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Conserved domains on  [gi|767933021|ref|XP_011530703|]
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bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 1 isoform X1 [Homo sapiens]

Protein Classification

APSK and ATPS domain-containing protein( domain architecture ID 10785574)

APSK and ATPS domain-containing protein

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, ...
 233-596 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 767933021 233 LPALKINKVDMQWVQVLAEGWATPLNGFMREREYLQCLHFDCLLDGgvINLSVPIVLTATHEDKERLDGCTAFALMYEGR 312
Cdd:cd00517    1 LPSVELSERDLCDLEMLAEGGFSPLTGFMTEADYLSVLEEMRLLDG--TLWPIPIVLDVSEEDAKRLKEGERVALRYPGQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767933021 313 RVAILRNPEFFEHRKEERCARQWGTTCKNHPYIKMVMEQGDWLIGGDLQVLDRVYWNDgLDQYRLTPTELKQKFKDMNAD 392
Cdd:cd00517   79 PLAILTVEEIYEPDKEEEAARVFGTTDPHHPGVKKVMEQGDWLVGGPIEVLELPPFPD-FDQYRLTPAELRALFKERGWR 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767933021 393 AVFAFQLRNPVHNGHALLMQDTHKQLLergyrRPVLLLHPLGGWTKDDDVPLMWRMKQHAAVLEEGVLnPETTVVAIFPS 472
Cdd:cd00517  158 RVVAFQTRNPMHRAHEELMKRAAEKLL-----NDGLLLHPLVGWTKPGDVPDEVRMRAYEALLEEYYL-PERTVLAILPL 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767933021 473 PMMYAGPTEVQWHCRARMVAGANFYIVGRDPAGMPHPETGKDLYEPSHGAKVLTMApglITLEIVPFRVAAYNKKKKRMD 552
Cdd:cd00517  232 PMRYAGPREALWHAIIRKNYGATHFIVGRDHAGVGHPGDYYGPYDAQEIFKKLAPE---LGIEPVPFREAAYCPKCDGMA 308

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 767933021 553 YYDSE-HHEDFEFISGTRMRKLAREGQKPPEGFMAPKAWTVLTEY 596
Cdd:cd00517  309 SEDTCpHGEDFLNISGTKLRKMLREGEKPPEWFMRPEVAKVLREY 353
CysC COG0529
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ...
 12-206 2.02e-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: 325.89  E-value: 2.02e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767933021  12 HHVSRNKRGQvvgtRGGFRGCTVWLTGLSGAGKTTVSMALEEYLVCHGIPCYTLDGDNIRQGLNKNLGFSPEDREENVRR 91
Cdd:COG0529    1 SAVTREERAA----LKGQKGFVVWFTGLSGSGKSTLANALERRLFERGRHVYLLDGDNVRHGLNKDLGFSKEDRDENIRR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767933021  92 IAEVAKLFADAGLVCITSFISPYTQDRNNARQIHEGAslPFFEVFVDAPLHVCEQRDVKGLYKKARAGEIKGFTGIDSEY 171
Cdd:COG0529   77 IGEVAKLLADAGLIVLVAFISPYRADREEARELIGEG--EFIEVYVDTPLEVCEARDPKGLYAKARAGEIKNFTGIDDPY 154

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 767933021 172 EKPEAPELVLKTDSCDVNDCVQQVVELLQERDIVP 206
Cdd:COG0529  155 EAPENPELVLDTDKESVEESVEKILAYLEERGYIS 189
 
Name Accession Description Interval E-value
ATPS cd00517
ATP-sulfurylase; ATP-sulfurylase (ATPS), also known as sulfate adenylate transferase, ...
 233-596 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 767933021 233 LPALKINKVDMQWVQVLAEGWATPLNGFMREREYLQCLHFDCLLDGgvINLSVPIVLTATHEDKERLDGCTAFALMYEGR 312
Cdd:cd00517    1 LPSVELSERDLCDLEMLAEGGFSPLTGFMTEADYLSVLEEMRLLDG--TLWPIPIVLDVSEEDAKRLKEGERVALRYPGQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767933021 313 RVAILRNPEFFEHRKEERCARQWGTTCKNHPYIKMVMEQGDWLIGGDLQVLDRVYWNDgLDQYRLTPTELKQKFKDMNAD 392
Cdd:cd00517   79 PLAILTVEEIYEPDKEEEAARVFGTTDPHHPGVKKVMEQGDWLVGGPIEVLELPPFPD-FDQYRLTPAELRALFKERGWR 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767933021 393 AVFAFQLRNPVHNGHALLMQDTHKQLLergyrRPVLLLHPLGGWTKDDDVPLMWRMKQHAAVLEEGVLnPETTVVAIFPS 472
Cdd:cd00517  158 RVVAFQTRNPMHRAHEELMKRAAEKLL-----NDGLLLHPLVGWTKPGDVPDEVRMRAYEALLEEYYL-PERTVLAILPL 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767933021 473 PMMYAGPTEVQWHCRARMVAGANFYIVGRDPAGMPHPETGKDLYEPSHGAKVLTMApglITLEIVPFRVAAYNKKKKRMD 552
Cdd:cd00517  232 PMRYAGPREALWHAIIRKNYGATHFIVGRDHAGVGHPGDYYGPYDAQEIFKKLAPE---LGIEPVPFREAAYCPKCDGMA 308

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 767933021 553 YYDSE-HHEDFEFISGTRMRKLAREGQKPPEGFMAPKAWTVLTEY 596
Cdd:cd00517  309 SEDTCpHGEDFLNISGTKLRKMLREGEKPPEWFMRPEVAKVLREY 353
sopT TIGR00339
ATP sulphurylase; This enzyme forms adenosine 5'-phosphosulfate (APS) from ATP and free ...
 212-595 1.40e-131

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: 390.21  E-value: 1.40e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767933021  212 EVKELYV--PENKlHLAKTDAETLPALKINKVDMQWVQVLAEGWATPLNGFMREREYLQCLHFDCLLDGgvINLSVPIVL 289
Cdd:TIGR00339   5 KLVELVVrdPDEE-HKLLAEAESLPSITLSDRQLCDLELLGNGAFSPLEGFMNEADYDSVVESMRLSDG--VLFSVPITL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767933021  290 TATHEDKERLDGCTAFALMYE-GRRVAILRNPEFFEHRKEERCARQWGTTCKNHPYIKMVMEQGDWLIGGDLQVLDRVYW 368
Cdd:TIGR00339  82 DIDDEDADDIKLGDRIALTDPkGQPLAILTIEEVYKPNKEKEAKKVFGTTDPEHPGVVYLNTAGNYYIGGPIEVINLPKF 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767933021  369 nDGLDQYRLTPTELKQKFKDMNADAVFAFQLRNPVHNGHALLMQDThkqlLERGyRRPVLLLHPLGGWTKDDDVPLMWRM 448
Cdd:TIGR00339 162 -YDFPRFRFTPAELREEFKERGWDTVVAFQTRNPMHRAHEELTKRA----AERL-PNAGVLVHPLVGLTKPGDIPAEVRM 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767933021  449 KQHAaVLEEGVLNPETTVVAIFPSPMMYAGPTEVQWHCRARMVAGANFYIVGRDPAGMPHPETGKDLYEPSHGAKVLTMA 528
Cdd:TIGR00339 236 RAYE-VLKEGYPNPERTVVSFLPLAMRYAGPREAIWHAIIRKNYGATHFIVGRDHAGPGSNSKGQDFYGPYDAQELFEKY 314

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767933021  529 PGLITLEIVPFRVAAYNKKKKRMDYYDS--EHHEDFEFISGTRMRKLAREGQKPPEGFMAPKAWTVLTE 595
Cdd:TIGR00339 315 KAELGIKIVPFRHVAYCPDEDEYAPADQagHTNLRTLNISGTKLRGMLRNGVFPPEWFSRPEVVKILRE 383
CysC COG0529
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ...
 12-206 2.02e-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: 325.89  E-value: 2.02e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767933021  12 HHVSRNKRGQvvgtRGGFRGCTVWLTGLSGAGKTTVSMALEEYLVCHGIPCYTLDGDNIRQGLNKNLGFSPEDREENVRR 91
Cdd:COG0529    1 SAVTREERAA----LKGQKGFVVWFTGLSGSGKSTLANALERRLFERGRHVYLLDGDNVRHGLNKDLGFSKEDRDENIRR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767933021  92 IAEVAKLFADAGLVCITSFISPYTQDRNNARQIHEGAslPFFEVFVDAPLHVCEQRDVKGLYKKARAGEIKGFTGIDSEY 171
Cdd:COG0529   77 IGEVAKLLADAGLIVLVAFISPYRADREEARELIGEG--EFIEVYVDTPLEVCEARDPKGLYAKARAGEIKNFTGIDDPY 154

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 767933021 172 EKPEAPELVLKTDSCDVNDCVQQVVELLQERDIVP 206
Cdd:COG0529  155 EAPENPELVLDTDKESVEESVEKILAYLEERGYIS 189
APS_kinase pfam01583
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3 ...
 30-184 2.19e-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: 2.19e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767933021   30 RGCTVWLTGLSGAGKTTVSMALEEYLVCHGIPCYTLDGDNIRQGLNKNLGFSPEDREENVRRIAEVAKLFADAGLVCITS 109
Cdd:pfam01583   1 RGCTIWLTGLSGAGKSTIANALERKLFEQGRSVYVLDGDNVRHGLNKDLGFSEEDRTENIRRIGEVAKLFADAGLIVITA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767933021  110 FISPYTQDRNNARQIHEGAslPFFEVFVDAPLHVCEQRDVKGLYKKARAGEIKGFTGIDSEYEKPEAPELVLKTD 184
Cdd:pfam01583  81 FISPYREDREQARELHEEG--KFIEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDSPYEAPENPELVLDTD 153
APSK cd02027
Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5 ...
 33-183 9.26e-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: 307.48  E-value: 9.26e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767933021  33 TVWLTGLSGAGKTTVSMALEEYLVCHGIPCYTLDGDNIRQGLNKNLGFSPEDREENVRRIAEVAKLFADAGLVCITSFIS 112
Cdd:cd02027    1 VIWLTGLSGSGKSTIARALEEKLFQRGRPVYVLDGDNVRHGLNKDLGFSREDREENIRRIAEVAKLLADAGLIVIAAFIS 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767933021 113 PYTQDRNNARQIHEGasLPFFEVFVDAPLHVCEQRDVKGLYKKARAGEIKGFTGIDSEYEKPEAPELVLKT 183
Cdd:cd02027   81 PYREDREAARKIIGG--GDFLEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDDPYEAPENPDLVLDT 149
ATP-sulfurylase pfam01747
ATP-sulfurylase; This domain is the catalytic domain of ATP-sulfurylase or sulfate ...
 373-596 4.38e-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: 287.51  E-value: 4.38e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767933021  373 DQYRLTPTELKQKFKDMNADAVFAFQLRNPVHNGHALLMQDTHKQLlERGYrrpvLLLHPLGGWTKDDDVPLMWRMKQHA 452
Cdd:pfam01747   1 DEYRLTPAETRALFKEKGWRTVVAFQTRNPLHRAHEELMKRALEEL-EADG----LLLHPLVGPTKPGDVPAEVRVRCYE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767933021  453 AVLEEgVLNPETTVVAIFPSPMMYAGPTEVQWHCRARMVAGANFYIVGRDPAGMPHpetgkdLYEPSHGAKVLTMAPGLI 532
Cdd:pfam01747  76 ALLEN-YLPPDRVVLALLPLAMRYAGPREALLHAIIRKNYGCTHFIVGRDHAGVGD------FYGPYDAQEIFDEYPGEL 148

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767933021  533 TLEIVPFRVAAYNKKKKRMDYYDSEHH-EDFEFISGTRMRKLAREGQKPPEGFMAPKAWTVLTEY 596
Cdd:pfam01747 149 GIEPVPFREAVYCKKCGEMASTKCPHGgEDRLFISGTKVRELLREGEEPPEWFSRPEVAKVLREY 213
PRK03846 PRK03846
adenylylsulfate kinase; Provisional
 5-205 7.72e-92

adenylylsulfate kinase; Provisional


Pssm-ID: 179661  Cd Length: 198  Bit Score: 281.06  E-value: 7.72e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767933021   5 TNVTYQAHHVSRNKRGQvvgtRGGFRGCTVWLTGLSGAGKTTVSMALEEYLVCHGIPCYTLDGDNIRQGLNKNLGFSPED 84
Cdd:PRK03846   2 ENIVWHQHPVTKAQREQ----LHGHKGVVLWFTGLSGSGKSTVAGALEEALHELGVSTYLLDGDNVRHGLCSDLGFSDAD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767933021  85 REENVRRIAEVAKLFADAGLVCITSFISPYTQDRNNARQIhegasLP---FFEVFVDAPLHVCEQRDVKGLYKKARAGEI 161
Cdd:PRK03846  78 RKENIRRVGEVAKLMVDAGLVVLTAFISPHRAERQMVRER-----LGegeFIEVFVDTPLAICEARDPKGLYKKARAGEI 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 767933021 162 KGFTGIDSEYEKPEAPELVLKTDSCDVNDCVQQVVELLQERDIV 205
Cdd:PRK03846 153 RNFTGIDSVYEAPESPEIHLDTGEQLVTNLVEQLLDYLRQRDII 196
apsK TIGR00455
adenylyl-sulfate kinase; This protein, adenylylsulfate kinase, is often found as a fusion ...
 13-199 3.46e-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: 3.46e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767933021   13 HVSRNKRGQVVGTRGgfrgCTVWLTGLSGAGKTTVSMALEEYLVCHGIPCYTLDGDNIRQGLNKNLGFSPEDREENVRRI 92
Cdd:TIGR00455   4 AITKDERQALNGHRG----VVIWLTGLSGSGKSTIANALEKKLESKGYRVYVLDGDNVRHGLNKDLGFSEEDRKENIRRI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767933021   93 AEVAKLFADAGLVCITSFISPYTQDRNNARQIHEGASlpFFEVFVDAPLHVCEQRDVKGLYKKARAGEIKGFTGIDSEYE 172
Cdd:TIGR00455  80 GEVAKLFVRNGIIVITSFISPYRADRQMVRELIEKGE--FIEVFVDCPLEVCEQRDPKGLYKKARNGEIKGFTGIDSPYE 157

                         170       180
                  ....*....|....*....|....*..
gi 767933021  173 KPEAPELVLKTDSCDVNDCVQQVVELL 199
Cdd:TIGR00455 158 APENPEVVLDTDQNDREECVGQIIEKL 184
MET3 COG2046
ATP sulfurylase (sulfate adenylyltransferase) [Inorganic ion transport and metabolism]; ATP ...
 212-602 3.78e-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: 228.87  E-value: 3.78e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767933021 212 EVKELYVPENKLHLAKTDAETLPALKINKVDMQWVQVLAEGWATPLNGFMREREYLQCLHFDCLLDGGVinLSVPIVLTA 291
Cdd:COG2046   11 KLVNRVVPGEEREALLEEAKGLPSIELSSRALSDLEMIAIGGFSPLTGFMNKADYESVVENMRLADGLL--WPIPITLDV 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767933021 292 THEDKERLDGCTAFALM-YEGRRVAILRNPEFFEHRKEERCARQWGTTCKNHPYIKMVMEQGDWLIGGDLQVLDRVYWND 370
Cdd:COG2046   89 SEEDAAGLKEGDEVALRdEEGEPLAVLEVEEIYEYDKEEEAEKVYGTTDPAHPGVAKLYERGDVYLGGPITLLNRPKHPD 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767933021 371 gLDQYRLTPTELKQKFKDMNADAVFAFQLRNPVHNGHALLMqdthKQLLERGYrrpVLLLHPLGGWTKDDDVPLMWRMKQ 450
Cdd:COG2046  169 -FPDYRLTPAETRALFEEKGWKTVVAFQTRNPMHRAHEYLQ----KRALETVD---GLLIHPLVGETKPGDIPAEVRVRC 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767933021 451 HAAVLEEGVlNPETTVVAIFPSPMMYAGPTEVQWH--CRARMvaGANFYIVGRDPAGMPhpetgkDLYEPsHGAKVL--T 526
Cdd:COG2046  241 YEALLENYY-PKDRVLLSGLPLAMRYAGPREALLHaiIRKNY--GCTHFIVGRDHAGVG------DYYGP-YDAQEIfdE 310

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767933021 527 MAPGLITLEIVPFRVAAYNKKKKRMDYYDSEHH--EDFEFISGTRMRKLAREGQKPPEGFMAPKAWTVLTEYYKSLEK 602
Cdd:COG2046  311 FPPGELGIEPLKFEEAFYCKKCGGMATSKTCPHdkEDRVSLSGTKVREMLREGEEPPPEFSRPEVAEILRKYYQPFGE 388
sat PRK04149
sulfate adenylyltransferase; Reviewed
 212-601 1.77e-61

sulfate adenylyltransferase; Reviewed


Pssm-ID: 235227  Cd Length: 391  Bit Score: 208.56  E-value: 1.77e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767933021 212 EVKELYVPENKLHLAKTDAETLPALKINKVDMQWVQVLAEGWATPLNGFMREREYLQCLHFDCLLDGGVinLSVPIVLTA 291
Cdd:PRK04149  10 ELVNRVVEGRDREEILEEAESLPRIELDERAASDLEMIAIGGFSPLTGFMGREDYDSVVEEMRLANGLV--WSIPITLDV 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767933021 292 THEDKERLDGCTAFALMYEGRRVAILRNPEFFEHRKEERCARQWGTTCKNHPYIKMVMEQGDWLIGGDLQVLDRVYwNDG 371
Cdd:PRK04149  88 SEEDAASLKEGDEVALVYKGEPYGVLEVEEIYTYDKKKEAEKVYKTTDEKHPGVKKLYEQGDVYLAGPVTLLNRKF-HEP 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767933021 372 LDQYRLTPTELKQKFKDMNADAVFAFQLRNPVHNGHALLMqdthKQLLE--RGyrrpvLLLHPLGGWTKDDDVPLMWRMK 449
Cdd:PRK04149 167 FPRFWLTPAETRELFEEKGWKTVVAFQTRNPPHRAHEYLQ----KCALEivDG-----LLLNPLVGETKSGDIPAEVRME 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767933021 450 QHAAVLeEGVLNPETTVVAIFPSPMMYAGPTEVQWHCRARMVAGANFYIVGRDPAGmphpeTGkDLYEP-------SHGA 522
Cdd:PRK04149 238 AYEALL-KNYYPKDRVLLSVTPAAMRYAGPREAIFHAIVRKNYGCTHFIVGRDHAG-----VG-DYYGPydaqeifDEFT 310

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767933021 523 KvltmaPGLITlEIVPFRVAAYNKKKKRMDY-----YDSEHHEDFefiSGTRMRKLAREGQKPPEGFMAPKAWTVLTEYY 597
Cdd:PRK04149 311 E-----EELGI-TPLKFEEAFYCPKCGGMASektcpHGKEDRVHL---SGTKVREMLREGEKPPPEFSRPEVAEVLIKGL 381


                 ....
gi 767933021 598 KSLE 601
Cdd:PRK04149 382 KKYG 385
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 36-102 3.22e-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: 3.22e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767933021    36 LTGLSGAGKTTVSMALEEYLVCHGIPCYTLDGDNIRQG-LNKNLGFSPEDREENVRRIAEVAKLFADA 102
Cdd:smart00382   7 IVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEvLDQLLLIIVGGKKASGSGELRLRLALALA 74
 
Name Accession Description Interval E-value
ATPS cd00517
ATP-sulfurylase; ATP-sulfurylase (ATPS), also known as sulfate adenylate transferase, ...
 233-596 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 767933021 233 LPALKINKVDMQWVQVLAEGWATPLNGFMREREYLQCLHFDCLLDGgvINLSVPIVLTATHEDKERLDGCTAFALMYEGR 312
Cdd:cd00517    1 LPSVELSERDLCDLEMLAEGGFSPLTGFMTEADYLSVLEEMRLLDG--TLWPIPIVLDVSEEDAKRLKEGERVALRYPGQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767933021 313 RVAILRNPEFFEHRKEERCARQWGTTCKNHPYIKMVMEQGDWLIGGDLQVLDRVYWNDgLDQYRLTPTELKQKFKDMNAD 392
Cdd:cd00517   79 PLAILTVEEIYEPDKEEEAARVFGTTDPHHPGVKKVMEQGDWLVGGPIEVLELPPFPD-FDQYRLTPAELRALFKERGWR 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767933021 393 AVFAFQLRNPVHNGHALLMQDTHKQLLergyrRPVLLLHPLGGWTKDDDVPLMWRMKQHAAVLEEGVLnPETTVVAIFPS 472
Cdd:cd00517  158 RVVAFQTRNPMHRAHEELMKRAAEKLL-----NDGLLLHPLVGWTKPGDVPDEVRMRAYEALLEEYYL-PERTVLAILPL 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767933021 473 PMMYAGPTEVQWHCRARMVAGANFYIVGRDPAGMPHPETGKDLYEPSHGAKVLTMApglITLEIVPFRVAAYNKKKKRMD 552
Cdd:cd00517  232 PMRYAGPREALWHAIIRKNYGATHFIVGRDHAGVGHPGDYYGPYDAQEIFKKLAPE---LGIEPVPFREAAYCPKCDGMA 308

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 767933021 553 YYDSE-HHEDFEFISGTRMRKLAREGQKPPEGFMAPKAWTVLTEY 596
Cdd:cd00517  309 SEDTCpHGEDFLNISGTKLRKMLREGEKPPEWFMRPEVAKVLREY 353
sopT TIGR00339
ATP sulphurylase; This enzyme forms adenosine 5'-phosphosulfate (APS) from ATP and free ...
 212-595 1.40e-131

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: 390.21  E-value: 1.40e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767933021  212 EVKELYV--PENKlHLAKTDAETLPALKINKVDMQWVQVLAEGWATPLNGFMREREYLQCLHFDCLLDGgvINLSVPIVL 289
Cdd:TIGR00339   5 KLVELVVrdPDEE-HKLLAEAESLPSITLSDRQLCDLELLGNGAFSPLEGFMNEADYDSVVESMRLSDG--VLFSVPITL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767933021  290 TATHEDKERLDGCTAFALMYE-GRRVAILRNPEFFEHRKEERCARQWGTTCKNHPYIKMVMEQGDWLIGGDLQVLDRVYW 368
Cdd:TIGR00339  82 DIDDEDADDIKLGDRIALTDPkGQPLAILTIEEVYKPNKEKEAKKVFGTTDPEHPGVVYLNTAGNYYIGGPIEVINLPKF 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767933021  369 nDGLDQYRLTPTELKQKFKDMNADAVFAFQLRNPVHNGHALLMQDThkqlLERGyRRPVLLLHPLGGWTKDDDVPLMWRM 448
Cdd:TIGR00339 162 -YDFPRFRFTPAELREEFKERGWDTVVAFQTRNPMHRAHEELTKRA----AERL-PNAGVLVHPLVGLTKPGDIPAEVRM 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767933021  449 KQHAaVLEEGVLNPETTVVAIFPSPMMYAGPTEVQWHCRARMVAGANFYIVGRDPAGMPHPETGKDLYEPSHGAKVLTMA 528
Cdd:TIGR00339 236 RAYE-VLKEGYPNPERTVVSFLPLAMRYAGPREAIWHAIIRKNYGATHFIVGRDHAGPGSNSKGQDFYGPYDAQELFEKY 314

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767933021  529 PGLITLEIVPFRVAAYNKKKKRMDYYDS--EHHEDFEFISGTRMRKLAREGQKPPEGFMAPKAWTVLTE 595
Cdd:TIGR00339 315 KAELGIKIVPFRHVAYCPDEDEYAPADQagHTNLRTLNISGTKLRGMLRNGVFPPEWFSRPEVVKILRE 383
CysC COG0529
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ...
 12-206 2.02e-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: 325.89  E-value: 2.02e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767933021  12 HHVSRNKRGQvvgtRGGFRGCTVWLTGLSGAGKTTVSMALEEYLVCHGIPCYTLDGDNIRQGLNKNLGFSPEDREENVRR 91
Cdd:COG0529    1 SAVTREERAA----LKGQKGFVVWFTGLSGSGKSTLANALERRLFERGRHVYLLDGDNVRHGLNKDLGFSKEDRDENIRR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767933021  92 IAEVAKLFADAGLVCITSFISPYTQDRNNARQIHEGAslPFFEVFVDAPLHVCEQRDVKGLYKKARAGEIKGFTGIDSEY 171
Cdd:COG0529   77 IGEVAKLLADAGLIVLVAFISPYRADREEARELIGEG--EFIEVYVDTPLEVCEARDPKGLYAKARAGEIKNFTGIDDPY 154

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 767933021 172 EKPEAPELVLKTDSCDVNDCVQQVVELLQERDIVP 206
Cdd:COG0529  155 EAPENPELVLDTDKESVEESVEKILAYLEERGYIS 189
APS_kinase pfam01583
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3 ...
 30-184 2.19e-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: 2.19e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767933021   30 RGCTVWLTGLSGAGKTTVSMALEEYLVCHGIPCYTLDGDNIRQGLNKNLGFSPEDREENVRRIAEVAKLFADAGLVCITS 109
Cdd:pfam01583   1 RGCTIWLTGLSGAGKSTIANALERKLFEQGRSVYVLDGDNVRHGLNKDLGFSEEDRTENIRRIGEVAKLFADAGLIVITA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767933021  110 FISPYTQDRNNARQIHEGAslPFFEVFVDAPLHVCEQRDVKGLYKKARAGEIKGFTGIDSEYEKPEAPELVLKTD 184
Cdd:pfam01583  81 FISPYREDREQARELHEEG--KFIEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDSPYEAPENPELVLDTD 153
APSK cd02027
Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5 ...
 33-183 9.26e-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: 307.48  E-value: 9.26e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767933021  33 TVWLTGLSGAGKTTVSMALEEYLVCHGIPCYTLDGDNIRQGLNKNLGFSPEDREENVRRIAEVAKLFADAGLVCITSFIS 112
Cdd:cd02027    1 VIWLTGLSGSGKSTIARALEEKLFQRGRPVYVLDGDNVRHGLNKDLGFSREDREENIRRIAEVAKLLADAGLIVIAAFIS 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767933021 113 PYTQDRNNARQIHEGasLPFFEVFVDAPLHVCEQRDVKGLYKKARAGEIKGFTGIDSEYEKPEAPELVLKT 183
Cdd:cd02027   81 PYREDREAARKIIGG--GDFLEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDDPYEAPENPDLVLDT 149
ATP-sulfurylase pfam01747
ATP-sulfurylase; This domain is the catalytic domain of ATP-sulfurylase or sulfate ...
 373-596 4.38e-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: 287.51  E-value: 4.38e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767933021  373 DQYRLTPTELKQKFKDMNADAVFAFQLRNPVHNGHALLMQDTHKQLlERGYrrpvLLLHPLGGWTKDDDVPLMWRMKQHA 452
Cdd:pfam01747   1 DEYRLTPAETRALFKEKGWRTVVAFQTRNPLHRAHEELMKRALEEL-EADG----LLLHPLVGPTKPGDVPAEVRVRCYE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767933021  453 AVLEEgVLNPETTVVAIFPSPMMYAGPTEVQWHCRARMVAGANFYIVGRDPAGMPHpetgkdLYEPSHGAKVLTMAPGLI 532
Cdd:pfam01747  76 ALLEN-YLPPDRVVLALLPLAMRYAGPREALLHAIIRKNYGCTHFIVGRDHAGVGD------FYGPYDAQEIFDEYPGEL 148

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767933021  533 TLEIVPFRVAAYNKKKKRMDYYDSEHH-EDFEFISGTRMRKLAREGQKPPEGFMAPKAWTVLTEY 596
Cdd:pfam01747 149 GIEPVPFREAVYCKKCGEMASTKCPHGgEDRLFISGTKVRELLREGEEPPEWFSRPEVAKVLREY 213
PRK03846 PRK03846
adenylylsulfate kinase; Provisional
 5-205 7.72e-92

adenylylsulfate kinase; Provisional


Pssm-ID: 179661  Cd Length: 198  Bit Score: 281.06  E-value: 7.72e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767933021   5 TNVTYQAHHVSRNKRGQvvgtRGGFRGCTVWLTGLSGAGKTTVSMALEEYLVCHGIPCYTLDGDNIRQGLNKNLGFSPED 84
Cdd:PRK03846   2 ENIVWHQHPVTKAQREQ----LHGHKGVVLWFTGLSGSGKSTVAGALEEALHELGVSTYLLDGDNVRHGLCSDLGFSDAD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767933021  85 REENVRRIAEVAKLFADAGLVCITSFISPYTQDRNNARQIhegasLP---FFEVFVDAPLHVCEQRDVKGLYKKARAGEI 161
Cdd:PRK03846  78 RKENIRRVGEVAKLMVDAGLVVLTAFISPHRAERQMVRER-----LGegeFIEVFVDTPLAICEARDPKGLYKKARAGEI 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 767933021 162 KGFTGIDSEYEKPEAPELVLKTDSCDVNDCVQQVVELLQERDIV 205
Cdd:PRK03846 153 RNFTGIDSVYEAPESPEIHLDTGEQLVTNLVEQLLDYLRQRDII 196
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
 2-204 3.97e-88

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 286.06  E-value: 3.97e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767933021   2 QRATNVTYQAHHVSRNKRGqvvgTRGGFRGCTVWLTGLSGAGKTTVSMALEEYLVCHGIPCYTLDGDNIRQGLNKNLGFS 81
Cdd:PRK05506 435 RRATNVHWQASDVSREARA----ARKGQKPATVWFTGLSGSGKSTIANLVERRLHALGRHTYLLDGDNVRHGLNRDLGFS 510

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767933021  82 PEDREENVRRIAEVAKLFADAGLVCITSFISPYTQDRNNARQIHEGAslPFFEVFVDAPLHVCEQRDVKGLYKKARAGEI 161
Cdd:PRK05506 511 DADRVENIRRVAEVARLMADAGLIVLVSFISPFREERELARALHGEG--EFVEVFVDTPLEVCEARDPKGLYAKARAGEI 588

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 767933021 162 KGFTGIDSEYEKPEAPELVLKTDSCDVNDCVQQVVELLQERDI 204
Cdd:PRK05506 589 KNFTGIDSPYEAPENPELRLDTTGRSPEELAEQVLELLRRRGA 631
apsK TIGR00455
adenylyl-sulfate kinase; This protein, adenylylsulfate kinase, is often found as a fusion ...
 13-199 3.46e-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: 3.46e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767933021   13 HVSRNKRGQVVGTRGgfrgCTVWLTGLSGAGKTTVSMALEEYLVCHGIPCYTLDGDNIRQGLNKNLGFSPEDREENVRRI 92
Cdd:TIGR00455   4 AITKDERQALNGHRG----VVIWLTGLSGSGKSTIANALEKKLESKGYRVYVLDGDNVRHGLNKDLGFSEEDRKENIRRI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767933021   93 AEVAKLFADAGLVCITSFISPYTQDRNNARQIHEGASlpFFEVFVDAPLHVCEQRDVKGLYKKARAGEIKGFTGIDSEYE 172
Cdd:TIGR00455  80 GEVAKLFVRNGIIVITSFISPYRADRQMVRELIEKGE--FIEVFVDCPLEVCEQRDPKGLYKKARNGEIKGFTGIDSPYE 157

                         170       180
                  ....*....|....*....|....*..
gi 767933021  173 KPEAPELVLKTDSCDVNDCVQQVVELL 199
Cdd:TIGR00455 158 APENPEVVLDTDQNDREECVGQIIEKL 184
PRK00889 PRK00889
adenylylsulfate kinase; Provisional
 30-206 2.06e-75

adenylylsulfate kinase; Provisional


Pssm-ID: 179157  Cd Length: 175  Bit Score: 238.00  E-value: 2.06e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767933021  30 RGCTVWLTGLSGAGKTTVSMALEEYLVCHGIPCYTLDGDNIRQGLNKNLGFSPEDREENVRRIAEVAKLFADAGLVCITS 109
Cdd:PRK00889   3 RGVTVWFTGLSGAGKTTIARALAEKLREAGYPVEVLDGDAVRTNLSKGLGFSKEDRDTNIRRIGFVANLLTRHGVIVLVS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767933021 110 FISPYTQDRNNARqihegASLP-FFEVFVDAPLHVCEQRDVKGLYKKARAGEIKGFTGIDSEYEKPEAPELVLKTDSCDV 188
Cdd:PRK00889  83 AISPYRETREEVR-----ANIGnFLEVFVDAPLEVCEQRDVKGLYAKARAGEIKHFTGIDDPYEPPLNPEVECRTDLESL 157

                        170
                 ....*....|....*...
gi 767933021 189 NDCVQQVVELLQERDIVP 206
Cdd:PRK00889 158 EESVDKVLQKLEELGYLV 175
MET3 COG2046
ATP sulfurylase (sulfate adenylyltransferase) [Inorganic ion transport and metabolism]; ATP ...
 212-602 3.78e-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: 228.87  E-value: 3.78e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767933021 212 EVKELYVPENKLHLAKTDAETLPALKINKVDMQWVQVLAEGWATPLNGFMREREYLQCLHFDCLLDGGVinLSVPIVLTA 291
Cdd:COG2046   11 KLVNRVVPGEEREALLEEAKGLPSIELSSRALSDLEMIAIGGFSPLTGFMNKADYESVVENMRLADGLL--WPIPITLDV 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767933021 292 THEDKERLDGCTAFALM-YEGRRVAILRNPEFFEHRKEERCARQWGTTCKNHPYIKMVMEQGDWLIGGDLQVLDRVYWND 370
Cdd:COG2046   89 SEEDAAGLKEGDEVALRdEEGEPLAVLEVEEIYEYDKEEEAEKVYGTTDPAHPGVAKLYERGDVYLGGPITLLNRPKHPD 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767933021 371 gLDQYRLTPTELKQKFKDMNADAVFAFQLRNPVHNGHALLMqdthKQLLERGYrrpVLLLHPLGGWTKDDDVPLMWRMKQ 450
Cdd:COG2046  169 -FPDYRLTPAETRALFEEKGWKTVVAFQTRNPMHRAHEYLQ----KRALETVD---GLLIHPLVGETKPGDIPAEVRVRC 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767933021 451 HAAVLEEGVlNPETTVVAIFPSPMMYAGPTEVQWH--CRARMvaGANFYIVGRDPAGMPhpetgkDLYEPsHGAKVL--T 526
Cdd:COG2046  241 YEALLENYY-PKDRVLLSGLPLAMRYAGPREALLHaiIRKNY--GCTHFIVGRDHAGVG------DYYGP-YDAQEIfdE 310

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767933021 527 MAPGLITLEIVPFRVAAYNKKKKRMDYYDSEHH--EDFEFISGTRMRKLAREGQKPPEGFMAPKAWTVLTEYYKSLEK 602
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.
 212-365 6.82e-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: 206.99  E-value: 6.82e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767933021  212 EVKELYVPENKLHLAKTDAETLPALKINKVDMQWVQVLAEGWATPLNGFMREREYLQCLHFDCLLDGGVinLSVPIVLTA 291
Cdd:pfam14306   7 KLVDLVVRDAEREELLAEAAELPSIELSKRELCDLELIAIGGFSPLTGFMGEADYLSVLEFMRLADGLL--WSIPITLDV 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767933021  292 THEDKERLDGCTAFALMY-EGRRVAILRNPEFFEHRKEERCARQWGTTCKNHPYIKMVMEQGDWLIGGDLQVLDR 365
Cdd:pfam14306  85 SEEDAASLKEGDRVALRDpEGEPLAILTVEEIYEPDKEEEAEKVFGTTDPAHPGVKKLYEQGDFYVGGDIEVLNR 159
sat PRK04149
sulfate adenylyltransferase; Reviewed
 212-601 1.77e-61

sulfate adenylyltransferase; Reviewed


Pssm-ID: 235227  Cd Length: 391  Bit Score: 208.56  E-value: 1.77e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767933021 212 EVKELYVPENKLHLAKTDAETLPALKINKVDMQWVQVLAEGWATPLNGFMREREYLQCLHFDCLLDGGVinLSVPIVLTA 291
Cdd:PRK04149  10 ELVNRVVEGRDREEILEEAESLPRIELDERAASDLEMIAIGGFSPLTGFMGREDYDSVVEEMRLANGLV--WSIPITLDV 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767933021 292 THEDKERLDGCTAFALMYEGRRVAILRNPEFFEHRKEERCARQWGTTCKNHPYIKMVMEQGDWLIGGDLQVLDRVYwNDG 371
Cdd:PRK04149  88 SEEDAASLKEGDEVALVYKGEPYGVLEVEEIYTYDKKKEAEKVYKTTDEKHPGVKKLYEQGDVYLAGPVTLLNRKF-HEP 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767933021 372 LDQYRLTPTELKQKFKDMNADAVFAFQLRNPVHNGHALLMqdthKQLLE--RGyrrpvLLLHPLGGWTKDDDVPLMWRMK 449
Cdd:PRK04149 167 FPRFWLTPAETRELFEEKGWKTVVAFQTRNPPHRAHEYLQ----KCALEivDG-----LLLNPLVGETKSGDIPAEVRME 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767933021 450 QHAAVLeEGVLNPETTVVAIFPSPMMYAGPTEVQWHCRARMVAGANFYIVGRDPAGmphpeTGkDLYEP-------SHGA 522
Cdd:PRK04149 238 AYEALL-KNYYPKDRVLLSVTPAAMRYAGPREAIFHAIVRKNYGCTHFIVGRDHAG-----VG-DYYGPydaqeifDEFT 310

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767933021 523 KvltmaPGLITlEIVPFRVAAYNKKKKRMDY-----YDSEHHEDFefiSGTRMRKLAREGQKPPEGFMAPKAWTVLTEYY 597
Cdd:PRK04149 311 E-----EELGI-TPLKFEEAFYCPKCGGMASektcpHGKEDRVHL---SGTKVREMLREGEKPPPEFSRPEVAEVLIKGL 381


                 ....
gi 767933021 598 KSLE 601
Cdd:PRK04149 382 KKYG 385
PRK05537 PRK05537
bifunctional sulfate adenylyltransferase/adenylylsulfate kinase;
31-202 1.44e-58

bifunctional sulfate adenylyltransferase/adenylylsulfate kinase;


Pssm-ID: 180124 [Multi-domain]  Cd Length: 568  Bit Score: 205.68  E-value: 1.44e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767933021  31 GCTVWLTGLSGAGKTTVSMALEEYLVCHGIPCYT-LDGDNIRQGLNKNLGFSPEDREENVRRIAEVAKLFADAGLVCITS 109
Cdd:PRK05537 392 GFTVFFTGLSGAGKSTIAKALMVKLMEMRGRPVTlLDGDVVRKHLSSELGFSKEDRDLNILRIGFVASEITKNGGIAICA 471

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767933021 110 FISPYTQDRNNARQIHEGASlPFFEVFVDAPLHVCEQRDVKGLYKKARAGEIKGFTGIDSEYEKPEAPELVLKTDSCDVN 189
Cdd:PRK05537 472 PIAPYRATRREVREMIEAYG-GFIEVHVATPLEVCEQRDRKGLYAKAREGKIKGFTGISDPYEPPANPELVIDTTNVTPD 550

                        170
                 ....*....|...
gi 767933021 190 DCVQQVVELLQER 202
Cdd:PRK05537 551 ECAHKILLYLEEK 563
PRK05537 PRK05537
bifunctional sulfate adenylyltransferase/adenylylsulfate kinase;
215-602 6.05e-46

bifunctional sulfate adenylyltransferase/adenylylsulfate kinase;


Pssm-ID: 180124 [Multi-domain]  Cd Length: 568  Bit Score: 170.62  E-value: 6.05e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767933021 215 ELYVPENKLHLAKTDAETLPALKINKVDMQWVQVLAEGWATPLNGFMREREYLQCLHFDCLLDGGVinLSVPIVLTATHE 294
Cdd:PRK05537  11 NLYVSPESREKLKAEALSLPSLDLSPRQICDLELLMNGGFSPLKGFMGRADYECVLENMRLADGTL--WPIPITLDVSEK 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767933021 295 DKERLDGCTAFALM-YEGRRVAILRNPEFFEHRKEERCARQWGTTCKNHPYI-KMVMEQGDWLIGGDLQVLDR-VYWNdg 371
Cdd:PRK05537  89 FAAGLEIGERIALRdQEGVLLAILTVSDIWEPDKEREAEAVFGTTDPAHPGVnYLHRWAGKFYLGGPLTGIQLpVHYD-- 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767933021 372 LDQYRLTPTELKQKFKDMNADAVFAFQLRNPVHNGHallmqdthKQLLERGYRR--PVLLLHPLGGWTKDDDVPLMWRMK 449
Cdd:PRK05537 167 FVQLRLTPAELRARFRKLGWRRVVAFQTRNPLHRAH--------EELTKRAAREvgANLLIHPVVGMTKPGDIDHFTRVR 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767933021 450 QHAAVLEEgvLNPETTVVAIFPSPMMYAGPTEVQWHCRARMVAGANFYIVGRDPAGMPHPETGKDLYEPSHGAKVLTMAP 529
Cdd:PRK05537 239 CYEALLDK--YPPATTLLSLLPLAMRMAGPREALWHAIIRRNYGCTHFIVGRDHAGPGKDSRGKPFYGPYDAQELFAKYA 316

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767933021 530 GLITLEIVPFRVAAYNKKKKRmdYY---DSEHHEDFEFISGTRMRKLAREGQKPPEGFMAPKAWTVLTEYYKSLEK 602
Cdd:PRK05537 317 DEIGITMVPFKEMVYVQDKAQ--YVpvdEVPQGATVLTISGTELRRRLREGLEIPEWFSFPEVVAELRRTYPPRHK 390
PRK05541 PRK05541
adenylylsulfate kinase; Provisional
 31-204 5.59e-27

adenylylsulfate kinase; Provisional


Pssm-ID: 235498  Cd Length: 176  Bit Score: 107.45  E-value: 5.59e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767933021  31 GCTVWLTGLSGAGKTTVSMALEEYLVCHGIPCYTLDGDNIRQGLNKNlGFSPEDREENVRRIAEVAKLFADAGLVCITSF 110
Cdd:PRK05541   7 GYVIWITGLAGSGKTTIAKALYERLKLKYSNVIYLDGDELREILGHY-GYDKQSRIEMALKRAKLAKFLADQGMIVIVTT 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767933021 111 ISPYTQDRNNARQIHEGaslpFFEVFVDAPLHVCEQRDVKGLYKKARAGEIKGFTGIDSEYEKPEAPELVLKTDSCDVND 190
Cdd:PRK05541  86 ISMFDEIYAYNRKHLPN----YFEVYLKCDMEELIRRDQKGLYTKALKGEIKNVVGVDIPFDEPKADLVIDNSCRTSLDE 161

                        170
                 ....*....|....
gi 767933021 191 CVQQVVELLQERDI 204
Cdd:PRK05541 162 KVDLILNKLKLRLI 175
Kti12 COG4088
tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) ...
 36-202 7.53e-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: 7.53e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767933021  36 LTGLSGAGKTTVSMALEEYLVCHGIPCYTLDGDNIRQGLnKNLGFSPEDREENVRRIAE-VAKLFADAGLVCIT--SFIS 112
Cdd:COG4088    9 LTGPPGSGKTTFAKALAQRLYAEGIAVALLHSDDFRRFL-VNESFPKETYEEVVEDVRTtTADNALDNGYSVIVdgTFYY 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767933021 113 PYTQDRnnARQIHEGASlPFFEVFVDAPLHVCEQRDVkglykkARAGEI--KGFTGIDSEYEKPE---APELVLKTDSCD 187
Cdd:COG4088   88 RSWQRD--FRNLAKHKA-PIHIIYLKAPLETALRRNR------ERGEPIpeRVIARMYRKFDKPGtkdRPDLVIDTTEDS 158

                        170
                 ....*....|....*
gi 767933021 188 VNDCVQQVVELLQER 202
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 ...
 34-183 4.77e-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: 55.01  E-value: 4.77e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767933021   34 VWLTGLSGAGKTTVSMALEEYLvchgiPCYTLDGDNIRQGLNKNLGFSPEDREEN----VRRIAEVAKLFADAGLVCI-- 107
Cdd:pfam13671   2 ILLVGLPGSGKSTLARRLLEEL-----GAVRLSSDDERKRLFGEGRPSISYYTDAtdrtYERLHELARIALRAGRPVIld 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767933021  108 TSFISPytQDRNNARQIHEGASLPFFEVFVDAPLHVCEQRDvkglykKARAgeikgftgiDSEYEKPEAPELVLKT 183
Cdd:pfam13671  77 ATNLRR--DERARLLALAREYGVPVRIVVFEAPEEVLRERL------AARA---------RAGGDPSDVPEEVLDR 135
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
34-147 1.13e-08

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


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 54.53  E-value: 1.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767933021  34 VWLTGLSGAGKTTVSMALEEYL-VCHgipcytLDGDNIRQGLnKNLGFSPEDREENVR-----RIAEVAKLFADAGLVCI 107
Cdd:COG0645    2 ILVCGLPGSGKSTLARALAERLgAVR------LRSDVVRKRL-FGAGLAPLERSPEATartyaRLLALARELLAAGRSVI 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 767933021 108 TSFISPYTQDRNNARQIHEGASLPFFEVFVDAPLHVCEQR 147
Cdd:COG0645   75 LDATFLRRAQREAFRALAEEAGAPFVLIWLDAPEEVLRER 114
CmkB COG1102
Cytidylate kinase [Nucleotide transport and metabolism];
38-204 1.17e-06

Cytidylate kinase [Nucleotide transport and metabolism];


Pssm-ID: 440719 [Multi-domain]  Cd Length: 188  Bit Score: 49.05  E-value: 1.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767933021  38 GLSGAGKTTVSMALEEYLvchGIPCYtlDGDNIRQgLNKNLGFSPEDREEN------------------VRRIAEVAKLF 99
Cdd:COG1102    7 REPGSGGTTIAKRLAEKL---GLPLY--DGEILRE-AAKERGLSEEEFEKLdekapsllyrdtaeedeiDRALDKVIREL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767933021 100 ADAGLVCITSFISPY-TQDRNNArqIHegaslpffeVFVDAPLHVCEQR-------DVKGLYK------KARAGEIKGFT 165
Cdd:COG1102   81 ARKGNCVIVGRLADWiLRDRPNV--LK---------VFLTAPLEVRVKRiaeregiSEEEAEKeikkrdKSRAKYYKYYY 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 767933021 166 GID----SEYekpeapELVLKTDSCDVNDCVQQVVELLQERDI 204
Cdd:COG1102  150 GIDwgdpSNY------DLVINTSRLGIEEAVDLILAAIEAREK 186
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 36-102 3.22e-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: 3.22e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767933021    36 LTGLSGAGKTTVSMALEEYLVCHGIPCYTLDGDNIRQG-LNKNLGFSPEDREENVRRIAEVAKLFADA 102
Cdd:smart00382   7 IVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEvLDQLLLIIVGGKKASGSGELRLRLALALA 74
GntK cd02021
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting ...
 36-178 4.63e-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: 4.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767933021  36 LTGLSGAGKTTVSMALEEYLVCHGIpcytlDGDNIRQGLNK-----NLGFSPEDRE---ENVRRIAEVAKLFADAGLVCI 107
Cdd:cd02021    4 VMGVSGSGKSTVGKALAERLGAPFI-----DGDDLHPPANIakmaaGIPLNDEDRWpwlQALTDALLAKLASAGEGVVVA 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767933021 108 TSFISPYTQDRnnARQIHEGASLPFfeVFVDAPLHVCEQRDvkglykKARAGEIKGFTGIDSEYEKPEAPE 178
Cdd:cd02021   79 CSALKRIYRDI--LRGGAANPRVRF--VHLDGPREVLAERL------AARKGHFMPADLLDSQFETLEPPG 139
NK cd02019
Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of ...
 33-105 5.97e-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: 5.97e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767933021  33 TVWLTGLSGAGKTTVSMALEEYLVCHGIPCYT----LDGdnirqglnknLGFSPEDREENVRRIAEVaKLFADAGLV 105
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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