQQPADGGPLVLIKETTQRefeGGTQIFIYAPDQHDFFAVTVAAMDQLNLNIH 732
Cdd:COG2844 632 EALWARLPDDYFLRHDPEEIAWHARLLLRADDSGKPLVLIRPDPDR---GGTEVFVYTPDRPGLFARIAGALAALGLNIL 708
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 733 DARIITSSSKFTLDTYIVLDNEGGSIgDNPERVQEIRNGLTEALRNPDDYPTIIKRRVPRQLKHFAFAPQVTIHNDAQRP 812
Cdd:COG2844 709 DARIHTTRDGYALDTFIVLDPDGEPI-DDPDRLERIEQALEEALSGEVPLPEPLARRLSRRLRHFPVPPRVTFDNDASNR 787
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488617883 813 VTVLELLAPDRPGLLARIGKIFLEFDLSLQNAKIATLGERVEDVFFITDANNHPLSDPQLCSQLQDAIVKQLSVNSE 889
Cdd:COG2844 788 YTVLEVSALDRPGLLYDIARVLADLGLNIHSAKIATLGERVEDVFYVTDLDGQKLTDPERQEALREALLEALDEEAE 864
|
|
| UTase_glnD |
TIGR01693 |
[Protein-PII] uridylyltransferase; This model describes GlnD, the uridylyltransferase ... |
36-884 |
0e+00 |
|
[Protein-PII] uridylyltransferase; This model describes GlnD, the uridylyltransferase/uridylyl-removing enzyme for the nitrogen regulatory protein PII. Not all homologs of PII share the property of uridylyltransferase modification on the characteristic Tyr residue (see Prosite pattern PS00496 and document PDOC00439), but the modification site is preserved in the PII homolog of all species with a member of this family. [Central intermediary metabolism, Nitrogen metabolism, Regulatory functions, Protein interactions]
Pssm-ID: 273761 [Multi-domain] Cd Length: 850 Bit Score: 1034.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 36 KDVLDDRFRSGRDIRRLIEDRAWFVDNILQKAWDQFEWSEDADIALLAVGGYGRGELHPYSDIDLLILLDSDDHEIFREP 115
Cdd:TIGR01693 1 REELLEEFARGGDGRELREGRSDLTDLLLIRLWDFIGISEHSGIALVAVGGYGRGELAPYSDIDLLFLHDGKPAEEVEPK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 116 IERFLTLLWDIGLEVGQSVRSVNECAQEGLADLTVITNLMESRTIAGPEHLRQRMLEVTSTQHMWPS-KEFFLAKHAEQK 194
Cdd:TIGR01693 81 IERFLYPLWDLGFEVGHSVRTLEECARIAKADLTVATNLLEARHLAGDEALFFRLKERVRREDWRNTaRSFLAAKVEEQD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 195 KRHHKYNDTEYNLEPNVKGSPGGLRDIQTILWVARRQYGTLNLHALAGEGFLLGSENALLASSQEFLWKVRYALHMLAGR 274
Cdd:TIGR01693 161 ERHARYGDTAYNLEPDIKEGPGGLRDLHTLFWVALYQLGVRRLEDLVKQGFLTDAEYKLLAEARDFLWDVRFALHLTTGR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 275 SEDRLLFDYQVRIAGLLGYEDsDAKLAIERFMQKYYRVVMSIAELSDLIIQHFEEVILSDDSGT------AQPINSRFQL 348
Cdd:TIGR01693 241 ADDRLLFDHQDEIAAALGYGD-EGNPAVERFMRRYFQAARRIGYLTEAFLRHYEEALLSRGPSArvrrpkRRPLDEGFVE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 349 HDGYIEATNPNVFKRTPFAMIEIFVLMAQHPEikGVRADTIRLLREHRHLINDDFRNDIRNTSLFIELFKCETGIHRNLR 428
Cdd:TIGR01693 320 DGGELVLARTAVFERDPALLLRLFAIAAQRGL--PIHPAALRQLTASLPLLPTPLREDPEARELFLELLTSGNGTVRALR 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 429 RMNRYGILGLYLPEFGHIVGQMQHDLFHIYTVDAHTLNLIKHLRKLQYTEVSEKFPLASKIMARLPKPELIYLAGLYHDI 508
Cdd:TIGR01693 398 AMNRAGVLGRFLPEWGRIVGQMQFDLFHVYTVDEHTLRTVVHLAPFARGRLAREHPLASELMPKIEDPELLYLAALLHDI 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 509 GKGRGGDHSELGAIDAQAFGTRHHLPDWDTRLIVWLVSNHLVMSTTAQRKDLSDPQVIHDFAQFVGDEVHLDYLYVLTVA 588
Cdd:TIGR01693 478 GKGRGGDHSVLGAEDARDVCPRLGLDRPDTELVAWLVRNHLLMSITAQRRDLNDPKTVFAFAEAVGDPERLEYLLALTVA 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 589 DINATNPTLWNSWRASLLRQLYTETKRALRRGLENPVDREEQIRRTQTAALDILvRNGTDPDDVEQLWSALGDDYFLRHT 668
Cdd:TIGR01693 558 DIRATGPGVWNSWKASLLRDLYNRTEQVLRGGLEPPADPAEPIAEQRKLAVALL-RTDYTSNEAEVLWLRAYDDYFLRFT 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 669 AGDVAWHSDAILQQPADGGPLVLIKETTQRefeGGTQIFIYAPDQHDFFAVTVAAMDQLNLNIHDARIITSSSKFTLDTY 748
Cdd:TIGR01693 637 HKEIAWHAESLRRALSSGGPLALIDGTRPS---GGTEVFIYAPDQPGLFAKVAGALAMLSLSVHDAQVNTTKDGVALDTF 713
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 749 IVLDNEGGSIGDNPeRVQEIRNGLTEALRNP-DDYPTIIKRR-VPRQLKHFAFAPQVTIHNDAQRPVTVLELLAPDRPGL 826
Cdd:TIGR01693 714 VVQDLFGSPPAAER-VFQELLQGLVDVLAGLaKDPDTISARRaRRRRLQHFAVPPRVTILNTASRKATIMEVRALDRPGL 792
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*...
gi 488617883 827 LARIGKIFLEFDLSLQNAKIATLGERVEDVFFITDANNHPLSDpQLCSQLQDAIVKQL 884
Cdd:TIGR01693 793 LARVGRTLEELGLSIQSAKITTFGEKAEDVFYVTDLFGLKLTD-EEEQRLLEVLAASV 849
|
|
| PRK05007 |
PRK05007 |
bifunctional uridylyltransferase/uridylyl-removing protein GlnD; |
1-887 |
0e+00 |
|
bifunctional uridylyltransferase/uridylyl-removing protein GlnD;
Pssm-ID: 235329 [Multi-domain] Cd Length: 884 Bit Score: 922.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 1 MPQVDPDLFDRGQFQAELAlkaspiaafKKAIRRAKDVLDDRFRSGRDIRRLIEDRAWFVDNILQKAWDQFEWSEDADIA 80
Cdd:PRK05007 12 GQPQSPLTWPDDELTVGGL---------KQHLDTFQQWLGDAFDAGISAEQLVEARTEFIDQLLQRLWIEAGFDQIPDLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 81 LLAVGGYGRGELHPYSDIDLLILLDSDDHEIFREPIERFLTLLWDIGLEVGQSVRSVNECAQEGLADLTVITNLMESRTI 160
Cdd:PRK05007 83 LVAVGGYGRGELHPLSDIDLLILSRKKLPDEQAQKVGELITLLWDLKLEVGHSVRTLEECLLEGLSDLTVATNLIESRLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 161 AGPEHLRQRMLEVTSTQHMWPSKEFFLAKHAEQKKRHHKYNDTEYNLEPNVKGSPGGLRDIQTILWVARRQYGTLNLHAL 240
Cdd:PRK05007 163 CGDVALFLELQKHIFSDGFWPSEKFYAAKVEEQNERHQRYHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSLDEM 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 241 AGEGFLLGSENALLASSQEFLWKVRYALHMLAGRSEDRLLFDYQVRIAGLLGYEDsDAKLAIERFMQKYYRVVMSIAELS 320
Cdd:PRK05007 243 VGFGFLTPAERAELNECQHFLWRIRFALHLVLSRYDNRLLFDRQLSVAQLLGYEG-EGNEPVERMMKDYYRTTRRVSELN 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 321 DLIIQHFEEVILS-DDSGTAQPINSRFQLHDGYIEATNPNVFKRTPFAMIEIFVLMAQHPEIKGVRADTIRLLREHRHLI 399
Cdd:PRK05007 322 QMLLQLFDEAILAlTADEKPRPIDDEFQLRGTLIDLRDETLFQRQPEAILRMFYLMARNSNITGIYSTTLRQLRHARRHL 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 400 NDDFRNDIRNTSLFIELFKCETGIHRNLRRMNRYGILGLYLPEFGHIVGQMQHDLFHIYTVDAHTLNLIKHLRKLQYTEV 479
Cdd:PRK05007 402 NQPLCEIPEARKLFMEILRHPGAVSRALLPMHRHSVLSAYMPQWSHIVGQMQFDLFHAYTVDEHTIRVLLKLESFADEET 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 480 SEKFPLASKIMARLPKPELIYLAGLYHDIGKGRGGDHSELGAIDAQAFGTRHHLPDWDTRLIVWLVSNHLVMSTTAQRKD 559
Cdd:PRK05007 482 RQRHPLCVELYPRLPKKELLLLAALFHDIAKGRGGDHSILGAQDALEFAELHGLNSRETQLVAWLVRNHLLMSVTAQRRD 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 560 LSDPQVIHDFAQFVGDEVHLDYLYVLTVADINATNPTLWNSWRASLLRQLYTETKRALRRGLENPVDREEQIRRTQTAAL 639
Cdd:PRK05007 562 IQDPDVIKQFAEEVQDENRLRYLVCLTVADICATNETLWNSWKQSLLRELYFATEKQLRRGMENPPDMRERVRHHQLQAL 641
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 640 DILVRNGTDPDDVEQLWSALGDDYFLRHTAGDVAWHSDAILQQPADgGPLVLIKETTQRefeGGTQIFIYAPDQHDFFAV 719
Cdd:PRK05007 642 ALLRMDNIDEEALHQIWSRCRADYFLRHTPNQLAWHARHLLQHDLD-KPLVLLSKQATR---GGTEIFIWSPDRPYLFAA 717
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 720 TVAAMDQLNLNIHDARIITSSSKFTLDTYIVLDNEGGSIgdNPERVQEIRNGLTEALRNPDdyPTIIK-RRVPRQLKHFA 798
Cdd:PRK05007 718 VCAELDRRNLSVHDAQIFTSRDGMAMDTFIVLEPDGSPL--SQDRHQVIRKALEQALTQSS--PQPPKpRRLPAKLRHFN 793
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 799 FAPQVTI---HNDAQrpvTVLELLAPDRPGLLARIGKIFLEFDLSLQNAKIATLGERVEDVFFITDANNHPLSDPQLcSQ 875
Cdd:PRK05007 794 VPTEVSFlptHTDRR---SYMELIALDQPGLLARVGKIFADLGISLHGARITTIGERVEDLFILATADRRALNEELQ-QE 869
|
890
....*....|..
gi 488617883 876 LQDAIVKQLSVN 887
Cdd:PRK05007 870 LRQRLTEALNPN 881
|
|
| PRK03059 |
PRK03059 |
PII uridylyl-transferase; Provisional |
18-886 |
0e+00 |
|
PII uridylyl-transferase; Provisional
Pssm-ID: 235101 [Multi-domain] Cd Length: 856 Bit Score: 867.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 18 LALKASPIAAFKKAIRRAKDVLDDRFRSGRDIRRLIEDRAWFVDNILQKAWDQFEWseDADIALLAVGGYGRGELHPYSD 97
Cdd:PRK03059 3 TAAPPPPAASLRAELKAAKAALLARFRQAPNVTALLHALSRLVDQALRRLWQECGL--PAGAALVAVGGYGRGELFPYSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 98 IDLLILLDSDDHEIFREPIERFLTLLWDIGLEVGQSVRSVNECAQEGLADLTVITNLMESRTIAGPEHLRQRMLevTSTQ 177
Cdd:PRK03059 81 VDLLVLLPDAPDAALDARIERFIGLCWDLGLEIGSSVRTVDECIEEAAQDVTVQTSLLEARLLTGSAALFERFQ--RRYR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 178 HMWPSKEFFLAKHAEQKKRHHKYNDTEYNLEPNVKGSPGGLRDIQTILWVARR-QYGTlNLHALAGEGFLLGSENALLAS 256
Cdd:PRK03059 159 AALDPRAFFQAKLLEMRQRHAKFQDTPYSLEPNCKESPGGLRDLQTILWIARAaGLGS-SWRELAKRGLITDREARQLRR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 257 SQEFLWKVRYALHMLAGRSEDRLLFDYQVRIAGLLGYEDSDAKLAIERFMQKYYRVVMSIAELSDLIIQHFEEVILSDDS 336
Cdd:PRK03059 238 NERFLKTLRARLHLLAGRREDRLVFDLQTALAESFGYRPTAAKRASEQLMRRYYWAAKAVTQLNTILLQNIEARLFPSTS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 337 GTAQPINSRFQLHDGYIEATNPNVFKRTPFAMIEIFVLMAQHPEIKGVRADTIRLLREHRHLINDDFRNDIRNTSLFIEL 416
Cdd:PRK03059 318 GITRVINERFVEKQGMLEIASDDLFERHPHAILEAFLLYQQTPGLKGLSARTLRALYNARDVMNAAFRRDPVNRALFMQI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 417 FKCETGIHRNLRRMNRYGILGLYLPEFGHIVGQMQHDLFHIYTVDAHTLNLIKHLRKLQYTEVSEKFPLASKIMARLPKP 496
Cdd:PRK03059 398 LQQPRGITHALRLMNQTSVLGRYLPNFRRIVGQMQHDLFHVYTVDQHILMVLRNLRRFAMAEHAHEYPFCSQLIANFDRP 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 497 ELIYLAGLYHDIGKGRGGDHSELGAIDAQAFGTRHHLPDWDTRLIVWLVSNHLVMSTTAQRKDLSDPQVIHDFAQFVGDE 576
Cdd:PRK03059 478 WLLYVAALFHDIAKGRGGDHSTLGAVDARRFCRQHGLAREDAELVVWLVEHHLTMSQVAQKQDLSDPEVIARFAELVGDE 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 577 VHLDYLYVLTVADINATNPTLWNSWRASLLRQLYTETKRALRRGlenPVDREEQIRRTQTAALDILVRNGTDPDDVEQLW 656
Cdd:PRK03059 558 RRLTALYLLTVADIRGTSPKVWNAWKGKLLEDLYRATLRVLGGA---APDAHSELEARKEEALALLRLEALPDDAHEALW 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 657 SALGDDYFLRHTAGDVAWHSDAILQQPADGGPLVlikETTQREFEGGTQIFIYAPDQHDFFAVTVAAMDQLNLNIHDARI 736
Cdd:PRK03059 635 DQLDVGYFLRHDAADIAWHTRHLYRHVDTDTPIV---RARLSPAGEGLQVMVYTPDQPDLFARICGYFDRAGFSILDARV 711
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 737 ITSSSKFTLDTYIVLDNEGGsiGDNPERVQEIRNGLTEALRNPDDYPTIIKRRVPRQLKHFAFAPQVTIHNDAQRPVTVL 816
Cdd:PRK03059 712 HTTRHGYALDTFQVLDPEED--VHYRDIINLVEHELAERLAEQAPLPEPSKGRLSRQVKHFPITPRVDLRPDERGQYYIL 789
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 817 ELLAPDRPGLLARIGKIFLEFDLSLQNAKIATLGERVEDVFFITDANnhpLSDPQLCSQLQDAIVKQLSV 886
Cdd:PRK03059 790 SVSANDRPGLLYAIARVLAEHRVSVHTAKINTLGERVEDTFLIDGSG---LSDNRLQIQLETELLDALAV 856
|
|
| glnD |
PRK01759 |
bifunctional uridylyltransferase/uridylyl-removing protein GlnD; |
48-885 |
0e+00 |
|
bifunctional uridylyltransferase/uridylyl-removing protein GlnD;
Pssm-ID: 234980 [Multi-domain] Cd Length: 854 Bit Score: 714.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 48 DIRRLIEDRAWFVDNILQKAWDQFEWSEDADIALLAVGGYGRGELHPYSDIDLLILLDSDDHEIFREPIERFLTLLWDIG 127
Cdd:PRK01759 26 DVFELIENRSDFYDQLLIHLWQQFGLEEQSDLALIAVGGYGRREMFPLSDLDILILTEQPPDEETEEKINQFFQFLWDCG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 128 LEVGQSVRSVNECAQEGLADLTVITNLMESRTIAGPEHLRQRMLEVTSTQHMWPSKEFFLAKHAEQKKRHHKYNDTEYNL 207
Cdd:PRK01759 106 FEVGASVRTLAECESEGRADITIATNLLESRFLTGNEKLFDALVELLQQADFWSKEAFFQAKIQEKIERYQRYHNTSYNL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 208 EPNVKGSPGGLRDIQTILWVARRQYGTLNLHALAGEGFLLGSENALLASSQEFLWKVRYALHMLAGRSEDRLLFDYQVRI 287
Cdd:PRK01759 186 EPDIKYSPGGLRDLHLLYWIALRHSGAKSLEEILQSGFIYPEEYAELQQSQQFLFKVRFALHLILKRYDNRLLFDRQLKV 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 288 AGLLGYEdSDAKLAIERFMQKYYRVVMSIAELSDLIIQHFEEVILSDDSGTA-QPINSRFQLHDGYIEATNPNVFKRTPF 366
Cdd:PRK01759 266 SELLGFQ-GEGNQGVEKMMKSFFQALQSISLLSDLLVKHYREHFLQPNQNVEiQPLDDDFYLINNAICLRNPDCFEQQPE 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 367 AMIEIFVLMAQHPEIKgVRADTIRLLREHRHLINDDFRNDIRNTSLFIELFKCETGIHRNLRRMNRYGILGLYLPEFGHI 446
Cdd:PRK01759 345 SILDLFFYLTQYPQAE-IHSTTLRQLRLALEQLQQPLCELPAARERFLRLFNQPNAIKRALVPMHQYGVLTAYLPQWKGI 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 447 VGQMQHDLFHIYTVDAHTLNLIKHLRKLQYTEVSEKFPLASKIMARLPKPELIYLAGLYHDIGKGRGGDHSELGAIDAQA 526
Cdd:PRK01759 424 VGLMQFDLFHIYTVDEHTLRVMLKLESFLDEESAEQHPICHQIFSQLSDRTLLYIAALFHDIAKGRGGDHAELGAVDMRQ 503
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 527 FGTRHHLPDWDTRLIVWLVSNHLVMSTTAQRKDLSDPQVIHDFAQFVGDEVHLDYLYVLTVADINATNPTLWNSWRASLL 606
Cdd:PRK01759 504 FAQQHGFDQREIETMAWLVQQHLLMSVTAQRRDIHDPEVVMNFAEEVQNQVRLDYLTCLTVADICATNETLWNSWKRSLF 583
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 607 RQLYTETKRALRRGLENPVDREEQIRRTQTAALDILVRNGTDPDD--VEQLWSALGDDYFLRHTAGDVAWHSDAILQQPA 684
Cdd:PRK01759 584 ATLYQFTNQQFQQGMDELLDYQEKAEENRQQALELLQQKYSALSEtqIEQLWQRCPEDYFLRNTPKQIAWHALLLLDFRG 663
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 685 DggPLVLIketTQREFEGGTQIFIYAPDQHDFFAVTVAAMDQLNLNIHDARIITSSSKFTLDTYIVLDNEGGSIGDnpER 764
Cdd:PRK01759 664 D--LLVKI---SNRFSRGGTEIFIYCQDQANLFLKVVSTIGAKKLSIHDAQIITSQDGYVLDSFIVTELNGKLLEF--DR 736
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 765 VQEIRNGLTEALRNpdDYPTIIKRRVPRQLKHFAFAPQVTIHNDAQRPVTVLELLAPDRPGLLARIGKIFLEFDLSLQNA 844
Cdd:PRK01759 737 RRQLEQALTKALNT--NKLKKLNLEENHKLQHFHVKTEVRFLNEEKQEQTEMELFALDRAGLLAQVSQVFSELNLNLLNA 814
|
810 820 830 840
....*....|....*....|....*....|....*....|.
gi 488617883 845 KIATLGERVEDVFFITDANNHPLSDPQLcSQLQDAIVKQLS 885
Cdd:PRK01759 815 KITTIGEKAEDFFILTNQQGQALDEEER-KALKSRLLSNLS 854
|
|
| PRK04374 |
PRK04374 |
[protein-PII] uridylyltransferase; |
16-880 |
0e+00 |
|
[protein-PII] uridylyltransferase;
Pssm-ID: 179839 [Multi-domain] Cd Length: 869 Bit Score: 624.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 16 AELALKASPIAAFKKAIRRAKDVLDDRFRSGRDIRRLIEDRAWFVDNILQKAWDQFeWSEDADIALLAVGGYGRGELHPY 95
Cdd:PRK04374 11 PGVAGDADWAAAARPLLVHADMRLCKRFDQGEPIERLLALRARAVDQLMRNAWTRC-IPADSGLSLHAVGGYGRGELFPR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 96 SDIDLLILLDSDDHEIFREPIERFLTLLWDIGLEVGQSVRSVNECaQEGLADLTVITNLMESRTIAGPEHLRQRMLEVTS 175
Cdd:PRK04374 90 SDVDLLVLGETAAQQRHEQALARLFALLWDVGLPISHAVRSPAQC-TAAAADQTVLTALIESRPLVADAAARAALAAAIA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 176 TQHMWPSKEFFLAKHAEQKKRHHKYNDTEYNLEPNVKGSPGGLRDIQTILWVARRQYGTLNLHALAGEGFLLGSENALLA 255
Cdd:PRK04374 169 PQQVWPPRAFFQAKREELLARHQRFGDTADNLEPDIKDGPGGLRDLQTLGWMALRAFGVKDLEALVGLGHVGCDEAAALR 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 256 SSQEFLWKVRYALHMLAGRSEDRLLFDYQVRIAGLLGYEDSDAKLAIERFMQKYYRVVMSIAELSDLIIQHFEEVIlsDD 335
Cdd:PRK04374 249 REREELARLRFGLHLVANRPEERLRFDYQKTLAERLGFADDPESLGVEKMMQRFYRSAALIRRISDRLLQRFEEQF--DG 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 336 SGTAQPINSRFQLHDGYIEATNPNVFKRTPFAMIEIFVLMAQHPEIKGVRADTIRLLREHRHLINDDFRNDIRNTSLFIE 415
Cdd:PRK04374 327 EATPEPLGGGFSLRRGYLAADADSWPDGDVLQVFALFAQWAAHREVRGLHSLTARALAEVLRDLPAYDVADATARERFMA 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 416 LFKCETGIhRNLRRMNRYGILGLYLPEFGHIVGQMQHDLFHIYTVDAHTLNLIKHLRKLQYTEVSEKFPLASKIMARLPK 495
Cdd:PRK04374 407 LLRGPRAV-ETLNRMARLGVLGQWIPAFASVSGRMQFDLFHVYTVDQHTLMVLRNIALFAAGRADERFSIAHEVWPRLRK 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 496 PELIYLAGLYHDIGKGRGGDHSELGAIDAQAFGTRHHLPDWDTRLIVWLVSNHLVMSTTAQRKDLSDPQVIHDFAQFVGD 575
Cdd:PRK04374 486 PELLLLAGLFHDIAKGRGGDHSELGAVDARAFCLAHRLSEGDTELVTWLVEQHLRMSVTAQKQDISDPEVIHRFATLVGT 565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 576 EVHLDYLYVLTVADINATNPTLWNSWRASLLRQLYTETKRALRRGLENPVDREEQIRRTQTAALDILVRNGTDPDDVEQL 655
Cdd:PRK04374 566 RERLDYLYLLTCADIAGTSPKLWNAWKDRLLADLYFAARRALREGLEHPPPREERLREARESARALMQAQGHDDATIDRQ 645
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 656 WSALGDDYFLRHTAGDVAWHSDAILQQPAdGGPLVLIKETTQRefEGGTQIFIYAPDQHDFFAVTVAAMDQLNLNIHDAR 735
Cdd:PRK04374 646 FAGMPDENFLRFRPEQLAWQAASLIEVEI-GQTLVKARRAVPD--NDALEVFVYSPDRDGLFAAIVATLDRKGYGIHRAR 722
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 736 IITSSSKFTLDTYIVLDNEGGSIGDNpervQEIRNGLTEALRNPDDYPTIIKRRVPRQLKHFAFAPQVTIHNDAQRPVTV 815
Cdd:PRK04374 723 VLDAPHDAIFDVFEVLPQDTYADGDP----QRLAAALRQVLAGDLQKVRPARRAVPRQLRHFRFAPRVEFSESAGGRRTR 798
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488617883 816 LELLAPDRPGLLARIGKIFLEFDLSLQNAKIATLGERVEDVFFITDANNHPLSDPQLcSQLQDAI 880
Cdd:PRK04374 799 ISLVAPDRPGLLADVAHVLRMQHLRVHDARIATFGERAEDQFQITDEHDRPLSESAR-QALRDAL 862
|
|
| PRK05092 |
PRK05092 |
PII uridylyl-transferase; Provisional |
6-871 |
0e+00 |
|
PII uridylyl-transferase; Provisional
Pssm-ID: 235342 [Multi-domain] Cd Length: 931 Bit Score: 597.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 6 PDLFDRGQFQAEL------------ALKASPIAAFKKAIRRAKDVLDDRFRSGRDIRRLIEDRAWFVDNILQKAWDQFEW 73
Cdd:PRK05092 13 SEIFDRAALRAELdalaadaagdpdALRAAVLALLKQALARGRAEARERLEADGSGRACARRLAYLTDELIRALYDFATT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 74 --------SEDADIALLAVGGYGRGE-----------LHPYSDIDLLILLdsddheifrepIERFLTLLWDIGLEVGQSV 134
Cdd:PRK05092 93 hlypadnpSEGERLAVLAVGGYGRGElapgsdidllfLLPYKQTAWAESV-----------VEYMLYMLWDLGLKVGHAT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 135 RSVNECAQEGLADLTVITNLMESRTIAGP----EHLRQRMLE--VTSTqhmwpSKEFFLAKHAEQKKRHHKYNDTEYNLE 208
Cdd:PRK05092 162 RSIDECIRLAREDMTIRTALLEARFLAGDralfEELETRFDKevVKGT-----AAEFVAAKLAERDERHRRAGDSRYLVE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 209 PNVKGSPGGLRDIQTILWVARRQYGTLNLHALAGEGFLLGSENALLASSQEFLWKVRYALHMLAGRSEDRLLFDYQVRIA 288
Cdd:PRK05092 237 PNVKEGKGGLRDLHTLFWIAKYVYRVRDAAELVKLGVFTREEYRLFRRAEDFLWAVRCHLHFLTGRAEERLSFDLQPEIA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 289 GLLGYEDSDAKLAIERFMQKYYRVVMSIAEL-----SDLIIQHFEEVILSDDSGTAQ---PINSRFQLHDGYIEATNPNV 360
Cdd:PRK05092 317 ERMGYTDHPGLSGVERFMKHYFLVAKDVGDLtrifcAALEAQHAKRAPGLNRFARRRrkaLDSDGFVVDNGRINLADPDV 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 361 FKRTPFAMIEIFVL-----MAQHPeikgvraDTIRLLREHRHLINDDFRNDIRNTSLFIELFKCETGIHRNLRRMNRYGI 435
Cdd:PRK05092 397 FERDPVNLIRLFHLadrhgLDIHP-------DAMRLVTRSLRLIDAALREDPEANRLFLDILTSRRNPERVLRRMNEAGV 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 436 LGLYLPEFGHIVGQMQHDLFHIYTVDAHTLNLIKHLRKLQYTEVSEKFPLASKIMARLPKPELIYLAGLYHDIGKGRGGD 515
Cdd:PRK05092 470 LGRFIPDFGRIVAMMQFNMYHHYTVDEHTIRAIGVLAEIERGELADEHPLASELMPKIESRRALYVAVLLHDIAKGRPED 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 516 HSELGAIDAQAFGTRHHLPDWDTRLIVWLVSNHLVMSTTAQRKDLSDPQVIHDFAQFVGDEVHLDYLYVLTVADINATNP 595
Cdd:PRK05092 550 HSIAGARIARRLCPRLGLSPAETETVAWLVEHHLLMSDTAQKRDLSDPKTIEDFADAVQSPERLKLLLILTVADIRAVGP 629
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 596 TLWNSWRASLLRQLYTETKRALRRGLENpVDREEQIRRTQTAALDILvrNGTDPDDVEQLWSALGDDYFLRHTAGDVAWH 675
Cdd:PRK05092 630 GVWNGWKAQLLRTLYYETEEVLTGGFSE-LNRAERVAAAKEALREAL--SDWPKADRDAYLARHYPAYWLAVDLDTQARH 706
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 676 SDAILQQPADGGPLVLikETTQREFEGGTQIFIYAPDQHDFFAVTVAAMDQLNLNIHDARIITSSSKFTLDTYIVLDNEG 755
Cdd:PRK05092 707 ARFIRDADDAGRPLAT--EVRPDPARGVTEVTVLAADHPGLFSRIAGACAAAGANIVDARIFTTTDGRALDTFWIQDAFG 784
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 756 GSIgDNPERVQEIRNGLTEALRNPDDYPTIIKRRVP--RQLKHFAFAPQVTIHNDAQRPVTVLELLAPDRPGLLARIGKI 833
Cdd:PRK05092 785 RDE-DEPRRLARLAKAIEDALSGEVRLPEALAKRTKpkKRARAFHVPPRVTIDNEASNRFTVIEVNGRDRPGLLYDLTRA 863
|
890 900 910
....*....|....*....|....*....|....*...
gi 488617883 834 FLEFDLSLQNAKIATLGERVEDVFFITDANNHPLSDPQ 871
Cdd:PRK05092 864 LSDLNLNIASAHIATYGERAVDVFYVTDLFGLKITNEA 901
|
|
| PRK03381 |
PRK03381 |
PII uridylyl-transferase; Provisional |
75-881 |
3.82e-77 |
|
PII uridylyl-transferase; Provisional
Pssm-ID: 235123 [Multi-domain] Cd Length: 774 Bit Score: 267.24 E-value: 3.82e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 75 EDADIALLAVGGYGRGELHPYSDIDLLILLDSDDHEIFREPIERFLTLLWDIGLEVGQSVRSVNECAQEGLADLTVITNL 154
Cdd:PRK03381 54 DGSGVALVAVGGLGRRELLPYSDLDLVLLHDGRPADDVAEVADRLWYPLWDAGIRLDHSVRTVPEALKVAGSDLKAALGL 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 155 MESRTIAGPEHLRQRMLEVTSTQhmW----PSKEFFLAKHAEQkkRHHKYNDTEYNLEPNVKGSPGGLRDIQTilwvarr 230
Cdd:PRK03381 134 LDARHIAGDADLSALLIGGVRRQ--WrngaRRRLPELVELTRA--RWERSGEIAHLAEPDLKEGRGGLRDVQL------- 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 231 qygtlnLHALAGEGFLLGSENALLASSQEFLwKVRYALHMLAGRSEDRLLFDYQVRIAGLLGYEDSDAkLAierfmqkyy 310
Cdd:PRK03381 203 ------LRALAAAQLADAPGGGLDAAHRRLL-DVRTELHRVSGRGRDRLLAQEADEVAAALGLGDRFD-LA--------- 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 311 RVVMS----IAELSDLIIQHFEEVILSDDSGTAQPINSRFQLHDGYIEATNPNVFKRT---------------------- 364
Cdd:PRK03381 266 RALSDaartISYAVDVGWRTAANALPRRGLSALRRRPVRRPLDEGVVEHAGEVVLARDarpardpglvlrvaaaaattgl 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 365 PFAMIEIFVLMAQHPEI-----KGVRADTIRLLREHRHLInddfrndirntslfielfkcetgihRNLRRMNRYGILGLY 439
Cdd:PRK03381 346 PIAAATLSRLAASAPPLptpwpAEARDDLLVLLGAGPAAV-------------------------AVIEALDRTGLWGRL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 440 LPEFGHIVGQMQHDLFHIYTVDAHtlnlikhlrkLQYTEVSekfplASKIMARLPKPELIYLAGLYHDIGKGRGGDHSEL 519
Cdd:PRK03381 401 LPEWEAVRDLPPRDPVHRWTVDRH----------LVETAVR-----AAALTRRVARPDLLLLGALLHDIGKGRGGDHSVV 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 520 GAIDAQAFGTRHHLPDWDTRLIVWLVSNHLVMSTTAQRKDLSDPQVIHDFAQFVG-DEVHLDYLYVLTVADINATNPTLW 598
Cdd:PRK03381 466 GAELARQIGARLGLSPADVALLSALVRHHLLLPETATRRDLDDPATIEAVAEALGgDPVLLELLHALTEADSLATGPGVW 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 599 NSWRASLLRQLytetkralrrglenpvdreeqIRRTqTAALDilvrnGTDPDDVEQLwsalgddyflrhtagdvawhSDA 678
Cdd:PRK03381 546 SDWKASLVGDL---------------------VRRC-RAVLA-----GEPLPEPEPL--------------------DPA 578
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 679 ILQQPADGGPLVLIKETTQREFEggtqIFIYAPDQHDFFAvTVAAMDQLN-LNIHDARiITSSSKFTLDTYIVldneGGS 757
Cdd:PRK03381 579 QLALAADGGVHVEIAPADPHMVE----VTVVAPDRRGLLS-KAAGVLALHrLRVRSAS-VRSHDGVAVLEFVV----SPR 648
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 758 IGDNPE----RVQEIR--NG---LTEALRNPD-DYPTIIKRRVPRqlkhfafAPQVTIHNDAQRPVTVLELLAPDRPGLL 827
Cdd:PRK03381 649 FGSPPDaallRQDLRRalDGdldVLARLAAREaAAAAVPVRRPAA-------PPRVLWLDGASPDATVLEVRAADRPGLL 721
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....
gi 488617883 828 ARIGKIFLEFDLSLQNAKIATLGERVEDVFFITDANNHPLSDPQlcSQLQDAIV 881
Cdd:PRK03381 722 ARLARALERAGVDVRWARVATLGADVVDVFYVTGAAGGPLADAR--AAVEQAVL 773
|
|
| GlnD_UR_UTase |
pfam08335 |
GlnD PII-uridylyltransferase; This is a family of bifunctional uridylyl-removing enzymes ... |
185-324 |
1.05e-50 |
|
GlnD PII-uridylyltransferase; This is a family of bifunctional uridylyl-removing enzymes/uridylyltransferases (UR/UTases, GlnD) that are responsible for the modification (EC:2.7.7.59) of the regulatory protein P-II, or GlnB (pfam00543). In response to nitrogen limitation, these transferases catalyze the uridylylation of the PII protein, which in turn stimulates deadenylylation of glutamine synthetase (GlnA). Deadenylylated glutamine synthetase is the more active form of the enzyme. Moreover, uridylylated PII can act together with NtrB and NtrC to increase transcription of genes in the sigma54 regulon, which include glnA and other nitrogen-level controlled genes. It has also been suggested that the product of the glnD gene is involved in other physiological functions such as control of iron metabolism in certain species. The region described in this family is found in many of its members to be C-terminal to a nucleotidyltransferase domain (pfam01909), and N-terminal to an HD domain (pfam01966) and two ACT domains (pfam01842).
Pssm-ID: 462432 [Multi-domain] Cd Length: 140 Bit Score: 174.69 E-value: 1.05e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 185 FFLAKHAEQKKRHHKYNDTEYNLEPNVKGSPGGLRDIQTILWVARRQYGTLNLHALAGEGFLLGSENALLASSQEFLWKV 264
Cdd:pfam08335 2 FMKAKIEEQVARHGRYGDTAYNLEPNIKLGPGGLRDIEFIVWIAQLIFTLRALEELVELGLLTREEARELRRAYRFLRRV 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 265 RYALHMLAGRSEDRLLFDYQVRIAGLLGYEDSDaKLAIERFMQKYYRVVMSIAELSDLII 324
Cdd:pfam08335 82 RHRLHLLADRQTDRLPFDLQRRLARALGYARDG-WLAVERFMRRLFRHAHRVSRLFEILL 140
|
|
| ACT_ACR-UUR-like_2 |
cd04899 |
C-terminal ACT domains of the bacterial signal-transducing uridylyltransferase ... |
814-884 |
4.38e-27 |
|
C-terminal ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) enzyme, GlnD and related domains; This ACT domain family, ACT_ACR-UUR-like_2, includes the second of two C-terminal ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) enzyme, GlnD; including those enzymes similar to the GlnD found in enteric Escherichia coli and those found in photosynthetic, nitrogen-fixing bacterium Rhodospirillum rubrum. Also included in this CD are the second and fourth ACT domains of a novel protein composed almost entirely of ACT domain repeats, the ACR protein. These ACR proteins, found in Arabidopsis and Oryza, are proposed to function as novel regulatory or sensor proteins in plants. Members of this CD belong to the superfamily of ACT regulatory domains.
Pssm-ID: 153171 [Multi-domain] Cd Length: 70 Bit Score: 104.84 E-value: 4.38e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488617883 814 TVLELLAPDRPGLLARIGKIFLEFDLSLQNAKIATLGERVEDVFFITDANNHPLsDPQLCSQLQDAIVKQL 884
Cdd:cd04899 1 TVLELTALDRPGLLADVTRVLAELGLNIHSAKIATLGERAEDVFYVTDADGQPL-DPERQEALRAALGEAL 70
|
|
| glnD |
PRK00227 |
[protein-PII] uridylyltransferase; |
80-609 |
4.73e-26 |
|
[protein-PII] uridylyltransferase;
Pssm-ID: 178937 [Multi-domain] Cd Length: 693 Bit Score: 114.86 E-value: 4.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 80 ALLAVGGYGRGELHPYSDIDLLILLDSDDHEifrEPIERFLTLLWDIGLEVGQSVRSVNECAQEGLADLTVITNLMESRT 159
Cdd:PRK00227 29 ALAATGSLARREMTPYSDLDLILLHPPGATP---DGVEDLWYPIWDAKKRLDYSVRTPQECAAMISADSTAALALLDLRF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 160 IAGPEHL----RQRMLEvtstqhMWPS--KEFFLAKHAEQKKRHHKYNDTEYNLEPNVKGSPGGLRDIQTIlwvarrqyg 233
Cdd:PRK00227 106 VAGDEQLtastRAKILE------KWRRelNKNFDAVVDTAIARWRRSGSVVAMTRPDLKHGRGGLRDIELI--------- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 234 tlnlHALAgegflLG--SENALLASSQEFLWKVRYALHMLAGRSEDRLLFDYQVRIAGLLGYEDsdaKLAIERFMQKYYR 311
Cdd:PRK00227 171 ----RALA-----LGhlCDAPPLDSQHQLLLDVRTLLHVHARRARDVLDPEFAVDIALDLGFVD---RYHLSREIADAAR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 312 VVMSIAELSDLIIQHfeevILSDDSG----TAQPINSRFQLHDGYIE-ATNPNVfkRTPFAMIEifVLMAQHPEIKGVRA 386
Cdd:PRK00227 239 AIDDALTAALATARG----ALPRRTAfrnaVRRPLDVDVVDANGTIAlSRTPDL--DDPALPLR--VAAAAARTGLPVSE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 387 DTIRLLREHRHLINddfRNDIRNTSLFIELFKCETGIHRNLRRMNRYGILGLYLPEFGHIVGQMQHDLFHIYTVDAHTLN 466
Cdd:PRK00227 311 SVWKRLEECPELPE---PWPASAAGDFFRLLSSPVNSRRVIKQMDRHGLWERIVPEWDRIRGLMPREPSHIHTIDEHSLN 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 467 LIKHlrklqytevsekfplASKIMARLPKPELIYLAGLYHDIGKGRGGDHSELGAIDAQAFGTRHHLPDWDTRLIVWLVS 546
Cdd:PRK00227 388 TVAN---------------CALETVTVARPDLLLLGALYHDIGKGYPRPHEQVGAEMVARAARRMGLNLRDRAVVQTLVA 452
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488617883 547 NHLVMSTTAQRKDLSDPQVIHDFAQFVG-DEVHLDYLYVLTVADINATNPTLWNSWRASLLRQL 609
Cdd:PRK00227 453 EHTTLARIAGRLDPTSEEAVDKLLDAVRyDLLTLNLLEVLTEADAEGTGPGVWTARLEQGLRIV 516
|
|
| ACT_UUR-like_1 |
cd04900 |
ACT domain family, ACT_UUR-like_1, includes the first of two C-terminal ACT domains of the ... |
703-776 |
1.82e-25 |
|
ACT domain family, ACT_UUR-like_1, includes the first of two C-terminal ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) enzyme, GlnD and related domains; This ACT domain family, ACT_UUR-like_1, includes the first of two C-terminal ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) enzyme, GlnD; including those enzymes similar to the GlnD found in enteric Escherichia coli and those found in photosynthetic, nitrogen-fixing bacterium Rhodospirillum rubrum. Also included in this CD is the N-terminal ACT domain of a yet characterized Arabidopsis/Oryza predicted tyrosine kinase. Members of this CD belong to the superfamily of ACT regulatory domains.
Pssm-ID: 153172 [Multi-domain] Cd Length: 73 Bit Score: 100.24 E-value: 1.82e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488617883 703 GTQIFIYAPDQHDFFAVTVAAMDQLNLNIHDARIITSSSKFTLDTYIVLDNEGGSIGDnPERVQEIRNGLTEAL 776
Cdd:cd04900 1 GTEVFIYTPDRPGLFARIAGALDQLGLNILDARIFTTRDGYALDTFVVLDPDGEPIGE-RERLARIREALEDAL 73
|
|
| ACT_UUR-ACR-like |
cd04873 |
ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) ... |
814-884 |
3.35e-21 |
|
ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) enzyme, GlnD; This ACT domain family, ACT_UUR_ACR-like, includes the two C-terminal ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) enzyme, GlnD; including those enzymes similar to the GlnD found in enteric Escherichia coli and those found in photosynthetic, nitrogen-fixing bacterium Rhodospirillum rubrum. Also included in this CD are the four ACT domains of a novel protein composed almost entirely of ACT domain repeats (the ACR protein) and like proteins. These ACR proteins, found in Arabidopsis and Oryza, are proposed to function as novel regulatory or sensor proteins in plants. This CD also includes the first of the two ACT domains that comprise the Glycine Cleavage System Transcriptional Repressor (GcvR) protein and related domains, as well as, the N-terminal ACT domain of a yet characterized Arabidopsis/Oryza predicted tyrosine kinase. Members of this CD belong to the superfamily of ACT regulatory domains.
Pssm-ID: 153145 [Multi-domain] Cd Length: 70 Bit Score: 87.99 E-value: 3.35e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488617883 814 TVLELLAPDRPGLLARIGKIFLEFDLSLQNAKIATLGERVEDVFFITDANNHPLsDPQLCSQLQDAIVKQL 884
Cdd:cd04873 1 TVVEVYAPDRPGLLADITRVLADLGLNIHDARISTTGERALDVFYVTDSDGRPL-DPERIARLEEALEDAL 70
|
|
| ACT_UUR-ACR-like |
cd04873 |
ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) ... |
704-776 |
6.86e-17 |
|
ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) enzyme, GlnD; This ACT domain family, ACT_UUR_ACR-like, includes the two C-terminal ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) enzyme, GlnD; including those enzymes similar to the GlnD found in enteric Escherichia coli and those found in photosynthetic, nitrogen-fixing bacterium Rhodospirillum rubrum. Also included in this CD are the four ACT domains of a novel protein composed almost entirely of ACT domain repeats (the ACR protein) and like proteins. These ACR proteins, found in Arabidopsis and Oryza, are proposed to function as novel regulatory or sensor proteins in plants. This CD also includes the first of the two ACT domains that comprise the Glycine Cleavage System Transcriptional Repressor (GcvR) protein and related domains, as well as, the N-terminal ACT domain of a yet characterized Arabidopsis/Oryza predicted tyrosine kinase. Members of this CD belong to the superfamily of ACT regulatory domains.
Pssm-ID: 153145 [Multi-domain] Cd Length: 70 Bit Score: 75.66 E-value: 6.86e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488617883 704 TQIFIYAPDQHDFFAVTVAAMDQLNLNIHDARIITSSSKFtLDTYIVLDNEGGSigDNPERVQEIRNGLTEAL 776
Cdd:cd04873 1 TVVEVYAPDRPGLLADITRVLADLGLNIHDARISTTGERA-LDVFYVTDSDGRP--LDPERIARLEEALEDAL 70
|
|
| NT_GlnE_GlnD_like |
cd05401 |
Nucleotidyltransferase (NT) domain of Escherichia coli adenylyltransferase (GlnE), Escherichia ... |
29-172 |
3.17e-16 |
|
Nucleotidyltransferase (NT) domain of Escherichia coli adenylyltransferase (GlnE), Escherichia coli uridylyl transferase (GlnD), and similar proteins; Escherichia coli GlnD and -E participate in the Glutamine synthetase (GS)/Glutamate synthase (GOGAT) pathway for the assimilation of ammonium nitrogen. In nitrogen sufficiency, GlnE adenylates GS, reducing GS activity; when nitrogen is limiting, GlnE deadenylates GS-AMP, restoring GS activity. When nitrogen is limiting, GlnD uridylylates the nitrogen regulatory protein PII to PII-UTP, and in nitrogen sufficiency, it removes the modifying groups. The activity of Escherichia coli GlnE is modulated by PII-proteins. PII-UMP promotes GlnE deadenylation activity, and PII promotes GlnE adenylation activity. Escherichia coli GlnE has two separate NT domains. The N-terminal NT domain catalyzes the deadenylylation of GS, and the C-terminal NT domain the adenylylation reaction. The majority of proteins in this family contain a C-terminal NT domain which is associated with a cystathionine beta-synthase (CBS) domain pair and a CAP_ED (cAMP receptor protein effector ) domain. This family belongs to the Pol beta-like NT superfamily. In the majority of enzymes in this superfamily, two carboxylates, Dx[D/E], together with a third more distal carboxylate, coordinate two divalent metal cations involved in a two-metal ion mechanism of nucleotide addition. For the majority of proteins in this family, these carboxylate residues are conserved.
Pssm-ID: 143391 [Multi-domain] Cd Length: 172 Bit Score: 77.38 E-value: 3.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 29 KKAIRRAKDVLDDRFRSGRDIRRLIEDRAWFVDNILQKAWDQ-----FEWSEDADIALLAVGGYGRGELHPY-------S 96
Cdd:cd05401 1 RAKLRQLRRILRRDLLGGASIRAISRALSDLADALLRRALELalaelGKGPPPVPFALLALGSYGRGELNPSsdqdlllL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 97 DIDLLILLDSDDHEIFREPIERFLTL-----LWDIGLEVGQSVRSVNECAQEGLADLTV------ITNLMESRTIAGPEH 165
Cdd:cd05401 81 YDDDGDEVAAYFEELAERLIKILSEAggpycLGDVMLRPPGWRRSLAEWLDAARDWLTEpgrlweRTALLDARPVAGDRA 160
|
....*..
gi 488617883 166 LRQRMLE 172
Cdd:cd05401 161 LAEELRR 167
|
|
| ACT_ACR_4 |
cd04926 |
C-terminal ACT domain, of a novel type of ACT domain-containing protein which is composed ... |
816-884 |
4.66e-11 |
|
C-terminal ACT domain, of a novel type of ACT domain-containing protein which is composed almost entirely of four ACT domain repeats (the "ACR" protein); This CD includes the C-terminal ACT domain, of a novel type of ACT domain-containing protein which is composed almost entirely of four ACT domain repeats (the "ACR" protein). ACR proteins, found only in Arabidopsis and Oryza, as yet, are proposed to function as novel regulatory or sensor proteins in plants. Nine ACR gene products have been described (ACR1-8 in Arabidopsis and OsARC1-9 in Oryza) and are represented in this CD. Members of this CD belong to the superfamily of ACT regulatory domains.
Pssm-ID: 153198 Cd Length: 72 Bit Score: 59.29 E-value: 4.66e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488617883 816 LELLAPDRPGLLARIGKIFLEFDLSLQNAKIATLGERVEDVFFITDANNHPLsDPQLCsqlqDAIVKQL 884
Cdd:cd04926 4 LELRTEDRVGLLSDVTRVFRENGLTVTRAEISTQGDMAVNVFYVTDANGNPV-DPKTI----EAVRQEI 67
|
|
| ACT_ACR_2 |
cd04925 |
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats ... |
814-878 |
1.38e-06 |
|
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats (the "ACR" protein); This CD includes the second ACT domain, of a novel type of ACT domain-containing protein which is composed almost entirely of four ACT domain repeats (the "ACR" protein). ACR proteins, found only in Arabidopsis and Oryza, as yet, are proposed to function as novel regulatory or sensor proteins in plants. Nine ACR gene products have been described (ACR1-8 in Arabidopsis and OsARC1-9 in Oryza) and are represented in this CD. Members of this CD belong to the superfamily of ACT regulatory domains.
Pssm-ID: 153197 Cd Length: 74 Bit Score: 46.65 E-value: 1.38e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488617883 814 TVLELLAPDRPGLLARIGKIFLEFDLSLQNAKIATLGERVEDVFFITDANNH-PLSDPQLCSQLQD 878
Cdd:cd04925 1 TAIELTGTDRPGLLSEVFAVLADLHCNVVEARAWTHNGRLACVIYVRDEETGaPIDDPIRLASIED 66
|
|
| ACT_UUR-like_1 |
cd04900 |
ACT domain family, ACT_UUR-like_1, includes the first of two C-terminal ACT domains of the ... |
820-884 |
4.11e-06 |
|
ACT domain family, ACT_UUR-like_1, includes the first of two C-terminal ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) enzyme, GlnD and related domains; This ACT domain family, ACT_UUR-like_1, includes the first of two C-terminal ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) enzyme, GlnD; including those enzymes similar to the GlnD found in enteric Escherichia coli and those found in photosynthetic, nitrogen-fixing bacterium Rhodospirillum rubrum. Also included in this CD is the N-terminal ACT domain of a yet characterized Arabidopsis/Oryza predicted tyrosine kinase. Members of this CD belong to the superfamily of ACT regulatory domains.
Pssm-ID: 153172 [Multi-domain] Cd Length: 73 Bit Score: 45.16 E-value: 4.11e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488617883 820 APDRPGLLARIGKIFLEFDLSLQNAKIATLGE-RVEDVFFITDANNHPLSDPQLCSQLQDAIVKQL 884
Cdd:cd04900 8 TPDRPGLFARIAGALDQLGLNILDARIFTTRDgYALDTFVVLDPDGEPIGERERLARIREALEDAL 73
|
|
| HDc |
smart00471 |
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ... |
456-602 |
4.90e-06 |
|
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic nucleotide phosphodiesterases (PDEc). This profile/HMM does not detect HD homologues in bacterial glycine aminoacyl-tRNA synthetases (beta subunit).
Pssm-ID: 214679 [Multi-domain] Cd Length: 124 Bit Score: 46.52 E-value: 4.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 456 HIYTVDAHTLNLIKHLRKLqytevsekfplASKImaRLPKPELIYLAGLYHDIGKGRGGD-----------HSELGAIDA 524
Cdd:smart00471 1 SDYHVFEHSLRVAQLAAAL-----------AEEL--GLLDIELLLLAALLHDIGKPGTPDsflvktsvledHHFIGAEIL 67
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488617883 525 QafgtRHHLPDWDTRLIVWLVSNHlvmsttaqrkdlsdpqviHDFAQFVGDEVHLDYLYVLTVADINATNPTLWNSWR 602
Cdd:smart00471 68 L----EEEEPRILEEILRTAILSH------------------HERPDGLRGEPITLEARIVKVADRLDALRADRRYRR 123
|
|
| RnaY |
COG1418 |
HD superfamily phosphodieaserase, includes HD domain of RNase Y [Translation, ribosomal ... |
451-548 |
1.18e-05 |
|
HD superfamily phosphodieaserase, includes HD domain of RNase Y [Translation, ribosomal structure and biogenesis, General function prediction only];
Pssm-ID: 441028 [Multi-domain] Cd Length: 191 Bit Score: 46.82 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 451 QHDLFHIYtvdahtlnlikhlrklqytEVSEkfpLASKIMARLP-KPELIYLAGLYHDIGK----GRGGDHSELGAIDAQ 525
Cdd:COG1418 17 QHDLQHSL-------------------RVAK---LAGLIAAEEGaDVEVAKRAALLHDIGKakdhEVEGSHAEIGAELAR 74
|
90 100
....*....|....*....|...
gi 488617883 526 AFGTRHHLPDWDTRLIVWLVSNH 548
Cdd:COG1418 75 KYLESLGFPEEEIEAVVHAIEAH 97
|
|
| ACT |
pfam01842 |
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ... |
814-869 |
2.06e-05 |
|
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to a wide range of metabolic enzymes that are regulated by amino acid concentration. Pairs of ACT domains bind specifically to a particular amino acid leading to regulation of the linked enzyme. The ACT domain is found in: D-3-phosphoglycerate dehydrogenase EC:1.1.1.95, which is inhibited by serine. Aspartokinase EC:2.7.2.4, which is regulated by lysine. Acetolactate synthase small regulatory subunit, which is inhibited by valine. Phenylalanine-4-hydroxylase EC:1.14.16.1, which is regulated by phenylalanine. Prephenate dehydrogenase EC:4.2.1.51. formyltetrahydrofolate deformylase EC:3.5.1.10, which is activated by methionine and inhibited by glycine. GTP pyrophosphokinase EC:2.7.6.5
Pssm-ID: 426468 [Multi-domain] Cd Length: 66 Bit Score: 43.06 E-value: 2.06e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 488617883 814 TVLELLAPDRPGLLARIGKIFLEFDLSLQNAKIATLGERVEDVFFITDANNHPLSD 869
Cdd:pfam01842 1 TVLEVLVPDRPGLLARVLGALADRGINITSIEQGTSEDKGGIVFVVIVVDEEDLEE 56
|
|
| ACT |
cd02116 |
ACT domains are commonly involved in specifically binding an amino acid or other small ligand ... |
816-866 |
5.25e-05 |
|
ACT domains are commonly involved in specifically binding an amino acid or other small ligand leading to regulation of the enzyme; Members of this CD belong to the superfamily of ACT regulatory domains. Pairs of ACT domains are commonly involved in specifically binding an amino acid or other small ligand leading to regulation of the enzyme. The ACT domain has been detected in a number of diverse proteins; some of these proteins are involved in amino acid and purine biosynthesis, phenylalanine hydroxylation, regulation of bacterial metabolism and transcription, and many remain to be characterized. ACT domain-containing enzymes involved in amino acid and purine synthesis are in many cases allosteric enzymes with complex regulation enforced by the binding of ligands. The ACT domain is commonly involved in the binding of a small regulatory molecule, such as the amino acids L-Ser and L-Phe in the case of D-3-phosphoglycerate dehydrogenase and the bifunctional chorismate mutase-prephenate dehydratase enzyme (P-protein), respectively. Aspartokinases typically consist of two C-terminal ACT domains in a tandem repeat, but the second ACT domain is inserted within the first, resulting in, what is normally the terminal beta strand of ACT2, formed from a region N-terminal of ACT1. ACT domain repeats have been shown to have nonequivalent ligand-binding sites with complex regulatory patterns such as those seen in the bifunctional enzyme, aspartokinase-homoserine dehydrogenase (ThrA). In other enzymes, such as phenylalanine hydroxylases, the ACT domain appears to function as a flexible small module providing allosteric regulation via transmission of conformational changes, these conformational changes are not necessarily initiated by regulatory ligand binding at the ACT domain itself. ACT domains are present either singularly, N- or C-terminal, or in pairs present C-terminal or between two catalytic domains. Unique to cyanobacteria are four ACT domains C-terminal to an aspartokinase domain. A few proteins are composed almost entirely of ACT domain repeats as seen in the four ACT domain protein, the ACR protein, found in higher plants; and the two ACT domain protein, the glycine cleavage system transcriptional repressor (GcvR) protein, found in some bacteria. Also seen are single ACT domain proteins similar to the Streptococcus pneumoniae ACT domain protein (uncharacterized pdb structure 1ZPV) found in both bacteria and archaea. Purportedly, the ACT domain is an evolutionarily mobile ligand binding regulatory module that has been fused to different enzymes at various times.
Pssm-ID: 153139 [Multi-domain] Cd Length: 60 Bit Score: 41.89 E-value: 5.25e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 488617883 816 LELLAPDRPGLLARIGKIFLEFDLSLQNAKIATLG-ERVEDVFFITDANNHP 866
Cdd:cd02116 1 LTVSGPDRPGLLAKVLSVLAEAGINITSIEQRTSGdGGEADIFIVVDGDGDL 52
|
|
| HD |
pfam01966 |
HD domain; HD domains are metal dependent phosphohydrolases. |
485-563 |
5.30e-05 |
|
HD domain; HD domains are metal dependent phosphohydrolases.
Pssm-ID: 460398 [Multi-domain] Cd Length: 110 Bit Score: 43.38 E-value: 5.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 485 LASKIMARLP--KPELIYLAGLYHDIGKGRGGD----------HSELGAIDAQAFGTRHHLPDwdtrlIVWLVSNHLVMS 552
Cdd:pfam01966 11 LARELAEELGelDRELLLLAALLHDIGKGPFGDekpefeiflgHAVVGAEILRELEKRLGLED-----VLKLILEHHESW 85
|
90
....*....|.
gi 488617883 553 TTAQRKDLSDP 563
Cdd:pfam01966 86 EGAGYPEEISL 96
|
|
| HDc |
cd00077 |
Metal dependent phosphohydrolases with conserved 'HD' motif |
458-610 |
9.23e-05 |
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Metal dependent phosphohydrolases with conserved 'HD' motif
Pssm-ID: 238032 [Multi-domain] Cd Length: 145 Bit Score: 43.48 E-value: 9.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 458 YTVDAHTLNLIKHLRKLqytevsekfplASKIMARLPKPELIYLAGLYHDIGKG------------RGGDHSELGAIDAQ 525
Cdd:cd00077 1 EHRFEHSLRVAQLARRL-----------AEELGLSEEDIELLRLAALLHDIGKPgtpdaiteeeseLEKDHAIVGAEILR 69
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 526 AFGTRHHLpdwdtRLIVWLVSNHLvmSTTAQRKDLSDPQVIhdfaqfVGDEVHLDYLYVLTVAD-INATNPTLWNSWRAS 604
Cdd:cd00077 70 ELLLEEVI-----KLIDELILAVD--ASHHERLDGLGYPDG------LKGEEITLEARIVKLADrLDALRRDSREKRRRI 136
|
....*.
gi 488617883 605 LLRQLY 610
Cdd:cd00077 137 AEEDLE 142
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| ACT_ACR-UUR-like_2 |
cd04899 |
C-terminal ACT domains of the bacterial signal-transducing uridylyltransferase ... |
704-776 |
1.39e-04 |
|
C-terminal ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) enzyme, GlnD and related domains; This ACT domain family, ACT_ACR-UUR-like_2, includes the second of two C-terminal ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) enzyme, GlnD; including those enzymes similar to the GlnD found in enteric Escherichia coli and those found in photosynthetic, nitrogen-fixing bacterium Rhodospirillum rubrum. Also included in this CD are the second and fourth ACT domains of a novel protein composed almost entirely of ACT domain repeats, the ACR protein. These ACR proteins, found in Arabidopsis and Oryza, are proposed to function as novel regulatory or sensor proteins in plants. Members of this CD belong to the superfamily of ACT regulatory domains.
Pssm-ID: 153171 [Multi-domain] Cd Length: 70 Bit Score: 40.90 E-value: 1.39e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488617883 704 TQIFIYAPDQ----HDFFAVTVaamdQLNLNIHDARIITSSSKfTLDTYIVLDNEGGSigDNPERVQEIRNGLTEAL 776
Cdd:cd04899 1 TVLELTALDRpgllADVTRVLA----ELGLNIHSAKIATLGER-AEDVFYVTDADGQP--LDPERQEALRAALGEAL 70
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| ACT_ACR-like_2 |
cd04927 |
Second ACT domain, of a novel type of ACT domain-containing protein which is composed almost ... |
815-880 |
2.61e-04 |
|
Second ACT domain, of a novel type of ACT domain-containing protein which is composed almost entirely of four ACT domain repeats (the "ACR" protein); This CD includes the second ACT domain, of a novel type of ACT domain-containing protein which is composed almost entirely of four ACT domain repeats (the "ACR" protein). ACR proteins, found only in Arabidopsis and Oryza, as yet, are proposed to function as novel regulatory or sensor proteins in plants. Nine ACR gene products (ACR1-8 in Arabidopsis and OsARC1-9 in Oryza) have been described, however, the ACR-like sequences in this CD are distinct from those characterized. This CD includes the Oryza sativa ACR-like protein (Os05g0113000) encoded on chromosome 5 and the Arabidopsis thaliana predicted gene product, At2g39570. Members of this CD belong to the superfamily of ACT regulatory domains.
Pssm-ID: 153199 Cd Length: 76 Bit Score: 40.14 E-value: 2.61e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 815 VLELLAPDRPGLLARIGKIFLEFDLSLQNAKIATLGE-RVEDVFFITDANN--HPLS-DPQLCSQLQDAI 880
Cdd:cd04927 2 LLKLFCSDRKGLLHDVTEVLYELELTIERVKVSTTPDgRVLDLFFITDAREllHTKKrREETYDYLRAVL 71
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| HDIG |
TIGR00277 |
HDIG domain; This domain is found in a few known nucleotidyltransferes and in a large number ... |
487-532 |
3.04e-03 |
|
HDIG domain; This domain is found in a few known nucleotidyltransferes and in a large number of uncharacterized proteins. It contains four widely separated His residues, the second of which is part of an invariant dipeptide His-Asp in a region matched approximately by the motif HDIG. This model may annotate homologous domains in which one or more of the His residues is conserved but misaligned, and some probable false-positive hits.
Pssm-ID: 272994 [Multi-domain] Cd Length: 80 Bit Score: 37.32 E-value: 3.04e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488617883 487 SKIMARL--PKPELIYLAGLYHDIGKGR------GGDHSELGAIDAQAFG---------TRHH 532
Cdd:TIGR00277 16 AEALARElgLDVELARRGALLHDIGKPItregviFESHVVVGAEIARKYGeplevidiiAEHH 78
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| Cas3''_I |
cd09641 |
CRISPR/Cas system-associated protein Cas3''; CRISPR (Clustered Regularly Interspaced Short ... |
458-548 |
3.85e-03 |
|
CRISPR/Cas system-associated protein Cas3''; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; HD-like nuclease, specifically digesting double-stranded oligonucleotides and preferably cleaving at G:C pairs; signature gene for Type I
Pssm-ID: 193608 [Multi-domain] Cd Length: 200 Bit Score: 39.56 E-value: 3.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488617883 458 YTVDAHTLNLIKHLRKLqYTEVSEKFPLASKImarlpKPELIYLAGLYHDIGK--------------------GRGGDHS 517
Cdd:cd09641 7 QPLLEHLLDVAAWDAEL-AEEFARKLGLELGL-----SRELLALAGLLHDLGKatpafqkylrggkealregkRKEVRHS 80
|
90 100 110
....*....|....*....|....*....|.
gi 488617883 518 ELGAIDAQAFGTRHHLPDWDTRLIVWLVSNH 548
Cdd:cd09641 81 LLGALLLYELLKELGLDEELALLLAYAIAGH 111
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