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Conserved domains on  [gi|46094058|ref|NP_005434|]
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bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 1 [Homo sapiens]

Protein Classification

sulfate adenylyltransferase; tryptophan--tRNA ligase( domain architecture ID 10785574)

sulfate adenylyltransferase converts ATP and sulfate to adenosine-5'-phosphosulfate (APS) and pyrophosphate; tryptophan--tRNA ligase, a class I tRNA synthetase, aminoacylates the 2'-OH of the nucleotide at the 3' end of the tRNA

Graphical summary

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List of domain hits

 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: 538.76  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46094058 254 LPALKINKVDMQWVQVLAEGWATPLNGFMREREYLQCLHFDCLLDGgvINLSVPIVLTATHEDKERLDGCTAFALMYEGR 333
Cdd:cd00517   1 LPSVELSERDLCDLEMLAEGGFSPLTGFMTEADYLSVLEEMRLLDG--TLWPIPIVLDVSEEDAKRLKEGERVALRYPGQ 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46094058 334 RVAILRNPEFFEHRKEERCARQWGTTCKNHPYIKMVMEQGDWLIGGDLQVLDRVYWNDgLDQYRLTPTELKQKFKDMNAD 413
Cdd:cd00517  79 PLAILTVEEIYEPDKEEEAARVFGTTDPHHPGVKKVMEQGDWLVGGPIEVLELPPFPD-FDQYRLTPAELRALFKERGWR 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46094058 414 AVFAFQLRNPVHNGHALLMQDTHKQLLergyrRPVLLLHPLGGWTKDDDVPLMWRMKQHAAVLEEGVLnPETTVVAIFPS 493
Cdd:cd00517 158 RVVAFQTRNPMHRAHEELMKRAAEKLL-----NDGLLLHPLVGWTKPGDVPDEVRMRAYEALLEEYYL-PERTVLAILPL 231

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46094058 494 PMMYAGPTEVQWHCRARMVAGANFYIVGRDPAGMPHPETGKDLYEPSHGAKVLTMApglITLEIVPFRVAAYNKKKKRMD 573
Cdd:cd00517 232 PMRYAGPREALWHAIIRKNYGATHFIVGRDHAGVGHPGDYYGPYDAQEIFKKLAPE---LGIEPVPFREAAYCPKCDGMA 308

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*
gi 46094058 574 YYDSE-HHEDFEFISGTRMRKLAREGQKPPEGFMAPKAWTVLTEY 617
Cdd:cd00517 309 SEDTCpHGEDFLNISGTKLRKMLREGEKPPEWFMRPEVAKVLREY 353
CysC COG0529
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ...
 33-227 1.94e-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: 326.66  E-value: 1.94e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46094058  33 HHVSRNKRGQvvgtRGGFRGCTVWLTGLSGAGKTTVSMALEEYLVCHGIPCYTLDGDNIRQGLNKNLGFSPEDREENVRR 112
Cdd:COG0529   1 SAVTREERAA----LKGQKGFVVWFTGLSGSGKSTLANALERRLFERGRHVYLLDGDNVRHGLNKDLGFSKEDRDENIRR 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46094058 113 IAEVAKLFADAGLVCITSFISPYTQDRNNARQIHEGAslPFFEVFVDAPLHVCEQRDVKGLYKKARAGEIKGFTGIDSEY 192
Cdd:COG0529  77 IGEVAKLLADAGLIVLVAFISPYRADREEARELIGEG--EFIEVYVDTPLEVCEARDPKGLYAKARAGEIKNFTGIDDPY 154

                       170       180       190
                ....*....|....*....|....*....|....*
gi 46094058 193 EKPEAPELVLKTDSCDVNDCVQQVVELLQERDIVP 227
Cdd:COG0529 155 EAPENPELVLDTDKESVEESVEKILAYLEERGYIS 189
 
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: 538.76  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46094058 254 LPALKINKVDMQWVQVLAEGWATPLNGFMREREYLQCLHFDCLLDGgvINLSVPIVLTATHEDKERLDGCTAFALMYEGR 333
Cdd:cd00517   1 LPSVELSERDLCDLEMLAEGGFSPLTGFMTEADYLSVLEEMRLLDG--TLWPIPIVLDVSEEDAKRLKEGERVALRYPGQ 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46094058 334 RVAILRNPEFFEHRKEERCARQWGTTCKNHPYIKMVMEQGDWLIGGDLQVLDRVYWNDgLDQYRLTPTELKQKFKDMNAD 413
Cdd:cd00517  79 PLAILTVEEIYEPDKEEEAARVFGTTDPHHPGVKKVMEQGDWLVGGPIEVLELPPFPD-FDQYRLTPAELRALFKERGWR 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46094058 414 AVFAFQLRNPVHNGHALLMQDTHKQLLergyrRPVLLLHPLGGWTKDDDVPLMWRMKQHAAVLEEGVLnPETTVVAIFPS 493
Cdd:cd00517 158 RVVAFQTRNPMHRAHEELMKRAAEKLL-----NDGLLLHPLVGWTKPGDVPDEVRMRAYEALLEEYYL-PERTVLAILPL 231

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46094058 494 PMMYAGPTEVQWHCRARMVAGANFYIVGRDPAGMPHPETGKDLYEPSHGAKVLTMApglITLEIVPFRVAAYNKKKKRMD 573
Cdd:cd00517 232 PMRYAGPREALWHAIIRKNYGATHFIVGRDHAGVGHPGDYYGPYDAQEIFKKLAPE---LGIEPVPFREAAYCPKCDGMA 308

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*
gi 46094058 574 YYDSE-HHEDFEFISGTRMRKLAREGQKPPEGFMAPKAWTVLTEY 617
Cdd:cd00517 309 SEDTCpHGEDFLNISGTKLRKMLREGEKPPEWFMRPEVAKVLREY 353
sopT TIGR00339
ATP sulphurylase; This enzyme forms adenosine 5'-phosphosulfate (APS) from ATP and free ...
 233-616 8.52e-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: 391.75  E-value: 8.52e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46094058   233 EVKELYV--PENKlHLAKTDAETLPALKINKVDMQWVQVLAEGWATPLNGFMREREYLQCLHFDCLLDGgvINLSVPIVL 310
Cdd:TIGR00339   5 KLVELVVrdPDEE-HKLLAEAESLPSITLSDRQLCDLELLGNGAFSPLEGFMNEADYDSVVESMRLSDG--VLFSVPITL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46094058   311 TATHEDKERLDGCTAFALMYE-GRRVAILRNPEFFEHRKEERCARQWGTTCKNHPYIKMVMEQGDWLIGGDLQVLDRVYW 389
Cdd:TIGR00339  82 DIDDEDADDIKLGDRIALTDPkGQPLAILTIEEVYKPNKEKEAKKVFGTTDPEHPGVVYLNTAGNYYIGGPIEVINLPKF 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46094058   390 nDGLDQYRLTPTELKQKFKDMNADAVFAFQLRNPVHNGHALLMQDThkqlLERGyRRPVLLLHPLGGWTKDDDVPLMWRM 469
Cdd:TIGR00339 162 -YDFPRFRFTPAELREEFKERGWDTVVAFQTRNPMHRAHEELTKRA----AERL-PNAGVLVHPLVGLTKPGDIPAEVRM 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46094058   470 KQHAaVLEEGVLNPETTVVAIFPSPMMYAGPTEVQWHCRARMVAGANFYIVGRDPAGMPHPETGKDLYEPSHGAKVLTMA 549
Cdd:TIGR00339 236 RAYE-VLKEGYPNPERTVVSFLPLAMRYAGPREAIWHAIIRKNYGATHFIVGRDHAGPGSNSKGQDFYGPYDAQELFEKY 314

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 46094058   550 PGLITLEIVPFRVAAYNKKKKRMDYYDS--EHHEDFEFISGTRMRKLAREGQKPPEGFMAPKAWTVLTE 616
Cdd:TIGR00339 315 KAELGIKIVPFRHVAYCPDEDEYAPADQagHTNLRTLNISGTKLRGMLRNGVFPPEWFSRPEVVKILRE 383
CysC COG0529
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ...
 33-227 1.94e-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: 326.66  E-value: 1.94e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46094058  33 HHVSRNKRGQvvgtRGGFRGCTVWLTGLSGAGKTTVSMALEEYLVCHGIPCYTLDGDNIRQGLNKNLGFSPEDREENVRR 112
Cdd:COG0529   1 SAVTREERAA----LKGQKGFVVWFTGLSGSGKSTLANALERRLFERGRHVYLLDGDNVRHGLNKDLGFSKEDRDENIRR 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46094058 113 IAEVAKLFADAGLVCITSFISPYTQDRNNARQIHEGAslPFFEVFVDAPLHVCEQRDVKGLYKKARAGEIKGFTGIDSEY 192
Cdd:COG0529  77 IGEVAKLLADAGLIVLVAFISPYRADREEARELIGEG--EFIEVYVDTPLEVCEARDPKGLYAKARAGEIKNFTGIDDPY 154

                       170       180       190
                ....*....|....*....|....*....|....*
gi 46094058 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 46094058    51 RGCTVWLTGLSGAGKTTVSMALEEYLVCHGIPCYTLDGDNIRQGLNKNLGFSPEDREENVRRIAEVAKLFADAGLVCITS 130
Cdd:pfam01583   1 RGCTIWLTGLSGAGKSTIANALERKLFEQGRSVYVLDGDNVRHGLNKDLGFSEEDRTENIRRIGEVAKLFADAGLIVITA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46094058   131 FISPYTQDRNNARQIHEGAslPFFEVFVDAPLHVCEQRDVKGLYKKARAGEIKGFTGIDSEYEKPEAPELVLKTD 205
Cdd:pfam01583  81 FISPYREDREQARELHEEG--KFIEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDSPYEAPENPELVLDTD 153
APSK cd02027
Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5 ...
 54-204 7.49e-103

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: 308.25  E-value: 7.49e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46094058  54 TVWLTGLSGAGKTTVSMALEEYLVCHGIPCYTLDGDNIRQGLNKNLGFSPEDREENVRRIAEVAKLFADAGLVCITSFIS 133
Cdd:cd02027   1 VIWLTGLSGSGKSTIARALEEKLFQRGRPVYVLDGDNVRHGLNKDLGFSREDREENIRRIAEVAKLLADAGLIVIAAFIS 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 46094058 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 2.28e-94

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: 289.05  E-value: 2.28e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46094058   394 DQYRLTPTELKQKFKDMNADAVFAFQLRNPVHNGHALLMQDTHKQLlERGYrrpvLLLHPLGGWTKDDDVPLMWRMKQHA 473
Cdd:pfam01747   1 DEYRLTPAETRALFKEKGWRTVVAFQTRNPLHRAHEELMKRALEEL-EADG----LLLHPLVGPTKPGDVPAEVRVRCYE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46094058   474 AVLEEgVLNPETTVVAIFPSPMMYAGPTEVQWHCRARMVAGANFYIVGRDPAGMPHpetgkdLYEPSHGAKVLTMAPGLI 553
Cdd:pfam01747  76 ALLEN-YLPPDRVVLALLPLAMRYAGPREALLHAIIRKNYGCTHFIVGRDHAGVGD------FYGPYDAQEIFDEYPGEL 148

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46094058   554 TLEIVPFRVAAYNKKKKRMDYYDSEHH-EDFEFISGTRMRKLAREGQKPPEGFMAPKAWTVLTEY 617
Cdd:pfam01747 149 GIEPVPFREAVYCKKCGEMASTKCPHGgEDRLFISGTKVRELLREGEEPPEWFSRPEVAKVLREY 213
PRK03846 PRK03846
adenylylsulfate kinase; Provisional
 26-226 6.96e-92

adenylylsulfate kinase; Provisional


Pssm-ID: 179661  Cd Length: 198  Bit Score: 281.83  E-value: 6.96e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46094058   26 TNVTYQAHHVSRNKRGQvvgtRGGFRGCTVWLTGLSGAGKTTVSMALEEYLVCHGIPCYTLDGDNIRQGLNKNLGFSPED 105
Cdd:PRK03846   2 ENIVWHQHPVTKAQREQ----LHGHKGVVLWFTGLSGSGKSTVAGALEEALHELGVSTYLLDGDNVRHGLCSDLGFSDAD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46094058  106 REENVRRIAEVAKLFADAGLVCITSFISPYTQDRNNARQIhegasLP---FFEVFVDAPLHVCEQRDVKGLYKKARAGEI 182
Cdd:PRK03846  78 RKENIRRVGEVAKLMVDAGLVVLTAFISPHRAERQMVRER-----LGegeFIEVFVDTPLAICEARDPKGLYKKARAGEI 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 46094058  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 3.93e-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: 263.94  E-value: 3.93e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46094058    34 HVSRNKRGQVVGTRGgfrgCTVWLTGLSGAGKTTVSMALEEYLVCHGIPCYTLDGDNIRQGLNKNLGFSPEDREENVRRI 113
Cdd:TIGR00455   4 AITKDERQALNGHRG----VVIWLTGLSGSGKSTIANALEKKLESKGYRVYVLDGDNVRHGLNKDLGFSEEDRKENIRRI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46094058   114 AEVAKLFADAGLVCITSFISPYTQDRNNARQIHEGASlpFFEVFVDAPLHVCEQRDVKGLYKKARAGEIKGFTGIDSEYE 193
Cdd:TIGR00455  80 GEVAKLFVRNGIIVITSFISPYRADRQMVRELIEKGE--FIEVFVDCPLEVCEQRDPKGLYKKARNGEIKGFTGIDSPYE 157

                         170       180
                  ....*....|....*....|....*..
gi 46094058   194 KPEAPELVLKTDSCDVNDCVQQVVELL 220
Cdd:TIGR00455 158 APENPEVVLDTDQNDREECVGQIIEKL 184
MET3 COG2046
ATP sulfurylase (sulfate adenylyltransferase) [Inorganic ion transport and metabolism]; ATP ...
 233-623 2.41e-69

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: 230.03  E-value: 2.41e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46094058 233 EVKELYVPENKLHLAKTDAETLPALKINKVDMQWVQVLAEGWATPLNGFMREREYLQCLHFDCLLDGGVinLSVPIVLTA 312
Cdd:COG2046  11 KLVNRVVPGEEREALLEEAKGLPSIELSSRALSDLEMIAIGGFSPLTGFMNKADYESVVENMRLADGLL--WPIPITLDV 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46094058 313 THEDKERLDGCTAFALM-YEGRRVAILRNPEFFEHRKEERCARQWGTTCKNHPYIKMVMEQGDWLIGGDLQVLDRVYWND 391
Cdd:COG2046  89 SEEDAAGLKEGDEVALRdEEGEPLAVLEVEEIYEYDKEEEAEKVYGTTDPAHPGVAKLYERGDVYLGGPITLLNRPKHPD 168

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46094058 392 gLDQYRLTPTELKQKFKDMNADAVFAFQLRNPVHNGHALLMqdthKQLLERGYrrpVLLLHPLGGWTKDDDVPLMWRMKQ 471
Cdd:COG2046 169 -FPDYRLTPAETRALFEEKGWKTVVAFQTRNPMHRAHEYLQ----KRALETVD---GLLIHPLVGETKPGDIPAEVRVRC 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46094058 472 HAAVLEEGVlNPETTVVAIFPSPMMYAGPTEVQWH--CRARMvaGANFYIVGRDPAGMPhpetgkDLYEPsHGAKVL--T 547
Cdd:COG2046 241 YEALLENYY-PKDRVLLSGLPLAMRYAGPREALLHaiIRKNY--GCTHFIVGRDHAGVG------DYYGP-YDAQEIfdE 310

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46094058 548 MAPGLITLEIVPFRVAAYNKKKKRMDYYDSEHH--EDFEFISGTRMRKLAREGQKPPEGFMAPKAWTVLTEYYKSLEK 623
Cdd:COG2046 311 FPPGELGIEPLKFEEAFYCKKCGGMATSKTCPHdkEDRVSLSGTKVREMLREGEEPPPEFSRPEVAEILRKYYQPFGE 388
sat PRK04149
sulfate adenylyltransferase; Reviewed
 233-622 1.22e-61

sulfate adenylyltransferase; Reviewed


Pssm-ID: 235227  Cd Length: 391  Bit Score: 209.72  E-value: 1.22e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46094058  233 EVKELYVPENKLHLAKTDAETLPALKINKVDMQWVQVLAEGWATPLNGFMREREYLQCLHFDCLLDGGVinLSVPIVLTA 312
Cdd:PRK04149  10 ELVNRVVEGRDREEILEEAESLPRIELDERAASDLEMIAIGGFSPLTGFMGREDYDSVVEEMRLANGLV--WSIPITLDV 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46094058  313 THEDKERLDGCTAFALMYEGRRVAILRNPEFFEHRKEERCARQWGTTCKNHPYIKMVMEQGDWLIGGDLQVLDRVYwNDG 392
Cdd:PRK04149  88 SEEDAASLKEGDEVALVYKGEPYGVLEVEEIYTYDKKKEAEKVYKTTDEKHPGVKKLYEQGDVYLAGPVTLLNRKF-HEP 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46094058  393 LDQYRLTPTELKQKFKDMNADAVFAFQLRNPVHNGHALLMqdthKQLLE--RGyrrpvLLLHPLGGWTKDDDVPLMWRMK 470
Cdd:PRK04149 167 FPRFWLTPAETRELFEEKGWKTVVAFQTRNPPHRAHEYLQ----KCALEivDG-----LLLNPLVGETKSGDIPAEVRME 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46094058  471 QHAAVLeEGVLNPETTVVAIFPSPMMYAGPTEVQWHCRARMVAGANFYIVGRDPAGmphpeTGkDLYEP-------SHGA 543
Cdd:PRK04149 238 AYEALL-KNYYPKDRVLLSVTPAAMRYAGPREAIFHAIVRKNYGCTHFIVGRDHAG-----VG-DYYGPydaqeifDEFT 310

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46094058  544 KvltmaPGLITlEIVPFRVAAYNKKKKRMDY-----YDSEHHEDFefiSGTRMRKLAREGQKPPEGFMAPKAWTVLTEYY 618
Cdd:PRK04149 311 E-----EELGI-TPLKFEEAFYCPKCGGMASektcpHGKEDRVHL---SGTKVREMLREGEKPPPEFSRPEVAEVLIKGL 381


                 ....
gi 46094058  619 KSLE 622
Cdd:PRK04149 382 KKYG 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 46094058     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: 538.76  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46094058 254 LPALKINKVDMQWVQVLAEGWATPLNGFMREREYLQCLHFDCLLDGgvINLSVPIVLTATHEDKERLDGCTAFALMYEGR 333
Cdd:cd00517   1 LPSVELSERDLCDLEMLAEGGFSPLTGFMTEADYLSVLEEMRLLDG--TLWPIPIVLDVSEEDAKRLKEGERVALRYPGQ 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46094058 334 RVAILRNPEFFEHRKEERCARQWGTTCKNHPYIKMVMEQGDWLIGGDLQVLDRVYWNDgLDQYRLTPTELKQKFKDMNAD 413
Cdd:cd00517  79 PLAILTVEEIYEPDKEEEAARVFGTTDPHHPGVKKVMEQGDWLVGGPIEVLELPPFPD-FDQYRLTPAELRALFKERGWR 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46094058 414 AVFAFQLRNPVHNGHALLMQDTHKQLLergyrRPVLLLHPLGGWTKDDDVPLMWRMKQHAAVLEEGVLnPETTVVAIFPS 493
Cdd:cd00517 158 RVVAFQTRNPMHRAHEELMKRAAEKLL-----NDGLLLHPLVGWTKPGDVPDEVRMRAYEALLEEYYL-PERTVLAILPL 231

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46094058 494 PMMYAGPTEVQWHCRARMVAGANFYIVGRDPAGMPHPETGKDLYEPSHGAKVLTMApglITLEIVPFRVAAYNKKKKRMD 573
Cdd:cd00517 232 PMRYAGPREALWHAIIRKNYGATHFIVGRDHAGVGHPGDYYGPYDAQEIFKKLAPE---LGIEPVPFREAAYCPKCDGMA 308

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*
gi 46094058 574 YYDSE-HHEDFEFISGTRMRKLAREGQKPPEGFMAPKAWTVLTEY 617
Cdd:cd00517 309 SEDTCpHGEDFLNISGTKLRKMLREGEKPPEWFMRPEVAKVLREY 353
sopT TIGR00339
ATP sulphurylase; This enzyme forms adenosine 5'-phosphosulfate (APS) from ATP and free ...
 233-616 8.52e-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: 391.75  E-value: 8.52e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46094058   233 EVKELYV--PENKlHLAKTDAETLPALKINKVDMQWVQVLAEGWATPLNGFMREREYLQCLHFDCLLDGgvINLSVPIVL 310
Cdd:TIGR00339   5 KLVELVVrdPDEE-HKLLAEAESLPSITLSDRQLCDLELLGNGAFSPLEGFMNEADYDSVVESMRLSDG--VLFSVPITL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46094058   311 TATHEDKERLDGCTAFALMYE-GRRVAILRNPEFFEHRKEERCARQWGTTCKNHPYIKMVMEQGDWLIGGDLQVLDRVYW 389
Cdd:TIGR00339  82 DIDDEDADDIKLGDRIALTDPkGQPLAILTIEEVYKPNKEKEAKKVFGTTDPEHPGVVYLNTAGNYYIGGPIEVINLPKF 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46094058   390 nDGLDQYRLTPTELKQKFKDMNADAVFAFQLRNPVHNGHALLMQDThkqlLERGyRRPVLLLHPLGGWTKDDDVPLMWRM 469
Cdd:TIGR00339 162 -YDFPRFRFTPAELREEFKERGWDTVVAFQTRNPMHRAHEELTKRA----AERL-PNAGVLVHPLVGLTKPGDIPAEVRM 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46094058   470 KQHAaVLEEGVLNPETTVVAIFPSPMMYAGPTEVQWHCRARMVAGANFYIVGRDPAGMPHPETGKDLYEPSHGAKVLTMA 549
Cdd:TIGR00339 236 RAYE-VLKEGYPNPERTVVSFLPLAMRYAGPREAIWHAIIRKNYGATHFIVGRDHAGPGSNSKGQDFYGPYDAQELFEKY 314

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 46094058   550 PGLITLEIVPFRVAAYNKKKKRMDYYDS--EHHEDFEFISGTRMRKLAREGQKPPEGFMAPKAWTVLTE 616
Cdd:TIGR00339 315 KAELGIKIVPFRHVAYCPDEDEYAPADQagHTNLRTLNISGTKLRGMLRNGVFPPEWFSRPEVVKILRE 383
CysC COG0529
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ...
 33-227 1.94e-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: 326.66  E-value: 1.94e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46094058  33 HHVSRNKRGQvvgtRGGFRGCTVWLTGLSGAGKTTVSMALEEYLVCHGIPCYTLDGDNIRQGLNKNLGFSPEDREENVRR 112
Cdd:COG0529   1 SAVTREERAA----LKGQKGFVVWFTGLSGSGKSTLANALERRLFERGRHVYLLDGDNVRHGLNKDLGFSKEDRDENIRR 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46094058 113 IAEVAKLFADAGLVCITSFISPYTQDRNNARQIHEGAslPFFEVFVDAPLHVCEQRDVKGLYKKARAGEIKGFTGIDSEY 192
Cdd:COG0529  77 IGEVAKLLADAGLIVLVAFISPYRADREEARELIGEG--EFIEVYVDTPLEVCEARDPKGLYAKARAGEIKNFTGIDDPY 154

                       170       180       190
                ....*....|....*....|....*....|....*
gi 46094058 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 46094058    51 RGCTVWLTGLSGAGKTTVSMALEEYLVCHGIPCYTLDGDNIRQGLNKNLGFSPEDREENVRRIAEVAKLFADAGLVCITS 130
Cdd:pfam01583   1 RGCTIWLTGLSGAGKSTIANALERKLFEQGRSVYVLDGDNVRHGLNKDLGFSEEDRTENIRRIGEVAKLFADAGLIVITA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46094058   131 FISPYTQDRNNARQIHEGAslPFFEVFVDAPLHVCEQRDVKGLYKKARAGEIKGFTGIDSEYEKPEAPELVLKTD 205
Cdd:pfam01583  81 FISPYREDREQARELHEEG--KFIEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDSPYEAPENPELVLDTD 153
APSK cd02027
Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5 ...
 54-204 7.49e-103

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: 308.25  E-value: 7.49e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46094058  54 TVWLTGLSGAGKTTVSMALEEYLVCHGIPCYTLDGDNIRQGLNKNLGFSPEDREENVRRIAEVAKLFADAGLVCITSFIS 133
Cdd:cd02027   1 VIWLTGLSGSGKSTIARALEEKLFQRGRPVYVLDGDNVRHGLNKDLGFSREDREENIRRIAEVAKLLADAGLIVIAAFIS 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 46094058 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 2.28e-94

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: 289.05  E-value: 2.28e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46094058   394 DQYRLTPTELKQKFKDMNADAVFAFQLRNPVHNGHALLMQDTHKQLlERGYrrpvLLLHPLGGWTKDDDVPLMWRMKQHA 473
Cdd:pfam01747   1 DEYRLTPAETRALFKEKGWRTVVAFQTRNPLHRAHEELMKRALEEL-EADG----LLLHPLVGPTKPGDVPAEVRVRCYE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46094058   474 AVLEEgVLNPETTVVAIFPSPMMYAGPTEVQWHCRARMVAGANFYIVGRDPAGMPHpetgkdLYEPSHGAKVLTMAPGLI 553
Cdd:pfam01747  76 ALLEN-YLPPDRVVLALLPLAMRYAGPREALLHAIIRKNYGCTHFIVGRDHAGVGD------FYGPYDAQEIFDEYPGEL 148

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46094058   554 TLEIVPFRVAAYNKKKKRMDYYDSEHH-EDFEFISGTRMRKLAREGQKPPEGFMAPKAWTVLTEY 617
Cdd:pfam01747 149 GIEPVPFREAVYCKKCGEMASTKCPHGgEDRLFISGTKVRELLREGEEPPEWFSRPEVAKVLREY 213
PRK03846 PRK03846
adenylylsulfate kinase; Provisional
 26-226 6.96e-92

adenylylsulfate kinase; Provisional


Pssm-ID: 179661  Cd Length: 198  Bit Score: 281.83  E-value: 6.96e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46094058   26 TNVTYQAHHVSRNKRGQvvgtRGGFRGCTVWLTGLSGAGKTTVSMALEEYLVCHGIPCYTLDGDNIRQGLNKNLGFSPED 105
Cdd:PRK03846   2 ENIVWHQHPVTKAQREQ----LHGHKGVVLWFTGLSGSGKSTVAGALEEALHELGVSTYLLDGDNVRHGLCSDLGFSDAD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46094058  106 REENVRRIAEVAKLFADAGLVCITSFISPYTQDRNNARQIhegasLP---FFEVFVDAPLHVCEQRDVKGLYKKARAGEI 182
Cdd:PRK03846  78 RKENIRRVGEVAKLMVDAGLVVLTAFISPHRAERQMVRER-----LGegeFIEVFVDTPLAICEARDPKGLYKKARAGEI 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 46094058  183 KGFTGIDSEYEKPEAPELVLKTDSCDVNDCVQQVVELLQERDIV 226
Cdd:PRK03846 153 RNFTGIDSVYEAPESPEIHLDTGEQLVTNLVEQLLDYLRQRDII 196
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
 12-225 5.06e-89

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 289.14  E-value: 5.06e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46094058   12 KLSNNAQNWGM-----QRATNVTYQAHHVSRNKRGqvvgTRGGFRGCTVWLTGLSGAGKTTVSMALEEYLVCHGIPCYTL 86
Cdd:PRK05506 419 RLTNATVGAGMidfalRRATNVHWQASDVSREARA----ARKGQKPATVWFTGLSGSGKSTIANLVERRLHALGRHTYLL 494

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46094058   87 DGDNIRQGLNKNLGFSPEDREENVRRIAEVAKLFADAGLVCITSFISPYTQDRNNARQIHEGAslPFFEVFVDAPLHVCE 166
Cdd:PRK05506 495 DGDNVRHGLNRDLGFSDADRVENIRRVAEVARLMADAGLIVLVSFISPFREERELARALHGEG--EFVEVFVDTPLEVCE 572

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 46094058  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 3.93e-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: 263.94  E-value: 3.93e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46094058    34 HVSRNKRGQVVGTRGgfrgCTVWLTGLSGAGKTTVSMALEEYLVCHGIPCYTLDGDNIRQGLNKNLGFSPEDREENVRRI 113
Cdd:TIGR00455   4 AITKDERQALNGHRG----VVIWLTGLSGSGKSTIANALEKKLESKGYRVYVLDGDNVRHGLNKDLGFSEEDRKENIRRI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46094058   114 AEVAKLFADAGLVCITSFISPYTQDRNNARQIHEGASlpFFEVFVDAPLHVCEQRDVKGLYKKARAGEIKGFTGIDSEYE 193
Cdd:TIGR00455  80 GEVAKLFVRNGIIVITSFISPYRADRQMVRELIEKGE--FIEVFVDCPLEVCEQRDPKGLYKKARNGEIKGFTGIDSPYE 157

                         170       180
                  ....*....|....*....|....*..
gi 46094058   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 46094058   51 RGCTVWLTGLSGAGKTTVSMALEEYLVCHGIPCYTLDGDNIRQGLNKNLGFSPEDREENVRRIAEVAKLFADAGLVCITS 130
Cdd:PRK00889   3 RGVTVWFTGLSGAGKTTIARALAEKLREAGYPVEVLDGDAVRTNLSKGLGFSKEDRDTNIRRIGFVANLLTRHGVIVLVS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46094058  131 FISPYTQDRNNARqihegASLP-FFEVFVDAPLHVCEQRDVKGLYKKARAGEIKGFTGIDSEYEKPEAPELVLKTDSCDV 209
Cdd:PRK00889  83 AISPYRETREEVR-----ANIGnFLEVFVDAPLEVCEQRDVKGLYAKARAGEIKHFTGIDDPYEPPLNPEVECRTDLESL 157

                        170
                 ....*....|....*...
gi 46094058  210 NDCVQQVVELLQERDIVP 227
Cdd:PRK00889 158 EESVDKVLQKLEELGYLV 175
MET3 COG2046
ATP sulfurylase (sulfate adenylyltransferase) [Inorganic ion transport and metabolism]; ATP ...
 233-623 2.41e-69

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: 230.03  E-value: 2.41e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46094058 233 EVKELYVPENKLHLAKTDAETLPALKINKVDMQWVQVLAEGWATPLNGFMREREYLQCLHFDCLLDGGVinLSVPIVLTA 312
Cdd:COG2046  11 KLVNRVVPGEEREALLEEAKGLPSIELSSRALSDLEMIAIGGFSPLTGFMNKADYESVVENMRLADGLL--WPIPITLDV 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46094058 313 THEDKERLDGCTAFALM-YEGRRVAILRNPEFFEHRKEERCARQWGTTCKNHPYIKMVMEQGDWLIGGDLQVLDRVYWND 391
Cdd:COG2046  89 SEEDAAGLKEGDEVALRdEEGEPLAVLEVEEIYEYDKEEEAEKVYGTTDPAHPGVAKLYERGDVYLGGPITLLNRPKHPD 168

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46094058 392 gLDQYRLTPTELKQKFKDMNADAVFAFQLRNPVHNGHALLMqdthKQLLERGYrrpVLLLHPLGGWTKDDDVPLMWRMKQ 471
Cdd:COG2046 169 -FPDYRLTPAETRALFEEKGWKTVVAFQTRNPMHRAHEYLQ----KRALETVD---GLLIHPLVGETKPGDIPAEVRVRC 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46094058 472 HAAVLEEGVlNPETTVVAIFPSPMMYAGPTEVQWH--CRARMvaGANFYIVGRDPAGMPhpetgkDLYEPsHGAKVL--T 547
Cdd:COG2046 241 YEALLENYY-PKDRVLLSGLPLAMRYAGPREALLHaiIRKNY--GCTHFIVGRDHAGVG------DYYGP-YDAQEIfdE 310

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46094058 548 MAPGLITLEIVPFRVAAYNKKKKRMDYYDSEHH--EDFEFISGTRMRKLAREGQKPPEGFMAPKAWTVLTEYYKSLEK 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 6.76e-64

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: 207.37  E-value: 6.76e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46094058   233 EVKELYVPENKLHLAKTDAETLPALKINKVDMQWVQVLAEGWATPLNGFMREREYLQCLHFDCLLDGGVinLSVPIVLTA 312
Cdd:pfam14306   7 KLVDLVVRDAEREELLAEAAELPSIELSKRELCDLELIAIGGFSPLTGFMGEADYLSVLEFMRLADGLL--WSIPITLDV 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46094058   313 THEDKERLDGCTAFALMY-EGRRVAILRNPEFFEHRKEERCARQWGTTCKNHPYIKMVMEQGDWLIGGDLQVLDR 386
Cdd:pfam14306  85 SEEDAASLKEGDRVALRDpEGEPLAILTVEEIYEPDKEEEAEKVFGTTDPAHPGVKKLYEQGDFYVGGDIEVLNR 159
sat PRK04149
sulfate adenylyltransferase; Reviewed
 233-622 1.22e-61

sulfate adenylyltransferase; Reviewed


Pssm-ID: 235227  Cd Length: 391  Bit Score: 209.72  E-value: 1.22e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46094058  233 EVKELYVPENKLHLAKTDAETLPALKINKVDMQWVQVLAEGWATPLNGFMREREYLQCLHFDCLLDGGVinLSVPIVLTA 312
Cdd:PRK04149  10 ELVNRVVEGRDREEILEEAESLPRIELDERAASDLEMIAIGGFSPLTGFMGREDYDSVVEEMRLANGLV--WSIPITLDV 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46094058  313 THEDKERLDGCTAFALMYEGRRVAILRNPEFFEHRKEERCARQWGTTCKNHPYIKMVMEQGDWLIGGDLQVLDRVYwNDG 392
Cdd:PRK04149  88 SEEDAASLKEGDEVALVYKGEPYGVLEVEEIYTYDKKKEAEKVYKTTDEKHPGVKKLYEQGDVYLAGPVTLLNRKF-HEP 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46094058  393 LDQYRLTPTELKQKFKDMNADAVFAFQLRNPVHNGHALLMqdthKQLLE--RGyrrpvLLLHPLGGWTKDDDVPLMWRMK 470
Cdd:PRK04149 167 FPRFWLTPAETRELFEEKGWKTVVAFQTRNPPHRAHEYLQ----KCALEivDG-----LLLNPLVGETKSGDIPAEVRME 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46094058  471 QHAAVLeEGVLNPETTVVAIFPSPMMYAGPTEVQWHCRARMVAGANFYIVGRDPAGmphpeTGkDLYEP-------SHGA 543
Cdd:PRK04149 238 AYEALL-KNYYPKDRVLLSVTPAAMRYAGPREAIFHAIVRKNYGCTHFIVGRDHAG-----VG-DYYGPydaqeifDEFT 310

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46094058  544 KvltmaPGLITlEIVPFRVAAYNKKKKRMDY-----YDSEHHEDFefiSGTRMRKLAREGQKPPEGFMAPKAWTVLTEYY 618
Cdd:PRK04149 311 E-----EELGI-TPLKFEEAFYCPKCGGMASektcpHGKEDRVHL---SGTKVREMLREGEKPPPEFSRPEVAEVLIKGL 381


                 ....
gi 46094058  619 KSLE 622
Cdd:PRK04149 382 KKYG 385
PRK05537 PRK05537
bifunctional sulfate adenylyltransferase/adenylylsulfate kinase;
52-223 1.20e-58

bifunctional sulfate adenylyltransferase/adenylylsulfate kinase;


Pssm-ID: 180124 [Multi-domain]  Cd Length: 568  Bit Score: 206.45  E-value: 1.20e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46094058   52 GCTVWLTGLSGAGKTTVSMALEEYLVCHGIPCYT-LDGDNIRQGLNKNLGFSPEDREENVRRIAEVAKLFADAGLVCITS 130
Cdd:PRK05537 392 GFTVFFTGLSGAGKSTIAKALMVKLMEMRGRPVTlLDGDVVRKHLSSELGFSKEDRDLNILRIGFVASEITKNGGIAICA 471

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46094058  131 FISPYTQDRNNARQIHEGASlPFFEVFVDAPLHVCEQRDVKGLYKKARAGEIKGFTGIDSEYEKPEAPELVLKTDSCDVN 210
Cdd:PRK05537 472 PIAPYRATRREVREMIEAYG-GFIEVHVATPLEVCEQRDRKGLYAKAREGKIKGFTGISDPYEPPANPELVIDTTNVTPD 550

                        170
                 ....*....|...
gi 46094058  211 DCVQQVVELLQER 223
Cdd:PRK05537 551 ECAHKILLYLEEK 563
PRK05537 PRK05537
bifunctional sulfate adenylyltransferase/adenylylsulfate kinase;
236-623 4.44e-46

bifunctional sulfate adenylyltransferase/adenylylsulfate kinase;


Pssm-ID: 180124 [Multi-domain]  Cd Length: 568  Bit Score: 171.39  E-value: 4.44e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46094058  236 ELYVPENKLHLAKTDAETLPALKINKVDMQWVQVLAEGWATPLNGFMREREYLQCLHFDCLLDGGVinLSVPIVLTATHE 315
Cdd:PRK05537  11 NLYVSPESREKLKAEALSLPSLDLSPRQICDLELLMNGGFSPLKGFMGRADYECVLENMRLADGTL--WPIPITLDVSEK 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46094058  316 DKERLDGCTAFALM-YEGRRVAILRNPEFFEHRKEERCARQWGTTCKNHPYI-KMVMEQGDWLIGGDLQVLDR-VYWNdg 392
Cdd:PRK05537  89 FAAGLEIGERIALRdQEGVLLAILTVSDIWEPDKEREAEAVFGTTDPAHPGVnYLHRWAGKFYLGGPLTGIQLpVHYD-- 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46094058  393 LDQYRLTPTELKQKFKDMNADAVFAFQLRNPVHNGHallmqdthKQLLERGYRR--PVLLLHPLGGWTKDDDVPLMWRMK 470
Cdd:PRK05537 167 FVQLRLTPAELRARFRKLGWRRVVAFQTRNPLHRAH--------EELTKRAAREvgANLLIHPVVGMTKPGDIDHFTRVR 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46094058  471 QHAAVLEEgvLNPETTVVAIFPSPMMYAGPTEVQWHCRARMVAGANFYIVGRDPAGMPHPETGKDLYEPSHGAKVLTMAP 550
Cdd:PRK05537 239 CYEALLDK--YPPATTLLSLLPLAMRMAGPREALWHAIIRRNYGCTHFIVGRDHAGPGKDSRGKPFYGPYDAQELFAKYA 316

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46094058  551 GLITLEIVPFRVAAYNKKKKRmdYY---DSEHHEDFEFISGTRMRKLAREGQKPPEGFMAPKAWTVLTEYYKSLEK 623
Cdd:PRK05537 317 DEIGITMVPFKEMVYVQDKAQ--YVpvdEVPQGATVLTISGTELRRRLREGLEIPEWFSFPEVVAELRRTYPPRHK 390
PRK05541 PRK05541
adenylylsulfate kinase; Provisional
 52-225 5.99e-27

adenylylsulfate kinase; Provisional


Pssm-ID: 235498  Cd Length: 176  Bit Score: 107.45  E-value: 5.99e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46094058   52 GCTVWLTGLSGAGKTTVSMALEEYLVCHGIPCYTLDGDNIRQGLNKNlGFSPEDREENVRRIAEVAKLFADAGLVCITSF 131
Cdd:PRK05541   7 GYVIWITGLAGSGKTTIAKALYERLKLKYSNVIYLDGDELREILGHY-GYDKQSRIEMALKRAKLAKFLADQGMIVIVTT 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46094058  132 ISPYTQDRNNARQIHEGaslpFFEVFVDAPLHVCEQRDVKGLYKKARAGEIKGFTGIDSEYEKPEAPELVLKTDSCDVND 211
Cdd:PRK05541  86 ISMFDEIYAYNRKHLPN----YFEVYLKCDMEELIRRDQKGLYTKALKGEIKNVVGVDIPFDEPKADLVIDNSCRTSLDE 161

                        170
                 ....*....|....
gi 46094058  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 46094058  57 LTGLSGAGKTTVSMALEEYLVCHGIPCYTLDGDNIRQGLnKNLGFSPEDREENVRRIAE-VAKLFADAGLVCIT--SFIS 133
Cdd:COG4088   9 LTGPPGSGKTTFAKALAQRLYAEGIAVALLHSDDFRRFL-VNESFPKETYEEVVEDVRTtTADNALDNGYSVIVdgTFYY 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46094058 134 PYTQDRnnARQIHEGASlPFFEVFVDAPLHVCEQRDVkglykkARAGEI--KGFTGIDSEYEKPE---APELVLKTDSCD 208
Cdd:COG4088  88 RSWQRD--FRNLAKHKA-PIHIIYLKAPLETALRRNR------ERGEPIpeRVIARMYRKFDKPGtkdRPDLVIDTTEDS 158

                       170
                ....*....|....*
gi 46094058 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 3.75e-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: 3.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46094058    55 VWLTGLSGAGKTTVSMALEEYLvchgiPCYTLDGDNIRQGLNKNLGFSPEDREEN----VRRIAEVAKLFADAGLVCI-- 128
Cdd:pfam13671   2 ILLVGLPGSGKSTLARRLLEEL-----GAVRLSSDDERKRLFGEGRPSISYYTDAtdrtYERLHELARIALRAGRPVIld 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46094058   129 TSFISPytQDRNNARQIHEGASLPFFEVFVDAPLHVCEQRDvkglykKARAgeikgftgiDSEYEKPEAPELVLKT 204
Cdd:pfam13671  77 ATNLRR--DERARLLALAREYGVPVRIVVFEAPEEVLRERL------AARA---------RAGGDPSDVPEEVLDR 135
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
55-168 7.48e-09

Predicted kinase, contains AAA domain [General function prediction only];


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 55.30  E-value: 7.48e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46094058  55 VWLTGLSGAGKTTVSMALEEYL-VCHgipcytLDGDNIRQGLnKNLGFSPEDREENVR-----RIAEVAKLFADAGLVCI 128
Cdd:COG0645   2 ILVCGLPGSGKSTLARALAERLgAVR------LRSDVVRKRL-FGAGLAPLERSPEATartyaRLLALARELLAAGRSVI 74

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 46094058 129 TSFISPYTQDRNNARQIHEGASLPFFEVFVDAPLHVCEQR 168
Cdd:COG0645  75 LDATFLRRAQREAFRALAEEAGAPFVLIWLDAPEEVLRER 114
CmkB COG1102
Cytidylate kinase [Nucleotide transport and metabolism];
59-225 8.55e-07

Cytidylate kinase [Nucleotide transport and metabolism];


Pssm-ID: 440719 [Multi-domain]  Cd Length: 188  Bit Score: 49.82  E-value: 8.55e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46094058  59 GLSGAGKTTVSMALEEYLvchGIPCYtlDGDNIRQgLNKNLGFSPEDREEN------------------VRRIAEVAKLF 120
Cdd:COG1102   7 REPGSGGTTIAKRLAEKL---GLPLY--DGEILRE-AAKERGLSEEEFEKLdekapsllyrdtaeedeiDRALDKVIREL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46094058 121 ADAGLVCITSFISPY-TQDRNNArqIHegaslpffeVFVDAPLHVCEQR-------DVKGLYK------KARAGEIKGFT 186
Cdd:COG1102  81 ARKGNCVIVGRLADWiLRDRPNV--LK---------VFLTAPLEVRVKRiaeregiSEEEAEKeikkrdKSRAKYYKYYY 149

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 46094058 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 46094058     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 3.55e-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: 41.47  E-value: 3.55e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46094058  57 LTGLSGAGKTTVSMALEEYLVCHGIpcytlDGDNIRQGLNK-----NLGFSPEDRE---ENVRRIAEVAKLFADAGLVCI 128
Cdd:cd02021   4 VMGVSGSGKSTVGKALAERLGAPFI-----DGDDLHPPANIakmaaGIPLNDEDRWpwlQALTDALLAKLASAGEGVVVA 78

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 46094058 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 46094058  54 TVWLTGLSGAGKTTVSMALEEYLVCHGIPCYT----LDGdnirqglnknLGFSPEDREENVRRIAEVaKLFADAGLV 126
Cdd:cd02019   1 IIAITGGSGSGKSTVAKKLAEQLGGRSVVVLDeiviLEG----------LYASYKSRDARIRDLADL-KIYLDADLV 66
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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