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Conserved domains on  [gi|62912492|ref|NP_001015880|]
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bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 2 isoform b [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, ...
 244-612 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 62912492 244 LPSLSITKLDLQWVQVLSEGWATPLKGFMREKEYLQVMHFDTLLDGmalpdgvINMSIPIVLPVSAEDKTRLEGCSKFVL 323
Cdd:cd00517   1 LPSVELSERDLCDLEMLAEGGFSPLTGFMTEADYLSVLEEMRLLDG-------TLWPIPIVLDVSEEDAKRLKEGERVAL 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912492 324 AHGGRRVAILRDAEFYEHRKEERCSRVWGTTCTKHPHIKMVMESGDWLVGGDLQVLEKIRWNDgLDQYRLTPLELKQKCK 403
Cdd:cd00517  74 RYPGQPLAILTVEEIYEPDKEEEAARVFGTTDPHHPGVKKVMEQGDWLVGGPIEVLELPPFPD-FDQYRLTPAELRALFK 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912492 404 EMNADAVFAFQLRNPVHNGHALLMQDTRRRLLErgykhPVLLLHPLGGWTKDDDVPLDWRMKQHAAVLEEGVLdPKSTIV 483
Cdd:cd00517 153 ERGWRRVVAFQTRNPMHRAHEELMKRAAEKLLN-----DGLLLHPLVGWTKPGDVPDEVRMRAYEALLEEYYL-PERTVL 226

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912492 484 AIFPSPMLYAGPTEVQWHCRSRMIAGANFYIVGRDPAGMPHPETKKDLYEPTHGGKVLSMApglTSVEIIPFRVAAYNKA 563
Cdd:cd00517 227 AILPLPMRYAGPREALWHAIIRKNYGATHFIVGRDHAGVGHPGDYYGPYDAQEIFKKLAPE---LGIEPVPFREAAYCPK 303

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|
gi 62912492 564 KKAMDFYDPARHNE-FDFISGTRMRKLAREGENPPDGFMAPKAWKVLTDY 612
Cdd:cd00517 304 CDGMASEDTCPHGEdFLNISGTKLRKMLREGEKPPEWFMRPEVAKVLREY 353
CysC COG0529
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ...
 23-217 1.48e-103

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: 311.64  E-value: 1.48e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912492  23 HHVSRNKRGQvvgtRGGFRGCTVWLTGLSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRHGLNRNLGFSPGDREENIRR 102
Cdd:COG0529   1 SAVTREERAA----LKGQKGFVVWFTGLSGSGKSTLANALERRLFERGRHVYLLDGDNVRHGLNKDLGFSKEDRDENIRR 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912492 103 IAEVAKLFADAGLVCITSFISPFAKDRENARKIHESAglPFFEIFVDAPLNICESRDVKGLYKRARAGEIKGFTGIDSDY 182
Cdd:COG0529  77 IGEVAKLLADAGLIVLVAFISPYRADREEARELIGEG--EFIEVYVDTPLEVCEARDPKGLYAKARAGEIKNFTGIDDPY 154

                       170       180       190
                ....*....|....*....|....*....|....*
gi 62912492 183 EKPETPERVLKTNLSTVSDCVHQVVELLQEQNIVP 217
Cdd:COG0529 155 EAPENPELVLDTDKESVEESVEKILAYLEERGYIS 189
 
Name Accession Description Interval E-value
ATPS cd00517
ATP-sulfurylase; ATP-sulfurylase (ATPS), also known as sulfate adenylate transferase, ...
 244-612 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 62912492 244 LPSLSITKLDLQWVQVLSEGWATPLKGFMREKEYLQVMHFDTLLDGmalpdgvINMSIPIVLPVSAEDKTRLEGCSKFVL 323
Cdd:cd00517   1 LPSVELSERDLCDLEMLAEGGFSPLTGFMTEADYLSVLEEMRLLDG-------TLWPIPIVLDVSEEDAKRLKEGERVAL 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912492 324 AHGGRRVAILRDAEFYEHRKEERCSRVWGTTCTKHPHIKMVMESGDWLVGGDLQVLEKIRWNDgLDQYRLTPLELKQKCK 403
Cdd:cd00517  74 RYPGQPLAILTVEEIYEPDKEEEAARVFGTTDPHHPGVKKVMEQGDWLVGGPIEVLELPPFPD-FDQYRLTPAELRALFK 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912492 404 EMNADAVFAFQLRNPVHNGHALLMQDTRRRLLErgykhPVLLLHPLGGWTKDDDVPLDWRMKQHAAVLEEGVLdPKSTIV 483
Cdd:cd00517 153 ERGWRRVVAFQTRNPMHRAHEELMKRAAEKLLN-----DGLLLHPLVGWTKPGDVPDEVRMRAYEALLEEYYL-PERTVL 226

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912492 484 AIFPSPMLYAGPTEVQWHCRSRMIAGANFYIVGRDPAGMPHPETKKDLYEPTHGGKVLSMApglTSVEIIPFRVAAYNKA 563
Cdd:cd00517 227 AILPLPMRYAGPREALWHAIIRKNYGATHFIVGRDHAGVGHPGDYYGPYDAQEIFKKLAPE---LGIEPVPFREAAYCPK 303

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|
gi 62912492 564 KKAMDFYDPARHNE-FDFISGTRMRKLAREGENPPDGFMAPKAWKVLTDY 612
Cdd:cd00517 304 CDGMASEDTCPHGEdFLNISGTKLRKMLREGEKPPEWFMRPEVAKVLREY 353
sopT TIGR00339
ATP sulphurylase; This enzyme forms adenosine 5'-phosphosulfate (APS) from ATP and free ...
 226-611 2.38e-138

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: 408.31  E-value: 2.38e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912492   226 ELFVPENKLDH-VRAEAETLPSLSITKLDLQWVQVLSEGWATPLKGFMREKEYLQVMHFDTLLDGmalpdgvINMSIPIV 304
Cdd:TIGR00339   8 ELVVRDPDEEHkLLAEAESLPSITLSDRQLCDLELLGNGAFSPLEGFMNEADYDSVVESMRLSDG-------VLFSVPIT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912492   305 LPVSAEDKTRLEGCSKFVLAH-GGRRVAILRDAEFYEHRKEERCSRVWGTTCTKHPHIKMVMESGDWLVGGDLQVLEKIR 383
Cdd:TIGR00339  81 LDIDDEDADDIKLGDRIALTDpKGQPLAILTIEEVYKPNKEKEAKKVFGTTDPEHPGVVYLNTAGNYYIGGPIEVINLPK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912492   384 WnDGLDQYRLTPLELKQKCKEMNADAVFAFQLRNPVHNGHALLMQDTRRRLlergyKHPVLLLHPLGGWTKDDDVPLDWR 463
Cdd:TIGR00339 161 F-YDFPRFRFTPAELREEFKERGWDTVVAFQTRNPMHRAHEELTKRAAERL-----PNAGVLVHPLVGLTKPGDIPAEVR 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912492   464 MKQHAaVLEEGVLDPKSTIVAIFPSPMLYAGPTEVQWHCRSRMIAGANFYIVGRDPAGMPHPETKKDLYEPTHGGKVLSM 543
Cdd:TIGR00339 235 MRAYE-VLKEGYPNPERTVVSFLPLAMRYAGPREAIWHAIIRKNYGATHFIVGRDHAGPGSNSKGQDFYGPYDAQELFEK 313

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912492   544 APGLTSVEIIPFRVAAYNKAKKAMDFYDPARHNEFDF--ISGTRMRKLAREGENPPDGFMAPKAWKVLTD 611
Cdd:TIGR00339 314 YKAELGIKIVPFRHVAYCPDEDEYAPADQAGHTNLRTlnISGTKLRGMLRNGVFPPEWFSRPEVVKILRE 383
CysC COG0529
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ...
 23-217 1.48e-103

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: 311.64  E-value: 1.48e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912492  23 HHVSRNKRGQvvgtRGGFRGCTVWLTGLSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRHGLNRNLGFSPGDREENIRR 102
Cdd:COG0529   1 SAVTREERAA----LKGQKGFVVWFTGLSGSGKSTLANALERRLFERGRHVYLLDGDNVRHGLNKDLGFSKEDRDENIRR 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912492 103 IAEVAKLFADAGLVCITSFISPFAKDRENARKIHESAglPFFEIFVDAPLNICESRDVKGLYKRARAGEIKGFTGIDSDY 182
Cdd:COG0529  77 IGEVAKLLADAGLIVLVAFISPYRADREEARELIGEG--EFIEVYVDTPLEVCEARDPKGLYAKARAGEIKNFTGIDDPY 154

                       170       180       190
                ....*....|....*....|....*....|....*
gi 62912492 183 EKPETPERVLKTNLSTVSDCVHQVVELLQEQNIVP 217
Cdd:COG0529 155 EAPENPELVLDTDKESVEESVEKILAYLEERGYIS 189
APSK cd02027
Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5 ...
 44-194 1.32e-99

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: 299.78  E-value: 1.32e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912492  44 TVWLTGLSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRHGLNRNLGFSPGDREENIRRIAEVAKLFADAGLVCITSFIS 123
Cdd:cd02027   1 VIWLTGLSGSGKSTIARALEEKLFQRGRPVYVLDGDNVRHGLNKDLGFSREDREENIRRIAEVAKLLADAGLIVIAAFIS 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62912492 124 PFAKDRENARKIHEsaGLPFFEIFVDAPLNICESRDVKGLYKRARAGEIKGFTGIDSDYEKPETPERVLKT 194
Cdd:cd02027  81 PYREDREAARKIIG--GGDFLEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDDPYEAPENPDLVLDT 149
APS_kinase pfam01583
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3 ...
 41-194 2.30e-96

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: 291.53  E-value: 2.30e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912492    41 RGCTVWLTGLSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRHGLNRNLGFSPGDREENIRRIAEVAKLFADAGLVCITS 120
Cdd:pfam01583   1 RGCTIWLTGLSGAGKSTIANALERKLFEQGRSVYVLDGDNVRHGLNKDLGFSEEDRTENIRRIGEVAKLFADAGLIVITA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62912492   121 FISPFAKDRENARKIHESAglPFFEIFVDAPLNICESRDVKGLYKRARAGEIKGFTGIDSDYEKPETPERVLKT 194
Cdd:pfam01583  81 FISPYREDREQARELHEEG--KFIEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDSPYEAPENPELVLDT 152
ATP-sulfurylase pfam01747
ATP-sulfurylase; This domain is the catalytic domain of ATP-sulfurylase or sulfate ...
 389-612 7.11e-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: 282.51  E-value: 7.11e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912492   389 DQYRLTPLELKQKCKEMNADAVFAFQLRNPVHNGHALLMQDTRRRLlERGYkhpvLLLHPLGGWTKDDDVPLDWRMKQHA 468
Cdd:pfam01747   1 DEYRLTPAETRALFKEKGWRTVVAFQTRNPLHRAHEELMKRALEEL-EADG----LLLHPLVGPTKPGDVPAEVRVRCYE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912492   469 AVLEEgVLDPKSTIVAIFPSPMLYAGPTEVQWHCRSRMIAGANFYIVGRDPAGMPHpetkkdLYEPTHGGKVLSMAPGLT 548
Cdd:pfam01747  76 ALLEN-YLPPDRVVLALLPLAMRYAGPREALLHAIIRKNYGCTHFIVGRDHAGVGD------FYGPYDAQEIFDEYPGEL 148

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 62912492   549 SVEIIPFRVAAYNKAKKAM-DFYDPARHNEFDFISGTRMRKLAREGENPPDGFMAPKAWKVLTDY 612
Cdd:pfam01747 149 GIEPVPFREAVYCKKCGEMaSTKCPHGGEDRLFISGTKVRELLREGEEPPEWFSRPEVAKVLREY 213
PRK03846 PRK03846
adenylylsulfate kinase; Provisional
 15-216 7.49e-90

adenylylsulfate kinase; Provisional


Pssm-ID: 179661  Cd Length: 198  Bit Score: 276.44  E-value: 7.49e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912492   15 STNVVYQAHHVSRNKRGQvvgtRGGFRGCTVWLTGLSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRHGLNRNLGFSPG 94
Cdd:PRK03846   1 DENIVWHQHPVTKAQREQ----LHGHKGVVLWFTGLSGSGKSTVAGALEEALHELGVSTYLLDGDNVRHGLCSDLGFSDA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912492   95 DREENIRRIAEVAKLFADAGLVCITSFISPFAKDRENARKIhesagLP---FFEIFVDAPLNICESRDVKGLYKRARAGE 171
Cdd:PRK03846  77 DRKENIRRVGEVAKLMVDAGLVVLTAFISPHRAERQMVRER-----LGegeFIEVFVDTPLAICEARDPKGLYKKARAGE 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 62912492  172 IKGFTGIDSDYEKPETPERVLKTNLSTVSDCVHQVVELLQEQNIV 216
Cdd:PRK03846 152 IRNFTGIDSVYEAPESPEIHLDTGEQLVTNLVEQLLDYLRQRDII 196
apsK TIGR00455
adenylyl-sulfate kinase; This protein, adenylylsulfate kinase, is often found as a fusion ...
 24-210 4.51e-81

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: 253.16  E-value: 4.51e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912492    24 HVSRNKRGQVVGTRGgfrgCTVWLTGLSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRHGLNRNLGFSPGDREENIRRI 103
Cdd:TIGR00455   4 AITKDERQALNGHRG----VVIWLTGLSGSGKSTIANALEKKLESKGYRVYVLDGDNVRHGLNKDLGFSEEDRKENIRRI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912492   104 AEVAKLFADAGLVCITSFISPFAKDRENARKIHESAglPFFEIFVDAPLNICESRDVKGLYKRARAGEIKGFTGIDSDYE 183
Cdd:TIGR00455  80 GEVAKLFVRNGIIVITSFISPYRADRQMVRELIEKG--EFIEVFVDCPLEVCEQRDPKGLYKKARNGEIKGFTGIDSPYE 157

                         170       180
                  ....*....|....*....|....*..
gi 62912492   184 KPETPERVLKTNLSTVSDCVHQVVELL 210
Cdd:TIGR00455 158 APENPEVVLDTDQNDREECVGQIIEKL 184
MET3 COG2046
ATP sulfurylase (sulfate adenylyltransferase) [Inorganic ion transport and metabolism]; ATP ...
 226-618 2.81e-74

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: 242.74  E-value: 2.81e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912492 226 ELFVPENKLDHVRAEAETLPSLSITKLDLQWVQVLSEGWATPLKGFMREKEYLQVmhfdtlLDGMALPDGVInMSIPIVL 305
Cdd:COG2046  14 NRVVPGEEREALLEEAKGLPSIELSSRALSDLEMIAIGGFSPLTGFMNKADYESV------VENMRLADGLL-WPIPITL 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912492 306 PVSAEDKTRLEGCSKFVL-AHGGRRVAILRDAEFYEHRKEERCSRVWGTTCTKHPHIKMVMESGDWLVGGDLQVLEKIRW 384
Cdd:COG2046  87 DVSEEDAAGLKEGDEVALrDEEGEPLAVLEVEEIYEYDKEEEAEKVYGTTDPAHPGVAKLYERGDVYLGGPITLLNRPKH 166

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912492 385 NDgLDQYRLTPLELKQKCKEMNADAVFAFQLRNPVHNGHALLMqdtrRRLLERGYkhpVLLLHPLGGWTKDDDVPLDWRM 464
Cdd:COG2046 167 PD-FPDYRLTPAETRALFEEKGWKTVVAFQTRNPMHRAHEYLQ----KRALETVD---GLLIHPLVGETKPGDIPAEVRV 238

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912492 465 KQHAAVLEEGVlDPKSTIVAIFPSPMLYAGPTEVQWH--CRSRMiaGANFYIVGRDPAGMPhpetkkDLYEP-------- 534
Cdd:COG2046 239 RCYEALLENYY-PKDRVLLSGLPLAMRYAGPREALLHaiIRKNY--GCTHFIVGRDHAGVG------DYYGPydaqeifd 309

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912492 535 THGGKVLSMapgltsvEIIPFRVAAYNKAKKAMDFYDPARHNEFDF--ISGTRMRKLAREGENPPDGFMAPKAWKVLTDY 612
Cdd:COG2046 310 EFPPGELGI-------EPLKFEEAFYCKKCGGMATSKTCPHDKEDRvsLSGTKVREMLREGEEPPPEFSRPEVAEILRKY 382


                ....*.
gi 62912492 613 YRSLEK 618
Cdd:COG2046 383 YQPFGE 388
sat PRK04149
sulfate adenylyltransferase; Reviewed
 226-617 3.86e-64

sulfate adenylyltransferase; Reviewed


Pssm-ID: 235227  Cd Length: 391  Bit Score: 216.27  E-value: 3.86e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912492  226 ELFVPENKLDHVRAEAETLPSLSITKLDLQWVQVLSEGWATPLKGFMREKEYLQVmhfdtlLDGMALPDGVInMSIPIVL 305
Cdd:PRK04149  13 NRVVEGRDREEILEEAESLPRIELDERAASDLEMIAIGGFSPLTGFMGREDYDSV------VEEMRLANGLV-WSIPITL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912492  306 PVSAEDKTRLEGCSKFVLAHGGRRVAILRDAEFYEHRKEERCSRVWGTTCTKHPHIKMVMESGDWLVGGDLQVLEKIRwN 385
Cdd:PRK04149  86 DVSEEDAASLKEGDEVALVYKGEPYGVLEVEEIYTYDKKKEAEKVYKTTDEKHPGVKKLYEQGDVYLAGPVTLLNRKF-H 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912492  386 DGLDQYRLTPLELKQKCKEMNADAVFAFQLRNPVHNGHALLMqdtrrrllergyKHPV-----LLLHPLGGWTKDDDVPL 460
Cdd:PRK04149 165 EPFPRFWLTPAETRELFEEKGWKTVVAFQTRNPPHRAHEYLQ------------KCALeivdgLLLNPLVGETKSGDIPA 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912492  461 DWRMKQHAAVLeEGVLDPKSTIVAIFPSPMLYAGPTEVQWHCRSRMIAGANFYIVGRDPAGMphpetkKDLYEPTHGGKV 540
Cdd:PRK04149 233 EVRMEAYEALL-KNYYPKDRVLLSVTPAAMRYAGPREAIFHAIVRKNYGCTHFIVGRDHAGV------GDYYGPYDAQEI 305

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912492  541 LSM--APGLtSVEIIPFRVAAYNKAKKAMDFYDPARHNEFD--FISGTRMRKLAREGENPPDGFMAPKAWKVLTDYYRSL 616
Cdd:PRK04149 306 FDEftEEEL-GITPLKFEEAFYCPKCGGMASEKTCPHGKEDrvHLSGTKVREMLREGEKPPPEFSRPEVAEVLIKGLKKY 384


                 .
gi 62912492  617 E 617
Cdd:PRK04149 385 G 385
 
Name Accession Description Interval E-value
ATPS cd00517
ATP-sulfurylase; ATP-sulfurylase (ATPS), also known as sulfate adenylate transferase, ...
 244-612 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 62912492 244 LPSLSITKLDLQWVQVLSEGWATPLKGFMREKEYLQVMHFDTLLDGmalpdgvINMSIPIVLPVSAEDKTRLEGCSKFVL 323
Cdd:cd00517   1 LPSVELSERDLCDLEMLAEGGFSPLTGFMTEADYLSVLEEMRLLDG-------TLWPIPIVLDVSEEDAKRLKEGERVAL 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912492 324 AHGGRRVAILRDAEFYEHRKEERCSRVWGTTCTKHPHIKMVMESGDWLVGGDLQVLEKIRWNDgLDQYRLTPLELKQKCK 403
Cdd:cd00517  74 RYPGQPLAILTVEEIYEPDKEEEAARVFGTTDPHHPGVKKVMEQGDWLVGGPIEVLELPPFPD-FDQYRLTPAELRALFK 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912492 404 EMNADAVFAFQLRNPVHNGHALLMQDTRRRLLErgykhPVLLLHPLGGWTKDDDVPLDWRMKQHAAVLEEGVLdPKSTIV 483
Cdd:cd00517 153 ERGWRRVVAFQTRNPMHRAHEELMKRAAEKLLN-----DGLLLHPLVGWTKPGDVPDEVRMRAYEALLEEYYL-PERTVL 226

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912492 484 AIFPSPMLYAGPTEVQWHCRSRMIAGANFYIVGRDPAGMPHPETKKDLYEPTHGGKVLSMApglTSVEIIPFRVAAYNKA 563
Cdd:cd00517 227 AILPLPMRYAGPREALWHAIIRKNYGATHFIVGRDHAGVGHPGDYYGPYDAQEIFKKLAPE---LGIEPVPFREAAYCPK 303

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|
gi 62912492 564 KKAMDFYDPARHNE-FDFISGTRMRKLAREGENPPDGFMAPKAWKVLTDY 612
Cdd:cd00517 304 CDGMASEDTCPHGEdFLNISGTKLRKMLREGEKPPEWFMRPEVAKVLREY 353
sopT TIGR00339
ATP sulphurylase; This enzyme forms adenosine 5'-phosphosulfate (APS) from ATP and free ...
 226-611 2.38e-138

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: 408.31  E-value: 2.38e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912492   226 ELFVPENKLDH-VRAEAETLPSLSITKLDLQWVQVLSEGWATPLKGFMREKEYLQVMHFDTLLDGmalpdgvINMSIPIV 304
Cdd:TIGR00339   8 ELVVRDPDEEHkLLAEAESLPSITLSDRQLCDLELLGNGAFSPLEGFMNEADYDSVVESMRLSDG-------VLFSVPIT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912492   305 LPVSAEDKTRLEGCSKFVLAH-GGRRVAILRDAEFYEHRKEERCSRVWGTTCTKHPHIKMVMESGDWLVGGDLQVLEKIR 383
Cdd:TIGR00339  81 LDIDDEDADDIKLGDRIALTDpKGQPLAILTIEEVYKPNKEKEAKKVFGTTDPEHPGVVYLNTAGNYYIGGPIEVINLPK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912492   384 WnDGLDQYRLTPLELKQKCKEMNADAVFAFQLRNPVHNGHALLMQDTRRRLlergyKHPVLLLHPLGGWTKDDDVPLDWR 463
Cdd:TIGR00339 161 F-YDFPRFRFTPAELREEFKERGWDTVVAFQTRNPMHRAHEELTKRAAERL-----PNAGVLVHPLVGLTKPGDIPAEVR 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912492   464 MKQHAaVLEEGVLDPKSTIVAIFPSPMLYAGPTEVQWHCRSRMIAGANFYIVGRDPAGMPHPETKKDLYEPTHGGKVLSM 543
Cdd:TIGR00339 235 MRAYE-VLKEGYPNPERTVVSFLPLAMRYAGPREAIWHAIIRKNYGATHFIVGRDHAGPGSNSKGQDFYGPYDAQELFEK 313

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912492   544 APGLTSVEIIPFRVAAYNKAKKAMDFYDPARHNEFDF--ISGTRMRKLAREGENPPDGFMAPKAWKVLTD 611
Cdd:TIGR00339 314 YKAELGIKIVPFRHVAYCPDEDEYAPADQAGHTNLRTlnISGTKLRGMLRNGVFPPEWFSRPEVVKILRE 383
CysC COG0529
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ...
 23-217 1.48e-103

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: 311.64  E-value: 1.48e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912492  23 HHVSRNKRGQvvgtRGGFRGCTVWLTGLSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRHGLNRNLGFSPGDREENIRR 102
Cdd:COG0529   1 SAVTREERAA----LKGQKGFVVWFTGLSGSGKSTLANALERRLFERGRHVYLLDGDNVRHGLNKDLGFSKEDRDENIRR 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912492 103 IAEVAKLFADAGLVCITSFISPFAKDRENARKIHESAglPFFEIFVDAPLNICESRDVKGLYKRARAGEIKGFTGIDSDY 182
Cdd:COG0529  77 IGEVAKLLADAGLIVLVAFISPYRADREEARELIGEG--EFIEVYVDTPLEVCEARDPKGLYAKARAGEIKNFTGIDDPY 154

                       170       180       190
                ....*....|....*....|....*....|....*
gi 62912492 183 EKPETPERVLKTNLSTVSDCVHQVVELLQEQNIVP 217
Cdd:COG0529 155 EAPENPELVLDTDKESVEESVEKILAYLEERGYIS 189
APSK cd02027
Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5 ...
 44-194 1.32e-99

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: 299.78  E-value: 1.32e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912492  44 TVWLTGLSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRHGLNRNLGFSPGDREENIRRIAEVAKLFADAGLVCITSFIS 123
Cdd:cd02027   1 VIWLTGLSGSGKSTIARALEEKLFQRGRPVYVLDGDNVRHGLNKDLGFSREDREENIRRIAEVAKLLADAGLIVIAAFIS 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62912492 124 PFAKDRENARKIHEsaGLPFFEIFVDAPLNICESRDVKGLYKRARAGEIKGFTGIDSDYEKPETPERVLKT 194
Cdd:cd02027  81 PYREDREAARKIIG--GGDFLEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDDPYEAPENPDLVLDT 149
APS_kinase pfam01583
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3 ...
 41-194 2.30e-96

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: 291.53  E-value: 2.30e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912492    41 RGCTVWLTGLSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRHGLNRNLGFSPGDREENIRRIAEVAKLFADAGLVCITS 120
Cdd:pfam01583   1 RGCTIWLTGLSGAGKSTIANALERKLFEQGRSVYVLDGDNVRHGLNKDLGFSEEDRTENIRRIGEVAKLFADAGLIVITA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62912492   121 FISPFAKDRENARKIHESAglPFFEIFVDAPLNICESRDVKGLYKRARAGEIKGFTGIDSDYEKPETPERVLKT 194
Cdd:pfam01583  81 FISPYREDREQARELHEEG--KFIEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDSPYEAPENPELVLDT 152
ATP-sulfurylase pfam01747
ATP-sulfurylase; This domain is the catalytic domain of ATP-sulfurylase or sulfate ...
 389-612 7.11e-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: 282.51  E-value: 7.11e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912492   389 DQYRLTPLELKQKCKEMNADAVFAFQLRNPVHNGHALLMQDTRRRLlERGYkhpvLLLHPLGGWTKDDDVPLDWRMKQHA 468
Cdd:pfam01747   1 DEYRLTPAETRALFKEKGWRTVVAFQTRNPLHRAHEELMKRALEEL-EADG----LLLHPLVGPTKPGDVPAEVRVRCYE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912492   469 AVLEEgVLDPKSTIVAIFPSPMLYAGPTEVQWHCRSRMIAGANFYIVGRDPAGMPHpetkkdLYEPTHGGKVLSMAPGLT 548
Cdd:pfam01747  76 ALLEN-YLPPDRVVLALLPLAMRYAGPREALLHAIIRKNYGCTHFIVGRDHAGVGD------FYGPYDAQEIFDEYPGEL 148

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 62912492   549 SVEIIPFRVAAYNKAKKAM-DFYDPARHNEFDFISGTRMRKLAREGENPPDGFMAPKAWKVLTDY 612
Cdd:pfam01747 149 GIEPVPFREAVYCKKCGEMaSTKCPHGGEDRLFISGTKVRELLREGEEPPEWFSRPEVAKVLREY 213
PRK03846 PRK03846
adenylylsulfate kinase; Provisional
 15-216 7.49e-90

adenylylsulfate kinase; Provisional


Pssm-ID: 179661  Cd Length: 198  Bit Score: 276.44  E-value: 7.49e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912492   15 STNVVYQAHHVSRNKRGQvvgtRGGFRGCTVWLTGLSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRHGLNRNLGFSPG 94
Cdd:PRK03846   1 DENIVWHQHPVTKAQREQ----LHGHKGVVLWFTGLSGSGKSTVAGALEEALHELGVSTYLLDGDNVRHGLCSDLGFSDA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912492   95 DREENIRRIAEVAKLFADAGLVCITSFISPFAKDRENARKIhesagLP---FFEIFVDAPLNICESRDVKGLYKRARAGE 171
Cdd:PRK03846  77 DRKENIRRVGEVAKLMVDAGLVVLTAFISPHRAERQMVRER-----LGegeFIEVFVDTPLAICEARDPKGLYKKARAGE 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 62912492  172 IKGFTGIDSDYEKPETPERVLKTNLSTVSDCVHQVVELLQEQNIV 216
Cdd:PRK03846 152 IRNFTGIDSVYEAPESPEIHLDTGEQLVTNLVEQLLDYLRQRDII 196
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
 13-213 4.44e-86

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 281.05  E-value: 4.44e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912492   13 QKSTNVVYQAHHVSRNKRGqvvgTRGGFRGCTVWLTGLSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRHGLNRNLGFS 92
Cdd:PRK05506 435 RRATNVHWQASDVSREARA----ARKGQKPATVWFTGLSGSGKSTIANLVERRLHALGRHTYLLDGDNVRHGLNRDLGFS 510

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912492   93 PGDREENIRRIAEVAKLFADAGLVCITSFISPFAKDRENARKIHESAglPFFEIFVDAPLNICESRDVKGLYKRARAGEI 172
Cdd:PRK05506 511 DADRVENIRRVAEVARLMADAGLIVLVSFISPFREERELARALHGEG--EFVEVFVDTPLEVCEARDPKGLYAKARAGEI 588

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 62912492  173 KGFTGIDSDYEKPETPERVLKTNLSTVSDCVHQVVELLQEQ 213
Cdd:PRK05506 589 KNFTGIDSPYEAPENPELRLDTTGRSPEELAEQVLELLRRR 629
apsK TIGR00455
adenylyl-sulfate kinase; This protein, adenylylsulfate kinase, is often found as a fusion ...
 24-210 4.51e-81

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: 253.16  E-value: 4.51e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912492    24 HVSRNKRGQVVGTRGgfrgCTVWLTGLSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRHGLNRNLGFSPGDREENIRRI 103
Cdd:TIGR00455   4 AITKDERQALNGHRG----VVIWLTGLSGSGKSTIANALEKKLESKGYRVYVLDGDNVRHGLNKDLGFSEEDRKENIRRI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912492   104 AEVAKLFADAGLVCITSFISPFAKDRENARKIHESAglPFFEIFVDAPLNICESRDVKGLYKRARAGEIKGFTGIDSDYE 183
Cdd:TIGR00455  80 GEVAKLFVRNGIIVITSFISPYRADRQMVRELIEKG--EFIEVFVDCPLEVCEQRDPKGLYKKARNGEIKGFTGIDSPYE 157

                         170       180
                  ....*....|....*....|....*..
gi 62912492   184 KPETPERVLKTNLSTVSDCVHQVVELL 210
Cdd:TIGR00455 158 APENPEVVLDTDQNDREECVGQIIEKL 184
MET3 COG2046
ATP sulfurylase (sulfate adenylyltransferase) [Inorganic ion transport and metabolism]; ATP ...
 226-618 2.81e-74

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: 242.74  E-value: 2.81e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912492 226 ELFVPENKLDHVRAEAETLPSLSITKLDLQWVQVLSEGWATPLKGFMREKEYLQVmhfdtlLDGMALPDGVInMSIPIVL 305
Cdd:COG2046  14 NRVVPGEEREALLEEAKGLPSIELSSRALSDLEMIAIGGFSPLTGFMNKADYESV------VENMRLADGLL-WPIPITL 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912492 306 PVSAEDKTRLEGCSKFVL-AHGGRRVAILRDAEFYEHRKEERCSRVWGTTCTKHPHIKMVMESGDWLVGGDLQVLEKIRW 384
Cdd:COG2046  87 DVSEEDAAGLKEGDEVALrDEEGEPLAVLEVEEIYEYDKEEEAEKVYGTTDPAHPGVAKLYERGDVYLGGPITLLNRPKH 166

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912492 385 NDgLDQYRLTPLELKQKCKEMNADAVFAFQLRNPVHNGHALLMqdtrRRLLERGYkhpVLLLHPLGGWTKDDDVPLDWRM 464
Cdd:COG2046 167 PD-FPDYRLTPAETRALFEEKGWKTVVAFQTRNPMHRAHEYLQ----KRALETVD---GLLIHPLVGETKPGDIPAEVRV 238

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912492 465 KQHAAVLEEGVlDPKSTIVAIFPSPMLYAGPTEVQWH--CRSRMiaGANFYIVGRDPAGMPhpetkkDLYEP-------- 534
Cdd:COG2046 239 RCYEALLENYY-PKDRVLLSGLPLAMRYAGPREALLHaiIRKNY--GCTHFIVGRDHAGVG------DYYGPydaqeifd 309

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912492 535 THGGKVLSMapgltsvEIIPFRVAAYNKAKKAMDFYDPARHNEFDF--ISGTRMRKLAREGENPPDGFMAPKAWKVLTDY 612
Cdd:COG2046 310 EFPPGELGI-------EPLKFEEAFYCKKCGGMATSKTCPHDKEDRvsLSGTKVREMLREGEEPPPEFSRPEVAEILRKY 382


                ....*.
gi 62912492 613 YRSLEK 618
Cdd:COG2046 383 YQPFGE 388
PRK00889 PRK00889
adenylylsulfate kinase; Provisional
 41-217 1.35e-69

adenylylsulfate kinase; Provisional


Pssm-ID: 179157  Cd Length: 175  Bit Score: 222.97  E-value: 1.35e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912492   41 RGCTVWLTGLSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRHGLNRNLGFSPGDREENIRRIAEVAKLFADAGLVCITS 120
Cdd:PRK00889   3 RGVTVWFTGLSGAGKTTIARALAEKLREAGYPVEVLDGDAVRTNLSKGLGFSKEDRDTNIRRIGFVANLLTRHGVIVLVS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912492  121 FISPFAKDRENARkihesAGLP-FFEIFVDAPLNICESRDVKGLYKRARAGEIKGFTGIDSDYEKPETPERVLKTNLSTV 199
Cdd:PRK00889  83 AISPYRETREEVR-----ANIGnFLEVFVDAPLEVCEQRDVKGLYAKARAGEIKHFTGIDDPYEPPLNPEVECRTDLESL 157

                        170
                 ....*....|....*...
gi 62912492  200 SDCVHQVVELLQEQNIVP 217
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.
 226-381 4.52e-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: 4.52e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912492   226 ELFVPENKLDHVRAEAETLPSLSITKLDLQWVQVLSEGWATPLKGFMREKEYLQVMHFdtlldgMALPDGVInMSIPIVL 305
Cdd:pfam14306  10 DLVVRDAEREELLAEAAELPSIELSKRELCDLELIAIGGFSPLTGFMGEADYLSVLEF------MRLADGLL-WSIPITL 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 62912492   306 PVSAEDKTRLEGCSKFVLAHG-GRRVAILRDAEFYEHRKEERCSRVWGTTCTKHPHIKMVMESGDWLVGGDLQVLEK 381
Cdd:pfam14306  83 DVSEEDAASLKEGDRVALRDPeGEPLAILTVEEIYEPDKEEEAEKVFGTTDPAHPGVKKLYEQGDFYVGGDIEVLNR 159
sat PRK04149
sulfate adenylyltransferase; Reviewed
 226-617 3.86e-64

sulfate adenylyltransferase; Reviewed


Pssm-ID: 235227  Cd Length: 391  Bit Score: 216.27  E-value: 3.86e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912492  226 ELFVPENKLDHVRAEAETLPSLSITKLDLQWVQVLSEGWATPLKGFMREKEYLQVmhfdtlLDGMALPDGVInMSIPIVL 305
Cdd:PRK04149  13 NRVVEGRDREEILEEAESLPRIELDERAASDLEMIAIGGFSPLTGFMGREDYDSV------VEEMRLANGLV-WSIPITL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912492  306 PVSAEDKTRLEGCSKFVLAHGGRRVAILRDAEFYEHRKEERCSRVWGTTCTKHPHIKMVMESGDWLVGGDLQVLEKIRwN 385
Cdd:PRK04149  86 DVSEEDAASLKEGDEVALVYKGEPYGVLEVEEIYTYDKKKEAEKVYKTTDEKHPGVKKLYEQGDVYLAGPVTLLNRKF-H 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912492  386 DGLDQYRLTPLELKQKCKEMNADAVFAFQLRNPVHNGHALLMqdtrrrllergyKHPV-----LLLHPLGGWTKDDDVPL 460
Cdd:PRK04149 165 EPFPRFWLTPAETRELFEEKGWKTVVAFQTRNPPHRAHEYLQ------------KCALeivdgLLLNPLVGETKSGDIPA 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912492  461 DWRMKQHAAVLeEGVLDPKSTIVAIFPSPMLYAGPTEVQWHCRSRMIAGANFYIVGRDPAGMphpetkKDLYEPTHGGKV 540
Cdd:PRK04149 233 EVRMEAYEALL-KNYYPKDRVLLSVTPAAMRYAGPREAIFHAIVRKNYGCTHFIVGRDHAGV------GDYYGPYDAQEI 305

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912492  541 LSM--APGLtSVEIIPFRVAAYNKAKKAMDFYDPARHNEFD--FISGTRMRKLAREGENPPDGFMAPKAWKVLTDYYRSL 616
Cdd:PRK04149 306 FDEftEEEL-GITPLKFEEAFYCPKCGGMASEKTCPHGKEDrvHLSGTKVREMLREGEKPPPEFSRPEVAEVLIKGLKKY 384


                 .
gi 62912492  617 E 617
Cdd:PRK04149 385 G 385
PRK05537 PRK05537
bifunctional sulfate adenylyltransferase/adenylylsulfate kinase;
42-213 1.25e-53

bifunctional sulfate adenylyltransferase/adenylylsulfate kinase;


Pssm-ID: 180124 [Multi-domain]  Cd Length: 568  Bit Score: 192.58  E-value: 1.25e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912492   42 GCTVWLTGLSGAGKTTISFALEEYLVSH-AIPCYSLDGDNVRHGLNRNLGFSPGDREENIRRIAEVAKLFADAGLVCITS 120
Cdd:PRK05537 392 GFTVFFTGLSGAGKSTIAKALMVKLMEMrGRPVTLLDGDVVRKHLSSELGFSKEDRDLNILRIGFVASEITKNGGIAICA 471

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912492  121 FISPFAKDRENARKIHESAGlPFFEIFVDAPLNICESRDVKGLYKRARAGEIKGFTGIDSDYEKPETPERVLKTNLSTVS 200
Cdd:PRK05537 472 PIAPYRATRREVREMIEAYG-GFIEVHVATPLEVCEQRDRKGLYAKAREGKIKGFTGISDPYEPPANPELVIDTTNVTPD 550

                        170
                 ....*....|...
gi 62912492  201 DCVHQVVELLQEQ 213
Cdd:PRK05537 551 ECAHKILLYLEEK 563
PRK05537 PRK05537
bifunctional sulfate adenylyltransferase/adenylylsulfate kinase;
215-609 3.02e-51

bifunctional sulfate adenylyltransferase/adenylylsulfate kinase;


Pssm-ID: 180124 [Multi-domain]  Cd Length: 568  Bit Score: 186.03  E-value: 3.02e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912492  215 IVPYTiiKDIHELFVPENKLDHVRAEAETLPSLSITKLDLQWVQVLSEGWATPLKGFMREKEYLQVMHFDTLLDGMALPd 294
Cdd:PRK05537   2 ILPNG--GPLPNLYVSPESREKLKAEALSLPSLDLSPRQICDLELLMNGGFSPLKGFMGRADYECVLENMRLADGTLWP- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912492  295 gvinmsIPIVLPVSAEDKTRLEGCSKFVLAHG-GRRVAILRDAEFYEHRKEERCSRVWGTTCTKHPHI-KMVMESGDWLV 372
Cdd:PRK05537  79 ------IPITLDVSEKFAAGLEIGERIALRDQeGVLLAILTVSDIWEPDKEREAEAVFGTTDPAHPGVnYLHRWAGKFYL 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912492  373 GGDLQVLEKIRWNDgLDQYRLTPLELKQKCKEMNADAVFAFQLRNPVHNGHALLmqdTRRRLLERGYKhpvLLLHPLGGW 452
Cdd:PRK05537 153 GGPLTGIQLPVHYD-FVQLRLTPAELRARFRKLGWRRVVAFQTRNPLHRAHEEL---TKRAAREVGAN---LLIHPVVGM 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912492  453 TKDDDVPLDWRMKQHAAVLEEgvLDPKSTIVAIFPSPMLYAGPTEVQWHCRSRMIAGANFYIVGRDPAGMPHPETKKDLY 532
Cdd:PRK05537 226 TKPGDIDHFTRVRCYEALLDK--YPPATTLLSLLPLAMRMAGPREALWHAIIRRNYGCTHFIVGRDHAGPGKDSRGKPFY 303

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 62912492  533 EPTHGGKVLSMAPGLTSVEIIPFRVAAYNKAKKAMDFYDPARHNE-FDFISGTRMRKLAREGENPPDGFMAPKAWKVL 609
Cdd:PRK05537 304 GPYDAQELFAKYADEIGITMVPFKEMVYVQDKAQYVPVDEVPQGAtVLTISGTELRRRLREGLEIPEWFSFPEVVAEL 381
PRK05541 PRK05541
adenylylsulfate kinase; Provisional
 42-215 1.23e-23

adenylylsulfate kinase; Provisional


Pssm-ID: 235498  Cd Length: 176  Bit Score: 98.20  E-value: 1.23e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912492   42 GCTVWLTGLSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRHGLNRNlGFSPGDREENIRRIAEVAKLFADAGLVCITSF 121
Cdd:PRK05541   7 GYVIWITGLAGSGKTTIAKALYERLKLKYSNVIYLDGDELREILGHY-GYDKQSRIEMALKRAKLAKFLADQGMIVIVTT 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912492  122 ISPFakdRENARkiHESAGLP-FFEIFVDAPLNICESRDVKGLYKRARAGEIKGFTGIDSDYEKPETPERVLKTNLSTVS 200
Cdd:PRK05541  86 ISMF---DEIYA--YNRKHLPnYFEVYLKCDMEELIRRDQKGLYTKALKGEIKNVVGVDIPFDEPKADLVIDNSCRTSLD 160

                        170
                 ....*....|....*
gi 62912492  201 DCVHQVVELLQEQNI 215
Cdd:PRK05541 161 EKVDLILNKLKLRLI 175
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
45-176 2.31e-08

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


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 53.76  E-value: 2.31e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912492  45 VWLTGLSGAGKTTISFALEEYLvsHAIPcysLDGDNVRHGLnRNLGFSPGDREENIR-----RIAEVAKLFADAGLVCIt 119
Cdd:COG0645   2 ILVCGLPGSGKSTLARALAERL--GAVR---LRSDVVRKRL-FGAGLAPLERSPEATartyaRLLALARELLAAGRSVI- 74

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 62912492 120 sFISPFAK--DRENARKIHESAGLPFFEIFVDAPLNICESRdvkgLYKRARAGEIKGFT 176
Cdd:COG0645  75 -LDATFLRraQREAFRALAEEAGAPFVLIWLDAPEEVLRER----LEARNAEGGDSDAT 128
Kti12 COG4088
tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) ...
 47-212 1.80e-07

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: 51.65  E-value: 1.80e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912492  47 LTGLSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRHGLNRNLGFSPgDREENIRRIAE-VAKLFADAGLVCITSFISPF 125
Cdd:COG4088   9 LTGPPGSGKTTFAKALAQRLYAEGIAVALLHSDDFRRFLVNESFPKE-TYEEVVEDVRTtTADNALDNGYSVIVDGTFYY 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912492 126 AKDRENARKIHESAGlPFFEIFVDAPLNICESRDvkglykRARAGEI--KGFTGIDSDYEKPET---PERVLKTNLSTVS 200
Cdd:COG4088  88 RSWQRDFRNLAKHKA-PIHIIYLKAPLETALRRN------RERGEPIpeRVIARMYRKFDKPGTkdrPDLVIDTTEDSVS 160

                       170
                ....*....|..
gi 62912492 201 DCVHQVVELLQE 212
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 ...
 45-171 4.61e-06

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: 46.53  E-value: 4.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912492    45 VWLTGLSGAGKTTISFALEEylvshAIPCYSLDGDNVRHGLNRNLGFSPGDREENI----RRIAEVAKLFADAGLVCITS 120
Cdd:pfam13671   2 ILLVGLPGSGKSTLARRLLE-----ELGAVRLSSDDERKRLFGEGRPSISYYTDATdrtyERLHELARIALRAGRPVILD 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 62912492   121 FisPFAKDRENARKIH--ESAGLPFFEIFVDAPLNICESRDVkglyKRARAGE 171
Cdd:pfam13671  77 A--TNLRRDERARLLAlaREYGVPVRIVVFEAPEEVLRERLA----ARARAGG 123
GntK cd02021
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting ...
 47-190 1.50e-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: 39.54  E-value: 1.50e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62912492  47 LTGLSGAGKTTISFALeeylvSHAIPCYSLDGDNVRHGLNRNL---GFSPGDRE-----ENIRRIAEVAKLFADAGLVCI 118
Cdd:cd02021   4 VMGVSGSGKSTVGKAL-----AERLGAPFIDGDDLHPPANIAKmaaGIPLNDEDrwpwlQALTDALLAKLASAGEGVVVA 78

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62912492 119 TSFIspfaKD--RENARKIHESAGLPFfeIFVDAPLNICESRDvkglykRARAGEIKGFTGIDSDYEKPETPER 190
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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