|
Name |
Accession |
Description |
Interval |
E-value |
| ATPS |
cd00517 |
ATP-sulfurylase; ATP-sulfurylase (ATPS), also known as sulfate adenylate transferase, ... |
254-617 |
0e+00 |
|
ATP-sulfurylase; ATP-sulfurylase (ATPS), also known as sulfate adenylate transferase, catalyzes the transfer of an adenylyl group from ATP to sulfate, forming adenosine 5'-phosphosulfate (APS). This reaction is generally accompanied by a further reaction, catalyzed by APS kinase, in which APS is phosphorylated to yield 3'-phospho-APS (PAPS). In some organisms the APS kinase is a separate protein, while in others it is incorporated with ATP sulfurylase in a bifunctional enzyme that catalyzes both reactions. In bifunctional proteins, the domain that performs the kinase activity can be attached at the N-terminal end of the sulfurylase unit or at the C-terminal end, depending on the organism. While the reaction is ubiquitous among organisms, the physiological role of the reaction varies. In some organisms it is used to generate APS from sulfate and ATP, while in others it proceeds in the opposite direction to generate ATP from APS and pyrophosphate. ATP sulfurylase can be a monomer, a homodimer, or a homo-oligomer, depending on the organism. ATPS belongs to a large superfamily of nucleotidyltransferases that includes pantothenate synthetase (PanC), phosphopantetheine adenylyltransferase (PPAT), and the amino-acyl tRNA synthetases. The enzymes of this family are structurally similar and share a dinucleotide-binding domain.
Pssm-ID: 173895 [Multi-domain] Cd Length: 353 Bit Score: 536.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259126 254 LPALKINKVDMQWVQVLAEGWATPLNGFMREREYLQCLHFDCLLDGgvINLSVPIVLTATQEDKERLDGCTAFALVYEGR 333
Cdd:cd00517 1 LPSVELSERDLCDLEMLAEGGFSPLTGFMTEADYLSVLEEMRLLDG--TLWPIPIVLDVSEEDAKRLKEGERVALRYPGQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259126 334 RVAILRNPEFFEHRKEERCARQWGTTCRSHPYIKMILEQGDWLIGGDLQVLDRIYWNDgLDQYRLTPAELKQKFKDMNAD 413
Cdd:cd00517 79 PLAILTVEEIYEPDKEEEAARVFGTTDPHHPGVKKVMEQGDWLVGGPIEVLELPPFPD-FDQYRLTPAELRALFKERGWR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259126 414 AVFAFQLRNPVHNGHALLMQDTHKQLLergyrRPVLLLHPLGGWTKDDDVPLMWRMKQHAAVLEEGILnPETTVVAIFPS 493
Cdd:cd00517 158 RVVAFQTRNPMHRAHEELMKRAAEKLL-----NDGLLLHPLVGWTKPGDVPDEVRMRAYEALLEEYYL-PERTVLAILPL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259126 494 PMMYAGPTEVQWHCRARMVAGANFYIVGRDPAGMPHPETGKDLYEPTHGAKVLTMApglITLEIVPFRVAAYNKKKKRMD 573
Cdd:cd00517 232 PMRYAGPREALWHAIIRKNYGATHFIVGRDHAGVGHPGDYYGPYDAQEIFKKLAPE---LGIEPVPFREAAYCPKCDGMA 308
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2047259126 574 YYD-SDHHEDFEFISGTRMRKLAREGQKPPEGFMAPKAWTVLVEY 617
Cdd:cd00517 309 SEDtCPHGEDFLNISGTKLRKMLREGEKPPEWFMRPEVAKVLREY 353
|
|
| sopT |
TIGR00339 |
ATP sulphurylase; This enzyme forms adenosine 5'-phosphosulfate (APS) from ATP and free ... |
233-616 |
1.56e-132 |
|
ATP sulphurylase; This enzyme forms adenosine 5'-phosphosulfate (APS) from ATP and free sulfate, the first step in the formation of the activated sulfate donor 3'-phosphoadenylylsulfate (PAPS). In some cases, it is found in a bifunctional protein in which the other domain, APS kinase, catalyzes the second and final step, the phosphorylation of APS to PAPS; the combined ATP sulfurylase/APS kinase may be called PAPS synthase. Members of this family also include the dissimilatory sulfate adenylyltransferase (sat) of the sulfate reducer Archaeoglobus fulgidus. [Central intermediary metabolism, Sulfur metabolism]
Pssm-ID: 273023 Cd Length: 383 Bit Score: 393.67 E-value: 1.56e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259126 233 EVKELYV--PENKlHLAKTDAEALPALKINKVDMQWVQVLAEGWATPLNGFMREREYLQCLHFDCLLDGgvINLSVPIVL 310
Cdd:TIGR00339 5 KLVELVVrdPDEE-HKLLAEAESLPSITLSDRQLCDLELLGNGAFSPLEGFMNEADYDSVVESMRLSDG--VLFSVPITL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259126 311 TATQEDKERLDGCTAFALVYE-GRRVAILRNPEFFEHRKEERCARQWGTTCRSHPYIKMILEQGDWLIGGDLQVLDRIYW 389
Cdd:TIGR00339 82 DIDDEDADDIKLGDRIALTDPkGQPLAILTIEEVYKPNKEKEAKKVFGTTDPEHPGVVYLNTAGNYYIGGPIEVINLPKF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259126 390 nDGLDQYRLTPAELKQKFKDMNADAVFAFQLRNPVHNGHALLMQDThkqlLERGyRRPVLLLHPLGGWTKDDDVPLMWRM 469
Cdd:TIGR00339 162 -YDFPRFRFTPAELREEFKERGWDTVVAFQTRNPMHRAHEELTKRA----AERL-PNAGVLVHPLVGLTKPGDIPAEVRM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259126 470 KQHAaVLEEGILNPETTVVAIFPSPMMYAGPTEVQWHCRARMVAGANFYIVGRDPAGMPHPETGKDLYEPTHGAKVLTMA 549
Cdd:TIGR00339 236 RAYE-VLKEGYPNPERTVVSFLPLAMRYAGPREAIWHAIIRKNYGATHFIVGRDHAGPGSNSKGQDFYGPYDAQELFEKY 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2047259126 550 PGLITLEIVPFRVAAYNKKKKRMDYYD-SDHH-EDFEFISGTRMRKLAREGQKPPEGFMAPKAWTVLVE 616
Cdd:TIGR00339 315 KAELGIKIVPFRHVAYCPDEDEYAPADqAGHTnLRTLNISGTKLRGMLRNGVFPPEWFSRPEVVKILRE 383
|
|
| CysC |
COG0529 |
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ... |
33-227 |
3.36e-109 |
|
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; Adenylylsulfate kinase or related kinase is part of the Pathway/BioSystem: Cysteine biosynthesis
Pssm-ID: 440295 [Multi-domain] Cd Length: 189 Bit Score: 326.28 E-value: 3.36e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259126 33 HHVSRNKRGQvvgtRGGFRGCTVWLTGLSGAGKTTVSMALEEYLVCHGIPCYTLDGDNIRQGLNKNLGFSPEDREENVRR 112
Cdd:COG0529 1 SAVTREERAA----LKGQKGFVVWFTGLSGSGKSTLANALERRLFERGRHVYLLDGDNVRHGLNKDLGFSKEDRDENIRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259126 113 IAEVAKLFADAGLVCITSFISPYTQDRNNARQIHEGAslPFFEVFVDAPLHVCEQRDVKGLYKKARAGEIKGFTGIDSEY 192
Cdd:COG0529 77 IGEVAKLLADAGLIVLVAFISPYRADREEARELIGEG--EFIEVYVDTPLEVCEARDPKGLYAKARAGEIKNFTGIDDPY 154
|
170 180 190
....*....|....*....|....*....|....*
gi 2047259126 193 EKPEAPELVLKTDSCDVNDCVQQVVELLQERDIVP 227
Cdd:COG0529 155 EAPENPELVLDTDKESVEESVEKILAYLEERGYIS 189
|
|
| APS_kinase |
pfam01583 |
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3 ... |
51-205 |
3.90e-103 |
|
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3'-phosphoadenylylsulfate. This domain contains an ATP binding P-loop motif.
Pssm-ID: 396247 [Multi-domain] Cd Length: 154 Bit Score: 309.25 E-value: 3.90e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259126 51 RGCTVWLTGLSGAGKTTVSMALEEYLVCHGIPCYTLDGDNIRQGLNKNLGFSPEDREENVRRIAEVAKLFADAGLVCITS 130
Cdd:pfam01583 1 RGCTIWLTGLSGAGKSTIANALERKLFEQGRSVYVLDGDNVRHGLNKDLGFSEEDRTENIRRIGEVAKLFADAGLIVITA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2047259126 131 FISPYTQDRNNARQIHEGAslPFFEVFVDAPLHVCEQRDVKGLYKKARAGEIKGFTGIDSEYEKPEAPELVLKTD 205
Cdd:pfam01583 81 FISPYREDREQARELHEEG--KFIEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDSPYEAPENPELVLDTD 153
|
|
| APSK |
cd02027 |
Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5 ... |
54-204 |
1.75e-102 |
|
Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5'-phosphosulfate to form 3'-phosphoadenosine 5'-phosphosulfate (PAPS). The end-product PAPS is a biologically "activated" sulfate form important for the assimilation of inorganic sulfate.
Pssm-ID: 238985 [Multi-domain] Cd Length: 149 Bit Score: 307.48 E-value: 1.75e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259126 54 TVWLTGLSGAGKTTVSMALEEYLVCHGIPCYTLDGDNIRQGLNKNLGFSPEDREENVRRIAEVAKLFADAGLVCITSFIS 133
Cdd:cd02027 1 VIWLTGLSGSGKSTIARALEEKLFQRGRPVYVLDGDNVRHGLNKDLGFSREDREENIRRIAEVAKLLADAGLIVIAAFIS 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2047259126 134 PYTQDRNNARQIHEGasLPFFEVFVDAPLHVCEQRDVKGLYKKARAGEIKGFTGIDSEYEKPEAPELVLKT 204
Cdd:cd02027 81 PYREDREAARKIIGG--GDFLEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDDPYEAPENPDLVLDT 149
|
|
| ATP-sulfurylase |
pfam01747 |
ATP-sulfurylase; This domain is the catalytic domain of ATP-sulfurylase or sulfate ... |
394-617 |
8.89e-96 |
|
ATP-sulfurylase; This domain is the catalytic domain of ATP-sulfurylase or sulfate adenylyltransferase EC:2.7.7.4 some of which are part of a bifunctional polypeptide chain associated with adenosyl phosphosulphate (APS) kinase pfam01583. Both enzymes are required for PAPS (phosphoadenosine-phosphosulfate) synthesis from inorganic sulphate. ATP sulfurylase catalyzes the synthesis of adenosine-phosphosulfate APS from ATP and inorganic sulphate.
Pssm-ID: 460310 Cd Length: 213 Bit Score: 292.52 E-value: 8.89e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259126 394 DQYRLTPAELKQKFKDMNADAVFAFQLRNPVHNGHALLMQDTHKQLlERGYrrpvLLLHPLGGWTKDDDVPLMWRMKQHA 473
Cdd:pfam01747 1 DEYRLTPAETRALFKEKGWRTVVAFQTRNPLHRAHEELMKRALEEL-EADG----LLLHPLVGPTKPGDVPAEVRVRCYE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259126 474 AVLEEgILNPETTVVAIFPSPMMYAGPTEVQWHCRARMVAGANFYIVGRDPAGMPHpetgkdLYEPTHGAKVLTMAPGLI 553
Cdd:pfam01747 76 ALLEN-YLPPDRVVLALLPLAMRYAGPREALLHAIIRKNYGCTHFIVGRDHAGVGD------FYGPYDAQEIFDEYPGEL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2047259126 554 TLEIVPFRVAAYNKKKKRMDYYDSDHH-EDFEFISGTRMRKLAREGQKPPEGFMAPKAWTVLVEY 617
Cdd:pfam01747 149 GIEPVPFREAVYCKKCGEMASTKCPHGgEDRLFISGTKVRELLREGEEPPEWFSRPEVAKVLREY 213
|
|
| PRK03846 |
PRK03846 |
adenylylsulfate kinase; Provisional |
26-226 |
9.92e-92 |
|
adenylylsulfate kinase; Provisional
Pssm-ID: 179661 Cd Length: 198 Bit Score: 281.44 E-value: 9.92e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259126 26 TNVTYQAHHVSRNKRGQvvgtRGGFRGCTVWLTGLSGAGKTTVSMALEEYLVCHGIPCYTLDGDNIRQGLNKNLGFSPED 105
Cdd:PRK03846 2 ENIVWHQHPVTKAQREQ----LHGHKGVVLWFTGLSGSGKSTVAGALEEALHELGVSTYLLDGDNVRHGLCSDLGFSDAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259126 106 REENVRRIAEVAKLFADAGLVCITSFISPYTQDRNNARQIhegasLP---FFEVFVDAPLHVCEQRDVKGLYKKARAGEI 182
Cdd:PRK03846 78 RKENIRRVGEVAKLMVDAGLVVLTAFISPHRAERQMVRER-----LGegeFIEVFVDTPLAICEARDPKGLYKKARAGEI 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2047259126 183 KGFTGIDSEYEKPEAPELVLKTDSCDVNDCVQQVVELLQERDIV 226
Cdd:PRK03846 153 RNFTGIDSVYEAPESPEIHLDTGEQLVTNLVEQLLDYLRQRDII 196
|
|
| apsK |
TIGR00455 |
adenylyl-sulfate kinase; This protein, adenylylsulfate kinase, is often found as a fusion ... |
34-220 |
5.25e-85 |
|
adenylyl-sulfate kinase; This protein, adenylylsulfate kinase, is often found as a fusion protein with sulfate adenylyltransferase. Important residue (active site in E.coli) is residue 100 of the seed alignment. [Central intermediary metabolism, Sulfur metabolism]
Pssm-ID: 129547 Cd Length: 184 Bit Score: 263.56 E-value: 5.25e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259126 34 HVSRNKRGQVVGTRGgfrgCTVWLTGLSGAGKTTVSMALEEYLVCHGIPCYTLDGDNIRQGLNKNLGFSPEDREENVRRI 113
Cdd:TIGR00455 4 AITKDERQALNGHRG----VVIWLTGLSGSGKSTIANALEKKLESKGYRVYVLDGDNVRHGLNKDLGFSEEDRKENIRRI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259126 114 AEVAKLFADAGLVCITSFISPYTQDRNNARQIHEGASlpFFEVFVDAPLHVCEQRDVKGLYKKARAGEIKGFTGIDSEYE 193
Cdd:TIGR00455 80 GEVAKLFVRNGIIVITSFISPYRADRQMVRELIEKGE--FIEVFVDCPLEVCEQRDPKGLYKKARNGEIKGFTGIDSPYE 157
|
170 180
....*....|....*....|....*..
gi 2047259126 194 KPEAPELVLKTDSCDVNDCVQQVVELL 220
Cdd:TIGR00455 158 APENPEVVLDTDQNDREECVGQIIEKL 184
|
|
| MET3 |
COG2046 |
ATP sulfurylase (sulfate adenylyltransferase) [Inorganic ion transport and metabolism]; ATP ... |
233-623 |
2.47e-71 |
|
ATP sulfurylase (sulfate adenylyltransferase) [Inorganic ion transport and metabolism]; ATP sulfurylase (sulfate adenylyltransferase) is part of the Pathway/BioSystem: Cysteine biosynthesis
Pssm-ID: 441649 Cd Length: 388 Bit Score: 235.04 E-value: 2.47e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259126 233 EVKELYVPENKLHLAKTDAEALPALKINKVDMQWVQVLAEGWATPLNGFMREREYLQCLHFDCLLDGGVinLSVPIVLTA 312
Cdd:COG2046 11 KLVNRVVPGEEREALLEEAKGLPSIELSSRALSDLEMIAIGGFSPLTGFMNKADYESVVENMRLADGLL--WPIPITLDV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259126 313 TQEDKERLDGCTAFALV-YEGRRVAILRNPEFFEHRKEERCARQWGTTCRSHPYIKMILEQGDWLIGGDLQVLDRIYWND 391
Cdd:COG2046 89 SEEDAAGLKEGDEVALRdEEGEPLAVLEVEEIYEYDKEEEAEKVYGTTDPAHPGVAKLYERGDVYLGGPITLLNRPKHPD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259126 392 gLDQYRLTPAELKQKFKDMNADAVFAFQLRNPVHNGHALLMqdthKQLLERGYrrpVLLLHPLGGWTKDDDVPLMWRMKQ 471
Cdd:COG2046 169 -FPDYRLTPAETRALFEEKGWKTVVAFQTRNPMHRAHEYLQ----KRALETVD---GLLIHPLVGETKPGDIPAEVRVRC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259126 472 HAAVLEEGIlNPETTVVAIFPSPMMYAGPTEVQWH--CRARMvaGANFYIVGRDPAGMPhpetgkDLYEPtHGAKVL--T 547
Cdd:COG2046 241 YEALLENYY-PKDRVLLSGLPLAMRYAGPREALLHaiIRKNY--GCTHFIVGRDHAGVG------DYYGP-YDAQEIfdE 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2047259126 548 MAPGLITLEIVPFRVAAYNKKKKRMDYYDSDHH--EDFEFISGTRMRKLAREGQKPPEGFMAPKAWTVLVEYYKSLEK 623
Cdd:COG2046 311 FPPGELGIEPLKFEEAFYCKKCGGMATSKTCPHdkEDRVSLSGTKVREMLREGEEPPPEFSRPEVAEILRKYYQPFGE 388
|
|
| sat |
PRK04149 |
sulfate adenylyltransferase; Reviewed |
233-622 |
2.44e-61 |
|
sulfate adenylyltransferase; Reviewed
Pssm-ID: 235227 Cd Length: 391 Bit Score: 208.95 E-value: 2.44e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259126 233 EVKELYVPENKLHLAKTDAEALPALKINKVDMQWVQVLAEGWATPLNGFMREREYLQCLHFDCLLDGGVinLSVPIVLTA 312
Cdd:PRK04149 10 ELVNRVVEGRDREEILEEAESLPRIELDERAASDLEMIAIGGFSPLTGFMGREDYDSVVEEMRLANGLV--WSIPITLDV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259126 313 TQEDKERLDGCTAFALVYEGRRVAILRNPEFFEHRKEERCARQWGTTCRSHPYIKMILEQGDWLIGGDLQVLDRIYwNDG 392
Cdd:PRK04149 88 SEEDAASLKEGDEVALVYKGEPYGVLEVEEIYTYDKKKEAEKVYKTTDEKHPGVKKLYEQGDVYLAGPVTLLNRKF-HEP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259126 393 LDQYRLTPAELKQKFKDMNADAVFAFQLRNPVHNGHALLMqdthKQLLE--RGyrrpvLLLHPLGGWTKDDDVPLMWRMK 470
Cdd:PRK04149 167 FPRFWLTPAETRELFEEKGWKTVVAFQTRNPPHRAHEYLQ----KCALEivDG-----LLLNPLVGETKSGDIPAEVRME 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259126 471 QHAAVLeEGILNPETTVVAIFPSPMMYAGPTEVQWHCRARMVAGANFYIVGRDPAGmphpeTGkDLYEP-------THGA 543
Cdd:PRK04149 238 AYEALL-KNYYPKDRVLLSVTPAAMRYAGPREAIFHAIVRKNYGCTHFIVGRDHAG-----VG-DYYGPydaqeifDEFT 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259126 544 KvltmaPGLITlEIVPFRVAAYNKKKKRMDYY-DSDH-HEDFEFISGTRMRKLAREGQKPPEGFMAPKAWTVLVEYYKSL 621
Cdd:PRK04149 311 E-----EELGI-TPLKFEEAFYCPKCGGMASEkTCPHgKEDRVHLSGTKVREMLREGEKPPPEFSRPEVAEVLIKGLKKY 384
|
.
gi 2047259126 622 E 622
Cdd:PRK04149 385 G 385
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
57-123 |
3.35e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 41.20 E-value: 3.35e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2047259126 57 LTGLSGAGKTTVSMALEEYLVCHGIPCYTLDGDNIRQG-LNKNLGFSPEDREENVRRIAEVAKLFADA 123
Cdd:smart00382 7 IVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEvLDQLLLIIVGGKKASGSGELRLRLALALA 74
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ATPS |
cd00517 |
ATP-sulfurylase; ATP-sulfurylase (ATPS), also known as sulfate adenylate transferase, ... |
254-617 |
0e+00 |
|
ATP-sulfurylase; ATP-sulfurylase (ATPS), also known as sulfate adenylate transferase, catalyzes the transfer of an adenylyl group from ATP to sulfate, forming adenosine 5'-phosphosulfate (APS). This reaction is generally accompanied by a further reaction, catalyzed by APS kinase, in which APS is phosphorylated to yield 3'-phospho-APS (PAPS). In some organisms the APS kinase is a separate protein, while in others it is incorporated with ATP sulfurylase in a bifunctional enzyme that catalyzes both reactions. In bifunctional proteins, the domain that performs the kinase activity can be attached at the N-terminal end of the sulfurylase unit or at the C-terminal end, depending on the organism. While the reaction is ubiquitous among organisms, the physiological role of the reaction varies. In some organisms it is used to generate APS from sulfate and ATP, while in others it proceeds in the opposite direction to generate ATP from APS and pyrophosphate. ATP sulfurylase can be a monomer, a homodimer, or a homo-oligomer, depending on the organism. ATPS belongs to a large superfamily of nucleotidyltransferases that includes pantothenate synthetase (PanC), phosphopantetheine adenylyltransferase (PPAT), and the amino-acyl tRNA synthetases. The enzymes of this family are structurally similar and share a dinucleotide-binding domain.
Pssm-ID: 173895 [Multi-domain] Cd Length: 353 Bit Score: 536.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259126 254 LPALKINKVDMQWVQVLAEGWATPLNGFMREREYLQCLHFDCLLDGgvINLSVPIVLTATQEDKERLDGCTAFALVYEGR 333
Cdd:cd00517 1 LPSVELSERDLCDLEMLAEGGFSPLTGFMTEADYLSVLEEMRLLDG--TLWPIPIVLDVSEEDAKRLKEGERVALRYPGQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259126 334 RVAILRNPEFFEHRKEERCARQWGTTCRSHPYIKMILEQGDWLIGGDLQVLDRIYWNDgLDQYRLTPAELKQKFKDMNAD 413
Cdd:cd00517 79 PLAILTVEEIYEPDKEEEAARVFGTTDPHHPGVKKVMEQGDWLVGGPIEVLELPPFPD-FDQYRLTPAELRALFKERGWR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259126 414 AVFAFQLRNPVHNGHALLMQDTHKQLLergyrRPVLLLHPLGGWTKDDDVPLMWRMKQHAAVLEEGILnPETTVVAIFPS 493
Cdd:cd00517 158 RVVAFQTRNPMHRAHEELMKRAAEKLL-----NDGLLLHPLVGWTKPGDVPDEVRMRAYEALLEEYYL-PERTVLAILPL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259126 494 PMMYAGPTEVQWHCRARMVAGANFYIVGRDPAGMPHPETGKDLYEPTHGAKVLTMApglITLEIVPFRVAAYNKKKKRMD 573
Cdd:cd00517 232 PMRYAGPREALWHAIIRKNYGATHFIVGRDHAGVGHPGDYYGPYDAQEIFKKLAPE---LGIEPVPFREAAYCPKCDGMA 308
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2047259126 574 YYD-SDHHEDFEFISGTRMRKLAREGQKPPEGFMAPKAWTVLVEY 617
Cdd:cd00517 309 SEDtCPHGEDFLNISGTKLRKMLREGEKPPEWFMRPEVAKVLREY 353
|
|
| sopT |
TIGR00339 |
ATP sulphurylase; This enzyme forms adenosine 5'-phosphosulfate (APS) from ATP and free ... |
233-616 |
1.56e-132 |
|
ATP sulphurylase; This enzyme forms adenosine 5'-phosphosulfate (APS) from ATP and free sulfate, the first step in the formation of the activated sulfate donor 3'-phosphoadenylylsulfate (PAPS). In some cases, it is found in a bifunctional protein in which the other domain, APS kinase, catalyzes the second and final step, the phosphorylation of APS to PAPS; the combined ATP sulfurylase/APS kinase may be called PAPS synthase. Members of this family also include the dissimilatory sulfate adenylyltransferase (sat) of the sulfate reducer Archaeoglobus fulgidus. [Central intermediary metabolism, Sulfur metabolism]
Pssm-ID: 273023 Cd Length: 383 Bit Score: 393.67 E-value: 1.56e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259126 233 EVKELYV--PENKlHLAKTDAEALPALKINKVDMQWVQVLAEGWATPLNGFMREREYLQCLHFDCLLDGgvINLSVPIVL 310
Cdd:TIGR00339 5 KLVELVVrdPDEE-HKLLAEAESLPSITLSDRQLCDLELLGNGAFSPLEGFMNEADYDSVVESMRLSDG--VLFSVPITL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259126 311 TATQEDKERLDGCTAFALVYE-GRRVAILRNPEFFEHRKEERCARQWGTTCRSHPYIKMILEQGDWLIGGDLQVLDRIYW 389
Cdd:TIGR00339 82 DIDDEDADDIKLGDRIALTDPkGQPLAILTIEEVYKPNKEKEAKKVFGTTDPEHPGVVYLNTAGNYYIGGPIEVINLPKF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259126 390 nDGLDQYRLTPAELKQKFKDMNADAVFAFQLRNPVHNGHALLMQDThkqlLERGyRRPVLLLHPLGGWTKDDDVPLMWRM 469
Cdd:TIGR00339 162 -YDFPRFRFTPAELREEFKERGWDTVVAFQTRNPMHRAHEELTKRA----AERL-PNAGVLVHPLVGLTKPGDIPAEVRM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259126 470 KQHAaVLEEGILNPETTVVAIFPSPMMYAGPTEVQWHCRARMVAGANFYIVGRDPAGMPHPETGKDLYEPTHGAKVLTMA 549
Cdd:TIGR00339 236 RAYE-VLKEGYPNPERTVVSFLPLAMRYAGPREAIWHAIIRKNYGATHFIVGRDHAGPGSNSKGQDFYGPYDAQELFEKY 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2047259126 550 PGLITLEIVPFRVAAYNKKKKRMDYYD-SDHH-EDFEFISGTRMRKLAREGQKPPEGFMAPKAWTVLVE 616
Cdd:TIGR00339 315 KAELGIKIVPFRHVAYCPDEDEYAPADqAGHTnLRTLNISGTKLRGMLRNGVFPPEWFSRPEVVKILRE 383
|
|
| CysC |
COG0529 |
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ... |
33-227 |
3.36e-109 |
|
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; Adenylylsulfate kinase or related kinase is part of the Pathway/BioSystem: Cysteine biosynthesis
Pssm-ID: 440295 [Multi-domain] Cd Length: 189 Bit Score: 326.28 E-value: 3.36e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259126 33 HHVSRNKRGQvvgtRGGFRGCTVWLTGLSGAGKTTVSMALEEYLVCHGIPCYTLDGDNIRQGLNKNLGFSPEDREENVRR 112
Cdd:COG0529 1 SAVTREERAA----LKGQKGFVVWFTGLSGSGKSTLANALERRLFERGRHVYLLDGDNVRHGLNKDLGFSKEDRDENIRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259126 113 IAEVAKLFADAGLVCITSFISPYTQDRNNARQIHEGAslPFFEVFVDAPLHVCEQRDVKGLYKKARAGEIKGFTGIDSEY 192
Cdd:COG0529 77 IGEVAKLLADAGLIVLVAFISPYRADREEARELIGEG--EFIEVYVDTPLEVCEARDPKGLYAKARAGEIKNFTGIDDPY 154
|
170 180 190
....*....|....*....|....*....|....*
gi 2047259126 193 EKPEAPELVLKTDSCDVNDCVQQVVELLQERDIVP 227
Cdd:COG0529 155 EAPENPELVLDTDKESVEESVEKILAYLEERGYIS 189
|
|
| APS_kinase |
pfam01583 |
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3 ... |
51-205 |
3.90e-103 |
|
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3'-phosphoadenylylsulfate. This domain contains an ATP binding P-loop motif.
Pssm-ID: 396247 [Multi-domain] Cd Length: 154 Bit Score: 309.25 E-value: 3.90e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259126 51 RGCTVWLTGLSGAGKTTVSMALEEYLVCHGIPCYTLDGDNIRQGLNKNLGFSPEDREENVRRIAEVAKLFADAGLVCITS 130
Cdd:pfam01583 1 RGCTIWLTGLSGAGKSTIANALERKLFEQGRSVYVLDGDNVRHGLNKDLGFSEEDRTENIRRIGEVAKLFADAGLIVITA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2047259126 131 FISPYTQDRNNARQIHEGAslPFFEVFVDAPLHVCEQRDVKGLYKKARAGEIKGFTGIDSEYEKPEAPELVLKTD 205
Cdd:pfam01583 81 FISPYREDREQARELHEEG--KFIEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDSPYEAPENPELVLDTD 153
|
|
| APSK |
cd02027 |
Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5 ... |
54-204 |
1.75e-102 |
|
Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5'-phosphosulfate to form 3'-phosphoadenosine 5'-phosphosulfate (PAPS). The end-product PAPS is a biologically "activated" sulfate form important for the assimilation of inorganic sulfate.
Pssm-ID: 238985 [Multi-domain] Cd Length: 149 Bit Score: 307.48 E-value: 1.75e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259126 54 TVWLTGLSGAGKTTVSMALEEYLVCHGIPCYTLDGDNIRQGLNKNLGFSPEDREENVRRIAEVAKLFADAGLVCITSFIS 133
Cdd:cd02027 1 VIWLTGLSGSGKSTIARALEEKLFQRGRPVYVLDGDNVRHGLNKDLGFSREDREENIRRIAEVAKLLADAGLIVIAAFIS 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2047259126 134 PYTQDRNNARQIHEGasLPFFEVFVDAPLHVCEQRDVKGLYKKARAGEIKGFTGIDSEYEKPEAPELVLKT 204
Cdd:cd02027 81 PYREDREAARKIIGG--GDFLEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDDPYEAPENPDLVLDT 149
|
|
| ATP-sulfurylase |
pfam01747 |
ATP-sulfurylase; This domain is the catalytic domain of ATP-sulfurylase or sulfate ... |
394-617 |
8.89e-96 |
|
ATP-sulfurylase; This domain is the catalytic domain of ATP-sulfurylase or sulfate adenylyltransferase EC:2.7.7.4 some of which are part of a bifunctional polypeptide chain associated with adenosyl phosphosulphate (APS) kinase pfam01583. Both enzymes are required for PAPS (phosphoadenosine-phosphosulfate) synthesis from inorganic sulphate. ATP sulfurylase catalyzes the synthesis of adenosine-phosphosulfate APS from ATP and inorganic sulphate.
Pssm-ID: 460310 Cd Length: 213 Bit Score: 292.52 E-value: 8.89e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259126 394 DQYRLTPAELKQKFKDMNADAVFAFQLRNPVHNGHALLMQDTHKQLlERGYrrpvLLLHPLGGWTKDDDVPLMWRMKQHA 473
Cdd:pfam01747 1 DEYRLTPAETRALFKEKGWRTVVAFQTRNPLHRAHEELMKRALEEL-EADG----LLLHPLVGPTKPGDVPAEVRVRCYE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259126 474 AVLEEgILNPETTVVAIFPSPMMYAGPTEVQWHCRARMVAGANFYIVGRDPAGMPHpetgkdLYEPTHGAKVLTMAPGLI 553
Cdd:pfam01747 76 ALLEN-YLPPDRVVLALLPLAMRYAGPREALLHAIIRKNYGCTHFIVGRDHAGVGD------FYGPYDAQEIFDEYPGEL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2047259126 554 TLEIVPFRVAAYNKKKKRMDYYDSDHH-EDFEFISGTRMRKLAREGQKPPEGFMAPKAWTVLVEY 617
Cdd:pfam01747 149 GIEPVPFREAVYCKKCGEMASTKCPHGgEDRLFISGTKVRELLREGEEPPEWFSRPEVAKVLREY 213
|
|
| PRK03846 |
PRK03846 |
adenylylsulfate kinase; Provisional |
26-226 |
9.92e-92 |
|
adenylylsulfate kinase; Provisional
Pssm-ID: 179661 Cd Length: 198 Bit Score: 281.44 E-value: 9.92e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259126 26 TNVTYQAHHVSRNKRGQvvgtRGGFRGCTVWLTGLSGAGKTTVSMALEEYLVCHGIPCYTLDGDNIRQGLNKNLGFSPED 105
Cdd:PRK03846 2 ENIVWHQHPVTKAQREQ----LHGHKGVVLWFTGLSGSGKSTVAGALEEALHELGVSTYLLDGDNVRHGLCSDLGFSDAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259126 106 REENVRRIAEVAKLFADAGLVCITSFISPYTQDRNNARQIhegasLP---FFEVFVDAPLHVCEQRDVKGLYKKARAGEI 182
Cdd:PRK03846 78 RKENIRRVGEVAKLMVDAGLVVLTAFISPHRAERQMVRER-----LGegeFIEVFVDTPLAICEARDPKGLYKKARAGEI 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2047259126 183 KGFTGIDSEYEKPEAPELVLKTDSCDVNDCVQQVVELLQERDIV 226
Cdd:PRK03846 153 RNFTGIDSVYEAPESPEIHLDTGEQLVTNLVEQLLDYLRQRDII 196
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
12-225 |
9.51e-89 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 288.37 E-value: 9.51e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259126 12 KLSNNAQNWGM-----QRATNVTYQAHHVSRNKRGqvvgTRGGFRGCTVWLTGLSGAGKTTVSMALEEYLVCHGIPCYTL 86
Cdd:PRK05506 419 RLTNATVGAGMidfalRRATNVHWQASDVSREARA----ARKGQKPATVWFTGLSGSGKSTIANLVERRLHALGRHTYLL 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259126 87 DGDNIRQGLNKNLGFSPEDREENVRRIAEVAKLFADAGLVCITSFISPYTQDRNNARQIHEGAslPFFEVFVDAPLHVCE 166
Cdd:PRK05506 495 DGDNVRHGLNRDLGFSDADRVENIRRVAEVARLMADAGLIVLVSFISPFREERELARALHGEG--EFVEVFVDTPLEVCE 572
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2047259126 167 QRDVKGLYKKARAGEIKGFTGIDSEYEKPEAPELVLKTDSCDVNDCVQQVVELLQERDI 225
Cdd:PRK05506 573 ARDPKGLYAKARAGEIKNFTGIDSPYEAPENPELRLDTTGRSPEELAEQVLELLRRRGA 631
|
|
| apsK |
TIGR00455 |
adenylyl-sulfate kinase; This protein, adenylylsulfate kinase, is often found as a fusion ... |
34-220 |
5.25e-85 |
|
adenylyl-sulfate kinase; This protein, adenylylsulfate kinase, is often found as a fusion protein with sulfate adenylyltransferase. Important residue (active site in E.coli) is residue 100 of the seed alignment. [Central intermediary metabolism, Sulfur metabolism]
Pssm-ID: 129547 Cd Length: 184 Bit Score: 263.56 E-value: 5.25e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259126 34 HVSRNKRGQVVGTRGgfrgCTVWLTGLSGAGKTTVSMALEEYLVCHGIPCYTLDGDNIRQGLNKNLGFSPEDREENVRRI 113
Cdd:TIGR00455 4 AITKDERQALNGHRG----VVIWLTGLSGSGKSTIANALEKKLESKGYRVYVLDGDNVRHGLNKDLGFSEEDRKENIRRI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259126 114 AEVAKLFADAGLVCITSFISPYTQDRNNARQIHEGASlpFFEVFVDAPLHVCEQRDVKGLYKKARAGEIKGFTGIDSEYE 193
Cdd:TIGR00455 80 GEVAKLFVRNGIIVITSFISPYRADRQMVRELIEKGE--FIEVFVDCPLEVCEQRDPKGLYKKARNGEIKGFTGIDSPYE 157
|
170 180
....*....|....*....|....*..
gi 2047259126 194 KPEAPELVLKTDSCDVNDCVQQVVELL 220
Cdd:TIGR00455 158 APENPEVVLDTDQNDREECVGQIIEKL 184
|
|
| PRK00889 |
PRK00889 |
adenylylsulfate kinase; Provisional |
51-227 |
3.29e-75 |
|
adenylylsulfate kinase; Provisional
Pssm-ID: 179157 Cd Length: 175 Bit Score: 238.00 E-value: 3.29e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259126 51 RGCTVWLTGLSGAGKTTVSMALEEYLVCHGIPCYTLDGDNIRQGLNKNLGFSPEDREENVRRIAEVAKLFADAGLVCITS 130
Cdd:PRK00889 3 RGVTVWFTGLSGAGKTTIARALAEKLREAGYPVEVLDGDAVRTNLSKGLGFSKEDRDTNIRRIGFVANLLTRHGVIVLVS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259126 131 FISPYTQDRNNARqihegASLP-FFEVFVDAPLHVCEQRDVKGLYKKARAGEIKGFTGIDSEYEKPEAPELVLKTDSCDV 209
Cdd:PRK00889 83 AISPYRETREEVR-----ANIGnFLEVFVDAPLEVCEQRDVKGLYAKARAGEIKHFTGIDDPYEPPLNPEVECRTDLESL 157
|
170
....*....|....*...
gi 2047259126 210 NDCVQQVVELLQERDIVP 227
Cdd:PRK00889 158 EESVDKVLQKLEELGYLV 175
|
|
| MET3 |
COG2046 |
ATP sulfurylase (sulfate adenylyltransferase) [Inorganic ion transport and metabolism]; ATP ... |
233-623 |
2.47e-71 |
|
ATP sulfurylase (sulfate adenylyltransferase) [Inorganic ion transport and metabolism]; ATP sulfurylase (sulfate adenylyltransferase) is part of the Pathway/BioSystem: Cysteine biosynthesis
Pssm-ID: 441649 Cd Length: 388 Bit Score: 235.04 E-value: 2.47e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259126 233 EVKELYVPENKLHLAKTDAEALPALKINKVDMQWVQVLAEGWATPLNGFMREREYLQCLHFDCLLDGGVinLSVPIVLTA 312
Cdd:COG2046 11 KLVNRVVPGEEREALLEEAKGLPSIELSSRALSDLEMIAIGGFSPLTGFMNKADYESVVENMRLADGLL--WPIPITLDV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259126 313 TQEDKERLDGCTAFALV-YEGRRVAILRNPEFFEHRKEERCARQWGTTCRSHPYIKMILEQGDWLIGGDLQVLDRIYWND 391
Cdd:COG2046 89 SEEDAAGLKEGDEVALRdEEGEPLAVLEVEEIYEYDKEEEAEKVYGTTDPAHPGVAKLYERGDVYLGGPITLLNRPKHPD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259126 392 gLDQYRLTPAELKQKFKDMNADAVFAFQLRNPVHNGHALLMqdthKQLLERGYrrpVLLLHPLGGWTKDDDVPLMWRMKQ 471
Cdd:COG2046 169 -FPDYRLTPAETRALFEEKGWKTVVAFQTRNPMHRAHEYLQ----KRALETVD---GLLIHPLVGETKPGDIPAEVRVRC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259126 472 HAAVLEEGIlNPETTVVAIFPSPMMYAGPTEVQWH--CRARMvaGANFYIVGRDPAGMPhpetgkDLYEPtHGAKVL--T 547
Cdd:COG2046 241 YEALLENYY-PKDRVLLSGLPLAMRYAGPREALLHaiIRKNY--GCTHFIVGRDHAGVG------DYYGP-YDAQEIfdE 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2047259126 548 MAPGLITLEIVPFRVAAYNKKKKRMDYYDSDHH--EDFEFISGTRMRKLAREGQKPPEGFMAPKAWTVLVEYYKSLEK 623
Cdd:COG2046 311 FPPGELGIEPLKFEEAFYCKKCGGMATSKTCPHdkEDRVSLSGTKVREMLREGEEPPPEFSRPEVAEILRKYYQPFGE 388
|
|
| PUA_2 |
pfam14306 |
PUA-like domain; This PUA like domain is found at the N-terminus of ATP-sulfurylase enzymes. |
233-386 |
4.94e-63 |
|
PUA-like domain; This PUA like domain is found at the N-terminus of ATP-sulfurylase enzymes.
Pssm-ID: 464131 [Multi-domain] Cd Length: 159 Bit Score: 205.45 E-value: 4.94e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259126 233 EVKELYVPENKLHLAKTDAEALPALKINKVDMQWVQVLAEGWATPLNGFMREREYLQCLHFDCLLDGGVinLSVPIVLTA 312
Cdd:pfam14306 7 KLVDLVVRDAEREELLAEAAELPSIELSKRELCDLELIAIGGFSPLTGFMGEADYLSVLEFMRLADGLL--WSIPITLDV 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2047259126 313 TQEDKERLDGCTAFALVY-EGRRVAILRNPEFFEHRKEERCARQWGTTCRSHPYIKMILEQGDWLIGGDLQVLDR 386
Cdd:pfam14306 85 SEEDAASLKEGDRVALRDpEGEPLAILTVEEIYEPDKEEEAEKVFGTTDPAHPGVKKLYEQGDFYVGGDIEVLNR 159
|
|
| sat |
PRK04149 |
sulfate adenylyltransferase; Reviewed |
233-622 |
2.44e-61 |
|
sulfate adenylyltransferase; Reviewed
Pssm-ID: 235227 Cd Length: 391 Bit Score: 208.95 E-value: 2.44e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259126 233 EVKELYVPENKLHLAKTDAEALPALKINKVDMQWVQVLAEGWATPLNGFMREREYLQCLHFDCLLDGGVinLSVPIVLTA 312
Cdd:PRK04149 10 ELVNRVVEGRDREEILEEAESLPRIELDERAASDLEMIAIGGFSPLTGFMGREDYDSVVEEMRLANGLV--WSIPITLDV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259126 313 TQEDKERLDGCTAFALVYEGRRVAILRNPEFFEHRKEERCARQWGTTCRSHPYIKMILEQGDWLIGGDLQVLDRIYwNDG 392
Cdd:PRK04149 88 SEEDAASLKEGDEVALVYKGEPYGVLEVEEIYTYDKKKEAEKVYKTTDEKHPGVKKLYEQGDVYLAGPVTLLNRKF-HEP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259126 393 LDQYRLTPAELKQKFKDMNADAVFAFQLRNPVHNGHALLMqdthKQLLE--RGyrrpvLLLHPLGGWTKDDDVPLMWRMK 470
Cdd:PRK04149 167 FPRFWLTPAETRELFEEKGWKTVVAFQTRNPPHRAHEYLQ----KCALEivDG-----LLLNPLVGETKSGDIPAEVRME 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259126 471 QHAAVLeEGILNPETTVVAIFPSPMMYAGPTEVQWHCRARMVAGANFYIVGRDPAGmphpeTGkDLYEP-------THGA 543
Cdd:PRK04149 238 AYEALL-KNYYPKDRVLLSVTPAAMRYAGPREAIFHAIVRKNYGCTHFIVGRDHAG-----VG-DYYGPydaqeifDEFT 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259126 544 KvltmaPGLITlEIVPFRVAAYNKKKKRMDYY-DSDH-HEDFEFISGTRMRKLAREGQKPPEGFMAPKAWTVLVEYYKSL 621
Cdd:PRK04149 311 E-----EELGI-TPLKFEEAFYCPKCGGMASEkTCPHgKEDRVHLSGTKVREMLREGEKPPPEFSRPEVAEVLIKGLKKY 384
|
.
gi 2047259126 622 E 622
Cdd:PRK04149 385 G 385
|
|
| PRK05537 |
PRK05537 |
bifunctional sulfate adenylyltransferase/adenylylsulfate kinase; |
52-223 |
1.47e-58 |
|
bifunctional sulfate adenylyltransferase/adenylylsulfate kinase;
Pssm-ID: 180124 [Multi-domain] Cd Length: 568 Bit Score: 206.06 E-value: 1.47e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259126 52 GCTVWLTGLSGAGKTTVSMALEEYLVCHGIPCYT-LDGDNIRQGLNKNLGFSPEDREENVRRIAEVAKLFADAGLVCITS 130
Cdd:PRK05537 392 GFTVFFTGLSGAGKSTIAKALMVKLMEMRGRPVTlLDGDVVRKHLSSELGFSKEDRDLNILRIGFVASEITKNGGIAICA 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259126 131 FISPYTQDRNNARQIHEGASlPFFEVFVDAPLHVCEQRDVKGLYKKARAGEIKGFTGIDSEYEKPEAPELVLKTDSCDVN 210
Cdd:PRK05537 472 PIAPYRATRREVREMIEAYG-GFIEVHVATPLEVCEQRDRKGLYAKAREGKIKGFTGISDPYEPPANPELVIDTTNVTPD 550
|
170
....*....|...
gi 2047259126 211 DCVQQVVELLQER 223
Cdd:PRK05537 551 ECAHKILLYLEEK 563
|
|
| PRK05537 |
PRK05537 |
bifunctional sulfate adenylyltransferase/adenylylsulfate kinase; |
236-623 |
3.29e-47 |
|
bifunctional sulfate adenylyltransferase/adenylylsulfate kinase;
Pssm-ID: 180124 [Multi-domain] Cd Length: 568 Bit Score: 174.86 E-value: 3.29e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259126 236 ELYVPENKLHLAKTDAEALPALKINKVDMQWVQVLAEGWATPLNGFMREREYLQCLHFDCLLDGGVinLSVPIVLTATQE 315
Cdd:PRK05537 11 NLYVSPESREKLKAEALSLPSLDLSPRQICDLELLMNGGFSPLKGFMGRADYECVLENMRLADGTL--WPIPITLDVSEK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259126 316 DKERLDGCTAFALV-YEGRRVAILRNPEFFEHRKEERCARQWGTTCRSHPYIKMILEQ-GDWLIGGDLQVLDR-IYWNdg 392
Cdd:PRK05537 89 FAAGLEIGERIALRdQEGVLLAILTVSDIWEPDKEREAEAVFGTTDPAHPGVNYLHRWaGKFYLGGPLTGIQLpVHYD-- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259126 393 LDQYRLTPAELKQKFKDMNADAVFAFQLRNPVHNGHallmqdthKQLLERGYRR--PVLLLHPLGGWTKDDDVPLMWRMK 470
Cdd:PRK05537 167 FVQLRLTPAELRARFRKLGWRRVVAFQTRNPLHRAH--------EELTKRAAREvgANLLIHPVVGMTKPGDIDHFTRVR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259126 471 QHAAVLEEgiLNPETTVVAIFPSPMMYAGPTEVQWHCRARMVAGANFYIVGRDPAGMPHPETGKDLYEPTHGAKVLTMAP 550
Cdd:PRK05537 239 CYEALLDK--YPPATTLLSLLPLAMRMAGPREALWHAIIRRNYGCTHFIVGRDHAGPGKDSRGKPFYGPYDAQELFAKYA 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2047259126 551 GLITLEIVPFRVAAYNKKKKRmdYYDSDHHEDFE---FISGTRMRKLAREGQKPPEGFMAPKAWTVLVEYYKSLEK 623
Cdd:PRK05537 317 DEIGITMVPFKEMVYVQDKAQ--YVPVDEVPQGAtvlTISGTELRRRLREGLEIPEWFSFPEVVAELRRTYPPRHK 390
|
|
| PRK05541 |
PRK05541 |
adenylylsulfate kinase; Provisional |
52-225 |
6.60e-27 |
|
adenylylsulfate kinase; Provisional
Pssm-ID: 235498 Cd Length: 176 Bit Score: 107.45 E-value: 6.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259126 52 GCTVWLTGLSGAGKTTVSMALEEYLVCHGIPCYTLDGDNIRQGLNKNlGFSPEDREENVRRIAEVAKLFADAGLVCITSF 131
Cdd:PRK05541 7 GYVIWITGLAGSGKTTIAKALYERLKLKYSNVIYLDGDELREILGHY-GYDKQSRIEMALKRAKLAKFLADQGMIVIVTT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259126 132 ISPYTQDRNNARQIHEGaslpFFEVFVDAPLHVCEQRDVKGLYKKARAGEIKGFTGIDSEYEKPEAPELVLKTDSCDVND 211
Cdd:PRK05541 86 ISMFDEIYAYNRKHLPN----YFEVYLKCDMEELIRRDQKGLYTKALKGEIKNVVGVDIPFDEPKADLVIDNSCRTSLDE 161
|
170
....*....|....
gi 2047259126 212 CVQQVVELLQERDI 225
Cdd:PRK05541 162 KVDLILNKLKLRLI 175
|
|
| Kti12 |
COG4088 |
tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) ... |
57-223 |
7.85e-12 |
|
tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) [Translation, ribosomal structure and biogenesis, Defense mechanisms];
Pssm-ID: 443264 [Multi-domain] Cd Length: 179 Bit Score: 64.36 E-value: 7.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259126 57 LTGLSGAGKTTVSMALEEYLVCHGIPCYTLDGDNIRQGLnKNLGFSPEDREENVRRIAE-VAKLFADAGLVCIT--SFIS 133
Cdd:COG4088 9 LTGPPGSGKTTFAKALAQRLYAEGIAVALLHSDDFRRFL-VNESFPKETYEEVVEDVRTtTADNALDNGYSVIVdgTFYY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259126 134 PYTQDRnnARQIHEGASlPFFEVFVDAPLHVCEQRDVkglykkARAGEI--KGFTGIDSEYEKPE---APELVLKTDSCD 208
Cdd:COG4088 88 RSWQRD--FRNLAKHKA-PIHIIYLKAPLETALRRNR------ERGEPIpeRVIARMYRKFDKPGtkdRPDLVIDTTEDS 158
|
170
....*....|....*
gi 2047259126 209 VNDCVQQVVELLQER 223
Cdd:COG4088 159 VSETLDAILKAIETW 173
|
|
| AAA_33 |
pfam13671 |
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ... |
55-204 |
4.72e-09 |
|
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the AAA superfamily. Many of the proteins in this family are just short fragments so there is no Walker B motif.
Pssm-ID: 463952 [Multi-domain] Cd Length: 143 Bit Score: 55.39 E-value: 4.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259126 55 VWLTGLSGAGKTTVSMALEEYLvchgiPCYTLDGDNIRQGLNKNLGFSPEDREEN----VRRIAEVAKLFADAGLVCI-- 128
Cdd:pfam13671 2 ILLVGLPGSGKSTLARRLLEEL-----GAVRLSSDDERKRLFGEGRPSISYYTDAtdrtYERLHELARIALRAGRPVIld 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2047259126 129 TSFISPytQDRNNARQIHEGASLPFFEVFVDAPLHVCEQRDvkglykKARAgeikgftgiDSEYEKPEAPELVLKT 204
Cdd:pfam13671 77 ATNLRR--DERARLLALAREYGVPVRIVVFEAPEEVLRERL------AARA---------RAGGDPSDVPEEVLDR 135
|
|
| COG0645 |
COG0645 |
Predicted kinase, contains AAA domain [General function prediction only]; |
55-168 |
1.17e-08 |
|
Predicted kinase, contains AAA domain [General function prediction only];
Pssm-ID: 440410 [Multi-domain] Cd Length: 164 Bit Score: 54.53 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259126 55 VWLTGLSGAGKTTVSMALEEYL-VCHgipcytLDGDNIRQGLnKNLGFSPEDREENVR-----RIAEVAKLFADAGLVCI 128
Cdd:COG0645 2 ILVCGLPGSGKSTLARALAERLgAVR------LRSDVVRKRL-FGAGLAPLERSPEATartyaRLLALARELLAAGRSVI 74
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2047259126 129 TSFISPYTQDRNNARQIHEGASLPFFEVFVDAPLHVCEQR 168
Cdd:COG0645 75 LDATFLRRAQREAFRALAEEAGAPFVLIWLDAPEEVLRER 114
|
|
| CmkB |
COG1102 |
Cytidylate kinase [Nucleotide transport and metabolism]; |
59-225 |
1.37e-06 |
|
Cytidylate kinase [Nucleotide transport and metabolism];
Pssm-ID: 440719 [Multi-domain] Cd Length: 188 Bit Score: 49.05 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259126 59 GLSGAGKTTVSMALEEYLvchGIPCYtlDGDNIRQgLNKNLGFSPEDREEN------------------VRRIAEVAKLF 120
Cdd:COG1102 7 REPGSGGTTIAKRLAEKL---GLPLY--DGEILRE-AAKERGLSEEEFEKLdekapsllyrdtaeedeiDRALDKVIREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259126 121 ADAGLVCITSFISPY-TQDRNNArqihegaslpfFEVFVDAPLHVCEQR-------DVKGLYK------KARAGEIKGFT 186
Cdd:COG1102 81 ARKGNCVIVGRLADWiLRDRPNV-----------LKVFLTAPLEVRVKRiaeregiSEEEAEKeikkrdKSRAKYYKYYY 149
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2047259126 187 GID----SEYekpeapELVLKTDSCDVNDCVQQVVELLQERDI 225
Cdd:COG1102 150 GIDwgdpSNY------DLVINTSRLGIEEAVDLILAAIEAREK 186
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
57-123 |
3.35e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 41.20 E-value: 3.35e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2047259126 57 LTGLSGAGKTTVSMALEEYLVCHGIPCYTLDGDNIRQG-LNKNLGFSPEDREENVRRIAEVAKLFADA 123
Cdd:smart00382 7 IVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEvLDQLLLIIVGGKKASGSGELRLRLALALA 74
|
|
| GntK |
cd02021 |
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting ... |
57-199 |
4.77e-04 |
|
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting product gluconate-6-phoshate is an important precursor of gluconate metabolism. GntK acts as a dimmer composed of two identical subunits.
Pssm-ID: 238979 [Multi-domain] Cd Length: 150 Bit Score: 41.08 E-value: 4.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047259126 57 LTGLSGAGKTTVSMALEEYLVCHGIpcytlDGDNIRQGLNK-----NLGFSPEDRE---ENVRRIAEVAKLFADAGLVCI 128
Cdd:cd02021 4 VMGVSGSGKSTVGKALAERLGAPFI-----DGDDLHPPANIakmaaGIPLNDEDRWpwlQALTDALLAKLASAGEGVVVA 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2047259126 129 TSFISPYTQDRnnARQIHEGASLPFfeVFVDAPLHVCEQRDvkglykKARAGEIKGFTGIDSEYEKPEAPE 199
Cdd:cd02021 79 CSALKRIYRDI--LRGGAANPRVRF--VHLDGPREVLAERL------AARKGHFMPADLLDSQFETLEPPG 139
|
|
| NK |
cd02019 |
Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of ... |
54-126 |
6.18e-03 |
|
Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of enzymes that share structural similarity and are functionally related to the catalysis of the reversible phosphate group transfer from nucleoside triphosphates to nucleosides/nucleotides, nucleoside monophosphates, or sugars. Members of this family play a wide variety of essential roles in nucleotide metabolism, the biosynthesis of coenzymes and aromatic compounds, as well as the metabolism of sugar and sulfate.
Pssm-ID: 238977 [Multi-domain] Cd Length: 69 Bit Score: 35.78 E-value: 6.18e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2047259126 54 TVWLTGLSGAGKTTVSMALEEYLVCHGIPCYT----LDGdnirqglnknLGFSPEDREENVRRIAEVaKLFADAGLV 126
Cdd:cd02019 1 IIAITGGSGSGKSTVAKKLAEQLGGRSVVVLDeiviLEG----------LYASYKSRDARIRDLADL-KIYLDADLV 66
|
|
| |
