|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05007 |
PRK05007 |
bifunctional uridylyltransferase/uridylyl-removing protein GlnD; |
8-891 |
0e+00 |
|
bifunctional uridylyltransferase/uridylyl-removing protein GlnD;
Pssm-ID: 235329 [Multi-domain] Cd Length: 884 Bit Score: 1831.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 8 QYANTALASLPGLPAQPATWPQDALHCAAIKQHLDDFQRWLGVAFDSGVSAEDLVEARTEFIDQLLQRLWLHYGFGDTEE 87
Cdd:PRK05007 1 QYANTALPTLPGQPQSPLTWPDDELTVGGLKQHLDTFQQWLGDAFDAGISAEQLVEARTEFIDQLLQRLWIEAGFDQIPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 88 TALVAVGGYGRGELHPLSDIDLLILSRKRLPDAQAQKVGELLTLLWDVKLEVGHSVRTLEECLLEGLSDLTVATNLIESR 167
Cdd:PRK05007 81 LALVAVGGYGRGELHPLSDIDLLILSRKKLPDEQAQKVGELITLLWDLKLEVGHSVRTLEECLLEGLSDLTVATNLIESR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 168 LLIGDVALFLELQKHIFSDGFWPSEKFFPAKVEEQNERHQRYHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSLR 247
Cdd:PRK05007 161 LLCGDVALFLELQKHIFSDGFWPSEKFYAAKVEEQNERHQRYHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSLD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 248 EMVGFGFLTEAERNELDECQHLLWRIRFALHLELNRYDNRLLFDRQLSVAQRLNYQGEGNEPVEQMMKDFYRVTRRVGEL 327
Cdd:PRK05007 241 EMVGFGFLTPAERAELNECQHFLWRIRFALHLVLSRYDNRLLFDRQLSVAQLLGYEGEGNEPVERMMKDYYRTTRRVSEL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 328 NQMLLQLFDEAILALSTDEKPRPLDDDFQLRGTLIDLRDETLFIREPQAILRMFYAMVRNRDITGIYSTTLRHLRHARRH 407
Cdd:PRK05007 321 NQMLLQLFDEAILALTADEKPRPIDDEFQLRGTLIDLRDETLFQRQPEAILRMFYLMARNSNITGIYSTTLRQLRHARRH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 408 LKQPLCYIPEARSLFLTMLRHPGAVSRGLVPMHRHSVLWAYMPQWSHIVGQMQFDLFHAYTVDEHTIRVLQKLESFSLEE 487
Cdd:PRK05007 401 LNQPLCEIPEARKLFMEILRHPGAVSRALLPMHRHSVLSAYMPQWSHIVGQMQFDLFHAYTVDEHTIRVLLKLESFADEE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 488 TRSKHPLCVDLWPRLSHPELILIAALFHDIAKGRGGDHSVLGAQDVLKFAELHGLNSRETQLVAWLVRQHLLMSVTAQRR 567
Cdd:PRK05007 481 TRQRHPLCVELYPRLPKKELLLLAALFHDIAKGRGGDHSILGAQDALEFAELHGLNSRETQLVAWLVRNHLLMSVTAQRR 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 568 DIQDPEVIKQFAEEVQTENRLRFLVCLTVADICATNETLWNSWKQSLLRELYFATEKQLRRGMQNTPDMRERVRHHQVQA 647
Cdd:PRK05007 561 DIQDPDVIKQFAEEVQDENRLRYLVCLTVADICATNETLWNSWKQSLLRELYFATEKQLRRGMENPPDMRERVRHHQLQA 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 648 LALLRMENINEEALHHIWARCRANYFVRHSPNQLAWHARHLLKHDLSQPLILLSPQATRGGTEIFIWSPDRPYLFAAVCA 727
Cdd:PRK05007 641 LALLRMDNIDEEALHQIWSRCRADYFLRHTPNQLAWHARHLLQHDLDKPLVLLSKQATRGGTEIFIWSPDRPYLFAAVCA 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 728 ELDRRNLSVHDAQIFTTRDGMAMDTFIVLEPDGSPLSADRHEAIRHGLEQAITQRTWQPPQPRRQPAKLRHFTVETEVNF 807
Cdd:PRK05007 721 ELDRRNLSVHDAQIFTSRDGMAMDTFIVLEPDGSPLSQDRHQVIRKALEQALTQSSPQPPKPRRLPAKLRHFNVPTEVSF 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 808 LPTHTERRSFLELIALDQPGLLARVGQVFADLGISLHGARITTIGERVEDLFIIATADRRALNNVLQQEVQQRLTAALNP 887
Cdd:PRK05007 801 LPTHTDRRSYMELIALDQPGLLARVGKIFADLGISLHGARITTIGERVEDLFILATADRRALNEELQQELRQRLTEALNP 880
|
....
gi 639221815 888 NDKG 891
Cdd:PRK05007 881 NDKG 884
|
|
| GlnD |
COG2844 |
UTP:GlnB (protein PII) uridylyltransferase [Posttranslational modification, protein turnover, ... |
31-890 |
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: 1260.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 31 ALHCAAIKQHLDDFQRWLGVAFDSGVSAEDLVEARTEFIDQLLQRLWLHYGFGDTEETALVAVGGYGRGELHPLSDIDLL 110
Cdd:COG2844 1 AAALAALREALAEGRAALRERFRAGADGRELVRARAALVDQLLRALWDLAGLTEPERLALVAVGGYGRGELAPHSDIDLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 111 ILSRKRLPDAQAQKVGELLTLLWDVKLEVGHSVRTLEECLLEGLSDLTVATNLIESRLLIGDVALFLELQKHIFSDGFWP 190
Cdd:COG2844 81 FLLPDKPTPALEEVIEAFLYLLWDLGLEVGHSVRTVDECLREAREDITVRTALLEARLLAGDEALFEELRERFRADVFWD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 191 SEKFFPAKVEEQNERHQRYHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSLREMVGFGFLTEAERNELDECQHLL 270
Cdd:COG2844 161 SRAFFEAKLAEQRERHAKYGDTRYNLEPNIKEGPGGLRDLQTLLWIAKRHFGVRSLEELVKKGLLTEEEYRELRRAEDFL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 271 WRIRFALHLELNRYDNRLLFDRQLSVAQRLNYQG-EGNEPVEQMMKDFYRVTRRVGELNQMLLQLFDEAILALSTDEKPR 349
Cdd:COG2844 241 WRVRFALHLLAGRAEDRLLFDLQREVAERLGYQDtEGNRAVERFMQRYYRTAKAVGRLNEILLQRLEEAILKPPGLRRPR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 350 PLDDDFQLRGTLIDLRDETLFIREPQAILRMFYAMVRNRDITGIYSTTLRHLRHARRHLKQPLCYIPEARSLFLTMLRHP 429
Cdd:COG2844 321 PINEGFQLRNGRLEVADPDVFERDPVALLRLFLLAAQHPEGLGIHPDTLRLLRRALRLIDDAFRRDPEARRLFLEILRQP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 430 GAVSRGLVPMHRHSVLWAYMPQWSHIVGQMQFDLFHAYTVDEHTIRVLQKLESFSLEETRSKHPLCVDLWPRLSHPELIL 509
Cdd:COG2844 401 RGITRALRRMNEYGVLGRYIPEFGRIVGQMQFDLFHVYTVDEHTLRVVRNLRRFERGELAEEFPLASELIAELPKPELLY 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 510 IAALFHDIAKGRGGDHSVLGAQDVLKFAELHGLNSRETQLVAWLVRQHLLMSVTAQRRDIQDPEVIKQFAEEVQTENRLR 589
Cdd:COG2844 481 LAALFHDIAKGRGGDHSELGAEDARRFCPRHGLSPEDTELVAWLVRHHLLMSHTAQRRDISDPEVIRDFARLVGSEERLD 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 590 FLVCLTVADICATNETLWNSWKQSLLRELYFATEKQLRRGMQnTPDMRERVRHHQVQALALLRMENINEEALHHIWARCR 669
Cdd:COG2844 561 YLYLLTVADIRATGPKVWNSWKASLLRELYRATLRALRGGLE-PPDREERIEERKEEALALLADQGWDEEEIEALWARLP 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 670 ANYFVRHSPNQLAWHARHLLKH-DLSQPLILLSPQATRGGTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDGM 748
Cdd:COG2844 640 DDYFLRHDPEEIAWHARLLLRAdDSGKPLVLIRPDPDRGGTEVFVYTPDRPGLFARIAGALAALGLNILDARIHTTRDGY 719
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 749 AMDTFIVLEPDGSPLS-ADRHEAIRHGLEQAITQRTWQP-PQPRRQPAKLRHFTVETEVNFLPTHTERRSFLELIALDQP 826
Cdd:COG2844 720 ALDTFIVLDPDGEPIDdPDRLERIEQALEEALSGEVPLPePLARRLSRRLRHFPVPPRVTFDNDASNRYTVLEVSALDRP 799
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 639221815 827 GLLARVGQVFADLGISLHGARITTIGERVEDLFIIATADRRALNN-VLQQEVQQRLTAALNPNDK 890
Cdd:COG2844 800 GLLYDIARVLADLGLNIHSAKIATLGERVEDVFYVTDLDGQKLTDpERQEALREALLEALDEEAE 864
|
|
| glnD |
PRK01759 |
bifunctional uridylyltransferase/uridylyl-removing protein GlnD; |
35-886 |
0e+00 |
|
bifunctional uridylyltransferase/uridylyl-removing protein GlnD;
Pssm-ID: 234980 [Multi-domain] Cd Length: 854 Bit Score: 1031.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 35 AAIKQHLDDFQRWLGVAFdSGVSAEDLVEARTEFIDQLLQRLWLHYGFGDTEETALVAVGGYGRGELHPLSDIDLLILSR 114
Cdd:PRK01759 5 SAVKIQKENLKQFELENF-SQEDVFELIENRSDFYDQLLIHLWQQFGLEEQSDLALIAVGGYGRREMFPLSDLDILILTE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 115 KRLPDAQAQKVGELLTLLWDVKLEVGHSVRTLEECLLEGLSDLTVATNLIESRLLIGDVALFLELQKHIFSDGFWPSEKF 194
Cdd:PRK01759 84 QPPDEETEEKINQFFQFLWDCGFEVGASVRTLAECESEGRADITIATNLLESRFLTGNEKLFDALVELLQQADFWSKEAF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 195 FPAKVEEQNERHQRYHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSLREMVGFGFLTEAERNELDECQHLLWRIR 274
Cdd:PRK01759 164 FQAKIQEKIERYQRYHNTSYNLEPDIKYSPGGLRDLHLLYWIALRHSGAKSLEEILQSGFIYPEEYAELQQSQQFLFKVR 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 275 FALHLELNRYDNRLLFDRQLSVAQRLNYQGEGNEPVEQMMKDFYRVTRRVGELNQMLLQLFDEAILALSTDEKPRPLDDD 354
Cdd:PRK01759 244 FALHLILKRYDNRLLFDRQLKVSELLGFQGEGNQGVEKMMKSFFQALQSISLLSDLLVKHYREHFLQPNQNVEIQPLDDD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 355 FQLRGTLIDLRDETLFIREPQAILRMFYAMVRNRDITgIYSTTLRHLRHARRHLKQPLCYIPEARSLFLTMLRHPGAVSR 434
Cdd:PRK01759 324 FYLINNAICLRNPDCFEQQPESILDLFFYLTQYPQAE-IHSTTLRQLRLALEQLQQPLCELPAARERFLRLFNQPNAIKR 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 435 GLVPMHRHSVLWAYMPQWSHIVGQMQFDLFHAYTVDEHTIRVLQKLESFSLEETRSKHPLCVDLWPRLSHPELILIAALF 514
Cdd:PRK01759 403 ALVPMHQYGVLTAYLPQWKGIVGLMQFDLFHIYTVDEHTLRVMLKLESFLDEESAEQHPICHQIFSQLSDRTLLYIAALF 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 515 HDIAKGRGGDHSVLGAQDVLKFAELHGLNSRETQLVAWLVRQHLLMSVTAQRRDIQDPEVIKQFAEEVQTENRLRFLVCL 594
Cdd:PRK01759 483 HDIAKGRGGDHAELGAVDMRQFAQQHGFDQREIETMAWLVQQHLLMSVTAQRRDIHDPEVVMNFAEEVQNQVRLDYLTCL 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 595 TVADICATNETLWNSWKQSLLRELYFATEKQLRRGMQNTPDMRERVRHHQVQALALLRMENINEEALH--HIWARCRANY 672
Cdd:PRK01759 563 TVADICATNETLWNSWKRSLFATLYQFTNQQFQQGMDELLDYQEKAEENRQQALELLQQKYSALSETQieQLWQRCPEDY 642
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 673 FVRHSPNQLAWHARHLLKhDLSQPLILLSPQATRGGTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDGMAMDT 752
Cdd:PRK01759 643 FLRNTPKQIAWHALLLLD-FRGDLLVKISNRFSRGGTEIFIYCQDQANLFLKVVSTIGAKKLSIHDAQIITSQDGYVLDS 721
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 753 FIVLEPDGSPLSADRHEAIRHGLEQAITQRTWQPPQPRRQPaKLRHFTVETEVNFLPTHTERRSFLELIALDQPGLLARV 832
Cdd:PRK01759 722 FIVTELNGKLLEFDRRRQLEQALTKALNTNKLKKLNLEENH-KLQHFHVKTEVRFLNEEKQEQTEMELFALDRAGLLAQV 800
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....
gi 639221815 833 GQVFADLGISLHGARITTIGERVEDLFIIATADRRALNNVLQQEVQQRLTAALN 886
Cdd:PRK01759 801 SQVFSELNLNLLNAKITTIGEKAEDFFILTNQQGQALDEEERKALKSRLLSNLS 854
|
|
| UTase_glnD |
TIGR01693 |
[Protein-PII] uridylyltransferase; This model describes GlnD, the uridylyltransferase ... |
52-885 |
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: 927.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 52 FDSGVSAEDLVEARTEFIDQLLQRLWLHYGFGDTEETALVAVGGYGRGELHPLSDIDLLILSRKRLPDAQAQKVGELLTL 131
Cdd:TIGR01693 8 FARGGDGRELREGRSDLTDLLLIRLWDFIGISEHSGIALVAVGGYGRGELAPYSDIDLLFLHDGKPAEEVEPKIERFLYP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 132 LWDVKLEVGHSVRTLEECLLEGLSDLTVATNLIESRLLIGDVALFLELQKHIFSDGFWPS-EKFFPAKVEEQNERHQRYH 210
Cdd:TIGR01693 88 LWDLGFEVGHSVRTLEECARIAKADLTVATNLLEARHLAGDEALFFRLKERVRREDWRNTaRSFLAAKVEEQDERHARYG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 211 GTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSLREMVGFGFLTEAERNELDECQHLLWRIRFALHLELNRYDNRLLF 290
Cdd:TIGR01693 168 DTAYNLEPDIKEGPGGLRDLHTLFWVALYQLGVRRLEDLVKQGFLTDAEYKLLAEARDFLWDVRFALHLTTGRADDRLLF 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 291 DRQLSVAQRLNYQGEGNEPVEQMMKDFYRVTRRVGELNQMLLQLFDEAIL-----ALSTDEKPRPLDDDFQLRGTLIDLR 365
Cdd:TIGR01693 248 DHQDEIAAALGYGDEGNPAVERFMRRYFQAARRIGYLTEAFLRHYEEALLsrgpsARVRRPKRRPLDEGFVEDGGELVLA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 366 DETLFIREPQAILRMFYAMVRNRDitGIYSTTLRHLRHARRHLKQPLCYIPEARSLFLTMLRHPGAVSRGLVPMHRHSVL 445
Cdd:TIGR01693 328 RTAVFERDPALLLRLFAIAAQRGL--PIHPAALRQLTASLPLLPTPLREDPEARELFLELLTSGNGTVRALRAMNRAGVL 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 446 WAYMPQWSHIVGQMQFDLFHAYTVDEHTIRVLQKLESFSLEETRSKHPLCVDLWPRLSHPELILIAALFHDIAKGRGGDH 525
Cdd:TIGR01693 406 GRFLPEWGRIVGQMQFDLFHVYTVDEHTLRTVVHLAPFARGRLAREHPLASELMPKIEDPELLYLAALLHDIGKGRGGDH 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 526 SVLGAQDVLKFAELHGLNSRETQLVAWLVRQHLLMSVTAQRRDIQDPEVIKQFAEEVQTENRLRFLVCLTVADICATNET 605
Cdd:TIGR01693 486 SVLGAEDARDVCPRLGLDRPDTELVAWLVRNHLLMSITAQRRDLNDPKTVFAFAEAVGDPERLEYLLALTVADIRATGPG 565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 606 LWNSWKQSLLRELYFATEKQLRRGMQNTPDMRERVRHHQVQALALLRMEnINEEALHHIWARCRANYFVRHSPNQLAWHA 685
Cdd:TIGR01693 566 VWNSWKASLLRDLYNRTEQVLRGGLEPPADPAEPIAEQRKLAVALLRTD-YTSNEAEVLWLRAYDDYFLRFTHKEIAWHA 644
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 686 RHLLKHDLS-QPLILLSPQATRGGTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDGMAMDTFIVLEPDGSPLS 764
Cdd:TIGR01693 645 ESLRRALSSgGPLALIDGTRPSGGTEVFIYAPDQPGLFAKVAGALAMLSLSVHDAQVNTTKDGVALDTFVVQDLFGSPPA 724
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 765 ADR-HEAIRHGLEQAITQRTWQPPQP---RRQPAKLRHFTVETEVNFLPTHTERRSFLELIALDQPGLLARVGQVFADLG 840
Cdd:TIGR01693 725 AERvFQELLQGLVDVLAGLAKDPDTIsarRARRRRLQHFAVPPRVTILNTASRKATIMEVRALDRPGLLARVGRTLEELG 804
|
810 820 830 840
....*....|....*....|....*....|....*....|....*
gi 639221815 841 ISLHGARITTIGERVEDLFIIATADRRALNNVLQQEVQQRLTAAL 885
Cdd:TIGR01693 805 LSIQSAKITTFGEKAEDVFYVTDLFGLKLTDEEEQRLLEVLAASV 849
|
|
| glnD |
PRK00275 |
PII uridylyl-transferase; Provisional |
6-881 |
0e+00 |
|
PII uridylyl-transferase; Provisional
Pssm-ID: 234709 [Multi-domain] Cd Length: 895 Bit Score: 887.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 6 PEQYANTALASLPGLPAQPATWPQDALHCAaiKQHLDDfqrwlgvAFDSGVSAEDLVEARTEFIDQLLQRLWLHYGFGDT 85
Cdd:PRK00275 6 PELFDRGQFQAELALKASPIAAFKKAIRQA--REVLDE-------RFRSGRDIRRLIEDRAWFVDQILQQAWHQFDWSDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 86 EETALVAVGGYGRGELHPLSDIDLLILSRKRLPDAQAQKVGELLTLLWDVKLEVGHSVRTLEECLLEGLSDLTVATNLIE 165
Cdd:PRK00275 77 ADIALVAVGGYGRGELHPYSDIDLLILLDSADHEEFREPIERFLTLLWDIGLEIGQSVRSVDECAEEARADLTVITNLME 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 166 SRLLIGDVALFLELQKHIFSDGFWPSEKFFPAKVEEQNERHQRYHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATS 245
Cdd:PRK00275 157 SRTIAGPESLRQRMLEVTSSEHMWPSKEFFLAKRAEQKARHHKYNDTEYNLEPNVKGSPGGLRDIQTILWVAKRQFGTLN 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 246 LREMVGFGFLTEAERNELDECQHLLWRIRFALHLELNRYDNRLLFDRQLSVAQRLNYQGEG-NEPVEQMMKDFYRVTRRV 324
Cdd:PRK00275 237 LHALVGEGFLTESEYGLLASGQEFLWKVRYALHMLAGRAEDRLLFDHQRSIATLLGYEDSDaKLAVEQFMQKYYRVVMAL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 325 GELNQMLLQLFDEAILALSTDEKPRPLDDDFQLRGTLIDLRDETLFIREPQAILRMFYAMVRNRDITGIYSTTLRHLRHA 404
Cdd:PRK00275 317 AELNDLILQHFEEVILAADDSGTIQPLNSRFQLRDGYIEATHPNVFKRTPFALLEIFVLMAQHPEIKGVRADTIRLLREH 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 405 RRHLKQPLCYIPEARSLFLTMLRHPGAVSRGLVPMHRHSVLWAYMPQWSHIVGQMQFDLFHAYTVDEHTIRVLQKLESFS 484
Cdd:PRK00275 397 RHLIDDAFRNDIRNTSLFIELFKCPIGIHRNLRRMNRYGILGRYLPEFGHIVGQMQHDLFHIYTVDAHTLNLIKNLRKLR 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 485 LEETRSKHPLCVDLWPRLSHPELILIAALFHDIAKGRGGDHSVLGAQDVLKFAELHGLNSRETQLVAWLVRQHLLMSVTA 564
Cdd:PRK00275 477 YPEVSEKFPLASKLMGRLPKPELLYIAGLYHDIGKGRGGDHSELGAVDAEAFCQRHQLPAWDTRLVVWLVENHLLMSTTA 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 565 QRRDIQDPEVIKQFAEEVQTENRLRFLVCLTVADICATNETLWNSWKQSLLRELYFATEKQLRRGMQNTPDMRERVRHHQ 644
Cdd:PRK00275 557 QRKDLSDPQVIHDFALKVGDQTHLDYLYVLTVADINATNPTLWNSWRASLLRQLYTETKRALRRGLENPVDREEQIRQTQ 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 645 VQALALLRMENINEEALHHIWARCRANYFVRHSPNQLAWHARHLLKH-DLSQPLILLSPQATR---GGTEIFIWSPDRPY 720
Cdd:PRK00275 637 SAALDILVRKGTDPDDAEQLWSQLGDDYFLRHTAGDIAWHTEAILQHpDDGGPLVLIKETTQRefeGGTQIFIYAPDQHD 716
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 721 LFAAVCAELDRRNLSVHDAQIFTTRDGMAMDTFIVLEPDGSPLSAD--RHEAIRHGLEQAITQRTWQPPQ-PRRQPAKLR 797
Cdd:PRK00275 717 FFAATVAAMDQLNLNIHDARIITSSSQFTLDTYIVLDDDGEPIGDNpaRIEQIREGLTEALRNPDDYPTIiQRRVPRQLK 796
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 798 HFTVETEVNFLPTHTERRSFLELIALDQPGLLARVGQVFADLGISLHGARITTIGERVEDLFIIATADRRALNN-VLQQE 876
Cdd:PRK00275 797 HFAFPTQVTISNDAQRPVTVLEIIAPDRPGLLARIGRIFLEFDLSLQNAKIATLGERVEDVFFITDADNQPLSDpQLCSR 876
|
....*
gi 639221815 877 VQQRL 881
Cdd:PRK00275 877 LQDAI 881
|
|
| PRK03059 |
PRK03059 |
PII uridylyl-transferase; Provisional |
30-886 |
0e+00 |
|
PII uridylyl-transferase; Provisional
Pssm-ID: 235101 [Multi-domain] Cd Length: 856 Bit Score: 736.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 30 DALHCAAIKQHLDDFQRWLGVAFDSGVSAEDLVEARTEFIDQLLQRLWLHYGFGDteETALVAVGGYGRGELHPLSDIDL 109
Cdd:PRK03059 6 PPPPAASLRAELKAAKAALLARFRQAPNVTALLHALSRLVDQALRRLWQECGLPA--GAALVAVGGYGRGELFPYSDVDL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 110 LILsrkrLPD----AQAQKVGELLTLLWDVKLEVGHSVRTLEECLLEGLSDLTVATNLIESRLLIGDVALFLELQKHIFS 185
Cdd:PRK03059 84 LVL----LPDapdaALDARIERFIGLCWDLGLEIGSSVRTVDECIEEAAQDVTVQTSLLEARLLTGSAALFERFQRRYRA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 186 DgfWPSEKFFPAKVEEQNERHQRYHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSLREMVGFGFLTEAERNELDE 265
Cdd:PRK03059 160 A--LDPRAFFQAKLLEMRQRHAKFQDTPYSLEPNCKESPGGLRDLQTILWIARAAGLGSSWRELAKRGLITDREARQLRR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 266 CQHLLWRIRFALHLELNRYDNRLLFDRQLSVAQRLNYQGEGNE-PVEQMMKDFYRVTRRVGELNQMLLQLFDEAILAlST 344
Cdd:PRK03059 238 NERFLKTLRARLHLLAGRREDRLVFDLQTALAESFGYRPTAAKrASEQLMRRYYWAAKAVTQLNTILLQNIEARLFP-ST 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 345 DEKPRPLDDDFQLRGTLIDLRDETLFIREPQAILRMFYAMVRNRDITGIYSTTLRHLRHARRHLKQPLCYIPEARSLFLT 424
Cdd:PRK03059 317 SGITRVINERFVEKQGMLEIASDDLFERHPHAILEAFLLYQQTPGLKGLSARTLRALYNARDVMNAAFRRDPVNRALFMQ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 425 MLRHPGAVSRGLVPMHRHSVLWAYMPQWSHIVGQMQFDLFHAYTVDEHTIRVLQKLESFSLEETRSKHPLCVDLWPRLSH 504
Cdd:PRK03059 397 ILQQPRGITHALRLMNQTSVLGRYLPNFRRIVGQMQHDLFHVYTVDQHILMVLRNLRRFAMAEHAHEYPFCSQLIANFDR 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 505 PELILIAALFHDIAKGRGGDHSVLGAQDVLKFAELHGLNSRETQLVAWLVRQHLLMSVTAQRRDIQDPEVIKQFAEEVQT 584
Cdd:PRK03059 477 PWLLYVAALFHDIAKGRGGDHSTLGAVDARRFCRQHGLAREDAELVVWLVEHHLTMSQVAQKQDLSDPEVIARFAELVGD 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 585 ENRLRFLVCLTVADICATNETLWNSWKQSLLRELYFATEKQLRRGmqnTPDMRERVRHHQVQALALLRMENINEEALHHI 664
Cdd:PRK03059 557 ERRLTALYLLTVADIRGTSPKVWNAWKGKLLEDLYRATLRVLGGA---APDAHSELEARKEEALALLRLEALPDDAHEAL 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 665 WARCRANYFVRHSPNQLAWHARHLLKH-DLSQPLILLSPQATRGGTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFT 743
Cdd:PRK03059 634 WDQLDVGYFLRHDAADIAWHTRHLYRHvDTDTPIVRARLSPAGEGLQVMVYTPDQPDLFARICGYFDRAGFSILDARVHT 713
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 744 TRDGMAMDTFIVLEPDGSplSADRHEA--IRHGLEQAIT-QRTWQPPQPRRQPAKLRHFTVETEVNFLPTHTERRSFLEL 820
Cdd:PRK03059 714 TRHGYALDTFQVLDPEED--VHYRDIInlVEHELAERLAeQAPLPEPSKGRLSRQVKHFPITPRVDLRPDERGQYYILSV 791
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 639221815 821 IALDQPGLLARVGQVFADLGISLHGARITTIGERVEDLFIIATADRRalNNVLQQEVQQRLTAALN 886
Cdd:PRK03059 792 SANDRPGLLYAIARVLAEHRVSVHTAKINTLGERVEDTFLIDGSGLS--DNRLQIQLETELLDALA 855
|
|
| PRK05092 |
PRK05092 |
PII uridylyl-transferase; Provisional |
35-885 |
0e+00 |
|
PII uridylyl-transferase; Provisional
Pssm-ID: 235342 [Multi-domain] Cd Length: 931 Bit Score: 582.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 35 AAIKQHLDDFQRWLGVAFDSGVSAEDLVEARTEFIDQLLQRLwlhYGFGDT-----------EETALVAVGGYGRGELHP 103
Cdd:PRK05092 45 ALLKQALARGRAEARERLEADGSGRACARRLAYLTDELIRAL---YDFATThlypadnpsegERLAVLAVGGYGRGELAP 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 104 LSDIDLLILSRKRlPDAQAQKVGE-LLTLLWDVKLEVGHSVRTLEECLLEGLSDLTVATNLIESRLLIGDVALFLELQKH 182
Cdd:PRK05092 122 GSDIDLLFLLPYK-QTAWAESVVEyMLYMLWDLGLKVGHATRSIDECIRLAREDMTIRTALLEARFLAGDRALFEELETR 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 183 IFSDGFWPSEK-FFPAKVEEQNERHQRYHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSLREMVGFGFLTEAERN 261
Cdd:PRK05092 201 FDKEVVKGTAAeFVAAKLAERDERHRRAGDSRYLVEPNVKEGKGGLRDLHTLFWIAKYVYRVRDAAELVKLGVFTREEYR 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 262 ELDECQHLLWRIRFALHLELNRYDNRLLFDRQLSVAQRLNYQG-EGNEPVEQMMKDFYRVTRRVGELNQMLL------QL 334
Cdd:PRK05092 281 LFRRAEDFLWAVRCHLHFLTGRAEERLSFDLQPEIAERMGYTDhPGLSGVERFMKHYFLVAKDVGDLTRIFCaaleaqHA 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 335 FDEAILALSTDEKPRPLD-DDFQLRGTLIDLRDETLFIREPQAILRMFY-AMVRNRDItgiYSTTLRHLRHARRHLKQPL 412
Cdd:PRK05092 361 KRAPGLNRFARRRRKALDsDGFVVDNGRINLADPDVFERDPVNLIRLFHlADRHGLDI---HPDAMRLVTRSLRLIDAAL 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 413 CYIPEARSLFLTMLRHPGAVSRGLVPMHRHSVLWAYMPQWSHIVGQMQFDLFHAYTVDEHTIR---VLQKLESFSLEETr 489
Cdd:PRK05092 438 REDPEANRLFLDILTSRRNPERVLRRMNEAGVLGRFIPDFGRIVAMMQFNMYHHYTVDEHTIRaigVLAEIERGELADE- 516
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 490 skHPLCVDLWPRLSHPELILIAALFHDIAKGRGGDHSVLGAQDVLKFAELHGLNSRETQLVAWLVRQHLLMSVTAQRRDI 569
Cdd:PRK05092 517 --HPLASELMPKIESRRALYVAVLLHDIAKGRPEDHSIAGARIARRLCPRLGLSPAETETVAWLVEHHLLMSDTAQKRDL 594
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 570 QDPEVIKQFAEEVQTENRLRFLVCLTVADICATNETLWNSWKQSLLRELYFATEKQLRRGMQNTpDMRERVRHHQVQALA 649
Cdd:PRK05092 595 SDPKTIEDFADAVQSPERLKLLLILTVADIRAVGPGVWNGWKAQLLRTLYYETEEVLTGGFSEL-NRAERVAAAKEALRE 673
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 650 LLrmENINEEALHHIWARCRANYFVRHSPNQLAWHARHLLKHD-LSQPL-ILLSPQATRGGTEIFIWSPDRPYLFAAVCA 727
Cdd:PRK05092 674 AL--SDWPKADRDAYLARHYPAYWLAVDLDTQARHARFIRDADdAGRPLaTEVRPDPARGVTEVTVLAADHPGLFSRIAG 751
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 728 ELDRRNLSVHDAQIFTTRDGMAMDTFIVLEPDGSPL-SADRHEAIRHGLEQAITQRTWQPPQPRRQP---AKLRHFTVET 803
Cdd:PRK05092 752 ACAAAGANIVDARIFTTTDGRALDTFWIQDAFGRDEdEPRRLARLAKAIEDALSGEVRLPEALAKRTkpkKRARAFHVPP 831
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 804 EVNFLPTHTERRSFLELIALDQPGLLARVGQVFADLGISLHGARITTIGERVEDLFIIA-------TADRRalnnvlQQE 876
Cdd:PRK05092 832 RVTIDNEASNRFTVIEVNGRDRPGLLYDLTRALSDLNLNIASAHIATYGERAVDVFYVTdlfglkiTNEAR------QAA 905
|
....*....
gi 639221815 877 VQQRLTAAL 885
Cdd:PRK05092 906 IRRALLAAL 914
|
|
| PRK04374 |
PRK04374 |
[protein-PII] uridylyltransferase; |
30-888 |
0e+00 |
|
[protein-PII] uridylyltransferase;
Pssm-ID: 179839 [Multi-domain] Cd Length: 869 Bit Score: 581.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 30 DALHCAAIKQHLDDFQRWLGVAFDSGVSAEDLVEARTEFIDQLLQRLWLHYGFGDTEeTALVAVGGYGRGELHPLSDIDL 109
Cdd:PRK04374 16 DADWAAAARPLLVHADMRLCKRFDQGEPIERLLALRARAVDQLMRNAWTRCIPADSG-LSLHAVGGYGRGELFPRSDVDL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 110 LILSRKRLPDAQAQKVGELLTLLWDVKLEVGHSVRTLEECLlEGLSDLTVATNLIESRLLIGDVALFLELQKHIFSDGFW 189
Cdd:PRK04374 95 LVLGETAAQQRHEQALARLFALLWDVGLPISHAVRSPAQCT-AAAADQTVLTALIESRPLVADAAARAALAAAIAPQQVW 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 190 PSEKFFPAKVEEQNERHQRYHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSLREMVGFGFLTEAERNELDECQHL 269
Cdd:PRK04374 174 PPRAFFQAKREELLARHQRFGDTADNLEPDIKDGPGGLRDLQTLGWMALRAFGVKDLEALVGLGHVGCDEAAALRREREE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 270 LWRIRFALHLELNRYDNRLLFDRQLSVAQRLNYQGEG-NEPVEQMMKDFYRVTRRVGELNQMLLQLFDEAilaLSTDEKP 348
Cdd:PRK04374 254 LARLRFGLHLVANRPEERLRFDYQKTLAERLGFADDPeSLGVEKMMQRFYRSAALIRRISDRLLQRFEEQ---FDGEATP 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 349 RPLDDDFQLRGTLIDLRDETLFIREPQAILRMFYAMVRNRDITGIYSTTLRHLRHARRHLKQPLCYIPEARSLFLTMLRH 428
Cdd:PRK04374 331 EPLGGGFSLRRGYLAADADSWPDGDVLQVFALFAQWAAHREVRGLHSLTARALAEVLRDLPAYDVADATARERFMALLRG 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 429 PGAVSRgLVPMHRHSVLWAYMPQWSHIVGQMQFDLFHAYTVDEHTIRVLQKLESFSLEETRSKHPLCVDLWPRLSHPELI 508
Cdd:PRK04374 411 PRAVET-LNRMARLGVLGQWIPAFASVSGRMQFDLFHVYTVDQHTLMVLRNIALFAAGRADERFSIAHEVWPRLRKPELL 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 509 LIAALFHDIAKGRGGDHSVLGAQDVLKFAELHGLNSRETQLVAWLVRQHLLMSVTAQRRDIQDPEVIKQFAEEVQTENRL 588
Cdd:PRK04374 490 LLAGLFHDIAKGRGGDHSELGAVDARAFCLAHRLSEGDTELVTWLVEQHLRMSVTAQKQDISDPEVIHRFATLVGTRERL 569
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 589 RFLVCLTVADICATNETLWNSWKQSLLRELYFATEKQLRRGMQNTPDMRERVRHHQVQALALLRMENINEEALHHIWARC 668
Cdd:PRK04374 570 DYLYLLTCADIAGTSPKLWNAWKDRLLADLYFAARRALREGLEHPPPREERLREARESARALMQAQGHDDATIDRQFAGM 649
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 669 RANYFVRHSPNQLAWHARHLLKHDLSQPLILLSPQAT-RGGTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDG 747
Cdd:PRK04374 650 PDENFLRFRPEQLAWQAASLIEVEIGQTLVKARRAVPdNDALEVFVYSPDRDGLFAAIVATLDRKGYGIHRARVLDAPHD 729
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 748 MAMDTFIVLEPD--GSPLSADRHEAIRHGLEQAITQRTwqpPQPRRQPAKLRHFTVETEVNFLPTHTERRSFLELIALDQ 825
Cdd:PRK04374 730 AIFDVFEVLPQDtyADGDPQRLAAALRQVLAGDLQKVR---PARRAVPRQLRHFRFAPRVEFSESAGGRRTRISLVAPDR 806
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 639221815 826 PGLLARVGQVFADLGISLHGARITTIGERVEDLFIIATADRRALNNVLQQEVQQRLTAALNPN 888
Cdd:PRK04374 807 PGLLADVAHVLRMQHLRVHDARIATFGERAEDQFQITDEHDRPLSESARQALRDALCACLDPV 869
|
|
| PRK03381 |
PRK03381 |
PII uridylyl-transferase; Provisional |
53-883 |
1.82e-86 |
|
PII uridylyl-transferase; Provisional
Pssm-ID: 235123 [Multi-domain] Cd Length: 774 Bit Score: 292.67 E-value: 1.82e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 53 DSGVSAEDLVEARTEFIDQLLQRLWLHYGFGDTEETALVAVGGYGRGELHPLSDIDLLILSRKRLPDAQAQKVGELLTLL 132
Cdd:PRK03381 23 GGHLDGAALRAALADLHEFWLAGLAAEAGIADGSGVALVAVGGLGRRELLPYSDLDLVLLHDGRPADDVAEVADRLWYPL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 133 WDVKLEVGHSVRTLEECLLEGLSDLTVATNLIESRLLIGDVALFLELQKHIFSDgfWPSE--KFFPAKVEEQNERHQRYH 210
Cdd:PRK03381 103 WDAGIRLDHSVRTVPEALKVAGSDLKAALGLLDARHIAGDADLSALLIGGVRRQ--WRNGarRRLPELVELTRARWERSG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 211 GTSYNLEPDIKSSPGGLRDIHTLQWVARRHfgatslremvgfgfLTEAERNELDECQHLLWRIRFALHLELNRYDNRLLF 290
Cdd:PRK03381 181 EIAHLAEPDLKEGRGGLRDVQLLRALAAAQ--------------LADAPGGGLDAAHRRLLDVRTELHRVSGRGRDRLLA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 291 DRQLSVAQRLNYqgEGNEPVEQMMKDFYRV--------TRRVGELnqmllqLFDEAILALSTDEKPRPLDDDFQLRGTLI 362
Cdd:PRK03381 247 QEADEVAAALGL--GDRFDLARALSDAARTisyavdvgWRTAANA------LPRRGLSALRRRPVRRPLDEGVVEHAGEV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 363 DLRDETLFIREPQAILRMFYAMVRnrdiTG--IYSTTLRHLRHARRHLKQPlcYIPEARSLFLTMLrhpgAVSRGLVP-- 438
Cdd:PRK03381 319 VLARDARPARDPGLVLRVAAAAAT----TGlpIAAATLSRLAASAPPLPTP--WPAEARDDLLVLL----GAGPAAVAvi 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 439 --MHRHSVLWAYMPQWSHIVGQMQFDLFHAYTVDEHTIRVLQKLESFsleeTRskhplcvdlwpRLSHPELILIAALFHD 516
Cdd:PRK03381 389 eaLDRTGLWGRLLPEWEAVRDLPPRDPVHRWTVDRHLVETAVRAAAL----TR-----------RVARPDLLLLGALLHD 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 517 IAKGRGGDHSVLGAQDVLKFAELHGLNSRETQLVAWLVRQHLLMSVTAQRRDIQDPEVIKQFAEEVQTENR-LRFLVCLT 595
Cdd:PRK03381 454 IGKGRGGDHSVVGAELARQIGARLGLSPADVALLSALVRHHLLLPETATRRDLDDPATIEAVAEALGGDPVlLELLHALT 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 596 VADICATNETLWNSWKQSLLRELYfatekqlrrgmqntpdmrERVRhhqvqalALLRMENINEealhhiwarcranyfvr 675
Cdd:PRK03381 534 EADSLATGPGVWSDWKASLVGDLV------------------RRCR-------AVLAGEPLPE----------------- 571
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 676 hsPNQLAWHARHLLKHDlsQPLILLSPqATRGGTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTrDGMAMDTFIV 755
Cdd:PRK03381 572 --PEPLDPAQLALAADG--GVHVEIAP-ADPHMVEVTVVAPDRRGLLSKAAGVLALHRLRVRSASVRSH-DGVAVLEFVV 645
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 756 LEPDGSPLSADRheaIRHGLEQAIT----------QRTWQPPQPRRQPAklrhfTVETEVNFLPTHTERRSFLELIALDQ 825
Cdd:PRK03381 646 SPRFGSPPDAAL---LRQDLRRALDgdldvlarlaAREAAAAAVPVRRP-----AAPPRVLWLDGASPDATVLEVRAADR 717
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*...
gi 639221815 826 PGLLARVGQVFADLGISLHGARITTIGERVEDLFIIATADRRALNNVlQQEVQQRLTA 883
Cdd:PRK03381 718 PGLLARLARALERAGVDVRWARVATLGADVVDVFYVTGAAGGPLADA-RAAVEQAVLA 774
|
|
| GlnD_UR_UTase |
pfam08335 |
GlnD PII-uridylyltransferase; This is a family of bifunctional uridylyl-removing enzymes ... |
193-332 |
1.13e-49 |
|
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: 171.61 E-value: 1.13e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 193 KFFPAKVEEQNERHQRYHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSLREMVGFGFLTEAERNELDECQHLLWR 272
Cdd:pfam08335 1 RFMKAKIEEQVARHGRYGDTAYNLEPNIKLGPGGLRDIEFIVWIAQLIFTLRALEELVELGLLTREEARELRRAYRFLRR 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 273 IRFALHLELNRYDNRLLFDRQLSVAQRLNYQGEGNEPVEQMMKDFYRVTRRVGELNQMLL 332
Cdd:pfam08335 81 VRHRLHLLADRQTDRLPFDLQRRLARALGYARDGWLAVERFMRRLFRHAHRVSRLFEILL 140
|
|
| glnD |
PRK00227 |
[protein-PII] uridylyltransferase; |
57-636 |
3.56e-38 |
|
[protein-PII] uridylyltransferase;
Pssm-ID: 178937 [Multi-domain] Cd Length: 693 Bit Score: 152.61 E-value: 3.56e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 57 SAEDLVEARTEFIDQLLQRLWLHYGfgdteeTALVAVGGYGRGELHPLSDIDLLILSRkrlPDAQAQKVGELLTLLWDVK 136
Cdd:PRK00227 3 TPAQLREDAEASALALLGSLQLPPG------TALAATGSLARREMTPYSDLDLILLHP---PGATPDGVEDLWYPIWDAK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 137 LEVGHSVRTLEECLLEGLSDLTVATNLIESRLLIGDVALFLELQKHIFSDgfWPSE--KFFPAKVEEQNERHQRYHGTSY 214
Cdd:PRK00227 74 KRLDYSVRTPQECAAMISADSTAALALLDLRFVAGDEQLTASTRAKILEK--WRRElnKNFDAVVDTAIARWRRSGSVVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 215 NLEPDIKSSPGGLRDIHTLQWVArrhfgatslremvgFGFLTEAERneLDECQHLLWRIRFALHLELNRYDNRLLFDRQL 294
Cdd:PRK00227 152 MTRPDLKHGRGGLRDIELIRALA--------------LGHLCDAPP--LDSQHQLLLDVRTLLHVHARRARDVLDPEFAV 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 295 SVAQRLNYQgegnepveqmmkDFYRVTRRVGELNQMLlqlfDEAI-LALST------------DEKPRPLDDDFQLRGTL 361
Cdd:PRK00227 216 DIALDLGFV------------DRYHLSREIADAARAI----DDALtAALATargalprrtafrNAVRRPLDVDVVDANGT 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 362 IDLrDETLFIREPQAILRMFYAMVRnrdiTG--IYSTTLRHLRHARRhLKQPlcYIPEARSLFLTMLRHPGAVSRGLVPM 439
Cdd:PRK00227 280 IAL-SRTPDLDDPALPLRVAAAAAR----TGlpVSESVWKRLEECPE-LPEP--WPASAAGDFFRLLSSPVNSRRVIKQM 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 440 HRHSVLWAYMPQWSHIVGQMQFDLFHAYTVDEHTIRVLQKlesfsleetrskhplCVDLWPRLSHPELILIAALFHDIAK 519
Cdd:PRK00227 352 DRHGLWERIVPEWDRIRGLMPREPSHIHTIDEHSLNTVAN---------------CALETVTVARPDLLLLGALYHDIGK 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 520 GRGGDHSVLGAQDVLKFAELHGLNSRETQLVAWLVRQHLLMSVTAQRRDIQDPEVIKQFAEEVQTEN-RLRFLVCLTVAD 598
Cdd:PRK00227 417 GYPRPHEQVGAEMVARAARRMGLNLRDRAVVQTLVAEHTTLARIAGRLDPTSEEAVDKLLDAVRYDLlTLNLLEVLTEAD 496
|
570 580 590
....*....|....*....|....*....|....*...
gi 639221815 599 ICATNETLWNSWKQSLLRELYFATEKQLRRGMQNTPDM 636
Cdd:PRK00227 497 AEGTGPGVWTARLEQGLRIVCSRARARLTDIRPVAPMF 534
|
|
| ACT_UUR-like_1 |
cd04900 |
ACT domain family, ACT_UUR-like_1, includes the first of two C-terminal ACT domains of the ... |
708-779 |
4.92e-29 |
|
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: 110.26 E-value: 4.92e-29
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 639221815 708 GTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDGMAMDTFIVLEPDGSPLSA-DRHEAIRHGLEQAI 779
Cdd:cd04900 1 GTEVFIYTPDRPGLFARIAGALDQLGLNILDARIFTTRDGYALDTFVVLDPDGEPIGErERLARIREALEDAL 73
|
|
| ACT_ACR-UUR-like_2 |
cd04899 |
C-terminal ACT domains of the bacterial signal-transducing uridylyltransferase ... |
818-885 |
9.46e-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: 95.21 E-value: 9.46e-24
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 639221815 818 LELIALDQPGLLARVGQVFADLGISLHGARITTIGERVEDLFIIATADRRALNNVLQQEVQQRLTAAL 885
Cdd:cd04899 3 LELTALDRPGLLADVTRVLAELGLNIHSAKIATLGERAEDVFYVTDADGQPLDPERQEALRAALGEAL 70
|
|
| NT_GlnE_GlnD_like |
cd05401 |
Nucleotidyltransferase (NT) domain of Escherichia coli adenylyltransferase (GlnE), Escherichia ... |
52-184 |
2.51e-23 |
|
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: 97.79 E-value: 2.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 52 FDSGVSAEDLVEARTEFIDQLLQRLW----LHYGFG-DTEETALVAVGGYGRGELHPLSDIDLLILSRKRLPDAQ----- 121
Cdd:cd05401 15 LLGGASIRAISRALSDLADALLRRALelalAELGKGpPPVPFALLALGSYGRGELNPSSDQDLLLLYDDDGDEVAayfee 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 639221815 122 -AQKVGELLTL------LWDVKLEVGHSVRTLEECLLEGLSDLTV------ATNLIESRLLIGDVALFLELQKHIF 184
Cdd:cd05401 95 lAERLIKILSEaggpycLGDVMLRPPGWRRSLAEWLDAARDWLTEpgrlweRTALLDARPVAGDRALAEELRRRIR 170
|
|
| ACT_UUR-ACR-like |
cd04873 |
ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) ... |
709-779 |
6.35e-20 |
|
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: 84.52 E-value: 6.35e-20
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 639221815 709 TEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDgMAMDTFIVLEPDGSPLSADRHEAIRHGLEQAI 779
Cdd:cd04873 1 TVVEVYAPDRPGLLADITRVLADLGLNIHDARISTTGE-RALDVFYVTDSDGRPLDPERIARLEEALEDAL 70
|
|
| ACT_UUR-ACR-like |
cd04873 |
ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) ... |
818-885 |
9.02e-20 |
|
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: 83.75 E-value: 9.02e-20
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 639221815 818 LELIALDQPGLLARVGQVFADLGISLHGARITTIGERVEDLFIIATADRRALNNVLQQEVQQRLTAAL 885
Cdd:cd04873 3 VEVYAPDRPGLLADITRVLADLGLNIHDARISTTGERALDVFYVTDSDGRPLDPERIARLEEALEDAL 70
|
|
| HD |
pfam01966 |
HD domain; HD domains are metal dependent phosphohydrolases. |
469-575 |
3.02e-09 |
|
HD domain; HD domains are metal dependent phosphohydrolases.
Pssm-ID: 460398 [Multi-domain] Cd Length: 110 Bit Score: 55.32 E-value: 3.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 469 VDEHTIRVLQKLESFSLEETRSKhplcvdlwprlshPELILIAALFHDIAKGRGGD----------HSVLGAQDVLKFAE 538
Cdd:pfam01966 1 RLEHSLRVALLARELAEELGELD-------------RELLLLAALLHDIGKGPFGDekpefeiflgHAVVGAEILRELEK 67
|
90 100 110
....*....|....*....|....*....|....*..
gi 639221815 539 LHGLnsretQLVAWLVRQHLLMSVTAQRRDIQDPEVI 575
Cdd:pfam01966 68 RLGL-----EDVLKLILEHHESWEGAGYPEEISLEAR 99
|
|
| ACT |
pfam01842 |
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ... |
818-875 |
1.34e-08 |
|
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: 51.92 E-value: 1.34e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 639221815 818 LELIALDQPGLLARVGQVFADLGISLHGARITTIGERVEDLFIIATADRRALNNVLQQ 875
Cdd:pfam01842 3 LEVLVPDRPGLLARVLGALADRGINITSIEQGTSEDKGGIVFVVIVVDEEDLEEVLEA 60
|
|
| ACT_ACR-UUR-like_2 |
cd04899 |
C-terminal ACT domains of the bacterial signal-transducing uridylyltransferase ... |
709-779 |
2.33e-08 |
|
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: 51.30 E-value: 2.33e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 639221815 709 TEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIfTTRDGMAMDTFIVLEPDGSPLSADRHEAIRHGLEQAI 779
Cdd:cd04899 1 TVLELTALDRPGLLADVTRVLAELGLNIHSAKI-ATLGERAEDVFYVTDADGQPLDPERQEALRAALGEAL 70
|
|
| HDc |
smart00471 |
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ... |
465-612 |
4.09e-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: 49.60 E-value: 4.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 465 HAYTVDEHTIRVLQKLESFSLEEtrskhplcvdlwpRLSHPELILIAALFHDIAKGRGGD-----------HSVLGAQDV 533
Cdd:smart00471 1 SDYHVFEHSLRVAQLAAALAEEL-------------GLLDIELLLLAALLHDIGKPGTPDsflvktsvledHHFIGAEIL 67
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 639221815 534 LKFAElhglNSRETQLVAWLVRQHLLMSVTAQRRDIqDPEVIkqfaeevqtenrlrflvCLTVADICATNETLWNSWKQ 612
Cdd:smart00471 68 LEEEE----PRILEEILRTAILSHHERPDGLRGEPI-TLEAR-----------------IVKVADRLDALRADRRYRRV 124
|
|
| ACT |
cd02116 |
ACT domains are commonly involved in specifically binding an amino acid or other small ligand ... |
818-875 |
6.67e-07 |
|
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: 46.90 E-value: 6.67e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 639221815 818 LELIALDQPGLLARVGQVFADLGISLHGARITTIGERVEDLFIIATADRRALNNVLQQ 875
Cdd:cd02116 1 LTVSGPDRPGLLAKVLSVLAEAGINITSIEQRTSGDGGEADIFIVVDGDGDLEKLLEA 58
|
|
| HDc |
cd00077 |
Metal dependent phosphohydrolases with conserved 'HD' motif |
467-619 |
1.16e-06 |
|
Metal dependent phosphohydrolases with conserved 'HD' motif
Pssm-ID: 238032 [Multi-domain] Cd Length: 145 Bit Score: 48.87 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 467 YTVDEHTIRVLQKLESFSLEETRSKHPlcvdlwprlshPELILIAALFHDIAKG------------RGGDHSVLGAQDVL 534
Cdd:cd00077 1 EHRFEHSLRVAQLARRLAEELGLSEED-----------IELLRLAALLHDIGKPgtpdaiteeeseLEKDHAIVGAEILR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 535 KFaelhgLNSRETQLVAWLVRQHLLMsvTAQRRDIQDPEVIKqfaeevQTENRLRFLVCLTVADIC-ATNETLWNSWKQS 613
Cdd:cd00077 70 EL-----LLEEVIKLIDELILAVDAS--HHERLDGLGYPDGL------KGEEITLEARIVKLADRLdALRRDSREKRRRI 136
|
....*.
gi 639221815 614 LLRELY 619
Cdd:cd00077 137 AEEDLE 142
|
|
| NTP_transf_2 |
pfam01909 |
Nucleotidyltransferase domain; Members of this family belong to a large family of ... |
88-151 |
4.58e-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: 45.87 E-value: 4.58e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 639221815 88 TALVAVGGYGRGELHPLSDIDLLILSRKRLPDAQAQKVGELLTLL-WDVKLEVGHSVRTLEECLL 151
Cdd:pfam01909 15 AEVVLFGSYARGTALPGSDIDLLVVFPEPVEEERLLKLAKIIKELeELLGLEVDLVTREKIEFPL 79
|
|
| ACT_UUR-like_1 |
cd04900 |
ACT domain family, ACT_UUR-like_1, includes the first of two C-terminal ACT domains of the ... |
824-885 |
1.22e-05 |
|
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: 44.01 E-value: 1.22e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 639221815 824 DQPGLLARVGQVFADLGISLHGARI-TTIGERVEDLFIIATADRRALNNVLQ-QEVQQRLTAAL 885
Cdd:cd04900 10 DRPGLFARIAGALDQLGLNILDARIfTTRDGYALDTFVVLDPDGEPIGERERlARIREALEDAL 73
|
|
| ACT |
cd02116 |
ACT domains are commonly involved in specifically binding an amino acid or other small ligand ... |
711-760 |
1.37e-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: 43.43 E-value: 1.37e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 639221815 711 IFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDGMAMDTFIVLEPDG 760
Cdd:cd02116 1 LTVSGPDRPGLLAKVLSVLAEAGINITSIEQRTSGDGGEADIFIVVDGDG 50
|
|
| ACT_ACR_4 |
cd04926 |
C-terminal ACT domain, of a novel type of ACT domain-containing protein which is composed ... |
708-772 |
1.26e-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: 41.18 E-value: 1.26e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 639221815 708 GTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIfTTRDGMAMDTFIVLEPDGSPLSADRHEAIR 772
Cdd:cd04926 1 GVRLELRTEDRVGLLSDVTRVFRENGLTVTRAEI-STQGDMAVNVFYVTDANGNPVDPKTIEAVR 64
|
|
| ACT_RelA-SpoT |
cd04876 |
ACT domain found C-terminal of the RelA/SpoT domains; ACT_RelA-SpoT: the ACT domain found ... |
818-875 |
1.62e-04 |
|
ACT domain found C-terminal of the RelA/SpoT domains; ACT_RelA-SpoT: the ACT domain found C-terminal of the RelA/SpoT domains. Enzymes of the Rel/Spo family enable bacteria to survive prolonged periods of nutrient limitation by controlling guanosine-3'-diphosphate-5'-(tri)diphosphate ((p)ppGpp) production and subsequent rRNA repression (stringent response). Both the synthesis of (p)ppGpp from ATP and GDP(GTP), and its hydrolysis to GDP(GTP) and pyrophosphate, are catalyzed by Rel/Spo proteins. In Escherichia coli and its close relatives, the metabolism of (p)ppGpp is governed by two homologous proteins, RelA and SpoT. The RelA protein catalyzes (p)ppGpp synthesis in a reaction requiring its binding to ribosomes bearing codon-specified uncharged tRNA. The major role of the SpoT protein is the breakdown of (p)ppGpp by a manganese-dependent (p)ppGpp pyrophosphohydrolase activity. Although the stringent response appears to be tightly regulated by these two enzymes in E. coli, a bifunctional Rel/Spo protein has been discovered in most gram-positive organisms studied so far. These bifunctional Rel/Spo homologs (rsh) appear to modulate (p)ppGpp levels through two distinct active sites that are controlled by a reciprocal regulatory mechanism ensuring inverse coupling of opposing activities. In studies with the Streptococcus equisimilis Rel/Spo homolog, the C-terminal domain appears to be involved in this reciprocal regulation of the two opposing catalytic activities present in the N-terminal domain, ensuring that both synthesis and degradation activities are not coinduced. Members of this CD belong to the superfamily of ACT regulatory domains.
Pssm-ID: 153148 [Multi-domain] Cd Length: 71 Bit Score: 40.51 E-value: 1.62e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 639221815 818 LELIALDQPGLLARVGQVFADLGISLHGARITTIGER-VEDLFIIATADRRALNNVLQQ 875
Cdd:cd04876 1 IRVEAIDRPGLLADITTVIAEEKINILSVNTRTDDDGlATIRLTLEVRDLEHLARIMRK 59
|
|
| ACT_TyrKc |
cd04928 |
Uncharacterized, N-terminal ACT domain of an Arabidopsis/Oryza predicted tyrosine kinase and ... |
710-779 |
2.94e-04 |
|
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: 39.85 E-value: 2.94e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639221815 710 EIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDGMAMDTFIVlepDGspLSADRHEAIRHGLEQAI 779
Cdd:cd04928 3 EITFAAGDKPKLLSQLSSLLGDLGLNIAEAHAFSTDDGLALDIFVV---TG--WKRGETAALGHALQKEI 67
|
|
| MJ0604 |
COG1708 |
Predicted nucleotidyltransferase, MJ0604 family [General function prediction only]; |
94-132 |
1.03e-03 |
|
Predicted nucleotidyltransferase, MJ0604 family [General function prediction only];
Pssm-ID: 441314 Cd Length: 95 Bit Score: 39.24 E-value: 1.03e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 639221815 94 GGYGRGELHPLSDIDLLILSRK-RLPDAQAQKVGELLTLL 132
Cdd:COG1708 29 GSYARGDARPDSDIDLLVVVDDpPLPDERLELLADLLREL 68
|
|
| ACT_ACR_2 |
cd04925 |
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats ... |
818-855 |
1.95e-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: 37.79 E-value: 1.95e-03
10 20 30
....*....|....*....|....*....|....*...
gi 639221815 818 LELIALDQPGLLARVGQVFADLGISLHGARITTIGERV 855
Cdd:cd04925 3 IELTGTDRPGLLSEVFAVLADLHCNVVEARAWTHNGRL 40
|
|
| NT_KNTase_like |
cd05403 |
Nucleotidyltransferase (NT) domain of Staphylococcus aureus kanamycin nucleotidyltransferase, ... |
67-139 |
2.42e-03 |
|
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: 38.17 E-value: 2.42e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 639221815 67 EFIDQLLQRLWLHYGFGDteetALVAVGGYGRGELHPLSDIDLLILSRKRLPDAQAQKVGELLTLLWDVKLEV 139
Cdd:cd05403 2 EILEEILEILRELLGGVE----KVYLFGSYARGDARPDSDIDLLVIFDDPLDPLELARLLEELELLLGRPVDL 70
|
|
| ACT_4 |
pfam13291 |
ACT domain; ACT domains bind to amino acids and regulate associated enzyme domains. These ACT ... |
818-873 |
2.60e-03 |
|
ACT domain; ACT domains bind to amino acids and regulate associated enzyme domains. These ACT domains are found at the C-terminus of the RelA protein.
Pssm-ID: 463831 [Multi-domain] Cd Length: 79 Bit Score: 37.54 E-value: 2.60e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 639221815 818 LELIALDQPGLLARVGQVFADLGISLHGARITTI--GERVEDLFIIATADRRALNNVL 873
Cdd:pfam13291 8 LEVEAIDRPGLLADITQVISEEKANIVSVNAKTRkkDGTAEIKITLEVKDVEHLERLM 65
|
|
| RnaY |
COG1418 |
HD superfamily phosphodieaserase, includes HD domain of RNase Y [Translation, ribosomal ... |
505-557 |
2.91e-03 |
|
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: 39.88 E-value: 2.91e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 639221815 505 PELILIAALFHDIAK----GRGGDHSVLGAQDVLKFAELHGLNSRETQLVAWLVRQH 557
Cdd:COG1418 41 VEVAKRAALLHDIGKakdhEVEGSHAEIGAELARKYLESLGFPEEEIEAVVHAIEAH 97
|
|
| ACT_HSDH-Hom |
cd04881 |
ACT_HSDH_Hom CD includes the C-terminal ACT domain of the NAD(P)H-dependent, homoserine ... |
817-844 |
4.33e-03 |
|
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: 36.72 E-value: 4.33e-03
10 20
....*....|....*....|....*...
gi 639221815 817 FLELIALDQPGLLARVGQVFADLGISLH 844
Cdd:cd04881 2 YLRLTVKDKPGVLAKITGILAEHGISIE 29
|
|
| ACT_ACR_4 |
cd04926 |
C-terminal ACT domain, of a novel type of ACT domain-containing protein which is composed ... |
818-881 |
7.02e-03 |
|
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: 36.17 E-value: 7.02e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 639221815 818 LELIALDQPGLLARVGQVFADLGISLHGARITTIGERVEDLFIIATADRRALNNVLQQEVQQRL 881
Cdd:cd04926 4 LELRTEDRVGLLSDVTRVFRENGLTVTRAEISTQGDMAVNVFYVTDANGNPVDPKTIEAVRQEI 67
|
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