|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05007 |
PRK05007 |
bifunctional uridylyltransferase/uridylyl-removing protein GlnD; |
7-890 |
0e+00 |
|
bifunctional uridylyltransferase/uridylyl-removing protein GlnD;
Pssm-ID: 235329 [Multi-domain] Cd Length: 884 Bit Score: 1841.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 7 QYANTALPTLPGQPQNPCVWPRDELTVGGIKAHIDTFQRWLGDAFDNGISAEQLIEARTEFIDQLLQRLWIEAGFSQIAD 86
Cdd:PRK05007 1 QYANTALPTLPGQPQSPLTWPDDELTVGGLKQHLDTFQQWLGDAFDAGISAEQLVEARTEFIDQLLQRLWIEAGFDQIPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 87 LALVAVGGYGRGELHPLSDIDLLILSRKKLPDDQAQKVGELLTLLWDVKLEVGHSVRTLEECMLEGLSDLTVATNLIESR 166
Cdd:PRK05007 81 LALVAVGGYGRGELHPLSDIDLLILSRKKLPDEQAQKVGELITLLWDLKLEVGHSVRTLEECLLEGLSDLTVATNLIESR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 167 LLIGDVALFLELQKHIFSEGFWPSDKFYAAKVEEQNQRHQRYHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSLD 246
Cdd:PRK05007 161 LLCGDVALFLELQKHIFSDGFWPSEKFYAAKVEEQNERHQRYHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSLD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 247 EMVGFGFLTSAERAELNECLHILWRIRFALHLVVSRYDNRLLFDRQLSVAQRLNYSGEGNEPVERMMKDYFRVTRRVSEL 326
Cdd:PRK05007 241 EMVGFGFLTPAERAELNECQHFLWRIRFALHLVLSRYDNRLLFDRQLSVAQLLGYEGEGNEPVERMMKDYYRTTRRVSEL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 327 NQMLLQLFDEAILALPADEKPRPIDDEFQLRGTLIDLRDETLFMRQPEAILRMFYTMVRNSAITGIYSTTLRQLRHARRH 406
Cdd:PRK05007 321 NQMLLQLFDEAILALTADEKPRPIDDEFQLRGTLIDLRDETLFQRQPEAILRMFYLMARNSNITGIYSTTLRQLRHARRH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 407 LQQPLCNIPQARKLFLSILRHPGAVRRGLLPMHRHSVLGAYMPQWSHIVGQMQFDLFHAYTVDEHTIRVMLKLESFASEE 486
Cdd:PRK05007 401 LNQPLCEIPEARKLFMEILRHPGAVSRALLPMHRHSVLSAYMPQWSHIVGQMQFDLFHAYTVDEHTIRVLLKLESFADEE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 487 TRQRHPLCVNVWPRLPSTELIFIAALFHDIAKGRGGDHSILGAQDVVHFAELHGLNSRETQLVAWLVRQHLLMSVTAQRR 566
Cdd:PRK05007 481 TRQRHPLCVELYPRLPKKELLLLAALFHDIAKGRGGDHSILGAQDALEFAELHGLNSRETQLVAWLVRNHLLMSVTAQRR 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 567 DIQDPEVIKQFAEEVQTENRLRYLVCLTVADICATNETLWNSWKQSLLRELYFATEKQLRRGMQNTPDMRERVRHHQLQA 646
Cdd:PRK05007 561 DIQDPDVIKQFAEEVQDENRLRYLVCLTVADICATNETLWNSWKQSLLRELYFATEKQLRRGMENPPDMRERVRHHQLQA 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 647 LALLRMDNIDEEVLHQIWSRCRANYFVRHSPNQLAWHARHLLQHDLSKPLVLLSPQATRGGTEIFIWSPDRPYLFAAVCA 726
Cdd:PRK05007 641 LALLRMDNIDEEALHQIWSRCRADYFLRHTPNQLAWHARHLLQHDLDKPLVLLSKQATRGGTEIFIWSPDRPYLFAAVCA 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 727 ELDRRNLSVHDAQIFTTRDGMAMDTFIVLEPDGSPLSADRHEVIRFGLEQVLTQSSWQPPQPRRQPAKLRHFTVETEVTF 806
Cdd:PRK05007 721 ELDRRNLSVHDAQIFTSRDGMAMDTFIVLEPDGSPLSQDRHQVIRKALEQALTQSSPQPPKPRRLPAKLRHFNVPTEVSF 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 807 LPTHTDRKSFLELIALDQPGLLARVGKIFADLGISLHGARITTIGERVEDLFIIATADRRALNNELQQEVHQRLTEALNP 886
Cdd:PRK05007 801 LPTHTDRRSYMELIALDQPGLLARVGKIFADLGISLHGARITTIGERVEDLFILATADRRALNEELQQELRQRLTEALNP 880
|
....
gi 15829423 887 NDKG 890
Cdd:PRK05007 881 NDKG 884
|
|
| GlnD |
COG2844 |
UTP:GlnB (protein PII) uridylyltransferase [Posttranslational modification, protein turnover, ... |
30-889 |
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: 1262.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 30 ELTVGGIKAHIDTFQRWLGDAFDNGISAEQLIEARTEFIDQLLQRLWIEAGFSQIADLALVAVGGYGRGELHPLSDIDLL 109
Cdd:COG2844 1 AAALAALREALAEGRAALRERFRAGADGRELVRARAALVDQLLRALWDLAGLTEPERLALVAVGGYGRGELAPHSDIDLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 110 ILSRKKLPDDQAQKVGELLTLLWDVKLEVGHSVRTLEECMLEGLSDLTVATNLIESRLLIGDVALFLELQKHIFSEGFWP 189
Cdd:COG2844 81 FLLPDKPTPALEEVIEAFLYLLWDLGLEVGHSVRTVDECLREAREDITVRTALLEARLLAGDEALFEELRERFRADVFWD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 190 SDKFYAAKVEEQNQRHQRYHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSLDEMVGFGFLTSAERAELNECLHIL 269
Cdd:COG2844 161 SRAFFEAKLAEQRERHAKYGDTRYNLEPNIKEGPGGLRDLQTLLWIAKRHFGVRSLEELVKKGLLTEEEYRELRRAEDFL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 270 WRIRFALHLVVSRYDNRLLFDRQLSVAQRLNYSG-EGNEPVERMMKDYFRVTRRVSELNQMLLQLFDEAILALPADEKPR 348
Cdd:COG2844 241 WRVRFALHLLAGRAEDRLLFDLQREVAERLGYQDtEGNRAVERFMQRYYRTAKAVGRLNEILLQRLEEAILKPPGLRRPR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 349 PIDDEFQLRGTLIDLRDETLFMRQPEAILRMFYTMVRNSAITGIYSTTLRQLRHARRHLQQPLCNIPQARKLFLSILRHP 428
Cdd:COG2844 321 PINEGFQLRNGRLEVADPDVFERDPVALLRLFLLAAQHPEGLGIHPDTLRLLRRALRLIDDAFRRDPEARRLFLEILRQP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 429 GAVRRGLLPMHRHSVLGAYMPQWSHIVGQMQFDLFHAYTVDEHTIRVMLKLESFASEETRQRHPLCVNVWPRLPSTELIF 508
Cdd:COG2844 401 RGITRALRRMNEYGVLGRYIPEFGRIVGQMQFDLFHVYTVDEHTLRVVRNLRRFERGELAEEFPLASELIAELPKPELLY 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 509 IAALFHDIAKGRGGDHSILGAQDVVHFAELHGLNSRETQLVAWLVRQHLLMSVTAQRRDIQDPEVIKQFAEEVQTENRLR 588
Cdd:COG2844 481 LAALFHDIAKGRGGDHSELGAEDARRFCPRHGLSPEDTELVAWLVRHHLLMSHTAQRRDISDPEVIRDFARLVGSEERLD 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 589 YLVCLTVADICATNETLWNSWKQSLLRELYFATEKQLRRGMQnTPDMRERVRHHQLQALALLRMDNIDEEVLHQIWSRCR 668
Cdd:COG2844 561 YLYLLTVADIRATGPKVWNSWKASLLRELYRATLRALRGGLE-PPDREERIEERKEEALALLADQGWDEEEIEALWARLP 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 669 ANYFVRHSPNQLAWHARHLLQH-DLSKPLVLLSPQATRGGTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDGM 747
Cdd:COG2844 640 DDYFLRHDPEEIAWHARLLLRAdDSGKPLVLIRPDPDRGGTEVFVYTPDRPGLFARIAGALAALGLNILDARIHTTRDGY 719
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 748 AMDTFIVLEPDGSPLS-ADRHEVIRFGLEQVLTQSSWQP-PQPRRQPAKLRHFTVETEVTFLPTHTDRKSFLELIALDQP 825
Cdd:COG2844 720 ALDTFIVLDPDGEPIDdPDRLERIEQALEEALSGEVPLPePLARRLSRRLRHFPVPPRVTFDNDASNRYTVLEVSALDRP 799
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15829423 826 GLLARVGKIFADLGISLHGARITTIGERVEDLFIIATADRRALNN-ELQQEVHQRLTEALNPNDK 889
Cdd:COG2844 800 GLLYDIARVLADLGLNIHSAKIATLGERVEDVFYVTDLDGQKLTDpERQEALREALLEALDEEAE 864
|
|
| glnD |
PRK01759 |
bifunctional uridylyltransferase/uridylyl-removing protein GlnD; |
30-885 |
0e+00 |
|
bifunctional uridylyltransferase/uridylyl-removing protein GlnD;
Pssm-ID: 234980 [Multi-domain] Cd Length: 854 Bit Score: 1051.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 30 ELTVGGIKAHIDTFQRWLGDAFDNgISAEQLIEARTEFIDQLLQRLWIEAGFSQIADLALVAVGGYGRGELHPLSDIDLL 109
Cdd:PRK01759 1 LLTPSAVKIQKENLKQFELENFSQ-EDVFELIENRSDFYDQLLIHLWQQFGLEEQSDLALIAVGGYGRREMFPLSDLDIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 110 ILSRKKLPDDQAQKVGELLTLLWDVKLEVGHSVRTLEECMLEGLSDLTVATNLIESRLLIGDVALFLELQKHIFSEGFWP 189
Cdd:PRK01759 80 ILTEQPPDEETEEKINQFFQFLWDCGFEVGASVRTLAECESEGRADITIATNLLESRFLTGNEKLFDALVELLQQADFWS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 190 SDKFYAAKVEEQNQRHQRYHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSLDEMVGFGFLTSAERAELNECLHIL 269
Cdd:PRK01759 160 KEAFFQAKIQEKIERYQRYHNTSYNLEPDIKYSPGGLRDLHLLYWIALRHSGAKSLEEILQSGFIYPEEYAELQQSQQFL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 270 WRIRFALHLVVSRYDNRLLFDRQLSVAQRLNYSGEGNEPVERMMKDYFRVTRRVSELNQMLLQLFDEAILALPADEKPRP 349
Cdd:PRK01759 240 FKVRFALHLILKRYDNRLLFDRQLKVSELLGFQGEGNQGVEKMMKSFFQALQSISLLSDLLVKHYREHFLQPNQNVEIQP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 350 IDDEFQLRGTLIDLRDETLFMRQPEAILRMFYTMVRNSAITgIYSTTLRQLRHARRHLQQPLCNIPQARKLFLSILRHPG 429
Cdd:PRK01759 320 LDDDFYLINNAICLRNPDCFEQQPESILDLFFYLTQYPQAE-IHSTTLRQLRLALEQLQQPLCELPAARERFLRLFNQPN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 430 AVRRGLLPMHRHSVLGAYMPQWSHIVGQMQFDLFHAYTVDEHTIRVMLKLESFASEETRQRHPLCVNVWPRLPSTELIFI 509
Cdd:PRK01759 399 AIKRALVPMHQYGVLTAYLPQWKGIVGLMQFDLFHIYTVDEHTLRVMLKLESFLDEESAEQHPICHQIFSQLSDRTLLYI 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 510 AALFHDIAKGRGGDHSILGAQDVVHFAELHGLNSRETQLVAWLVRQHLLMSVTAQRRDIQDPEVIKQFAEEVQTENRLRY 589
Cdd:PRK01759 479 AALFHDIAKGRGGDHAELGAVDMRQFAQQHGFDQREIETMAWLVQQHLLMSVTAQRRDIHDPEVVMNFAEEVQNQVRLDY 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 590 LVCLTVADICATNETLWNSWKQSLLRELYFATEKQLRRGMQNTPDMRERVRHHQLQALALLRMDNIDEEVLH--QIWSRC 667
Cdd:PRK01759 559 LTCLTVADICATNETLWNSWKRSLFATLYQFTNQQFQQGMDELLDYQEKAEENRQQALELLQQKYSALSETQieQLWQRC 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 668 RANYFVRHSPNQLAWHARHLLQhDLSKPLVLLSPQATRGGTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDGM 747
Cdd:PRK01759 639 PEDYFLRNTPKQIAWHALLLLD-FRGDLLVKISNRFSRGGTEIFIYCQDQANLFLKVVSTIGAKKLSIHDAQIITSQDGY 717
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 748 AMDTFIVLEPDGSPLSADRHEVIRFGLEQVLTQSSWQPPQPRRQPaKLRHFTVETEVTFLPTHTDRKSFLELIALDQPGL 827
Cdd:PRK01759 718 VLDSFIVTELNGKLLEFDRRRQLEQALTKALNTNKLKKLNLEENH-KLQHFHVKTEVRFLNEEKQEQTEMELFALDRAGL 796
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*...
gi 15829423 828 LARVGKIFADLGISLHGARITTIGERVEDLFIIATADRRALNNELQQEVHQRLTEALN 885
Cdd:PRK01759 797 LAQVSQVFSELNLNLLNAKITTIGEKAEDFFILTNQQGQALDEEERKALKSRLLSNLS 854
|
|
| UTase_glnD |
TIGR01693 |
[Protein-PII] uridylyltransferase; This model describes GlnD, the uridylyltransferase ... |
51-884 |
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: 937.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 51 FDNGISAEQLIEARTEFIDQLLQRLWIEAGFSQIADLALVAVGGYGRGELHPLSDIDLLILSRKKLPDDQAQKVGELLTL 130
Cdd:TIGR01693 8 FARGGDGRELREGRSDLTDLLLIRLWDFIGISEHSGIALVAVGGYGRGELAPYSDIDLLFLHDGKPAEEVEPKIERFLYP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 131 LWDVKLEVGHSVRTLEECMLEGLSDLTVATNLIESRLLIGDVALFLELQKHIFSEGFWPSD-KFYAAKVEEQNQRHQRYH 209
Cdd:TIGR01693 88 LWDLGFEVGHSVRTLEECARIAKADLTVATNLLEARHLAGDEALFFRLKERVRREDWRNTArSFLAAKVEEQDERHARYG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 210 GTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSLDEMVGFGFLTSAERAELNECLHILWRIRFALHLVVSRYDNRLLF 289
Cdd:TIGR01693 168 DTAYNLEPDIKEGPGGLRDLHTLFWVALYQLGVRRLEDLVKQGFLTDAEYKLLAEARDFLWDVRFALHLTTGRADDRLLF 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 290 DRQLSVAQRLNYSGEGNEPVERMMKDYFRVTRRVSELNQMLLQLFDEAIL-----ALPADEKPRPIDDEFQLRGTLIDLR 364
Cdd:TIGR01693 248 DHQDEIAAALGYGDEGNPAVERFMRRYFQAARRIGYLTEAFLRHYEEALLsrgpsARVRRPKRRPLDEGFVEDGGELVLA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 365 DETLFMRQPEAILRMFYTMVRNSaiTGIYSTTLRQLRHARRHLQQPLCNIPQARKLFLSILRHPGAVRRGLLPMHRHSVL 444
Cdd:TIGR01693 328 RTAVFERDPALLLRLFAIAAQRG--LPIHPAALRQLTASLPLLPTPLREDPEARELFLELLTSGNGTVRALRAMNRAGVL 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 445 GAYMPQWSHIVGQMQFDLFHAYTVDEHTIRVMLKLESFASEETRQRHPLCVNVWPRLPSTELIFIAALFHDIAKGRGGDH 524
Cdd:TIGR01693 406 GRFLPEWGRIVGQMQFDLFHVYTVDEHTLRTVVHLAPFARGRLAREHPLASELMPKIEDPELLYLAALLHDIGKGRGGDH 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 525 SILGAQDVVHFAELHGLNSRETQLVAWLVRQHLLMSVTAQRRDIQDPEVIKQFAEEVQTENRLRYLVCLTVADICATNET 604
Cdd:TIGR01693 486 SVLGAEDARDVCPRLGLDRPDTELVAWLVRNHLLMSITAQRRDLNDPKTVFAFAEAVGDPERLEYLLALTVADIRATGPG 565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 605 LWNSWKQSLLRELYFATEKQLRRGMQNTPDMRERVRHHQLQALALLRMDNIDEEVlHQIWSRCRANYFVRHSPNQLAWHA 684
Cdd:TIGR01693 566 VWNSWKASLLRDLYNRTEQVLRGGLEPPADPAEPIAEQRKLAVALLRTDYTSNEA-EVLWLRAYDDYFLRFTHKEIAWHA 644
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 685 RHLLQHDLS-KPLVLLSPQATRGGTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDGMAMDTFIVLEPDGSPLS 763
Cdd:TIGR01693 645 ESLRRALSSgGPLALIDGTRPSGGTEVFIYAPDQPGLFAKVAGALAMLSLSVHDAQVNTTKDGVALDTFVVQDLFGSPPA 724
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 764 ADR-HEVIRFGLEQVLTQSSWQPPQP---RRQPAKLRHFTVETEVTFLPTHTDRKSFLELIALDQPGLLARVGKIFADLG 839
Cdd:TIGR01693 725 AERvFQELLQGLVDVLAGLAKDPDTIsarRARRRRLQHFAVPPRVTILNTASRKATIMEVRALDRPGLLARVGRTLEELG 804
|
810 820 830 840
....*....|....*....|....*....|....*....|....*
gi 15829423 840 ISLHGARITTIGERVEDLFIIATADRRALNNELQQEVHQRLTEAL 884
Cdd:TIGR01693 805 LSIQSAKITTFGEKAEDVFYVTDLFGLKLTDEEEQRLLEVLAASV 849
|
|
| glnD |
PRK00275 |
PII uridylyl-transferase; Provisional |
47-887 |
0e+00 |
|
PII uridylyl-transferase; Provisional
Pssm-ID: 234709 [Multi-domain] Cd Length: 895 Bit Score: 889.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 47 LGDAFDNGISAEQLIEARTEFIDQLLQRLWIEAGFSQIADLALVAVGGYGRGELHPLSDIDLLILSRKKLPDDQAQKVGE 126
Cdd:PRK00275 39 LDERFRSGRDIRRLIEDRAWFVDQILQQAWHQFDWSDDADIALVAVGGYGRGELHPYSDIDLLILLDSADHEEFREPIER 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 127 LLTLLWDVKLEVGHSVRTLEECMLEGLSDLTVATNLIESRLLIGDVALFLELQKHIFSEGFWPSDKFYAAKVEEQNQRHQ 206
Cdd:PRK00275 119 FLTLLWDIGLEIGQSVRSVDECAEEARADLTVITNLMESRTIAGPESLRQRMLEVTSSEHMWPSKEFFLAKRAEQKARHH 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 207 RYHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSLDEMVGFGFLTSAERAELNECLHILWRIRFALHLVVSRYDNR 286
Cdd:PRK00275 199 KYNDTEYNLEPNVKGSPGGLRDIQTILWVAKRQFGTLNLHALVGEGFLTESEYGLLASGQEFLWKVRYALHMLAGRAEDR 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 287 LLFDRQLSVAQRLNYSGEG-NEPVERMMKDYFRVTRRVSELNQMLLQLFDEAILALPADEKPRPIDDEFQLRGTLIDLRD 365
Cdd:PRK00275 279 LLFDHQRSIATLLGYEDSDaKLAVEQFMQKYYRVVMALAELNDLILQHFEEVILAADDSGTIQPLNSRFQLRDGYIEATH 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 366 ETLFMRQPEAILRMFYTMVRNSAITGIYSTTLRQLRHARRHLQQPLCNIPQARKLFLSILRHPGAVRRGLLPMHRHSVLG 445
Cdd:PRK00275 359 PNVFKRTPFALLEIFVLMAQHPEIKGVRADTIRLLREHRHLIDDAFRNDIRNTSLFIELFKCPIGIHRNLRRMNRYGILG 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 446 AYMPQWSHIVGQMQFDLFHAYTVDEHTIRVMLKLESFASEETRQRHPLCVNVWPRLPSTELIFIAALFHDIAKGRGGDHS 525
Cdd:PRK00275 439 RYLPEFGHIVGQMQHDLFHIYTVDAHTLNLIKNLRKLRYPEVSEKFPLASKLMGRLPKPELLYIAGLYHDIGKGRGGDHS 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 526 ILGAQDVVHFAELHGLNSRETQLVAWLVRQHLLMSVTAQRRDIQDPEVIKQFAEEVQTENRLRYLVCLTVADICATNETL 605
Cdd:PRK00275 519 ELGAVDAEAFCQRHQLPAWDTRLVVWLVENHLLMSTTAQRKDLSDPQVIHDFALKVGDQTHLDYLYVLTVADINATNPTL 598
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 606 WNSWKQSLLRELYFATEKQLRRGMQNTPDMRERVRHHQLQALALLRMDNIDEEVLHQIWSRCRANYFVRHSPNQLAWHAR 685
Cdd:PRK00275 599 WNSWRASLLRQLYTETKRALRRGLENPVDREEQIRQTQSAALDILVRKGTDPDDAEQLWSQLGDDYFLRHTAGDIAWHTE 678
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 686 HLLQH-DLSKPLVLLSPQATR---GGTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDGMAMDTFIVLEPDGSP 761
Cdd:PRK00275 679 AILQHpDDGGPLVLIKETTQRefeGGTQIFIYAPDQHDFFAATVAAMDQLNLNIHDARIITSSSQFTLDTYIVLDDDGEP 758
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 762 LSAD--RHEVIRFGLEQVLTQSSWQPPQ-PRRQPAKLRHFTVETEVTFLPTHTDRKSFLELIALDQPGLLARVGKIFADL 838
Cdd:PRK00275 759 IGDNpaRIEQIREGLTEALRNPDDYPTIiQRRVPRQLKHFAFPTQVTISNDAQRPVTVLEIIAPDRPGLLARIGRIFLEF 838
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....
gi 15829423 839 GISLHGARITTIGERVEDLFIIATADRRALNN-----ELQQEVHQRLTEALNPN 887
Cdd:PRK00275 839 DLSLQNAKIATLGERVEDVFFITDADNQPLSDpqlcsRLQDAICEQLDARNEKD 892
|
|
| PRK03059 |
PRK03059 |
PII uridylyl-transferase; Provisional |
47-885 |
0e+00 |
|
PII uridylyl-transferase; Provisional
Pssm-ID: 235101 [Multi-domain] Cd Length: 856 Bit Score: 740.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 47 LGDAFDNGISAEQLIEARTEFIDQLLQRLWIEAGFSqiADLALVAVGGYGRGELHPLSDIDLLILSRKKLPDDQAQKVGE 126
Cdd:PRK03059 24 LLARFRQAPNVTALLHALSRLVDQALRRLWQECGLP--AGAALVAVGGYGRGELFPYSDVDLLVLLPDAPDAALDARIER 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 127 LLTLLWDVKLEVGHSVRTLEECMLEGLSDLTVATNLIESRLLIGDVALFLELQKHiFSEGFWPSDkFYAAKVEEQNQRHQ 206
Cdd:PRK03059 102 FIGLCWDLGLEIGSSVRTVDECIEEAAQDVTVQTSLLEARLLTGSAALFERFQRR-YRAALDPRA-FFQAKLLEMRQRHA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 207 RYHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSLDEMVGFGFLTSAERAELNECLHILWRIRFALHLVVSRYDNR 286
Cdd:PRK03059 180 KFQDTPYSLEPNCKESPGGLRDLQTILWIARAAGLGSSWRELAKRGLITDREARQLRRNERFLKTLRARLHLLAGRREDR 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 287 LLFDRQLSVAQRLNYSGEGNE-PVERMMKDYFRVTRRVSELNQMLLQLFDEAILALPaDEKPRPIDDEFQLRGTLIDLRD 365
Cdd:PRK03059 260 LVFDLQTALAESFGYRPTAAKrASEQLMRRYYWAAKAVTQLNTILLQNIEARLFPST-SGITRVINERFVEKQGMLEIAS 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 366 ETLFMRQPEAILRMFYTMVRNSAITGIYSTTLRQLRHARRHLQQPLCNIPQARKLFLSILRHPGAVRRGLLPMHRHSVLG 445
Cdd:PRK03059 339 DDLFERHPHAILEAFLLYQQTPGLKGLSARTLRALYNARDVMNAAFRRDPVNRALFMQILQQPRGITHALRLMNQTSVLG 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 446 AYMPQWSHIVGQMQFDLFHAYTVDEHTIRVMLKLESFASEETRQRHPLCVNVWPRLPSTELIFIAALFHDIAKGRGGDHS 525
Cdd:PRK03059 419 RYLPNFRRIVGQMQHDLFHVYTVDQHILMVLRNLRRFAMAEHAHEYPFCSQLIANFDRPWLLYVAALFHDIAKGRGGDHS 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 526 ILGAQDVVHFAELHGLNSRETQLVAWLVRQHLLMSVTAQRRDIQDPEVIKQFAEEVQTENRLRYLVCLTVADICATNETL 605
Cdd:PRK03059 499 TLGAVDARRFCRQHGLAREDAELVVWLVEHHLTMSQVAQKQDLSDPEVIARFAELVGDERRLTALYLLTVADIRGTSPKV 578
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 606 WNSWKQSLLRELYFATEKQLRRGmqnTPDMRERVRHHQLQALALLRMDNIDEEVLHQIWSRCRANYFVRHSPNQLAWHAR 685
Cdd:PRK03059 579 WNAWKGKLLEDLYRATLRVLGGA---APDAHSELEARKEEALALLRLEALPDDAHEALWDQLDVGYFLRHDAADIAWHTR 655
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 686 HLLQH-DLSKPLVLLSPQATRGGTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDGMAMDTFIVLEPDGSPLSA 764
Cdd:PRK03059 656 HLYRHvDTDTPIVRARLSPAGEGLQVMVYTPDQPDLFARICGYFDRAGFSILDARVHTTRHGYALDTFQVLDPEEDVHYR 735
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 765 DRHEVIRFGLEQVLTQSS-WQPPQPRRQPAKLRHFTVETEVTFLPTHTDRKSFLELIALDQPGLLARVGKIFADLGISLH 843
Cdd:PRK03059 736 DIINLVEHELAERLAEQApLPEPSKGRLSRQVKHFPITPRVDLRPDERGQYYILSVSANDRPGLLYAIARVLAEHRVSVH 815
|
810 820 830 840
....*....|....*....|....*....|....*....|..
gi 15829423 844 GARITTIGERVEDLFIIATADRRalNNELQQEVHQRLTEALN 885
Cdd:PRK03059 816 TAKINTLGERVEDTFLIDGSGLS--DNRLQIQLETELLDALA 855
|
|
| PRK05092 |
PRK05092 |
PII uridylyl-transferase; Provisional |
87-884 |
0e+00 |
|
PII uridylyl-transferase; Provisional
Pssm-ID: 235342 [Multi-domain] Cd Length: 931 Bit Score: 593.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 87 LALVAVGGYGRGELHPLSDIDLLILsrkkLPDDQ---AQKVGE-LLTLLWDVKLEVGHSVRTLEECMLEGLSDLTVATNL 162
Cdd:PRK05092 106 LAVLAVGGYGRGELAPGSDIDLLFL----LPYKQtawAESVVEyMLYMLWDLGLKVGHATRSIDECIRLAREDMTIRTAL 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 163 IESRLLIGDVALFLELQKHIFSEGFWPSDK-FYAAKVEEQNQRHQRYHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFG 241
Cdd:PRK05092 182 LEARFLAGDRALFEELETRFDKEVVKGTAAeFVAAKLAERDERHRRAGDSRYLVEPNVKEGKGGLRDLHTLFWIAKYVYR 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 242 ATSLDEMVGFGFLTSAERAELNECLHILWRIRFALHLVVSRYDNRLLFDRQLSVAQRLNYSG-EGNEPVERMMKDYFRVT 320
Cdd:PRK05092 262 VRDAAELVKLGVFTREEYRLFRRAEDFLWAVRCHLHFLTGRAEERLSFDLQPEIAERMGYTDhPGLSGVERFMKHYFLVA 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 321 RRVSELNQMLL------QLFDEAILALPADEKPR-PIDDEFQLRGTLIDLRDETLFMRQPEAILRMFYTMVRNSaiTGIY 393
Cdd:PRK05092 342 KDVGDLTRIFCaaleaqHAKRAPGLNRFARRRRKaLDSDGFVVDNGRINLADPDVFERDPVNLIRLFHLADRHG--LDIH 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 394 STTLRQLRHARRHLQQPLCNIPQARKLFLSILRHPGAVRRGLLPMHRHSVLGAYMPQWSHIVGQMQFDLFHAYTVDEHTI 473
Cdd:PRK05092 420 PDAMRLVTRSLRLIDAALREDPEANRLFLDILTSRRNPERVLRRMNEAGVLGRFIPDFGRIVAMMQFNMYHHYTVDEHTI 499
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 474 RVMLKLESFASEETRQRHPLCVNVWPRLPSTELIFIAALFHDIAKGRGGDHSILGAQDVVHFAELHGLNSRETQLVAWLV 553
Cdd:PRK05092 500 RAIGVLAEIERGELADEHPLASELMPKIESRRALYVAVLLHDIAKGRPEDHSIAGARIARRLCPRLGLSPAETETVAWLV 579
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 554 RQHLLMSVTAQRRDIQDPEVIKQFAEEVQTENRLRYLVCLTVADICATNETLWNSWKQSLLRELYFATEKQLRRGMQNTp 633
Cdd:PRK05092 580 EHHLLMSDTAQKRDLSDPKTIEDFADAVQSPERLKLLLILTVADIRAVGPGVWNGWKAQLLRTLYYETEEVLTGGFSEL- 658
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 634 DMRERVRHHQLQALALLRmdNIDEEVLHQIWSRCRANYFVRHSPNQLAWHARHLLQ--HDLSKPLVLLSPQATRGGTEIF 711
Cdd:PRK05092 659 NRAERVAAAKEALREALS--DWPKADRDAYLARHYPAYWLAVDLDTQARHARFIRDadDAGRPLATEVRPDPARGVTEVT 736
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 712 IWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDGMAMDTFIVLEPDGSPL-SADRHEVIRFGLEQVLTQSSWQPPQPRR 790
Cdd:PRK05092 737 VLAADHPGLFSRIAGACAAAGANIVDARIFTTTDGRALDTFWIQDAFGRDEdEPRRLARLAKAIEDALSGEVRLPEALAK 816
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 791 QP---AKLRHFTVETEVTFLPTHTDRKSFLELIALDQPGLLARVGKIFADLGISLHGARITTIGERVEDLFIIATADRRA 867
Cdd:PRK05092 817 RTkpkKRARAFHVPPRVTIDNEASNRFTVIEVNGRDRPGLLYDLTRALSDLNLNIASAHIATYGERAVDVFYVTDLFGLK 896
|
810
....*....|....*...
gi 15829423 868 LNNELQQE-VHQRLTEAL 884
Cdd:PRK05092 897 ITNEARQAaIRRALLAAL 914
|
|
| PRK04374 |
PRK04374 |
[protein-PII] uridylyltransferase; |
51-887 |
0e+00 |
|
[protein-PII] uridylyltransferase;
Pssm-ID: 179839 [Multi-domain] Cd Length: 869 Bit Score: 586.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 51 FDNGISAEQLIEARTEFIDQLLQRLWIEAgFSQIADLALVAVGGYGRGELHPLSDIDLLILSRKKLPDDQAQKVGELLTL 130
Cdd:PRK04374 38 FDQGEPIERLLALRARAVDQLMRNAWTRC-IPADSGLSLHAVGGYGRGELFPRSDVDLLVLGETAAQQRHEQALARLFAL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 131 LWDVKLEVGHSVRTLEECMlEGLSDLTVATNLIESRLLIGDVALFLELQKHIFSEGFWPSDKFYAAKVEEQNQRHQRYHG 210
Cdd:PRK04374 117 LWDVGLPISHAVRSPAQCT-AAAADQTVLTALIESRPLVADAAARAALAAAIAPQQVWPPRAFFQAKREELLARHQRFGD 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 211 TSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSLDEMVGFGFLTSAERAELNECLHILWRIRFALHLVVSRYDNRLLFD 290
Cdd:PRK04374 196 TADNLEPDIKDGPGGLRDLQTLGWMALRAFGVKDLEALVGLGHVGCDEAAALRREREELARLRFGLHLVANRPEERLRFD 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 291 RQLSVAQRLNYSGEG-NEPVERMMKDYFRVTRRVSELNQMLLQLFDEAilaLPADEKPRPIDDEFQLRGTLIDLRDETLF 369
Cdd:PRK04374 276 YQKTLAERLGFADDPeSLGVEKMMQRFYRSAALIRRISDRLLQRFEEQ---FDGEATPEPLGGGFSLRRGYLAADADSWP 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 370 MRQPEAILRMFYTMVRNSAITGIYSTTLRQLRHARRHLQQPLCNIPQARKLFLSILRHPGAVRRgLLPMHRHSVLGAYMP 449
Cdd:PRK04374 353 DGDVLQVFALFAQWAAHREVRGLHSLTARALAEVLRDLPAYDVADATARERFMALLRGPRAVET-LNRMARLGVLGQWIP 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 450 QWSHIVGQMQFDLFHAYTVDEHTIRVMLKLESFASEETRQRHPLCVNVWPRLPSTELIFIAALFHDIAKGRGGDHSILGA 529
Cdd:PRK04374 432 AFASVSGRMQFDLFHVYTVDQHTLMVLRNIALFAAGRADERFSIAHEVWPRLRKPELLLLAGLFHDIAKGRGGDHSELGA 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 530 QDVVHFAELHGLNSRETQLVAWLVRQHLLMSVTAQRRDIQDPEVIKQFAEEVQTENRLRYLVCLTVADICATNETLWNSW 609
Cdd:PRK04374 512 VDARAFCLAHRLSEGDTELVTWLVEQHLRMSVTAQKQDISDPEVIHRFATLVGTRERLDYLYLLTCADIAGTSPKLWNAW 591
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 610 KQSLLRELYFATEKQLRRGMQNTPDMRERVRHHQLQALALLRMDNIDEEVLHQIWSRCRANYFVRHSPNQLAWHARHLLQ 689
Cdd:PRK04374 592 KDRLLADLYFAARRALREGLEHPPPREERLREARESARALMQAQGHDDATIDRQFAGMPDENFLRFRPEQLAWQAASLIE 671
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 690 HDLSKPLVLLSPQAT-RGGTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDGMAMDTFIVLEPD----GSP--L 762
Cdd:PRK04374 672 VEIGQTLVKARRAVPdNDALEVFVYSPDRDGLFAAIVATLDRKGYGIHRARVLDAPHDAIFDVFEVLPQDtyadGDPqrL 751
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 763 SADRHEVIRFGLEQVltqsswqPPQPRRQPAKLRHFTVETEVTFLPTHTDRKSFLELIALDQPGLLARVGKIFADLGISL 842
Cdd:PRK04374 752 AAALRQVLAGDLQKV-------RPARRAVPRQLRHFRFAPRVEFSESAGGRRTRISLVAPDRPGLLADVAHVLRMQHLRV 824
|
810 820 830 840
....*....|....*....|....*....|....*....|....*
gi 15829423 843 HGARITTIGERVEDLFIIATADRRALNNELQQEVHQRLTEALNPN 887
Cdd:PRK04374 825 HDARIATFGERAEDQFQITDEHDRPLSESARQALRDALCACLDPV 869
|
|
| PRK03381 |
PRK03381 |
PII uridylyl-transferase; Provisional |
52-868 |
7.11e-83 |
|
PII uridylyl-transferase; Provisional
Pssm-ID: 235123 [Multi-domain] Cd Length: 774 Bit Score: 283.04 E-value: 7.11e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 52 DNGISAEQLIEARTEFIDQLLQRLWIEAGFSQIADLALVAVGGYGRGELHPLSDIDLLILSRKKLPDDQAQKVGELLTLL 131
Cdd:PRK03381 23 GGHLDGAALRAALADLHEFWLAGLAAEAGIADGSGVALVAVGGLGRRELLPYSDLDLVLLHDGRPADDVAEVADRLWYPL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 132 WDVKLEVGHSVRTLEECMLEGLSDLTVATNLIESRLLIGDVALFLELQKHIFSEgfWPSD--KFYAAKVEEQNQRHQRYH 209
Cdd:PRK03381 103 WDAGIRLDHSVRTVPEALKVAGSDLKAALGLLDARHIAGDADLSALLIGGVRRQ--WRNGarRRLPELVELTRARWERSG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 210 GTSYNLEPDIKSSPGGLRDIHTLQWVARRHfgatsldemvgfgfLTSAERAELNECLHILWRIRFALHLVVSRYDNRLLF 289
Cdd:PRK03381 181 EIAHLAEPDLKEGRGGLRDVQLLRALAAAQ--------------LADAPGGGLDAAHRRLLDVRTELHRVSGRGRDRLLA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 290 DRQLSVAQRLNYSgegnepvermmkDYFRVTRRVSELNQMLLQLFD----EAILALP------ADEKP--RPIDD----- 352
Cdd:PRK03381 247 QEADEVAAALGLG------------DRFDLARALSDAARTISYAVDvgwrTAANALPrrglsaLRRRPvrRPLDEgvveh 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 353 --EFQLRGTLIDLRDETLFMRQPEAilrmfytmvrnSAITG--IYSTTLRQLRHARRHLQQPLcnIPQARKLFLSILrhp 428
Cdd:PRK03381 315 agEVVLARDARPARDPGLVLRVAAA-----------AATTGlpIAAATLSRLAASAPPLPTPW--PAEARDDLLVLL--- 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 429 gAVRRGLLP----MHRHSVLGAYMPQWSHIVGQMQFDLFHAYTVDEHTIRVMlkleSFASEETRqrhplcvnvwpRLPST 504
Cdd:PRK03381 379 -GAGPAAVAvieaLDRTGLWGRLLPEWEAVRDLPPRDPVHRWTVDRHLVETA----VRAAALTR-----------RVARP 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 505 ELIFIAALFHDIAKGRGGDHSILGAQDVVHFAELHGLNSRETQLVAWLVRQHLLMSVTAQRRDIQDPEVIKQFAEEVQTE 584
Cdd:PRK03381 443 DLLLLGALLHDIGKGRGGDHSVVGAELARQIGARLGLSPADVALLSALVRHHLLLPETATRRDLDDPATIEAVAEALGGD 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 585 NR-LRYLVCLTVADICATNETLWNSWKQSLLRELYfatekqlrrgmqntpdmrERVRhhqlqalALLRMDNIDEevlhqi 663
Cdd:PRK03381 523 PVlLELLHALTEADSLATGPGVWSDWKASLVGDLV------------------RRCR-------AVLAGEPLPE------ 571
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 664 wsrcranyfvrhsPNQLAWHARHLLQHDlsKPLVLLSPqATRGGTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTT 743
Cdd:PRK03381 572 -------------PEPLDPAQLALAADG--GVHVEIAP-ADPHMVEVTVVAPDRRGLLSKAAGVLALHRLRVRSASVRSH 635
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 744 rDGMAMDTFIVLEPDGSPLSAD--RHEVIR-----FGLEQVLTQSSWQPPQPRRQPAklrhfTVETEVTFLPTHTDRKSF 816
Cdd:PRK03381 636 -DGVAVLEFVVSPRFGSPPDAAllRQDLRRaldgdLDVLARLAAREAAAAAVPVRRP-----AAPPRVLWLDGASPDATV 709
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|..
gi 15829423 817 LELIALDQPGLLARVGKIFADLGISLHGARITTIGERVEDLFIIATADRRAL 868
Cdd:PRK03381 710 LEVRAADRPGLLARLARALERAGVDVRWARVATLGADVVDVFYVTGAAGGPL 761
|
|
| GlnD_UR_UTase |
pfam08335 |
GlnD PII-uridylyltransferase; This is a family of bifunctional uridylyl-removing enzymes ... |
192-331 |
7.17e-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: 175.08 E-value: 7.17e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 192 KFYAAKVEEQNQRHQRYHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSLDEMVGFGFLTSAERAELNECLHILWR 271
Cdd:pfam08335 1 RFMKAKIEEQVARHGRYGDTAYNLEPNIKLGPGGLRDIEFIVWIAQLIFTLRALEELVELGLLTREEARELRRAYRFLRR 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 272 IRFALHLVVSRYDNRLLFDRQLSVAQRLNYSGEGNEPVERMMKDYFRVTRRVSELNQMLL 331
Cdd:pfam08335 81 VRHRLHLLADRQTDRLPFDLQRRLARALGYARDGWLAVERFMRRLFRHAHRVSRLFEILL 140
|
|
| glnD |
PRK00227 |
[protein-PII] uridylyltransferase; |
56-635 |
6.51e-36 |
|
[protein-PII] uridylyltransferase;
Pssm-ID: 178937 [Multi-domain] Cd Length: 693 Bit Score: 145.68 E-value: 6.51e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 56 SAEQLIEARTEFIDQLLQRLWIEAGFsqiadlALVAVGGYGRGELHPLSDIDLLILSrkklPDDQAQKVGE-LLTLLWDV 134
Cdd:PRK00227 3 TPAQLREDAEASALALLGSLQLPPGT------ALAATGSLARREMTPYSDLDLILLH----PPGATPDGVEdLWYPIWDA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 135 KLEVGHSVRTLEECMLEGLSDLTVATNLIESRLLIGDVALFLELQKHIFSEgfWPSD--KFYAAKVEEQNQRHQRYHGTS 212
Cdd:PRK00227 73 KKRLDYSVRTPQECAAMISADSTAALALLDLRFVAGDEQLTASTRAKILEK--WRRElnKNFDAVVDTAIARWRRSGSVV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 213 YNLEPDIKSSPGGLRDIHTLQWVARRHF-GATSLDEmvgfgfltsaERAelneclhILWRIRFALHLVVSRYDNRLLFDR 291
Cdd:PRK00227 151 AMTRPDLKHGRGGLRDIELIRALALGHLcDAPPLDS----------QHQ-------LLLDVRTLLHVHARRARDVLDPEF 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 292 QLSVAQRLNYSgegnepvermmkDYFRVTRRVSE----LNQMLLQLFDEAILALP---ADEKP--RPID-DEFQLRGTL- 360
Cdd:PRK00227 214 AVDIALDLGFV------------DRYHLSREIADaaraIDDALTAALATARGALPrrtAFRNAvrRPLDvDVVDANGTIa 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 361 ----IDLRDETLFMRQPEAilrmfytmvrnSAITG--IYSTTLRQLRHARRhLQQPLcnIPQARKLFLSILRHPGAVRRG 434
Cdd:PRK00227 282 lsrtPDLDDPALPLRVAAA-----------AARTGlpVSESVWKRLEECPE-LPEPW--PASAAGDFFRLLSSPVNSRRV 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 435 LLPMHRHSVLGAYMPQWSHIVGQMQFDLFHAYTVDEHTIRVMLKlesfASEETrqrhplcvnvwPRLPSTELIFIAALFH 514
Cdd:PRK00227 348 IKQMDRHGLWERIVPEWDRIRGLMPREPSHIHTIDEHSLNTVAN----CALET-----------VTVARPDLLLLGALYH 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 515 DIAKGRGGDHSILGAQDVVHFAELHGLNSRETQLVAWLVRQHLLMSVTAQRRDIQDPEVIKQFAEEVQTEN-RLRYLVCL 593
Cdd:PRK00227 413 DIGKGYPRPHEQVGAEMVARAARRMGLNLRDRAVVQTLVAEHTTLARIAGRLDPTSEEAVDKLLDAVRYDLlTLNLLEVL 492
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 15829423 594 TVADICATNETLWNSWKQSLLRELYFATEKQLRRGMQNTPDM 635
Cdd:PRK00227 493 TEADAEGTGPGVWTARLEQGLRIVCSRARARLTDIRPVAPMF 534
|
|
| ACT_UUR-like_1 |
cd04900 |
ACT domain family, ACT_UUR-like_1, includes the first of two C-terminal ACT domains of the ... |
707-778 |
1.10e-28 |
|
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: 109.49 E-value: 1.10e-28
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15829423 707 GTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDGMAMDTFIVLEPDGSPLSA-DRHEVIRFGLEQVL 778
Cdd:cd04900 1 GTEVFIYTPDRPGLFARIAGALDQLGLNILDARIFTTRDGYALDTFVVLDPDGEPIGErERLARIREALEDAL 73
|
|
| NT_GlnE_GlnD_like |
cd05401 |
Nucleotidyltransferase (NT) domain of Escherichia coli adenylyltransferase (GlnE), Escherichia ... |
51-183 |
9.23e-25 |
|
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: 101.65 E-value: 9.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 51 FDNGISAEQLIEARTEFIDQLLQRLWIEAG-----FSQIADLALVAVGGYGRGELHPLSDIDLLILSRKKLPDDQ----- 120
Cdd:cd05401 15 LLGGASIRAISRALSDLADALLRRALELALaelgkGPPPVPFALLALGSYGRGELNPSSDQDLLLLYDDDGDEVAayfee 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15829423 121 -AQKVGELLTL------LWDVKLEVGHSVRTLEECMLEGLSDLTV------ATNLIESRLLIGDVALFLELQKHIF 183
Cdd:cd05401 95 lAERLIKILSEaggpycLGDVMLRPPGWRRSLAEWLDAARDWLTEpgrlweRTALLDARPVAGDRALAEELRRRIR 170
|
|
| ACT_ACR-UUR-like_2 |
cd04899 |
C-terminal ACT domains of the bacterial signal-transducing uridylyltransferase ... |
817-884 |
4.69e-24 |
|
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: 95.98 E-value: 4.69e-24
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15829423 817 LELIALDQPGLLARVGKIFADLGISLHGARITTIGERVEDLFIIATADRRALNNELQQEVHQRLTEAL 884
Cdd:cd04899 3 LELTALDRPGLLADVTRVLAELGLNIHSAKIATLGERAEDVFYVTDADGQPLDPERQEALRAALGEAL 70
|
|
| ACT_UUR-ACR-like |
cd04873 |
ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) ... |
817-884 |
2.43e-19 |
|
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: 82.60 E-value: 2.43e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15829423 817 LELIALDQPGLLARVGKIFADLGISLHGARITTIGERVEDLFIIATADRRALNNELQQEVHQRLTEAL 884
Cdd:cd04873 3 VEVYAPDRPGLLADITRVLADLGLNIHDARISTTGERALDVFYVTDSDGRPLDPERIARLEEALEDAL 70
|
|
| ACT_UUR-ACR-like |
cd04873 |
ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) ... |
708-778 |
5.46e-19 |
|
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: 81.83 E-value: 5.46e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15829423 708 TEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDgMAMDTFIVLEPDGSPLSADRHEVIRFGLEQVL 778
Cdd:cd04873 1 TVVEVYAPDRPGLLADITRVLADLGLNIHDARISTTGE-RALDVFYVTDSDGRPLDPERIARLEEALEDAL 70
|
|
| HD |
pfam01966 |
HD domain; HD domains are metal dependent phosphohydrolases. |
468-574 |
1.30e-08 |
|
HD domain; HD domains are metal dependent phosphohydrolases.
Pssm-ID: 460398 [Multi-domain] Cd Length: 110 Bit Score: 53.39 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 468 VDEHTIRVMLKLESFASEETRqrhplcVNVwprlpstELIFIAALFHDIAKGRGGD----------HSILGAQDVVHFAE 537
Cdd:pfam01966 1 RLEHSLRVALLARELAEELGE------LDR-------ELLLLAALLHDIGKGPFGDekpefeiflgHAVVGAEILRELEK 67
|
90 100 110
....*....|....*....|....*....|....*..
gi 15829423 538 LHGLnsretQLVAWLVRQHLLMSVTAQRRDIQDPEVI 574
Cdd:pfam01966 68 RLGL-----EDVLKLILEHHESWEGAGYPEEISLEAR 99
|
|
| HDc |
smart00471 |
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ... |
464-611 |
2.91e-08 |
|
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: 53.07 E-value: 2.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 464 HAYTVDEHTIRVMLKLESFASEEtrqrhplcvnvwpRLPSTELIFIAALFHDIAKGRGGD-----------HSILGAQDV 532
Cdd:smart00471 1 SDYHVFEHSLRVAQLAAALAEEL-------------GLLDIELLLLAALLHDIGKPGTPDsflvktsvledHHFIGAEIL 67
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15829423 533 VHFAElhglNSRETQLVAWLVRQHLLMSVTaqrrdiqdpevikqfaeeVQTENRLRYLVCLTVADICATNETLWNSWKQ 611
Cdd:smart00471 68 LEEEE----PRILEEILRTAILSHHERPDG------------------LRGEPITLEARIVKVADRLDALRADRRYRRV 124
|
|
| ACT_ACR-UUR-like_2 |
cd04899 |
C-terminal ACT domains of the bacterial signal-transducing uridylyltransferase ... |
708-778 |
1.25e-07 |
|
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: 49.37 E-value: 1.25e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15829423 708 TEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIfTTRDGMAMDTFIVLEPDGSPLSADRHEVIRFGLEQVL 778
Cdd:cd04899 1 TVLELTALDRPGLLADVTRVLAELGLNIHSAKI-ATLGERAEDVFYVTDADGQPLDPERQEALRAALGEAL 70
|
|
| ACT |
pfam01842 |
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ... |
817-874 |
1.44e-07 |
|
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: 49.23 E-value: 1.44e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 15829423 817 LELIALDQPGLLARVGKIFADLGISLHGARITTIGERVEDLFIIATADRRALNNELQQ 874
Cdd:pfam01842 3 LEVLVPDRPGLLARVLGALADRGINITSIEQGTSEDKGGIVFVVIVVDEEDLEEVLEA 60
|
|
| NTP_transf_2 |
pfam01909 |
Nucleotidyltransferase domain; Members of this family belong to a large family of ... |
86-150 |
1.04e-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: 47.41 E-value: 1.04e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15829423 86 DLALVAVGGYGRGELHPLSDIDLLILSRKKLPDDQAQK-------VGELLTLLWDV----KLEVGHSVRTLEECML 150
Cdd:pfam01909 14 VAEVVLFGSYARGTALPGSDIDLLVVFPEPVEEERLLKlakiikeLEELLGLEVDLvtreKIEFPLVKIDILEERI 89
|
|
| HDc |
cd00077 |
Metal dependent phosphohydrolases with conserved 'HD' motif |
466-618 |
1.36e-06 |
|
Metal dependent phosphohydrolases with conserved 'HD' motif
Pssm-ID: 238032 [Multi-domain] Cd Length: 145 Bit Score: 48.87 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 466 YTVDEHTIRVMLKLESFASEETRQRhplcvnvwprlPSTELIFIAALFHDIAKG------------RGGDHSILGAQDVV 533
Cdd:cd00077 1 EHRFEHSLRVAQLARRLAEELGLSE-----------EDIELLRLAALLHDIGKPgtpdaiteeeseLEKDHAIVGAEILR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829423 534 HFaelhgLNSRETQLVAWLVRQHLLMsvTAQRRDIQDPEVIKqfaeevQTENRLRYLVCLTVADIC-ATNETLWNSWKQS 612
Cdd:cd00077 70 EL-----LLEEVIKLIDELILAVDAS--HHERLDGLGYPDGL------KGEEITLEARIVKLADRLdALRRDSREKRRRI 136
|
....*.
gi 15829423 613 LLRELY 618
Cdd:cd00077 137 AEEDLE 142
|
|
| ACT |
cd02116 |
ACT domains are commonly involved in specifically binding an amino acid or other small ligand ... |
817-877 |
9.90e-06 |
|
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: 43.82 E-value: 9.90e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15829423 817 LELIALDQPGLLARVGKIFADLGISLHGARITTIGERVEDLFIIATADRRALnNELQQEVH 877
Cdd:cd02116 1 LTVSGPDRPGLLAKVLSVLAEAGINITSIEQRTSGDGGEADIFIVVDGDGDL-EKLLEALE 60
|
|
| ACT |
cd02116 |
ACT domains are commonly involved in specifically binding an amino acid or other small ligand ... |
710-759 |
1.67e-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: 43.05 E-value: 1.67e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 15829423 710 IFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDGMAMDTFIVLEPDG 759
Cdd:cd02116 1 LTVSGPDRPGLLAKVLSVLAEAGINITSIEQRTSGDGGEADIFIVVDGDG 50
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| MJ0604 |
COG1708 |
Predicted nucleotidyltransferase, MJ0604 family [General function prediction only]; |
68-131 |
3.51e-05 |
|
Predicted nucleotidyltransferase, MJ0604 family [General function prediction only];
Pssm-ID: 441314 Cd Length: 95 Bit Score: 43.48 E-value: 3.51e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15829423 68 IDQLLQRLwIEAGFSQIADLALVAVGGYGRGELHPLSDIDLLILSRK-KLPDDQAQKVGELLTLL 131
Cdd:COG1708 5 LRELLEEI-VEALRRGPEVAAVYLFGSYARGDARPDSDIDLLVVVDDpPLPDERLELLADLLREL 68
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| ACT_UUR-like_1 |
cd04900 |
ACT domain family, ACT_UUR-like_1, includes the first of two C-terminal ACT domains of the ... |
823-884 |
1.13e-04 |
|
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: 41.31 E-value: 1.13e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15829423 823 DQPGLLARVGKIFADLGISLHGARI-TTIGERVEDLFIIATADRRALNN-ELQQEVHQRLTEAL 884
Cdd:cd04900 10 DRPGLFARIAGALDQLGLNILDARIfTTRDGYALDTFVVLDPDGEPIGErERLARIREALEDAL 73
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| NT_KNTase_like |
cd05403 |
Nucleotidyltransferase (NT) domain of Staphylococcus aureus kanamycin nucleotidyltransferase, ... |
69-138 |
5.97e-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: 39.71 E-value: 5.97e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15829423 69 DQLLQRL--WIEAGFSQIADLALVavGGYGRGELHPLSDIDLLILSRKKLPDDQAQKVGELLTLLWDVKLEV 138
Cdd:cd05403 1 EEILEEIleILRELLGGVEKVYLF--GSYARGDARPDSDIDLLVIFDDPLDPLELARLLEELELLLGRPVDL 70
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| ACT_ACR_4 |
cd04926 |
C-terminal ACT domain, of a novel type of ACT domain-containing protein which is composed ... |
817-883 |
7.46e-04 |
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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: 38.87 E-value: 7.46e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15829423 817 LELIALDQPGLLARVGKIFADLGISLHGARITTIGERVEDLFIIATADRRALNNELQQEVHQRLTEA 883
Cdd:cd04926 4 LELRTEDRVGLLSDVTRVFRENGLTVTRAEISTQGDMAVNVFYVTDANGNPVDPKTIEAVRQEIGPA 70
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| ACT_ACR_4 |
cd04926 |
C-terminal ACT domain, of a novel type of ACT domain-containing protein which is composed ... |
707-771 |
9.35e-04 |
|
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: 38.49 E-value: 9.35e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15829423 707 GTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIfTTRDGMAMDTFIVLEPDGSPLSADRHEVIR 771
Cdd:cd04926 1 GVRLELRTEDRVGLLSDVTRVFRENGLTVTRAEI-STQGDMAVNVFYVTDANGNPVDPKTIEAVR 64
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| ACT_TyrKc |
cd04928 |
Uncharacterized, N-terminal ACT domain of an Arabidopsis/Oryza predicted tyrosine kinase and ... |
709-754 |
2.56e-03 |
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Uncharacterized, N-terminal ACT domain of an Arabidopsis/Oryza predicted tyrosine kinase and other related ACT domains; This CD includes a novel, yet uncharacterized, N-terminal ACT domain of an Arabidopsis/Oryza predicted tyrosine kinase and other related ACT domains. Members of this CD belong to the superfamily of ACT regulatory domains.
Pssm-ID: 153200 Cd Length: 68 Bit Score: 37.15 E-value: 2.56e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 15829423 709 EIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDGMAMDTFIV 754
Cdd:cd04928 3 EITFAAGDKPKLLSQLSSLLGDLGLNIAEAHAFSTDDGLALDIFVV 48
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| ACT_HSDH-Hom |
cd04881 |
ACT_HSDH_Hom CD includes the C-terminal ACT domain of the NAD(P)H-dependent, homoserine ... |
816-843 |
2.98e-03 |
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ACT_HSDH_Hom CD includes the C-terminal ACT domain of the NAD(P)H-dependent, homoserine dehydrogenase (HSDH) and related domains; The ACT_HSDH_Hom CD includes the C-terminal ACT domain of the NAD(P)H-dependent, homoserine dehydrogenase (HSDH) encoded by the hom gene of Bacillus subtilis and other related sequences. HSDH reduces aspartate semi-aldehyde to the amino acid homoserine, one that is required for the biosynthesis of Met, Thr, and Ile from Asp. Neither the enzyme nor the aspartate pathway is found in the animal kingdom. This mostly bacterial HSDH group has a C-terminal ACT domain and is believed to be involved in enzyme regulation. A C-terminal deletion in the Corynebacterium glutamicum HSDH abolished allosteric inhibition by L-threonine. Members of this CD belong to the superfamily of ACT regulatory domains.
Pssm-ID: 153153 [Multi-domain] Cd Length: 79 Bit Score: 37.50 E-value: 2.98e-03
10 20
....*....|....*....|....*...
gi 15829423 816 FLELIALDQPGLLARVGKIFADLGISLH 843
Cdd:cd04881 2 YLRLTVKDKPGVLAKITGILAEHGISIE 29
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| ACT_ACR_2 |
cd04925 |
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats ... |
817-854 |
6.19e-03 |
|
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: 36.25 E-value: 6.19e-03
10 20 30
....*....|....*....|....*....|....*...
gi 15829423 817 LELIALDQPGLLARVGKIFADLGISLHGARITTIGERV 854
Cdd:cd04925 3 IELTGTDRPGLLSEVFAVLADLHCNVVEARAWTHNGRL 40
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| Polbeta |
pfam18765 |
Polymerase beta, Nucleotidyltransferase; A member of the nucleotidyltransferase fold found in ... |
93-120 |
7.75e-03 |
|
Polymerase beta, Nucleotidyltransferase; A member of the nucleotidyltransferase fold found in polymorphic toxins (NTox45) and polyvalent proteins.
Pssm-ID: 465859 Cd Length: 93 Bit Score: 36.74 E-value: 7.75e-03
10 20
....*....|....*....|....*...
gi 15829423 93 GGYGRGELHPLSDIDLLILSRKKLPDDQ 120
Cdd:pfam18765 20 GSRAKGDAREDSDIDLAVLYDEKLDFEE 47
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