|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05092 |
PRK05092 |
PII uridylyl-transferase; Provisional |
1-931 |
0e+00 |
|
PII uridylyl-transferase; Provisional
Pssm-ID: 235342 [Multi-domain] Cd Length: 931 Bit Score: 1685.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 1 MDSVVTEDRPEADDRFDTARVTAAVDALAEKHAGREDVFRSALAQLLKAEMIAARATAQAVLLKDRHGRRCAERLCFMQD 80
Cdd:PRK05092 1 PDPPMAPRPLSLSEIFDRAALRAELDALAADAAGDPDALRAAVLALLKQALARGRAEARERLEADGSGRACARRLAYLTD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 81 EIIRILYSAATRHLYRSHVPSGAERMAVVATGGYGRGLMAPESDIDLLFILPYKQTAWGEQVAEAILYCLWDMGLKVGHA 160
Cdd:PRK05092 81 ELIRALYDFATTHLYPADNPSEGERLAVLAVGGYGRGELAPGSDIDLLFLLPYKQTAWAESVVEYMLYMLWDLGLKVGHA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 161 TRSVDECIRQARGDMTIRTAILETRFLTGDQPLYDELVARFDKDVVQGTASEFVTAKLAEREERHRRAGQSRYLVEPNVK 240
Cdd:PRK05092 161 TRSIDECIRLAREDMTIRTALLEARFLAGDRALFEELETRFDKEVVKGTAAEFVAAKLAERDERHRRAGDSRYLVEPNVK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 241 DGKGGLRDLHTLFWIAKYVYRVRETDELVERGVFDAQEYRTFRRCADFLWSVRCNLHFVSGRAEERLSFDMQREIAVRLG 320
Cdd:PRK05092 241 EGKGGLRDLHTLFWIAKYVYRVRDAAELVKLGVFTREEYRLFRRAEDFLWAVRCHLHFLTGRAEERLSFDLQPEIAERMG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 321 YTSHPGMQDVERFMKHYFLVAKDVGDLTAILCAKLEDEQAKPAPVLsrmvarLRPGAKRRRVPDSDDFIIDNNRINLAAP 400
Cdd:PRK05092 321 YTDHPGLSGVERFMKHYFLVAKDVGDLTRIFCAALEAQHAKRAPGL------NRFARRRRKALDSDGFVVDNGRINLADP 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 401 DVFKHDPVNLIRIFHLAQKNNLAFHPDAMRMVTRSLKLVNTQLRENPEANRLFMEILTS-NDAETVLRRMNETGVLGHFI 479
Cdd:PRK05092 395 DVFERDPVNLIRLFHLADRHGLDIHPDAMRLVTRSLRLIDAALREDPEANRLFLDILTSrRNPERVLRRMNEAGVLGRFI 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 480 RAFGKIVSMMQFNMYHHYTVDEHLIRCIGFLQEIERGG-NDEFTVASDLFRKIQPehRAVIYIATLLHDVAKGRPEDHSI 558
Cdd:PRK05092 475 PDFGRIVAMMQFNMYHHYTVDEHTIRAIGVLAEIERGElADEHPLASELMPKIES--RRALYVAVLLHDIAKGRPEDHSI 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 559 AGARVARRLCPRLGFSAADTELVAWLIEEHLTMSTVAQSRDLSDRKTIENFAAVVQSVEQMKLLTILTTADIRGVGPGVW 638
Cdd:PRK05092 553 AGARIARRLCPRLGLSPAETETVAWLVEHHLLMSDTAQKRDLSDPKTIEDFADAVQSPERLKLLLILTVADIRAVGPGVW 632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 639 NGWKAQLLRTLYYETEPVLTGGFSEVNRAQRIAVAQSEFRAAFTEWPEAELNAYIARHYPAYWLKVDLPRKIRQARFIRA 718
Cdd:PRK05092 633 NGWKAQLLRTLYYETEEVLTGGFSELNRAERVAAAKEALREALSDWPKADRDAYLARHYPAYWLAVDLDTQARHARFIRD 712
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 719 SEQAGHQLAINVGFDEARGVTELTILATDHPWLLSIIAGACASAGANIVDAQIYTTTDGRALDTIAISREYDRDEDEGRR 798
Cdd:PRK05092 713 ADDAGRPLATEVRPDPARGVTEVTVLAADHPGLFSRIAGACAAAGANIVDARIFTTTDGRALDTFWIQDAFGRDEDEPRR 792
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 799 ATRIGEMIEHVLEGKLRLPEVVARKAANRGKVRAFVVEPEVTINNQWSDRYTVIEVSGLDRPGLLYQLTTAISKLNLNIA 878
Cdd:PRK05092 793 LARLAKAIEDALSGEVRLPEALAKRTKPKKRARAFHVPPRVTIDNEASNRFTVIEVNGRDRPGLLYDLTRALSDLNLNIA 872
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|...
gi 1047432450 879 SAHVATFGERARDVFYVTDLLGAQITAPTRQAAIKSALIHLLSSEDNVAKPAA 931
Cdd:PRK05092 873 SAHIATYGERAVDVFYVTDLFGLKITNEARQAAIRRALLAALAEGEAEARAAR 925
|
|
| GlnD |
COG2844 |
UTP:GlnB (protein PII) uridylyltransferase [Posttranslational modification, protein turnover, ... |
41-925 |
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: 1204.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 41 SALAQLLKAEMIAARATAQAVLLKDRHGRRCAERLCFMQDEIIRilysaatrHLYRSHVPSGAERMAVVATGGYGRGLMA 120
Cdd:COG2844 1 AAALAALREALAEGRAALRERFRAGADGRELVRARAALVDQLLR--------ALWDLAGLTEPERLALVAVGGYGRGELA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 121 PESDIDLLFILPYKQTAWGEQVAEAILYCLWDMGLKVGHATRSVDECIRQARGDMTIRTAILETRFLTGDQPLYDELVAR 200
Cdd:COG2844 73 PHSDIDLLFLLPDKPTPALEEVIEAFLYLLWDLGLEVGHSVRTVDECLREAREDITVRTALLEARLLAGDEALFEELRER 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 201 FDKDVVqGTASEFVTAKLAEREERHRRAGQSRYLVEPNVKDGKGGLRDLHTLFWIAKYVYRVRETDELVERGVFDAQEYR 280
Cdd:COG2844 153 FRADVF-WDSRAFFEAKLAEQRERHAKYGDTRYNLEPNIKEGPGGLRDLQTLLWIAKRHFGVRSLEELVKKGLLTEEEYR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 281 TFRRCADFLWSVRCNLHFVSGRAEERLSFDMQREIAVRLGYTSHPGMQDVERFMKHYFLVAKDVGDLTAILCAKLEDEQA 360
Cdd:COG2844 232 ELRRAEDFLWRVRFALHLLAGRAEDRLLFDLQREVAERLGYQDTEGNRAVERFMQRYYRTAKAVGRLNEILLQRLEEAIL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 361 KPAPVlsrmvarlrpgakRRRVPDSDDFIIDNNRINLAAPDVFKHDPVNLIRIFHLAQKN--NLAFHPDAMRMVTRSLKL 438
Cdd:COG2844 312 KPPGL-------------RRPRPINEGFQLRNGRLEVADPDVFERDPVALLRLFLLAAQHpeGLGIHPDTLRLLRRALRL 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 439 VNTQLRENPEANRLFMEILTS-NDAETVLRRMNETGVLGHFIRAFGKIVSMMQFNMYHHYTVDEHLIRCIGFLQEIERG- 516
Cdd:COG2844 379 IDDAFRRDPEARRLFLEILRQpRGITRALRRMNEYGVLGRYIPEFGRIVGQMQFDLFHVYTVDEHTLRVVRNLRRFERGe 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 517 GNDEFTVASDLFRKIqpEHRAVIYIATLLHDVAKGRPEDHSIAGARVARRLCPRLGFSAADTELVAWLIEEHLTMSTVAQ 596
Cdd:COG2844 459 LAEEFPLASELIAEL--PKPELLYLAALFHDIAKGRGGDHSELGAEDARRFCPRHGLSPEDTELVAWLVRHHLLMSHTAQ 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 597 SRDLSDRKTIENFAAVVQSVEQMKLLTILTTADIRGVGPGVWNGWKAQLLRTLYYETEPVLTGGFSEVNRAQRIAVAQSE 676
Cdd:COG2844 537 RRDISDPEVIRDFARLVGSEERLDYLYLLTVADIRATGPKVWNSWKASLLRELYRATLRALRGGLEPPDREERIEERKEE 616
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 677 FRAAFTE--WPEAELNAYIARHYPAYWLKVDLPRKIRQARFIRASEQAGhQLAINVGFDEARGVTELTILATDHPWLLSI 754
Cdd:COG2844 617 ALALLADqgWDEEEIEALWARLPDDYFLRHDPEEIAWHARLLLRADDSG-KPLVLIRPDPDRGGTEVFVYTPDRPGLFAR 695
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 755 IAGACASAGANIVDAQIYTTTDGRALDTIAISREYDRDEDEGRRATRIGEMIEHVLEGKLRLPEVVARKAanRGKVRAFV 834
Cdd:COG2844 696 IAGALAALGLNILDARIHTTRDGYALDTFIVLDPDGEPIDDPDRLERIEQALEEALSGEVPLPEPLARRL--SRRLRHFP 773
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 835 VEPEVTINNQWSDRYTVIEVSGLDRPGLLYQLTTAISKLNLNIASAHVATFGERARDVFYVTDLLGAQITAPTRQAAIKS 914
Cdd:COG2844 774 VPPRVTFDNDASNRYTVLEVSALDRPGLLYDIARVLADLGLNIHSAKIATLGERVEDVFYVTDLDGQKLTDPERQEALRE 853
|
890
....*....|.
gi 1047432450 915 ALIHLLSSEDN 925
Cdd:COG2844 854 ALLEALDEEAE 864
|
|
| UTase_glnD |
TIGR01693 |
[Protein-PII] uridylyltransferase; This model describes GlnD, the uridylyltransferase ... |
55-917 |
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: 875.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 55 RATAQAVLLKDRHGRRCAERLCFMQDEIIRILYSAATRHLyrshvpsgAERMAVVATGGYGRGLMAPESDIDLLFILPYK 134
Cdd:TIGR01693 1 REELLEEFARGGDGRELREGRSDLTDLLLIRLWDFIGISE--------HSGIALVAVGGYGRGELAPYSDIDLLFLHDGK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 135 QTAWGEQVAEAILYCLWDMGLKVGHATRSVDECIRQARGDMTIRTAILETRFLTGDQPLYDELVARFDKDVVQGTASEFV 214
Cdd:TIGR01693 73 PAEEVEPKIERFLYPLWDLGFEVGHSVRTLEECARIAKADLTVATNLLEARHLAGDEALFFRLKERVRREDWRNTARSFL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 215 TAKLAEREERHRRAGQSRYLVEPNVKDGKGGLRDLHTLFWIAKYVYRVRETDELVERGVFDAQEYRTFRRCADFLWSVRC 294
Cdd:TIGR01693 153 AAKVEEQDERHARYGDTAYNLEPDIKEGPGGLRDLHTLFWVALYQLGVRRLEDLVKQGFLTDAEYKLLAEARDFLWDVRF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 295 NLHFVSGRAEERLSFDMQREIAVRLGYTShPGMQDVERFMKHYFLVAKDVGDLTAILCAKLEDEQAKPAPvlsrmVARLR 374
Cdd:TIGR01693 233 ALHLTTGRADDRLLFDHQDEIAAALGYGD-EGNPAVERFMRRYFQAARRIGYLTEAFLRHYEEALLSRGP-----SARVR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 375 pgaKRRRVPDSDDFIIDNNRINLAAPDVFKHDPVNLIRIFHLAQKNNLAFHPDAMRMVTRSLKLVNTQLRENPEANRLFM 454
Cdd:TIGR01693 307 ---RPKRRPLDEGFVEDGGELVLARTAVFERDPALLLRLFAIAAQRGLPIHPAALRQLTASLPLLPTPLREDPEARELFL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 455 EILTS-NDAETVLRRMNETGVLGHFIRAFGKIVSMMQFNMYHHYTVDEHLIRCIGFLQEIERGGN-DEFTVASDLFRKIq 532
Cdd:TIGR01693 384 ELLTSgNGTVRALRAMNRAGVLGRFLPEWGRIVGQMQFDLFHVYTVDEHTLRTVVHLAPFARGRLaREHPLASELMPKI- 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 533 pEHRAVIYIATLLHDVAKGRPEDHSIAGARVARRLCPRLGFSAADTELVAWLIEEHLTMSTVAQSRDLSDRKTIENFAAV 612
Cdd:TIGR01693 463 -EDPELLYLAALLHDIGKGRGGDHSVLGAEDARDVCPRLGLDRPDTELVAWLVRNHLLMSITAQRRDLNDPKTVFAFAEA 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 613 VQSVEQMKLLTILTTADIRGVGPGVWNGWKAQLLRTLYYETEPVLTGGFSE-VNRAQRIAVAQS-EFRAAFTEWPEAELN 690
Cdd:TIGR01693 542 VGDPERLEYLLALTVADIRATGPGVWNSWKASLLRDLYNRTEQVLRGGLEPpADPAEPIAEQRKlAVALLRTDYTSNEAE 621
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 691 AYIARHYPAYWLKVDLPRKIRQARFIRASEQAGHQLAINVGfDEARGVTELTILATDHPWLLSIIAGACASAGANIVDAQ 770
Cdd:TIGR01693 622 VLWLRAYDDYFLRFTHKEIAWHAESLRRALSSGGPLALIDG-TRPSGGTEVFIYAPDQPGLFAKVAGALAMLSLSVHDAQ 700
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 771 IYTTTDGRALDTIAISREYDRDEDEGRRATRIGEMIEHVLEGKLRLPEVVARKAANRGKVRAFVVEPEVTINNQWSDRYT 850
Cdd:TIGR01693 701 VNTTKDGVALDTFVVQDLFGSPPAAERVFQELLQGLVDVLAGLAKDPDTISARRARRRRLQHFAVPPRVTILNTASRKAT 780
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1047432450 851 VIEVSGLDRPGLLYQLTTAISKLNLNIASAHVATFGERARDVFYVTDLLGAQITApTRQAAIKSALI 917
Cdd:TIGR01693 781 IMEVRALDRPGLLARVGRTLEELGLSIQSAKITTFGEKAEDVFYVTDLFGLKLTD-EEEQRLLEVLA 846
|
|
| GlnD_UR_UTase |
pfam08335 |
GlnD PII-uridylyltransferase; This is a family of bifunctional uridylyl-removing enzymes ... |
213-351 |
1.52e-48 |
|
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: 168.53 E-value: 1.52e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 213 FVTAKLAEREERHRRAGQSRYLVEPNVKDGKGGLRDLHTLFWIAKYVYRVRETDELVERGVFDAQEYRTFRRCADFLWSV 292
Cdd:pfam08335 2 FMKAKIEEQVARHGRYGDTAYNLEPNIKLGPGGLRDIEFIVWIAQLIFTLRALEELVELGLLTREEARELRRAYRFLRRV 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1047432450 293 RCNLHFVSGRAEERLSFDMQREIAVRLGYTsHPGMQDVERFMKHYFLVAKDVGDLTAIL 351
Cdd:pfam08335 82 RHRLHLLADRQTDRLPFDLQRRLARALGYA-RDGWLAVERFMRRLFRHAHRVSRLFEIL 139
|
|
| NT_GlnE_GlnD_like |
cd05401 |
Nucleotidyltransferase (NT) domain of Escherichia coli adenylyltransferase (GlnE), Escherichia ... |
53-201 |
6.67e-25 |
|
Nucleotidyltransferase (NT) domain of Escherichia coli adenylyltransferase (GlnE), Escherichia coli uridylyl transferase (GlnD), and similar proteins; Escherichia coli GlnD and -E participate in the Glutamine synthetase (GS)/Glutamate synthase (GOGAT) pathway for the assimilation of ammonium nitrogen. In nitrogen sufficiency, GlnE adenylates GS, reducing GS activity; when nitrogen is limiting, GlnE deadenylates GS-AMP, restoring GS activity. When nitrogen is limiting, GlnD uridylylates the nitrogen regulatory protein PII to PII-UTP, and in nitrogen sufficiency, it removes the modifying groups. The activity of Escherichia coli GlnE is modulated by PII-proteins. PII-UMP promotes GlnE deadenylation activity, and PII promotes GlnE adenylation activity. Escherichia coli GlnE has two separate NT domains. The N-terminal NT domain catalyzes the deadenylylation of GS, and the C-terminal NT domain the adenylylation reaction. The majority of proteins in this family contain a C-terminal NT domain which is associated with a cystathionine beta-synthase (CBS) domain pair and a CAP_ED (cAMP receptor protein effector ) domain. This family belongs to the Pol beta-like NT superfamily. In the majority of enzymes in this superfamily, two carboxylates, Dx[D/E], together with a third more distal carboxylate, coordinate two divalent metal cations involved in a two-metal ion mechanism of nucleotide addition. For the majority of proteins in this family, these carboxylate residues are conserved.
Pssm-ID: 143391 [Multi-domain] Cd Length: 172 Bit Score: 102.42 E-value: 6.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 53 AARATAQAVLLKDRHGRRCAERLCFMQDEIIRILYSAATRHLYRSHVPSGaerMAVVATGGYGRGLMAPESDIDLLFILP 132
Cdd:cd05401 6 QLRRILRRDLLGGASIRAISRALSDLADALLRRALELALAELGKGPPPVP---FALLALGSYGRGELNPSSDQDLLLLYD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 133 YKQ---TAWGEQVAEAI---------LYCLWDMGLKVGHATRSVDECIRQARGDMTI------RTAILETRFLTGDQPLY 194
Cdd:cd05401 83 DDGdevAAYFEELAERLikilseaggPYCLGDVMLRPPGWRRSLAEWLDAARDWLTEpgrlweRTALLDARPVAGDRALA 162
|
....*..
gi 1047432450 195 DELVARF 201
Cdd:cd05401 163 EELRRRI 169
|
|
| HDc |
smart00471 |
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ... |
495-606 |
4.23e-04 |
|
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: 41.13 E-value: 4.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 495 HHYTVDEHLIRCIGFLQEIerggndeftvasdlFRKIQPEHRAVIYIATLLHDVAKGRP-----------EDHSIAGARV 563
Cdd:smart00471 1 SDYHVFEHSLRVAQLAAAL--------------AEELGLLDIELLLLAALLHDIGKPGTpdsflvktsvlEDHHFIGAEI 66
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1047432450 564 ARrlcpRLGFSAADTELVAWLIEEHLTMSTVAQSRDLSDRKTI 606
Cdd:smart00471 67 LL----EEEEPRILEEILRTAILSHHERPDGLRGEPITLEARI 105
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05092 |
PRK05092 |
PII uridylyl-transferase; Provisional |
1-931 |
0e+00 |
|
PII uridylyl-transferase; Provisional
Pssm-ID: 235342 [Multi-domain] Cd Length: 931 Bit Score: 1685.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 1 MDSVVTEDRPEADDRFDTARVTAAVDALAEKHAGREDVFRSALAQLLKAEMIAARATAQAVLLKDRHGRRCAERLCFMQD 80
Cdd:PRK05092 1 PDPPMAPRPLSLSEIFDRAALRAELDALAADAAGDPDALRAAVLALLKQALARGRAEARERLEADGSGRACARRLAYLTD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 81 EIIRILYSAATRHLYRSHVPSGAERMAVVATGGYGRGLMAPESDIDLLFILPYKQTAWGEQVAEAILYCLWDMGLKVGHA 160
Cdd:PRK05092 81 ELIRALYDFATTHLYPADNPSEGERLAVLAVGGYGRGELAPGSDIDLLFLLPYKQTAWAESVVEYMLYMLWDLGLKVGHA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 161 TRSVDECIRQARGDMTIRTAILETRFLTGDQPLYDELVARFDKDVVQGTASEFVTAKLAEREERHRRAGQSRYLVEPNVK 240
Cdd:PRK05092 161 TRSIDECIRLAREDMTIRTALLEARFLAGDRALFEELETRFDKEVVKGTAAEFVAAKLAERDERHRRAGDSRYLVEPNVK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 241 DGKGGLRDLHTLFWIAKYVYRVRETDELVERGVFDAQEYRTFRRCADFLWSVRCNLHFVSGRAEERLSFDMQREIAVRLG 320
Cdd:PRK05092 241 EGKGGLRDLHTLFWIAKYVYRVRDAAELVKLGVFTREEYRLFRRAEDFLWAVRCHLHFLTGRAEERLSFDLQPEIAERMG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 321 YTSHPGMQDVERFMKHYFLVAKDVGDLTAILCAKLEDEQAKPAPVLsrmvarLRPGAKRRRVPDSDDFIIDNNRINLAAP 400
Cdd:PRK05092 321 YTDHPGLSGVERFMKHYFLVAKDVGDLTRIFCAALEAQHAKRAPGL------NRFARRRRKALDSDGFVVDNGRINLADP 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 401 DVFKHDPVNLIRIFHLAQKNNLAFHPDAMRMVTRSLKLVNTQLRENPEANRLFMEILTS-NDAETVLRRMNETGVLGHFI 479
Cdd:PRK05092 395 DVFERDPVNLIRLFHLADRHGLDIHPDAMRLVTRSLRLIDAALREDPEANRLFLDILTSrRNPERVLRRMNEAGVLGRFI 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 480 RAFGKIVSMMQFNMYHHYTVDEHLIRCIGFLQEIERGG-NDEFTVASDLFRKIQPehRAVIYIATLLHDVAKGRPEDHSI 558
Cdd:PRK05092 475 PDFGRIVAMMQFNMYHHYTVDEHTIRAIGVLAEIERGElADEHPLASELMPKIES--RRALYVAVLLHDIAKGRPEDHSI 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 559 AGARVARRLCPRLGFSAADTELVAWLIEEHLTMSTVAQSRDLSDRKTIENFAAVVQSVEQMKLLTILTTADIRGVGPGVW 638
Cdd:PRK05092 553 AGARIARRLCPRLGLSPAETETVAWLVEHHLLMSDTAQKRDLSDPKTIEDFADAVQSPERLKLLLILTVADIRAVGPGVW 632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 639 NGWKAQLLRTLYYETEPVLTGGFSEVNRAQRIAVAQSEFRAAFTEWPEAELNAYIARHYPAYWLKVDLPRKIRQARFIRA 718
Cdd:PRK05092 633 NGWKAQLLRTLYYETEEVLTGGFSELNRAERVAAAKEALREALSDWPKADRDAYLARHYPAYWLAVDLDTQARHARFIRD 712
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 719 SEQAGHQLAINVGFDEARGVTELTILATDHPWLLSIIAGACASAGANIVDAQIYTTTDGRALDTIAISREYDRDEDEGRR 798
Cdd:PRK05092 713 ADDAGRPLATEVRPDPARGVTEVTVLAADHPGLFSRIAGACAAAGANIVDARIFTTTDGRALDTFWIQDAFGRDEDEPRR 792
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 799 ATRIGEMIEHVLEGKLRLPEVVARKAANRGKVRAFVVEPEVTINNQWSDRYTVIEVSGLDRPGLLYQLTTAISKLNLNIA 878
Cdd:PRK05092 793 LARLAKAIEDALSGEVRLPEALAKRTKPKKRARAFHVPPRVTIDNEASNRFTVIEVNGRDRPGLLYDLTRALSDLNLNIA 872
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|...
gi 1047432450 879 SAHVATFGERARDVFYVTDLLGAQITAPTRQAAIKSALIHLLSSEDNVAKPAA 931
Cdd:PRK05092 873 SAHIATYGERAVDVFYVTDLFGLKITNEARQAAIRRALLAALAEGEAEARAAR 925
|
|
| GlnD |
COG2844 |
UTP:GlnB (protein PII) uridylyltransferase [Posttranslational modification, protein turnover, ... |
41-925 |
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: 1204.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 41 SALAQLLKAEMIAARATAQAVLLKDRHGRRCAERLCFMQDEIIRilysaatrHLYRSHVPSGAERMAVVATGGYGRGLMA 120
Cdd:COG2844 1 AAALAALREALAEGRAALRERFRAGADGRELVRARAALVDQLLR--------ALWDLAGLTEPERLALVAVGGYGRGELA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 121 PESDIDLLFILPYKQTAWGEQVAEAILYCLWDMGLKVGHATRSVDECIRQARGDMTIRTAILETRFLTGDQPLYDELVAR 200
Cdd:COG2844 73 PHSDIDLLFLLPDKPTPALEEVIEAFLYLLWDLGLEVGHSVRTVDECLREAREDITVRTALLEARLLAGDEALFEELRER 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 201 FDKDVVqGTASEFVTAKLAEREERHRRAGQSRYLVEPNVKDGKGGLRDLHTLFWIAKYVYRVRETDELVERGVFDAQEYR 280
Cdd:COG2844 153 FRADVF-WDSRAFFEAKLAEQRERHAKYGDTRYNLEPNIKEGPGGLRDLQTLLWIAKRHFGVRSLEELVKKGLLTEEEYR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 281 TFRRCADFLWSVRCNLHFVSGRAEERLSFDMQREIAVRLGYTSHPGMQDVERFMKHYFLVAKDVGDLTAILCAKLEDEQA 360
Cdd:COG2844 232 ELRRAEDFLWRVRFALHLLAGRAEDRLLFDLQREVAERLGYQDTEGNRAVERFMQRYYRTAKAVGRLNEILLQRLEEAIL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 361 KPAPVlsrmvarlrpgakRRRVPDSDDFIIDNNRINLAAPDVFKHDPVNLIRIFHLAQKN--NLAFHPDAMRMVTRSLKL 438
Cdd:COG2844 312 KPPGL-------------RRPRPINEGFQLRNGRLEVADPDVFERDPVALLRLFLLAAQHpeGLGIHPDTLRLLRRALRL 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 439 VNTQLRENPEANRLFMEILTS-NDAETVLRRMNETGVLGHFIRAFGKIVSMMQFNMYHHYTVDEHLIRCIGFLQEIERG- 516
Cdd:COG2844 379 IDDAFRRDPEARRLFLEILRQpRGITRALRRMNEYGVLGRYIPEFGRIVGQMQFDLFHVYTVDEHTLRVVRNLRRFERGe 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 517 GNDEFTVASDLFRKIqpEHRAVIYIATLLHDVAKGRPEDHSIAGARVARRLCPRLGFSAADTELVAWLIEEHLTMSTVAQ 596
Cdd:COG2844 459 LAEEFPLASELIAEL--PKPELLYLAALFHDIAKGRGGDHSELGAEDARRFCPRHGLSPEDTELVAWLVRHHLLMSHTAQ 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 597 SRDLSDRKTIENFAAVVQSVEQMKLLTILTTADIRGVGPGVWNGWKAQLLRTLYYETEPVLTGGFSEVNRAQRIAVAQSE 676
Cdd:COG2844 537 RRDISDPEVIRDFARLVGSEERLDYLYLLTVADIRATGPKVWNSWKASLLRELYRATLRALRGGLEPPDREERIEERKEE 616
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 677 FRAAFTE--WPEAELNAYIARHYPAYWLKVDLPRKIRQARFIRASEQAGhQLAINVGFDEARGVTELTILATDHPWLLSI 754
Cdd:COG2844 617 ALALLADqgWDEEEIEALWARLPDDYFLRHDPEEIAWHARLLLRADDSG-KPLVLIRPDPDRGGTEVFVYTPDRPGLFAR 695
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 755 IAGACASAGANIVDAQIYTTTDGRALDTIAISREYDRDEDEGRRATRIGEMIEHVLEGKLRLPEVVARKAanRGKVRAFV 834
Cdd:COG2844 696 IAGALAALGLNILDARIHTTRDGYALDTFIVLDPDGEPIDDPDRLERIEQALEEALSGEVPLPEPLARRL--SRRLRHFP 773
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 835 VEPEVTINNQWSDRYTVIEVSGLDRPGLLYQLTTAISKLNLNIASAHVATFGERARDVFYVTDLLGAQITAPTRQAAIKS 914
Cdd:COG2844 774 VPPRVTFDNDASNRYTVLEVSALDRPGLLYDIARVLADLGLNIHSAKIATLGERVEDVFYVTDLDGQKLTDPERQEALRE 853
|
890
....*....|.
gi 1047432450 915 ALIHLLSSEDN 925
Cdd:COG2844 854 ALLEALDEEAE 864
|
|
| UTase_glnD |
TIGR01693 |
[Protein-PII] uridylyltransferase; This model describes GlnD, the uridylyltransferase ... |
55-917 |
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: 875.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 55 RATAQAVLLKDRHGRRCAERLCFMQDEIIRILYSAATRHLyrshvpsgAERMAVVATGGYGRGLMAPESDIDLLFILPYK 134
Cdd:TIGR01693 1 REELLEEFARGGDGRELREGRSDLTDLLLIRLWDFIGISE--------HSGIALVAVGGYGRGELAPYSDIDLLFLHDGK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 135 QTAWGEQVAEAILYCLWDMGLKVGHATRSVDECIRQARGDMTIRTAILETRFLTGDQPLYDELVARFDKDVVQGTASEFV 214
Cdd:TIGR01693 73 PAEEVEPKIERFLYPLWDLGFEVGHSVRTLEECARIAKADLTVATNLLEARHLAGDEALFFRLKERVRREDWRNTARSFL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 215 TAKLAEREERHRRAGQSRYLVEPNVKDGKGGLRDLHTLFWIAKYVYRVRETDELVERGVFDAQEYRTFRRCADFLWSVRC 294
Cdd:TIGR01693 153 AAKVEEQDERHARYGDTAYNLEPDIKEGPGGLRDLHTLFWVALYQLGVRRLEDLVKQGFLTDAEYKLLAEARDFLWDVRF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 295 NLHFVSGRAEERLSFDMQREIAVRLGYTShPGMQDVERFMKHYFLVAKDVGDLTAILCAKLEDEQAKPAPvlsrmVARLR 374
Cdd:TIGR01693 233 ALHLTTGRADDRLLFDHQDEIAAALGYGD-EGNPAVERFMRRYFQAARRIGYLTEAFLRHYEEALLSRGP-----SARVR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 375 pgaKRRRVPDSDDFIIDNNRINLAAPDVFKHDPVNLIRIFHLAQKNNLAFHPDAMRMVTRSLKLVNTQLRENPEANRLFM 454
Cdd:TIGR01693 307 ---RPKRRPLDEGFVEDGGELVLARTAVFERDPALLLRLFAIAAQRGLPIHPAALRQLTASLPLLPTPLREDPEARELFL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 455 EILTS-NDAETVLRRMNETGVLGHFIRAFGKIVSMMQFNMYHHYTVDEHLIRCIGFLQEIERGGN-DEFTVASDLFRKIq 532
Cdd:TIGR01693 384 ELLTSgNGTVRALRAMNRAGVLGRFLPEWGRIVGQMQFDLFHVYTVDEHTLRTVVHLAPFARGRLaREHPLASELMPKI- 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 533 pEHRAVIYIATLLHDVAKGRPEDHSIAGARVARRLCPRLGFSAADTELVAWLIEEHLTMSTVAQSRDLSDRKTIENFAAV 612
Cdd:TIGR01693 463 -EDPELLYLAALLHDIGKGRGGDHSVLGAEDARDVCPRLGLDRPDTELVAWLVRNHLLMSITAQRRDLNDPKTVFAFAEA 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 613 VQSVEQMKLLTILTTADIRGVGPGVWNGWKAQLLRTLYYETEPVLTGGFSE-VNRAQRIAVAQS-EFRAAFTEWPEAELN 690
Cdd:TIGR01693 542 VGDPERLEYLLALTVADIRATGPGVWNSWKASLLRDLYNRTEQVLRGGLEPpADPAEPIAEQRKlAVALLRTDYTSNEAE 621
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 691 AYIARHYPAYWLKVDLPRKIRQARFIRASEQAGHQLAINVGfDEARGVTELTILATDHPWLLSIIAGACASAGANIVDAQ 770
Cdd:TIGR01693 622 VLWLRAYDDYFLRFTHKEIAWHAESLRRALSSGGPLALIDG-TRPSGGTEVFIYAPDQPGLFAKVAGALAMLSLSVHDAQ 700
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 771 IYTTTDGRALDTIAISREYDRDEDEGRRATRIGEMIEHVLEGKLRLPEVVARKAANRGKVRAFVVEPEVTINNQWSDRYT 850
Cdd:TIGR01693 701 VNTTKDGVALDTFVVQDLFGSPPAAERVFQELLQGLVDVLAGLAKDPDTISARRARRRRLQHFAVPPRVTILNTASRKAT 780
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1047432450 851 VIEVSGLDRPGLLYQLTTAISKLNLNIASAHVATFGERARDVFYVTDLLGAQITApTRQAAIKSALI 917
Cdd:TIGR01693 781 IMEVRALDRPGLLARVGRTLEELGLSIQSAKITTFGEKAEDVFYVTDLFGLKLTD-EEEQRLLEVLA 846
|
|
| PRK03059 |
PRK03059 |
PII uridylyl-transferase; Provisional |
41-921 |
4.00e-177 |
|
PII uridylyl-transferase; Provisional
Pssm-ID: 235101 [Multi-domain] Cd Length: 856 Bit Score: 535.25 E-value: 4.00e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 41 SALAQLLKAEMIAARATAQAVLLKDRHGRRCAERLCFMQDEIIRILYSAAtrhlyrsHVPSGAermAVVATGGYGRGLMA 120
Cdd:PRK03059 7 PPPAASLRAELKAAKAALLARFRQAPNVTALLHALSRLVDQALRRLWQEC-------GLPAGA---ALVAVGGYGRGELF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 121 PESDIDLLFILPYKQTAWGEQVAEAILYCLWDMGLKVGHATRSVDECIRQARGDMTIRTAILETRFLTGDQPLYDELVAR 200
Cdd:PRK03059 77 PYSDVDLLVLLPDAPDAALDARIERFIGLCWDLGLEIGSSVRTVDECIEEAAQDVTVQTSLLEARLLTGSAALFERFQRR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 201 FDKDVvqgTASEFVTAKLAEREERHRRAGQSRYLVEPNVKDGKGGLRDLHTLFWIAKYVYRVRETDELVERGVFDAQEYR 280
Cdd:PRK03059 157 YRAAL---DPRAFFQAKLLEMRQRHAKFQDTPYSLEPNCKESPGGLRDLQTILWIARAAGLGSSWRELAKRGLITDREAR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 281 TFRRCADFLWSVRCNLHFVSGRAEERLSFDMQREIAVRLGYTSHPGMQDVERFMKHYFLVAKDVGDLTAILCAKLEdeqa 360
Cdd:PRK03059 234 QLRRNERFLKTLRARLHLLAGRREDRLVFDLQTALAESFGYRPTAAKRASEQLMRRYYWAAKAVTQLNTILLQNIE---- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 361 kpapvlsrmvARLRPGAKRRRVPDSDDFIIDNNRINLAAPDVFKHDPVNLIRIFHLAQKnnlafHPDAMRMVTRSLK--- 437
Cdd:PRK03059 310 ----------ARLFPSTSGITRVINERFVEKQGMLEIASDDLFERHPHAILEAFLLYQQ-----TPGLKGLSARTLRaly 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 438 ----LVNTQLRENPEANRLFMEILTSNDAET-VLRRMNETGVLGHFIRAFGKIVSMMQFNMYHHYTVDEHLIRCigfLQE 512
Cdd:PRK03059 375 nardVMNAAFRRDPVNRALFMQILQQPRGIThALRLMNQTSVLGRYLPNFRRIVGQMQHDLFHVYTVDQHILMV---LRN 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 513 IERGGNDEFT----VASDLFRKI-QPEhraVIYIATLLHDVAKGRPEDHSIAGARVARRLCPRLGFSAADTELVAWLIEE 587
Cdd:PRK03059 452 LRRFAMAEHAheypFCSQLIANFdRPW---LLYVAALFHDIAKGRGGDHSTLGAVDARRFCRQHGLAREDAELVVWLVEH 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 588 HLTMSTVAQSRDLSDRKTIENFAAVVQSVEQMKLLTILTTADIRGVGPGVWNGWKAQLLRTLYYETEPVLTGgfSEVNRA 667
Cdd:PRK03059 529 HLTMSQVAQKQDLSDPEVIARFAELVGDERRLTALYLLTVADIRGTSPKVWNAWKGKLLEDLYRATLRVLGG--AAPDAH 606
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 668 QRIAVAQSEFRAA---FTEWPEAelnayiarhYPAYWLKVDLprkirqARFIR--ASEQAGH--QLAINVGFDE----AR 736
Cdd:PRK03059 607 SELEARKEEALALlrlEALPDDA---------HEALWDQLDV------GYFLRhdAADIAWHtrHLYRHVDTDTpivrAR 671
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 737 ------GVtELTILATDHPWLLSIIAGACASAGANIVDAQIYTTTDGRALDTIAISreyDRDEDEGRRAtrIGEMIEHVL 810
Cdd:PRK03059 672 lspageGL-QVMVYTPDQPDLFARICGYFDRAGFSILDARVHTTRHGYALDTFQVL---DPEEDVHYRD--IINLVEHEL 745
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 811 EGKLRLPEVVARKAANR--GKVRAFVVEPEVTINNQWSDRYTVIEVSGLDRPGLLYQLTTAISKLNLNIASAHVATFGER 888
Cdd:PRK03059 746 AERLAEQAPLPEPSKGRlsRQVKHFPITPRVDLRPDERGQYYILSVSANDRPGLLYAIARVLAEHRVSVHTAKINTLGER 825
|
890 900 910
....*....|....*....|....*....|...
gi 1047432450 889 ARDVFYVTdllGAQITAPTRQAAIKSALIHLLS 921
Cdd:PRK03059 826 VEDTFLID---GSGLSDNRLQIQLETELLDALA 855
|
|
| glnD |
PRK00275 |
PII uridylyl-transferase; Provisional |
105-921 |
1.60e-174 |
|
PII uridylyl-transferase; Provisional
Pssm-ID: 234709 [Multi-domain] Cd Length: 895 Bit Score: 530.01 E-value: 1.60e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 105 RMAVVATGGYGRGLMAPESDIDLLFILPYK-QTAWGEQVaEAILYCLWDMGLKVGHATRSVDECIRQARGDMTIRTAILE 183
Cdd:PRK00275 78 DIALVAVGGYGRGELHPYSDIDLLILLDSAdHEEFREPI-ERFLTLLWDIGLEIGQSVRSVDECAEEARADLTVITNLME 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 184 TRFLTGDQPLYDELVARFDKDVVQgTASEFVTAKLAEREERHRRAGQSRYLVEPNVKDGKGGLRDLHTLFWIAKYVYRVR 263
Cdd:PRK00275 157 SRTIAGPESLRQRMLEVTSSEHMW-PSKEFFLAKRAEQKARHHKYNDTEYNLEPNVKGSPGGLRDIQTILWVAKRQFGTL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 264 ETDELVERGVFDAQEYRTFRRCADFLWSVRCNLHFVSGRAEERLSFDMQREIAVRLGYTSHPGMQDVERFMKHYFLVAKD 343
Cdd:PRK00275 236 NLHALVGEGFLTESEYGLLASGQEFLWKVRYALHMLAGRAEDRLLFDHQRSIATLLGYEDSDAKLAVEQFMQKYYRVVMA 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 344 VGDLTAILCAKLEDeqakpapvlsrmvARLRPGAKRRRVPDSDDFIIDNNRINLAAPDVFKHDPVNLIRIFHLaqknnLA 423
Cdd:PRK00275 316 LAELNDLILQHFEE-------------VILAADDSGTIQPLNSRFQLRDGYIEATHPNVFKRTPFALLEIFVL-----MA 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 424 FHP-------DAMRMVTRSLKLVNTQLRENPEANRLFMEILTSNDA-ETVLRRMNETGVLGHFIRAFGKIVSMMQFNMYH 495
Cdd:PRK00275 378 QHPeikgvraDTIRLLREHRHLIDDAFRNDIRNTSLFIELFKCPIGiHRNLRRMNRYGILGRYLPEFGHIVGQMQHDLFH 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 496 HYTVDEHLIRCIGFLQEIER-GGNDEFTVASDLFRKIQ-PEhraVIYIATLLHDVAKGRPEDHSIAGARVARRLCPRLGF 573
Cdd:PRK00275 458 IYTVDAHTLNLIKNLRKLRYpEVSEKFPLASKLMGRLPkPE---LLYIAGLYHDIGKGRGGDHSELGAVDAEAFCQRHQL 534
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 574 SAADTELVAWLIEEHLTMSTVAQSRDLSDRKTIENFAAVVQSVEQMKLLTILTTADIRGVGPGVWNGWKAQLLRTLYYET 653
Cdd:PRK00275 535 PAWDTRLVVWLVENHLLMSTTAQRKDLSDPQVIHDFALKVGDQTHLDYLYVLTVADINATNPTLWNSWRASLLRQLYTET 614
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 654 EPVLTGGFSE-VNRAQRIAVAQSEFRAAF----TEWPEAEL------NAYIARHYPA--YWLK---VDLPRKIRQARFIR 717
Cdd:PRK00275 615 KRALRRGLENpVDREEQIRQTQSAALDILvrkgTDPDDAEQlwsqlgDDYFLRHTAGdiAWHTeaiLQHPDDGGPLVLIK 694
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 718 ASEQaghqlainvgfDEARGVTELTILATDHPWLLSIIAGACASAGANIVDAQIYTTTDGRALDTIAISReyDRDEDEGR 797
Cdd:PRK00275 695 ETTQ-----------REFEGGTQIFIYAPDQHDFFAATVAAMDQLNLNIHDARIITSSSQFTLDTYIVLD--DDGEPIGD 761
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 798 RATRIgEMIEHVLEGKLRLPE----VVARKAANRGKvrAFVVEPEVTINNQWSDRYTVIEVSGLDRPGLLYQLTTAISKL 873
Cdd:PRK00275 762 NPARI-EQIREGLTEALRNPDdyptIIQRRVPRQLK--HFAFPTQVTISNDAQRPVTVLEIIAPDRPGLLARIGRIFLEF 838
|
810 820 830 840
....*....|....*....|....*....|....*....|....*...
gi 1047432450 874 NLNIASAHVATFGERARDVFYVTDLLGAQITAPTRQAAIKSALIHLLS 921
Cdd:PRK00275 839 DLSLQNAKIATLGERVEDVFFITDADNQPLSDPQLCSRLQDAICEQLD 886
|
|
| PRK05007 |
PRK05007 |
bifunctional uridylyltransferase/uridylyl-removing protein GlnD; |
77-926 |
3.21e-155 |
|
bifunctional uridylyltransferase/uridylyl-removing protein GlnD;
Pssm-ID: 235329 [Multi-domain] Cd Length: 884 Bit Score: 479.47 E-value: 3.21e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 77 FMQDEIIRILYSAATRH-------LYRSHVPSGAERMAVVATGGYGRGLMAPESDIDLLFILPYKQTAWGEQVAEAILYC 149
Cdd:PRK05007 45 FDAGISAEQLVEARTEFidqllqrLWIEAGFDQIPDLALVAVGGYGRGELHPLSDIDLLILSRKKLPDEQAQKVGELITL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 150 LWDMGLKVGHATRSVDECIRQARGDMTIRTAILETRFLTGDQPLYDELvarfDKDVVQG---TASEFVTAKLAEREERHR 226
Cdd:PRK05007 125 LWDLKLEVGHSVRTLEECLLEGLSDLTVATNLIESRLLCGDVALFLEL----QKHIFSDgfwPSEKFYAAKVEEQNERHQ 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 227 RAGQSRYLVEPNVKDGKGGLRDLHTLFWIAKYVYRVRETDELVERGVFDAQEYRTFRRCADFLWSVRCNLHFVSGRAEER 306
Cdd:PRK05007 201 RYHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSLDEMVGFGFLTPAERAELNECQHFLWRIRFALHLVLSRYDNR 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 307 LSFDMQREIAVRLGYTSHpGMQDVERFMKHYFLVAKDVGDLTAILCaKLEDEqakpapvlsrmvARLRPGAKRRRVPDSD 386
Cdd:PRK05007 281 LLFDRQLSVAQLLGYEGE-GNEPVERMMKDYYRTTRRVSELNQMLL-QLFDE------------AILALTADEKPRPIDD 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 387 DFIIDNNRINLAAPDVFKHDPVNLIRIFHLAQKNN--LAFHPDAMRMVTRSLKLVNTQLRENPEANRLFMEILTSNDA-E 463
Cdd:PRK05007 347 EFQLRGTLIDLRDETLFQRQPEAILRMFYLMARNSniTGIYSTTLRQLRHARRHLNQPLCEIPEARKLFMEILRHPGAvS 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 464 TVLRRMNETGVLGHFIRAFGKIVSMMQFNMYHHYTVDEHLIRcigFLQEIERGGN----DEFTVASDLFRKIQpeHRAVI 539
Cdd:PRK05007 427 RALLPMHRHSVLSAYMPQWSHIVGQMQFDLFHAYTVDEHTIR---VLLKLESFADeetrQRHPLCVELYPRLP--KKELL 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 540 YIATLLHDVAKGRPEDHSIAGARVARRLCPRLGFSAADTELVAWLIEEHLTMSTVAQSRDLSDRKTIENFAAVVQSVEQM 619
Cdd:PRK05007 502 LLAALFHDIAKGRGGDHSILGAQDALEFAELHGLNSRETQLVAWLVRNHLLMSVTAQRRDIQDPDVIKQFAEEVQDENRL 581
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 620 KLLTILTTADIRGVGPGVWNGWKAQLLRTLYYETEPVLTGGFSEV---------NRAQRIAVAQSEfraAFTEWpeaELN 690
Cdd:PRK05007 582 RYLVCLTVADICATNETLWNSWKQSLLRELYFATEKQLRRGMENPpdmrervrhHQLQALALLRMD---NIDEE---ALH 655
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 691 A--------YIARHYPAY--WLKVDLPRKIRQARFIRASEQAghqlainvgfdeARGVTELTILATDHPWLLSIIAGACA 760
Cdd:PRK05007 656 QiwsrcradYFLRHTPNQlaWHARHLLQHDLDKPLVLLSKQA------------TRGGTEIFIWSPDRPYLFAAVCAELD 723
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 761 SAGANIVDAQIYTTTDGRALDTIAIsREYDRDEDEGRRATRIGEMIEHVLE-GKLRLPEVvaRKAANrgKVRAFVVEPEV 839
Cdd:PRK05007 724 RRNLSVHDAQIFTSRDGMAMDTFIV-LEPDGSPLSQDRHQVIRKALEQALTqSSPQPPKP--RRLPA--KLRHFNVPTEV 798
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 840 TINNQWSDRYTVIEVSGLDRPGLLYQLTTAISKLNLNIASAHVATFGERARDVFYVTDLLGAQITaPTRQAAIKSALIHL 919
Cdd:PRK05007 799 SFLPTHTDRRSYMELIALDQPGLLARVGKIFADLGISLHGARITTIGERVEDLFILATADRRALN-EELQQELRQRLTEA 877
|
....*..
gi 1047432450 920 LSSEDNV 926
Cdd:PRK05007 878 LNPNDKG 884
|
|
| glnD |
PRK01759 |
bifunctional uridylyltransferase/uridylyl-removing protein GlnD; |
87-921 |
6.00e-141 |
|
bifunctional uridylyltransferase/uridylyl-removing protein GlnD;
Pssm-ID: 234980 [Multi-domain] Cd Length: 854 Bit Score: 441.10 E-value: 6.00e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 87 YSAATRHLYRSHVPSGAERMAVVATGGYGRGLMAPESDIDLLFILPYKQTAWGEQVAEAILYCLWDMGLKVGHATRSVDE 166
Cdd:PRK01759 38 YDQLLIHLWQQFGLEEQSDLALIAVGGYGRREMFPLSDLDILILTEQPPDEETEEKINQFFQFLWDCGFEVGASVRTLAE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 167 CIRQARGDMTIRTAILETRFLTGDQPLYDELVAR-FDKDVVQGTAseFVTAKLAEREERHRRAGQSRYLVEPNVKDGKGG 245
Cdd:PRK01759 118 CESEGRADITIATNLLESRFLTGNEKLFDALVELlQQADFWSKEA--FFQAKIQEKIERYQRYHNTSYNLEPDIKYSPGG 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 246 LRDLHTLFWIAKYVYRVRETDELVERGVFDAQEYRTFRRCADFLWSVRCNLHFVSGRAEERLSFDMQREIAVRLGYTShP 325
Cdd:PRK01759 196 LRDLHLLYWIALRHSGAKSLEEILQSGFIYPEEYAELQQSQQFLFKVRFALHLILKRYDNRLLFDRQLKVSELLGFQG-E 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 326 GMQDVERFMKHYFLVAKDVGDLTAILCAKLEDEqakpapVLSRMvarlrpGAKRRRVPDsDDFIIDNNRINLAAPDVFKH 405
Cdd:PRK01759 275 GNQGVEKMMKSFFQALQSISLLSDLLVKHYREH------FLQPN------QNVEIQPLD-DDFYLINNAICLRNPDCFEQ 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 406 DPVNLIRIF-HLAQKNNLAFHPDAMRMVTRSLKLVNTQLRENPEANRLFMEILTSNDA-ETVLRRMNETGVLGHFIRAFG 483
Cdd:PRK01759 342 QPESILDLFfYLTQYPQAEIHSTTLRQLRLALEQLQQPLCELPAARERFLRLFNQPNAiKRALVPMHQYGVLTAYLPQWK 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 484 KIVSMMQFNMYHHYTVDEHLIRCI----GFLQEierGGNDEFTVASDLFRKIQpeHRAVIYIATLLHDVAKGRPEDHSIA 559
Cdd:PRK01759 422 GIVGLMQFDLFHIYTVDEHTLRVMlkleSFLDE---ESAEQHPICHQIFSQLS--DRTLLYIAALFHDIAKGRGGDHAEL 496
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 560 GARVARRLCPRLGFSAADTELVAWLIEEHLTMSTVAQSRDLSDRKTIENFAAVVQSVEQMKLLTILTTADIRGVGPGVWN 639
Cdd:PRK01759 497 GAVDMRQFAQQHGFDQREIETMAWLVQQHLLMSVTAQRRDIHDPEVVMNFAEEVQNQVRLDYLTCLTVADICATNETLWN 576
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 640 GWKAQLLRTLYYETEPVLTGGF---------SEVNRAQriavAQSEFRAAFTEWPEAELNAYIARHYPAYWLKvDLPRKI 710
Cdd:PRK01759 577 SWKRSLFATLYQFTNQQFQQGMdelldyqekAEENRQQ----ALELLQQKYSALSETQIEQLWQRCPEDYFLR-NTPKQI 651
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 711 RQARFIRASEQAghQLAINVGFDEARGVTELTILATDHPWLLSIIAGACASAGANIVDAQIYTTTDGRALDTIAISrEYD 790
Cdd:PRK01759 652 AWHALLLLDFRG--DLLVKISNRFSRGGTEIFIYCQDQANLFLKVVSTIGAKKLSIHDAQIITSQDGYVLDSFIVT-ELN 728
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 791 RDE-DEGRRatrigEMIEHVLEGKLRLPEVVARKAANRGKVRAFVVEPEVTINNQWSDRYTVIEVSGLDRPGLLYQLTTA 869
Cdd:PRK01759 729 GKLlEFDRR-----RQLEQALTKALNTNKLKKLNLEENHKLQHFHVKTEVRFLNEEKQEQTEMELFALDRAGLLAQVSQV 803
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|..
gi 1047432450 870 ISKLNLNIASAHVATFGERARDVFYVTDLLGAQITAPTRQaAIKSALIHLLS 921
Cdd:PRK01759 804 FSELNLNLLNAKITTIGEKAEDFFILTNQQGQALDEEERK-ALKSRLLSNLS 854
|
|
| PRK04374 |
PRK04374 |
[protein-PII] uridylyltransferase; |
92-910 |
9.50e-107 |
|
[protein-PII] uridylyltransferase;
Pssm-ID: 179839 [Multi-domain] Cd Length: 869 Bit Score: 350.81 E-value: 9.50e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 92 RHLYRSHVPSGAErMAVVATGGYGRGLMAPESDIDLLFILPYKQTAWGEQVAEAILYCLWDMGLKVGHATRSVDECiRQA 171
Cdd:PRK04374 60 RNAWTRCIPADSG-LSLHAVGGYGRGELFPRSDVDLLVLGETAAQQRHEQALARLFALLWDVGLPISHAVRSPAQC-TAA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 172 RGDMTIRTAILETRFLTGDQPLYDELVARFDKDVVQgTASEFVTAKLAEREERHRRAGQSRYLVEPNVKDGKGGLRDLHT 251
Cdd:PRK04374 138 AADQTVLTALIESRPLVADAAARAALAAAIAPQQVW-PPRAFFQAKREELLARHQRFGDTADNLEPDIKDGPGGLRDLQT 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 252 LFWIAKYVYRVRETDELVERGVFDAQEYRTFRRCADFLWSVRCNLHFVSGRAEERLSFDMQREIAVRLGYTSHPGMQDVE 331
Cdd:PRK04374 217 LGWMALRAFGVKDLEALVGLGHVGCDEAAALRREREELARLRFGLHLVANRPEERLRFDYQKTLAERLGFADDPESLGVE 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 332 RFMKHYFLVAKDVGDLTAILCAKLE---DEQAKPAPvlsrmvarLRPGAKRRR---VPDSDDFiidnnrinlaaPDvfkH 405
Cdd:PRK04374 297 KMMQRFYRSAALIRRISDRLLQRFEeqfDGEATPEP--------LGGGFSLRRgylAADADSW-----------PD---G 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 406 DPVNLIRIFH--LAQKNNLAFHPDAMRMVTRSLKLVNTQLRENPEANRLFMEILTSNDAETVLRRMNETGVLGHFIRAFG 483
Cdd:PRK04374 355 DVLQVFALFAqwAAHREVRGLHSLTARALAEVLRDLPAYDVADATARERFMALLRGPRAVETLNRMARLGVLGQWIPAFA 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 484 KIVSMMQFNMYHHYTVDEHLIRCIGFLQEIERGGNDE-FTVASDLFRKI-QPEhraVIYIATLLHDVAKGRPEDHSIAGA 561
Cdd:PRK04374 435 SVSGRMQFDLFHVYTVDQHTLMVLRNIALFAAGRADErFSIAHEVWPRLrKPE---LLLLAGLFHDIAKGRGGDHSELGA 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 562 RVARRLCPRLGFSAADTELVAWLIEEHLTMSTVAQSRDLSDRKTIENFAAVVQSVEQMKLLTILTTADIRGVGPGVWNGW 641
Cdd:PRK04374 512 VDARAFCLAHRLSEGDTELVTWLVEQHLRMSVTAQKQDISDPEVIHRFATLVGTRERLDYLYLLTCADIAGTSPKLWNAW 591
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 642 KAQLLRTLYYETEPVLTGGFSE-VNRAQRIAVAQSEFRAAFTEwpEAELNAYIARHYPAywlkvdLPRKirqaRFIR-AS 719
Cdd:PRK04374 592 KDRLLADLYFAARRALREGLEHpPPREERLREARESARALMQA--QGHDDATIDRQFAG------MPDE----NFLRfRP 659
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 720 EQAGHQLA------INVGFDEARGVT------ELTILATDHPWLLSIIAGACASAGANIVDAQIYTTTDGRALDTIAISr 787
Cdd:PRK04374 660 EQLAWQAAslieveIGQTLVKARRAVpdndalEVFVYSPDRDGLFAAIVATLDRKGYGIHRARVLDAPHDAIFDVFEVL- 738
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 788 eyDRDEDEGRRATRIGEMIEHVLEGKLRlpEVVARKAANRGKVRAFVVEPEVTINNQWSDRYTVIEVSGLDRPGLLYQLT 867
Cdd:PRK04374 739 --PQDTYADGDPQRLAAALRQVLAGDLQ--KVRPARRAVPRQLRHFRFAPRVEFSESAGGRRTRISLVAPDRPGLLADVA 814
|
810 820 830 840
....*....|....*....|....*....|....*....|...
gi 1047432450 868 TAISKLNLNIASAHVATFGERARDVFYVTDLLGAQITAPTRQA 910
Cdd:PRK04374 815 HVLRMQHLRVHDARIATFGERAEDQFQITDEHDRPLSESARQA 857
|
|
| PRK03381 |
PRK03381 |
PII uridylyl-transferase; Provisional |
107-916 |
2.74e-89 |
|
PII uridylyl-transferase; Provisional
Pssm-ID: 235123 [Multi-domain] Cd Length: 774 Bit Score: 301.14 E-value: 2.74e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 107 AVVATGGYGRGLMAPESDIDLLFILPYKQTAWGEQVAEAILYCLWDMGLKVGHATRSVDECIRQARGDMTIRTAILETRF 186
Cdd:PRK03381 59 ALVAVGGLGRRELLPYSDLDLVLLHDGRPADDVAEVADRLWYPLWDAGIRLDHSVRTVPEALKVAGSDLKAALGLLDARH 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 187 LTGDQPLYDELVARFDKDVVQGTASEFvtAKLAER-EERHRRAGQSRYLVEPNVKDGKGGLRDLHTLfwiakyvyrvret 265
Cdd:PRK03381 139 IAGDADLSALLIGGVRRQWRNGARRRL--PELVELtRARWERSGEIAHLAEPDLKEGRGGLRDVQLL------------- 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 266 DELVERGVFDAQEYRtFRRCADFLWSVRCNLHFVSGRAEERLSFDMQREIAVRLGYTSHPGMQ----DVERFMKHYFlva 341
Cdd:PRK03381 204 RALAAAQLADAPGGG-LDAAHRRLLDVRTELHRVSGRGRDRLLAQEADEVAAALGLGDRFDLAralsDAARTISYAV--- 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 342 kDVGDLTAilcakledEQAKPapvlSRMVARLRPGAKRRrvPDSDDFIIDNNRINLAAPDVFKHDPVNLIRIFHLAQKNN 421
Cdd:PRK03381 280 -DVGWRTA--------ANALP----RRGLSALRRRPVRR--PLDEGVVEHAGEVVLARDARPARDPGLVLRVAAAAATTG 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 422 LAFHPDAMRMVTRSLKlvntQLRE--NPEANRLFMEILTSNDAET-VLRRMNETGVLGHFIRAFGKIVSMMQFNMYHHYT 498
Cdd:PRK03381 345 LPIAAATLSRLAASAP----PLPTpwPAEARDDLLVLLGAGPAAVaVIEALDRTGLWGRLLPEWEAVRDLPPRDPVHRWT 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 499 VDEHLI----RCIGFLQEIERggndeftvaSDLfrkiqpehravIYIATLLHDVAKGRPEDHSIAGARVARRLCPRLGFS 574
Cdd:PRK03381 421 VDRHLVetavRAAALTRRVAR---------PDL-----------LLLGALLHDIGKGRGGDHSVVGAELARQIGARLGLS 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 575 AADTELVAWLIEEHLTMSTVAQSRDLSDRKTIENFAAVVQSVEQ-MKLLTILTTADIRGVGPGVWNGWKAQLLRTLYYET 653
Cdd:PRK03381 481 PADVALLSALVRHHLLLPETATRRDLDDPATIEAVAEALGGDPVlLELLHALTEADSLATGPGVWSDWKASLVGDLVRRC 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 654 EPVLTGGfsEVNRAQRIAVAQSEFRAAftewpeaelnayiarhypaywlkvdlprkirqarfiraseqagHQLAINVGFD 733
Cdd:PRK03381 561 RAVLAGE--PLPEPEPLDPAQLALAAD-------------------------------------------GGVHVEIAPA 595
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 734 EARGVtELTILATDHPWLLSIIAGACASAGANIVDAQIyTTTDGRALDTIAISREYDRDEDegrrATRIGEMIEHVLEGK 813
Cdd:PRK03381 596 DPHMV-EVTVVAPDRRGLLSKAAGVLALHRLRVRSASV-RSHDGVAVLEFVVSPRFGSPPD----AALLRQDLRRALDGD 669
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 814 LRLPEVVARK--AANRGKVRAFVVEPEVTINNQWSDRYTVIEVSGLDRPGLLYQLTTAISKLNLNIASAHVATFGERARD 891
Cdd:PRK03381 670 LDVLARLAAReaAAAAVPVRRPAAPPRVLWLDGASPDATVLEVRAADRPGLLARLARALERAGVDVRWARVATLGADVVD 749
|
810 820
....*....|....*....|....*
gi 1047432450 892 VFYVTDllGAQITAPTRQAAIKSAL 916
Cdd:PRK03381 750 VFYVTG--AAGGPLADARAAVEQAV 772
|
|
| GlnD_UR_UTase |
pfam08335 |
GlnD PII-uridylyltransferase; This is a family of bifunctional uridylyl-removing enzymes ... |
213-351 |
1.52e-48 |
|
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: 168.53 E-value: 1.52e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 213 FVTAKLAEREERHRRAGQSRYLVEPNVKDGKGGLRDLHTLFWIAKYVYRVRETDELVERGVFDAQEYRTFRRCADFLWSV 292
Cdd:pfam08335 2 FMKAKIEEQVARHGRYGDTAYNLEPNIKLGPGGLRDIEFIVWIAQLIFTLRALEELVELGLLTREEARELRRAYRFLRRV 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1047432450 293 RCNLHFVSGRAEERLSFDMQREIAVRLGYTsHPGMQDVERFMKHYFLVAKDVGDLTAIL 351
Cdd:pfam08335 82 RHRLHLLADRQTDRLPFDLQRRLARALGYA-RDGWLAVERFMRRLFRHAHRVSRLFEIL 139
|
|
| glnD |
PRK00227 |
[protein-PII] uridylyltransferase; |
87-649 |
3.24e-37 |
|
[protein-PII] uridylyltransferase;
Pssm-ID: 178937 [Multi-domain] Cd Length: 693 Bit Score: 149.92 E-value: 3.24e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 87 YSAATRHLYRSHVPSGAermAVVATGGYGRGLMAPESDIDLLFILPYKQTawgEQVAEAILYCLWDMGLKVGHATRSVDE 166
Cdd:PRK00227 12 EASALALLGSLQLPPGT---ALAATGSLARREMTPYSDLDLILLHPPGAT---PDGVEDLWYPIWDAKKRLDYSVRTPQE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 167 CIRQARGDMTIRTAILETRFLTGDQPLYD------------ELVARFDkDVVQGTASefvtaklaereeRHRRAGQSRYL 234
Cdd:PRK00227 86 CAAMISADSTAALALLDLRFVAGDEQLTAstrakilekwrrELNKNFD-AVVDTAIA------------RWRRSGSVVAM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 235 VEPNVKDGKGGLRDLHTLfwiakyvyRVRETDELVERGVFDAQEyrtfrrcaDFLWSVRCNLHFVSGRAEERLSFDMQRE 314
Cdd:PRK00227 153 TRPDLKHGRGGLRDIELI--------RALALGHLCDAPPLDSQH--------QLLLDVRTLLHVHARRARDVLDPEFAVD 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 315 IAVRLGytshpgmqdverFMKHYFLVAKDVGDLTAILCAkLEDEQAKPAPVLSRMVARLRPgakrRRVPDSDDFIIDNNR 394
Cdd:PRK00227 217 IALDLG------------FVDRYHLSREIADAARAIDDA-LTAALATARGALPRRTAFRNA----VRRPLDVDVVDANGT 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 395 INLA-APDVfkHDPVNLIRIFHLAQKNNLAFHPDamrmvtrslklVNTQLRENPE--------ANRLFMEILTSND-AET 464
Cdd:PRK00227 280 IALSrTPDL--DDPALPLRVAAAAARTGLPVSES-----------VWKRLEECPElpepwpasAAGDFFRLLSSPVnSRR 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 465 VLRRMNETGVLGHFIRAFGKIVSMMQFNMYHHYTVDEHLIRcigflqeierggndefTVASDLFRKIQPEHRAVIYIATL 544
Cdd:PRK00227 347 VIKQMDRHGLWERIVPEWDRIRGLMPREPSHIHTIDEHSLN----------------TVANCALETVTVARPDLLLLGAL 410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 545 LHDVAKGRPEDHSIAGARVARRLCPRLGFSAADTELVAWLIEEHLTMSTVAQSRDLSDRKTIENFA-AVVQSVEQMKLLT 623
Cdd:PRK00227 411 YHDIGKGYPRPHEQVGAEMVARAARRMGLNLRDRAVVQTLVAEHTTLARIAGRLDPTSEEAVDKLLdAVRYDLLTLNLLE 490
|
570 580
....*....|....*....|....*.
gi 1047432450 624 ILTTADIRGVGPGVWNGWKAQLLRTL 649
Cdd:PRK00227 491 VLTEADAEGTGPGVWTARLEQGLRIV 516
|
|
| NT_GlnE_GlnD_like |
cd05401 |
Nucleotidyltransferase (NT) domain of Escherichia coli adenylyltransferase (GlnE), Escherichia ... |
53-201 |
6.67e-25 |
|
Nucleotidyltransferase (NT) domain of Escherichia coli adenylyltransferase (GlnE), Escherichia coli uridylyl transferase (GlnD), and similar proteins; Escherichia coli GlnD and -E participate in the Glutamine synthetase (GS)/Glutamate synthase (GOGAT) pathway for the assimilation of ammonium nitrogen. In nitrogen sufficiency, GlnE adenylates GS, reducing GS activity; when nitrogen is limiting, GlnE deadenylates GS-AMP, restoring GS activity. When nitrogen is limiting, GlnD uridylylates the nitrogen regulatory protein PII to PII-UTP, and in nitrogen sufficiency, it removes the modifying groups. The activity of Escherichia coli GlnE is modulated by PII-proteins. PII-UMP promotes GlnE deadenylation activity, and PII promotes GlnE adenylation activity. Escherichia coli GlnE has two separate NT domains. The N-terminal NT domain catalyzes the deadenylylation of GS, and the C-terminal NT domain the adenylylation reaction. The majority of proteins in this family contain a C-terminal NT domain which is associated with a cystathionine beta-synthase (CBS) domain pair and a CAP_ED (cAMP receptor protein effector ) domain. This family belongs to the Pol beta-like NT superfamily. In the majority of enzymes in this superfamily, two carboxylates, Dx[D/E], together with a third more distal carboxylate, coordinate two divalent metal cations involved in a two-metal ion mechanism of nucleotide addition. For the majority of proteins in this family, these carboxylate residues are conserved.
Pssm-ID: 143391 [Multi-domain] Cd Length: 172 Bit Score: 102.42 E-value: 6.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 53 AARATAQAVLLKDRHGRRCAERLCFMQDEIIRILYSAATRHLYRSHVPSGaerMAVVATGGYGRGLMAPESDIDLLFILP 132
Cdd:cd05401 6 QLRRILRRDLLGGASIRAISRALSDLADALLRRALELALAELGKGPPPVP---FALLALGSYGRGELNPSSDQDLLLLYD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 133 YKQ---TAWGEQVAEAI---------LYCLWDMGLKVGHATRSVDECIRQARGDMTI------RTAILETRFLTGDQPLY 194
Cdd:cd05401 83 DDGdevAAYFEELAERLikilseaggPYCLGDVMLRPPGWRRSLAEWLDAARDWLTEpgrlweRTALLDARPVAGDRALA 162
|
....*..
gi 1047432450 195 DELVARF 201
Cdd:cd05401 163 EELRRRI 169
|
|
| ACT_ACR-UUR-like_2 |
cd04899 |
C-terminal ACT domains of the bacterial signal-transducing uridylyltransferase ... |
850-920 |
4.49e-22 |
|
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: 90.59 E-value: 4.49e-22
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1047432450 850 TVIEVSGLDRPGLLYQLTTAISKLNLNIASAHVATFGERARDVFYVTDLLGAQITaPTRQAAIKSALIHLL 920
Cdd:cd04899 1 TVLELTALDRPGLLADVTRVLAELGLNIHSAKIATLGERAEDVFYVTDADGQPLD-PERQEALRAALGEAL 70
|
|
| ACT_UUR-ACR-like |
cd04873 |
ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) ... |
850-920 |
5.14e-19 |
|
ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) enzyme, GlnD; This ACT domain family, ACT_UUR_ACR-like, includes the two C-terminal ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) enzyme, GlnD; including those enzymes similar to the GlnD found in enteric Escherichia coli and those found in photosynthetic, nitrogen-fixing bacterium Rhodospirillum rubrum. Also included in this CD are the four ACT domains of a novel protein composed almost entirely of ACT domain repeats (the ACR protein) and like proteins. These ACR proteins, found in Arabidopsis and Oryza, are proposed to function as novel regulatory or sensor proteins in plants. This CD also includes the first of the two ACT domains that comprise the Glycine Cleavage System Transcriptional Repressor (GcvR) protein and related domains, as well as, the N-terminal ACT domain of a yet characterized Arabidopsis/Oryza predicted tyrosine kinase. Members of this CD belong to the superfamily of ACT regulatory domains.
Pssm-ID: 153145 [Multi-domain] Cd Length: 70 Bit Score: 81.83 E-value: 5.14e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1047432450 850 TVIEVSGLDRPGLLYQLTTAISKLNLNIASAHVATFGERARDVFYVTDLLGAQITaPTRQAAIKSALIHLL 920
Cdd:cd04873 1 TVVEVYAPDRPGLLADITRVLADLGLNIHDARISTTGERALDVFYVTDSDGRPLD-PERIARLEEALEDAL 70
|
|
| ACT_UUR-like_1 |
cd04900 |
ACT domain family, ACT_UUR-like_1, includes the first of two C-terminal ACT domains of the ... |
738-810 |
1.23e-18 |
|
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: 80.98 E-value: 1.23e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1047432450 738 VTELTILATDHPWLLSIIAGACASAGANIVDAQIYTTTDGRALDTIAISREYDRDEDEGRRATRIGEMIEHVL 810
Cdd:cd04900 1 GTEVFIYTPDRPGLFARIAGALDQLGLNILDARIFTTRDGYALDTFVVLDPDGEPIGERERLARIREALEDAL 73
|
|
| ACT_UUR-ACR-like |
cd04873 |
ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) ... |
739-810 |
5.95e-10 |
|
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: 56.02 E-value: 5.95e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1047432450 739 TELTILATDHPWLLSIIAGACASAGANIVDAQIyTTTDGRALDTIAISREYDRDEDEgRRATRIGEMIEHVL 810
Cdd:cd04873 1 TVVEVYAPDRPGLLADITRVLADLGLNIHDARI-STTGERALDVFYVTDSDGRPLDP-ERIARLEEALEDAL 70
|
|
| ACT_ACR_2 |
cd04925 |
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats ... |
850-920 |
1.46e-09 |
|
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: 55.13 E-value: 1.46e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1047432450 850 TVIEVSGLDRPGLLYQLTTAISKLNLNIASAHVATFGERARDVFYVTD-LLGAQITAPTRQAAIKSALIHLL 920
Cdd:cd04925 1 TAIELTGTDRPGLLSEVFAVLADLHCNVVEARAWTHNGRLACVIYVRDeETGAPIDDPIRLASIEDRLDNVL 72
|
|
| ACT_UUR-like_1 |
cd04900 |
ACT domain family, ACT_UUR-like_1, includes the first of two C-terminal ACT domains of the ... |
858-920 |
1.59e-07 |
|
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: 49.40 E-value: 1.59e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1047432450 858 DRPGLLYQLTTAISKLNLNIASAHVATFGE-RARDVFYVTDLLGAQITAPTRQAAIKSALIHLL 920
Cdd:cd04900 10 DRPGLFARIAGALDQLGLNILDARIFTTRDgYALDTFVVLDPDGEPIGERERLARIREALEDAL 73
|
|
| ACT_ACR_1 |
cd04895 |
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats ... |
850-916 |
1.09e-06 |
|
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats (the "ACR" protein); This CD includes the N-terminal ACT domain, of a novel type of ACT domain-containing protein which is composed almost entirely of four ACT domain repeats (the "ACR" protein). ACR proteins, found only in Arabidopsis and Oryza, as yet, are proposed to function as novel regulatory or sensor proteins in plants. Nine ACR gene products have been described (ACR1-8 in Arabidopsis and OsARC1-9 in Oryza) and are represented in this CD. Members of this CD belong to the superfamily of ACT regulatory domains.
Pssm-ID: 153167 [Multi-domain] Cd Length: 72 Bit Score: 47.06 E-value: 1.09e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1047432450 850 TVIEVSGLDRPGLLYQLTTAISKLNLNIASAHVATFGERARDVFYVTDLLGAQITAPTRQAAIKSAL 916
Cdd:cd04895 2 TLVKVDSARKPGILLEAVQVLTDLDLCITKAYISSDGGWFMDVFHVTDQLGNKLTDDSLIAYIEKSL 68
|
|
| ACT_ACR_4 |
cd04926 |
C-terminal ACT domain, of a novel type of ACT domain-containing protein which is composed ... |
852-913 |
2.44e-06 |
|
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: 45.80 E-value: 2.44e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1047432450 852 IEVSGLDRPGLLYQLTTAISKLNLNIASAHVATFGERARDVFYVTDLLGAQITAPTRQAAIK 913
Cdd:cd04926 4 LELRTEDRVGLLSDVTRVFRENGLTVTRAEISTQGDMAVNVFYVTDANGNPVDPKTIEAVRQ 65
|
|
| ACT |
cd02116 |
ACT domains are commonly involved in specifically binding an amino acid or other small ligand ... |
852-897 |
5.16e-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: 44.59 E-value: 5.16e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1047432450 852 IEVSGLDRPGLLYQLTTAISKLNLNIASAHVATFG-ERARDVFYVTD 897
Cdd:cd02116 1 LTVSGPDRPGLLAKVLSVLAEAGINITSIEQRTSGdGGEADIFIVVD 47
|
|
| HD |
pfam01966 |
HD domain; HD domains are metal dependent phosphohydrolases. |
523-592 |
8.53e-06 |
|
HD domain; HD domains are metal dependent phosphohydrolases.
Pssm-ID: 460398 [Multi-domain] Cd Length: 110 Bit Score: 45.69 E-value: 8.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 523 VASDLFRKIQPEHRAVIYIATLLHDVAKGRPED----------HSIAGARVARRLCPRLGFsaadtELVAWLIEEHLTMS 592
Cdd:pfam01966 11 LARELAEELGELDRELLLLAALLHDIGKGPFGDekpefeiflgHAVVGAEILRELEKRLGL-----EDVLKLILEHHESW 85
|
|
| ACT |
pfam01842 |
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ... |
850-895 |
9.94e-06 |
|
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to a wide range of metabolic enzymes that are regulated by amino acid concentration. Pairs of ACT domains bind specifically to a particular amino acid leading to regulation of the linked enzyme. The ACT domain is found in: D-3-phosphoglycerate dehydrogenase EC:1.1.1.95, which is inhibited by serine. Aspartokinase EC:2.7.2.4, which is regulated by lysine. Acetolactate synthase small regulatory subunit, which is inhibited by valine. Phenylalanine-4-hydroxylase EC:1.14.16.1, which is regulated by phenylalanine. Prephenate dehydrogenase EC:4.2.1.51. formyltetrahydrofolate deformylase EC:3.5.1.10, which is activated by methionine and inhibited by glycine. GTP pyrophosphokinase EC:2.7.6.5
Pssm-ID: 426468 [Multi-domain] Cd Length: 66 Bit Score: 43.84 E-value: 9.94e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1047432450 850 TVIEVSGLDRPGLLYQLTTAISKLNLNIASAHVATFGERARDVFYV 895
Cdd:pfam01842 1 TVLEVLVPDRPGLLARVLGALADRGINITSIEQGTSEDKGGIVFVV 46
|
|
| SpoT |
COG0317 |
(p)ppGpp synthase/hydrolase, HD superfamily [Signal transduction mechanisms, Transcription]; |
836-884 |
5.07e-05 |
|
(p)ppGpp synthase/hydrolase, HD superfamily [Signal transduction mechanisms, Transcription];
Pssm-ID: 440086 [Multi-domain] Cd Length: 722 Bit Score: 47.07 E-value: 5.07e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1047432450 836 EPEVTINNQWSD----RYTV-IEVSGLDRPGLLYQLTTAISKLNLNIASAHVAT 884
Cdd:COG0317 628 EPERLIDVEWGEdssgVFPVdIRIEALDRPGLLADITSVIAEEKINILSVNTRS 681
|
|
| ACT_RelA-SpoT |
cd04876 |
ACT domain found C-terminal of the RelA/SpoT domains; ACT_RelA-SpoT: the ACT domain found ... |
852-888 |
1.68e-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: 1.68e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1047432450 852 IEVSGLDRPGLLYQLTTAISKLNLNIASAHVATFGER 888
Cdd:cd04876 1 IRVEAIDRPGLLADITTVIAEEKINILSVNTRTDDDG 37
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|
| GcvR |
COG2716 |
Glycine cleavage system regulator GcvR [Amino acid transport and metabolism]; |
741-926 |
3.30e-04 |
|
Glycine cleavage system regulator GcvR [Amino acid transport and metabolism];
Pssm-ID: 442029 [Multi-domain] Cd Length: 174 Bit Score: 42.51 E-value: 3.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 741 LTILATDHPWLLSIIAGACASAGANIVDAqiytttdgraldtiaisreydrdedegrRATRIGE------MIEHVLEGKL 814
Cdd:COG2716 6 ITAIGPDRPGIVAALARAVSEHGCNILDS----------------------------RMARLGGefagilLVSGPWDAIA 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 815 RLPEVVARKAANRG-KVRAFVVEPEVTINNqwSDRYTViEVSGLDRPGLLYQLTTAISKLNLNIA--SAHVATFGERARD 891
Cdd:COG2716 58 KLEAALPALAAELGlLVTVKRTEPHEAPPA--GLPYVV-EVVGNDRPGIVAEVTQFLAERGINIEdlSTKTYPAPMSGTP 134
|
170 180 190
....*....|....*....|....*....|....*..
gi 1047432450 892 VFYVTdllgAQITAPTRQ--AAIKSALiHLLSSEDNV 926
Cdd:COG2716 135 LFSAQ----ITVHVPAGLdiDALRDAL-EDLADELNV 166
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|
| HDc |
smart00471 |
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ... |
495-606 |
4.23e-04 |
|
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: 41.13 E-value: 4.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 495 HHYTVDEHLIRCIGFLQEIerggndeftvasdlFRKIQPEHRAVIYIATLLHDVAKGRP-----------EDHSIAGARV 563
Cdd:smart00471 1 SDYHVFEHSLRVAQLAAAL--------------AEELGLLDIELLLLAALLHDIGKPGTpdsflvktsvlEDHHFIGAEI 66
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1047432450 564 ARrlcpRLGFSAADTELVAWLIEEHLTMSTVAQSRDLSDRKTI 606
Cdd:smart00471 67 LL----EEEEPRILEEILRTAILSHHERPDGLRGEPITLEARI 105
|
|
| RnaY |
COG1418 |
HD superfamily phosphodieaserase, includes HD domain of RNase Y [Translation, ribosomal ... |
538-588 |
1.11e-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: 1.11e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1047432450 538 VIYIATLLHDVAKGRP----EDHSIAGARVARRLCPRLGFSAADTELVAWLIEEH 588
Cdd:COG1418 43 VAKRAALLHDIGKAKDheveGSHAEIGAELARKYLESLGFPEEEIEAVVHAIEAH 97
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|
| NTP_transf_2 |
pfam01909 |
Nucleotidyltransferase domain; Members of this family belong to a large family of ... |
108-132 |
2.01e-03 |
|
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: 38.17 E-value: 2.01e-03
|
| ACT_6 |
pfam13740 |
ACT domain; ACT domains bind to amino acids and regulate associated enzyme domains. |
848-916 |
2.08e-03 |
|
ACT domain; ACT domains bind to amino acids and regulate associated enzyme domains.
Pssm-ID: 433446 [Multi-domain] Cd Length: 76 Bit Score: 37.92 E-value: 2.08e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1047432450 848 RYTVIEVSGLDRPGLLYQLTTAISKLNLNIASAHVATFGERardvfyVTdlLGAQITAP-TRQAAIKSAL 916
Cdd:pfam13740 1 EILLITATGPDRPGLTASLTAVLAEHGCNILDSGQAVIHNR------LS--LGLLVSGPwDALARLEKDL 62
|
|
| ACT_TyrKc |
cd04928 |
Uncharacterized, N-terminal ACT domain of an Arabidopsis/Oryza predicted tyrosine kinase and ... |
852-896 |
2.24e-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: 37.54 E-value: 2.24e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1047432450 852 IEVSGLDRPGLLYQLTTAISKLNLNIASAHV-ATFGERARDVFYVT 896
Cdd:cd04928 4 ITFAAGDKPKLLSQLSSLLGDLGLNIAEAHAfSTDDGLALDIFVVT 49
|
|
| ACT_GcvR_2 |
cd04869 |
ACT domains that comprise the Glycine Cleavage System Transcriptional Repressor (GcvR) protein, ... |
851-879 |
2.82e-03 |
|
ACT domains that comprise the Glycine Cleavage System Transcriptional Repressor (GcvR) protein, and other related domains; This CD includes the second of the two ACT domains that comprise the Glycine Cleavage System Transcriptional Repressor (GcvR) protein, and other related domains. The glycine cleavage enzyme system in Escherichia coli provides one-carbon units for cellular methylation reactions. This enzyme system, encoded by the gcvTHP operon and lpd gene, catalyzes the cleavage of glycine into CO2 + NH3 and transfers a one-carbon unit to tetrahydrofolate, producing 5,10-methylenetetrahydrofolate. The gcvTHP operon is activated by the GcvA protein in response to glycine and repressed by a GcvA/GcvR interaction in the absence of glycine. It has been proposed that the co-activator glycine acts through a mechanism of de-repression by binding to GcvR and preventing GcvR from interacting with GcvA to block GcvA's activator function. Evidence also suggests that GcvR interacts directly with GcvA rather than binding to DNA to cause repression. Members of this CD belong to the superfamily of ACT regulatory domains.
Pssm-ID: 153141 [Multi-domain] Cd Length: 81 Bit Score: 37.59 E-value: 2.82e-03
10 20
....*....|....*....|....*....
gi 1047432450 851 VIEVSGLDRPGLLYQLTTAISKLNLNIAS 879
Cdd:cd04869 1 VVEVVGNDRPGIVHEVTQFLAQRNINIED 29
|
|
| ACT_4 |
pfam13291 |
ACT domain; ACT domains bind to amino acids and regulate associated enzyme domains. These ACT ... |
848-884 |
4.49e-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: 36.77 E-value: 4.49e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1047432450 848 RYTV-IEVSGLDRPGLLYQLTTAISKLNLNIASAHVAT 884
Cdd:pfam13291 3 SYPVdLEVEAIDRPGLLADITQVISEEKANIVSVNAKT 40
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