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Conserved domains on  [gi|194376436|dbj|BAG62977|]
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unnamed protein product [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, ...
 248-611 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: 522.19  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194376436 248 LPSLSITKLDLQWVQVLSEGWATPLKGFMREKEYLQVMHFDTLLDDgvINMSIPIVLPVSAEDKTRLEGCSKFVLAHGGR 327
Cdd:cd00517    1 LPSVELSERDLCDLEMLAEGGFSPLTGFMTEADYLSVLEEMRLLDG--TLWPIPIVLDVSEEDAKRLKEGERVALRYPGQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194376436 328 RVAILRDAEFYEHRKEERCSRVWGTTCTKHPHIKMVMESGDWLVGGDLQVLEKIRWNDgLDQYRLTPLELKQKCKEMNAD 407
Cdd:cd00517   79 PLAILTVEEIYEPDKEEEAARVFGTTDPHHPGVKKVMEQGDWLVGGPIEVLELPPFPD-FDQYRLTPAELRALFKERGWR 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194376436 408 AVFAFQLRNPVHNGHALLMQDTRRRLLErgykhPVLLLHPLGGWTKDDDVPLDWRMKQHAAVLEEGVLdPKSTIVAIFPS 487
Cdd:cd00517  158 RVVAFQTRNPMHRAHEELMKRAAEKLLN-----DGLLLHPLVGWTKPGDVPDEVRMRAYEALLEEYYL-PERTVLAILPL 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194376436 488 PMLYAGPTEVQWHCRSRMIAGANFYIVGRDPAGMPHPETKKDLYEPTHGGKVLSMApglTSVEIIPFRVAAYNKAKKAMD 567
Cdd:cd00517  232 PMRYAGPREALWHAIIRKNYGATHFIVGRDHAGVGHPGDYYGPYDAQEIFKKLAPE---LGIEPVPFREAAYCPKCDGMA 308

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 194376436 568 FYDPARHNE-FDFISGTRMRKLAREGENPPDGFMAPKAWKVLTDY 611
Cdd:cd00517  309 SEDTCPHGEdFLNISGTKLRKMLREGEKPPEWFMRPEVAKVLREY 353
CysC COG0529
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ...
 27-221 8.81e-102

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: 307.02  E-value: 8.81e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194376436  27 HHVSRNKRGQvvgtRGGFRGCTVWLTGFSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRHGLNRNLGFSPGDREENIRR 106
Cdd:COG0529    1 SAVTREERAA----LKGQKGFVVWFTGLSGSGKSTLANALERRLFERGRHVYLLDGDNVRHGLNKDLGFSKEDRDENIRR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194376436 107 IAEVAKLFADAGLVCITSFISPFAKDRENARKIHESAglPFFEIFVDAPLNICESRDVKGLYKRARAGEIKGFTGIDSDY 186
Cdd:COG0529   77 IGEVAKLLADAGLIVLVAFISPYRADREEARELIGEG--EFIEVYVDTPLEVCEARDPKGLYAKARAGEIKNFTGIDDPY 154

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 194376436 187 EKPETPERVLKTNLSTVSDCVHQVVELLQEQNIVP 221
Cdd:COG0529  155 EAPENPELVLDTDKESVEESVEKILAYLEERGYIS 189
 
Name Accession Description Interval E-value
ATPS cd00517
ATP-sulfurylase; ATP-sulfurylase (ATPS), also known as sulfate adenylate transferase, ...
 248-611 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: 522.19  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194376436 248 LPSLSITKLDLQWVQVLSEGWATPLKGFMREKEYLQVMHFDTLLDDgvINMSIPIVLPVSAEDKTRLEGCSKFVLAHGGR 327
Cdd:cd00517    1 LPSVELSERDLCDLEMLAEGGFSPLTGFMTEADYLSVLEEMRLLDG--TLWPIPIVLDVSEEDAKRLKEGERVALRYPGQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194376436 328 RVAILRDAEFYEHRKEERCSRVWGTTCTKHPHIKMVMESGDWLVGGDLQVLEKIRWNDgLDQYRLTPLELKQKCKEMNAD 407
Cdd:cd00517   79 PLAILTVEEIYEPDKEEEAARVFGTTDPHHPGVKKVMEQGDWLVGGPIEVLELPPFPD-FDQYRLTPAELRALFKERGWR 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194376436 408 AVFAFQLRNPVHNGHALLMQDTRRRLLErgykhPVLLLHPLGGWTKDDDVPLDWRMKQHAAVLEEGVLdPKSTIVAIFPS 487
Cdd:cd00517  158 RVVAFQTRNPMHRAHEELMKRAAEKLLN-----DGLLLHPLVGWTKPGDVPDEVRMRAYEALLEEYYL-PERTVLAILPL 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194376436 488 PMLYAGPTEVQWHCRSRMIAGANFYIVGRDPAGMPHPETKKDLYEPTHGGKVLSMApglTSVEIIPFRVAAYNKAKKAMD 567
Cdd:cd00517  232 PMRYAGPREALWHAIIRKNYGATHFIVGRDHAGVGHPGDYYGPYDAQEIFKKLAPE---LGIEPVPFREAAYCPKCDGMA 308

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 194376436 568 FYDPARHNE-FDFISGTRMRKLAREGENPPDGFMAPKAWKVLTDY 611
Cdd:cd00517  309 SEDTCPHGEdFLNISGTKLRKMLREGEKPPEWFMRPEVAKVLREY 353
sopT TIGR00339
ATP sulphurylase; This enzyme forms adenosine 5'-phosphosulfate (APS) from ATP and free ...
 230-610 9.49e-139

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: 409.08  E-value: 9.49e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194376436  230 ELFVPENKLDH-VRAEAETLPSLSITKLDLQWVQVLSEGWATPLKGFMREKEYLQVMHfDTLLDDGViNMSIPIVLPVSA 308
Cdd:TIGR00339   8 ELVVRDPDEEHkLLAEAESLPSITLSDRQLCDLELLGNGAFSPLEGFMNEADYDSVVE-SMRLSDGV-LFSVPITLDIDD 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194376436  309 EDKTRLEGCSKFVLAH-GGRRVAILRDAEFYEHRKEERCSRVWGTTCTKHPHIKMVMESGDWLVGGDLQVLEKIRWnDGL 387
Cdd:TIGR00339  86 EDADDIKLGDRIALTDpKGQPLAILTIEEVYKPNKEKEAKKVFGTTDPEHPGVVYLNTAGNYYIGGPIEVINLPKF-YDF 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194376436  388 DQYRLTPLELKQKCKEMNADAVFAFQLRNPVHNGHALLMQDTRRRLlergyKHPVLLLHPLGGWTKDDDVPLDWRMKQHA 467
Cdd:TIGR00339 165 PRFRFTPAELREEFKERGWDTVVAFQTRNPMHRAHEELTKRAAERL-----PNAGVLVHPLVGLTKPGDIPAEVRMRAYE 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194376436  468 aVLEEGVLDPKSTIVAIFPSPMLYAGPTEVQWHCRSRMIAGANFYIVGRDPAGMPHPETKKDLYEPTHGGKVLSMAPGLT 547
Cdd:TIGR00339 240 -VLKEGYPNPERTVVSFLPLAMRYAGPREAIWHAIIRKNYGATHFIVGRDHAGPGSNSKGQDFYGPYDAQELFEKYKAEL 318

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 194376436  548 SVEIIPFRVAAYNKAKKAMDFYDPARHNEFDF--ISGTRMRKLAREGENPPDGFMAPKAWKVLTD 610
Cdd:TIGR00339 319 GIKIVPFRHVAYCPDEDEYAPADQAGHTNLRTlnISGTKLRGMLRNGVFPPEWFSRPEVVKILRE 383
CysC COG0529
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ...
 27-221 8.81e-102

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: 307.02  E-value: 8.81e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194376436  27 HHVSRNKRGQvvgtRGGFRGCTVWLTGFSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRHGLNRNLGFSPGDREENIRR 106
Cdd:COG0529    1 SAVTREERAA----LKGQKGFVVWFTGLSGSGKSTLANALERRLFERGRHVYLLDGDNVRHGLNKDLGFSKEDRDENIRR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194376436 107 IAEVAKLFADAGLVCITSFISPFAKDRENARKIHESAglPFFEIFVDAPLNICESRDVKGLYKRARAGEIKGFTGIDSDY 186
Cdd:COG0529   77 IGEVAKLLADAGLIVLVAFISPYRADREEARELIGEG--EFIEVYVDTPLEVCEARDPKGLYAKARAGEIKNFTGIDDPY 154

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 194376436 187 EKPETPERVLKTNLSTVSDCVHQVVELLQEQNIVP 221
Cdd:COG0529  155 EAPENPELVLDTDKESVEESVEKILAYLEERGYIS 189
APSK cd02027
Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5 ...
 48-198 4.53e-98

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: 295.93  E-value: 4.53e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194376436  48 TVWLTGFSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRHGLNRNLGFSPGDREENIRRIAEVAKLFADAGLVCITSFIS 127
Cdd:cd02027    1 VIWLTGLSGSGKSTIARALEEKLFQRGRPVYVLDGDNVRHGLNKDLGFSREDREENIRRIAEVAKLLADAGLIVIAAFIS 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 194376436 128 PFAKDRENARKIHEsaGLPFFEIFVDAPLNICESRDVKGLYKRARAGEIKGFTGIDSDYEKPETPERVLKT 198
Cdd:cd02027   81 PYREDREAARKIIG--GGDFLEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDDPYEAPENPDLVLDT 149
APS_kinase pfam01583
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3 ...
 45-198 2.04e-95

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: 289.22  E-value: 2.04e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194376436   45 RGCTVWLTGFSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRHGLNRNLGFSPGDREENIRRIAEVAKLFADAGLVCITS 124
Cdd:pfam01583   1 RGCTIWLTGLSGAGKSTIANALERKLFEQGRSVYVLDGDNVRHGLNKDLGFSEEDRTENIRRIGEVAKLFADAGLIVITA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 194376436  125 FISPFAKDRENARKIHESAglPFFEIFVDAPLNICESRDVKGLYKRARAGEIKGFTGIDSDYEKPETPERVLKT 198
Cdd:pfam01583  81 FISPYREDREQARELHEEG--KFIEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDSPYEAPENPELVLDT 152
ATP-sulfurylase pfam01747
ATP-sulfurylase; This domain is the catalytic domain of ATP-sulfurylase or sulfate ...
 388-611 7.08e-92

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: 282.12  E-value: 7.08e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194376436  388 DQYRLTPLELKQKCKEMNADAVFAFQLRNPVHNGHALLMQDTRRRLlERGYkhpvLLLHPLGGWTKDDDVPLDWRMKQHA 467
Cdd:pfam01747   1 DEYRLTPAETRALFKEKGWRTVVAFQTRNPLHRAHEELMKRALEEL-EADG----LLLHPLVGPTKPGDVPAEVRVRCYE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194376436  468 AVLEEgVLDPKSTIVAIFPSPMLYAGPTEVQWHCRSRMIAGANFYIVGRDPAGMPHpetkkdLYEPTHGGKVLSMAPGLT 547
Cdd:pfam01747  76 ALLEN-YLPPDRVVLALLPLAMRYAGPREALLHAIIRKNYGCTHFIVGRDHAGVGD------FYGPYDAQEIFDEYPGEL 148

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 194376436  548 SVEIIPFRVAAYNKAKKAM-DFYDPARHNEFDFISGTRMRKLAREGENPPDGFMAPKAWKVLTDY 611
Cdd:pfam01747 149 GIEPVPFREAVYCKKCGEMaSTKCPHGGEDRLFISGTKVRELLREGEEPPEWFSRPEVAKVLREY 213
PRK03846 PRK03846
adenylylsulfate kinase; Provisional
 19-220 6.80e-89

adenylylsulfate kinase; Provisional


Pssm-ID: 179661  Cd Length: 198  Bit Score: 274.13  E-value: 6.80e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194376436  19 STNVVYQAHHVSRNKRGQvvgtRGGFRGCTVWLTGFSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRHGLNRNLGFSPG 98
Cdd:PRK03846   1 DENIVWHQHPVTKAQREQ----LHGHKGVVLWFTGLSGSGKSTVAGALEEALHELGVSTYLLDGDNVRHGLCSDLGFSDA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194376436  99 DREENIRRIAEVAKLFADAGLVCITSFISPFAKDRENARKIhesagLP---FFEIFVDAPLNICESRDVKGLYKRARAGE 175
Cdd:PRK03846  77 DRKENIRRVGEVAKLMVDAGLVVLTAFISPHRAERQMVRER-----LGegeFIEVFVDTPLAICEARDPKGLYKKARAGE 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 194376436 176 IKGFTGIDSDYEKPETPERVLKTNLSTVSDCVHQVVELLQEQNIV 220
Cdd:PRK03846 152 IRNFTGIDSVYEAPESPEIHLDTGEQLVTNLVEQLLDYLRQRDII 196
apsK TIGR00455
adenylyl-sulfate kinase; This protein, adenylylsulfate kinase, is often found as a fusion ...
 28-214 3.49e-80

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: 250.85  E-value: 3.49e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194376436   28 HVSRNKRGQVVGTRGgfrgCTVWLTGFSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRHGLNRNLGFSPGDREENIRRI 107
Cdd:TIGR00455   4 AITKDERQALNGHRG----VVIWLTGLSGSGKSTIANALEKKLESKGYRVYVLDGDNVRHGLNKDLGFSEEDRKENIRRI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194376436  108 AEVAKLFADAGLVCITSFISPFAKDRENARKIHESAglPFFEIFVDAPLNICESRDVKGLYKRARAGEIKGFTGIDSDYE 187
Cdd:TIGR00455  80 GEVAKLFVRNGIIVITSFISPYRADRQMVRELIEKG--EFIEVFVDCPLEVCEQRDPKGLYKKARNGEIKGFTGIDSPYE 157

                         170       180
                  ....*....|....*....|....*..
gi 194376436  188 KPETPERVLKTNLSTVSDCVHQVVELL 214
Cdd:TIGR00455 158 APENPEVVLDTDQNDREECVGQIIEKL 184
MET3 COG2046
ATP sulfurylase (sulfate adenylyltransferase) [Inorganic ion transport and metabolism]; ATP ...
 230-617 8.15e-72

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: 236.19  E-value: 8.15e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194376436 230 ELFVPENKLDHVRAEAETLPSLSITKLDLQWVQVLSEGWATPLKGFMREKEYLQV---MHfdtlLDDGVInMSIPIVLPV 306
Cdd:COG2046   14 NRVVPGEEREALLEEAKGLPSIELSSRALSDLEMIAIGGFSPLTGFMNKADYESVvenMR----LADGLL-WPIPITLDV 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194376436 307 SAEDKTRLEGCSKFVL-AHGGRRVAILRDAEFYEHRKEERCSRVWGTTCTKHPHIKMVMESGDWLVGGDLQVLEKIRWND 385
Cdd:COG2046   89 SEEDAAGLKEGDEVALrDEEGEPLAVLEVEEIYEYDKEEEAEKVYGTTDPAHPGVAKLYERGDVYLGGPITLLNRPKHPD 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194376436 386 gLDQYRLTPLELKQKCKEMNADAVFAFQLRNPVHNGHALLMqdtrRRLLERGYkhpVLLLHPLGGWTKDDDVPLDWRMKQ 465
Cdd:COG2046  169 -FPDYRLTPAETRALFEEKGWKTVVAFQTRNPMHRAHEYLQ----KRALETVD---GLLIHPLVGETKPGDIPAEVRVRC 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194376436 466 HAAVLEEGVlDPKSTIVAIFPSPMLYAGPTEVQWH--CRSRMiaGANFYIVGRDPAGMPhpetkkDLYEP--------TH 535
Cdd:COG2046  241 YEALLENYY-PKDRVLLSGLPLAMRYAGPREALLHaiIRKNY--GCTHFIVGRDHAGVG------DYYGPydaqeifdEF 311

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194376436 536 GGKVLSMapgltsvEIIPFRVAAYNKAKKAMDFYDPARHNEFDF--ISGTRMRKLAREGENPPDGFMAPKAWKVLTDYYR 613
Cdd:COG2046  312 PPGELGI-------EPLKFEEAFYCKKCGGMATSKTCPHDKEDRvsLSGTKVREMLREGEEPPPEFSRPEVAEILRKYYQ 384


                 ....
gi 194376436 614 SLEK 617
Cdd:COG2046  385 PFGE 388
sat PRK04149
sulfate adenylyltransferase; Reviewed
 230-616 8.80e-62

sulfate adenylyltransferase; Reviewed


Pssm-ID: 235227  Cd Length: 391  Bit Score: 209.72  E-value: 8.80e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194376436 230 ELFVPENKLDHVRAEAETLPSLSITKLDLQWVQVLSEGWATPLKGFMREKEYLQVMHFDTLLDDGVinMSIPIVLPVSAE 309
Cdd:PRK04149  13 NRVVEGRDREEILEEAESLPRIELDERAASDLEMIAIGGFSPLTGFMGREDYDSVVEEMRLANGLV--WSIPITLDVSEE 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194376436 310 DKTRLEGCSKFVLAHGGRRVAILRDAEFYEHRKEERCSRVWGTTCTKHPHIKMVMESGDWLVGGDLQVLEKIRwNDGLDQ 389
Cdd:PRK04149  91 DAASLKEGDEVALVYKGEPYGVLEVEEIYTYDKKKEAEKVYKTTDEKHPGVKKLYEQGDVYLAGPVTLLNRKF-HEPFPR 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194376436 390 YRLTPLELKQKCKEMNADAVFAFQLRNPVHNGHALLMqdtrrrllergyKHPV-----LLLHPLGGWTKDDDVPLDWRMK 464
Cdd:PRK04149 170 FWLTPAETRELFEEKGWKTVVAFQTRNPPHRAHEYLQ------------KCALeivdgLLLNPLVGETKSGDIPAEVRME 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194376436 465 QHAAVLeEGVLDPKSTIVAIFPSPMLYAGPTEVQWHCRSRMIAGANFYIVGRDPAGMphpetkKDLYEPTHGGKVLSM-- 542
Cdd:PRK04149 238 AYEALL-KNYYPKDRVLLSVTPAAMRYAGPREAIFHAIVRKNYGCTHFIVGRDHAGV------GDYYGPYDAQEIFDEft 310

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 194376436 543 APGLtSVEIIPFRVAAYNKAKKAMDFYDPARHNEFD--FISGTRMRKLAREGENPPDGFMAPKAWKVLTDYYRSLE 616
Cdd:PRK04149 311 EEEL-GITPLKFEEAFYCPKCGGMASEKTCPHGKEDrvHLSGTKVREMLREGEKPPPEFSRPEVAEVLIKGLKKYG 385
 
Name Accession Description Interval E-value
ATPS cd00517
ATP-sulfurylase; ATP-sulfurylase (ATPS), also known as sulfate adenylate transferase, ...
 248-611 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: 522.19  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194376436 248 LPSLSITKLDLQWVQVLSEGWATPLKGFMREKEYLQVMHFDTLLDDgvINMSIPIVLPVSAEDKTRLEGCSKFVLAHGGR 327
Cdd:cd00517    1 LPSVELSERDLCDLEMLAEGGFSPLTGFMTEADYLSVLEEMRLLDG--TLWPIPIVLDVSEEDAKRLKEGERVALRYPGQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194376436 328 RVAILRDAEFYEHRKEERCSRVWGTTCTKHPHIKMVMESGDWLVGGDLQVLEKIRWNDgLDQYRLTPLELKQKCKEMNAD 407
Cdd:cd00517   79 PLAILTVEEIYEPDKEEEAARVFGTTDPHHPGVKKVMEQGDWLVGGPIEVLELPPFPD-FDQYRLTPAELRALFKERGWR 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194376436 408 AVFAFQLRNPVHNGHALLMQDTRRRLLErgykhPVLLLHPLGGWTKDDDVPLDWRMKQHAAVLEEGVLdPKSTIVAIFPS 487
Cdd:cd00517  158 RVVAFQTRNPMHRAHEELMKRAAEKLLN-----DGLLLHPLVGWTKPGDVPDEVRMRAYEALLEEYYL-PERTVLAILPL 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194376436 488 PMLYAGPTEVQWHCRSRMIAGANFYIVGRDPAGMPHPETKKDLYEPTHGGKVLSMApglTSVEIIPFRVAAYNKAKKAMD 567
Cdd:cd00517  232 PMRYAGPREALWHAIIRKNYGATHFIVGRDHAGVGHPGDYYGPYDAQEIFKKLAPE---LGIEPVPFREAAYCPKCDGMA 308

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 194376436 568 FYDPARHNE-FDFISGTRMRKLAREGENPPDGFMAPKAWKVLTDY 611
Cdd:cd00517  309 SEDTCPHGEdFLNISGTKLRKMLREGEKPPEWFMRPEVAKVLREY 353
sopT TIGR00339
ATP sulphurylase; This enzyme forms adenosine 5'-phosphosulfate (APS) from ATP and free ...
 230-610 9.49e-139

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: 409.08  E-value: 9.49e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194376436  230 ELFVPENKLDH-VRAEAETLPSLSITKLDLQWVQVLSEGWATPLKGFMREKEYLQVMHfDTLLDDGViNMSIPIVLPVSA 308
Cdd:TIGR00339   8 ELVVRDPDEEHkLLAEAESLPSITLSDRQLCDLELLGNGAFSPLEGFMNEADYDSVVE-SMRLSDGV-LFSVPITLDIDD 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194376436  309 EDKTRLEGCSKFVLAH-GGRRVAILRDAEFYEHRKEERCSRVWGTTCTKHPHIKMVMESGDWLVGGDLQVLEKIRWnDGL 387
Cdd:TIGR00339  86 EDADDIKLGDRIALTDpKGQPLAILTIEEVYKPNKEKEAKKVFGTTDPEHPGVVYLNTAGNYYIGGPIEVINLPKF-YDF 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194376436  388 DQYRLTPLELKQKCKEMNADAVFAFQLRNPVHNGHALLMQDTRRRLlergyKHPVLLLHPLGGWTKDDDVPLDWRMKQHA 467
Cdd:TIGR00339 165 PRFRFTPAELREEFKERGWDTVVAFQTRNPMHRAHEELTKRAAERL-----PNAGVLVHPLVGLTKPGDIPAEVRMRAYE 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194376436  468 aVLEEGVLDPKSTIVAIFPSPMLYAGPTEVQWHCRSRMIAGANFYIVGRDPAGMPHPETKKDLYEPTHGGKVLSMAPGLT 547
Cdd:TIGR00339 240 -VLKEGYPNPERTVVSFLPLAMRYAGPREAIWHAIIRKNYGATHFIVGRDHAGPGSNSKGQDFYGPYDAQELFEKYKAEL 318

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 194376436  548 SVEIIPFRVAAYNKAKKAMDFYDPARHNEFDF--ISGTRMRKLAREGENPPDGFMAPKAWKVLTD 610
Cdd:TIGR00339 319 GIKIVPFRHVAYCPDEDEYAPADQAGHTNLRTlnISGTKLRGMLRNGVFPPEWFSRPEVVKILRE 383
CysC COG0529
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ...
 27-221 8.81e-102

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: 307.02  E-value: 8.81e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194376436  27 HHVSRNKRGQvvgtRGGFRGCTVWLTGFSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRHGLNRNLGFSPGDREENIRR 106
Cdd:COG0529    1 SAVTREERAA----LKGQKGFVVWFTGLSGSGKSTLANALERRLFERGRHVYLLDGDNVRHGLNKDLGFSKEDRDENIRR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194376436 107 IAEVAKLFADAGLVCITSFISPFAKDRENARKIHESAglPFFEIFVDAPLNICESRDVKGLYKRARAGEIKGFTGIDSDY 186
Cdd:COG0529   77 IGEVAKLLADAGLIVLVAFISPYRADREEARELIGEG--EFIEVYVDTPLEVCEARDPKGLYAKARAGEIKNFTGIDDPY 154

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 194376436 187 EKPETPERVLKTNLSTVSDCVHQVVELLQEQNIVP 221
Cdd:COG0529  155 EAPENPELVLDTDKESVEESVEKILAYLEERGYIS 189
APSK cd02027
Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5 ...
 48-198 4.53e-98

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: 295.93  E-value: 4.53e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194376436  48 TVWLTGFSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRHGLNRNLGFSPGDREENIRRIAEVAKLFADAGLVCITSFIS 127
Cdd:cd02027    1 VIWLTGLSGSGKSTIARALEEKLFQRGRPVYVLDGDNVRHGLNKDLGFSREDREENIRRIAEVAKLLADAGLIVIAAFIS 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 194376436 128 PFAKDRENARKIHEsaGLPFFEIFVDAPLNICESRDVKGLYKRARAGEIKGFTGIDSDYEKPETPERVLKT 198
Cdd:cd02027   81 PYREDREAARKIIG--GGDFLEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDDPYEAPENPDLVLDT 149
APS_kinase pfam01583
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3 ...
 45-198 2.04e-95

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: 289.22  E-value: 2.04e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194376436   45 RGCTVWLTGFSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRHGLNRNLGFSPGDREENIRRIAEVAKLFADAGLVCITS 124
Cdd:pfam01583   1 RGCTIWLTGLSGAGKSTIANALERKLFEQGRSVYVLDGDNVRHGLNKDLGFSEEDRTENIRRIGEVAKLFADAGLIVITA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 194376436  125 FISPFAKDRENARKIHESAglPFFEIFVDAPLNICESRDVKGLYKRARAGEIKGFTGIDSDYEKPETPERVLKT 198
Cdd:pfam01583  81 FISPYREDREQARELHEEG--KFIEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDSPYEAPENPELVLDT 152
ATP-sulfurylase pfam01747
ATP-sulfurylase; This domain is the catalytic domain of ATP-sulfurylase or sulfate ...
 388-611 7.08e-92

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: 282.12  E-value: 7.08e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194376436  388 DQYRLTPLELKQKCKEMNADAVFAFQLRNPVHNGHALLMQDTRRRLlERGYkhpvLLLHPLGGWTKDDDVPLDWRMKQHA 467
Cdd:pfam01747   1 DEYRLTPAETRALFKEKGWRTVVAFQTRNPLHRAHEELMKRALEEL-EADG----LLLHPLVGPTKPGDVPAEVRVRCYE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194376436  468 AVLEEgVLDPKSTIVAIFPSPMLYAGPTEVQWHCRSRMIAGANFYIVGRDPAGMPHpetkkdLYEPTHGGKVLSMAPGLT 547
Cdd:pfam01747  76 ALLEN-YLPPDRVVLALLPLAMRYAGPREALLHAIIRKNYGCTHFIVGRDHAGVGD------FYGPYDAQEIFDEYPGEL 148

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 194376436  548 SVEIIPFRVAAYNKAKKAM-DFYDPARHNEFDFISGTRMRKLAREGENPPDGFMAPKAWKVLTDY 611
Cdd:pfam01747 149 GIEPVPFREAVYCKKCGEMaSTKCPHGGEDRLFISGTKVRELLREGEEPPEWFSRPEVAKVLREY 213
PRK03846 PRK03846
adenylylsulfate kinase; Provisional
 19-220 6.80e-89

adenylylsulfate kinase; Provisional


Pssm-ID: 179661  Cd Length: 198  Bit Score: 274.13  E-value: 6.80e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194376436  19 STNVVYQAHHVSRNKRGQvvgtRGGFRGCTVWLTGFSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRHGLNRNLGFSPG 98
Cdd:PRK03846   1 DENIVWHQHPVTKAQREQ----LHGHKGVVLWFTGLSGSGKSTVAGALEEALHELGVSTYLLDGDNVRHGLCSDLGFSDA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194376436  99 DREENIRRIAEVAKLFADAGLVCITSFISPFAKDRENARKIhesagLP---FFEIFVDAPLNICESRDVKGLYKRARAGE 175
Cdd:PRK03846  77 DRKENIRRVGEVAKLMVDAGLVVLTAFISPHRAERQMVRER-----LGegeFIEVFVDTPLAICEARDPKGLYKKARAGE 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 194376436 176 IKGFTGIDSDYEKPETPERVLKTNLSTVSDCVHQVVELLQEQNIV 220
Cdd:PRK03846 152 IRNFTGIDSVYEAPESPEIHLDTGEQLVTNLVEQLLDYLRQRDII 196
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
 17-217 7.28e-85

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 277.97  E-value: 7.28e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194376436  17 QKSTNVVYQAHHVSRNKRGqvvgTRGGFRGCTVWLTGFSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRHGLNRNLGFS 96
Cdd:PRK05506 435 RRATNVHWQASDVSREARA----ARKGQKPATVWFTGLSGSGKSTIANLVERRLHALGRHTYLLDGDNVRHGLNRDLGFS 510

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194376436  97 PGDREENIRRIAEVAKLFADAGLVCITSFISPFAKDRENARKIHESAglPFFEIFVDAPLNICESRDVKGLYKRARAGEI 176
Cdd:PRK05506 511 DADRVENIRRVAEVARLMADAGLIVLVSFISPFREERELARALHGEG--EFVEVFVDTPLEVCEARDPKGLYAKARAGEI 588

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 194376436 177 KGFTGIDSDYEKPETPERVLKTNLSTVSDCVHQVVELLQEQ 217
Cdd:PRK05506 589 KNFTGIDSPYEAPENPELRLDTTGRSPEELAEQVLELLRRR 629
apsK TIGR00455
adenylyl-sulfate kinase; This protein, adenylylsulfate kinase, is often found as a fusion ...
 28-214 3.49e-80

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: 250.85  E-value: 3.49e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194376436   28 HVSRNKRGQVVGTRGgfrgCTVWLTGFSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRHGLNRNLGFSPGDREENIRRI 107
Cdd:TIGR00455   4 AITKDERQALNGHRG----VVIWLTGLSGSGKSTIANALEKKLESKGYRVYVLDGDNVRHGLNKDLGFSEEDRKENIRRI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194376436  108 AEVAKLFADAGLVCITSFISPFAKDRENARKIHESAglPFFEIFVDAPLNICESRDVKGLYKRARAGEIKGFTGIDSDYE 187
Cdd:TIGR00455  80 GEVAKLFVRNGIIVITSFISPYRADRQMVRELIEKG--EFIEVFVDCPLEVCEQRDPKGLYKKARNGEIKGFTGIDSPYE 157

                         170       180
                  ....*....|....*....|....*..
gi 194376436  188 KPETPERVLKTNLSTVSDCVHQVVELL 214
Cdd:TIGR00455 158 APENPEVVLDTDQNDREECVGQIIEKL 184
MET3 COG2046
ATP sulfurylase (sulfate adenylyltransferase) [Inorganic ion transport and metabolism]; ATP ...
 230-617 8.15e-72

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: 236.19  E-value: 8.15e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194376436 230 ELFVPENKLDHVRAEAETLPSLSITKLDLQWVQVLSEGWATPLKGFMREKEYLQV---MHfdtlLDDGVInMSIPIVLPV 306
Cdd:COG2046   14 NRVVPGEEREALLEEAKGLPSIELSSRALSDLEMIAIGGFSPLTGFMNKADYESVvenMR----LADGLL-WPIPITLDV 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194376436 307 SAEDKTRLEGCSKFVL-AHGGRRVAILRDAEFYEHRKEERCSRVWGTTCTKHPHIKMVMESGDWLVGGDLQVLEKIRWND 385
Cdd:COG2046   89 SEEDAAGLKEGDEVALrDEEGEPLAVLEVEEIYEYDKEEEAEKVYGTTDPAHPGVAKLYERGDVYLGGPITLLNRPKHPD 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194376436 386 gLDQYRLTPLELKQKCKEMNADAVFAFQLRNPVHNGHALLMqdtrRRLLERGYkhpVLLLHPLGGWTKDDDVPLDWRMKQ 465
Cdd:COG2046  169 -FPDYRLTPAETRALFEEKGWKTVVAFQTRNPMHRAHEYLQ----KRALETVD---GLLIHPLVGETKPGDIPAEVRVRC 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194376436 466 HAAVLEEGVlDPKSTIVAIFPSPMLYAGPTEVQWH--CRSRMiaGANFYIVGRDPAGMPhpetkkDLYEP--------TH 535
Cdd:COG2046  241 YEALLENYY-PKDRVLLSGLPLAMRYAGPREALLHaiIRKNY--GCTHFIVGRDHAGVG------DYYGPydaqeifdEF 311

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194376436 536 GGKVLSMapgltsvEIIPFRVAAYNKAKKAMDFYDPARHNEFDF--ISGTRMRKLAREGENPPDGFMAPKAWKVLTDYYR 613
Cdd:COG2046  312 PPGELGI-------EPLKFEEAFYCKKCGGMATSKTCPHDKEDRvsLSGTKVREMLREGEEPPPEFSRPEVAEILRKYYQ 384


                 ....
gi 194376436 614 SLEK 617
Cdd:COG2046  385 PFGE 388
PRK00889 PRK00889
adenylylsulfate kinase; Provisional
 45-221 1.28e-68

adenylylsulfate kinase; Provisional


Pssm-ID: 179157  Cd Length: 175  Bit Score: 220.28  E-value: 1.28e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194376436  45 RGCTVWLTGFSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRHGLNRNLGFSPGDREENIRRIAEVAKLFADAGLVCITS 124
Cdd:PRK00889   3 RGVTVWFTGLSGAGKTTIARALAEKLREAGYPVEVLDGDAVRTNLSKGLGFSKEDRDTNIRRIGFVANLLTRHGVIVLVS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194376436 125 FISPFAKDRENARkihesAGLP-FFEIFVDAPLNICESRDVKGLYKRARAGEIKGFTGIDSDYEKPETPERVLKTNLSTV 203
Cdd:PRK00889  83 AISPYRETREEVR-----ANIGnFLEVFVDAPLEVCEQRDVKGLYAKARAGEIKHFTGIDDPYEPPLNPEVECRTDLESL 157

                        170
                 ....*....|....*...
gi 194376436 204 SDCVHQVVELLQEQNIVP 221
Cdd:PRK00889 158 EESVDKVLQKLEELGYLV 175
PUA_2 pfam14306
PUA-like domain; This PUA like domain is found at the N-terminus of ATP-sulfurylase enzymes.
 230-380 3.94e-66

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: 213.15  E-value: 3.94e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194376436  230 ELFVPENKLDHVRAEAETLPSLSITKLDLQWVQVLSEGWATPLKGFMREKEYLQVMHFDTlLDDGVInMSIPIVLPVSAE 309
Cdd:pfam14306  10 DLVVRDAEREELLAEAAELPSIELSKRELCDLELIAIGGFSPLTGFMGEADYLSVLEFMR-LADGLL-WSIPITLDVSEE 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 194376436  310 DKTRLEGCSKFVLAHG-GRRVAILRDAEFYEHRKEERCSRVWGTTCTKHPHIKMVMESGDWLVGGDLQVLEK 380
Cdd:pfam14306  88 DAASLKEGDRVALRDPeGEPLAILTVEEIYEPDKEEEAEKVFGTTDPAHPGVKKLYEQGDFYVGGDIEVLNR 159
sat PRK04149
sulfate adenylyltransferase; Reviewed
 230-616 8.80e-62

sulfate adenylyltransferase; Reviewed


Pssm-ID: 235227  Cd Length: 391  Bit Score: 209.72  E-value: 8.80e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194376436 230 ELFVPENKLDHVRAEAETLPSLSITKLDLQWVQVLSEGWATPLKGFMREKEYLQVMHFDTLLDDGVinMSIPIVLPVSAE 309
Cdd:PRK04149  13 NRVVEGRDREEILEEAESLPRIELDERAASDLEMIAIGGFSPLTGFMGREDYDSVVEEMRLANGLV--WSIPITLDVSEE 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194376436 310 DKTRLEGCSKFVLAHGGRRVAILRDAEFYEHRKEERCSRVWGTTCTKHPHIKMVMESGDWLVGGDLQVLEKIRwNDGLDQ 389
Cdd:PRK04149  91 DAASLKEGDEVALVYKGEPYGVLEVEEIYTYDKKKEAEKVYKTTDEKHPGVKKLYEQGDVYLAGPVTLLNRKF-HEPFPR 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194376436 390 YRLTPLELKQKCKEMNADAVFAFQLRNPVHNGHALLMqdtrrrllergyKHPV-----LLLHPLGGWTKDDDVPLDWRMK 464
Cdd:PRK04149 170 FWLTPAETRELFEEKGWKTVVAFQTRNPPHRAHEYLQ------------KCALeivdgLLLNPLVGETKSGDIPAEVRME 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194376436 465 QHAAVLeEGVLDPKSTIVAIFPSPMLYAGPTEVQWHCRSRMIAGANFYIVGRDPAGMphpetkKDLYEPTHGGKVLSM-- 542
Cdd:PRK04149 238 AYEALL-KNYYPKDRVLLSVTPAAMRYAGPREAIFHAIVRKNYGCTHFIVGRDHAGV------GDYYGPYDAQEIFDEft 310

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 194376436 543 APGLtSVEIIPFRVAAYNKAKKAMDFYDPARHNEFD--FISGTRMRKLAREGENPPDGFMAPKAWKVLTDYYRSLE 616
Cdd:PRK04149 311 EEEL-GITPLKFEEAFYCPKCGGMASEKTCPHGKEDrvHLSGTKVREMLREGEKPPPEFSRPEVAEVLIKGLKKYG 385
PRK05537 PRK05537
bifunctional sulfate adenylyltransferase/adenylylsulfate kinase;
46-217 2.56e-53

bifunctional sulfate adenylyltransferase/adenylylsulfate kinase;


Pssm-ID: 180124 [Multi-domain]  Cd Length: 568  Bit Score: 191.42  E-value: 2.56e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194376436  46 GCTVWLTGFSGAGKTTISFALEEYLVSH-AIPCYSLDGDNVRHGLNRNLGFSPGDREENIRRIAEVAKLFADAGLVCITS 124
Cdd:PRK05537 392 GFTVFFTGLSGAGKSTIAKALMVKLMEMrGRPVTLLDGDVVRKHLSSELGFSKEDRDLNILRIGFVASEITKNGGIAICA 471

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194376436 125 FISPFAKDRENARKIHESAGlPFFEIFVDAPLNICESRDVKGLYKRARAGEIKGFTGIDSDYEKPETPERVLKTNLSTVS 204
Cdd:PRK05537 472 PIAPYRATRREVREMIEAYG-GFIEVHVATPLEVCEQRDRKGLYAKAREGKIKGFTGISDPYEPPANPELVIDTTNVTPD 550

                        170
                 ....*....|...
gi 194376436 205 DCVHQVVELLQEQ 217
Cdd:PRK05537 551 ECAHKILLYLEEK 563
PRK05537 PRK05537
bifunctional sulfate adenylyltransferase/adenylylsulfate kinase;
219-608 7.10e-51

bifunctional sulfate adenylyltransferase/adenylylsulfate kinase;


Pssm-ID: 180124 [Multi-domain]  Cd Length: 568  Bit Score: 184.87  E-value: 7.10e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194376436 219 IVPYTiiKDIHELFVPENKLDHVRAEAETLPSLSITKLDLQWVQVLSEGWATPLKGFMREKEYLQVMHfDTLLDDGVInM 298
Cdd:PRK05537   2 ILPNG--GPLPNLYVSPESREKLKAEALSLPSLDLSPRQICDLELLMNGGFSPLKGFMGRADYECVLE-NMRLADGTL-W 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194376436 299 SIPIVLPVSAEDKTRLEGCSKFVLAHG-GRRVAILRDAEFYEHRKEERCSRVWGTTCTKHPHI-KMVMESGDWLVGGDLQ 376
Cdd:PRK05537  78 PIPITLDVSEKFAAGLEIGERIALRDQeGVLLAILTVSDIWEPDKEREAEAVFGTTDPAHPGVnYLHRWAGKFYLGGPLT 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194376436 377 VLEKIRWNDgLDQYRLTPLELKQKCKEMNADAVFAFQLRNPVHNGHALLmqdTRRRLLERGYKhpvLLLHPLGGWTKDDD 456
Cdd:PRK05537 158 GIQLPVHYD-FVQLRLTPAELRARFRKLGWRRVVAFQTRNPLHRAHEEL---TKRAAREVGAN---LLIHPVVGMTKPGD 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194376436 457 VPLDWRMKQHAAVLEEgvLDPKSTIVAIFPSPMLYAGPTEVQWHCRSRMIAGANFYIVGRDPAGMPHPETKKDLYEPTHG 536
Cdd:PRK05537 231 IDHFTRVRCYEALLDK--YPPATTLLSLLPLAMRMAGPREALWHAIIRRNYGCTHFIVGRDHAGPGKDSRGKPFYGPYDA 308

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 194376436 537 GKVLSMAPGLTSVEIIPFRVAAYNKAKKAMDFYDPARHNE-FDFISGTRMRKLAREGENPPDGFMAPKAWKVL 608
Cdd:PRK05537 309 QELFAKYADEIGITMVPFKEMVYVQDKAQYVPVDEVPQGAtVLTISGTELRRRLREGLEIPEWFSFPEVVAEL 381
PRK05541 PRK05541
adenylylsulfate kinase; Provisional
 46-219 8.98e-23

adenylylsulfate kinase; Provisional


Pssm-ID: 235498  Cd Length: 176  Bit Score: 95.51  E-value: 8.98e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194376436  46 GCTVWLTGFSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRHGLNRNlGFSPGDREENIRRIAEVAKLFADAGLVCITSF 125
Cdd:PRK05541   7 GYVIWITGLAGSGKTTIAKALYERLKLKYSNVIYLDGDELREILGHY-GYDKQSRIEMALKRAKLAKFLADQGMIVIVTT 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194376436 126 ISPFakdRENARkiHESAGLP-FFEIFVDAPLNICESRDVKGLYKRARAGEIKGFTGIDSDYEKPETPERVLKTNLSTVS 204
Cdd:PRK05541  86 ISMF---DEIYA--YNRKHLPnYFEVYLKCDMEELIRRDQKGLYTKALKGEIKNVVGVDIPFDEPKADLVIDNSCRTSLD 160

                        170
                 ....*....|....*
gi 194376436 205 DCVHQVVELLQEQNI 219
Cdd:PRK05541 161 EKVDLILNKLKLRLI 175
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
49-180 8.05e-08

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


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 52.22  E-value: 8.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194376436  49 VWLTGFSGAGKTTISFALEEYLvsHAIPcysLDGDNVRHGLnRNLGFSPGDREENIR-----RIAEVAKLFADAGLVCIt 123
Cdd:COG0645    2 ILVCGLPGSGKSTLARALAERL--GAVR---LRSDVVRKRL-FGAGLAPLERSPEATartyaRLLALARELLAAGRSVI- 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 194376436 124 sFISPFAK--DRENARKIHESAGLPFFEIFVDAPLNICESRdvkgLYKRARAGEIKGFT 180
Cdd:COG0645   75 -LDATFLRraQREAFRALAEEAGAPFVLIWLDAPEEVLRER----LEARNAEGGDSDAT 128
Kti12 COG4088
tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) ...
 51-216 1.46e-06

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: 48.95  E-value: 1.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194376436  51 LTGFSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRHGLNRNLGFSPgDREENIRRIAE-VAKLFADAGLVCITSFISPF 129
Cdd:COG4088    9 LTGPPGSGKTTFAKALAQRLYAEGIAVALLHSDDFRRFLVNESFPKE-TYEEVVEDVRTtTADNALDNGYSVIVDGTFYY 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194376436 130 AKDRENARKIHESAGlPFFEIFVDAPLNICESRDvkglykRARAGEI--KGFTGIDSDYEKPET---PERVLKTNLSTVS 204
Cdd:COG4088   88 RSWQRDFRNLAKHKA-PIHIIYLKAPLETALRRN------RERGEPIpeRVIARMYRKFDKPGTkdrPDLVIDTTEDSVS 160

                        170
                 ....*....|..
gi 194376436 205 DCVHQVVELLQE 216
Cdd:COG4088  161 ETLDAILKAIET 172
AAA_33 pfam13671
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ...
 49-175 2.05e-05

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: 44.61  E-value: 2.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194376436   49 VWLTGFSGAGKTTISFALEEylvshAIPCYSLDGDNVRHGLNRNLGFSPGDREENI----RRIAEVAKLFADAGLVCITS 124
Cdd:pfam13671   2 ILLVGLPGSGKSTLARRLLE-----ELGAVRLSSDDERKRLFGEGRPSISYYTDATdrtyERLHELARIALRAGRPVILD 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 194376436  125 FisPFAKDRENARKIH--ESAGLPFFEIFVDAPLNICESRDVkglyKRARAGE 175
Cdd:pfam13671  77 A--TNLRRDERARLLAlaREYGVPVRIVVFEAPEEVLRERLA----ARARAGG 123
GntK cd02021
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting ...
 51-194 7.81e-03

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: 37.23  E-value: 7.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194376436  51 LTGFSGAGKTTISFALeeylvSHAIPCYSLDGDNVRHGLNRNL---GFSPGDRE-----ENIRRIAEVAKLFADAGLVCI 122
Cdd:cd02021    4 VMGVSGSGKSTVGKAL-----AERLGAPFIDGDDLHPPANIAKmaaGIPLNDEDrwpwlQALTDALLAKLASAGEGVVVA 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 194376436 123 TSFIspfaKD--RENARKIHESAGLPFfeIFVDAPLNICESRDvkglykRARAGEIKGFTGIDSDYEKPETPER 194
Cdd:cd02021   79 CSAL----KRiyRDILRGGAANPRVRF--VHLDGPREVLAERL------AARKGHFMPADLLDSQFETLEPPGE 140
 
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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