|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05092 |
PRK05092 |
PII uridylyl-transferase; Provisional |
1-930 |
0e+00 |
|
PII uridylyl-transferase; Provisional
Pssm-ID: 235342 [Multi-domain] Cd Length: 931 Bit Score: 1680.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 1 MDSVVTPTPSVADDRFDTARITAAVDALAAKHSGREDVFRTSVAQLLKAEMVEARAVAQAVLLKDRHGRRCAERLCFVQD 80
Cdd:PRK05092 1 PDPPMAPRPLSLSEIFDRAALRAELDALAADAAGDPDALRAAVLALLKQALARGRAEARERLEADGSGRACARRLAYLTD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 81 EIIRILYSAATRHLYRSQVPTGAERMAVVATGGYGRGLMAPESDIDLLFILPYKQTAWGEQVAEAILYCLWDMGLKVGHA 160
Cdd:PRK05092 81 ELIRALYDFATTHLYPADNPSEGERLAVLAVGGYGRGELAPGSDIDLLFLLPYKQTAWAESVVEYMLYMLWDLGLKVGHA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 161 TRSVDESIRQARGDMTIRTAILETRFLTGDQPLYDELVERFDKEVVQGTAAEFVTAKLAEREERHRRAGQSRYLVEPNVK 240
Cdd:PRK05092 161 TRSIDECIRLAREDMTIRTALLEARFLAGDRALFEELETRFDKEVVKGTAAEFVAAKLAERDERHRRAGDSRYLVEPNVK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 241 DGKGGLRDLHTLFWIAKYVYRVREVNELVERGVFDAQEYRTFRRCADFLWSVRCNIHFFSGRAEERLSFDMQREIAIRLG 320
Cdd:PRK05092 241 EGKGGLRDLHTLFWIAKYVYRVRDAAELVKLGVFTREEYRLFRRAEDFLWAVRCHLHFLTGRAEERLSFDLQPEIAERMG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 321 YTSHPGMQDVERFMKHYFLVAKDVGDLTAILCAKLEDQQAKPAPVLSRVMARlrpsnhRRRVPESDDFIIDNNRINLAAP 400
Cdd:PRK05092 321 YTDHPGLSGVERFMKHYFLVAKDVGDLTRIFCAALEAQHAKRAPGLNRFARR------RRKALDSDGFVVDNGRINLADP 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 401 DVFKHDPVNLIRIFRLAQKNNLAFHPDAMRTVTRSLKLINTPLRENPEANRLFMEILTS-NDAEIVLRRMNETGVLGHFI 479
Cdd:PRK05092 395 DVFERDPVNLIRLFHLADRHGLDIHPDAMRLVTRSLRLIDAALREDPEANRLFLDILTSrRNPERVLRRMNEAGVLGRFI 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 480 RAFGKIVSMMQFNMYHHYTVDEHLLRCVGYLQDIERGG-NDEFTVASDLMRKIQPehRAVIYITTLLHDIAKGRPEDHSN 558
Cdd:PRK05092 475 PDFGRIVAMMQFNMYHHYTVDEHTIRAIGVLAEIERGElADEHPLASELMPKIES--RRALYVAVLLHDIAKGRPEDHSI 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 559 AGAKVARRLCPRLGFSAADTELIAWLIEQHLTMSTVAQSRDLSDRKTIENFAAVVQSVEQMKLLTILTTADIRGVGPGVW 638
Cdd:PRK05092 553 AGARIARRLCPRLGLSPAETETVAWLVEHHLLMSDTAQKRDLSDPKTIEDFADAVQSPERLKLLLILTVADIRAVGPGVW 632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 639 NGWKAQLLRTLYYETEPVLTGGFSEVNRAQRIEMAQREFRAAFTEWPEEELNAYIGRHYPAYWLKVELARKIRHARFLRA 718
Cdd:PRK05092 633 NGWKAQLLRTLYYETEEVLTGGFSELNRAERVAAAKEALREALSDWPKADRDAYLARHYPAYWLAVDLDTQARHARFIRD 712
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 719 SEQAGHKLAINVGFDEARGVTELTILATDHPWLLSIIAGACASAGANIVDAQIYTTTDGRALDTIAISREYDRDEDEGRR 798
Cdd:PRK05092 713 ADDAGRPLATEVRPDPARGVTEVTVLAADHPGLFSRIAGACAAAGANIVDARIFTTTDGRALDTFWIQDAFGRDEDEPRR 792
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 799 ATRIGEMIEDVLEGKLRLPEVVARRAAGRK-VRPFVVEPEVTLNNQWSDRYTVIEVSGLDRPGLLYQLTTAISKLNLNIA 877
Cdd:PRK05092 793 LARLAKAIEDALSGEVRLPEALAKRTKPKKrARAFHVPPRVTIDNEASNRFTVIEVNGRDRPGLLYDLTRALSDLNLNIA 872
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|...
gi 2049174268 878 SAHVATFGERARDVFYVTDLLGAQITAPTRQAAIKSALIHLLSSEDAVAKPAA 930
Cdd:PRK05092 873 SAHIATYGERAVDVFYVTDLFGLKITNEARQAAIRRALLAALAEGEAEARAAR 925
|
|
| GlnD |
COG2844 |
UTP:GlnB (protein PII) uridylyltransferase [Posttranslational modification, protein turnover, ... |
42-924 |
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: 1200.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 42 SVAQLLKAEMVEARAVAQAVLLKDRHGRRCAERLCFVQDEIIRilysaatrHLYRSQVPTGAERMAVVATGGYGRGLMAP 121
Cdd:COG2844 2 AALAALREALAEGRAALRERFRAGADGRELVRARAALVDQLLR--------ALWDLAGLTEPERLALVAVGGYGRGELAP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 122 ESDIDLLFILPYKQTAWGEQVAEAILYCLWDMGLKVGHATRSVDESIRQARGDMTIRTAILETRFLTGDQPLYDELVERF 201
Cdd:COG2844 74 HSDIDLLFLLPDKPTPALEEVIEAFLYLLWDLGLEVGHSVRTVDECLREAREDITVRTALLEARLLAGDEALFEELRERF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 202 DKEVVqGTAAEFVTAKLAEREERHRRAGQSRYLVEPNVKDGKGGLRDLHTLFWIAKYVYRVREVNELVERGVFDAQEYRT 281
Cdd:COG2844 154 RADVF-WDSRAFFEAKLAEQRERHAKYGDTRYNLEPNIKEGPGGLRDLQTLLWIAKRHFGVRSLEELVKKGLLTEEEYRE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 282 FRRCADFLWSVRCNIHFFSGRAEERLSFDMQREIAIRLGYTSHPGMQDVERFMKHYFLVAKDVGDLTAILCAKLEDQQAK 361
Cdd:COG2844 233 LRRAEDFLWRVRFALHLLAGRAEDRLLFDLQREVAERLGYQDTEGNRAVERFMQRYYRTAKAVGRLNEILLQRLEEAILK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 362 PAPVlsrvmarlrpsnhRRRVPESDDFIIDNNRINLAAPDVFKHDPVNLIRIFRLAQKN--NLAFHPDAMRTVTRSLKLI 439
Cdd:COG2844 313 PPGL-------------RRPRPINEGFQLRNGRLEVADPDVFERDPVALLRLFLLAAQHpeGLGIHPDTLRLLRRALRLI 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 440 NTPLRENPEANRLFMEILTS-NDAEIVLRRMNETGVLGHFIRAFGKIVSMMQFNMYHHYTVDEHLLRCVGYLQDIERG-G 517
Cdd:COG2844 380 DDAFRRDPEARRLFLEILRQpRGITRALRRMNEYGVLGRYIPEFGRIVGQMQFDLFHVYTVDEHTLRVVRNLRRFERGeL 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 518 NDEFTVASDLMRKIqpEHRAVIYITTLLHDIAKGRPEDHSNAGAKVARRLCPRLGFSAADTELIAWLIEQHLTMSTVAQS 597
Cdd:COG2844 460 AEEFPLASELIAEL--PKPELLYLAALFHDIAKGRGGDHSELGAEDARRFCPRHGLSPEDTELVAWLVRHHLLMSHTAQR 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 598 RDLSDRKTIENFAAVVQSVEQMKLLTILTTADIRGVGPGVWNGWKAQLLRTLYYETEPVLTGGFSEVNRAQRIEMAQREF 677
Cdd:COG2844 538 RDISDPEVIRDFARLVGSEERLDYLYLLTVADIRATGPKVWNSWKASLLRELYRATLRALRGGLEPPDREERIEERKEEA 617
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 678 RAAFTE--WPEEELNAYIGRHYPAYWLKVELARKIRHARFLRASEQAGHKLaINVGFDEARGVTELTILATDHPWLLSII 755
Cdd:COG2844 618 LALLADqgWDEEEIEALWARLPDDYFLRHDPEEIAWHARLLLRADDSGKPL-VLIRPDPDRGGTEVFVYTPDRPGLFARI 696
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 756 AGACASAGANIVDAQIYTTTDGRALDTIAISREYDRDEDEGRRATRIGEMIEDVLEGKLRLPEVVARRaAGRKVRPFVVE 835
Cdd:COG2844 697 AGALAALGLNILDARIHTTRDGYALDTFIVLDPDGEPIDDPDRLERIEQALEEALSGEVPLPEPLARR-LSRRLRHFPVP 775
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 836 PEVTLNNQWSDRYTVIEVSGLDRPGLLYQLTTAISKLNLNIASAHVATFGERARDVFYVTDLLGAQITAPTRQAAIKSAL 915
Cdd:COG2844 776 PRVTFDNDASNRYTVLEVSALDRPGLLYDIARVLADLGLNIHSAKIATLGERVEDVFYVTDLDGQKLTDPERQEALREAL 855
|
....*....
gi 2049174268 916 IHLLSSEDA 924
Cdd:COG2844 856 LEALDEEAE 864
|
|
| UTase_glnD |
TIGR01693 |
[Protein-PII] uridylyltransferase; This model describes GlnD, the uridylyltransferase ... |
55-916 |
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: 877.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 55 RAVAQAVLLKDRHGRRCAERLCFVQDEIIRILYSAATRHLyrsqvptgAERMAVVATGGYGRGLMAPESDIDLLFILPYK 134
Cdd:TIGR01693 1 REELLEEFARGGDGRELREGRSDLTDLLLIRLWDFIGISE--------HSGIALVAVGGYGRGELAPYSDIDLLFLHDGK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 135 QTAWGEQVAEAILYCLWDMGLKVGHATRSVDESIRQARGDMTIRTAILETRFLTGDQPLYDELVERFDKEVVQGTAAEFV 214
Cdd:TIGR01693 73 PAEEVEPKIERFLYPLWDLGFEVGHSVRTLEECARIAKADLTVATNLLEARHLAGDEALFFRLKERVRREDWRNTARSFL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 215 TAKLAEREERHRRAGQSRYLVEPNVKDGKGGLRDLHTLFWIAKYVYRVREVNELVERGVFDAQEYRTFRRCADFLWSVRC 294
Cdd:TIGR01693 153 AAKVEEQDERHARYGDTAYNLEPDIKEGPGGLRDLHTLFWVALYQLGVRRLEDLVKQGFLTDAEYKLLAEARDFLWDVRF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 295 NIHFFSGRAEERLSFDMQREIAIRLGYTShPGMQDVERFMKHYFLVAKDVGDLTAILCAKLEDQQAK--PAPVLSRvmar 372
Cdd:TIGR01693 233 ALHLTTGRADDRLLFDHQDEIAAALGYGD-EGNPAVERFMRRYFQAARRIGYLTEAFLRHYEEALLSrgPSARVRR---- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 373 lrpsnhRRRVPESDDFIIDNNRINLAAPDVFKHDPVNLIRIFRLAQKNNLAFHPDAMRTVTRSLKLINTPLRENPEANRL 452
Cdd:TIGR01693 308 ------PKRRPLDEGFVEDGGELVLARTAVFERDPALLLRLFAIAAQRGLPIHPAALRQLTASLPLLPTPLREDPEAREL 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 453 FMEILTS-NDAEIVLRRMNETGVLGHFIRAFGKIVSMMQFNMYHHYTVDEHLLRCVGYLQDIERGGN-DEFTVASDLMRK 530
Cdd:TIGR01693 382 FLELLTSgNGTVRALRAMNRAGVLGRFLPEWGRIVGQMQFDLFHVYTVDEHTLRTVVHLAPFARGRLaREHPLASELMPK 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 531 IqpEHRAVIYITTLLHDIAKGRPEDHSNAGAKVARRLCPRLGFSAADTELIAWLIEQHLTMSTVAQSRDLSDRKTIENFA 610
Cdd:TIGR01693 462 I--EDPELLYLAALLHDIGKGRGGDHSVLGAEDARDVCPRLGLDRPDTELVAWLVRNHLLMSITAQRRDLNDPKTVFAFA 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 611 AVVQSVEQMKLLTILTTADIRGVGPGVWNGWKAQLLRTLYYETEPVLTGGFSEV--NRAQRIEMAQREFRAAFTEWPEEE 688
Cdd:TIGR01693 540 EAVGDPERLEYLLALTVADIRATGPGVWNSWKASLLRDLYNRTEQVLRGGLEPPadPAEPIAEQRKLAVALLRTDYTSNE 619
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 689 LNAYIGRHYPAYWLKVELARKIRHARFLRASEQAGHKLAINVGfDEARGVTELTILATDHPWLLSIIAGACASAGANIVD 768
Cdd:TIGR01693 620 AEVLWLRAYDDYFLRFTHKEIAWHAESLRRALSSGGPLALIDG-TRPSGGTEVFIYAPDQPGLFAKVAGALAMLSLSVHD 698
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 769 AQIYTTTDGRALDTIAISREYDRDEDEGRRATRIGEMIEDVLEGKLRLPEVV-ARRAAGRKVRPFVVEPEVTLNNQWSDR 847
Cdd:TIGR01693 699 AQVNTTKDGVALDTFVVQDLFGSPPAAERVFQELLQGLVDVLAGLAKDPDTIsARRARRRRLQHFAVPPRVTILNTASRK 778
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2049174268 848 YTVIEVSGLDRPGLLYQLTTAISKLNLNIASAHVATFGERARDVFYVTDLLGAQITApTRQAAIKSALI 916
Cdd:TIGR01693 779 ATIMEVRALDRPGLLARVGRTLEELGLSIQSAKITTFGEKAEDVFYVTDLFGLKLTD-EEEQRLLEVLA 846
|
|
| GlnD_UR_UTase |
pfam08335 |
GlnD PII-uridylyltransferase; This is a family of bifunctional uridylyl-removing enzymes ... |
213-351 |
7.64e-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: 166.60 E-value: 7.64e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 213 FVTAKLAEREERHRRAGQSRYLVEPNVKDGKGGLRDLHTLFWIAKYVYRVREVNELVERGVFDAQEYRTFRRCADFLWSV 292
Cdd:pfam08335 2 FMKAKIEEQVARHGRYGDTAYNLEPNIKLGPGGLRDIEFIVWIAQLIFTLRALEELVELGLLTREEARELRRAYRFLRRV 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2049174268 293 RCNIHFFSGRAEERLSFDMQREIAIRLGYTsHPGMQDVERFMKHYFLVAKDVGDLTAIL 351
Cdd:pfam08335 82 RHRLHLLADRQTDRLPFDLQRRLARALGYA-RDGWLAVERFMRRLFRHAHRVSRLFEIL 139
|
|
| NT_GlnE_GlnD_like |
cd05401 |
Nucleotidyltransferase (NT) domain of Escherichia coli adenylyltransferase (GlnE), Escherichia ... |
48-201 |
9.80e-25 |
|
Nucleotidyltransferase (NT) domain of Escherichia coli adenylyltransferase (GlnE), Escherichia coli uridylyl transferase (GlnD), and similar proteins; Escherichia coli GlnD and -E participate in the Glutamine synthetase (GS)/Glutamate synthase (GOGAT) pathway for the assimilation of ammonium nitrogen. In nitrogen sufficiency, GlnE adenylates GS, reducing GS activity; when nitrogen is limiting, GlnE deadenylates GS-AMP, restoring GS activity. When nitrogen is limiting, GlnD uridylylates the nitrogen regulatory protein PII to PII-UTP, and in nitrogen sufficiency, it removes the modifying groups. The activity of Escherichia coli GlnE is modulated by PII-proteins. PII-UMP promotes GlnE deadenylation activity, and PII promotes GlnE adenylation activity. Escherichia coli GlnE has two separate NT domains. The N-terminal NT domain catalyzes the deadenylylation of GS, and the C-terminal NT domain the adenylylation reaction. The majority of proteins in this family contain a C-terminal NT domain which is associated with a cystathionine beta-synthase (CBS) domain pair and a CAP_ED (cAMP receptor protein effector ) domain. This family belongs to the Pol beta-like NT superfamily. In the majority of enzymes in this superfamily, two carboxylates, Dx[D/E], together with a third more distal carboxylate, coordinate two divalent metal cations involved in a two-metal ion mechanism of nucleotide addition. For the majority of proteins in this family, these carboxylate residues are conserved.
Pssm-ID: 143391 [Multi-domain] Cd Length: 172 Bit Score: 101.65 E-value: 9.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 48 KAEMVEARAVAQAVLLKDRHGRRCAERLCFVQDEIIRILYSAATRHLYRsqvPTGAERMAVVATGGYGRGLMAPESDIDL 127
Cdd:cd05401 1 RAKLRQLRRILRRDLLGGASIRAISRALSDLADALLRRALELALAELGK---GPPPVPFALLALGSYGRGELNPSSDQDL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 128 LFILPYKQ---TAWGEQVAEAI---------LYCLWDMGLKVGHATRSVDESIRQARGDMTI------RTAILETRFLTG 189
Cdd:cd05401 78 LLLYDDDGdevAAYFEELAERLikilseaggPYCLGDVMLRPPGWRRSLAEWLDAARDWLTEpgrlweRTALLDARPVAG 157
|
170
....*....|..
gi 2049174268 190 DQPLYDELVERF 201
Cdd:cd05401 158 DRALAEELRRRI 169
|
|
| HDc |
smart00471 |
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ... |
495-606 |
6.37e-03 |
|
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: 37.66 E-value: 6.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 495 HHYTVDEHLLRCVGYLQDIERGGNDEFtvasdlmrkiqpehRAVIYITTLLHDIAKGRP-----------EDHSNAGAKV 563
Cdd:smart00471 1 SDYHVFEHSLRVAQLAAALAEELGLLD--------------IELLLLAALLHDIGKPGTpdsflvktsvlEDHHFIGAEI 66
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2049174268 564 ARrlcpRLGFSAADTELIAWLIEQHLTMSTVAQSRDLSDRKTI 606
Cdd:smart00471 67 LL----EEEEPRILEEILRTAILSHHERPDGLRGEPITLEARI 105
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05092 |
PRK05092 |
PII uridylyl-transferase; Provisional |
1-930 |
0e+00 |
|
PII uridylyl-transferase; Provisional
Pssm-ID: 235342 [Multi-domain] Cd Length: 931 Bit Score: 1680.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 1 MDSVVTPTPSVADDRFDTARITAAVDALAAKHSGREDVFRTSVAQLLKAEMVEARAVAQAVLLKDRHGRRCAERLCFVQD 80
Cdd:PRK05092 1 PDPPMAPRPLSLSEIFDRAALRAELDALAADAAGDPDALRAAVLALLKQALARGRAEARERLEADGSGRACARRLAYLTD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 81 EIIRILYSAATRHLYRSQVPTGAERMAVVATGGYGRGLMAPESDIDLLFILPYKQTAWGEQVAEAILYCLWDMGLKVGHA 160
Cdd:PRK05092 81 ELIRALYDFATTHLYPADNPSEGERLAVLAVGGYGRGELAPGSDIDLLFLLPYKQTAWAESVVEYMLYMLWDLGLKVGHA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 161 TRSVDESIRQARGDMTIRTAILETRFLTGDQPLYDELVERFDKEVVQGTAAEFVTAKLAEREERHRRAGQSRYLVEPNVK 240
Cdd:PRK05092 161 TRSIDECIRLAREDMTIRTALLEARFLAGDRALFEELETRFDKEVVKGTAAEFVAAKLAERDERHRRAGDSRYLVEPNVK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 241 DGKGGLRDLHTLFWIAKYVYRVREVNELVERGVFDAQEYRTFRRCADFLWSVRCNIHFFSGRAEERLSFDMQREIAIRLG 320
Cdd:PRK05092 241 EGKGGLRDLHTLFWIAKYVYRVRDAAELVKLGVFTREEYRLFRRAEDFLWAVRCHLHFLTGRAEERLSFDLQPEIAERMG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 321 YTSHPGMQDVERFMKHYFLVAKDVGDLTAILCAKLEDQQAKPAPVLSRVMARlrpsnhRRRVPESDDFIIDNNRINLAAP 400
Cdd:PRK05092 321 YTDHPGLSGVERFMKHYFLVAKDVGDLTRIFCAALEAQHAKRAPGLNRFARR------RRKALDSDGFVVDNGRINLADP 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 401 DVFKHDPVNLIRIFRLAQKNNLAFHPDAMRTVTRSLKLINTPLRENPEANRLFMEILTS-NDAEIVLRRMNETGVLGHFI 479
Cdd:PRK05092 395 DVFERDPVNLIRLFHLADRHGLDIHPDAMRLVTRSLRLIDAALREDPEANRLFLDILTSrRNPERVLRRMNEAGVLGRFI 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 480 RAFGKIVSMMQFNMYHHYTVDEHLLRCVGYLQDIERGG-NDEFTVASDLMRKIQPehRAVIYITTLLHDIAKGRPEDHSN 558
Cdd:PRK05092 475 PDFGRIVAMMQFNMYHHYTVDEHTIRAIGVLAEIERGElADEHPLASELMPKIES--RRALYVAVLLHDIAKGRPEDHSI 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 559 AGAKVARRLCPRLGFSAADTELIAWLIEQHLTMSTVAQSRDLSDRKTIENFAAVVQSVEQMKLLTILTTADIRGVGPGVW 638
Cdd:PRK05092 553 AGARIARRLCPRLGLSPAETETVAWLVEHHLLMSDTAQKRDLSDPKTIEDFADAVQSPERLKLLLILTVADIRAVGPGVW 632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 639 NGWKAQLLRTLYYETEPVLTGGFSEVNRAQRIEMAQREFRAAFTEWPEEELNAYIGRHYPAYWLKVELARKIRHARFLRA 718
Cdd:PRK05092 633 NGWKAQLLRTLYYETEEVLTGGFSELNRAERVAAAKEALREALSDWPKADRDAYLARHYPAYWLAVDLDTQARHARFIRD 712
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 719 SEQAGHKLAINVGFDEARGVTELTILATDHPWLLSIIAGACASAGANIVDAQIYTTTDGRALDTIAISREYDRDEDEGRR 798
Cdd:PRK05092 713 ADDAGRPLATEVRPDPARGVTEVTVLAADHPGLFSRIAGACAAAGANIVDARIFTTTDGRALDTFWIQDAFGRDEDEPRR 792
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 799 ATRIGEMIEDVLEGKLRLPEVVARRAAGRK-VRPFVVEPEVTLNNQWSDRYTVIEVSGLDRPGLLYQLTTAISKLNLNIA 877
Cdd:PRK05092 793 LARLAKAIEDALSGEVRLPEALAKRTKPKKrARAFHVPPRVTIDNEASNRFTVIEVNGRDRPGLLYDLTRALSDLNLNIA 872
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|...
gi 2049174268 878 SAHVATFGERARDVFYVTDLLGAQITAPTRQAAIKSALIHLLSSEDAVAKPAA 930
Cdd:PRK05092 873 SAHIATYGERAVDVFYVTDLFGLKITNEARQAAIRRALLAALAEGEAEARAAR 925
|
|
| GlnD |
COG2844 |
UTP:GlnB (protein PII) uridylyltransferase [Posttranslational modification, protein turnover, ... |
42-924 |
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: 1200.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 42 SVAQLLKAEMVEARAVAQAVLLKDRHGRRCAERLCFVQDEIIRilysaatrHLYRSQVPTGAERMAVVATGGYGRGLMAP 121
Cdd:COG2844 2 AALAALREALAEGRAALRERFRAGADGRELVRARAALVDQLLR--------ALWDLAGLTEPERLALVAVGGYGRGELAP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 122 ESDIDLLFILPYKQTAWGEQVAEAILYCLWDMGLKVGHATRSVDESIRQARGDMTIRTAILETRFLTGDQPLYDELVERF 201
Cdd:COG2844 74 HSDIDLLFLLPDKPTPALEEVIEAFLYLLWDLGLEVGHSVRTVDECLREAREDITVRTALLEARLLAGDEALFEELRERF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 202 DKEVVqGTAAEFVTAKLAEREERHRRAGQSRYLVEPNVKDGKGGLRDLHTLFWIAKYVYRVREVNELVERGVFDAQEYRT 281
Cdd:COG2844 154 RADVF-WDSRAFFEAKLAEQRERHAKYGDTRYNLEPNIKEGPGGLRDLQTLLWIAKRHFGVRSLEELVKKGLLTEEEYRE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 282 FRRCADFLWSVRCNIHFFSGRAEERLSFDMQREIAIRLGYTSHPGMQDVERFMKHYFLVAKDVGDLTAILCAKLEDQQAK 361
Cdd:COG2844 233 LRRAEDFLWRVRFALHLLAGRAEDRLLFDLQREVAERLGYQDTEGNRAVERFMQRYYRTAKAVGRLNEILLQRLEEAILK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 362 PAPVlsrvmarlrpsnhRRRVPESDDFIIDNNRINLAAPDVFKHDPVNLIRIFRLAQKN--NLAFHPDAMRTVTRSLKLI 439
Cdd:COG2844 313 PPGL-------------RRPRPINEGFQLRNGRLEVADPDVFERDPVALLRLFLLAAQHpeGLGIHPDTLRLLRRALRLI 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 440 NTPLRENPEANRLFMEILTS-NDAEIVLRRMNETGVLGHFIRAFGKIVSMMQFNMYHHYTVDEHLLRCVGYLQDIERG-G 517
Cdd:COG2844 380 DDAFRRDPEARRLFLEILRQpRGITRALRRMNEYGVLGRYIPEFGRIVGQMQFDLFHVYTVDEHTLRVVRNLRRFERGeL 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 518 NDEFTVASDLMRKIqpEHRAVIYITTLLHDIAKGRPEDHSNAGAKVARRLCPRLGFSAADTELIAWLIEQHLTMSTVAQS 597
Cdd:COG2844 460 AEEFPLASELIAEL--PKPELLYLAALFHDIAKGRGGDHSELGAEDARRFCPRHGLSPEDTELVAWLVRHHLLMSHTAQR 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 598 RDLSDRKTIENFAAVVQSVEQMKLLTILTTADIRGVGPGVWNGWKAQLLRTLYYETEPVLTGGFSEVNRAQRIEMAQREF 677
Cdd:COG2844 538 RDISDPEVIRDFARLVGSEERLDYLYLLTVADIRATGPKVWNSWKASLLRELYRATLRALRGGLEPPDREERIEERKEEA 617
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 678 RAAFTE--WPEEELNAYIGRHYPAYWLKVELARKIRHARFLRASEQAGHKLaINVGFDEARGVTELTILATDHPWLLSII 755
Cdd:COG2844 618 LALLADqgWDEEEIEALWARLPDDYFLRHDPEEIAWHARLLLRADDSGKPL-VLIRPDPDRGGTEVFVYTPDRPGLFARI 696
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 756 AGACASAGANIVDAQIYTTTDGRALDTIAISREYDRDEDEGRRATRIGEMIEDVLEGKLRLPEVVARRaAGRKVRPFVVE 835
Cdd:COG2844 697 AGALAALGLNILDARIHTTRDGYALDTFIVLDPDGEPIDDPDRLERIEQALEEALSGEVPLPEPLARR-LSRRLRHFPVP 775
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 836 PEVTLNNQWSDRYTVIEVSGLDRPGLLYQLTTAISKLNLNIASAHVATFGERARDVFYVTDLLGAQITAPTRQAAIKSAL 915
Cdd:COG2844 776 PRVTFDNDASNRYTVLEVSALDRPGLLYDIARVLADLGLNIHSAKIATLGERVEDVFYVTDLDGQKLTDPERQEALREAL 855
|
....*....
gi 2049174268 916 IHLLSSEDA 924
Cdd:COG2844 856 LEALDEEAE 864
|
|
| UTase_glnD |
TIGR01693 |
[Protein-PII] uridylyltransferase; This model describes GlnD, the uridylyltransferase ... |
55-916 |
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: 877.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 55 RAVAQAVLLKDRHGRRCAERLCFVQDEIIRILYSAATRHLyrsqvptgAERMAVVATGGYGRGLMAPESDIDLLFILPYK 134
Cdd:TIGR01693 1 REELLEEFARGGDGRELREGRSDLTDLLLIRLWDFIGISE--------HSGIALVAVGGYGRGELAPYSDIDLLFLHDGK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 135 QTAWGEQVAEAILYCLWDMGLKVGHATRSVDESIRQARGDMTIRTAILETRFLTGDQPLYDELVERFDKEVVQGTAAEFV 214
Cdd:TIGR01693 73 PAEEVEPKIERFLYPLWDLGFEVGHSVRTLEECARIAKADLTVATNLLEARHLAGDEALFFRLKERVRREDWRNTARSFL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 215 TAKLAEREERHRRAGQSRYLVEPNVKDGKGGLRDLHTLFWIAKYVYRVREVNELVERGVFDAQEYRTFRRCADFLWSVRC 294
Cdd:TIGR01693 153 AAKVEEQDERHARYGDTAYNLEPDIKEGPGGLRDLHTLFWVALYQLGVRRLEDLVKQGFLTDAEYKLLAEARDFLWDVRF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 295 NIHFFSGRAEERLSFDMQREIAIRLGYTShPGMQDVERFMKHYFLVAKDVGDLTAILCAKLEDQQAK--PAPVLSRvmar 372
Cdd:TIGR01693 233 ALHLTTGRADDRLLFDHQDEIAAALGYGD-EGNPAVERFMRRYFQAARRIGYLTEAFLRHYEEALLSrgPSARVRR---- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 373 lrpsnhRRRVPESDDFIIDNNRINLAAPDVFKHDPVNLIRIFRLAQKNNLAFHPDAMRTVTRSLKLINTPLRENPEANRL 452
Cdd:TIGR01693 308 ------PKRRPLDEGFVEDGGELVLARTAVFERDPALLLRLFAIAAQRGLPIHPAALRQLTASLPLLPTPLREDPEAREL 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 453 FMEILTS-NDAEIVLRRMNETGVLGHFIRAFGKIVSMMQFNMYHHYTVDEHLLRCVGYLQDIERGGN-DEFTVASDLMRK 530
Cdd:TIGR01693 382 FLELLTSgNGTVRALRAMNRAGVLGRFLPEWGRIVGQMQFDLFHVYTVDEHTLRTVVHLAPFARGRLaREHPLASELMPK 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 531 IqpEHRAVIYITTLLHDIAKGRPEDHSNAGAKVARRLCPRLGFSAADTELIAWLIEQHLTMSTVAQSRDLSDRKTIENFA 610
Cdd:TIGR01693 462 I--EDPELLYLAALLHDIGKGRGGDHSVLGAEDARDVCPRLGLDRPDTELVAWLVRNHLLMSITAQRRDLNDPKTVFAFA 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 611 AVVQSVEQMKLLTILTTADIRGVGPGVWNGWKAQLLRTLYYETEPVLTGGFSEV--NRAQRIEMAQREFRAAFTEWPEEE 688
Cdd:TIGR01693 540 EAVGDPERLEYLLALTVADIRATGPGVWNSWKASLLRDLYNRTEQVLRGGLEPPadPAEPIAEQRKLAVALLRTDYTSNE 619
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 689 LNAYIGRHYPAYWLKVELARKIRHARFLRASEQAGHKLAINVGfDEARGVTELTILATDHPWLLSIIAGACASAGANIVD 768
Cdd:TIGR01693 620 AEVLWLRAYDDYFLRFTHKEIAWHAESLRRALSSGGPLALIDG-TRPSGGTEVFIYAPDQPGLFAKVAGALAMLSLSVHD 698
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 769 AQIYTTTDGRALDTIAISREYDRDEDEGRRATRIGEMIEDVLEGKLRLPEVV-ARRAAGRKVRPFVVEPEVTLNNQWSDR 847
Cdd:TIGR01693 699 AQVNTTKDGVALDTFVVQDLFGSPPAAERVFQELLQGLVDVLAGLAKDPDTIsARRARRRRLQHFAVPPRVTILNTASRK 778
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2049174268 848 YTVIEVSGLDRPGLLYQLTTAISKLNLNIASAHVATFGERARDVFYVTDLLGAQITApTRQAAIKSALI 916
Cdd:TIGR01693 779 ATIMEVRALDRPGLLARVGRTLEELGLSIQSAKITTFGEKAEDVFYVTDLFGLKLTD-EEEQRLLEVLA 846
|
|
| PRK03059 |
PRK03059 |
PII uridylyl-transferase; Provisional |
47-920 |
5.23e-175 |
|
PII uridylyl-transferase; Provisional
Pssm-ID: 235101 [Multi-domain] Cd Length: 856 Bit Score: 529.86 E-value: 5.23e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 47 LKAEMVEARAVAQAVLLKDRHGRRCAERLCFVQDEIIRILYSAAtrhlyrsQVPTGAermAVVATGGYGRGLMAPESDID 126
Cdd:PRK03059 13 LRAELKAAKAALLARFRQAPNVTALLHALSRLVDQALRRLWQEC-------GLPAGA---ALVAVGGYGRGELFPYSDVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 127 LLFILPYKQTAWGEQVAEAILYCLWDMGLKVGHATRSVDESIRQARGDMTIRTAILETRFLTGDQPLYDELVERFDKevv 206
Cdd:PRK03059 83 LLVLLPDAPDAALDARIERFIGLCWDLGLEIGSSVRTVDECIEEAAQDVTVQTSLLEARLLTGSAALFERFQRRYRA--- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 207 QGTAAEFVTAKLAEREERHRRAGQSRYLVEPNVKDGKGGLRDLHTLFWIAKYVYRVREVNELVERGVFDAQEYRTFRRCA 286
Cdd:PRK03059 160 ALDPRAFFQAKLLEMRQRHAKFQDTPYSLEPNCKESPGGLRDLQTILWIARAAGLGSSWRELAKRGLITDREARQLRRNE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 287 DFLWSVRCNIHFFSGRAEERLSFDMQREIAIRLGYTSHPGMQDVERFMKHYFLVAKDVGDLTAILCAKLEdqqakpapvl 366
Cdd:PRK03059 240 RFLKTLRARLHLLAGRREDRLVFDLQTALAESFGYRPTAAKRASEQLMRRYYWAAKAVTQLNTILLQNIE---------- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 367 srvmARLRPSNHRRRVPESDDFIIDNNRINLAAPDVFKHDPVNLIRIFRLAQKN-NLA-FHPDAMRTVTRSLKLINTPLR 444
Cdd:PRK03059 310 ----ARLFPSTSGITRVINERFVEKQGMLEIASDDLFERHPHAILEAFLLYQQTpGLKgLSARTLRALYNARDVMNAAFR 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 445 ENPEANRLFMEILtSNDAEIV--LRRMNETGVLGHFIRAFGKIVSMMQFNMYHHYTVDEHLLRCvgyLQDIERGGNDEFT 522
Cdd:PRK03059 386 RDPVNRALFMQIL-QQPRGIThaLRLMNQTSVLGRYLPNFRRIVGQMQHDLFHVYTVDQHILMV---LRNLRRFAMAEHA 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 523 ----VASDLMRKI-QPEhraVIYITTLLHDIAKGRPEDHSNAGAKVARRLCPRLGFSAADTELIAWLIEQHLTMSTVAQS 597
Cdd:PRK03059 462 heypFCSQLIANFdRPW---LLYVAALFHDIAKGRGGDHSTLGAVDARRFCRQHGLAREDAELVVWLVEHHLTMSQVAQK 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 598 RDLSDRKTIENFAAVVQSVEQMKLLTILTTADIRGVGPGVWNGWKAQLLRTLYYETEPVLTGgfSEVNRAQRIEMAQREF 677
Cdd:PRK03059 539 QDLSDPEVIARFAELVGDERRLTALYLLTVADIRGTSPKVWNAWKGKLLEDLYRATLRVLGG--AAPDAHSELEARKEEA 616
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 678 RA--AFTEWPEEElnayigrhYPAYWLKVELARKIRHArflrASEQAGHK--LAINVGFDE----AR------GVtELTI 743
Cdd:PRK03059 617 LAllRLEALPDDA--------HEALWDQLDVGYFLRHD----AADIAWHTrhLYRHVDTDTpivrARlspageGL-QVMV 683
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 744 LATDHPWLLSIIAGACASAGANIVDAQIYTTTDGRALDTIAISreyDRDEDEGRRAtrIGEMIEDVLEGKLR----LPEV 819
Cdd:PRK03059 684 YTPDQPDLFARICGYFDRAGFSILDARVHTTRHGYALDTFQVL---DPEEDVHYRD--IINLVEHELAERLAeqapLPEP 758
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 820 VARRAAgRKVRPFVVEPEVTLNNQWSDRYTVIEVSGLDRPGLLYQLTTAISKLNLNIASAHVATFGERARDVFYVTdllG 899
Cdd:PRK03059 759 SKGRLS-RQVKHFPITPRVDLRPDERGQYYILSVSANDRPGLLYAIARVLAEHRVSVHTAKINTLGERVEDTFLID---G 834
|
890 900
....*....|....*....|.
gi 2049174268 900 AQITAPTRQAAIKSALIHLLS 920
Cdd:PRK03059 835 SGLSDNRLQIQLETELLDALA 855
|
|
| glnD |
PRK00275 |
PII uridylyl-transferase; Provisional |
9-920 |
1.44e-174 |
|
PII uridylyl-transferase; Provisional
Pssm-ID: 234709 [Multi-domain] Cd Length: 895 Bit Score: 530.01 E-value: 1.44e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 9 PSVADDRFDTARITAAvdaLAAKHSGREdVFRTSVAQllkaemveARAVAQAVLLKDRHGRR-CAERLCFVqDEIIRILY 87
Cdd:PRK00275 2 PQVDPELFDRGQFQAE---LALKASPIA-AFKKAIRQ--------AREVLDERFRSGRDIRRlIEDRAWFV-DQILQQAW 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 88 SaatrhlyRSQVPTGAeRMAVVATGGYGRGLMAPESDIDLLFILPYK-QTAWGEQVaEAILYCLWDMGLKVGHATRSVDE 166
Cdd:PRK00275 69 H-------QFDWSDDA-DIALVAVGGYGRGELHPYSDIDLLILLDSAdHEEFREPI-ERFLTLLWDIGLEIGQSVRSVDE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 167 SIRQARGDMTIRTAILETRFLTGDQPLYDELVERFDKEVVQgTAAEFVTAKLAEREERHRRAGQSRYLVEPNVKDGKGGL 246
Cdd:PRK00275 140 CAEEARADLTVITNLMESRTIAGPESLRQRMLEVTSSEHMW-PSKEFFLAKRAEQKARHHKYNDTEYNLEPNVKGSPGGL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 247 RDLHTLFWIAKYVYRVREVNELVERGVFDAQEYRTFRRCADFLWSVRCNIHFFSGRAEERLSFDMQREIAIRLGYTSHPG 326
Cdd:PRK00275 219 RDIQTILWVAKRQFGTLNLHALVGEGFLTESEYGLLASGQEFLWKVRYALHMLAGRAEDRLLFDHQRSIATLLGYEDSDA 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 327 MQDVERFMKHYFLVAKDVGDLTAILCAKLEDqqakpapvlsrvmARLRPSNHRRRVPESDDFIIDNNRINLAAPDVFKHD 406
Cdd:PRK00275 299 KLAVEQFMQKYYRVVMALAELNDLILQHFEE-------------VILAADDSGTIQPLNSRFQLRDGYIEATHPNVFKRT 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 407 PVNLIRIFRLaqknnLAFHP-------DAMRTVTRSLKLINTPLRENPEANRLFMEILTSNDAeIV--LRRMNETGVLGH 477
Cdd:PRK00275 366 PFALLEIFVL-----MAQHPeikgvraDTIRLLREHRHLIDDAFRNDIRNTSLFIELFKCPIG-IHrnLRRMNRYGILGR 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 478 FIRAFGKIVSMMQFNMYHHYTVDEHLLRCVGYLQDIER-GGNDEFTVASDLMRKIQ-PEhraVIYITTLLHDIAKGRPED 555
Cdd:PRK00275 440 YLPEFGHIVGQMQHDLFHIYTVDAHTLNLIKNLRKLRYpEVSEKFPLASKLMGRLPkPE---LLYIAGLYHDIGKGRGGD 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 556 HSNAGAKVARRLCPRLGFSAADTELIAWLIEQHLTMSTVAQSRDLSDRKTIENFAAVVQSVEQMKLLTILTTADIRGVGP 635
Cdd:PRK00275 517 HSELGAVDAEAFCQRHQLPAWDTRLVVWLVENHLLMSTTAQRKDLSDPQVIHDFALKVGDQTHLDYLYVLTVADINATNP 596
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 636 GVWNGWKAQLLRTLYYETEPVLTGGFSE-VNRAQRIEMAQREFRA-----AFTEWPEEELNAYIGRHYpaywlkvelark 709
Cdd:PRK00275 597 TLWNSWRASLLRQLYTETKRALRRGLENpVDREEQIRQTQSAALDilvrkGTDPDDAEQLWSQLGDDY------------ 664
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 710 irharFLR--ASEQAGHKLAI--------------NVGFDEARGVTELTILATDHPWLLSIIAGACASAGANIVDAQIYT 773
Cdd:PRK00275 665 -----FLRhtAGDIAWHTEAIlqhpddggplvlikETTQREFEGGTQIFIYAPDQHDFFAATVAAMDQLNLNIHDARIIT 739
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 774 TTDGRALDTIAISReyDRDEDEGRRATRIgEMIEDVLEGKLRLPE----VVARRAAgRKVRPFVVEPEVTLNNQWSDRYT 849
Cdd:PRK00275 740 SSSQFTLDTYIVLD--DDGEPIGDNPARI-EQIREGLTEALRNPDdyptIIQRRVP-RQLKHFAFPTQVTISNDAQRPVT 815
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2049174268 850 VIEVSGLDRPGLLYQLTTAISKLNLNIASAHVATFGERARDVFYVTDLLGAQITAPTRQAAIKSALIHLLS 920
Cdd:PRK00275 816 VLEIIAPDRPGLLARIGRIFLEFDLSLQNAKIATLGERVEDVFFITDADNQPLSDPQLCSRLQDAICEQLD 886
|
|
| PRK05007 |
PRK05007 |
bifunctional uridylyltransferase/uridylyl-removing protein GlnD; |
107-925 |
4.85e-152 |
|
bifunctional uridylyltransferase/uridylyl-removing protein GlnD;
Pssm-ID: 235329 [Multi-domain] Cd Length: 884 Bit Score: 471.00 E-value: 4.85e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 107 AVVATGGYGRGLMAPESDIDLLFILPYKQTAWGEQVAEAILYCLWDMGLKVGHATRSVDESIRQARGDMTIRTAILETRF 186
Cdd:PRK05007 82 ALVAVGGYGRGELHPLSDIDLLILSRKKLPDEQAQKVGELITLLWDLKLEVGHSVRTLEECLLEGLSDLTVATNLIESRL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 187 LTGDQPLYDELverfDKEVVQG---TAAEFVTAKLAEREERHRRAGQSRYLVEPNVKDGKGGLRDLHTLFWIAKYVYRVR 263
Cdd:PRK05007 162 LCGDVALFLEL----QKHIFSDgfwPSEKFYAAKVEEQNERHQRYHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGAT 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 264 EVNELVERGVFDAQEYRTFRRCADFLWSVRCNIHFFSGRAEERLSFDMQREIAIRLGYTSHpGMQDVERFMKHYFLVAKD 343
Cdd:PRK05007 238 SLDEMVGFGFLTPAERAELNECQHFLWRIRFALHLVLSRYDNRLLFDRQLSVAQLLGYEGE-GNEPVERMMKDYYRTTRR 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 344 VGDLTAILCaKLEDQqakpapvlsrvmARLRPSNHRRRVPESDDFIIDNNRINLAAPDVFKHDPVNLIRIFRLAQKNN-- 421
Cdd:PRK05007 317 VSELNQMLL-QLFDE------------AILALTADEKPRPIDDEFQLRGTLIDLRDETLFQRQPEAILRMFYLMARNSni 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 422 LAFHPDAMRTVTRSLKLINTPLRENPEANRLFMEILTSNDA-EIVLRRMNETGVLGHFIRAFGKIVSMMQFNMYHHYTVD 500
Cdd:PRK05007 384 TGIYSTTLRQLRHARRHLNQPLCEIPEARKLFMEILRHPGAvSRALLPMHRHSVLSAYMPQWSHIVGQMQFDLFHAYTVD 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 501 EHLLRCvgyLQDIERGGN----DEFTVASDLMRKIQpeHRAVIYITTLLHDIAKGRPEDHSNAGAKVARRLCPRLGFSAA 576
Cdd:PRK05007 464 EHTIRV---LLKLESFADeetrQRHPLCVELYPRLP--KKELLLLAALFHDIAKGRGGDHSILGAQDALEFAELHGLNSR 538
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 577 DTELIAWLIEQHLTMSTVAQSRDLSDRKTIENFAAVVQSVEQMKLLTILTTADIRGVGPGVWNGWKAQLLRTLYYETEPV 656
Cdd:PRK05007 539 ETQLVAWLVRNHLLMSVTAQRRDIQDPDVIKQFAEEVQDENRLRYLVCLTVADICATNETLWNSWKQSLLRELYFATEKQ 618
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 657 LTGGF-SEVNRAQRIemaqREFRA-AFTE-----WPEEELNAYIGRHYPAYWLKVELARKIRHARFLRASEQAghKLAIN 729
Cdd:PRK05007 619 LRRGMeNPPDMRERV----RHHQLqALALlrmdnIDEEALHQIWSRCRADYFLRHTPNQLAWHARHLLQHDLD--KPLVL 692
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 730 VGFDEARGVTELTILATDHPWLLSIIAGACASAGANIVDAQIYTTTDGRALDTIAISREYDRDEDEGRRATRIGEMIEDV 809
Cdd:PRK05007 693 LSKQATRGGTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTSRDGMAMDTFIVLEPDGSPLSQDRHQVIRKALEQAL 772
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 810 LEGKLRLPEVvarRAAGRKVRPFVVEPEVTLNNQWSDRYTVIEVSGLDRPGLLYQLTTAISKLNLNIASAHVATFGERAR 889
Cdd:PRK05007 773 TQSSPQPPKP---RRLPAKLRHFNVPTEVSFLPTHTDRRSYMELIALDQPGLLARVGKIFADLGISLHGARITTIGERVE 849
|
810 820 830
....*....|....*....|....*....|....*.
gi 2049174268 890 DVFYVTDLLGAQITaPTRQAAIKSALIHLLSSEDAV 925
Cdd:PRK05007 850 DLFILATADRRALN-EELQQELRQRLTEALNPNDKG 884
|
|
| glnD |
PRK01759 |
bifunctional uridylyltransferase/uridylyl-removing protein GlnD; |
106-920 |
1.05e-138 |
|
bifunctional uridylyltransferase/uridylyl-removing protein GlnD;
Pssm-ID: 234980 [Multi-domain] Cd Length: 854 Bit Score: 435.32 E-value: 1.05e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 106 MAVVATGGYGRGLMAPESDIDLLFILPYKQTAWGEQVAEAILYCLWDMGLKVGHATRSVDESIRQARGDMTIRTAILETR 185
Cdd:PRK01759 57 LALIAVGGYGRREMFPLSDLDILILTEQPPDEETEEKINQFFQFLWDCGFEVGASVRTLAECESEGRADITIATNLLESR 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 186 FLTGDQPLYDELVERFDKEVVQGTAAeFVTAKLAEREERHRRAGQSRYLVEPNVKDGKGGLRDLHTLFWIAKYVYRVREV 265
Cdd:PRK01759 137 FLTGNEKLFDALVELLQQADFWSKEA-FFQAKIQEKIERYQRYHNTSYNLEPDIKYSPGGLRDLHLLYWIALRHSGAKSL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 266 NELVERGVFDAQEYRTFRRCADFLWSVRCNIHFFSGRAEERLSFDMQREIAIRLGYTShPGMQDVERFMKHYFLVAKDVG 345
Cdd:PRK01759 216 EEILQSGFIYPEEYAELQQSQQFLFKVRFALHLILKRYDNRLLFDRQLKVSELLGFQG-EGNQGVEKMMKSFFQALQSIS 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 346 DLTAILCAKLEDQqakpapvlsrvmaRLRPSNHRRRVPESDDFIIDNNRINLAAPDVFKHDPVNLIRIF-RLAQKNNLAF 424
Cdd:PRK01759 295 LLSDLLVKHYREH-------------FLQPNQNVEIQPLDDDFYLINNAICLRNPDCFEQQPESILDLFfYLTQYPQAEI 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 425 HPDAMRTVTRSLKLINTPLRENPEANRLFMEILTSNDA-EIVLRRMNETGVLGHFIRAFGKIVSMMQFNMYHHYTVDEHL 503
Cdd:PRK01759 362 HSTTLRQLRLALEQLQQPLCELPAARERFLRLFNQPNAiKRALVPMHQYGVLTAYLPQWKGIVGLMQFDLFHIYTVDEHT 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 504 LRCVGYLQD-IERGGNDEFTVASDLMRKIQpeHRAVIYITTLLHDIAKGRPEDHSNAGAKVARRLCPRLGFSAADTELIA 582
Cdd:PRK01759 442 LRVMLKLESfLDEESAEQHPICHQIFSQLS--DRTLLYIAALFHDIAKGRGGDHAELGAVDMRQFAQQHGFDQREIETMA 519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 583 WLIEQHLTMSTVAQSRDLSDRKTIENFAAVVQSVEQMKLLTILTTADIRGVGPGVWNGWKAQLLRTLYYETEPVLTGGF- 661
Cdd:PRK01759 520 WLVQQHLLMSVTAQRRDIHDPEVVMNFAEEVQNQVRLDYLTCLTVADICATNETLWNSWKRSLFATLYQFTNQQFQQGMd 599
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 662 --------SEVNRAQriemAQREFRAAFTE---------W---PEEelnaYIGRHYPA--YWlkvelarkirHARFLRAS 719
Cdd:PRK01759 600 elldyqekAEENRQQ----ALELLQQKYSAlsetqieqlWqrcPED----YFLRNTPKqiAW----------HALLLLDF 661
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 720 EQAghkLAINVGFDEARGVTELTILATDHPWLLSIIAGACASAGANIVDAQIYTTTDGRALDTIAISrEYDRDE-DEGRR 798
Cdd:PRK01759 662 RGD---LLVKISNRFSRGGTEIFIYCQDQANLFLKVVSTIGAKKLSIHDAQIITSQDGYVLDSFIVT-ELNGKLlEFDRR 737
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 799 atrigEMIEDVLEGKLRLPEVVARRAA-GRKVRPFVVEPEVT-LNNQWSDRyTVIEVSGLDRPGLLYQLTTAISKLNLNI 876
Cdd:PRK01759 738 -----RQLEQALTKALNTNKLKKLNLEeNHKLQHFHVKTEVRfLNEEKQEQ-TEMELFALDRAGLLAQVSQVFSELNLNL 811
|
810 820 830 840
....*....|....*....|....*....|....*....|....
gi 2049174268 877 ASAHVATFGERARDVFYVTDLLGAQITAPTRQaAIKSALIHLLS 920
Cdd:PRK01759 812 LNAKITTIGEKAEDFFILTNQQGQALDEEERK-ALKSRLLSNLS 854
|
|
| PRK04374 |
PRK04374 |
[protein-PII] uridylyltransferase; |
92-909 |
8.39e-107 |
|
[protein-PII] uridylyltransferase;
Pssm-ID: 179839 [Multi-domain] Cd Length: 869 Bit Score: 351.19 E-value: 8.39e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 92 RHLYRSQVPTGAErMAVVATGGYGRGLMAPESDIDLLFILPYKQTAWGEQVAEAILYCLWDMGLKVGHATRSVDESiRQA 171
Cdd:PRK04374 60 RNAWTRCIPADSG-LSLHAVGGYGRGELFPRSDVDLLVLGETAAQQRHEQALARLFALLWDVGLPISHAVRSPAQC-TAA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 172 RGDMTIRTAILETRFLTGDQPLYDELVERFDKEVVQgTAAEFVTAKLAEREERHRRAGQSRYLVEPNVKDGKGGLRDLHT 251
Cdd:PRK04374 138 AADQTVLTALIESRPLVADAAARAALAAAIAPQQVW-PPRAFFQAKREELLARHQRFGDTADNLEPDIKDGPGGLRDLQT 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 252 LFWIAKYVYRVREVNELVERGVFDAQEYRTFRRCADFLWSVRCNIHFFSGRAEERLSFDMQREIAIRLGYTSHPGMQDVE 331
Cdd:PRK04374 217 LGWMALRAFGVKDLEALVGLGHVGCDEAAALRREREELARLRFGLHLVANRPEERLRFDYQKTLAERLGFADDPESLGVE 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 332 RFMKHYFLVAKDVGDLTAILCAKLEDQ---QAKPAPVlsrvmarlrpsnhrrrvpeSDDFIIDNNRINLAAPDVFKHDPV 408
Cdd:PRK04374 297 KMMQRFYRSAALIRRISDRLLQRFEEQfdgEATPEPL-------------------GGGFSLRRGYLAADADSWPDGDVL 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 409 NLIRIFR--LAQKNNLAFHPDAMRTVTRSLKLINTPLRENPEANRLFMEILTSNDAEIVLRRMNETGVLGHFIRAFGKIV 486
Cdd:PRK04374 358 QVFALFAqwAAHREVRGLHSLTARALAEVLRDLPAYDVADATARERFMALLRGPRAVETLNRMARLGVLGQWIPAFASVS 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 487 SMMQFNMYHHYTVDEHLLRCVGYLQDIERGGNDE-FTVASDLMRKI-QPEhraVIYITTLLHDIAKGRPEDHSNAGAKVA 564
Cdd:PRK04374 438 GRMQFDLFHVYTVDQHTLMVLRNIALFAAGRADErFSIAHEVWPRLrKPE---LLLLAGLFHDIAKGRGGDHSELGAVDA 514
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 565 RRLCPRLGFSAADTELIAWLIEQHLTMSTVAQSRDLSDRKTIENFAAVVQSVEQMKLLTILTTADIRGVGPGVWNGWKAQ 644
Cdd:PRK04374 515 RAFCLAHRLSEGDTELVTWLVEQHLRMSVTAQKQDISDPEVIHRFATLVGTRERLDYLYLLTCADIAGTSPKLWNAWKDR 594
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 645 LLRTLYYETEPVLTGGFSE-VNRAQRIEMAQREFRAAFTEWPEEElnAYIGRHYPAywlkvelarkIRHARFLR-----A 718
Cdd:PRK04374 595 LLADLYFAARRALREGLEHpPPREERLREARESARALMQAQGHDD--ATIDRQFAG----------MPDENFLRfrpeqL 662
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 719 SEQAGHKLAINVG--FDEARGVT------ELTILATDHPWLLSIIAGACASAGANIVDAQIYTTTDGRALDTIAISreyD 790
Cdd:PRK04374 663 AWQAASLIEVEIGqtLVKARRAVpdndalEVFVYSPDRDGLFAAIVATLDRKGYGIHRARVLDAPHDAIFDVFEVL---P 739
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 791 RDEDEGRRATRIGEMIEDVLEGKL-RLPEvvARRAAGRKVRPFVVEPEVTLNNQWSDRYTVIEVSGLDRPGLLYQLTTAI 869
Cdd:PRK04374 740 QDTYADGDPQRLAAALRQVLAGDLqKVRP--ARRAVPRQLRHFRFAPRVEFSESAGGRRTRISLVAPDRPGLLADVAHVL 817
|
810 820 830 840
....*....|....*....|....*....|....*....|
gi 2049174268 870 SKLNLNIASAHVATFGERARDVFYVTDLLGAQITAPTRQA 909
Cdd:PRK04374 818 RMQHLRVHDARIATFGERAEDQFQITDEHDRPLSESARQA 857
|
|
| PRK03381 |
PRK03381 |
PII uridylyl-transferase; Provisional |
107-915 |
1.47e-89 |
|
PII uridylyl-transferase; Provisional
Pssm-ID: 235123 [Multi-domain] Cd Length: 774 Bit Score: 301.91 E-value: 1.47e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 107 AVVATGGYGRGLMAPESDIDLLFILPYKQTAWGEQVAEAILYCLWDMGLKVGHATRSVDESIRQARGDMTIRTAILETRF 186
Cdd:PRK03381 59 ALVAVGGLGRRELLPYSDLDLVLLHDGRPADDVAEVADRLWYPLWDAGIRLDHSVRTVPEALKVAGSDLKAALGLLDARH 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 187 LTGDQPLYDELVERFDKEVVQGTAAEFvtAKLAER-EERHRRAGQSRYLVEPNVKDGKGGLRDLHTLfwiakyvyrvrev 265
Cdd:PRK03381 139 IAGDADLSALLIGGVRRQWRNGARRRL--PELVELtRARWERSGEIAHLAEPDLKEGRGGLRDVQLL------------- 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 266 NELVERGVFDAQEYRtFRRCADFLWSVRCNIHFFSGRAEERLSFDMQREIAIRLGYTSHPGMQ----DVERFMKHYFlva 341
Cdd:PRK03381 204 RALAAAQLADAPGGG-LDAAHRRLLDVRTELHRVSGRGRDRLLAQEADEVAAALGLGDRFDLAralsDAARTISYAV--- 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 342 kDVGDLTAilcakledqqakPAPVLSRVMARLRPSNHRRrvPESDDFIIDNNRINLAAPDVFKHDPVNLIRIFRLAQKNN 421
Cdd:PRK03381 280 -DVGWRTA------------ANALPRRGLSALRRRPVRR--PLDEGVVEHAGEVVLARDARPARDPGLVLRVAAAAATTG 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 422 LAFHPDAMRTVTRSLKlintPLRE--NPEANRLFMEILTSNDAEI-VLRRMNETGVLGHFIRAFGKIVSMMQFNMYHHYT 498
Cdd:PRK03381 345 LPIAAATLSRLAASAP----PLPTpwPAEARDDLLVLLGAGPAAVaVIEALDRTGLWGRLLPEWEAVRDLPPRDPVHRWT 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 499 VDEHLLRCVGYlqdierggndeftvASDLMRKIQ-PEhraVIYITTLLHDIAKGRPEDHSNAGAKVARRLCPRLGFSAAD 577
Cdd:PRK03381 421 VDRHLVETAVR--------------AAALTRRVArPD---LLLLGALLHDIGKGRGGDHSVVGAELARQIGARLGLSPAD 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 578 TELIAWLIEQHLTMSTVAQSRDLSDRKTIENFAAVVQSVEQ-MKLLTILTTADIRGVGPGVWNGWKAQLLRTLYYETEPV 656
Cdd:PRK03381 484 VALLSALVRHHLLLPETATRRDLDDPATIEAVAEALGGDPVlLELLHALTEADSLATGPGVWSDWKASLVGDLVRRCRAV 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 657 LTGGfsEVNRAQRIEMAQREFRAAFTewpeeelnayigrhypaywLKVELArkirharflraseqaghklainvgfDEAR 736
Cdd:PRK03381 564 LAGE--PLPEPEPLDPAQLALAADGG-------------------VHVEIA-------------------------PADP 597
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 737 GVTELTILATDHPWLLSIIAGACASAGANIVDAQIyTTTDGRALDTIAISREYDRDEDegrrATRIGEMIEDVLEGKLRL 816
Cdd:PRK03381 598 HMVEVTVVAPDRRGLLSKAAGVLALHRLRVRSASV-RSHDGVAVLEFVVSPRFGSPPD----AALLRQDLRRALDGDLDV 672
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 817 PEVVARR---AAGRKVRPFVVEPEVTLNNQWSDRYTVIEVSGLDRPGLLYQLTTAISKLNLNIASAHVATFGERARDVFY 893
Cdd:PRK03381 673 LARLAAReaaAAAVPVRRPAAPPRVLWLDGASPDATVLEVRAADRPGLLARLARALERAGVDVRWARVATLGADVVDVFY 752
|
810 820
....*....|....*....|..
gi 2049174268 894 VTDllGAQITAPTRQAAIKSAL 915
Cdd:PRK03381 753 VTG--AAGGPLADARAAVEQAV 772
|
|
| GlnD_UR_UTase |
pfam08335 |
GlnD PII-uridylyltransferase; This is a family of bifunctional uridylyl-removing enzymes ... |
213-351 |
7.64e-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: 166.60 E-value: 7.64e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 213 FVTAKLAEREERHRRAGQSRYLVEPNVKDGKGGLRDLHTLFWIAKYVYRVREVNELVERGVFDAQEYRTFRRCADFLWSV 292
Cdd:pfam08335 2 FMKAKIEEQVARHGRYGDTAYNLEPNIKLGPGGLRDIEFIVWIAQLIFTLRALEELVELGLLTREEARELRRAYRFLRRV 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2049174268 293 RCNIHFFSGRAEERLSFDMQREIAIRLGYTsHPGMQDVERFMKHYFLVAKDVGDLTAIL 351
Cdd:pfam08335 82 RHRLHLLADRQTDRLPFDLQRRLARALGYA-RDGWLAVERFMRRLFRHAHRVSRLFEIL 139
|
|
| glnD |
PRK00227 |
[protein-PII] uridylyltransferase; |
87-649 |
1.51e-35 |
|
[protein-PII] uridylyltransferase;
Pssm-ID: 178937 [Multi-domain] Cd Length: 693 Bit Score: 144.52 E-value: 1.51e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 87 YSAATRHLYRSQVPTGAermAVVATGGYGRGLMAPESDIDLLFILPYKQTawgEQVAEAILYCLWDMGLKVGHATRSVDE 166
Cdd:PRK00227 12 EASALALLGSLQLPPGT---ALAATGSLARREMTPYSDLDLILLHPPGAT---PDGVEDLWYPIWDAKKRLDYSVRTPQE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 167 SIRQARGDMTIRTAILETRFLTGDQPLYD------------ELVERFDkEVVQGTAAefvtaklaereeRHRRAGQSRYL 234
Cdd:PRK00227 86 CAAMISADSTAALALLDLRFVAGDEQLTAstrakilekwrrELNKNFD-AVVDTAIA------------RWRRSGSVVAM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 235 VEPNVKDGKGGLRDLHTLfwiakyvyRVREVNELVERGVFDAQEyrtfrrcaDFLWSVRCNIHFFSGRAEERLSFDMQRE 314
Cdd:PRK00227 153 TRPDLKHGRGGLRDIELI--------RALALGHLCDAPPLDSQH--------QLLLDVRTLLHVHARRARDVLDPEFAVD 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 315 IAIRLGytshpgmqdverFMKHYFLVAKDVGDLTAILCAkLEDQQAKPAPVLSRvmarlRPSNHRR-RVPESDDFIIDNN 393
Cdd:PRK00227 217 IALDLG------------FVDRYHLSREIADAARAIDDA-LTAALATARGALPR-----RTAFRNAvRRPLDVDVVDANG 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 394 RINLA-APDVfkHDPVNLIRIFRLAQKNNLafhPDAMRTVTRSLKLINTPLRENPEANRLFMEILTSND-AEIVLRRMNE 471
Cdd:PRK00227 279 TIALSrTPDL--DDPALPLRVAAAAARTGL---PVSESVWKRLEECPELPEPWPASAAGDFFRLLSSPVnSRRVIKQMDR 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 472 TGVLGHFIRAFGKIVSMMQFNMYHHYTVDEHLLRcvgylqdierggndefTVASDLMRKIQPEHRAVIYITTLLHDIAKG 551
Cdd:PRK00227 354 HGLWERIVPEWDRIRGLMPREPSHIHTIDEHSLN----------------TVANCALETVTVARPDLLLLGALYHDIGKG 417
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 552 RPEDHSNAGAKVARRLCPRLGFSAADTELIAWLIEQHLTMSTVAQSRDLSDRKTIENFA-AVVQSVEQMKLLTILTTADI 630
Cdd:PRK00227 418 YPRPHEQVGAEMVARAARRMGLNLRDRAVVQTLVAEHTTLARIAGRLDPTSEEAVDKLLdAVRYDLLTLNLLEVLTEADA 497
|
570
....*....|....*....
gi 2049174268 631 RGVGPGVWNGWKAQLLRTL 649
Cdd:PRK00227 498 EGTGPGVWTARLEQGLRIV 516
|
|
| NT_GlnE_GlnD_like |
cd05401 |
Nucleotidyltransferase (NT) domain of Escherichia coli adenylyltransferase (GlnE), Escherichia ... |
48-201 |
9.80e-25 |
|
Nucleotidyltransferase (NT) domain of Escherichia coli adenylyltransferase (GlnE), Escherichia coli uridylyl transferase (GlnD), and similar proteins; Escherichia coli GlnD and -E participate in the Glutamine synthetase (GS)/Glutamate synthase (GOGAT) pathway for the assimilation of ammonium nitrogen. In nitrogen sufficiency, GlnE adenylates GS, reducing GS activity; when nitrogen is limiting, GlnE deadenylates GS-AMP, restoring GS activity. When nitrogen is limiting, GlnD uridylylates the nitrogen regulatory protein PII to PII-UTP, and in nitrogen sufficiency, it removes the modifying groups. The activity of Escherichia coli GlnE is modulated by PII-proteins. PII-UMP promotes GlnE deadenylation activity, and PII promotes GlnE adenylation activity. Escherichia coli GlnE has two separate NT domains. The N-terminal NT domain catalyzes the deadenylylation of GS, and the C-terminal NT domain the adenylylation reaction. The majority of proteins in this family contain a C-terminal NT domain which is associated with a cystathionine beta-synthase (CBS) domain pair and a CAP_ED (cAMP receptor protein effector ) domain. This family belongs to the Pol beta-like NT superfamily. In the majority of enzymes in this superfamily, two carboxylates, Dx[D/E], together with a third more distal carboxylate, coordinate two divalent metal cations involved in a two-metal ion mechanism of nucleotide addition. For the majority of proteins in this family, these carboxylate residues are conserved.
Pssm-ID: 143391 [Multi-domain] Cd Length: 172 Bit Score: 101.65 E-value: 9.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 48 KAEMVEARAVAQAVLLKDRHGRRCAERLCFVQDEIIRILYSAATRHLYRsqvPTGAERMAVVATGGYGRGLMAPESDIDL 127
Cdd:cd05401 1 RAKLRQLRRILRRDLLGGASIRAISRALSDLADALLRRALELALAELGK---GPPPVPFALLALGSYGRGELNPSSDQDL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 128 LFILPYKQ---TAWGEQVAEAI---------LYCLWDMGLKVGHATRSVDESIRQARGDMTI------RTAILETRFLTG 189
Cdd:cd05401 78 LLLYDDDGdevAAYFEELAERLikilseaggPYCLGDVMLRPPGWRRSLAEWLDAARDWLTEpgrlweRTALLDARPVAG 157
|
170
....*....|..
gi 2049174268 190 DQPLYDELVERF 201
Cdd:cd05401 158 DRALAEELRRRI 169
|
|
| ACT_ACR-UUR-like_2 |
cd04899 |
C-terminal ACT domains of the bacterial signal-transducing uridylyltransferase ... |
849-919 |
3.73e-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: 3.73e-22
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2049174268 849 TVIEVSGLDRPGLLYQLTTAISKLNLNIASAHVATFGERARDVFYVTDLLGAQITaPTRQAAIKSALIHLL 919
Cdd:cd04899 1 TVLELTALDRPGLLADVTRVLAELGLNIHSAKIATLGERAEDVFYVTDADGQPLD-PERQEALRAALGEAL 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 |
2.03e-19 |
|
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: 82.91 E-value: 2.03e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2049174268 738 VTELTILATDHPWLLSIIAGACASAGANIVDAQIYTTTDGRALDTIAISREYDRDEDEGRRATRIGEMIEDVL 810
Cdd:cd04900 1 GTEVFIYTPDRPGLFARIAGALDQLGLNILDARIFTTRDGYALDTFVVLDPDGEPIGERERLARIREALEDAL 73
|
|
| ACT_UUR-ACR-like |
cd04873 |
ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) ... |
849-919 |
4.06e-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: 4.06e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2049174268 849 TVIEVSGLDRPGLLYQLTTAISKLNLNIASAHVATFGERARDVFYVTDLLGAQITaPTRQAAIKSALIHLL 919
Cdd:cd04873 1 TVVEVYAPDRPGLLADITRVLADLGLNIHDARISTTGERALDVFYVTDSDGRPLD-PERIARLEEALEDAL 70
|
|
| ACT_UUR-ACR-like |
cd04873 |
ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) ... |
739-810 |
3.75e-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: 56.79 E-value: 3.75e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2049174268 739 TELTILATDHPWLLSIIAGACASAGANIVDAQIyTTTDGRALDTIAISREYDRDEDEgRRATRIGEMIEDVL 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 ... |
849-919 |
1.14e-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: 55.51 E-value: 1.14e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2049174268 849 TVIEVSGLDRPGLLYQLTTAISKLNLNIASAHVATFGERARDVFYVTD-LLGAQITAPTRQAAIKSALIHLL 919
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 ... |
857-919 |
1.32e-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: 1.32e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2049174268 857 DRPGLLYQLTTAISKLNLNIASAHVATFGE-RARDVFYVTDLLGAQITAPTRQAAIKSALIHLL 919
Cdd:cd04900 10 DRPGLFARIAGALDQLGLNILDARIFTTRDgYALDTFVVLDPDGEPIGERERLARIREALEDAL 73
|
|
| ACT_ACR_1 |
cd04895 |
ACT domain-containing protein which is composed almost entirely of four ACT domain repeats ... |
849-915 |
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 2049174268 849 TVIEVSGLDRPGLLYQLTTAISKLNLNIASAHVATFGERARDVFYVTDLLGAQITAPTRQAAIKSAL 915
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 ... |
851-912 |
2.54e-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: 2.54e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2049174268 851 IEVSGLDRPGLLYQLTTAISKLNLNIASAHVATFGERARDVFYVTDLLGAQITAPTRQAAIK 912
Cdd:cd04926 4 LELRTEDRVGLLSDVTRVFRENGLTVTRAEISTQGDMAVNVFYVTDANGNPVDPKTIEAVRQ 65
|
|
| ACT |
cd02116 |
ACT domains are commonly involved in specifically binding an amino acid or other small ligand ... |
851-896 |
4.81e-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: 4.81e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2049174268 851 IEVSGLDRPGLLYQLTTAISKLNLNIASAHVATFG-ERARDVFYVTD 896
Cdd:cd02116 1 LTVSGPDRPGLLAKVLSVLAEAGINITSIEQRTSGdGGEADIFIVVD 47
|
|
| ACT |
pfam01842 |
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ... |
849-894 |
9.54e-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: 44.22 E-value: 9.54e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2049174268 849 TVIEVSGLDRPGLLYQLTTAISKLNLNIASAHVATFGERARDVFYV 894
Cdd:pfam01842 1 TVLEVLVPDRPGLLARVLGALADRGINITSIEQGTSEDKGGIVFVV 46
|
|
| GcvR |
COG2716 |
Glycine cleavage system regulator GcvR [Amino acid transport and metabolism]; |
741-915 |
1.73e-05 |
|
Glycine cleavage system regulator GcvR [Amino acid transport and metabolism];
Pssm-ID: 442029 [Multi-domain] Cd Length: 174 Bit Score: 45.98 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 741 LTILATDHPWLLSIIAGACASAGANIVDAQIyTTTDGRALDTIAISREYDRdedegrrATRIGEMIEDvLEGKLRLpEVV 820
Cdd:COG2716 6 ITAIGPDRPGIVAALARAVSEHGCNILDSRM-ARLGGEFAGILLVSGPWDA-------IAKLEAALPA-LAAELGL-LVT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 821 ARRAAGRKVRPfvvePEVTLnnqwsdrytVIEVSGLDRPGLLYQLTTAISKLNLNIA--SAHVATFGERARDVFYVTdll 898
Cdd:COG2716 76 VKRTEPHEAPP----AGLPY---------VVEVVGNDRPGIVAEVTQFLAERGINIEdlSTKTYPAPMSGTPLFSAQ--- 139
|
170
....*....|....*....
gi 2049174268 899 gAQITAPTRQ--AAIKSAL 915
Cdd:COG2716 140 -ITVHVPAGLdiDALRDAL 157
|
|
| SpoT |
COG0317 |
(p)ppGpp synthase/hydrolase, HD superfamily [Signal transduction mechanisms, Transcription]; |
835-883 |
1.66e-04 |
|
(p)ppGpp synthase/hydrolase, HD superfamily [Signal transduction mechanisms, Transcription];
Pssm-ID: 440086 [Multi-domain] Cd Length: 722 Bit Score: 45.53 E-value: 1.66e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2049174268 835 EPEVTLNNQWSD----RYTV-IEVSGLDRPGLLYQLTTAISKLNLNIASAHVAT 883
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 ... |
851-887 |
1.70e-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: 1.70e-04
10 20 30
....*....|....*....|....*....|....*..
gi 2049174268 851 IEVSGLDRPGLLYQLTTAISKLNLNIASAHVATFGER 887
Cdd:cd04876 1 IRVEAIDRPGLLADITTVIAEEKINILSVNTRTDDDG 37
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|
| HD |
pfam01966 |
HD domain; HD domains are metal dependent phosphohydrolases. |
523-592 |
2.57e-04 |
|
HD domain; HD domains are metal dependent phosphohydrolases.
Pssm-ID: 460398 [Multi-domain] Cd Length: 110 Bit Score: 41.45 E-value: 2.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 523 VASDLMRKIQPEHRAVIYITTLLHDIAKGRPED----------HSNAGAKVARRLCPRLGFsaadtELIAWLIEQHLTMS 592
Cdd:pfam01966 11 LARELAEELGELDRELLLLAALLHDIGKGPFGDekpefeiflgHAVVGAEILRELEKRLGL-----EDVLKLILEHHESW 85
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|
| ACT_6 |
pfam13740 |
ACT domain; ACT domains bind to amino acids and regulate associated enzyme domains. |
847-915 |
1.96e-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: 1.96e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 847 RYTVIEVSGLDRPGLLYQLTTAISKLNLNIASAHVATFGERardvfyVTdlLGAQITAP-TRQAAIKSAL 915
Cdd:pfam13740 1 EILLITATGPDRPGLTASLTAVLAEHGCNILDSGQAVIHNR------LS--LGLLVSGPwDALARLEKDL 62
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|
| ACT_TyrKc |
cd04928 |
Uncharacterized, N-terminal ACT domain of an Arabidopsis/Oryza predicted tyrosine kinase and ... |
851-895 |
1.97e-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: 1.97e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2049174268 851 IEVSGLDRPGLLYQLTTAISKLNLNIASAHV-ATFGERARDVFYVT 895
Cdd:cd04928 4 ITFAAGDKPKLLSQLSSLLGDLGLNIAEAHAfSTDDGLALDIFVVT 49
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|
| NTP_transf_2 |
pfam01909 |
Nucleotidyltransferase domain; Members of this family belong to a large family of ... |
108-132 |
2.05e-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: 2.05e-03
|
| ACT_GcvR_2 |
cd04869 |
ACT domains that comprise the Glycine Cleavage System Transcriptional Repressor (GcvR) protein, ... |
850-878 |
2.65e-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: 2.65e-03
10 20
....*....|....*....|....*....
gi 2049174268 850 VIEVSGLDRPGLLYQLTTAISKLNLNIAS 878
Cdd:cd04869 1 VVEVVGNDRPGIVHEVTQFLAQRNINIED 29
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|
| ACT_4 |
pfam13291 |
ACT domain; ACT domains bind to amino acids and regulate associated enzyme domains. These ACT ... |
847-883 |
4.71e-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: 4.71e-03
10 20 30
....*....|....*....|....*....|....*...
gi 2049174268 847 RYTV-IEVSGLDRPGLLYQLTTAISKLNLNIASAHVAT 883
Cdd:pfam13291 3 SYPVdLEVEAIDRPGLLADITQVISEEKANIVSVNAKT 40
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|
| HDc |
smart00471 |
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ... |
495-606 |
6.37e-03 |
|
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: 37.66 E-value: 6.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2049174268 495 HHYTVDEHLLRCVGYLQDIERGGNDEFtvasdlmrkiqpehRAVIYITTLLHDIAKGRP-----------EDHSNAGAKV 563
Cdd:smart00471 1 SDYHVFEHSLRVAQLAAALAEELGLLD--------------IELLLLAALLHDIGKPGTpdsflvktsvlEDHHFIGAEI 66
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2049174268 564 ARrlcpRLGFSAADTELIAWLIEQHLTMSTVAQSRDLSDRKTI 606
Cdd:smart00471 67 LL----EEEEPRILEEILRTAILSHHERPDGLRGEPITLEARI 105
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