|
Name |
Accession |
Description |
Interval |
E-value |
| glnD |
PRK00275 |
PII uridylyl-transferase; Provisional |
1-895 |
0e+00 |
|
PII uridylyl-transferase; Provisional
Pssm-ID: 234709 [Multi-domain] Cd Length: 895 Bit Score: 1820.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 1 MPQVDPELFDRGQFQAELALKASPIAAFKKVIRQAREVLDQRFRAGRDIRRLIEDRAWFVDNILQQAWDQFNWCNQADIA 80
Cdd:PRK00275 1 MPQVDPELFDRGQFQAELALKASPIAAFKKAIRQAREVLDERFRSGRDIRRLIEDRAWFVDQILQQAWHQFDWSDDADIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 81 LVAVGGYGRGELHPYSDIDLLILLDKADHELFRDSIERFLTLLWDIGLEVGQSVRSVDECAEQARADLTIITNLMESRTV 160
Cdd:PRK00275 81 LVAVGGYGRGELHPYSDIDLLILLDSADHEEFREPIERFLTLLWDIGLEIGQSVRSVDECAEEARADLTVITNLMESRTI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 161 AGPERLRQRMLDVTSTAHMWPSKDFFLAKRAEQKARHHKYNDTEYNLEPNVKGSPGGLRDIQTILWVARRQYGTLNLRAL 240
Cdd:PRK00275 161 AGPESLRQRMLEVTSSEHMWPSKEFFLAKRAEQKARHHKYNDTEYNLEPNVKGSPGGLRDIQTILWVAKRQFGTLNLHAL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 241 AGEGFLVESEHALLASSQEFLWKVRYALHMLAGRAEDRLLFDHQRSIAELLGFTGEDTKQTIENFMQQYYRVVMSIAQLS 320
Cdd:PRK00275 241 VGEGFLTESEYGLLASGQEFLWKVRYALHMLAGRAEDRLLFDHQRSIATLLGYEDSDAKLAVEQFMQKYYRVVMALAELN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 321 DLIIQHFEEVILAPEDEAPPVPLNSRFQLHDGYIEATSDHVFKRTPFAMLEIFLLMAQHPEIKGVRADTIRLLREHRYLI 400
Cdd:PRK00275 321 DLILQHFEEVILAADDSGTIQPLNSRFQLRDGYIEATHPNVFKRTPFALLEIFVLMAQHPEIKGVRADTIRLLREHRHLI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 401 DDDFRNDIRNTSLFIELFKCKIGIHRNLRRMNRYGILGRYLPEFGFIVGQMQHDLFHIYTVDAHTLNLIKHLRKLQYTQT 480
Cdd:PRK00275 401 DDAFRNDIRNTSLFIELFKCPIGIHRNLRRMNRYGILGRYLPEFGHIVGQMQHDLFHIYTVDAHTLNLIKNLRKLRYPEV 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 481 SEKFPLATKLMAKLPKPELIYLAGLYHDIGKGRHGDHSEIGAIDAEAFCIRHHLPQWDTRLIVWLVQNHLVMSTTAQRKD 560
Cdd:PRK00275 481 SEKFPLASKLMGRLPKPELLYIAGLYHDIGKGRGGDHSELGAVDAEAFCQRHQLPAWDTRLVVWLVENHLLMSTTAQRKD 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 561 LSDPQVIHDFAQTVVDETRLDYLYVLTVADINATNPTLWNSWRASLLRQLYTETKRALRRGLENPVDREEQIRQTQSAAL 640
Cdd:PRK00275 561 LSDPQVIHDFALKVGDQTHLDYLYVLTVADINATNPTLWNSWRASLLRQLYTETKRALRRGLENPVDREEQIRQTQSAAL 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 641 DILVRGGNDPDDVEQLWSQLGDDYFLRHTAGDVAWHTDAILQQPVEGGPLVLIKETTQREFEGGTQIFIYAPDQHDFFAV 720
Cdd:PRK00275 641 DILVRKGTDPDDAEQLWSQLGDDYFLRHTAGDIAWHTEAILQHPDDGGPLVLIKETTQREFEGGTQIFIYAPDQHDFFAA 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 721 TVAAMDQLNLNIHDARIITSSSQFTLDTYIVLDNDGDSIGNNPVRIEKIRKGLTEALRNPDDYPNIIQRRVPRQLKHFAF 800
Cdd:PRK00275 721 TVAAMDQLNLNIHDARIITSSSQFTLDTYIVLDDDGEPIGDNPARIEQIREGLTEALRNPDDYPTIIQRRVPRQLKHFAF 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 801 APQVTIHNDAQRPVTVLELSAPDRPGLLARIGMIFLEFDLSLQNAKIATLGERVEDVFFITDANNQPLSDPQLCMRLQEA 880
Cdd:PRK00275 801 PTQVTISNDAQRPVTVLEIIAPDRPGLLARIGRIFLEFDLSLQNAKIATLGERVEDVFFITDADNQPLSDPQLCSRLQDA 880
|
890
....*....|....*
gi 860323935 881 IVEHLTVHQDSTTEP 895
Cdd:PRK00275 881 ICEQLDARNEKDTSP 895
|
|
| GlnD |
COG2844 |
UTP:GlnB (protein PII) uridylyltransferase [Posttranslational modification, protein turnover, ... |
22-890 |
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: 1303.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 22 ASPIAAFKKVIRQAREVLDQRFRAGRDIRRLIEDRAWFVDNILQQAWDQFNWCNQADIALVAVGGYGRGELHPYSDIDLL 101
Cdd:COG2844 1 AAALAALREALAEGRAALRERFRAGADGRELVRARAALVDQLLRALWDLAGLTEPERLALVAVGGYGRGELAPHSDIDLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 102 ILLDKADHELFRDSIERFLTLLWDIGLEVGQSVRSVDECAEQARADLTIITNLMESRTVAGPERLRQRMLDVTSTAHMWP 181
Cdd:COG2844 81 FLLPDKPTPALEEVIEAFLYLLWDLGLEVGHSVRTVDECLREAREDITVRTALLEARLLAGDEALFEELRERFRADVFWD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 182 SKDFFLAKRAEQKARHHKYNDTEYNLEPNVKGSPGGLRDIQTILWVARRQYGTLNLRALAGEGFLVESEHALLASSQEFL 261
Cdd:COG2844 161 SRAFFEAKLAEQRERHAKYGDTRYNLEPNIKEGPGGLRDLQTLLWIAKRHFGVRSLEELVKKGLLTEEEYRELRRAEDFL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 262 WKVRYALHMLAGRAEDRLLFDHQRSIAELLGFTGEDTKQTIENFMQQYYRVVMSIAQLSDLIIQHFEEVILAPEDEAPPV 341
Cdd:COG2844 241 WRVRFALHLLAGRAEDRLLFDLQREVAERLGYQDTEGNRAVERFMQRYYRTAKAVGRLNEILLQRLEEAILKPPGLRRPR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 342 PLNSRFQLHDGYIEATSDHVFKRTPFAMLEIFLLMAQHPEIKGVRADTIRLLREHRYLIDDDFRNDIRNTSLFIELFKCK 421
Cdd:COG2844 321 PINEGFQLRNGRLEVADPDVFERDPVALLRLFLLAAQHPEGLGIHPDTLRLLRRALRLIDDAFRRDPEARRLFLEILRQP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 422 IGIHRNLRRMNRYGILGRYLPEFGFIVGQMQHDLFHIYTVDAHTLNLIKHLRKLQYTQTSEKFPLATKLMAKLPKPELIY 501
Cdd:COG2844 401 RGITRALRRMNEYGVLGRYIPEFGRIVGQMQFDLFHVYTVDEHTLRVVRNLRRFERGELAEEFPLASELIAELPKPELLY 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 502 LAGLYHDIGKGRHGDHSEIGAIDAEAFCIRHHLPQWDTRLIVWLVQNHLVMSTTAQRKDLSDPQVIHDFAQTVVDETRLD 581
Cdd:COG2844 481 LAALFHDIAKGRGGDHSELGAEDARRFCPRHGLSPEDTELVAWLVRHHLLMSHTAQRRDISDPEVIRDFARLVGSEERLD 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 582 YLYVLTVADINATNPTLWNSWRASLLRQLYTETKRALRRGLEnPVDREEQIRQTQSAALDILVRGGNDPDDVEQLWSQLG 661
Cdd:COG2844 561 YLYLLTVADIRATGPKVWNSWKASLLRELYRATLRALRGGLE-PPDREERIEERKEEALALLADQGWDEEEIEALWARLP 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 662 DDYFLRHTAGDVAWHTDAILQQPVEGGPLVLIKETTQRefeGGTQIFIYAPDQHDFFAVTVAAMDQLNLNIHDARIITSS 741
Cdd:COG2844 640 DDYFLRHDPEEIAWHARLLLRADDSGKPLVLIRPDPDR---GGTEVFVYTPDRPGLFARIAGALAALGLNILDARIHTTR 716
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 742 SQFTLDTYIVLDNDGDSIgNNPVRIEKIRKGLTEALRNPDDYPNIIQRRVPRQLKHFAFAPQVTIHNDAQRPVTVLELSA 821
Cdd:COG2844 717 DGYALDTFIVLDPDGEPI-DDPDRLERIEQALEEALSGEVPLPEPLARRLSRRLRHFPVPPRVTFDNDASNRYTVLEVSA 795
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 860323935 822 PDRPGLLARIGMIFLEFDLSLQNAKIATLGERVEDVFFITDANNQPLSDPQLCMRLQEAIVEHLTVHQD 890
Cdd:COG2844 796 LDRPGLLYDIARVLADLGLNIHSAKIATLGERVEDVFYVTDLDGQKLTDPERQEALREALLEALDEEAE 864
|
|
| UTase_glnD |
TIGR01693 |
[Protein-PII] uridylyltransferase; This model describes GlnD, the uridylyltransferase ... |
36-885 |
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: 1064.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 36 REVLDQRFRAGRDIRRLIEDRAWFVDNILQQAWDQFNWCNQADIALVAVGGYGRGELHPYSDIDLLILLDKADHELFRDS 115
Cdd:TIGR01693 1 REELLEEFARGGDGRELREGRSDLTDLLLIRLWDFIGISEHSGIALVAVGGYGRGELAPYSDIDLLFLHDGKPAEEVEPK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 116 IERFLTLLWDIGLEVGQSVRSVDECAEQARADLTIITNLMESRTVAGPERLRQRMLDVTSTAHMWPS-KDFFLAKRAEQK 194
Cdd:TIGR01693 81 IERFLYPLWDLGFEVGHSVRTLEECARIAKADLTVATNLLEARHLAGDEALFFRLKERVRREDWRNTaRSFLAAKVEEQD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 195 ARHHKYNDTEYNLEPNVKGSPGGLRDIQTILWVARRQYGTLNLRALAGEGFLVESEHALLASSQEFLWKVRYALHMLAGR 274
Cdd:TIGR01693 161 ERHARYGDTAYNLEPDIKEGPGGLRDLHTLFWVALYQLGVRRLEDLVKQGFLTDAEYKLLAEARDFLWDVRFALHLTTGR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 275 AEDRLLFDHQRSIAELLGFTGEDtKQTIENFMQQYYRVVMSIAQLSDLIIQHFEEVILAPEDEA-----PPVPLNSRFQL 349
Cdd:TIGR01693 241 ADDRLLFDHQDEIAAALGYGDEG-NPAVERFMRRYFQAARRIGYLTEAFLRHYEEALLSRGPSArvrrpKRRPLDEGFVE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 350 HDGYIEATSDHVFKRTPFAMLEIFLLMAQHPEikGVRADTIRLLREHRYLIDDDFRNDIRNTSLFIELFKCKIGIHRNLR 429
Cdd:TIGR01693 320 DGGELVLARTAVFERDPALLLRLFAIAAQRGL--PIHPAALRQLTASLPLLPTPLREDPEARELFLELLTSGNGTVRALR 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 430 RMNRYGILGRYLPEFGFIVGQMQHDLFHIYTVDAHTLNLIKHLRKLQYTQTSEKFPLATKLMAKLPKPELIYLAGLYHDI 509
Cdd:TIGR01693 398 AMNRAGVLGRFLPEWGRIVGQMQFDLFHVYTVDEHTLRTVVHLAPFARGRLAREHPLASELMPKIEDPELLYLAALLHDI 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 510 GKGRHGDHSEIGAIDAEAFCIRHHLPQWDTRLIVWLVQNHLVMSTTAQRKDLSDPQVIHDFAQTVVDETRLDYLYVLTVA 589
Cdd:TIGR01693 478 GKGRGGDHSVLGAEDARDVCPRLGLDRPDTELVAWLVRNHLLMSITAQRRDLNDPKTVFAFAEAVGDPERLEYLLALTVA 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 590 DINATNPTLWNSWRASLLRQLYTETKRALRRGLENPVDREEQIRQTQSAALDILVRgGNDPDDVEQLWSQLGDDYFLRHT 669
Cdd:TIGR01693 558 DIRATGPGVWNSWKASLLRDLYNRTEQVLRGGLEPPADPAEPIAEQRKLAVALLRT-DYTSNEAEVLWLRAYDDYFLRFT 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 670 AGDVAWHTDAILQQPVEGGPLVLIKETTQRefeGGTQIFIYAPDQHDFFAVTVAAMDQLNLNIHDARIITSSSQFTLDTY 749
Cdd:TIGR01693 637 HKEIAWHAESLRRALSSGGPLALIDGTRPS---GGTEVFIYAPDQPGLFAKVAGALAMLSLSVHDAQVNTTKDGVALDTF 713
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 750 IVLDNDGDSIGNNPVRIEkIRKGLTEALRNP-DDYPNIIQRR-VPRQLKHFAFAPQVTIHNDAQRPVTVLELSAPDRPGL 827
Cdd:TIGR01693 714 VVQDLFGSPPAAERVFQE-LLQGLVDVLAGLaKDPDTISARRaRRRRLQHFAVPPRVTILNTASRKATIMEVRALDRPGL 792
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*...
gi 860323935 828 LARIGMIFLEFDLSLQNAKIATLGERVEDVFFITDANNQPLSDpQLCMRLQEAIVEHL 885
Cdd:TIGR01693 793 LARVGRTLEELGLSIQSAKITTFGEKAEDVFYVTDLFGLKLTD-EEEQRLLEVLAASV 849
|
|
| PRK05007 |
PRK05007 |
bifunctional uridylyltransferase/uridylyl-removing protein GlnD; |
1-886 |
0e+00 |
|
bifunctional uridylyltransferase/uridylyl-removing protein GlnD;
Pssm-ID: 235329 [Multi-domain] Cd Length: 884 Bit Score: 956.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 1 MPQVDPELFDRGQFQAELAlkaspiaafKKVIRQAREVLDQRFRAGRDIRRLIEDRAWFVDNILQQAWDQFNWCNQADIA 80
Cdd:PRK05007 12 GQPQSPLTWPDDELTVGGL---------KQHLDTFQQWLGDAFDAGISAEQLVEARTEFIDQLLQRLWIEAGFDQIPDLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 81 LVAVGGYGRGELHPYSDIDLLILLDKADHELFRDSIERFLTLLWDIGLEVGQSVRSVDECAEQARADLTIITNLMESRTV 160
Cdd:PRK05007 83 LVAVGGYGRGELHPLSDIDLLILSRKKLPDEQAQKVGELITLLWDLKLEVGHSVRTLEECLLEGLSDLTVATNLIESRLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 161 AGPERLRQRMLDVTSTAHMWPSKDFFLAKRAEQKARHHKYNDTEYNLEPNVKGSPGGLRDIQTILWVARRQYGTLNLRAL 240
Cdd:PRK05007 163 CGDVALFLELQKHIFSDGFWPSEKFYAAKVEEQNERHQRYHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSLDEM 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 241 AGEGFLVESEHALLASSQEFLWKVRYALHMLAGRAEDRLLFDHQRSIAELLGFTGEdTKQTIENFMQQYYRVVMSIAQLS 320
Cdd:PRK05007 243 VGFGFLTPAERAELNECQHFLWRIRFALHLVLSRYDNRLLFDRQLSVAQLLGYEGE-GNEPVERMMKDYYRTTRRVSELN 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 321 DLIIQHFEEVILAPEDEAPPVPLNSRFQLHDGYIEATSDHVFKRTPFAMLEIFLLMAQHPEIKGVRADTIRLLREHRYLI 400
Cdd:PRK05007 322 QMLLQLFDEAILALTADEKPRPIDDEFQLRGTLIDLRDETLFQRQPEAILRMFYLMARNSNITGIYSTTLRQLRHARRHL 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 401 DDDFRNDIRNTSLFIELFKCKIGIHRNLRRMNRYGILGRYLPEFGFIVGQMQHDLFHIYTVDAHTLNLIKHLRKLQYTQT 480
Cdd:PRK05007 402 NQPLCEIPEARKLFMEILRHPGAVSRALLPMHRHSVLSAYMPQWSHIVGQMQFDLFHAYTVDEHTIRVLLKLESFADEET 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 481 SEKFPLATKLMAKLPKPELIYLAGLYHDIGKGRHGDHSEIGAIDAEAFCIRHHLPQWDTRLIVWLVQNHLVMSTTAQRKD 560
Cdd:PRK05007 482 RQRHPLCVELYPRLPKKELLLLAALFHDIAKGRGGDHSILGAQDALEFAELHGLNSRETQLVAWLVRNHLLMSVTAQRRD 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 561 LSDPQVIHDFAQTVVDETRLDYLYVLTVADINATNPTLWNSWRASLLRQLYTETKRALRRGLENPVDREEQIRQTQSAAL 640
Cdd:PRK05007 562 IQDPDVIKQFAEEVQDENRLRYLVCLTVADICATNETLWNSWKQSLLRELYFATEKQLRRGMENPPDMRERVRHHQLQAL 641
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 641 DILVRGGNDPDDVEQLWSQLGDDYFLRHTAGDVAWHTDAILQQPVEgGPLVLIKETTQRefeGGTQIFIYAPDQHDFFAV 720
Cdd:PRK05007 642 ALLRMDNIDEEALHQIWSRCRADYFLRHTPNQLAWHARHLLQHDLD-KPLVLLSKQATR---GGTEIFIWSPDRPYLFAA 717
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 721 TVAAMDQLNLNIHDARIITSSSQFTLDTYIVLDNDGDSIgnNPVRIEKIRKGLTEALrNPDDYPNIIQRRVPRQLKHFAF 800
Cdd:PRK05007 718 VCAELDRRNLSVHDAQIFTSRDGMAMDTFIVLEPDGSPL--SQDRHQVIRKALEQAL-TQSSPQPPKPRRLPAKLRHFNV 794
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 801 APQVTI---HNDAQrpvTVLELSAPDRPGLLARIGMIFLEFDLSLQNAKIATLGERVEDVFFITDANNQPLSDPQLcMRL 877
Cdd:PRK05007 795 PTEVSFlptHTDRR---SYMELIALDQPGLLARVGKIFADLGISLHGARITTIGERVEDLFILATADRRALNEELQ-QEL 870
|
....*....
gi 860323935 878 QEAIVEHLT 886
Cdd:PRK05007 871 RQRLTEALN 879
|
|
| PRK03059 |
PRK03059 |
PII uridylyl-transferase; Provisional |
18-887 |
0e+00 |
|
PII uridylyl-transferase; Provisional
Pssm-ID: 235101 [Multi-domain] Cd Length: 856 Bit Score: 898.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 18 LALKASPIAAFKKVIRQAREVLDQRFRAGRDIRRLIEDRAWFVDNILQQAWDQFNWcnQADIALVAVGGYGRGELHPYSD 97
Cdd:PRK03059 3 TAAPPPPAASLRAELKAAKAALLARFRQAPNVTALLHALSRLVDQALRRLWQECGL--PAGAALVAVGGYGRGELFPYSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 98 IDLLILL-DKADHELfRDSIERFLTLLWDIGLEVGQSVRSVDECAEQARADLTIITNLMESRTVAGPERLRQRMLDVTsT 176
Cdd:PRK03059 81 VDLLVLLpDAPDAAL-DARIERFIGLCWDLGLEIGSSVRTVDECIEEAAQDVTVQTSLLEARLLTGSAALFERFQRRY-R 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 177 AHMWPsKDFFLAKRAEQKARHHKYNDTEYNLEPNVKGSPGGLRDIQTILWVARR-QYGTlNLRALAGEGFLVESEHALLA 255
Cdd:PRK03059 159 AALDP-RAFFQAKLLEMRQRHAKFQDTPYSLEPNCKESPGGLRDLQTILWIARAaGLGS-SWRELAKRGLITDREARQLR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 256 SSQEFLWKVRYALHMLAGRAEDRLLFDHQRSIAELLGFTGEDTKQTIENFMQQYYRVVMSIAQLSDLIIQHFEEvILAPE 335
Cdd:PRK03059 237 RNERFLKTLRARLHLLAGRREDRLVFDLQTALAESFGYRPTAAKRASEQLMRRYYWAAKAVTQLNTILLQNIEA-RLFPS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 336 DEAPPVPLNSRFQLHDGYIEATSDHVFKRTPFAMLEIFLLMAQHPEIKGVRADTIRLLREHRYLIDDDFRNDIRNTSLFI 415
Cdd:PRK03059 316 TSGITRVINERFVEKQGMLEIASDDLFERHPHAILEAFLLYQQTPGLKGLSARTLRALYNARDVMNAAFRRDPVNRALFM 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 416 ELFKCKIGIHRNLRRMNRYGILGRYLPEFGFIVGQMQHDLFHIYTVDAHTLNLIKHLRKLQYTQTSEKFPLATKLMAKLP 495
Cdd:PRK03059 396 QILQQPRGITHALRLMNQTSVLGRYLPNFRRIVGQMQHDLFHVYTVDQHILMVLRNLRRFAMAEHAHEYPFCSQLIANFD 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 496 KPELIYLAGLYHDIGKGRHGDHSEIGAIDAEAFCIRHHLPQWDTRLIVWLVQNHLVMSTTAQRKDLSDPQVIHDFAQTVV 575
Cdd:PRK03059 476 RPWLLYVAALFHDIAKGRGGDHSTLGAVDARRFCRQHGLAREDAELVVWLVEHHLTMSQVAQKQDLSDPEVIARFAELVG 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 576 DETRLDYLYVLTVADINATNPTLWNSWRASLLRQLYTETKRALRRGlenPVDREEQIRQTQSAALDILVRGGNDPDDVEQ 655
Cdd:PRK03059 556 DERRLTALYLLTVADIRGTSPKVWNAWKGKLLEDLYRATLRVLGGA---APDAHSELEARKEEALALLRLEALPDDAHEA 632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 656 LWSQLGDDYFLRHTAGDVAWHTDAILQQPVEGGPLVlikETTQREFEGGTQIFIYAPDQHDFFAVTVAAMDQLNLNIHDA 735
Cdd:PRK03059 633 LWDQLDVGYFLRHDAADIAWHTRHLYRHVDTDTPIV---RARLSPAGEGLQVMVYTPDQPDLFARICGYFDRAGFSILDA 709
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 736 RIITSSSQFTLDTYIVLDNDGDsiGNNPVRIEKIRKGLTEALRNPDDYPNIIQRRVPRQLKHFAFAPQVTIHNDAQRPVT 815
Cdd:PRK03059 710 RVHTTRHGYALDTFQVLDPEED--VHYRDIINLVEHELAERLAEQAPLPEPSKGRLSRQVKHFPITPRVDLRPDERGQYY 787
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 860323935 816 VLELSAPDRPGLLARIGMIFLEFDLSLQNAKIATLGERVEDVFFITDANnqpLSDPQLCMRLQEAIVEHLTV 887
Cdd:PRK03059 788 ILSVSANDRPGLLYAIARVLAEHRVSVHTAKINTLGERVEDTFLIDGSG---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: 730.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 48 DIRRLIEDRAWFVDNILQQAWDQFNWCNQADIALVAVGGYGRGELHPYSDIDLLILLD-KADHELfRDSIERFLTLLWDI 126
Cdd:PRK01759 26 DVFELIENRSDFYDQLLIHLWQQFGLEEQSDLALIAVGGYGRREMFPLSDLDILILTEqPPDEET-EEKINQFFQFLWDC 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 127 GLEVGQSVRSVDECAEQARADLTIITNLMESRTVAGPERLRQRMLDVTSTAHMWPSKDFFLAKRAEQKARHHKYNDTEYN 206
Cdd:PRK01759 105 GFEVGASVRTLAECESEGRADITIATNLLESRFLTGNEKLFDALVELLQQADFWSKEAFFQAKIQEKIERYQRYHNTSYN 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 207 LEPNVKGSPGGLRDIQTILWVARRQYGTLNLRALAGEGFLVESEHALLASSQEFLWKVRYALHMLAGRAEDRLLFDHQRS 286
Cdd:PRK01759 185 LEPDIKYSPGGLRDLHLLYWIALRHSGAKSLEEILQSGFIYPEEYAELQQSQQFLFKVRFALHLILKRYDNRLLFDRQLK 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 287 IAELLGFTGEDTkQTIENFMQQYYRVVMSIAQLSDLIIQHFEEVILAPEDEAPPVPLNSRFQLHDGYIEATSDHVFKRTP 366
Cdd:PRK01759 265 VSELLGFQGEGN-QGVEKMMKSFFQALQSISLLSDLLVKHYREHFLQPNQNVEIQPLDDDFYLINNAICLRNPDCFEQQP 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 367 FAMLEIFLLMAQHPEIKgVRADTIRLLRehrylidddFRNDIRNTSL---------FIELFKCKIGIHRNLRRMNRYGIL 437
Cdd:PRK01759 344 ESILDLFFYLTQYPQAE-IHSTTLRQLR---------LALEQLQQPLcelpaarerFLRLFNQPNAIKRALVPMHQYGVL 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 438 GRYLPEFGFIVGQMQHDLFHIYTVDAHTLNLIKHLRKLQYTQTSEKFPLATKLMAKLPKPELIYLAGLYHDIGKGRHGDH 517
Cdd:PRK01759 414 TAYLPQWKGIVGLMQFDLFHIYTVDEHTLRVMLKLESFLDEESAEQHPICHQIFSQLSDRTLLYIAALFHDIAKGRGGDH 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 518 SEIGAIDAEAFCIRHHLPQWDTRLIVWLVQNHLVMSTTAQRKDLSDPQVIHDFAQTVVDETRLDYLYVLTVADINATNPT 597
Cdd:PRK01759 494 AELGAVDMRQFAQQHGFDQREIETMAWLVQQHLLMSVTAQRRDIHDPEVVMNFAEEVQNQVRLDYLTCLTVADICATNET 573
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 598 LWNSWRASLLRQLYTETKRALRRGLENPVDREEQIRQTQSAALDILVRGGNDPDD--VEQLWSQLGDDYFLRHTAGDVAW 675
Cdd:PRK01759 574 LWNSWKRSLFATLYQFTNQQFQQGMDELLDYQEKAEENRQQALELLQQKYSALSEtqIEQLWQRCPEDYFLRNTPKQIAW 653
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 676 HTDAILQQPVEggPLVLIketTQREFEGGTQIFIYAPDQHDFFAVTVAAMDQLNLNIHDARIITSSSQFTLDTYIVLDND 755
Cdd:PRK01759 654 HALLLLDFRGD--LLVKI---SNRFSRGGTEIFIYCQDQANLFLKVVSTIGAKKLSIHDAQIITSQDGYVLDSFIVTELN 728
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 756 GDSIGNNpvRIEKIRKGLTEALRNpdDYPNIIQRRVPRQLKHFAFAPQVTIHNDAQRPVTVLELSAPDRPGLLARIGMIF 835
Cdd:PRK01759 729 GKLLEFD--RRRQLEQALTKALNT--NKLKKLNLEENHKLQHFHVKTEVRFLNEEKQEQTEMELFALDRAGLLAQVSQVF 804
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|
gi 860323935 836 LEFDLSLQNAKIATLGERVEDVFFITDANNQPLSDPQLcMRLQEAIVEHL 885
Cdd:PRK01759 805 SELNLNLLNAKITTIGEKAEDFFILTNQQGQALDEEER-KALKSRLLSNL 853
|
|
| PRK04374 |
PRK04374 |
[protein-PII] uridylyltransferase; |
16-871 |
0e+00 |
|
[protein-PII] uridylyltransferase;
Pssm-ID: 179839 [Multi-domain] Cd Length: 869 Bit Score: 642.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 16 AELALKASPIAAFKKVIRQAREVLDQRFRAGRDIRRLIEDRAWFVDNILQQAWDQfnwCNQAD--IALVAVGGYGRGELH 93
Cdd:PRK04374 11 PGVAGDADWAAAARPLLVHADMRLCKRFDQGEPIERLLALRARAVDQLMRNAWTR---CIPADsgLSLHAVGGYGRGELF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 94 PYSDIDLLILLDKADHELFRDSIERFLTLLWDIGLEVGQSVRSVDECAEQArADLTIITNLMESRTVAGPERLRQRMLDV 173
Cdd:PRK04374 88 PRSDVDLLVLGETAAQQRHEQALARLFALLWDVGLPISHAVRSPAQCTAAA-ADQTVLTALIESRPLVADAAARAALAAA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 174 TSTAHMWPSKDFFLAKRAEQKARHHKYNDTEYNLEPNVKGSPGGLRDIQTILWVARRQYGTLNLRALAGEGFLVESEHAL 253
Cdd:PRK04374 167 IAPQQVWPPRAFFQAKREELLARHQRFGDTADNLEPDIKDGPGGLRDLQTLGWMALRAFGVKDLEALVGLGHVGCDEAAA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 254 LASSQEFLWKVRYALHMLAGRAEDRLLFDHQRSIAELLGFTGEDTKQTIENFMQQYYRVVMSIAQLSDLIIQHFEEVIla 333
Cdd:PRK04374 247 LRREREELARLRFGLHLVANRPEERLRFDYQKTLAERLGFADDPESLGVEKMMQRFYRSAALIRRISDRLLQRFEEQF-- 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 334 pEDEAPPVPLNSRFQLHDGYIEATSDHVFKRTPFAMLEIFLLMAQHPEIKGVRADTIRLLREHRYLIDDDFRNDIRNTSL 413
Cdd:PRK04374 325 -DGEATPEPLGGGFSLRRGYLAADADSWPDGDVLQVFALFAQWAAHREVRGLHSLTARALAEVLRDLPAYDVADATARER 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 414 FIELFKCKIGIhRNLRRMNRYGILGRYLPEFGFIVGQMQHDLFHIYTVDAHTLNLIKHLRKLQYTQTSEKFPLATKLMAK 493
Cdd:PRK04374 404 FMALLRGPRAV-ETLNRMARLGVLGQWIPAFASVSGRMQFDLFHVYTVDQHTLMVLRNIALFAAGRADERFSIAHEVWPR 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 494 LPKPELIYLAGLYHDIGKGRHGDHSEIGAIDAEAFCIRHHLPQWDTRLIVWLVQNHLVMSTTAQRKDLSDPQVIHDFAQT 573
Cdd:PRK04374 483 LRKPELLLLAGLFHDIAKGRGGDHSELGAVDARAFCLAHRLSEGDTELVTWLVEQHLRMSVTAQKQDISDPEVIHRFATL 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 574 VVDETRLDYLYVLTVADINATNPTLWNSWRASLLRQLYTETKRALRRGLENPVDREEQIRQTQSAALDILVRGGNDPDDV 653
Cdd:PRK04374 563 VGTRERLDYLYLLTCADIAGTSPKLWNAWKDRLLADLYFAARRALREGLEHPPPREERLREARESARALMQAQGHDDATI 642
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 654 EQLWSQLGDDYFLRHTAGDVAWHTDAILqqPVE-GGPLVLIKETTQRefEGGTQIFIYAPDQHDFFAVTVAAMDQLNLNI 732
Cdd:PRK04374 643 DRQFAGMPDENFLRFRPEQLAWQAASLI--EVEiGQTLVKARRAVPD--NDALEVFVYSPDRDGLFAAIVATLDRKGYGI 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 733 HDARIITSSSQFTLDTYIVLDNDGdSIGNNPVRIEkirKGLTEALRNPDDYPNIIQRRVPRQLKHFAFAPQVTIHNDAQR 812
Cdd:PRK04374 719 HRARVLDAPHDAIFDVFEVLPQDT-YADGDPQRLA---AALRQVLAGDLQKVRPARRAVPRQLRHFRFAPRVEFSESAGG 794
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*....
gi 860323935 813 PVTVLELSAPDRPGLLARIGMIFLEFDLSLQNAKIATLGERVEDVFFITDANNQPLSDP 871
Cdd:PRK04374 795 RRTRISLVAPDRPGLLADVAHVLRMQHLRVHDARIATFGERAEDQFQITDEHDRPLSES 853
|
|
| PRK05092 |
PRK05092 |
PII uridylyl-transferase; Provisional |
6-885 |
0e+00 |
|
PII uridylyl-transferase; Provisional
Pssm-ID: 235342 [Multi-domain] Cd Length: 931 Bit Score: 637.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 6 PELFDRGQFQAEL------------ALKASPIAAFKKVIRQAREVLDQRFRAGRDIRRLIEDRAWFVDNILQQAWDQ--- 70
Cdd:PRK05092 13 SEIFDRAALRAELdalaadaagdpdALRAAVLALLKQALARGRAEARERLEADGSGRACARRLAYLTDELIRALYDFatt 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 71 --FNWCNQAD---IALVAVGGYGRGELHPYSDIDLLILLDK---ADHElfrDSIERFLTLLWDIGLEVGQSVRSVDECAE 142
Cdd:PRK05092 93 hlYPADNPSEgerLAVLAVGGYGRGELAPGSDIDLLFLLPYkqtAWAE---SVVEYMLYMLWDLGLKVGHATRSIDECIR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 143 QARADLTIITNLMESRTVAGPERL----RQRMLD--VTSTAHmwpskDFFLAKRAEQKARHHKYNDTEYNLEPNVKGSPG 216
Cdd:PRK05092 170 LAREDMTIRTALLEARFLAGDRALfeelETRFDKevVKGTAA-----EFVAAKLAERDERHRRAGDSRYLVEPNVKEGKG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 217 GLRDIQTILWVARRQYGTLNLRALAGEGFLVESEHALLASSQEFLWKVRYALHMLAGRAEDRLLFDHQRSIAELLGFTGE 296
Cdd:PRK05092 245 GLRDLHTLFWIAKYVYRVRDAAELVKLGVFTREEYRLFRRAEDFLWAVRCHLHFLTGRAEERLSFDLQPEIAERMGYTDH 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 297 DTKQTIENFMQQYYRVVMSIAQL-----SDLIIQHF--EEVILAPEDEAPPVPLNSRFQLHDGYIEATSDHVFKRTPFAM 369
Cdd:PRK05092 325 PGLSGVERFMKHYFLVAKDVGDLtrifcAALEAQHAkrAPGLNRFARRRRKALDSDGFVVDNGRINLADPDVFERDPVNL 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 370 LEIFLL-----MAQHPeikgvraDTIRLLREHRYLIDDDFRNDIRNTSLFIELFKCKIGIHRNLRRMNRYGILGRYLPEF 444
Cdd:PRK05092 405 IRLFHLadrhgLDIHP-------DAMRLVTRSLRLIDAALREDPEANRLFLDILTSRRNPERVLRRMNEAGVLGRFIPDF 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 445 GFIVGQMQHDLFHIYTVDAHTLNLIKHLRKLQYTQTSEKFPLATKLMAKLPKPELIYLAGLYHDIGKGRHGDHSEIGAID 524
Cdd:PRK05092 478 GRIVAMMQFNMYHHYTVDEHTIRAIGVLAEIERGELADEHPLASELMPKIESRRALYVAVLLHDIAKGRPEDHSIAGARI 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 525 AEAFCIRHHLPQWDTRLIVWLVQNHLVMSTTAQRKDLSDPQVIHDFAQTVVDETRLDYLYVLTVADINATNPTLWNSWRA 604
Cdd:PRK05092 558 ARRLCPRLGLSPAETETVAWLVEHHLLMSDTAQKRDLSDPKTIEDFADAVQSPERLKLLLILTVADIRAVGPGVWNGWKA 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 605 SLLRQLYTETKRALRRGLENpVDREEQIRQTQSAALDILvrGGNDPDDVEQLWSQLGDDYFLRHTAGDVAWHTDAILQQP 684
Cdd:PRK05092 638 QLLRTLYYETEEVLTGGFSE-LNRAERVAAAKEALREAL--SDWPKADRDAYLARHYPAYWLAVDLDTQARHARFIRDAD 714
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 685 VEGGPLVLikETTQREFEGGTQIFIYAPDQHDFFAVTVAAMDQLNLNIHDARIITSSSQFTLDTYIVLDNDGDSIGnNPV 764
Cdd:PRK05092 715 DAGRPLAT--EVRPDPARGVTEVTVLAADHPGLFSRIAGACAAAGANIVDARIFTTTDGRALDTFWIQDAFGRDED-EPR 791
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 765 RIEKIRKGLTEALRNPDDYPNIIQRRVP--RQLKHFAFAPQVTIHNDAQRPVTVLELSAPDRPGLLARIGMIFLEFDLSL 842
Cdd:PRK05092 792 RLARLAKAIEDALSGEVRLPEALAKRTKpkKRARAFHVPPRVTIDNEASNRFTVIEVNGRDRPGLLYDLTRALSDLNLNI 871
|
890 900 910 920
....*....|....*....|....*....|....*....|...
gi 860323935 843 QNAKIATLGERVEDVFFITDANNQPLSDPqlcmRLQEAIVEHL 885
Cdd:PRK05092 872 ASAHIATYGERAVDVFYVTDLFGLKITNE----ARQAAIRRAL 910
|
|
| PRK03381 |
PRK03381 |
PII uridylyl-transferase; Provisional |
79-872 |
9.11e-84 |
|
PII uridylyl-transferase; Provisional
Pssm-ID: 235123 [Multi-domain] Cd Length: 774 Bit Score: 285.73 E-value: 9.11e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 79 IALVAVGGYGRGELHPYSDIDLLILLDKADHELFRDSIERFLTLLWDIGLEVGQSVRSVDECAEQARADLTIITNLMESR 158
Cdd:PRK03381 58 VALVAVGGLGRRELLPYSDLDLVLLHDGRPADDVAEVADRLWYPLWDAGIRLDHSVRTVPEALKVAGSDLKAALGLLDAR 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 159 TVAGPE----RLRQRMLDvtstahMWPS--KDFFLAKRAEQKARHHKYNDTEYNLEPNVKGSPGGLRDIQTilwvarrqy 232
Cdd:PRK03381 138 HIAGDAdlsaLLIGGVRR------QWRNgaRRRLPELVELTRARWERSGEIAHLAEPDLKEGRGGLRDVQL--------- 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 233 gtlnLRALAGEGfLVESEHALLASSQEFLWKVRYALHMLAGRAEDRLLFDHQRSIAELLGFTGEDTkqtienFMQQYYRV 312
Cdd:PRK03381 203 ----LRALAAAQ-LADAPGGGLDAAHRRLLDVRTELHRVSGRGRDRLLAQEADEVAAALGLGDRFD------LARALSDA 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 313 VMSIAQLSDLIIQHFEEVI----LAPEDEAPP-VPLNSRFQLHDGYIEATSDHVFKRTPFAMLEIFLLMAQ--HPeikgV 385
Cdd:PRK03381 272 ARTISYAVDVGWRTAANALprrgLSALRRRPVrRPLDEGVVEHAGEVVLARDARPARDPGLVLRVAAAAATtgLP----I 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 386 RADTI-RLLREHRYLID---DDFRNDirntslFIELFKCKIGIHRNLRRMNRYGILGRYLPEFGFIVGQMQHDLFHIYTV 461
Cdd:PRK03381 348 AAATLsRLAASAPPLPTpwpAEARDD------LLVLLGAGPAAVAVIEALDRTGLWGRLLPEWEAVRDLPPRDPVHRWTV 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 462 DAHtlnLIkhlrklqytQTSEKfplATKLMAKLPKPELIYLAGLYHDIGKGRHGDHSEIGAIDAEAFCIRHHLPQWDTRL 541
Cdd:PRK03381 422 DRH---LV---------ETAVR---AAALTRRVARPDLLLLGALLHDIGKGRGGDHSVVGAELARQIGARLGLSPADVAL 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 542 IVWLVQNHLVMSTTAQRKDLSDPQVIHDFAQTVVDETR-LDYLYVLTVADINATNPTLWNSWRASLLRQLYTETkRALRR 620
Cdd:PRK03381 487 LSALVRHHLLLPETATRRDLDDPATIEAVAEALGGDPVlLELLHALTEADSLATGPGVWSDWKASLVGDLVRRC-RAVLA 565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 621 GLENPvdreeqirqtqsaaldilvrggnDPDDVeqlwsqlgddyflrhtagdvawhTDAILQQPVEGGPLVLIKETTQRE 700
Cdd:PRK03381 566 GEPLP-----------------------EPEPL-----------------------DPAQLALAADGGVHVEIAPADPHM 599
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 701 FEggtqIFIYAPDQHDFFAvTVAAMDQLN-LNIHDARiITSSSQFTLDTYIVLDNDGDsignnPVRIEKIRKGLTEALRN 779
Cdd:PRK03381 600 VE----VTVVAPDRRGLLS-KAAGVLALHrLRVRSAS-VRSHDGVAVLEFVVSPRFGS-----PPDAALLRQDLRRALDG 668
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 780 PDDYPNIIQRR----VPRQLKHFAFAPQVTIHNDAQRPVTVLELSAPDRPGLLARIGMIFLEFDLSLQNAKIATLGERVE 855
Cdd:PRK03381 669 DLDVLARLAAReaaaAAVPVRRPAAPPRVLWLDGASPDATVLEVRAADRPGLLARLARALERAGVDVRWARVATLGADVV 748
|
810
....*....|....*..
gi 860323935 856 DVFFITDANNQPLSDPQ 872
Cdd:PRK03381 749 DVFYVTGAAGGPLADAR 765
|
|
| GlnD_UR_UTase |
pfam08335 |
GlnD PII-uridylyltransferase; This is a family of bifunctional uridylyl-removing enzymes ... |
184-324 |
4.89e-51 |
|
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: 175.46 E-value: 4.89e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 184 DFFLAKRAEQKARHHKYNDTEYNLEPNVKGSPGGLRDIQTILWVARRQYGTLNLRALAGEGFLVESEHALLASSQEFLWK 263
Cdd:pfam08335 1 RFMKAKIEEQVARHGRYGDTAYNLEPNIKLGPGGLRDIEFIVWIAQLIFTLRALEELVELGLLTREEARELRRAYRFLRR 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 860323935 264 VRYALHMLAGRAEDRLLFDHQRSIAELLGFTGEDTKQtIENFMQQYYRVVMSIAQLSDLII 324
Cdd:pfam08335 81 VRHRLHLLADRQTDRLPFDLQRRLARALGYARDGWLA-VERFMRRLFRHAHRVSRLFEILL 140
|
|
| glnD |
PRK00227 |
[protein-PII] uridylyltransferase; |
80-610 |
2.43e-31 |
|
[protein-PII] uridylyltransferase;
Pssm-ID: 178937 [Multi-domain] Cd Length: 693 Bit Score: 131.43 E-value: 2.43e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 80 ALVAVGGYGRGELHPYSDIDLlILLDKADHELfrDSIERFLTLLWDIGLEVGQSVRSVDECAEQARADLTIITNLMESRT 159
Cdd:PRK00227 29 ALAATGSLARREMTPYSDLDL-ILLHPPGATP--DGVEDLWYPIWDAKKRLDYSVRTPQECAAMISADSTAALALLDLRF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 160 VAGPERL----RQRMLDvtstahMWPS--KDFFLAKRAEQKARHHKYNDTEYNLEPNVKGSPGGLRDIQTILWVArrqYG 233
Cdd:PRK00227 106 VAGDEQLtastRAKILE------KWRRelNKNFDAVVDTAIARWRRSGSVVAMTRPDLKHGRGGLRDIELIRALA---LG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 234 TL-NLRALagegflvESEHALLASsqeflwkVRYALHMLAGRAEDRLLFDHQRSIAELLGFtgEDTkqtienfmqqyYRV 312
Cdd:PRK00227 177 HLcDAPPL-------DSQHQLLLD-------VRTLLHVHARRARDVLDPEFAVDIALDLGF--VDR-----------YHL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 313 VMSIAQLSDLIIQHFEEViLAPEDEAPP----VPLNSRFQLHDGYIEATSDHVFKRTPfAMLEIFLLMaqhpEIKGVRAD 388
Cdd:PRK00227 230 SREIADAARAIDDALTAA-LATARGALPrrtaFRNAVRRPLDVDVVDANGTIALSRTP-DLDDPALPL----RVAAAAAR 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 389 TIRLLREH-----RYLIDDDFRNDIRNTSLFIELFKCKIGIHRNLRRMNRYGILGRYLPEFGFIVGQMQHDLFHIYTVDA 463
Cdd:PRK00227 304 TGLPVSESvwkrlEECPELPEPWPASAAGDFFRLLSSPVNSRRVIKQMDRHGLWERIVPEWDRIRGLMPREPSHIHTIDE 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 464 HTLNLIKHlrklqytqtsekfplATKLMAKLPKPELIYLAGLYHDIGKGRHGDHSEIGAIDAEAFCIRHHLPQWDTRLIV 543
Cdd:PRK00227 384 HSLNTVAN---------------CALETVTVARPDLLLLGALYHDIGKGYPRPHEQVGAEMVARAARRMGLNLRDRAVVQ 448
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 860323935 544 WLVQNHLVMSTTAQRKDLSDPQVIHDFAQTV-VDETRLDYLYVLTVADINATNPTLWNSWRASLLRQL 610
Cdd:PRK00227 449 TLVAEHTTLARIAGRLDPTSEEAVDKLLDAVrYDLLTLNLLEVLTEADAEGTGPGVWTARLEQGLRIV 516
|
|
| ACT_ACR-UUR-like_2 |
cd04899 |
C-terminal ACT domains of the bacterial signal-transducing uridylyltransferase ... |
815-885 |
1.39e-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: 106.00 E-value: 1.39e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 860323935 815 TVLELSAPDRPGLLARIGMIFLEFDLSLQNAKIATLGERVEDVFFITDANNQPLsDPQLCMRLQEAIVEHL 885
Cdd:cd04899 1 TVLELTALDRPGLLADVTRVLAELGLNIHSAKIATLGERAEDVFYVTDADGQPL-DPERQEALRAALGEAL 70
|
|
| NT_GlnE_GlnD_like |
cd05401 |
Nucleotidyltransferase (NT) domain of Escherichia coli adenylyltransferase (GlnE), Escherichia ... |
33-172 |
1.84e-27 |
|
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: 109.74 E-value: 1.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 33 RQAREVLDQRFRAGRDIRRLIEDRAWFVDNILQQAWDQ-----FNWCNQADIALVAVGGYGRGELHPYSDIDLLILLD-- 105
Cdd:cd05401 5 RQLRRILRRDLLGGASIRAISRALSDLADALLRRALELalaelGKGPPPVPFALLALGSYGRGELNPSSDQDLLLLYDdd 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 106 -KADHELFRDSIER---------FLTLLWDIGLEVGQSVRSVDECAEQARADLTI------ITNLMESRTVAGPERLRQR 169
Cdd:cd05401 85 gDEVAAYFEELAERlikilseagGPYCLGDVMLRPPGWRRSLAEWLDAARDWLTEpgrlweRTALLDARPVAGDRALAEE 164
|
...
gi 860323935 170 MLD 172
Cdd:cd05401 165 LRR 167
|
|
| ACT_UUR-like_1 |
cd04900 |
ACT domain family, ACT_UUR-like_1, includes the first of two C-terminal ACT domains of the ... |
704-777 |
2.46e-26 |
|
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: 102.56 E-value: 2.46e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 860323935 704 GTQIFIYAPDQHDFFAVTVAAMDQLNLNIHDARIITSSSQFTLDTYIVLDNDGDSIGnNPVRIEKIRKGLTEAL 777
Cdd:cd04900 1 GTEVFIYTPDRPGLFARIAGALDQLGLNILDARIFTTRDGYALDTFVVLDPDGEPIG-ERERLARIREALEDAL 73
|
|
| ACT_UUR-ACR-like |
cd04873 |
ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) ... |
815-885 |
7.46e-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: 86.83 E-value: 7.46e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 860323935 815 TVLELSAPDRPGLLARIGMIFLEFDLSLQNAKIATLGERVEDVFFITDANNQPLsDPQLCMRLQEAIVEHL 885
Cdd:cd04873 1 TVVEVYAPDRPGLLADITRVLADLGLNIHDARISTTGERALDVFYVTDSDGRPL-DPERIARLEEALEDAL 70
|
|
| ACT_UUR-ACR-like |
cd04873 |
ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) ... |
705-777 |
5.23e-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: 76.05 E-value: 5.23e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 860323935 705 TQIFIYAPDQHDFFAVTVAAMDQLNLNIHDARIITSSSQFtLDTYIVLDNDGDSIgnNPVRIEKIRKGLTEAL 777
Cdd:cd04873 1 TVVEVYAPDRPGLLADITRVLADLGLNIHDARISTTGERA-LDVFYVTDSDGRPL--DPERIARLEEALEDAL 70
|
|
| ACT_ACR_4 |
cd04926 |
C-terminal ACT domain, of a novel type of ACT domain-containing protein which is composed ... |
817-867 |
1.25e-09 |
|
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: 55.05 E-value: 1.25e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 860323935 817 LELSAPDRPGLLARIGMIFLEFDLSLQNAKIATLGERVEDVFFITDANNQP 867
Cdd:cd04926 4 LELRTEDRVGLLSDVTRVFRENGLTVTRAEISTQGDMAVNVFYVTDANGNP 54
|
|
| HDc |
smart00471 |
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ... |
457-603 |
2.67e-07 |
|
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: 50.37 E-value: 2.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 457 HIYTVDAHTLNLIKHLRKLqytqtsekfplATKLmaKLPKPELIYLAGLYHDIGKGRHGD-----------HSEIGAIDA 525
Cdd:smart00471 1 SDYHVFEHSLRVAQLAAAL-----------AEEL--GLLDIELLLLAALLHDIGKPGTPDsflvktsvledHHFIGAEIL 67
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 860323935 526 EafciRHHLPQWDTRLIVWLVQNHlvmsttaqrkdlsdpqviHDFAQTVVDETRLDYLYVLTVADINATNPTLWNSWR 603
Cdd:smart00471 68 L----EEEEPRILEEILRTAILSH------------------HERPDGLRGEPITLEARIVKVADRLDALRADRRYRR 123
|
|
| ACT_UUR-like_1 |
cd04900 |
ACT domain family, ACT_UUR-like_1, includes the first of two C-terminal ACT domains of the ... |
821-885 |
4.72e-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: 4.72e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 860323935 821 APDRPGLLARIGMIFLEFDLSLQNAKIATLGE-RVEDVFFITDANNQPLSDPQLCMRLQEAIVEHL 885
Cdd:cd04900 8 TPDRPGLFARIAGALDQLGLNILDARIFTTRDgYALDTFVVLDPDGEPIGERERLARIREALEDAL 73
|
|
| NTP_transf_2 |
pfam01909 |
Nucleotidyltransferase domain; Members of this family belong to a large family of ... |
78-148 |
5.11e-06 |
|
Nucleotidyltransferase domain; Members of this family belong to a large family of nucleotidyltransferases. This family includes kanamycin nucleotidyltransferase (KNTase) which is a plasmid-coded enzyme responsible for some types of bacterial resistance to aminoglycosides. KNTase in-activates antibiotics by catalysing the addition of a nucleotidyl group onto the drug.
Pssm-ID: 396474 Cd Length: 91 Bit Score: 45.48 E-value: 5.11e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 860323935 78 DIALVAVGGYGRGELHPYSDIDLLILLDKADHELFRDSIERFLTLL-WDIGLEVGQSVRSVDECAEQARADL 148
Cdd:pfam01909 14 VAEVVLFGSYARGTALPGSDIDLLVVFPEPVEEERLLKLAKIIKELeELLGLEVDLVTREKIEFPLVKIDIL 85
|
|
| HDc |
cd00077 |
Metal dependent phosphohydrolases with conserved 'HD' motif |
459-611 |
1.28e-05 |
|
Metal dependent phosphohydrolases with conserved 'HD' motif
Pssm-ID: 238032 [Multi-domain] Cd Length: 145 Bit Score: 45.79 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 459 YTVDAHTLNLIKHLRKLqytqtsekfplATKLMAKLPKPELIYLAGLYHDIGKG------------RHGDHSEIGAIDAe 526
Cdd:cd00077 1 EHRFEHSLRVAQLARRL-----------AEELGLSEEDIELLRLAALLHDIGKPgtpdaiteeeseLEKDHAIVGAEIL- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 527 afciRHHLPQWDTRLIVWLVQNHLvmSTTAQRKDLSDPQVIhdfaqtVVDETRLDYLYVLTVAD-INATNPTLWNSWRAS 605
Cdd:cd00077 69 ----RELLLEEVIKLIDELILAVD--ASHHERLDGLGYPDG------LKGEEITLEARIVKLADrLDALRRDSREKRRRI 136
|
....*.
gi 860323935 606 LLRQLY 611
Cdd:cd00077 137 AEEDLE 142
|
|
| HD |
pfam01966 |
HD domain; HD domains are metal dependent phosphohydrolases. |
486-564 |
1.35e-05 |
|
HD domain; HD domains are metal dependent phosphohydrolases.
Pssm-ID: 460398 [Multi-domain] Cd Length: 110 Bit Score: 44.92 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 486 LATKLMAKLP--KPELIYLAGLYHDIGKGRHGD----------HSEIGAIDAEAFCIRHHLpqwdtRLIVWLVQNHLVMS 553
Cdd:pfam01966 11 LARELAEELGelDRELLLLAALLHDIGKGPFGDekpefeiflgHAVVGAEILRELEKRLGL-----EDVLKLILEHHESW 85
|
90
....*....|.
gi 860323935 554 TTAQRKDLSDP 564
Cdd:pfam01966 86 EGAGYPEEISL 96
|
|
| MJ0604 |
COG1708 |
Predicted nucleotidyltransferase, MJ0604 family [General function prediction only]; |
78-130 |
4.11e-05 |
|
Predicted nucleotidyltransferase, MJ0604 family [General function prediction only];
Pssm-ID: 441314 Cd Length: 95 Bit Score: 43.09 E-value: 4.11e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 860323935 78 DIALVAV-GGYGRGELHPYSDIDLLILLDkaDHELFRDSIERFLTLLWDIGLEV 130
Cdd:COG1708 21 EVAAVYLfGSYARGDARPDSDIDLLVVVD--DPPLPDERLELLADLLRELGLPV 72
|
|
| ACT |
pfam01842 |
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ... |
815-870 |
4.44e-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: 42.29 E-value: 4.44e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 860323935 815 TVLELSAPDRPGLLARIGMIFLEFDLSLQNAKIATLGERVEDVFFITDANNQPLSD 870
Cdd:pfam01842 1 TVLEVLVPDRPGLLARVLGALADRGINITSIEQGTSEDKGGIVFVVIVVDEEDLEE 56
|
|
| ACT_ACR_2 |
cd04925 |
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats ... |
815-871 |
5.25e-05 |
|
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: 42.03 E-value: 5.25e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 860323935 815 TVLELSAPDRPGLLARIGMIFLEFDLSLQNAKIATLGERVEDVFFITDANN-QPLSDP 871
Cdd:cd04925 1 TAIELTGTDRPGLLSEVFAVLADLHCNVVEARAWTHNGRLACVIYVRDEETgAPIDDP 58
|
|
| RnaY |
COG1418 |
HD superfamily phosphodieaserase, includes HD domain of RNase Y [Translation, ribosomal ... |
452-549 |
5.74e-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: 44.89 E-value: 5.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 452 QHDLFHIYTVdAHtlnlikhlrklqytqtsekfpLATKLMAKLP-KPELIYLAGLYHDIGK----GRHGDHSEIGAIDAE 526
Cdd:COG1418 17 QHDLQHSLRV-AK---------------------LAGLIAAEEGaDVEVAKRAALLHDIGKakdhEVEGSHAEIGAELAR 74
|
90 100
....*....|....*....|...
gi 860323935 527 AFCIRHHLPQWDTRLIVWLVQNH 549
Cdd:COG1418 75 KYLESLGFPEEEIEAVVHAIEAH 97
|
|
| ACT |
cd02116 |
ACT domains are commonly involved in specifically binding an amino acid or other small ligand ... |
817-867 |
1.04e-04 |
|
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: 40.74 E-value: 1.04e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 860323935 817 LELSAPDRPGLLARIGMIFLEFDLSLQNAKIATLG-ERVEDVFFITDANNQP 867
Cdd:cd02116 1 LTVSGPDRPGLLAKVLSVLAEAGINITSIEQRTSGdGGEADIFIVVDGDGDL 52
|
|
| NT_KNTase_like |
cd05403 |
Nucleotidyltransferase (NT) domain of Staphylococcus aureus kanamycin nucleotidyltransferase, ... |
77-130 |
2.17e-04 |
|
Nucleotidyltransferase (NT) domain of Staphylococcus aureus kanamycin nucleotidyltransferase, and similar proteins; S. aureus KNTase is a plasmid encoded enzyme which confers resistance to a wide range of aminoglycoside antibiotics which have a 4'- or 4''-hydroxyl group in the equatorial position, such as kanamycin A. This enzyme transfers a nucleoside monophosphate group from a nucleotide (ATP,GTP, or UTP) to the 4'-hydroxyl group of kanamycin A. This enzyme is a homodimer, having two NT active sites. The nucleotide and antibiotic binding sites of each active site include residues from each monomer. Included in this subgroup is Escherichia coli AadA5 which confers resistance to the antibiotic spectinomycin and is a putative aminoglycoside-3'-adenylyltransferase. It is part of the aadA5 cassette of a class 1 integron. This subgroup also includes Haemophilus influenzae HI0073 which forms a 2:2 heterotetramer with an unrelated protein HI0074. Structurally HI0074 is related to the substrate-binding domain of S. aureus KNTase. The genes encoding HI0073 and HI0074 form an operon. Little is known about the substrate specificity or function of two-component NTs. The characterized members of this subgroup may not be representive of the function of this subgroup. This subgroup 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, co-ordinate two divalent metal cations involved in a two-metal ion mechanism of nucleotide addition. These carboxylate residues are conserved in this subgroup.
Pssm-ID: 143393 Cd Length: 93 Bit Score: 40.86 E-value: 2.17e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 860323935 77 ADIALVAVGG-YGRGELHPYSDIDLLILLDKADHELFRDSIERFLTLLWDIGLEV 130
Cdd:cd05403 16 GGVEKVYLFGsYARGDARPDSDIDLLVIFDDPLDPLELARLLEELELLLGRPVDL 70
|
|
| PRK11072 |
PRK11072 |
bifunctional [glutamate--ammonia ligase]-adenylyl-L-tyrosine phosphorylase/ ... |
206-348 |
5.20e-04 |
|
bifunctional [glutamate--ammonia ligase]-adenylyl-L-tyrosine phosphorylase/[glutamate--ammonia-ligase] adenylyltransferase;
Pssm-ID: 236836 [Multi-domain] Cd Length: 943 Bit Score: 44.05 E-value: 5.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 206 NLEPNVKGSPGGLRDIQTILWV----------ARRQYGTLN-LRALAGEGFLVESEHALLASSQEFLWKVRYAL------ 268
Cdd:PRK11072 311 GLADNIKLGAGGIREIEFIVQVfqlirggrepSLQQRSLLEvLDALAELGLLPEEQVAELRDAYLFLRRLEHLLqaindq 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 860323935 269 --HMLAGRAEDRLLfdhqrsIAELLGFTGEDTkqtienFMQQyyrvvmsIAQLSDLIIQHFEEVILAPEDEAPPVPLNSR 346
Cdd:PRK11072 391 qtQTLPDDPLDRAR------LAWAMGFADWAA------LLDV-------LDAHRANVRRVFNQLIGDDEEETEEEAASEQ 451
|
..
gi 860323935 347 FQ 348
Cdd:PRK11072 452 WR 453
|
|
| ACT_ACR-UUR-like_2 |
cd04899 |
C-terminal ACT domains of the bacterial signal-transducing uridylyltransferase ... |
705-777 |
1.28e-03 |
|
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: 38.20 E-value: 1.28e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 860323935 705 TQIFIYAPDQ----HDFFAVTVaamdQLNLNIHDARIITSSSQfTLDTYIVLDNDGDSIgnNPVRIEKIRKGLTEAL 777
Cdd:cd04899 1 TVLELTALDRpgllADVTRVLA----ELGLNIHSAKIATLGER-AEDVFYVTDADGQPL--DPERQEALRAALGEAL 70
|
|
| ACT_ACR_1 |
cd04895 |
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats ... |
815-881 |
1.62e-03 |
|
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats (the "ACR" protein); This CD includes the N-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: 153167 [Multi-domain] Cd Length: 72 Bit Score: 37.82 E-value: 1.62e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 860323935 815 TVLELSAPDRPGLLARIGMIFLEFDLSLQNAKIATLGERVEDVFFITDANNQPLSDPQLCMRLQEAI 881
Cdd:cd04895 2 TLVKVDSARKPGILLEAVQVLTDLDLCITKAYISSDGGWFMDVFHVTDQLGNKLTDDSLIAYIEKSL 68
|
|
| ACT_ACR-like_2 |
cd04927 |
Second ACT domain, of a novel type of ACT domain-containing protein which is composed almost ... |
816-863 |
2.76e-03 |
|
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: 37.45 E-value: 2.76e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 860323935 816 VLELSAPDRPGLLARIGMIFLEFDLSLQNAKIATLGE-RVEDVFFITDA 863
Cdd:cd04927 2 LLKLFCSDRKGLLHDVTEVLYELELTIERVKVSTTPDgRVLDLFFITDA 50
|
|
| MJ0435 |
COG1669 |
Predicted nucleotidyltransferase MJ0435 [General function prediction only]; |
62-123 |
6.21e-03 |
|
Predicted nucleotidyltransferase MJ0435 [General function prediction only];
Pssm-ID: 441275 Cd Length: 96 Bit Score: 36.82 E-value: 6.21e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 860323935 62 NILQQAWDQFnwCNQADIALVAV-GGYGRGELHPYSDIDLLILLDKADHELFRDSIERFLTLL 123
Cdd:COG1669 8 EILREVIEEL--AERYGVSRLGLfGSVARGEAREDSDIDLLVEFDEPTSLFDLFELEEELEEL 68
|
|
| |
