|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05007 |
PRK05007 |
bifunctional uridylyltransferase/uridylyl-removing protein GlnD; |
5-856 |
0e+00 |
|
bifunctional uridylyltransferase/uridylyl-removing protein GlnD;
Pssm-ID: 235329 [Multi-domain] Cd Length: 884 Bit Score: 1217.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 5 KQANNEFSDWLNEQFERGGDIRELLHQRCQYVDDLLQQLWQHFELNHTP-ISLIAVGGYGRGELHPHSDVDLLILSLKTL 83
Cdd:PRK05007 31 KQHLDTFQQWLGDAFDAGISAEQLVEARTEFIDQLLQRLWIEAGFDQIPdLALVAVGGYGRGELHPLSDIDLLILSRKKL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 84 TNEQTEKISQFITFLWDIKFDIGHSVRTLEETISIGKSDITVATNLMESRLLNGPQELYQQLQLAIEQPDFWPSSEFYLA 163
Cdd:PRK05007 111 PDEQAQKVGELITLLWDLKLEVGHSVRTLEECLLEGLSDLTVATNLIESRLLCGDVALFLELQKHIFSDGFWPSEKFYAA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 164 KRDEQFQRHE--ANNAFDLEPNIKTCPGGLRDIQTVGWIAKRHFKTTIVEQLVQHGFLSQEELDKLLSCQDFLWSMRFAL 241
Cdd:PRK05007 191 KVEEQNERHQryHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSLDEMVGFGFLTPAERAELNECQHFLWRIRFAL 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 242 HQTAKRPEDKLLFNHQHDVANAMGYSDEDQLAVEVMMKQYYQQIREVDELCEMLLQLFKREFLGRIKTLDICIMNEQYQR 321
Cdd:PRK05007 271 HLVLSRYDNRLLFDRQLSVAQLLGYEGEGNEPVERMMKDYYRTTRRVSELNQMLLQLFDEAILALTADEKPRPIDDEFQL 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 322 RGHFIESTVDNLFNDKSQ-IITLFLNIAKDKEISGIYAPTLRQLRLARENLTAPLCDDAQCRTAFMNIIKHPDGI-RALS 399
Cdd:PRK05007 351 RGTLIDLRDETLFQRQPEaILRMFYLMARNSNITGIYSTTLRQLRHARRHLNQPLCEIPEARKLFMEILRHPGAVsRALL 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 400 MMHKHGILGSYMPAWQKISGQMQFDLFHAYTVDEHTHRLLKNIDRFSQPKYKDEFPLCSVLIHTLTKKGLLVLAAIFHDI 479
Cdd:PRK05007 431 PMHRHSVLSAYMPQWSHIVGQMQFDLFHAYTVDEHTIRVLLKLESFADEETRQRHPLCVELYPRLPKKELLLLAALFHDI 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 480 GKGRGGDHSELGALDALEFGRLHALNEHDTRLIAWLVENHLLMSVIAQRRDIHDPDVINSFASIVQDETRLAYLYCLTVA 559
Cdd:PRK05007 511 AKGRGGDHSILGAQDALEFAELHGLNSRETQLVAWLVRNHLLMSVTAQRRDIQDPDVIKQFAEEVQDENRLRYLVCLTVA 590
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 560 DICATNNKLWNNWKGSLLRELYFYTLRALRRGAQGDVDAEERITEYKAKALHQLHTNDafYDKHAVEELWGYFQDDYFLR 639
Cdd:PRK05007 591 DICATNETLWNSWKQSLLRELYFATEKQLRRGMENPPDMRERVRHHQLQALALLRMDN--IDEEALHQIWSRCRADYFLR 668
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 640 HTPIAIAQHCDLILRNQpPNKPIIAIFHNPNKTVSELFVYTQDMKNLFAKVMRVLGSKNVQINDAHVMATTGGWALDTFN 719
Cdd:PRK05007 669 HTPNQLAWHARHLLQHD-LDKPLVLLSKQATRGGTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTSRDGMAMDTFI 747
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 720 ISEHNGQPiLDERRVKSIVQTLTKSLTQKHFKPHNNRRIARRTKQFKVPTRISFITCDHGEHTLFELVALDMPGLLATVG 799
Cdd:PRK05007 748 VLEPDGSP-LSQDRHQVIRKALEQALTQSSPQPPKPRRLPAKLRHFNVPTEVSFLPTHTDRRSYMELIALDQPGLLARVG 826
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*..
gi 1101461855 800 DVFTKFKITLHNAKITTIGERVEDFFIITDKDENPLTQEQQNTLQQALVLAIEKLNR 856
Cdd:PRK05007 827 KIFADLGISLHGARITTIGERVEDLFILATADRRALNEELQQELRQRLTEALNPNDK 883
|
|
| GlnD |
COG2844 |
UTP:GlnB (protein PII) uridylyltransferase [Posttranslational modification, protein turnover, ... |
1-852 |
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: 1129.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 1 MASCKQANNEFSDWLNEQFERGGDIRELLHQRCQYVDDLLQQLWQHFEL-NHTPISLIAVGGYGRGELHPHSDVDLLILS 79
Cdd:COG2844 4 LAALREALAEGRAALRERFRAGADGRELVRARAALVDQLLRALWDLAGLtEPERLALVAVGGYGRGELAPHSDIDLLFLL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 80 LKTLTNEQTEKISQFITFLWDIKFDIGHSVRTLEETISIGKSDITVATNLMESRLLNGPQELYQQLQLAIEQPDFWPSSE 159
Cdd:COG2844 84 PDKPTPALEEVIEAFLYLLWDLGLEVGHSVRTVDECLREAREDITVRTALLEARLLAGDEALFEELRERFRADVFWDSRA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 160 FYLAKRDEQFQRHE--ANNAFDLEPNIKTCPGGLRDIQTVGWIAKRHFKTTIVEQLVQHGFLSQEELDKLLSCQDFLWSM 237
Cdd:COG2844 164 FFEAKLAEQRERHAkyGDTRYNLEPNIKEGPGGLRDLQTLLWIAKRHFGVRSLEELVKKGLLTEEEYRELRRAEDFLWRV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 238 RFALHQTAKRPEDKLLFNHQHDVANAMGYSDED-QLAVEVMMKQYYQQIREVDELCEMLLQLFKREFLGRIKTLDICIMN 316
Cdd:COG2844 244 RFALHLLAGRAEDRLLFDLQREVAERLGYQDTEgNRAVERFMQRYYRTAKAVGRLNEILLQRLEEAILKPPGLRRPRPIN 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 317 EQYQRRGHFIESTVDNLF-NDKSQIITLFLNIAKDKEISGIYAPTLRQLRLARENLTAPLCDDAQCRTAFMNIIKHPDGI 395
Cdd:COG2844 324 EGFQLRNGRLEVADPDVFeRDPVALLRLFLLAAQHPEGLGIHPDTLRLLRRALRLIDDAFRRDPEARRLFLEILRQPRGI 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 396 -RALSMMHKHGILGSYMPAWQKISGQMQFDLFHAYTVDEHTHRLLKNIDRFSQPKYKDEFPLCSVLIHTLTKKGLLVLAA 474
Cdd:COG2844 404 tRALRRMNEYGVLGRYIPEFGRIVGQMQFDLFHVYTVDEHTLRVVRNLRRFERGELAEEFPLASELIAELPKPELLYLAA 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 475 IFHDIGKGRGGDHSELGALDALEFGRLHALNEHDTRLIAWLVENHLLMSVIAQRRDIHDPDVINSFASIVQDETRLAYLY 554
Cdd:COG2844 484 LFHDIAKGRGGDHSELGAEDARRFCPRHGLSPEDTELVAWLVRHHLLMSHTAQRRDISDPEVIRDFARLVGSEERLDYLY 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 555 CLTVADICATNNKLWNNWKGSLLRELYFYTLRALRRGAQGdVDAEERITEYKAKALHQLhtNDAFYDKHAVEELWGYFQD 634
Cdd:COG2844 564 LLTVADIRATGPKVWNSWKASLLRELYRATLRALRGGLEP-PDREERIEERKEEALALL--ADQGWDEEEIEALWARLPD 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 635 DYFLRHTPIAIAQHCDLILRNQPPNKPIIAIFHNPNKTVSELFVYTQDMKNLFAKVMRVLGSKNVQINDAHVMATTGGWA 714
Cdd:COG2844 641 DYFLRHDPEEIAWHARLLLRADDSGKPLVLIRPDPDRGGTEVFVYTPDRPGLFARIAGALAALGLNILDARIHTTRDGYA 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 715 LDTFNISEHNGQPILDERRVKSIVQTLTKSLTQKH-FKPHNNRRIARRTKQFKVPTRISFITCDHGEHTLFELVALDMPG 793
Cdd:COG2844 721 LDTFIVLDPDGEPIDDPDRLERIEQALEEALSGEVpLPEPLARRLSRRLRHFPVPPRVTFDNDASNRYTVLEVSALDRPG 800
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 794 LLATVGDVFTKFKITLHNAKITTIGERVEDFFIITDKDENPLTQ-EQQNTLQQALVLAIE 852
Cdd:COG2844 801 LLYDIARVLADLGLNIHSAKIATLGERVEDVFYVTDLDGQKLTDpERQEALREALLEALD 860
|
|
| UTase_glnD |
TIGR01693 |
[Protein-PII] uridylyltransferase; This model describes GlnD, the uridylyltransferase ... |
15-852 |
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: 846.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 15 LNEQFERGGDIRELLHQRCQYVDDLLQQLWQHFELN-HTPISLIAVGGYGRGELHPHSDVDLLILSLKTLTNEQTEKISQ 93
Cdd:TIGR01693 4 LLEEFARGGDGRELREGRSDLTDLLLIRLWDFIGISeHSGIALVAVGGYGRGELAPYSDIDLLFLHDGKPAEEVEPKIER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 94 FITFLWDIKFDIGHSVRTLEETISIGKSDITVATNLMESRLLNGPQELYQQLQLAIEQPDFWPSSE-FYLAKRDEQFQRH 172
Cdd:TIGR01693 84 FLYPLWDLGFEVGHSVRTLEECARIAKADLTVATNLLEARHLAGDEALFFRLKERVRREDWRNTARsFLAAKVEEQDERH 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 173 E--ANNAFDLEPNIKTCPGGLRDIQTVGWIAKRHFKTTIVEQLVQHGFLSQEELDKLLSCQDFLWSMRFALHQTAKRPED 250
Cdd:TIGR01693 164 AryGDTAYNLEPDIKEGPGGLRDLHTLFWVALYQLGVRRLEDLVKQGFLTDAEYKLLAEARDFLWDVRFALHLTTGRADD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 251 KLLFNHQHDVANAMGYSDEDQLAVEVMMKQYYQQIREVDELCEMLLQ-----LFKREFLGRIKTLDICIMNEQYQRRGHF 325
Cdd:TIGR01693 244 RLLFDHQDEIAAALGYGDEGNPAVERFMRRYFQAARRIGYLTEAFLRhyeeaLLSRGPSARVRRPKRRPLDEGFVEDGGE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 326 IESTVDNLFN-DKSQIITLFLNIAKDKEisGIYAPTLRQLRLARENLTAPLCDDAQCRTAFMNIIKHPDGI-RALSMMHK 403
Cdd:TIGR01693 324 LVLARTAVFErDPALLLRLFAIAAQRGL--PIHPAALRQLTASLPLLPTPLREDPEARELFLELLTSGNGTvRALRAMNR 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 404 HGILGSYMPAWQKISGQMQFDLFHAYTVDEHTHRLLKNIDRFSQPKYKDEFPLCSVLIHTLTKKGLLVLAAIFHDIGKGR 483
Cdd:TIGR01693 402 AGVLGRFLPEWGRIVGQMQFDLFHVYTVDEHTLRTVVHLAPFARGRLAREHPLASELMPKIEDPELLYLAALLHDIGKGR 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 484 GGDHSELGALDALEFGRLHALNEHDTRLIAWLVENHLLMSVIAQRRDIHDPDVINSFASIVQDETRLAYLYCLTVADICA 563
Cdd:TIGR01693 482 GGDHSVLGAEDARDVCPRLGLDRPDTELVAWLVRNHLLMSITAQRRDLNDPKTVFAFAEAVGDPERLEYLLALTVADIRA 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 564 TNNKLWNNWKGSLLRELYFYTLRALRRGAQGDVDAEERITEyKAKALHQLHTNDafYDKHAVEELWGYFQDDYFLRHTPI 643
Cdd:TIGR01693 562 TGPGVWNSWKASLLRDLYNRTEQVLRGGLEPPADPAEPIAE-QRKLAVALLRTD--YTSNEAEVLWLRAYDDYFLRFTHK 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 644 AIAQHCDLILRNQPPNKPIIAIFHNPNKTVSELFVYTQDMKNLFAKVMRVLGSKNVQINDAHVMATTGGWALDTFNISEH 723
Cdd:TIGR01693 639 EIAWHAESLRRALSSGGPLALIDGTRPSGGTEVFIYAPDQPGLFAKVAGALAMLSLSVHDAQVNTTKDGVALDTFVVQDL 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 724 NGQPILDERRVKSIVQTLTKSLT-QKHFKPHNNRR--IARRTKQFKVPTRISFITCDHGEHTLFELVALDMPGLLATVGD 800
Cdd:TIGR01693 719 FGSPPAAERVFQELLQGLVDVLAgLAKDPDTISARraRRRRLQHFAVPPRVTILNTASRKATIMEVRALDRPGLLARVGR 798
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|..
gi 1101461855 801 VFTKFKITLHNAKITTIGERVEDFFIITDKDENPLTQEQQNTLQQALVLAIE 852
Cdd:TIGR01693 799 TLEELGLSIQSAKITTFGEKAEDVFYVTDLFGLKLTDEEEQRLLEVLAASVA 850
|
|
| GlnD_UR_UTase |
pfam08335 |
GlnD PII-uridylyltransferase; This is a family of bifunctional uridylyl-removing enzymes ... |
160-296 |
7.55e-46 |
|
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: 160.82 E-value: 7.55e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 160 FYLAKRDEQFQRHE--ANNAFDLEPNIKTCPGGLRDIQTVGWIAKRHFKTTIVEQLVQHGFLSQEELDKLLSCQDFLWSM 237
Cdd:pfam08335 2 FMKAKIEEQVARHGryGDTAYNLEPNIKLGPGGLRDIEFIVWIAQLIFTLRALEELVELGLLTREEARELRRAYRFLRRV 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1101461855 238 RFALHQTAKRPEDKLLFNHQHDVANAMGYSDEDQLAVEVMMKQYYQQIREVDELCEMLL 296
Cdd:pfam08335 82 RHRLHLLADRQTDRLPFDLQRRLARALGYARDGWLAVERFMRRLFRHAHRVSRLFEILL 140
|
|
| ACT_ACR-UUR-like_2 |
cd04899 |
C-terminal ACT domains of the bacterial signal-transducing uridylyltransferase ... |
782-851 |
6.12e-26 |
|
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: 101.38 E-value: 6.12e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 782 TLFELVALDMPGLLATVGDVFTKFKITLHNAKITTIGERVEDFFIITDKDENPLTQEQQNTLQQALVLAI 851
Cdd:cd04899 1 TVLELTALDRPGLLADVTRVLAELGLNIHSAKIATLGERAEDVFYVTDADGQPLDPERQEALRAALGEAL 70
|
|
| HDc |
smart00471 |
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ... |
464-573 |
2.34e-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: 38.82 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 464 LTKKGLLVLAAIFHDIGKGRGGD-----------HSELGALDALEFGrlhaLNEHDTRLIAWLVENHLLMSVIAQRRDIh 532
Cdd:smart00471 25 LLDIELLLLAALLHDIGKPGTPDsflvktsvledHHFIGAEILLEEE----EPRILEEILRTAILSHHERPDGLRGEPI- 99
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1101461855 533 dpdvinsfasivqdetrLAYLYCLTVADICATNNKLWNNWK 573
Cdd:smart00471 100 -----------------TLEARIVKVADRLDALRADRRYRR 123
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05007 |
PRK05007 |
bifunctional uridylyltransferase/uridylyl-removing protein GlnD; |
5-856 |
0e+00 |
|
bifunctional uridylyltransferase/uridylyl-removing protein GlnD;
Pssm-ID: 235329 [Multi-domain] Cd Length: 884 Bit Score: 1217.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 5 KQANNEFSDWLNEQFERGGDIRELLHQRCQYVDDLLQQLWQHFELNHTP-ISLIAVGGYGRGELHPHSDVDLLILSLKTL 83
Cdd:PRK05007 31 KQHLDTFQQWLGDAFDAGISAEQLVEARTEFIDQLLQRLWIEAGFDQIPdLALVAVGGYGRGELHPLSDIDLLILSRKKL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 84 TNEQTEKISQFITFLWDIKFDIGHSVRTLEETISIGKSDITVATNLMESRLLNGPQELYQQLQLAIEQPDFWPSSEFYLA 163
Cdd:PRK05007 111 PDEQAQKVGELITLLWDLKLEVGHSVRTLEECLLEGLSDLTVATNLIESRLLCGDVALFLELQKHIFSDGFWPSEKFYAA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 164 KRDEQFQRHE--ANNAFDLEPNIKTCPGGLRDIQTVGWIAKRHFKTTIVEQLVQHGFLSQEELDKLLSCQDFLWSMRFAL 241
Cdd:PRK05007 191 KVEEQNERHQryHGTSYNLEPDIKSSPGGLRDIHTLQWVARRHFGATSLDEMVGFGFLTPAERAELNECQHFLWRIRFAL 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 242 HQTAKRPEDKLLFNHQHDVANAMGYSDEDQLAVEVMMKQYYQQIREVDELCEMLLQLFKREFLGRIKTLDICIMNEQYQR 321
Cdd:PRK05007 271 HLVLSRYDNRLLFDRQLSVAQLLGYEGEGNEPVERMMKDYYRTTRRVSELNQMLLQLFDEAILALTADEKPRPIDDEFQL 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 322 RGHFIESTVDNLFNDKSQ-IITLFLNIAKDKEISGIYAPTLRQLRLARENLTAPLCDDAQCRTAFMNIIKHPDGI-RALS 399
Cdd:PRK05007 351 RGTLIDLRDETLFQRQPEaILRMFYLMARNSNITGIYSTTLRQLRHARRHLNQPLCEIPEARKLFMEILRHPGAVsRALL 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 400 MMHKHGILGSYMPAWQKISGQMQFDLFHAYTVDEHTHRLLKNIDRFSQPKYKDEFPLCSVLIHTLTKKGLLVLAAIFHDI 479
Cdd:PRK05007 431 PMHRHSVLSAYMPQWSHIVGQMQFDLFHAYTVDEHTIRVLLKLESFADEETRQRHPLCVELYPRLPKKELLLLAALFHDI 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 480 GKGRGGDHSELGALDALEFGRLHALNEHDTRLIAWLVENHLLMSVIAQRRDIHDPDVINSFASIVQDETRLAYLYCLTVA 559
Cdd:PRK05007 511 AKGRGGDHSILGAQDALEFAELHGLNSRETQLVAWLVRNHLLMSVTAQRRDIQDPDVIKQFAEEVQDENRLRYLVCLTVA 590
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 560 DICATNNKLWNNWKGSLLRELYFYTLRALRRGAQGDVDAEERITEYKAKALHQLHTNDafYDKHAVEELWGYFQDDYFLR 639
Cdd:PRK05007 591 DICATNETLWNSWKQSLLRELYFATEKQLRRGMENPPDMRERVRHHQLQALALLRMDN--IDEEALHQIWSRCRADYFLR 668
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 640 HTPIAIAQHCDLILRNQpPNKPIIAIFHNPNKTVSELFVYTQDMKNLFAKVMRVLGSKNVQINDAHVMATTGGWALDTFN 719
Cdd:PRK05007 669 HTPNQLAWHARHLLQHD-LDKPLVLLSKQATRGGTEIFIWSPDRPYLFAAVCAELDRRNLSVHDAQIFTSRDGMAMDTFI 747
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 720 ISEHNGQPiLDERRVKSIVQTLTKSLTQKHFKPHNNRRIARRTKQFKVPTRISFITCDHGEHTLFELVALDMPGLLATVG 799
Cdd:PRK05007 748 VLEPDGSP-LSQDRHQVIRKALEQALTQSSPQPPKPRRLPAKLRHFNVPTEVSFLPTHTDRRSYMELIALDQPGLLARVG 826
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*..
gi 1101461855 800 DVFTKFKITLHNAKITTIGERVEDFFIITDKDENPLTQEQQNTLQQALVLAIEKLNR 856
Cdd:PRK05007 827 KIFADLGISLHGARITTIGERVEDLFILATADRRALNEELQQELRQRLTEALNPNDK 883
|
|
| GlnD |
COG2844 |
UTP:GlnB (protein PII) uridylyltransferase [Posttranslational modification, protein turnover, ... |
1-852 |
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: 1129.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 1 MASCKQANNEFSDWLNEQFERGGDIRELLHQRCQYVDDLLQQLWQHFEL-NHTPISLIAVGGYGRGELHPHSDVDLLILS 79
Cdd:COG2844 4 LAALREALAEGRAALRERFRAGADGRELVRARAALVDQLLRALWDLAGLtEPERLALVAVGGYGRGELAPHSDIDLLFLL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 80 LKTLTNEQTEKISQFITFLWDIKFDIGHSVRTLEETISIGKSDITVATNLMESRLLNGPQELYQQLQLAIEQPDFWPSSE 159
Cdd:COG2844 84 PDKPTPALEEVIEAFLYLLWDLGLEVGHSVRTVDECLREAREDITVRTALLEARLLAGDEALFEELRERFRADVFWDSRA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 160 FYLAKRDEQFQRHE--ANNAFDLEPNIKTCPGGLRDIQTVGWIAKRHFKTTIVEQLVQHGFLSQEELDKLLSCQDFLWSM 237
Cdd:COG2844 164 FFEAKLAEQRERHAkyGDTRYNLEPNIKEGPGGLRDLQTLLWIAKRHFGVRSLEELVKKGLLTEEEYRELRRAEDFLWRV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 238 RFALHQTAKRPEDKLLFNHQHDVANAMGYSDED-QLAVEVMMKQYYQQIREVDELCEMLLQLFKREFLGRIKTLDICIMN 316
Cdd:COG2844 244 RFALHLLAGRAEDRLLFDLQREVAERLGYQDTEgNRAVERFMQRYYRTAKAVGRLNEILLQRLEEAILKPPGLRRPRPIN 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 317 EQYQRRGHFIESTVDNLF-NDKSQIITLFLNIAKDKEISGIYAPTLRQLRLARENLTAPLCDDAQCRTAFMNIIKHPDGI 395
Cdd:COG2844 324 EGFQLRNGRLEVADPDVFeRDPVALLRLFLLAAQHPEGLGIHPDTLRLLRRALRLIDDAFRRDPEARRLFLEILRQPRGI 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 396 -RALSMMHKHGILGSYMPAWQKISGQMQFDLFHAYTVDEHTHRLLKNIDRFSQPKYKDEFPLCSVLIHTLTKKGLLVLAA 474
Cdd:COG2844 404 tRALRRMNEYGVLGRYIPEFGRIVGQMQFDLFHVYTVDEHTLRVVRNLRRFERGELAEEFPLASELIAELPKPELLYLAA 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 475 IFHDIGKGRGGDHSELGALDALEFGRLHALNEHDTRLIAWLVENHLLMSVIAQRRDIHDPDVINSFASIVQDETRLAYLY 554
Cdd:COG2844 484 LFHDIAKGRGGDHSELGAEDARRFCPRHGLSPEDTELVAWLVRHHLLMSHTAQRRDISDPEVIRDFARLVGSEERLDYLY 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 555 CLTVADICATNNKLWNNWKGSLLRELYFYTLRALRRGAQGdVDAEERITEYKAKALHQLhtNDAFYDKHAVEELWGYFQD 634
Cdd:COG2844 564 LLTVADIRATGPKVWNSWKASLLRELYRATLRALRGGLEP-PDREERIEERKEEALALL--ADQGWDEEEIEALWARLPD 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 635 DYFLRHTPIAIAQHCDLILRNQPPNKPIIAIFHNPNKTVSELFVYTQDMKNLFAKVMRVLGSKNVQINDAHVMATTGGWA 714
Cdd:COG2844 641 DYFLRHDPEEIAWHARLLLRADDSGKPLVLIRPDPDRGGTEVFVYTPDRPGLFARIAGALAALGLNILDARIHTTRDGYA 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 715 LDTFNISEHNGQPILDERRVKSIVQTLTKSLTQKH-FKPHNNRRIARRTKQFKVPTRISFITCDHGEHTLFELVALDMPG 793
Cdd:COG2844 721 LDTFIVLDPDGEPIDDPDRLERIEQALEEALSGEVpLPEPLARRLSRRLRHFPVPPRVTFDNDASNRYTVLEVSALDRPG 800
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 794 LLATVGDVFTKFKITLHNAKITTIGERVEDFFIITDKDENPLTQ-EQQNTLQQALVLAIE 852
Cdd:COG2844 801 LLYDIARVLADLGLNIHSAKIATLGERVEDVFYVTDLDGQKLTDpERQEALREALLEALD 860
|
|
| glnD |
PRK00275 |
PII uridylyl-transferase; Provisional |
5-848 |
0e+00 |
|
PII uridylyl-transferase; Provisional
Pssm-ID: 234709 [Multi-domain] Cd Length: 895 Bit Score: 897.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 5 KQANNEFSDWLNEQFERGGDIRELLHQRCQYVDDLLQQLWQHFEL-NHTPISLIAVGGYGRGELHPHSDVDLLILSLKTL 83
Cdd:PRK00275 29 KKAIRQAREVLDERFRSGRDIRRLIEDRAWFVDQILQQAWHQFDWsDDADIALVAVGGYGRGELHPYSDIDLLILLDSAD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 84 TNEQTEKISQFITFLWDIKFDIGHSVRTLEETISIGKSDITVATNLMESRLLNGPQELYQQLQLAIEQPDFWPSSEFYLA 163
Cdd:PRK00275 109 HEEFREPIERFLTLLWDIGLEIGQSVRSVDECAEEARADLTVITNLMESRTIAGPESLRQRMLEVTSSEHMWPSKEFFLA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 164 KRDEQFQRHEANN--AFDLEPNIKTCPGGLRDIQTVGWIAKRHFKTTIVEQLVQHGFLSQEELDKLLSCQDFLWSMRFAL 241
Cdd:PRK00275 189 KRAEQKARHHKYNdtEYNLEPNVKGSPGGLRDIQTILWVAKRQFGTLNLHALVGEGFLTESEYGLLASGQEFLWKVRYAL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 242 HQTAKRPEDKLLFNHQHDVANAMGYSDEDQ-LAVEVMMKQYYQQIREVDELCEMLLQLFKREFLGRIKTLDICIMNEQYQ 320
Cdd:PRK00275 269 HMLAGRAEDRLLFDHQRSIATLLGYEDSDAkLAVEQFMQKYYRVVMALAELNDLILQHFEEVILAADDSGTIQPLNSRFQ 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 321 RRGHFIESTVDNLFNDK-SQIITLFLNIAKDKEISGIYAPTLRQLRLARENLTAPLCDDAQCRTAFMNIIKHPDGI-RAL 398
Cdd:PRK00275 349 LRDGYIEATHPNVFKRTpFALLEIFVLMAQHPEIKGVRADTIRLLREHRHLIDDAFRNDIRNTSLFIELFKCPIGIhRNL 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 399 SMMHKHGILGSYMPAWQKISGQMQFDLFHAYTVDEHTHRLLKNIDRFSQPKYKDEFPLCSVLIHTLTKKGLLVLAAIFHD 478
Cdd:PRK00275 429 RRMNRYGILGRYLPEFGHIVGQMQHDLFHIYTVDAHTLNLIKNLRKLRYPEVSEKFPLASKLMGRLPKPELLYIAGLYHD 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 479 IGKGRGGDHSELGALDALEFGRLHALNEHDTRLIAWLVENHLLMSVIAQRRDIHDPDVINSFASIVQDETRLAYLYCLTV 558
Cdd:PRK00275 509 IGKGRGGDHSELGAVDAEAFCQRHQLPAWDTRLVVWLVENHLLMSTTAQRKDLSDPQVIHDFALKVGDQTHLDYLYVLTV 588
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 559 ADICATNNKLWNNWKGSLLRELYFYTLRALRRGAQGDVDAEERITEYKAKALHQLHTNDafYDKHAVEELWGYFQDDYFL 638
Cdd:PRK00275 589 ADINATNPTLWNSWRASLLRQLYTETKRALRRGLENPVDREEQIRQTQSAALDILVRKG--TDPDDAEQLWSQLGDDYFL 666
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 639 RHTPIAIAQHCDLILRNQPPNKPIIAIFHNPNKTV---SELFVYTQDMKNLFAKVMRVLGSKNVQINDAHVMATTGGWAL 715
Cdd:PRK00275 667 RHTAGDIAWHTEAILQHPDDGGPLVLIKETTQREFeggTQIFIYAPDQHDFFAATVAAMDQLNLNIHDARIITSSSQFTL 746
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 716 DTFNISEHNGQPILDE-RRVKSIVQTLTKSL-TQKHFKPHNNRRIARRTKQFKVPTRISFITCDHGEHTLFELVALDMPG 793
Cdd:PRK00275 747 DTYIVLDDDGEPIGDNpARIEQIREGLTEALrNPDDYPTIIQRRVPRQLKHFAFPTQVTISNDAQRPVTVLEIIAPDRPG 826
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*.
gi 1101461855 794 LLATVGDVFTKFKITLHNAKITTIGERVEDFFIITDKDENPLTQEQ-QNTLQQALV 848
Cdd:PRK00275 827 LLARIGRIFLEFDLSLQNAKIATLGERVEDVFFITDADNQPLSDPQlCSRLQDAIC 882
|
|
| UTase_glnD |
TIGR01693 |
[Protein-PII] uridylyltransferase; This model describes GlnD, the uridylyltransferase ... |
15-852 |
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: 846.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 15 LNEQFERGGDIRELLHQRCQYVDDLLQQLWQHFELN-HTPISLIAVGGYGRGELHPHSDVDLLILSLKTLTNEQTEKISQ 93
Cdd:TIGR01693 4 LLEEFARGGDGRELREGRSDLTDLLLIRLWDFIGISeHSGIALVAVGGYGRGELAPYSDIDLLFLHDGKPAEEVEPKIER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 94 FITFLWDIKFDIGHSVRTLEETISIGKSDITVATNLMESRLLNGPQELYQQLQLAIEQPDFWPSSE-FYLAKRDEQFQRH 172
Cdd:TIGR01693 84 FLYPLWDLGFEVGHSVRTLEECARIAKADLTVATNLLEARHLAGDEALFFRLKERVRREDWRNTARsFLAAKVEEQDERH 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 173 E--ANNAFDLEPNIKTCPGGLRDIQTVGWIAKRHFKTTIVEQLVQHGFLSQEELDKLLSCQDFLWSMRFALHQTAKRPED 250
Cdd:TIGR01693 164 AryGDTAYNLEPDIKEGPGGLRDLHTLFWVALYQLGVRRLEDLVKQGFLTDAEYKLLAEARDFLWDVRFALHLTTGRADD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 251 KLLFNHQHDVANAMGYSDEDQLAVEVMMKQYYQQIREVDELCEMLLQ-----LFKREFLGRIKTLDICIMNEQYQRRGHF 325
Cdd:TIGR01693 244 RLLFDHQDEIAAALGYGDEGNPAVERFMRRYFQAARRIGYLTEAFLRhyeeaLLSRGPSARVRRPKRRPLDEGFVEDGGE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 326 IESTVDNLFN-DKSQIITLFLNIAKDKEisGIYAPTLRQLRLARENLTAPLCDDAQCRTAFMNIIKHPDGI-RALSMMHK 403
Cdd:TIGR01693 324 LVLARTAVFErDPALLLRLFAIAAQRGL--PIHPAALRQLTASLPLLPTPLREDPEARELFLELLTSGNGTvRALRAMNR 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 404 HGILGSYMPAWQKISGQMQFDLFHAYTVDEHTHRLLKNIDRFSQPKYKDEFPLCSVLIHTLTKKGLLVLAAIFHDIGKGR 483
Cdd:TIGR01693 402 AGVLGRFLPEWGRIVGQMQFDLFHVYTVDEHTLRTVVHLAPFARGRLAREHPLASELMPKIEDPELLYLAALLHDIGKGR 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 484 GGDHSELGALDALEFGRLHALNEHDTRLIAWLVENHLLMSVIAQRRDIHDPDVINSFASIVQDETRLAYLYCLTVADICA 563
Cdd:TIGR01693 482 GGDHSVLGAEDARDVCPRLGLDRPDTELVAWLVRNHLLMSITAQRRDLNDPKTVFAFAEAVGDPERLEYLLALTVADIRA 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 564 TNNKLWNNWKGSLLRELYFYTLRALRRGAQGDVDAEERITEyKAKALHQLHTNDafYDKHAVEELWGYFQDDYFLRHTPI 643
Cdd:TIGR01693 562 TGPGVWNSWKASLLRDLYNRTEQVLRGGLEPPADPAEPIAE-QRKLAVALLRTD--YTSNEAEVLWLRAYDDYFLRFTHK 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 644 AIAQHCDLILRNQPPNKPIIAIFHNPNKTVSELFVYTQDMKNLFAKVMRVLGSKNVQINDAHVMATTGGWALDTFNISEH 723
Cdd:TIGR01693 639 EIAWHAESLRRALSSGGPLALIDGTRPSGGTEVFIYAPDQPGLFAKVAGALAMLSLSVHDAQVNTTKDGVALDTFVVQDL 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 724 NGQPILDERRVKSIVQTLTKSLT-QKHFKPHNNRR--IARRTKQFKVPTRISFITCDHGEHTLFELVALDMPGLLATVGD 800
Cdd:TIGR01693 719 FGSPPAAERVFQELLQGLVDVLAgLAKDPDTISARraRRRRLQHFAVPPRVTILNTASRKATIMEVRALDRPGLLARVGR 798
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|..
gi 1101461855 801 VFTKFKITLHNAKITTIGERVEDFFIITDKDENPLTQEQQNTLQQALVLAIE 852
Cdd:TIGR01693 799 TLEELGLSIQSAKITTFGEKAEDVFYVTDLFGLKLTDEEEQRLLEVLAASVA 850
|
|
| glnD |
PRK01759 |
bifunctional uridylyltransferase/uridylyl-removing protein GlnD; |
24-847 |
0e+00 |
|
bifunctional uridylyltransferase/uridylyl-removing protein GlnD;
Pssm-ID: 234980 [Multi-domain] Cd Length: 854 Bit Score: 800.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 24 DIRELLHQRCQYVDDLLQQLWQHFELN-HTPISLIAVGGYGRGELHPHSDVDLLILSLKTLTNEQTEKISQFITFLWDIK 102
Cdd:PRK01759 26 DVFELIENRSDFYDQLLIHLWQQFGLEeQSDLALIAVGGYGRREMFPLSDLDILILTEQPPDEETEEKINQFFQFLWDCG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 103 FDIGHSVRTLEETISIGKSDITVATNLMESRLLNGPQELYQQLQLAIEQPDFWPSSEFYLAKRDEQFQRHEA--NNAFDL 180
Cdd:PRK01759 106 FEVGASVRTLAECESEGRADITIATNLLESRFLTGNEKLFDALVELLQQADFWSKEAFFQAKIQEKIERYQRyhNTSYNL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 181 EPNIKTCPGGLRDIQTVGWIAKRHFKTTIVEQLVQHGFLSQEELDKLLSCQDFLWSMRFALHQTAKRPEDKLLFNHQHDV 260
Cdd:PRK01759 186 EPDIKYSPGGLRDLHLLYWIALRHSGAKSLEEILQSGFIYPEEYAELQQSQQFLFKVRFALHLILKRYDNRLLFDRQLKV 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 261 ANAMGYSDEDQLAVEVMMKQYYQQIREVDELCEMLLQLFKREFLGRIKTLDICIMNEQYQRRGHFIESTVDNLFNDK-SQ 339
Cdd:PRK01759 266 SELLGFQGEGNQGVEKMMKSFFQALQSISLLSDLLVKHYREHFLQPNQNVEIQPLDDDFYLINNAICLRNPDCFEQQpES 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 340 IITLFLNIAKDKEISgIYAPTLRQLRLARENLTAPLCDDAQCRTAFMNIIKHPDGI-RALSMMHKHGILGSYMPAWQKIS 418
Cdd:PRK01759 346 ILDLFFYLTQYPQAE-IHSTTLRQLRLALEQLQQPLCELPAARERFLRLFNQPNAIkRALVPMHQYGVLTAYLPQWKGIV 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 419 GQMQFDLFHAYTVDEHTHRLLKNIDRFSQPKYKDEFPLCSVLIHTLTKKGLLVLAAIFHDIGKGRGGDHSELGALDALEF 498
Cdd:PRK01759 425 GLMQFDLFHIYTVDEHTLRVMLKLESFLDEESAEQHPICHQIFSQLSDRTLLYIAALFHDIAKGRGGDHAELGAVDMRQF 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 499 GRLHALNEHDTRLIAWLVENHLLMSVIAQRRDIHDPDVINSFASIVQDETRLAYLYCLTVADICATNNKLWNNWKGSLLR 578
Cdd:PRK01759 505 AQQHGFDQREIETMAWLVQQHLLMSVTAQRRDIHDPEVVMNFAEEVQNQVRLDYLTCLTVADICATNETLWNSWKRSLFA 584
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 579 ELYFYTLRALRRGAQGDVDAEERITEYKAKALHQLHTNDAFYDKHAVEELWGYFQDDYFLRHTPIAIAQHCDLILRNQpp 658
Cdd:PRK01759 585 TLYQFTNQQFQQGMDELLDYQEKAEENRQQALELLQQKYSALSETQIEQLWQRCPEDYFLRNTPKQIAWHALLLLDFR-- 662
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 659 NKPIIAIFHNPNKTVSELFVYTQDMKNLFAKVMRVLGSKNVQINDAHVMATTGGWALDTFNISEHNGQPILDERRvKSIV 738
Cdd:PRK01759 663 GDLLVKISNRFSRGGTEIFIYCQDQANLFLKVVSTIGAKKLSIHDAQIITSQDGYVLDSFIVTELNGKLLEFDRR-RQLE 741
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 739 QTLTKSLTQ---KHFKPHNNRRIArrtkQFKVPTRISFITCDHGEHTLFELVALDMPGLLATVGDVFTKFKITLHNAKIT 815
Cdd:PRK01759 742 QALTKALNTnklKKLNLEENHKLQ----HFHVKTEVRFLNEEKQEQTEMELFALDRAGLLAQVSQVFSELNLNLLNAKIT 817
|
810 820 830
....*....|....*....|....*....|..
gi 1101461855 816 TIGERVEDFFIITDKDENPLTQEQQNTLQQAL 847
Cdd:PRK01759 818 TIGEKAEDFFILTNQQGQALDEEERKALKSRL 849
|
|
| PRK03059 |
PRK03059 |
PII uridylyl-transferase; Provisional |
15-847 |
0e+00 |
|
PII uridylyl-transferase; Provisional
Pssm-ID: 235101 [Multi-domain] Cd Length: 856 Bit Score: 717.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 15 LNEQFERGGDIRELLHQRCQYVDDLLQQLWQHFELNHTpISLIAVGGYGRGELHPHSDVDLLILSLKTLTNEQTEKISQF 94
Cdd:PRK03059 24 LLARFRQAPNVTALLHALSRLVDQALRRLWQECGLPAG-AALVAVGGYGRGELFPYSDVDLLVLLPDAPDAALDARIERF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 95 ITFLWDIKFDIGHSVRTLEETISIGKSDITVATNLMESRLLNGPQELYQQLQLAI-EQPDfwpSSEFYLAKRDEQFQRHE 173
Cdd:PRK03059 103 IGLCWDLGLEIGSSVRTVDECIEEAAQDVTVQTSLLEARLLTGSAALFERFQRRYrAALD---PRAFFQAKLLEMRQRHA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 174 A--NNAFDLEPNIKTCPGGLRDIQTVGWIAK-----RHFKttiveQLVQHGFLSQEELDKLLSCQDFLWSMRFALHQTAK 246
Cdd:PRK03059 180 KfqDTPYSLEPNCKESPGGLRDLQTILWIARaaglgSSWR-----ELAKRGLITDREARQLRRNERFLKTLRARLHLLAG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 247 RPEDKLLFNHQHDVANAMGYSDE-DQLAVEVMMKQYYQQIREVDELCEMLLQLFKREFLGRIKTLDICImNEQYQRRGHF 325
Cdd:PRK03059 255 RREDRLVFDLQTALAESFGYRPTaAKRASEQLMRRYYWAAKAVTQLNTILLQNIEARLFPSTSGITRVI-NERFVEKQGM 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 326 IESTVDNLF-NDKSQIITLFLNIAKDKEISGIYAPTLRQLRLARENLTAPLCDDAQCRTAFMNIIKHPDGI-RALSMMHK 403
Cdd:PRK03059 334 LEIASDDLFeRHPHAILEAFLLYQQTPGLKGLSARTLRALYNARDVMNAAFRRDPVNRALFMQILQQPRGItHALRLMNQ 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 404 HGILGSYMPAWQKISGQMQFDLFHAYTVDEHTHRLLKNIDRFSQPKYKDEFPLCSVLIHTLTKKGLLVLAAIFHDIGKGR 483
Cdd:PRK03059 414 TSVLGRYLPNFRRIVGQMQHDLFHVYTVDQHILMVLRNLRRFAMAEHAHEYPFCSQLIANFDRPWLLYVAALFHDIAKGR 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 484 GGDHSELGALDALEFGRLHALNEHDTRLIAWLVENHLLMSVIAQRRDIHDPDVINSFASIVQDETRLAYLYCLTVADICA 563
Cdd:PRK03059 494 GGDHSTLGAVDARRFCRQHGLAREDAELVVWLVEHHLTMSQVAQKQDLSDPEVIARFAELVGDERRLTALYLLTVADIRG 573
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 564 TNNKLWNNWKGSLLRELYFYTLRALrRGAQGDVDAEerITEYKAKALHQLHTNDAfyDKHAVEELWGYFQDDYFLRHTPI 643
Cdd:PRK03059 574 TSPKVWNAWKGKLLEDLYRATLRVL-GGAAPDAHSE--LEARKEEALALLRLEAL--PDDAHEALWDQLDVGYFLRHDAA 648
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 644 AIAQHCDLILRNQPPNKPIIAIFHNPNKTVSELFVYTQDMKNLFAKVMRVLGSKNVQINDAHVMATTGGWALDTFNISeH 723
Cdd:PRK03059 649 DIAWHTRHLYRHVDTDTPIVRARLSPAGEGLQVMVYTPDQPDLFARICGYFDRAGFSILDARVHTTRHGYALDTFQVL-D 727
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 724 NGQPILDERRVKSIVQTLTKSLTQK-HFKPHNNRRIARRTKQFKVPTRISFITCDHGEHTLFELVALDMPGLLATVGDVF 802
Cdd:PRK03059 728 PEEDVHYRDIINLVEHELAERLAEQaPLPEPSKGRLSRQVKHFPITPRVDLRPDERGQYYILSVSANDRPGLLYAIARVL 807
|
810 820 830 840
....*....|....*....|....*....|....*....|....*
gi 1101461855 803 TKFKITLHNAKITTIGERVEDFFIITDKDenpltqEQQNTLQQAL 847
Cdd:PRK03059 808 AEHRVSVHTAKINTLGERVEDTFLIDGSG------LSDNRLQIQL 846
|
|
| PRK04374 |
PRK04374 |
[protein-PII] uridylyltransferase; |
15-847 |
0e+00 |
|
[protein-PII] uridylyltransferase;
Pssm-ID: 179839 [Multi-domain] Cd Length: 869 Bit Score: 558.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 15 LNEQFERGGDIRELLHQRCQYVDDLLQQLWQHFELNHTPISLIAVGGYGRGELHPHSDVDLLILSLKTLTNEQTEKISQF 94
Cdd:PRK04374 34 LCKRFDQGEPIERLLALRARAVDQLMRNAWTRCIPADSGLSLHAVGGYGRGELFPRSDVDLLVLGETAAQQRHEQALARL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 95 ITFLWDIKFDIGHSVRTLEETISiGKSDITVATNLMESRLLNGPQELYQQLQLAIEQPDFWPSSEFYLAKRDEQFQRHE- 173
Cdd:PRK04374 114 FALLWDVGLPISHAVRSPAQCTA-AAADQTVLTALIESRPLVADAAARAALAAAIAPQQVWPPRAFFQAKREELLARHQr 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 174 -ANNAFDLEPNIKTCPGGLRDIQTVGWIAKRHFKTTIVEQLVQHGFLSQEELDKLLSCQDFLWSMRFALHQTAKRPEDKL 252
Cdd:PRK04374 193 fGDTADNLEPDIKDGPGGLRDLQTLGWMALRAFGVKDLEALVGLGHVGCDEAAALRREREELARLRFGLHLVANRPEERL 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 253 LFNHQHDVANAMGYSDE-DQLAVEVMMKQYYQQIREVDELCEMLLQLFKREFLGriKTLDICIMNEQYQRRGHFIESTVD 331
Cdd:PRK04374 273 RFDYQKTLAERLGFADDpESLGVEKMMQRFYRSAALIRRISDRLLQRFEEQFDG--EATPEPLGGGFSLRRGYLAADADS 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 332 NLFNDKSQIITLFLNIAKDKEISGIYAPTLRQLRLARENLTAPLCDDAQCRTAFMNIIKHPDGIRALSMMHKHGILGSYM 411
Cdd:PRK04374 351 WPDGDVLQVFALFAQWAAHREVRGLHSLTARALAEVLRDLPAYDVADATARERFMALLRGPRAVETLNRMARLGVLGQWI 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 412 PAWQKISGQMQFDLFHAYTVDEHTHRLLKNIDRFSQPKYKDEFPLCSVLIHTLTKKGLLVLAAIFHDIGKGRGGDHSELG 491
Cdd:PRK04374 431 PAFASVSGRMQFDLFHVYTVDQHTLMVLRNIALFAAGRADERFSIAHEVWPRLRKPELLLLAGLFHDIAKGRGGDHSELG 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 492 ALDALEFGRLHALNEHDTRLIAWLVENHLLMSVIAQRRDIHDPDVINSFASIVQDETRLAYLYCLTVADICATNNKLWNN 571
Cdd:PRK04374 511 AVDARAFCLAHRLSEGDTELVTWLVEQHLRMSVTAQKQDISDPEVIHRFATLVGTRERLDYLYLLTCADIAGTSPKLWNA 590
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 572 WKGSLLRELYFYTLRALRRGAQGDVDAEERITEYK--AKALHQLHTndafYDKHAVEELWGYFQDDYFLRHTPIAIAQHC 649
Cdd:PRK04374 591 WKDRLLADLYFAARRALREGLEHPPPREERLREAResARALMQAQG----HDDATIDRQFAGMPDENFLRFRPEQLAWQA 666
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 650 DLILRNQPPNKPIIAIFHNPNKTVSELFVYTQDMKNLFAKVMRVLGSKNVQINDAHVMATTGGWALDTFNISEHNGQPIL 729
Cdd:PRK04374 667 ASLIEVEIGQTLVKARRAVPDNDALEVFVYSPDRDGLFAAIVATLDRKGYGIHRARVLDAPHDAIFDVFEVLPQDTYADG 746
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 730 DERRVKSIV-QTLTKSLTQkhFKPhNNRRIARRTKQFKVPTRISFITCDHGEHTLFELVALDMPGLLATVGDVFTKFKIT 808
Cdd:PRK04374 747 DPQRLAAALrQVLAGDLQK--VRP-ARRAVPRQLRHFRFAPRVEFSESAGGRRTRISLVAPDRPGLLADVAHVLRMQHLR 823
|
810 820 830
....*....|....*....|....*....|....*....
gi 1101461855 809 LHNAKITTIGERVEDFFIITDKDENPLTQEQQNTLQQAL 847
Cdd:PRK04374 824 VHDARIATFGERAEDQFQITDEHDRPLSESARQALRDAL 862
|
|
| PRK05092 |
PRK05092 |
PII uridylyl-transferase; Provisional |
5-852 |
2.64e-176 |
|
PII uridylyl-transferase; Provisional
Pssm-ID: 235342 [Multi-domain] Cd Length: 931 Bit Score: 532.91 E-value: 2.64e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 5 KQANNEFSDWLNEQFERGGDIRELLHQRCQYVDDLLQQLWQ------HFELNHTP---ISLIAVGGYGRGELHPHSDVDL 75
Cdd:PRK05092 48 KQALARGRAEARERLEADGSGRACARRLAYLTDELIRALYDfatthlYPADNPSEgerLAVLAVGGYGRGELAPGSDIDL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 76 LILslktLTNEQTEKISQFITF----LWDIKFDIGHSVRTLEETISIGKSDITVATNLMESRLLNGPQELYQQLQLAieq 151
Cdd:PRK05092 128 LFL----LPYKQTAWAESVVEYmlymLWDLGLKVGHATRSIDECIRLAREDMTIRTALLEARFLAGDRALFEELETR--- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 152 pdFW------PSSEFYLAKRDEQFQRHEANNA--FDLEPNIKTCPGGLRDIQTVGWIAKRHFKTTIVEQLVQHGFLSQEE 223
Cdd:PRK05092 201 --FDkevvkgTAAEFVAAKLAERDERHRRAGDsrYLVEPNVKEGKGGLRDLHTLFWIAKYVYRVRDAAELVKLGVFTREE 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 224 LDKLLSCQDFLWSMRFALHQTAKRPEDKLLFNHQHDVANAMGYSD-EDQLAVEVMMKQYYQQIREVDELCEMLL-----Q 297
Cdd:PRK05092 279 YRLFRRAEDFLWAVRCHLHFLTGRAEERLSFDLQPEIAERMGYTDhPGLSGVERFMKHYFLVAKDVGDLTRIFCaaleaQ 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 298 LFKRE--FLGRIKTLDICIMNEQYQRRGHFIESTVDNLF-NDKSQIITLFlNIAkDKEISGIYAPTLRQLRLARENLTAP 374
Cdd:PRK05092 359 HAKRApgLNRFARRRRKALDSDGFVVDNGRINLADPDVFeRDPVNLIRLF-HLA-DRHGLDIHPDAMRLVTRSLRLIDAA 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 375 LCDDAQCRTAFMNII-KHPDGIRALSMMHKHGILGSYMPAWQKISGQMQFDLFHAYTVDEHTHRLLKNIDRFSQPKYKDE 453
Cdd:PRK05092 437 LREDPEANRLFLDILtSRRNPERVLRRMNEAGVLGRFIPDFGRIVAMMQFNMYHHYTVDEHTIRAIGVLAEIERGELADE 516
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 454 FPLCSVLIHTLTKKGLLVLAAIFHDIGKGRGGDHSELGALDALEFG-RLhALNEHDTRLIAWLVENHLLMSVIAQRRDIH 532
Cdd:PRK05092 517 HPLASELMPKIESRRALYVAVLLHDIAKGRPEDHSIAGARIARRLCpRL-GLSPAETETVAWLVEHHLLMSDTAQKRDLS 595
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 533 DPDVINSFASIVQDETRLAYLYCLTVADICATNNKLWNNWKGSLLRELYFYTLRALrRGAQGDVDAEERITEYKAKALHQ 612
Cdd:PRK05092 596 DPKTIEDFADAVQSPERLKLLLILTVADIRAVGPGVWNGWKAQLLRTLYYETEEVL-TGGFSELNRAERVAAAKEALREA 674
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 613 LhtndAFYDKHAVEELWGYFQDDYFLRHTPIAIAQHCDLILRNQPPNKPIIAIFH-NPNKTVSELFVYTQDMKNLFAKVM 691
Cdd:PRK05092 675 L----SDWPKADRDAYLARHYPAYWLAVDLDTQARHARFIRDADDAGRPLATEVRpDPARGVTEVTVLAADHPGLFSRIA 750
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 692 RVLGSKNVQINDAHVMATTGGWALDTFNISEHNGQPILDERRVKSIVQTLTKSLTQKHFKPH---NNRRIARRTKQFKVP 768
Cdd:PRK05092 751 GACAAAGANIVDARIFTTTDGRALDTFWIQDAFGRDEDEPRRLARLAKAIEDALSGEVRLPEalaKRTKPKKRARAFHVP 830
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 769 TRISFITCDHGEHTLFELVALDMPGLLATVGDVFTKFKITLHNAKITTIGERVEDFFIITDKDENPLTQEQ-QNTLQQAL 847
Cdd:PRK05092 831 PRVTIDNEASNRFTVIEVNGRDRPGLLYDLTRALSDLNLNIASAHIATYGERAVDVFYVTDLFGLKITNEArQAAIRRAL 910
|
....*
gi 1101461855 848 VLAIE 852
Cdd:PRK05092 911 LAALA 915
|
|
| PRK03381 |
PRK03381 |
PII uridylyl-transferase; Provisional |
54-848 |
1.32e-59 |
|
PII uridylyl-transferase; Provisional
Pssm-ID: 235123 [Multi-domain] Cd Length: 774 Bit Score: 217.17 E-value: 1.32e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 54 ISLIAVGGYGRGELHPHSDVDLLILSLKTLTNEQTEKISQFITFLWDIKFDIGHSVRTLEETISIGKSDITVATNLMESR 133
Cdd:PRK03381 58 VALVAVGGLGRRELLPYSDLDLVLLHDGRPADDVAEVADRLWYPLWDAGIRLDHSVRTVPEALKVAGSDLKAALGLLDAR 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 134 LLNGPQELYQQL-QLAIEQpdfWPSSefyLAKRDEQF-----QRHEANN--AFDLEPNIKTCPGGLRDIQTVGWIAkrhf 205
Cdd:PRK03381 138 HIAGDADLSALLiGGVRRQ---WRNG---ARRRLPELveltrARWERSGeiAHLAEPDLKEGRGGLRDVQLLRALA---- 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 206 kttiVEQLVQ--HGFLSQEELDkllscqdfLWSMRFALHQTAKRPEDKLLFNHQHDVANAMGYSDEDQLAVEVmmkqyYQ 283
Cdd:PRK03381 208 ----AAQLADapGGGLDAAHRR--------LLDVRTELHRVSGRGRDRLLAQEADEVAAALGLGDRFDLARAL-----SD 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 284 QIREVDELCEMLL----QLFKREFLGRIKTLDicimneqyQRRgHFIESTVDN-----LFNDKS--QIITLFLNIAKDKE 352
Cdd:PRK03381 271 AARTISYAVDVGWrtaaNALPRRGLSALRRRP--------VRR-PLDEGVVEHagevvLARDARpaRDPGLVLRVAAAAA 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 353 ISG--IYAPTLRqlRLARE--NLTAPLCDDAqcRTAFMNIIKHPDG-IRALSMMHKHGILGSYMPAWQKISGQMQFDLFH 427
Cdd:PRK03381 342 TTGlpIAAATLS--RLAASapPLPTPWPAEA--RDDLLVLLGAGPAaVAVIEALDRTGLWGRLLPEWEAVRDLPPRDPVH 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 428 AYTVDEH-------THRLLKNIDRfsqPKykdefplcsvlihtltkkgLLVLAAIFHDIGKGRGGDHSELGALDALEFGR 500
Cdd:PRK03381 418 RWTVDRHlvetavrAAALTRRVAR---PD-------------------LLLLGALLHDIGKGRGGDHSVVGAELARQIGA 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 501 LHALNEHDTRLIAWLVENHLLMSVIAQRRDIHDPDVINSFASIVQDETR-LAYLYCLTVADICATNNKLWNNWKGSLLRE 579
Cdd:PRK03381 476 RLGLSPADVALLSALVRHHLLLPETATRRDLDDPATIEAVAEALGGDPVlLELLHALTEADSLATGPGVWSDWKASLVGD 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 580 LyfytlraLRRgaqgdVDAeeriteykAKALHQLHTNDAFyDKHAVEELwgyfqddyflrhtpiaiAQHCDLILRNQPPN 659
Cdd:PRK03381 556 L-------VRR-----CRA--------VLAGEPLPEPEPL-DPAQLALA-----------------ADGGVHVEIAPADP 597
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 660 KpiiaifhnpnktVSELFVYTQDMKNLFAKVMRVLGSKNVQINDAHVmATTGGWALDTFNISEHNGQP----ILDERRVK 735
Cdd:PRK03381 598 H------------MVEVTVVAPDRRGLLSKAAGVLALHRLRVRSASV-RSHDGVAVLEFVVSPRFGSPpdaaLLRQDLRR 664
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 736 SIVQTLtkSLTQkhfkphnnrRIARRTKQFK--------VPTRISFITCDHGEHTLFELVALDMPGLLATVGDVFTKFKI 807
Cdd:PRK03381 665 ALDGDL--DVLA---------RLAAREAAAAavpvrrpaAPPRVLWLDGASPDATVLEVRAADRPGLLARLARALERAGV 733
|
810 820 830 840
....*....|....*....|....*....|....*....|.
gi 1101461855 808 TLHNAKITTIGERVEDFFIITDKDENPLTQEQQnTLQQALV 848
Cdd:PRK03381 734 DVRWARVATLGADVVDVFYVTGAAGGPLADARA-AVEQAVL 773
|
|
| GlnD_UR_UTase |
pfam08335 |
GlnD PII-uridylyltransferase; This is a family of bifunctional uridylyl-removing enzymes ... |
160-296 |
7.55e-46 |
|
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: 160.82 E-value: 7.55e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 160 FYLAKRDEQFQRHE--ANNAFDLEPNIKTCPGGLRDIQTVGWIAKRHFKTTIVEQLVQHGFLSQEELDKLLSCQDFLWSM 237
Cdd:pfam08335 2 FMKAKIEEQVARHGryGDTAYNLEPNIKLGPGGLRDIEFIVWIAQLIFTLRALEELVELGLLTREEARELRRAYRFLRRV 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1101461855 238 RFALHQTAKRPEDKLLFNHQHDVANAMGYSDEDQLAVEVMMKQYYQQIREVDELCEMLL 296
Cdd:pfam08335 82 RHRLHLLADRQTDRLPFDLQRRLARALGYARDGWLAVERFMRRLFRHAHRVSRLFEILL 140
|
|
| glnD |
PRK00227 |
[protein-PII] uridylyltransferase; |
55-570 |
7.93e-32 |
|
[protein-PII] uridylyltransferase;
Pssm-ID: 178937 [Multi-domain] Cd Length: 693 Bit Score: 132.58 E-value: 7.93e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 55 SLIAVGGYGRGELHPHSDVDLLILSLKTLTneqTEKISQFITFLWDIKFDIGHSVRTLEETISIGKSDITVATNLMESRL 134
Cdd:PRK00227 29 ALAATGSLARREMTPYSDLDLILLHPPGAT---PDGVEDLWYPIWDAKKRLDYSVRTPQECAAMISADSTAALALLDLRF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 135 LNGPQELYQQLQLAIeqpdfwpssefyLAKrdeqfQRHEANNAFD-------------------LEPNIKTCPGGLRDIQ 195
Cdd:PRK00227 106 VAGDEQLTASTRAKI------------LEK-----WRRELNKNFDavvdtaiarwrrsgsvvamTRPDLKHGRGGLRDIE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 196 TVGWIAKRHFKttiveqlvqhgflsqeELDKLLSCQDFLWSMRFALHQTAKRPEDKLLFNHQHDVANAMGYSDEDQLAVE 275
Cdd:PRK00227 169 LIRALALGHLC----------------DAPPLDSQHQLLLDVRTLLHVHARRARDVLDPEFAVDIALDLGFVDRYHLSRE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 276 VMmkqyyQQIREVDELCEMLLQ-----LFKREFLGRI--KTLDICIMNEQYQRRghfIESTVDnlFNDKSqiitLFLNIA 348
Cdd:PRK00227 233 IA-----DAARAIDDALTAALAtargaLPRRTAFRNAvrRPLDVDVVDANGTIA---LSRTPD--LDDPA----LPLRVA 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 349 KDKEISGIYAPTLRQLRLaRENLTAPLCDDAQCRTAFMNIIKHPDGI-RALSMMHKHGILGSYMPAWQKISGQMQFDLFH 427
Cdd:PRK00227 299 AAAARTGLPVSESVWKRL-EECPELPEPWPASAAGDFFRLLSSPVNSrRVIKQMDRHGLWERIVPEWDRIRGLMPREPSH 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 428 AYTVDEHTHRLLKNidrfsqpkykdefplCSVLIHTLTKKGLLVLAAIFHDIGKGRGGDHSELGALDALEFGRLHALNEH 507
Cdd:PRK00227 378 IHTIDEHSLNTVAN---------------CALETVTVARPDLLLLGALYHDIGKGYPRPHEQVGAEMVARAARRMGLNLR 442
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1101461855 508 DTRLIAWLVENHLLMSVIAQRRDIHDPDVINSFASIVQ-DETRLAYLYCLTVADICATNNKLWN 570
Cdd:PRK00227 443 DRAVVQTLVAEHTTLARIAGRLDPTSEEAVDKLLDAVRyDLLTLNLLEVLTEADAEGTGPGVWT 506
|
|
| ACT_ACR-UUR-like_2 |
cd04899 |
C-terminal ACT domains of the bacterial signal-transducing uridylyltransferase ... |
782-851 |
6.12e-26 |
|
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: 101.38 E-value: 6.12e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 782 TLFELVALDMPGLLATVGDVFTKFKITLHNAKITTIGERVEDFFIITDKDENPLTQEQQNTLQQALVLAI 851
Cdd:cd04899 1 TVLELTALDRPGLLADVTRVLAELGLNIHSAKIATLGERAEDVFYVTDADGQPLDPERQEALRAALGEAL 70
|
|
| NT_GlnE_GlnD_like |
cd05401 |
Nucleotidyltransferase (NT) domain of Escherichia coli adenylyltransferase (GlnE), Escherichia ... |
5-151 |
1.29e-24 |
|
Nucleotidyltransferase (NT) domain of Escherichia coli adenylyltransferase (GlnE), Escherichia coli uridylyl transferase (GlnD), and similar proteins; Escherichia coli GlnD and -E participate in the Glutamine synthetase (GS)/Glutamate synthase (GOGAT) pathway for the assimilation of ammonium nitrogen. In nitrogen sufficiency, GlnE adenylates GS, reducing GS activity; when nitrogen is limiting, GlnE deadenylates GS-AMP, restoring GS activity. When nitrogen is limiting, GlnD uridylylates the nitrogen regulatory protein PII to PII-UTP, and in nitrogen sufficiency, it removes the modifying groups. The activity of Escherichia coli GlnE is modulated by PII-proteins. PII-UMP promotes GlnE deadenylation activity, and PII promotes GlnE adenylation activity. Escherichia coli GlnE has two separate NT domains. The N-terminal NT domain catalyzes the deadenylylation of GS, and the C-terminal NT domain the adenylylation reaction. The majority of proteins in this family contain a C-terminal NT domain which is associated with a cystathionine beta-synthase (CBS) domain pair and a CAP_ED (cAMP receptor protein effector ) domain. This family belongs to the Pol beta-like NT superfamily. In the majority of enzymes in this superfamily, two carboxylates, Dx[D/E], together with a third more distal carboxylate, coordinate two divalent metal cations involved in a two-metal ion mechanism of nucleotide addition. For the majority of proteins in this family, these carboxylate residues are conserved.
Pssm-ID: 143391 [Multi-domain] Cd Length: 172 Bit Score: 101.26 E-value: 1.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 5 KQANNEFSDWLNEQFERGGDIRELLHQRCQYVDDLLQQLWQHFELN------HTPISLIAVGGYGRGELHPHSDVDLLIL 78
Cdd:cd05401 1 RAKLRQLRRILRRDLLGGASIRAISRALSDLADALLRRALELALAElgkgppPVPFALLALGSYGRGELNPSSDQDLLLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 79 ------SLKTLTNEQTEKISQ------FITFLWDIKFDIGHSVRTLEETISIGKSDITV------ATNLMESRLLNGPQE 140
Cdd:cd05401 81 ydddgdEVAAYFEELAERLIKilseagGPYCLGDVMLRPPGWRRSLAEWLDAARDWLTEpgrlweRTALLDARPVAGDRA 160
|
170
....*....|.
gi 1101461855 141 LYQQLQLAIEQ 151
Cdd:cd05401 161 LAEELRRRIRE 171
|
|
| ACT_UUR-like_1 |
cd04900 |
ACT domain family, ACT_UUR-like_1, includes the first of two C-terminal ACT domains of the ... |
673-745 |
2.45e-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: 2.45e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1101461855 673 VSELFVYTQDMKNLFAKVMRVLGSKNVQINDAHVMATTGGWALDTFNISEHNGQPILDERRVKSIVQTLTKSL 745
Cdd:cd04900 1 GTEVFIYTPDRPGLFARIAGALDQLGLNILDARIFTTRDGYALDTFVVLDPDGEPIGERERLARIREALEDAL 73
|
|
| ACT_UUR-ACR-like |
cd04873 |
ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) ... |
782-851 |
1.35e-18 |
|
ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) enzyme, GlnD; This ACT domain family, ACT_UUR_ACR-like, includes the two C-terminal ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) enzyme, GlnD; including those enzymes similar to the GlnD found in enteric Escherichia coli and those found in photosynthetic, nitrogen-fixing bacterium Rhodospirillum rubrum. Also included in this CD are the four ACT domains of a novel protein composed almost entirely of ACT domain repeats (the ACR protein) and like proteins. These ACR proteins, found in Arabidopsis and Oryza, are proposed to function as novel regulatory or sensor proteins in plants. This CD also includes the first of the two ACT domains that comprise the Glycine Cleavage System Transcriptional Repressor (GcvR) protein and related domains, as well as, the N-terminal ACT domain of a yet characterized Arabidopsis/Oryza predicted tyrosine kinase. Members of this CD belong to the superfamily of ACT regulatory domains.
Pssm-ID: 153145 [Multi-domain] Cd Length: 70 Bit Score: 80.67 E-value: 1.35e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 782 TLFELVALDMPGLLATVGDVFTKFKITLHNAKITTIGERVEDFFIITDKDENPLTQEQQNTLQQALVLAI 851
Cdd:cd04873 1 TVVEVYAPDRPGLLADITRVLADLGLNIHDARISTTGERALDVFYVTDSDGRPLDPERIARLEEALEDAL 70
|
|
| ACT_UUR-ACR-like |
cd04873 |
ACT domains of the bacterial signal-transducing uridylyltransferase /uridylyl-removing (UUR) ... |
674-745 |
6.64e-14 |
|
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: 67.19 E-value: 6.64e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1101461855 674 SELFVYTQDMKNLFAKVMRVLGSKNVQINDAHVmATTGGWALDTFNISEHNGQPiLDERRVKSIVQTLTKSL 745
Cdd:cd04873 1 TVVEVYAPDRPGLLADITRVLADLGLNIHDARI-STTGERALDVFYVTDSDGRP-LDPERIARLEEALEDAL 70
|
|
| HD |
pfam01966 |
HD domain; HD domains are metal dependent phosphohydrolases. |
469-537 |
1.63e-05 |
|
HD domain; HD domains are metal dependent phosphohydrolases.
Pssm-ID: 460398 [Multi-domain] Cd Length: 110 Bit Score: 44.53 E-value: 1.63e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1101461855 469 LLVLAAIFHDIGKGRGGD----------HSELGALDALEFGRLHALNEhdtrlIAWLVENHLLMSVIAQRRDIHDPDVI 537
Cdd:pfam01966 26 LLLLAALLHDIGKGPFGDekpefeiflgHAVVGAEILRELEKRLGLED-----VLKLILEHHESWEGAGYPEEISLEAR 99
|
|
| ACT_ACR-UUR-like_2 |
cd04899 |
C-terminal ACT domains of the bacterial signal-transducing uridylyltransferase ... |
674-745 |
2.80e-05 |
|
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: 42.83 E-value: 2.80e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1101461855 674 SELFVYTQDMKNLFAKVMRVLGSKNVQINDAHVmATTGGWALDTFNISEHNGQPiLDERRVKSIVQTLTKSL 745
Cdd:cd04899 1 TVLELTALDRPGLLADVTRVLAELGLNIHSAKI-ATLGERAEDVFYVTDADGQP-LDPERQEALRAALGEAL 70
|
|
| NTP_transf_2 |
pfam01909 |
Nucleotidyltransferase domain; Members of this family belong to a large family of ... |
40-98 |
4.32e-05 |
|
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: 42.79 E-value: 4.32e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1101461855 40 LQQLWQHFELNHTPISLIAVGGYGRGELHPHSDVDLLILSLKTLTNEQTEKISQFITFL 98
Cdd:pfam01909 1 LRKLREILKELFPVAEVVLFGSYARGTALPGSDIDLLVVFPEPVEEERLLKLAKIIKEL 59
|
|
| HDc |
cd00077 |
Metal dependent phosphohydrolases with conserved 'HD' motif |
429-581 |
1.19e-04 |
|
Metal dependent phosphohydrolases with conserved 'HD' motif
Pssm-ID: 238032 [Multi-domain] Cd Length: 145 Bit Score: 43.10 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 429 YTVDEHTHRLLKNIDRfsqpkykdefpLCSVLIHTLTKKGLLVLAAIFHDIGKG------------RGGDHSELGALDAL 496
Cdd:cd00077 1 EHRFEHSLRVAQLARR-----------LAEELGLSEEDIELLRLAALLHDIGKPgtpdaiteeeseLEKDHAIVGAEILR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 497 EFgrlhaLNEHDTRLIAWLVENHLLMsvIAQRRDIHDPDVinsfasIVQDETRLAYLYCLTVADIC-ATNNKLWNNWKGS 575
Cdd:cd00077 70 EL-----LLEEVIKLIDELILAVDAS--HHERLDGLGYPD------GLKGEEITLEARIVKLADRLdALRRDSREKRRRI 136
|
....*.
gi 1101461855 576 LLRELY 581
Cdd:cd00077 137 AEEDLE 142
|
|
| NT_KNTase_like |
cd05403 |
Nucleotidyltransferase (NT) domain of Staphylococcus aureus kanamycin nucleotidyltransferase, ... |
34-105 |
3.59e-04 |
|
Nucleotidyltransferase (NT) domain of Staphylococcus aureus kanamycin nucleotidyltransferase, and similar proteins; S. aureus KNTase is a plasmid encoded enzyme which confers resistance to a wide range of aminoglycoside antibiotics which have a 4'- or 4''-hydroxyl group in the equatorial position, such as kanamycin A. This enzyme transfers a nucleoside monophosphate group from a nucleotide (ATP,GTP, or UTP) to the 4'-hydroxyl group of kanamycin A. This enzyme is a homodimer, having two NT active sites. The nucleotide and antibiotic binding sites of each active site include residues from each monomer. Included in this subgroup is Escherichia coli AadA5 which confers resistance to the antibiotic spectinomycin and is a putative aminoglycoside-3'-adenylyltransferase. It is part of the aadA5 cassette of a class 1 integron. This subgroup also includes Haemophilus influenzae HI0073 which forms a 2:2 heterotetramer with an unrelated protein HI0074. Structurally HI0074 is related to the substrate-binding domain of S. aureus KNTase. The genes encoding HI0073 and HI0074 form an operon. Little is known about the substrate specificity or function of two-component NTs. The characterized members of this subgroup may not be representive of the function of this subgroup. This subgroup belongs to the Pol beta-like NT superfamily. In the majority of enzymes in this superfamily, two carboxylates, Dx[D/E], together with a third more distal carboxylate, co-ordinate two divalent metal cations involved in a two-metal ion mechanism of nucleotide addition. These carboxylate residues are conserved in this subgroup.
Pssm-ID: 143393 Cd Length: 93 Bit Score: 40.48 E-value: 3.59e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1101461855 34 QYVDDLLQQLWQHFElnhTPISLIAVGGYGRGELHPHSDVDLLILSLKTLTNEQTEKISQFITFLWDIKFDI 105
Cdd:cd05403 2 EILEEILEILRELLG---GVEKVYLFGSYARGDARPDSDIDLLVIFDDPLDPLELARLLEELELLLGRPVDL 70
|
|
| MJ0604 |
COG1708 |
Predicted nucleotidyltransferase, MJ0604 family [General function prediction only]; |
34-114 |
3.71e-04 |
|
Predicted nucleotidyltransferase, MJ0604 family [General function prediction only];
Pssm-ID: 441314 Cd Length: 95 Bit Score: 40.40 E-value: 3.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 34 QYVDDLLQQLWQHFElnhtPISLIAVGGYGRGELHPHSDVDLLILSLK-TLTNEQTEKISQFITFLwDIKFDIghSVRTL 112
Cdd:COG1708 7 ELLEEIVEALRRGPE----VAAVYLFGSYARGDARPDSDIDLLVVVDDpPLPDERLELLADLLREL-GLPVDL--VVLTP 79
|
..
gi 1101461855 113 EE 114
Cdd:COG1708 80 AE 81
|
|
| ACT |
pfam01842 |
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ... |
782-835 |
4.97e-04 |
|
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: 39.21 E-value: 4.97e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1101461855 782 TLFELVALDMPGLLATVGDVFTKFKITLHNAKITTIGERVEDFFIITDKDENPL 835
Cdd:pfam01842 1 TVLEVLVPDRPGLLARVLGALADRGINITSIEQGTSEDKGGIVFVVIVVDEEDL 54
|
|
| RnaY |
COG1418 |
HD superfamily phosphodieaserase, includes HD domain of RNase Y [Translation, ribosomal ... |
469-519 |
8.12e-04 |
|
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: 41.42 E-value: 8.12e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1101461855 469 LLVLAAIFHDIGK----GRGGDHSELGALDALEFGRLHALNEHDTRLIAWLVENH 519
Cdd:COG1418 43 VAKRAALLHDIGKakdhEVEGSHAEIGAELARKYLESLGFPEEEIEAVVHAIEAH 97
|
|
| ACT_ACR-like_2 |
cd04927 |
Second ACT domain, of a novel type of ACT domain-containing protein which is composed almost ... |
783-851 |
2.01e-03 |
|
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); 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 (ACR1-8 in Arabidopsis and OsARC1-9 in Oryza) have been described, however, the ACR-like sequences in this CD are distinct from those characterized. This CD includes the Oryza sativa ACR-like protein (Os05g0113000) encoded on chromosome 5 and the Arabidopsis thaliana predicted gene product, At2g39570. Members of this CD belong to the superfamily of ACT regulatory domains.
Pssm-ID: 153199 Cd Length: 76 Bit Score: 37.83 E-value: 2.01e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 783 LFELVALDMPGLLATVGDVFTKFKITLHNAKI-TTIGERVEDFFIITDKDENPLTQEQQNTLQQALVLAI 851
Cdd:cd04927 2 LLKLFCSDRKGLLHDVTEVLYELELTIERVKVsTTPDGRVLDLFFITDARELLHTKKRREETYDYLRAVL 71
|
|
| HDc |
smart00471 |
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ... |
464-573 |
2.34e-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: 38.82 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101461855 464 LTKKGLLVLAAIFHDIGKGRGGD-----------HSELGALDALEFGrlhaLNEHDTRLIAWLVENHLLMSVIAQRRDIh 532
Cdd:smart00471 25 LLDIELLLLAALLHDIGKPGTPDsflvktsvledHHFIGAEILLEEE----EPRILEEILRTAILSHHERPDGLRGEPI- 99
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1101461855 533 dpdvinsfasivqdetrLAYLYCLTVADICATNNKLWNNWK 573
Cdd:smart00471 100 -----------------TLEARIVKVADRLDALRADRRYRR 123
|
|
| MJ0435 |
COG1669 |
Predicted nucleotidyltransferase MJ0435 [General function prediction only]; |
34-105 |
4.36e-03 |
|
Predicted nucleotidyltransferase MJ0435 [General function prediction only];
Pssm-ID: 441275 Cd Length: 96 Bit Score: 37.20 E-value: 4.36e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1101461855 34 QYVDDLLQQLWQHFelnhtPISLIAV-GGYGRGELHPHSDVDLLILSLKTLTNEQTEKISQFITFLWDIKFDI 105
Cdd:COG1669 8 EILREVIEELAERY-----GVSRLGLfGSVARGEAREDSDIDLLVEFDEPTSLFDLFELEEELEELLGRKVDL 75
|
|
| ACT |
cd02116 |
ACT domains are commonly involved in specifically binding an amino acid or other small ligand ... |
784-832 |
5.25e-03 |
|
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: 36.12 E-value: 5.25e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1101461855 784 FELVALDMPGLLATVGDVFTKFKITLHNAKITTIG-ERVEDFFIITDKDE 832
Cdd:cd02116 1 LTVSGPDRPGLLAKVLSVLAEAGINITSIEQRTSGdGGEADIFIVVDGDG 50
|
|
| ACT_ACR_4 |
cd04926 |
C-terminal ACT domain, of a novel type of ACT domain-containing protein which is composed ... |
785-838 |
7.81e-03 |
|
C-terminal ACT domain, of a novel type of ACT domain-containing protein which is composed almost entirely of four ACT domain repeats (the "ACR" protein); This CD includes the C-terminal ACT domain, of a novel type of ACT domain-containing protein which is composed almost entirely of four ACT domain repeats (the "ACR" protein). ACR proteins, found only in Arabidopsis and Oryza, as yet, are proposed to function as novel regulatory or sensor proteins in plants. Nine ACR gene products have been described (ACR1-8 in Arabidopsis and OsARC1-9 in Oryza) and are represented in this CD. Members of this CD belong to the superfamily of ACT regulatory domains.
Pssm-ID: 153198 Cd Length: 72 Bit Score: 35.79 E-value: 7.81e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1101461855 785 ELVALDMPGLLATVGDVFTKFKITLHNAKITTIGERVEDFFIITDKDENPLTQE 838
Cdd:cd04926 5 ELRTEDRVGLLSDVTRVFRENGLTVTRAEISTQGDMAVNVFYVTDANGNPVDPK 58
|
|
| |
