|
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: 1843.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 8 QYANTALPTLPDQPDNPGVWPSHELTCAHIKAHMDVFHRWLGSAFDAGVSAEQLIEARTEFIDQLLQRLWIDYGFGQISD 87
Cdd:PRK05007 1 QYANTALPTLPGQPQSPLTWPDDELTVGGLKQHLDTFQQWLGDAFDAGISAEQLVEARTEFIDQLLQRLWIEAGFDQIPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 88 VALVAVGGYGRGELHPLSDIDLLILSRKKLPDEQAQKIGELLTLLWDVKLEVGHSVRTLEECLLEGLSDLTVATNLIETR 167
Cdd:PRK05007 81 LALVAVGGYGRGELHPLSDIDLLILSRKKLPDEQAQKVGELITLLWDLKLEVGHSVRTLEECLLEGLSDLTVATNLIESR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 168 LLIGDVALFLELQKHIFSDGFWPSEKFFAAKVEEQNQRHQRYHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSMD 247
Cdd:PRK05007 161 LLCGDVALFLELQKHIFSDGFWPSEKFYAAKVEEQNERHQRYHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSLD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 248 EMVGFGFLTEAERNELNECLHLLWRIRFALHLEVTRYDNRLLFDRQLSVAQRLNYQGEGNEPVEHMMKDFFRVTRRVTEL 327
Cdd:PRK05007 241 EMVGFGFLTPAERAELNECQHFLWRIRFALHLVLSRYDNRLLFDRQLSVAQLLGYEGEGNEPVERMMKDYYRTTRRVSEL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 328 NQMLLQLFDEAILALTADEKPRPIDDEFQLRGTLIDLRDETLFIREPEAILRMFYTMVRNSTITGIYSTTLRHLRHARRH 407
Cdd:PRK05007 321 NQMLLQLFDEAILALTADEKPRPIDDEFQLRGTLIDLRDETLFQRQPEAILRMFYLMARNSNITGIYSTTLRQLRHARRH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 408 LTQPLCYIPEARSLFLSMLRHPGAVSRGLLPMHRHSVLWAYMPQWSHIVGQMQFDLFHAYTVDEHTIRVMLKLESFAKEE 487
Cdd:PRK05007 401 LNQPLCEIPEARKLFMEILRHPGAVSRALLPMHRHSVLSAYMPQWSHIVGQMQFDLFHAYTVDEHTIRVLLKLESFADEE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 488 TRSRHPLCVELWPRLTHPELILIAALFHDIAKGRGGDHSVLGAQDVLKFAELHGLNSRETQLVAWLVRHHLLMSVTAQRR 567
Cdd:PRK05007 481 TRQRHPLCVELYPRLPKKELLLLAALFHDIAKGRGGDHSILGAQDALEFAELHGLNSRETQLVAWLVRNHLLMSVTAQRR 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 568 DIQDPEVIKQFAEEVQTENRLRYLVCLTVADICATNETLWNSWKQSLLRELYFATEKQLRRGMQNTPDMRERVRHHQLQA 647
Cdd:PRK05007 561 DIQDPDVIKQFAEEVQDENRLRYLVCLTVADICATNETLWNSWKQSLLRELYFATEKQLRRGMENPPDMRERVRHHQLQA 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 648 LALLRMDNIDEEALHQIWARCRANYFVRHSPNQLAWHARHLLKHDLSQPMILLSPQATRGGTEIFIWSPDRPYLFAAVCA 727
Cdd:PRK05007 641 LALLRMDNIDEEALHQIWSRCRADYFLRHTPNQLAWHARHLLQHDLDKPLVLLSKQATRGGTEIFIWSPDRPYLFAAVCA 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 728 ELDRRNLSVHDAQIFTTRDGMAMDTFIVLEPDGSPLSSDRHEGIRFGLEQAITQRSWQPPQPRRQPAKLRHFTVDTEVNF 807
Cdd:PRK05007 721 ELDRRNLSVHDAQIFTSRDGMAMDTFIVLEPDGSPLSQDRHQVIRKALEQALTQSSPQPPKPRRLPAKLRHFNVPTEVSF 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 808 LPTHTDRKSFLELIALDQPGLLARVGQVFADLGISLHGARITTIGERVEDLFIIATADRRALNNDLQLEVQQRLTAALNP 887
Cdd:PRK05007 801 LPTHTDRRSYMELIALDQPGLLARVGKIFADLGISLHGARITTIGERVEDLFILATADRRALNEELQQELRQRLTEALNP 880
|
....
gi 658548751 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: 1253.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 31 ELTCAHIKAHMDVFHRWLGSAFDAGVSAEQLIEARTEFIDQLLQRLWIDYGFGQISDVALVAVGGYGRGELHPLSDIDLL 110
Cdd:COG2844 1 AAALAALREALAEGRAALRERFRAGADGRELVRARAALVDQLLRALWDLAGLTEPERLALVAVGGYGRGELAPHSDIDLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 111 ILSRKKLPDEQAQKIGELLTLLWDVKLEVGHSVRTLEECLLEGLSDLTVATNLIETRLLIGDVALFLELQKHIFSDGFWP 190
Cdd:COG2844 81 FLLPDKPTPALEEVIEAFLYLLWDLGLEVGHSVRTVDECLREAREDITVRTALLEARLLAGDEALFEELRERFRADVFWD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 191 SEKFFAAKVEEQNQRHQRYHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSMDEMVGFGFLTEAERNELNECLHLL 270
Cdd:COG2844 161 SRAFFEAKLAEQRERHAKYGDTRYNLEPNIKEGPGGLRDLQTLLWIAKRHFGVRSLEELVKKGLLTEEEYRELRRAEDFL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 271 WRIRFALHLEVTRYDNRLLFDRQLSVAQRLNYQG-EGNEPVEHMMKDFFRVTRRVTELNQMLLQLFDEAILALTADEKPR 349
Cdd:COG2844 241 WRVRFALHLLAGRAEDRLLFDLQREVAERLGYQDtEGNRAVERFMQRYYRTAKAVGRLNEILLQRLEEAILKPPGLRRPR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 350 PIDDEFQLRGTLIDLRDETLFIREPEAILRMFYTMVRNSTITGIYSTTLRHLRHARRHLTQPLCYIPEARSLFLSMLRHP 429
Cdd:COG2844 321 PINEGFQLRNGRLEVADPDVFERDPVALLRLFLLAAQHPEGLGIHPDTLRLLRRALRLIDDAFRRDPEARRLFLEILRQP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 430 GAVSRGLLPMHRHSVLWAYMPQWSHIVGQMQFDLFHAYTVDEHTIRVMLKLESFAKEETRSRHPLCVELWPRLTHPELIL 509
Cdd:COG2844 401 RGITRALRRMNEYGVLGRYIPEFGRIVGQMQFDLFHVYTVDEHTLRVVRNLRRFERGELAEEFPLASELIAELPKPELLY 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 510 IAALFHDIAKGRGGDHSVLGAQDVLKFAELHGLNSRETQLVAWLVRHHLLMSVTAQRRDIQDPEVIKQFAEEVQTENRLR 589
Cdd:COG2844 481 LAALFHDIAKGRGGDHSELGAEDARRFCPRHGLSPEDTELVAWLVRHHLLMSHTAQRRDISDPEVIRDFARLVGSEERLD 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 590 YLVCLTVADICATNETLWNSWKQSLLRELYFATEKQLRRGMQnTPDMRERVRHHQLQALALLRMDNIDEEALHQIWARCR 669
Cdd:COG2844 561 YLYLLTVADIRATGPKVWNSWKASLLRELYRATLRALRGGLE-PPDREERIEERKEEALALLADQGWDEEEIEALWARLP 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 670 ANYFVRHSPNQLAWHARHLLKH-DLSQPMILLSPQATRGGTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDGM 748
Cdd:COG2844 640 DDYFLRHDPEEIAWHARLLLRAdDSGKPLVLIRPDPDRGGTEVFVYTPDRPGLFARIAGALAALGLNILDARIHTTRDGY 719
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 749 AMDTFIVLEPDGSPLSS-DRHEGIRFGLEQAITQRSWQP-PQPRRQPAKLRHFTVDTEVNFLPTHTDRKSFLELIALDQP 826
Cdd:COG2844 720 ALDTFIVLDPDGEPIDDpDRLERIEQALEEALSGEVPLPePLARRLSRRLRHFPVPPRVTFDNDASNRYTVLEVSALDRP 799
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 658548751 827 GLLARVGQVFADLGISLHGARITTIGERVEDLFIIATADRRALNND-LQLEVQQRLTAALNPNDK 890
Cdd:COG2844 800 GLLYDIARVLADLGLNIHSAKIATLGERVEDVFYVTDLDGQKLTDPeRQEALREALLEALDEEAE 864
|
|
| glnD |
PRK01759 |
bifunctional uridylyltransferase/uridylyl-removing protein GlnD; |
60-886 |
0e+00 |
|
bifunctional uridylyltransferase/uridylyl-removing protein GlnD;
Pssm-ID: 234980 [Multi-domain] Cd Length: 854 Bit Score: 1037.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 60 QLIEARTEFIDQLLQRLWIDYGFGQISDVALVAVGGYGRGELHPLSDIDLLILSRKKLPDEQAQKIGELLTLLWDVKLEV 139
Cdd:PRK01759 29 ELIENRSDFYDQLLIHLWQQFGLEEQSDLALIAVGGYGRREMFPLSDLDILILTEQPPDEETEEKINQFFQFLWDCGFEV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 140 GHSVRTLEECLLEGLSDLTVATNLIETRLLIGDVALFLELQKHIFSDGFWPSEKFFAAKVEEQNQRHQRYHGTSYNLEPD 219
Cdd:PRK01759 109 GASVRTLAECESEGRADITIATNLLESRFLTGNEKLFDALVELLQQADFWSKEAFFQAKIQEKIERYQRYHNTSYNLEPD 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 220 IKSSPGGLRDIHTLQWVARRHFGATSMDEMVGFGFLTEAERNELNECLHLLWRIRFALHLEVTRYDNRLLFDRQLSVAQR 299
Cdd:PRK01759 189 IKYSPGGLRDLHLLYWIALRHSGAKSLEEILQSGFIYPEEYAELQQSQQFLFKVRFALHLILKRYDNRLLFDRQLKVSEL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 300 LNYQGEGNEPVEHMMKDFFRVTRRVTELNQMLLQLFDEAILALTADEKPRPIDDEFQLRGTLIDLRDETLFIREPEAILR 379
Cdd:PRK01759 269 LGFQGEGNQGVEKMMKSFFQALQSISLLSDLLVKHYREHFLQPNQNVEIQPLDDDFYLINNAICLRNPDCFEQQPESILD 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 380 MFYTMVRNSTITgIYSTTLRHLRHARRHLTQPLCYIPEARSLFLSMLRHPGAVSRGLLPMHRHSVLWAYMPQWSHIVGQM 459
Cdd:PRK01759 349 LFFYLTQYPQAE-IHSTTLRQLRLALEQLQQPLCELPAARERFLRLFNQPNAIKRALVPMHQYGVLTAYLPQWKGIVGLM 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 460 QFDLFHAYTVDEHTIRVMLKLESFAKEETRSRHPLCVELWPRLTHPELILIAALFHDIAKGRGGDHSVLGAQDVLKFAEL 539
Cdd:PRK01759 428 QFDLFHIYTVDEHTLRVMLKLESFLDEESAEQHPICHQIFSQLSDRTLLYIAALFHDIAKGRGGDHAELGAVDMRQFAQQ 507
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 540 HGLNSRETQLVAWLVRHHLLMSVTAQRRDIQDPEVIKQFAEEVQTENRLRYLVCLTVADICATNETLWNSWKQSLLRELY 619
Cdd:PRK01759 508 HGFDQREIETMAWLVQQHLLMSVTAQRRDIHDPEVVMNFAEEVQNQVRLDYLTCLTVADICATNETLWNSWKRSLFATLY 587
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 620 FATEKQLRRGMQNTPDMRERVRHHQLQALALLRMDNIDEEALH--QIWARCRANYFVRHSPNQLAWHARHLLKhDLSQPM 697
Cdd:PRK01759 588 QFTNQQFQQGMDELLDYQEKAEENRQQALELLQQKYSALSETQieQLWQRCPEDYFLRNTPKQIAWHALLLLD-FRGDLL 666
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 698 ILLSPQATRGGTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDGMAMDTFIVLEPDGSPLSSDRHEGIRFGLEQ 777
Cdd:PRK01759 667 VKISNRFSRGGTEIFIYCQDQANLFLKVVSTIGAKKLSIHDAQIITSQDGYVLDSFIVTELNGKLLEFDRRRQLEQALTK 746
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 778 AITQRSWQPPQPRRQPaKLRHFTVDTEVNFLPTHTDRKSFLELIALDQPGLLARVGQVFADLGISLHGARITTIGERVED 857
Cdd:PRK01759 747 ALNTNKLKKLNLEENH-KLQHFHVKTEVRFLNEEKQEQTEMELFALDRAGLLAQVSQVFSELNLNLLNAKITTIGEKAED 825
|
810 820
....*....|....*....|....*....
gi 658548751 858 LFIIATADRRALNNDLQLEVQQRLTAALN 886
Cdd:PRK01759 826 FFILTNQQGQALDEEERKALKSRLLSNLS 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: 922.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 52 FDAGVSAEQLIEARTEFIDQLLQRLWIDYGFGQISDVALVAVGGYGRGELHPLSDIDLLILSRKKLPDEQAQKIGELLTL 131
Cdd:TIGR01693 8 FARGGDGRELREGRSDLTDLLLIRLWDFIGISEHSGIALVAVGGYGRGELAPYSDIDLLFLHDGKPAEEVEPKIERFLYP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 132 LWDVKLEVGHSVRTLEECLLEGLSDLTVATNLIETRLLIGDVALFLELQKHIFSDGFWPS-EKFFAAKVEEQNQRHQRYH 210
Cdd:TIGR01693 88 LWDLGFEVGHSVRTLEECARIAKADLTVATNLLEARHLAGDEALFFRLKERVRREDWRNTaRSFLAAKVEEQDERHARYG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 211 GTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSMDEMVGFGFLTEAERNELNECLHLLWRIRFALHLEVTRYDNRLLF 290
Cdd:TIGR01693 168 DTAYNLEPDIKEGPGGLRDLHTLFWVALYQLGVRRLEDLVKQGFLTDAEYKLLAEARDFLWDVRFALHLTTGRADDRLLF 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 291 DRQLSVAQRLNYQGEGNEPVEHMMKDFFRVTRRVTELNQMLLQLFDEAIL-----ALTADEKPRPIDDEFQLRGTLIDLR 365
Cdd:TIGR01693 248 DHQDEIAAALGYGDEGNPAVERFMRRYFQAARRIGYLTEAFLRHYEEALLsrgpsARVRRPKRRPLDEGFVEDGGELVLA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 366 DETLFIREPEAILRMFYTMVRNSTitGIYSTTLRHLRHARRHLTQPLCYIPEARSLFLSMLRHPGAVSRGLLPMHRHSVL 445
Cdd:TIGR01693 328 RTAVFERDPALLLRLFAIAAQRGL--PIHPAALRQLTASLPLLPTPLREDPEARELFLELLTSGNGTVRALRAMNRAGVL 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 446 WAYMPQWSHIVGQMQFDLFHAYTVDEHTIRVMLKLESFAKEETRSRHPLCVELWPRLTHPELILIAALFHDIAKGRGGDH 525
Cdd:TIGR01693 406 GRFLPEWGRIVGQMQFDLFHVYTVDEHTLRTVVHLAPFARGRLAREHPLASELMPKIEDPELLYLAALLHDIGKGRGGDH 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 526 SVLGAQDVLKFAELHGLNSRETQLVAWLVRHHLLMSVTAQRRDIQDPEVIKQFAEEVQTENRLRYLVCLTVADICATNET 605
Cdd:TIGR01693 486 SVLGAEDARDVCPRLGLDRPDTELVAWLVRNHLLMSITAQRRDLNDPKTVFAFAEAVGDPERLEYLLALTVADIRATGPG 565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 606 LWNSWKQSLLRELYFATEKQLRRGMQNTPDMRERVRHHQLQALALLRMDnIDEEALHQIWARCRANYFVRHSPNQLAWHA 685
Cdd:TIGR01693 566 VWNSWKASLLRDLYNRTEQVLRGGLEPPADPAEPIAEQRKLAVALLRTD-YTSNEAEVLWLRAYDDYFLRFTHKEIAWHA 644
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 686 RHLLKHDLS-QPMILLSPQATRGGTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDGMAMDTFIVLEPDGSPLS 764
Cdd:TIGR01693 645 ESLRRALSSgGPLALIDGTRPSGGTEVFIYAPDQPGLFAKVAGALAMLSLSVHDAQVNTTKDGVALDTFVVQDLFGSPPA 724
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 765 SDR-HEGIRFGLEQAITQRSWQPPQP---RRQPAKLRHFTVDTEVNFLPTHTDRKSFLELIALDQPGLLARVGQVFADLG 840
Cdd:TIGR01693 725 AERvFQELLQGLVDVLAGLAKDPDTIsarRARRRRLQHFAVPPRVTILNTASRKATIMEVRALDRPGLLARVGRTLEELG 804
|
810 820 830 840
....*....|....*....|....*....|....*....|....*
gi 658548751 841 ISLHGARITTIGERVEDLFIIATADRRALNNDLQLEVQQRLTAAL 885
Cdd:TIGR01693 805 LSIQSAKITTFGEKAEDVFYVTDLFGLKLTDEEEQRLLEVLAASV 849
|
|
| glnD |
PRK00275 |
PII uridylyl-transferase; Provisional |
48-881 |
0e+00 |
|
PII uridylyl-transferase; Provisional
Pssm-ID: 234709 [Multi-domain] Cd Length: 895 Bit Score: 877.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 48 LGSAFDAGVSAEQLIEARTEFIDQLLQRLWIDYGFGQISDVALVAVGGYGRGELHPLSDIDLLILSRKKLPDEQAQKIGE 127
Cdd:PRK00275 39 LDERFRSGRDIRRLIEDRAWFVDQILQQAWHQFDWSDDADIALVAVGGYGRGELHPYSDIDLLILLDSADHEEFREPIER 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 128 LLTLLWDVKLEVGHSVRTLEECLLEGLSDLTVATNLIETRLLIGDVALFLELQKHIFSDGFWPSEKFFAAKVEEQNQRHQ 207
Cdd:PRK00275 119 FLTLLWDIGLEIGQSVRSVDECAEEARADLTVITNLMESRTIAGPESLRQRMLEVTSSEHMWPSKEFFLAKRAEQKARHH 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 208 RYHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSMDEMVGFGFLTEAERNELNECLHLLWRIRFALHLEVTRYDNR 287
Cdd:PRK00275 199 KYNDTEYNLEPNVKGSPGGLRDIQTILWVAKRQFGTLNLHALVGEGFLTESEYGLLASGQEFLWKVRYALHMLAGRAEDR 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 288 LLFDRQLSVAQRLNYQGEG-NEPVEHMMKDFFRVTRRVTELNQMLLQLFDEAILALTADEKPRPIDDEFQLRGTLIDLRD 366
Cdd:PRK00275 279 LLFDHQRSIATLLGYEDSDaKLAVEQFMQKYYRVVMALAELNDLILQHFEEVILAADDSGTIQPLNSRFQLRDGYIEATH 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 367 ETLFIREPEAILRMFYTMVRNSTITGIYSTTLRHLRHARRHLTQPLCYIPEARSLFLSMLRHPGAVSRGLLPMHRHSVLW 446
Cdd:PRK00275 359 PNVFKRTPFALLEIFVLMAQHPEIKGVRADTIRLLREHRHLIDDAFRNDIRNTSLFIELFKCPIGIHRNLRRMNRYGILG 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 447 AYMPQWSHIVGQMQFDLFHAYTVDEHTIRVMLKLESFAKEETRSRHPLCVELWPRLTHPELILIAALFHDIAKGRGGDHS 526
Cdd:PRK00275 439 RYLPEFGHIVGQMQHDLFHIYTVDAHTLNLIKNLRKLRYPEVSEKFPLASKLMGRLPKPELLYIAGLYHDIGKGRGGDHS 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 527 VLGAQDVLKFAELHGLNSRETQLVAWLVRHHLLMSVTAQRRDIQDPEVIKQFAEEVQTENRLRYLVCLTVADICATNETL 606
Cdd:PRK00275 519 ELGAVDAEAFCQRHQLPAWDTRLVVWLVENHLLMSTTAQRKDLSDPQVIHDFALKVGDQTHLDYLYVLTVADINATNPTL 598
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 607 WNSWKQSLLRELYFATEKQLRRGMQNTPDMRERVRHHQLQALALLRMDNIDEEALHQIWARCRANYFVRHSPNQLAWHAR 686
Cdd:PRK00275 599 WNSWRASLLRQLYTETKRALRRGLENPVDREEQIRQTQSAALDILVRKGTDPDDAEQLWSQLGDDYFLRHTAGDIAWHTE 678
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 687 HLLKH-DLSQPMILLSPQATR---GGTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDGMAMDTFIVLEPDGSP 762
Cdd:PRK00275 679 AILQHpDDGGPLVLIKETTQRefeGGTQIFIYAPDQHDFFAATVAAMDQLNLNIHDARIITSSSQFTLDTYIVLDDDGEP 758
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 763 LSSD--RHEGIRFGLEQAITQRSWQPPQ-PRRQPAKLRHFTVDTEVNFLPTHTDRKSFLELIALDQPGLLARVGQVFADL 839
Cdd:PRK00275 759 IGDNpaRIEQIREGLTEALRNPDDYPTIiQRRVPRQLKHFAFPTQVTISNDAQRPVTVLEIIAPDRPGLLARIGRIFLEF 838
|
810 820 830 840
....*....|....*....|....*....|....*....|...
gi 658548751 840 GISLHGARITTIGERVEDLFIIATADRRALNN-DLQLEVQQRL 881
Cdd:PRK00275 839 DLSLQNAKIATLGERVEDVFFITDADNQPLSDpQLCSRLQDAI 881
|
|
| PRK03059 |
PRK03059 |
PII uridylyl-transferase; Provisional |
51-886 |
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 658548751 51 AFDAGVSAEQLIEARTEFIDQLLQRLWIDYGFGQisDVALVAVGGYGRGELHPLSDIDLLILSRKKLPDEQAQKIGELLT 130
Cdd:PRK03059 27 RFRQAPNVTALLHALSRLVDQALRRLWQECGLPA--GAALVAVGGYGRGELFPYSDVDLLVLLPDAPDAALDARIERFIG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 131 LLWDVKLEVGHSVRTLEECLLEGLSDLTVATNLIETRLLIGDVALFLELQKHIFSDgfWPSEKFFAAKVEEQNQRHQRYH 210
Cdd:PRK03059 105 LCWDLGLEIGSSVRTVDECIEEAAQDVTVQTSLLEARLLTGSAALFERFQRRYRAA--LDPRAFFQAKLLEMRQRHAKFQ 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 211 GTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSMDEMVGFGFLTEAERNELNECLHLLWRIRFALHLEVTRYDNRLLF 290
Cdd:PRK03059 183 DTPYSLEPNCKESPGGLRDLQTILWIARAAGLGSSWRELAKRGLITDREARQLRRNERFLKTLRARLHLLAGRREDRLVF 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 291 DRQLSVAQRLNYQGEGNE-PVEHMMKDFFRVTRRVTELNQMLLQLFDEAILALTaDEKPRPIDDEFQLRGTLIDLRDETL 369
Cdd:PRK03059 263 DLQTALAESFGYRPTAAKrASEQLMRRYYWAAKAVTQLNTILLQNIEARLFPST-SGITRVINERFVEKQGMLEIASDDL 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 370 FIREPEAILRMFYTMVRNSTITGIYSTTLRHLRHARRHLTQPLCYIPEARSLFLSMLRHPGAVSRGLLPMHRHSVLWAYM 449
Cdd:PRK03059 342 FERHPHAILEAFLLYQQTPGLKGLSARTLRALYNARDVMNAAFRRDPVNRALFMQILQQPRGITHALRLMNQTSVLGRYL 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 450 PQWSHIVGQMQFDLFHAYTVDEHTIRVMLKLESFAKEETRSRHPLCVELWPRLTHPELILIAALFHDIAKGRGGDHSVLG 529
Cdd:PRK03059 422 PNFRRIVGQMQHDLFHVYTVDQHILMVLRNLRRFAMAEHAHEYPFCSQLIANFDRPWLLYVAALFHDIAKGRGGDHSTLG 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 530 AQDVLKFAELHGLNSRETQLVAWLVRHHLLMSVTAQRRDIQDPEVIKQFAEEVQTENRLRYLVCLTVADICATNETLWNS 609
Cdd:PRK03059 502 AVDARRFCRQHGLAREDAELVVWLVEHHLTMSQVAQKQDLSDPEVIARFAELVGDERRLTALYLLTVADIRGTSPKVWNA 581
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 610 WKQSLLRELYFATEKQLRRGmqnTPDMRERVRHHQLQALALLRMDNIDEEALHQIWARCRANYFVRHSPNQLAWHARHLL 689
Cdd:PRK03059 582 WKGKLLEDLYRATLRVLGGA---APDAHSELEARKEEALALLRLEALPDDAHEALWDQLDVGYFLRHDAADIAWHTRHLY 658
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 690 KH-DLSQPMILLSPQATRGGTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDGMAMDTFIVLEPDGSPLSSDRH 768
Cdd:PRK03059 659 RHvDTDTPIVRARLSPAGEGLQVMVYTPDQPDLFARICGYFDRAGFSILDARVHTTRHGYALDTFQVLDPEEDVHYRDII 738
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 769 EGIRFGLEQAIT-QRSWQPPQPRRQPAKLRHFTVDTEVNFLPTHTDRKSFLELIALDQPGLLARVGQVFADLGISLHGAR 847
Cdd:PRK03059 739 NLVEHELAERLAeQAPLPEPSKGRLSRQVKHFPITPRVDLRPDERGQYYILSVSANDRPGLLYAIARVLAEHRVSVHTAK 818
|
810 820 830
....*....|....*....|....*....|....*....
gi 658548751 848 ITTIGERVEDLFIIATADRRalNNDLQLEVQQRLTAALN 886
Cdd:PRK03059 819 INTLGERVEDTFLIDGSGLS--DNRLQIQLETELLDALA 855
|
|
| PRK05092 |
PRK05092 |
PII uridylyl-transferase; Provisional |
88-859 |
0e+00 |
|
PII uridylyl-transferase; Provisional
Pssm-ID: 235342 [Multi-domain] Cd Length: 931 Bit Score: 572.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 88 VALVAVGGYGRGELHPLSDIDLLILsrkkLPDEQ---AQKIGE-LLTLLWDVKLEVGHSVRTLEECLLEGLSDLTVATNL 163
Cdd:PRK05092 106 LAVLAVGGYGRGELAPGSDIDLLFL----LPYKQtawAESVVEyMLYMLWDLGLKVGHATRSIDECIRLAREDMTIRTAL 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 164 IETRLLIGDVALFLELQKHIFSDGFWPSEK-FFAAKVEEQNQRHQRYHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFG 242
Cdd:PRK05092 182 LEARFLAGDRALFEELETRFDKEVVKGTAAeFVAAKLAERDERHRRAGDSRYLVEPNVKEGKGGLRDLHTLFWIAKYVYR 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 243 ATSMDEMVGFGFLTEAERNELNECLHLLWRIRFALHLEVTRYDNRLLFDRQLSVAQRLNYQG-EGNEPVEHMMKDFFRVT 321
Cdd:PRK05092 262 VRDAAELVKLGVFTREEYRLFRRAEDFLWAVRCHLHFLTGRAEERLSFDLQPEIAERMGYTDhPGLSGVERFMKHYFLVA 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 322 RRVTELNQMLL------QLFDEAILALTADEKPR-PIDDEFQLRGTLIDLRDETLFIREPEAILRMFYTMVRNSTitGIY 394
Cdd:PRK05092 342 KDVGDLTRIFCaaleaqHAKRAPGLNRFARRRRKaLDSDGFVVDNGRINLADPDVFERDPVNLIRLFHLADRHGL--DIH 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 395 STTLRHLRHARRHLTQPLCYIPEARSLFLSMLRHPGAVSRGLLPMHRHSVLWAYMPQWSHIVGQMQFDLFHAYTVDEHTI 474
Cdd:PRK05092 420 PDAMRLVTRSLRLIDAALREDPEANRLFLDILTSRRNPERVLRRMNEAGVLGRFIPDFGRIVAMMQFNMYHHYTVDEHTI 499
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 475 RVMLKLESFAKEETRSRHPLCVELWPRLTHPELILIAALFHDIAKGRGGDHSVLGAQDVLKFAELHGLNSRETQLVAWLV 554
Cdd:PRK05092 500 RAIGVLAEIERGELADEHPLASELMPKIESRRALYVAVLLHDIAKGRPEDHSIAGARIARRLCPRLGLSPAETETVAWLV 579
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 555 RHHLLMSVTAQRRDIQDPEVIKQFAEEVQTENRLRYLVCLTVADICATNETLWNSWKQSLLRELYFATEKQLRRGMQNTp 634
Cdd:PRK05092 580 EHHLLMSDTAQKRDLSDPKTIEDFADAVQSPERLKLLLILTVADIRAVGPGVWNGWKAQLLRTLYYETEEVLTGGFSEL- 658
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 635 DMRERVRHHQLQALALLRmdNIDEEALHQIWARCRANYFVRHSPNQLAWHARHL--LKHDLSQPMILLSPQATRGGTEIF 712
Cdd:PRK05092 659 NRAERVAAAKEALREALS--DWPKADRDAYLARHYPAYWLAVDLDTQARHARFIrdADDAGRPLATEVRPDPARGVTEVT 736
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 713 IWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDGMAMDTFIVLEPDGSPLSSDRHEG-IRFGLEQAITQRSWQPPQPRR 791
Cdd:PRK05092 737 VLAADHPGLFSRIAGACAAAGANIVDARIFTTTDGRALDTFWIQDAFGRDEDEPRRLArLAKAIEDALSGEVRLPEALAK 816
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 658548751 792 QP---AKLRHFTVDTEVNFLPTHTDRKSFLELIALDQPGLLARVGQVFADLGISLHGARITTIGERVEDLF 859
Cdd:PRK05092 817 RTkpkKRARAFHVPPRVTIDNEASNRFTVIEVNGRDRPGLLYDLTRALSDLNLNIASAHIATYGERAVDVF 887
|
|
| PRK04374 |
PRK04374 |
[protein-PII] uridylyltransferase; |
52-888 |
0e+00 |
|
[protein-PII] uridylyltransferase;
Pssm-ID: 179839 [Multi-domain] Cd Length: 869 Bit Score: 568.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 52 FDAGVSAEQLIEARTEFIDQLLQRLWiDYGFGQISDVALVAVGGYGRGELHPLSDIDLLILSRKKLPDEQAQKIGELLTL 131
Cdd:PRK04374 38 FDQGEPIERLLALRARAVDQLMRNAW-TRCIPADSGLSLHAVGGYGRGELFPRSDVDLLVLGETAAQQRHEQALARLFAL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 132 LWDVKLEVGHSVRTLEECLlEGLSDLTVATNLIETRLLIGDVALFLELQKHIFSDGFWPSEKFFAAKVEEQNQRHQRYHG 211
Cdd:PRK04374 117 LWDVGLPISHAVRSPAQCT-AAAADQTVLTALIESRPLVADAAARAALAAAIAPQQVWPPRAFFQAKREELLARHQRFGD 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 212 TSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSMDEMVGFGFLTEAERNELNECLHLLWRIRFALHLEVTRYDNRLLFD 291
Cdd:PRK04374 196 TADNLEPDIKDGPGGLRDLQTLGWMALRAFGVKDLEALVGLGHVGCDEAAALRREREELARLRFGLHLVANRPEERLRFD 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 292 RQLSVAQRLNYQGEG-NEPVEHMMKDFFRVTRRVTELNQMLLQLFDEAilaLTADEKPRPIDDEFQLRGTLIDLRDETLF 370
Cdd:PRK04374 276 YQKTLAERLGFADDPeSLGVEKMMQRFYRSAALIRRISDRLLQRFEEQ---FDGEATPEPLGGGFSLRRGYLAADADSWP 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 371 IREPEAILRMFYTMVRNSTITGIYSTTLRHLRHARRHLTQPLCYIPEARSLFLSMLRHPGAVSRgLLPMHRHSVLWAYMP 450
Cdd:PRK04374 353 DGDVLQVFALFAQWAAHREVRGLHSLTARALAEVLRDLPAYDVADATARERFMALLRGPRAVET-LNRMARLGVLGQWIP 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 451 QWSHIVGQMQFDLFHAYTVDEHTIRVMLKLESFAKEETRSRHPLCVELWPRLTHPELILIAALFHDIAKGRGGDHSVLGA 530
Cdd:PRK04374 432 AFASVSGRMQFDLFHVYTVDQHTLMVLRNIALFAAGRADERFSIAHEVWPRLRKPELLLLAGLFHDIAKGRGGDHSELGA 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 531 QDVLKFAELHGLNSRETQLVAWLVRHHLLMSVTAQRRDIQDPEVIKQFAEEVQTENRLRYLVCLTVADICATNETLWNSW 610
Cdd:PRK04374 512 VDARAFCLAHRLSEGDTELVTWLVEQHLRMSVTAQKQDISDPEVIHRFATLVGTRERLDYLYLLTCADIAGTSPKLWNAW 591
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 611 KQSLLRELYFATEKQLRRGMQNTPDMRERVRHHQLQALALLRMDNIDEEALHQIWARCRANYFVRHSPNQLAWHARHLLK 690
Cdd:PRK04374 592 KDRLLADLYFAARRALREGLEHPPPREERLREARESARALMQAQGHDDATIDRQFAGMPDENFLRFRPEQLAWQAASLIE 671
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 691 HDLSQPMILLSPQAT-RGGTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDGMAMDTFIVLEPDGSplSSDRHE 769
Cdd:PRK04374 672 VEIGQTLVKARRAVPdNDALEVFVYSPDRDGLFAAIVATLDRKGYGIHRARVLDAPHDAIFDVFEVLPQDTY--ADGDPQ 749
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 770 GIRFGLEQAITQRSWQ-PPQPRRQPAKLRHFTVDTEVNFLPTHTDRKSFLELIALDQPGLLARVGQVFADLGISLHGARI 848
Cdd:PRK04374 750 RLAAALRQVLAGDLQKvRPARRAVPRQLRHFRFAPRVEFSESAGGRRTRISLVAPDRPGLLADVAHVLRMQHLRVHDARI 829
|
810 820 830 840
....*....|....*....|....*....|....*....|
gi 658548751 849 TTIGERVEDLFIIATADRRALNNDLQLEVQQRLTAALNPN 888
Cdd:PRK04374 830 ATFGERAEDQFQITDEHDRPLSESARQALRDALCACLDPV 869
|
|
| PRK03381 |
PRK03381 |
PII uridylyl-transferase; Provisional |
53-883 |
8.37e-85 |
|
PII uridylyl-transferase; Provisional
Pssm-ID: 235123 [Multi-domain] Cd Length: 774 Bit Score: 288.04 E-value: 8.37e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 53 DAGVSAEQLIEARTEFIDQLLQRLWIDYGFGQISDVALVAVGGYGRGELHPLSDIDLLILSRKKLPDEQAQKIGELLTLL 132
Cdd:PRK03381 23 GGHLDGAALRAALADLHEFWLAGLAAEAGIADGSGVALVAVGGLGRRELLPYSDLDLVLLHDGRPADDVAEVADRLWYPL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 133 WDVKLEVGHSVRTLEECLLEGLSDLTVATNLIETRLLIGDVALFLELQKHIFSDgfWPSE--KFFAAKVEEQNQRHQRYH 210
Cdd:PRK03381 103 WDAGIRLDHSVRTVPEALKVAGSDLKAALGLLDARHIAGDADLSALLIGGVRRQ--WRNGarRRLPELVELTRARWERSG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 211 GTSYNLEPDIKSSPGGLRDIHTLQWVARRHfgatsmdemvgfgfLTEAERNELNECLHLLWRIRFALHLEVTRYDNRLLF 290
Cdd:PRK03381 181 EIAHLAEPDLKEGRGGLRDVQLLRALAAAQ--------------LADAPGGGLDAAHRRLLDVRTELHRVSGRGRDRLLA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 291 DRQLSVAQRLNYQG---------EGNEPVEHMMKDFFRVTRRVtelnqmllqLFDEAILALTADEKPRPIDD-------E 354
Cdd:PRK03381 247 QEADEVAAALGLGDrfdlaralsDAARTISYAVDVGWRTAANA---------LPRRGLSALRRRPVRRPLDEgvvehagE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 355 FQLRGTLIDLRDETLFIREPEAilrmfytmvrnSTITG--IYSTTLRHLRHARRHLTQPlcYIPEARSLFLSMLrhpgAV 432
Cdd:PRK03381 318 VVLARDARPARDPGLVLRVAAA-----------AATTGlpIAAATLSRLAASAPPLPTP--WPAEARDDLLVLL----GA 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 433 SRGLLP----MHRHSVLWAYMPQWSHIVGQMQFDLFHAYTVDEHTIRVMLKLESFAKEETRsrhplcvelwprlthPELI 508
Cdd:PRK03381 381 GPAAVAvieaLDRTGLWGRLLPEWEAVRDLPPRDPVHRWTVDRHLVETAVRAAALTRRVAR---------------PDLL 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 509 LIAALFHDIAKGRGGDHSVLGAQDVLKFAELHGLNSRETQLVAWLVRHHLLMSVTAQRRDIQDPEVIKQFAEEVQTENR- 587
Cdd:PRK03381 446 LLGALLHDIGKGRGGDHSVVGAELARQIGARLGLSPADVALLSALVRHHLLLPETATRRDLDDPATIEAVAEALGGDPVl 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 588 LRYLVCLTVADICATNETLWNSWKQSLLRELYfatekqlrrgmqntpdmrERVRhhqlqalALLrmdniDEEALHQiwar 667
Cdd:PRK03381 526 LELLHALTEADSLATGPGVWSDWKASLVGDLV------------------RRCR-------AVL-----AGEPLPE---- 571
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 668 cranyfvrhsPNQLAWHARHLLKHDlsQPMILLSPqATRGGTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTrDG 747
Cdd:PRK03381 572 ----------PEPLDPAQLALAADG--GVHVEIAP-ADPHMVEVTVVAPDRRGLLSKAAGVLALHRLRVRSASVRSH-DG 637
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 748 MAMDTFIVLEPDGSPLSSDRhegIRFGLEQAIT------------QRSWQPPQPRRQPAKLRhftvdteVNFLPTHTDRK 815
Cdd:PRK03381 638 VAVLEFVVSPRFGSPPDAAL---LRQDLRRALDgdldvlarlaarEAAAAAVPVRRPAAPPR-------VLWLDGASPDA 707
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 658548751 816 SFLELIALDQPGLLARVGQVFADLGISLHGARITTIGERVEDLFIIATADRRALnNDLQLEVQQRLTA 883
Cdd:PRK03381 708 TVLEVRAADRPGLLARLARALERAGVDVRWARVATLGADVVDVFYVTGAAGGPL-ADARAAVEQAVLA 774
|
|
| GlnD_UR_UTase |
pfam08335 |
GlnD PII-uridylyltransferase; This is a family of bifunctional uridylyl-removing enzymes ... |
193-332 |
8.01e-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: 169.30 E-value: 8.01e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 193 KFFAAKVEEQNQRHQRYHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSMDEMVGFGFLTEAERNELNECLHLLWR 272
Cdd:pfam08335 1 RFMKAKIEEQVARHGRYGDTAYNLEPNIKLGPGGLRDIEFIVWIAQLIFTLRALEELVELGLLTREEARELRRAYRFLRR 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 273 IRFALHLEVTRYDNRLLFDRQLSVAQRLNYQGEGNEPVEHMMKDFFRVTRRVTELNQMLL 332
Cdd:pfam08335 81 VRHRLHLLADRQTDRLPFDLQRRLARALGYARDGWLAVERFMRRLFRHAHRVSRLFEILL 140
|
|
| glnD |
PRK00227 |
[protein-PII] uridylyltransferase; |
57-636 |
1.88e-37 |
|
[protein-PII] uridylyltransferase;
Pssm-ID: 178937 [Multi-domain] Cd Length: 693 Bit Score: 150.30 E-value: 1.88e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 57 SAEQLIEARTEFIDQLLQRLWIDYGFgqisdvALVAVGGYGRGELHPLSDIDLLILSRkklPDEQAQKIGELLTLLWDVK 136
Cdd:PRK00227 3 TPAQLREDAEASALALLGSLQLPPGT------ALAATGSLARREMTPYSDLDLILLHP---PGATPDGVEDLWYPIWDAK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 137 LEVGHSVRTLEECLLEGLSDLTVATNLIETRLLIGDVALFLELQKHIFSDgfWPSE--KFFAAKVEEQNQRHQRYHGTSY 214
Cdd:PRK00227 74 KRLDYSVRTPQECAAMISADSTAALALLDLRFVAGDEQLTASTRAKILEK--WRRElnKNFDAVVDTAIARWRRSGSVVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 215 NLEPDIKSSPGGLRDIHTLQWVArrhfgatsmdemvgFGFLTEAERneLNECLHLLWRIRFALHLEVTRydNRLLFDRQL 294
Cdd:PRK00227 152 MTRPDLKHGRGGLRDIELIRALA--------------LGHLCDAPP--LDSQHQLLLDVRTLLHVHARR--ARDVLDPEF 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 295 SVAQRLNYqgeGNEPVEHMMKDFFRVTRRVTELNQMLLQLFDEAILALTADEKP--RPID-DEFQLRGTLIDLRDETLfi 371
Cdd:PRK00227 214 AVDIALDL---GFVDRYHLSREIADAARAIDDALTAALATARGALPRRTAFRNAvrRPLDvDVVDANGTIALSRTPDL-- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 372 REPEAILRMFYTMVRnsTITGIYSTTLRHLRHARRhLTQPlcYIPEARSLFLSMLRHPGAVSRGLLPMHRHSVLWAYMPQ 451
Cdd:PRK00227 289 DDPALPLRVAAAAAR--TGLPVSESVWKRLEECPE-LPEP--WPASAAGDFFRLLSSPVNSRRVIKQMDRHGLWERIVPE 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 452 WSHIVGQMQFDLFHAYTVDEHTIRVMLKlesfakeetrsrhplCVELWPRLTHPELILIAALFHDIAKGRGGDHSVLGAQ 531
Cdd:PRK00227 364 WDRIRGLMPREPSHIHTIDEHSLNTVAN---------------CALETVTVARPDLLLLGALYHDIGKGYPRPHEQVGAE 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 532 DVLKFAELHGLNSRETQLVAWLVRHHLLMSVTAQRRDIQDPEVIKQFAEEVQTEN-RLRYLVCLTVADICATNETLWNSW 610
Cdd:PRK00227 429 MVARAARRMGLNLRDRAVVQTLVAEHTTLARIAGRLDPTSEEAVDKLLDAVRYDLlTLNLLEVLTEADAEGTGPGVWTAR 508
|
570 580
....*....|....*....|....*.
gi 658548751 611 KQSLLRELYFATEKQLRRGMQNTPDM 636
Cdd:PRK00227 509 LEQGLRIVCSRARARLTDIRPVAPMF 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 |
1.71e-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: 108.72 E-value: 1.71e-28
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 658548751 708 GTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDGMAMDTFIVLEPDGSPLSS-DRHEGIRFGLEQAI 779
Cdd:cd04900 1 GTEVFIYTPDRPGLFARIAGALDQLGLNILDARIFTTRDGYALDTFVVLDPDGEPIGErERLARIREALEDAL 73
|
|
| NT_GlnE_GlnD_like |
cd05401 |
Nucleotidyltransferase (NT) domain of Escherichia coli adenylyltransferase (GlnE), Escherichia ... |
52-184 |
2.43e-24 |
|
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: 100.49 E-value: 2.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 52 FDAGVSAEQLIEARTEFIDQLLQRLW----IDYGFG-QISDVALVAVGGYGRGELHPLSDIDLLILSRKKLPDEQ----- 121
Cdd:cd05401 15 LLGGASIRAISRALSDLADALLRRALelalAELGKGpPPVPFALLALGSYGRGELNPSSDQDLLLLYDDDGDEVAayfee 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 658548751 122 -AQKIGELLTL------LWDVKLEVGHSVRTLEECLLEGLSDLTV------ATNLIETRLLIGDVALFLELQKHIF 184
Cdd:cd05401 95 lAERLIKILSEaggpycLGDVMLRPPGWRRSLAEWLDAARDWLTEpgrlweRTALLDARPVAGDRALAEELRRRIR 170
|
|
| ACT_ACR-UUR-like_2 |
cd04899 |
C-terminal ACT domains of the bacterial signal-transducing uridylyltransferase ... |
818-885 |
1.68e-23 |
|
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: 94.44 E-value: 1.68e-23
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 658548751 818 LELIALDQPGLLARVGQVFADLGISLHGARITTIGERVEDLFIIATADRRALNNDLQLEVQQRLTAAL 885
Cdd:cd04899 3 LELTALDRPGLLADVTRVLAELGLNIHSAKIATLGERAEDVFYVTDADGQPLDPERQEALRAALGEAL 70
|
|
| ACT_UUR-ACR-like |
cd04873 |
ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) ... |
818-885 |
3.30e-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: 82.21 E-value: 3.30e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 658548751 818 LELIALDQPGLLARVGQVFADLGISLHGARITTIGERVEDLFIIATADRRALNNDLQLEVQQRLTAAL 885
Cdd:cd04873 3 VEVYAPDRPGLLADITRVLADLGLNIHDARISTTGERALDVFYVTDSDGRPLDPERIARLEEALEDAL 70
|
|
| ACT_UUR-ACR-like |
cd04873 |
ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) ... |
709-779 |
1.07e-18 |
|
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: 80.67 E-value: 1.07e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 658548751 709 TEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDgMAMDTFIVLEPDGSPLSSDRHEGIRFGLEQAI 779
Cdd:cd04873 1 TVVEVYAPDRPGLLADITRVLADLGLNIHDARISTTGE-RALDVFYVTDSDGRPLDPERIARLEEALEDAL 70
|
|
| HD |
pfam01966 |
HD domain; HD domains are metal dependent phosphohydrolases. |
469-575 |
2.03e-10 |
|
HD domain; HD domains are metal dependent phosphohydrolases.
Pssm-ID: 460398 [Multi-domain] Cd Length: 110 Bit Score: 58.79 E-value: 2.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 469 VDEHTIRVMLKLESFAKEETRsrhplcvelwprlTHPELILIAALFHDIAKGRGGD----------HSVLGAQDVLKFAE 538
Cdd:pfam01966 1 RLEHSLRVALLARELAEELGE-------------LDRELLLLAALLHDIGKGPFGDekpefeiflgHAVVGAEILRELEK 67
|
90 100 110
....*....|....*....|....*....|....*..
gi 658548751 539 LHGLnsretQLVAWLVRHHLLMSVTAQRRDIQDPEVI 575
Cdd:pfam01966 68 RLGL-----EDVLKLILEHHESWEGAGYPEEISLEAR 99
|
|
| HDc |
smart00471 |
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ... |
465-612 |
7.02e-09 |
|
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: 54.61 E-value: 7.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 465 HAYTVDEHTIRVMLKLESFAKEEtrsrhplcvelwpRLTHPELILIAALFHDIAKGRGGD-----------HSVLGAQDV 533
Cdd:smart00471 1 SDYHVFEHSLRVAQLAAALAEEL-------------GLLDIELLLLAALLHDIGKPGTPDsflvktsvledHHFIGAEIL 67
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 658548751 534 LKFAElhglNSRETQLVAWLVRHHLLMSVTaqrrdiqdpevikqfaeeVQTENRLRYLVCLTVADICATNETLWNSWKQ 612
Cdd:smart00471 68 LEEEE----PRILEEILRTAILSHHERPDG------------------LRGEPITLEARIVKVADRLDALRADRRYRRV 124
|
|
| ACT |
pfam01842 |
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ... |
818-867 |
2.06e-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: 48.84 E-value: 2.06e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 658548751 818 LELIALDQPGLLARVGQVFADLGISLHGARITTIGERVEDLFIIATADRR 867
Cdd:pfam01842 3 LEVLVPDRPGLLARVLGALADRGINITSIEQGTSEDKGGIVFVVIVVDEE 52
|
|
| HDc |
cd00077 |
Metal dependent phosphohydrolases with conserved 'HD' motif |
467-619 |
2.32e-07 |
|
Metal dependent phosphohydrolases with conserved 'HD' motif
Pssm-ID: 238032 [Multi-domain] Cd Length: 145 Bit Score: 50.80 E-value: 2.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 467 YTVDEHTIRVMLKLESFAKEETRSRHPlcvelwprlthPELILIAALFHDIAKG------------RGGDHSVLGAQDVL 534
Cdd:cd00077 1 EHRFEHSLRVAQLARRLAEELGLSEED-----------IELLRLAALLHDIGKPgtpdaiteeeseLEKDHAIVGAEILR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658548751 535 KFaelhgLNSRETQLVAWLVRHHLLMsvTAQRRDIQDPEVIKqfaeevQTENRLRYLVCLTVADIC-ATNETLWNSWKQS 613
Cdd:cd00077 70 EL-----LLEEVIKLIDELILAVDAS--HHERLDGLGYPDGL------KGEEITLEARIVKLADRLdALRRDSREKRRRI 136
|
....*.
gi 658548751 614 LLRELY 619
Cdd:cd00077 137 AEEDLE 142
|
|
| NTP_transf_2 |
pfam01909 |
Nucleotidyltransferase domain; Members of this family belong to a large family of ... |
86-151 |
2.52e-07 |
|
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: 49.34 E-value: 2.52e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 658548751 86 SDVALVAVGGYGRGELHPLSDIDLLILSRKKLPDEQAQKIGELLTLL-WDVKLEVGHSVRTLEECLL 151
Cdd:pfam01909 13 PVAEVVLFGSYARGTALPGSDIDLLVVFPEPVEEERLLKLAKIIKELeELLGLEVDLVTREKIEFPL 79
|
|
| ACT_ACR-UUR-like_2 |
cd04899 |
C-terminal ACT domains of the bacterial signal-transducing uridylyltransferase ... |
709-779 |
2.97e-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: 48.22 E-value: 2.97e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 658548751 709 TEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIfTTRDGMAMDTFIVLEPDGSPLSSDRHEGIRFGLEQAI 779
Cdd:cd04899 1 TVLELTALDRPGLLADVTRVLAELGLNIHSAKI-ATLGERAEDVFYVTDADGQPLDPERQEALRAALGEAL 70
|
|
| 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 |
7.41e-06 |
|
ACT domain family, ACT_UUR-like_1, includes the first of two C-terminal ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) enzyme, GlnD and related domains; This ACT domain family, ACT_UUR-like_1, includes the first of two C-terminal ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) enzyme, GlnD; including those enzymes similar to the GlnD found in enteric Escherichia coli and those found in photosynthetic, nitrogen-fixing bacterium Rhodospirillum rubrum. Also included in this CD is the N-terminal ACT domain of a yet characterized Arabidopsis/Oryza predicted tyrosine kinase. Members of this CD belong to the superfamily of ACT regulatory domains.
Pssm-ID: 153172 [Multi-domain] Cd Length: 73 Bit Score: 44.39 E-value: 7.41e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 658548751 824 DQPGLLARVGQVFADLGISLHGARI-TTIGERVEDLFIIATADRRALNNDLQL-EVQQRLTAAL 885
Cdd:cd04900 10 DRPGLFARIAGALDQLGLNILDARIfTTRDGYALDTFVVLDPDGEPIGERERLaRIREALEDAL 73
|
|
| ACT |
cd02116 |
ACT domains are commonly involved in specifically binding an amino acid or other small ligand ... |
818-874 |
8.47e-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: 8.47e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 658548751 818 LELIALDQPGLLARVGQVFADLGISLHGARITTIGERVEDLFIIATADRRALNNDLQ 874
Cdd:cd02116 1 LTVSGPDRPGLLAKVLSVLAEAGINITSIEQRTSGDGGEADIFIVVDGDGDLEKLLE 57
|
|
| ACT |
cd02116 |
ACT domains are commonly involved in specifically binding an amino acid or other small ligand ... |
711-760 |
1.57e-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: 1.57e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 658548751 711 IFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDGMAMDTFIVLEPDG 760
Cdd:cd02116 1 LTVSGPDRPGLLAKVLSVLAEAGINITSIEQRTSGDGGEADIFIVVDGDG 50
|
|
| MJ0604 |
COG1708 |
Predicted nucleotidyltransferase, MJ0604 family [General function prediction only]; |
67-132 |
8.62e-05 |
|
Predicted nucleotidyltransferase, MJ0604 family [General function prediction only];
Pssm-ID: 441314 Cd Length: 95 Bit Score: 42.32 E-value: 8.62e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 658548751 67 EFIDQLLQRLwidygfGQISDVALVAV-GGYGRGELHPLSDIDLLILSRK-KLPDEQAQKIGELLTLL 132
Cdd:COG1708 7 ELLEEIVEAL------RRGPEVAAVYLfGSYARGDARPDSDIDLLVVVDDpPLPDERLELLADLLREL 68
|
|
| NT_KNTase_like |
cd05403 |
Nucleotidyltransferase (NT) domain of Staphylococcus aureus kanamycin nucleotidyltransferase, ... |
86-139 |
3.39e-04 |
|
Nucleotidyltransferase (NT) domain of Staphylococcus aureus kanamycin nucleotidyltransferase, and similar proteins; S. aureus KNTase is a plasmid encoded enzyme which confers resistance to a wide range of aminoglycoside antibiotics which have a 4'- or 4''-hydroxyl group in the equatorial position, such as kanamycin A. This enzyme transfers a nucleoside monophosphate group from a nucleotide (ATP,GTP, or UTP) to the 4'-hydroxyl group of kanamycin A. This enzyme is a homodimer, having two NT active sites. The nucleotide and antibiotic binding sites of each active site include residues from each monomer. Included in this subgroup is Escherichia coli AadA5 which confers resistance to the antibiotic spectinomycin and is a putative aminoglycoside-3'-adenylyltransferase. It is part of the aadA5 cassette of a class 1 integron. This subgroup also includes Haemophilus influenzae HI0073 which forms a 2:2 heterotetramer with an unrelated protein HI0074. Structurally HI0074 is related to the substrate-binding domain of S. aureus KNTase. The genes encoding HI0073 and HI0074 form an operon. Little is known about the substrate specificity or function of two-component NTs. The characterized members of this subgroup may not be representive of the function of this subgroup. This subgroup belongs to the Pol beta-like NT superfamily. In the majority of enzymes in this superfamily, two carboxylates, Dx[D/E], together with a third more distal carboxylate, co-ordinate two divalent metal cations involved in a two-metal ion mechanism of nucleotide addition. These carboxylate residues are conserved in this subgroup.
Pssm-ID: 143393 Cd Length: 93 Bit Score: 40.48 E-value: 3.39e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 658548751 86 SDVALVAVGG-YGRGELHPLSDIDLLILSRKKLPDEQAQKIGELLTLLWDVKLEV 139
Cdd:cd05403 16 GGVEKVYLFGsYARGDARPDSDIDLLVIFDDPLDPLELARLLEELELLLGRPVDL 70
|
|
| ACT_ACR_4 |
cd04926 |
C-terminal ACT domain, of a novel type of ACT domain-containing protein which is composed ... |
708-772 |
7.33e-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: 38.87 E-value: 7.33e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 658548751 708 GTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIfTTRDGMAMDTFIVLEPDGSPLSSDRHEGIR 772
Cdd:cd04926 1 GVRLELRTEDRVGLLSDVTRVFRENGLTVTRAEI-STQGDMAVNVFYVTDANGNPVDPKTIEAVR 64
|
|
| RnaY |
COG1418 |
HD superfamily phosphodieaserase, includes HD domain of RNase Y [Translation, ribosomal ... |
505-557 |
1.04e-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: 41.04 E-value: 1.04e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 658548751 505 PELILIAALFHDIAK----GRGGDHSVLGAQDVLKFAELHGLNSRETQLVAWLVRHH 557
Cdd:COG1418 41 VEVAKRAALLHDIGKakdhEVEGSHAEIGAELARKYLESLGFPEEEIEAVVHAIEAH 97
|
|
| ACT_ACR_2 |
cd04925 |
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats ... |
818-855 |
1.93e-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: 1.93e-03
10 20 30
....*....|....*....|....*....|....*...
gi 658548751 818 LELIALDQPGLLARVGQVFADLGISLHGARITTIGERV 855
Cdd:cd04925 3 IELTGTDRPGLLSEVFAVLADLHCNVVEARAWTHNGRL 40
|
|
| ACT_RelA-SpoT |
cd04876 |
ACT domain found C-terminal of the RelA/SpoT domains; ACT_RelA-SpoT: the ACT domain found ... |
818-880 |
2.19e-03 |
|
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: 37.43 E-value: 2.19e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 658548751 818 LELIALDQPGLLARVGQVFADLGISLHGARITTigeRVEDLFIIatadrralnnDLQLEVQQR 880
Cdd:cd04876 1 IRVEAIDRPGLLADITTVIAEEKINILSVNTRT---DDDGLATI----------RLTLEVRDL 50
|
|
| Polbeta |
pfam18765 |
Polymerase beta, Nucleotidyltransferase; A member of the nucleotidyltransferase fold found in ... |
94-137 |
2.95e-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: 37.89 E-value: 2.95e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 658548751 94 GGYGRGELHPLSDIDLLILSRKKLPDEQ----AQKIGELLTLLwDVKL 137
Cdd:pfam18765 20 GSRAKGDAREDSDIDLAVLYDEKLDFEEllelASELEDILLLR-KVDL 66
|
|
| ACT_TyrKc |
cd04928 |
Uncharacterized, N-terminal ACT domain of an Arabidopsis/Oryza predicted tyrosine kinase and ... |
710-755 |
3.00e-03 |
|
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: 3.00e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 658548751 710 EIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTTRDGMAMDTFIV 755
Cdd:cd04928 3 EITFAAGDKPKLLSQLSSLLGDLGLNIAEAHAFSTDDGLALDIFVV 48
|
|
| ACT_HSDH-Hom |
cd04881 |
ACT_HSDH_Hom CD includes the C-terminal ACT domain of the NAD(P)H-dependent, homoserine ... |
817-844 |
4.17e-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: 37.11 E-value: 4.17e-03
10 20
....*....|....*....|....*...
gi 658548751 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 ... |
818-859 |
8.63e-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: 35.79 E-value: 8.63e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 658548751 818 LELIALDQPGLLARVGQVFADLGISLHGARITTIGERVEDLF 859
Cdd:cd04926 4 LELRTEDRVGLLSDVTRVFRENGLTVTRAEISTQGDMAVNVF 45
|
|
| HDIG |
TIGR00277 |
HDIG domain; This domain is found in a few known nucleotidyltransferes and in a large number ... |
494-538 |
9.22e-03 |
|
HDIG domain; This domain is found in a few known nucleotidyltransferes and in a large number of uncharacterized proteins. It contains four widely separated His residues, the second of which is part of an invariant dipeptide His-Asp in a region matched approximately by the motif HDIG. This model may annotate homologous domains in which one or more of the His residues is conserved but misaligned, and some probable false-positive hits.
Pssm-ID: 272994 [Multi-domain] Cd Length: 80 Bit Score: 36.16 E-value: 9.22e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 658548751 494 LCVELWPrltHPELILIAALFHDIAKGR------GGDHSVLGAQDVLKFAE 538
Cdd:TIGR00277 19 LARELGL---DVELARRGALLHDIGKPItregviFESHVVVGAEIARKYGE 66
|
|
| |
