|
Name |
Accession |
Description |
Interval |
E-value |
| ATPS |
cd00517 |
ATP-sulfurylase; ATP-sulfurylase (ATPS), also known as sulfate adenylate transferase, ... |
243-606 |
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: 516.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319918850 243 LPSLPITKLDLQWVQILSEGWATPLKGFMREKEYLQTLHFDTLLDDgvINMSIPIVLPVSADDKARLEGCSKFALMYEGR 322
Cdd:cd00517 1 LPSVELSERDLCDLEMLAEGGFSPLTGFMTEADYLSVLEEMRLLDG--TLWPIPIVLDVSEEDAKRLKEGERVALRYPGQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319918850 323 RVALLQDPEFYEHRKEERCSRVWGTATAKHPHIKMVMESGDWLVGGDLQVLERIRWDDgLDQYRLTPLELKQKCKDMNAD 402
Cdd:cd00517 79 PLAILTVEEIYEPDKEEEAARVFGTTDPHHPGVKKVMEQGDWLVGGPIEVLELPPFPD-FDQYRLTPAELRALFKERGWR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319918850 403 AVFAFQLRNPVHNGHALLMQDTRRRLLErgykhPVLLLHPLGGWTKDDDVPLEWRMKQHAAVLEERVLdPKSTIVAIFPS 482
Cdd:cd00517 158 RVVAFQTRNPMHRAHEELMKRAAEKLLN-----DGLLLHPLVGWTKPGDVPDEVRMRAYEALLEEYYL-PERTVLAILPL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319918850 483 PMLYAGPTEVQWHCRCRMIAGANFYIVGRDPAGMPHPETKKDLYEPTHGGKVLSMApglTSVEIIPFRVAAYNKIKKAMD 562
Cdd:cd00517 232 PMRYAGPREALWHAIIRKNYGATHFIVGRDHAGVGHPGDYYGPYDAQEIFKKLAPE---LGIEPVPFREAAYCPKCDGMA 308
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 319918850 563 FYDPARH-EEFDFISGTRMRKLAREGEDPPDGFMAPKAWKVLTDY 606
Cdd:cd00517 309 SEDTCPHgEDFLNISGTKLRKMLREGEKPPEWFMRPEVAKVLREY 353
|
|
| sopT |
TIGR00339 |
ATP sulphurylase; This enzyme forms adenosine 5'-phosphosulfate (APS) from ATP and free ... |
234-605 |
2.55e-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: 407.93 E-value: 2.55e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319918850 234 DQIRAEAETLPSLPITKLDLQWVQILSEGWATPLKGFMREKEYLQTLHfDTLLDDGViNMSIPIVLPVSADDKARLEGCS 313
Cdd:TIGR00339 18 HKLLAEAESLPSITLSDRQLCDLELLGNGAFSPLEGFMNEADYDSVVE-SMRLSDGV-LFSVPITLDIDDEDADDIKLGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319918850 314 KFALMYE-GRRVALLQDPEFYEHRKEERCSRVWGTATAKHPHIKMVMESGDWLVGGDLQVLERIRWDDgLDQYRLTPLEL 392
Cdd:TIGR00339 96 RIALTDPkGQPLAILTIEEVYKPNKEKEAKKVFGTTDPEHPGVVYLNTAGNYYIGGPIEVINLPKFYD-FPRFRFTPAEL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319918850 393 KQKCKDMNADAVFAFQLRNPVHNGHALLMQDTRRRLlergyKHPVLLLHPLGGWTKDDDVPLEWRMKQHAaVLEERVLDP 472
Cdd:TIGR00339 175 REEFKERGWDTVVAFQTRNPMHRAHEELTKRAAERL-----PNAGVLVHPLVGLTKPGDIPAEVRMRAYE-VLKEGYPNP 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319918850 473 KSTIVAIFPSPMLYAGPTEVQWHCRCRMIAGANFYIVGRDPAGMPHPETKKDLYEPTHGGKVLSMAPGLTSVEIIPFRVA 552
Cdd:TIGR00339 249 ERTVVSFLPLAMRYAGPREAIWHAIIRKNYGATHFIVGRDHAGPGSNSKGQDFYGPYDAQELFEKYKAELGIKIVPFRHV 328
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 319918850 553 AYNKIKKAMDFYDPARHEEFDF--ISGTRMRKLAREGEDPPDGFMAPKAWKVLTD 605
Cdd:TIGR00339 329 AYCPDEDEYAPADQAGHTNLRTlnISGTKLRGMLRNGVFPPEWFSRPEVVKILRE 383
|
|
| CysC |
COG0529 |
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ... |
22-216 |
7.10e-104 |
|
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: 312.02 E-value: 7.10e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319918850 22 HHVSRNKRGQvvgtRGGFRGCTVWLTGLSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRHGLNKNLGFSAGDREENIRR 101
Cdd:COG0529 1 SAVTREERAA----LKGQKGFVVWFTGLSGSGKSTLANALERRLFERGRHVYLLDGDNVRHGLNKDLGFSKEDRDENIRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319918850 102 IAEVARLFADAGLVCITSFISPFAKDRENARKIHESAglPFFEIFVDAPLNICESRDVKGLYKRARAGEIKGFTGIDSDY 181
Cdd:COG0529 77 IGEVAKLLADAGLIVLVAFISPYRADREEARELIGEG--EFIEVYVDTPLEVCEARDPKGLYAKARAGEIKNFTGIDDPY 154
|
170 180 190
....*....|....*....|....*....|....*
gi 319918850 182 EKPETPECVLKTNLSSVSDCVQQVVELLQEQNIVP 216
Cdd:COG0529 155 EAPENPELVLDTDKESVEESVEKILAYLEERGYIS 189
|
|
| APSK |
cd02027 |
Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5 ... |
43-193 |
5.03e-100 |
|
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: 300.55 E-value: 5.03e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319918850 43 TVWLTGLSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRHGLNKNLGFSAGDREENIRRIAEVARLFADAGLVCITSFIS 122
Cdd:cd02027 1 VIWLTGLSGSGKSTIARALEEKLFQRGRPVYVLDGDNVRHGLNKDLGFSREDREENIRRIAEVAKLLADAGLIVIAAFIS 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 319918850 123 PFAKDRENARKIHEsaGLPFFEIFVDAPLNICESRDVKGLYKRARAGEIKGFTGIDSDYEKPETPECVLKT 193
Cdd:cd02027 81 PYREDREAARKIIG--GGDFLEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDDPYEAPENPDLVLDT 149
|
|
| APS_kinase |
pfam01583 |
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3 ... |
40-193 |
7.75e-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: 289.99 E-value: 7.75e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319918850 40 RGCTVWLTGLSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRHGLNKNLGFSAGDREENIRRIAEVARLFADAGLVCITS 119
Cdd:pfam01583 1 RGCTIWLTGLSGAGKSTIANALERKLFEQGRSVYVLDGDNVRHGLNKDLGFSEEDRTENIRRIGEVAKLFADAGLIVITA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 319918850 120 FISPFAKDRENARKIHESAglPFFEIFVDAPLNICESRDVKGLYKRARAGEIKGFTGIDSDYEKPETPECVLKT 193
Cdd:pfam01583 81 FISPYREDREQARELHEEG--KFIEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDSPYEAPENPELVLDT 152
|
|
| ATP-sulfurylase |
pfam01747 |
ATP-sulfurylase; This domain is the catalytic domain of ATP-sulfurylase or sulfate ... |
383-606 |
5.64e-93 |
|
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: 285.20 E-value: 5.64e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319918850 383 DQYRLTPLELKQKCKDMNADAVFAFQLRNPVHNGHALLMQDTRRRLlERGYkhpvLLLHPLGGWTKDDDVPLEWRMKQHA 462
Cdd:pfam01747 1 DEYRLTPAETRALFKEKGWRTVVAFQTRNPLHRAHEELMKRALEEL-EADG----LLLHPLVGPTKPGDVPAEVRVRCYE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319918850 463 AVLEErVLDPKSTIVAIFPSPMLYAGPTEVQWHCRCRMIAGANFYIVGRDPAGMPHpetkkdLYEPTHGGKVLSMAPGLT 542
Cdd:pfam01747 76 ALLEN-YLPPDRVVLALLPLAMRYAGPREALLHAIIRKNYGCTHFIVGRDHAGVGD------FYGPYDAQEIFDEYPGEL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 319918850 543 SVEIIPFRVAAYNKIKKAM-DFYDPARHEEFDFISGTRMRKLAREGEDPPDGFMAPKAWKVLTDY 606
Cdd:pfam01747 149 GIEPVPFREAVYCKKCGEMaSTKCPHGGEDRLFISGTKVRELLREGEEPPEWFSRPEVAKVLREY 213
|
|
| PRK03846 |
PRK03846 |
adenylylsulfate kinase; Provisional |
14-215 |
7.53e-89 |
|
adenylylsulfate kinase; Provisional
Pssm-ID: 179661 Cd Length: 198 Bit Score: 273.74 E-value: 7.53e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319918850 14 STNVVYQAHHVSRNKRGQvvgtRGGFRGCTVWLTGLSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRHGLNKNLGFSAG 93
Cdd:PRK03846 1 DENIVWHQHPVTKAQREQ----LHGHKGVVLWFTGLSGSGKSTVAGALEEALHELGVSTYLLDGDNVRHGLCSDLGFSDA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319918850 94 DREENIRRIAEVARLFADAGLVCITSFISPFAKDRENARKIhesagLP---FFEIFVDAPLNICESRDVKGLYKRARAGE 170
Cdd:PRK03846 77 DRKENIRRVGEVAKLMVDAGLVVLTAFISPHRAERQMVRER-----LGegeFIEVFVDTPLAICEARDPKGLYKKARAGE 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 319918850 171 IKGFTGIDSDYEKPETPECVLKTNLSSVSDCVQQVVELLQEQNIV 215
Cdd:PRK03846 152 IRNFTGIDSVYEAPESPEIHLDTGEQLVTNLVEQLLDYLRQRDII 196
|
|
| apsK |
TIGR00455 |
adenylyl-sulfate kinase; This protein, adenylylsulfate kinase, is often found as a fusion ... |
23-209 |
5.68e-82 |
|
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: 255.47 E-value: 5.68e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319918850 23 HVSRNKRGQVVGTRGgfrgCTVWLTGLSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRHGLNKNLGFSAGDREENIRRI 102
Cdd:TIGR00455 4 AITKDERQALNGHRG----VVIWLTGLSGSGKSTIANALEKKLESKGYRVYVLDGDNVRHGLNKDLGFSEEDRKENIRRI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319918850 103 AEVARLFADAGLVCITSFISPFAKDRENARKIHESAglPFFEIFVDAPLNICESRDVKGLYKRARAGEIKGFTGIDSDYE 182
Cdd:TIGR00455 80 GEVAKLFVRNGIIVITSFISPYRADRQMVRELIEKG--EFIEVFVDCPLEVCEQRDPKGLYKKARNGEIKGFTGIDSPYE 157
|
170 180
....*....|....*....|....*..
gi 319918850 183 KPETPECVLKTNLSSVSDCVQQVVELL 209
Cdd:TIGR00455 158 APENPEVVLDTDQNDREECVGQIIEKL 184
|
|
| MET3 |
COG2046 |
ATP sulfurylase (sulfate adenylyltransferase) [Inorganic ion transport and metabolism]; ATP ... |
225-612 |
3.41e-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: 242.35 E-value: 3.41e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319918850 225 ELFVPENKVDQIRAEAETLPSLPITKLDLQWVQILSEGWATPLKGFMREKEYLQTLHfDTLLDDGVInMSIPIVLPVSAD 304
Cdd:COG2046 14 NRVVPGEEREALLEEAKGLPSIELSSRALSDLEMIAIGGFSPLTGFMNKADYESVVE-NMRLADGLL-WPIPITLDVSEE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319918850 305 DKARLEGCSKFALM-YEGRRVALLQDPEFYEHRKEERCSRVWGTATAKHPHIKMVMESGDWLVGGDLQVLERIRWDDgLD 383
Cdd:COG2046 92 DAAGLKEGDEVALRdEEGEPLAVLEVEEIYEYDKEEEAEKVYGTTDPAHPGVAKLYERGDVYLGGPITLLNRPKHPD-FP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319918850 384 QYRLTPLELKQKCKDMNADAVFAFQLRNPVHNGHALLMqdtrRRLLERGYkhpVLLLHPLGGWTKDDDVPLEWRMKQHAA 463
Cdd:COG2046 171 DYRLTPAETRALFEEKGWKTVVAFQTRNPMHRAHEYLQ----KRALETVD---GLLIHPLVGETKPGDIPAEVRVRCYEA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319918850 464 VLEERVlDPKSTIVAIFPSPMLYAGPTEVQWHCRCRMIAGANFYIVGRDPAGMPhpetkkDLYEP--------THGGKVL 535
Cdd:COG2046 244 LLENYY-PKDRVLLSGLPLAMRYAGPREALLHAIIRKNYGCTHFIVGRDHAGVG------DYYGPydaqeifdEFPPGEL 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 319918850 536 SMapgltsvEIIPFRVAAYNKIKKAMDFYD--PARHEEFDFISGTRMRKLAREGEDPPDGFMAPKAWKVLTDYYRSLEK 612
Cdd:COG2046 317 GI-------EPLKFEEAFYCKKCGGMATSKtcPHDKEDRVSLSGTKVREMLREGEEPPPEFSRPEVAEILRKYYQPFGE 388
|
|
| sat |
PRK04149 |
sulfate adenylyltransferase; Reviewed |
225-611 |
2.12e-63 |
|
sulfate adenylyltransferase; Reviewed
Pssm-ID: 235227 Cd Length: 391 Bit Score: 213.95 E-value: 2.12e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319918850 225 ELFVPENKVDQIRAEAETLPSLPITKLDLQWVQILSEGWATPLKGFMREKEYLQTLHFDTLLDDGVinMSIPIVLPVSAD 304
Cdd:PRK04149 13 NRVVEGRDREEILEEAESLPRIELDERAASDLEMIAIGGFSPLTGFMGREDYDSVVEEMRLANGLV--WSIPITLDVSEE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319918850 305 DKARLEGCSKFALMYEGRRVALLQDPEFYEHRKEERCSRVWGTATAKHPHIKMVMESGDWLVGGDLQVLERIRwDDGLDQ 384
Cdd:PRK04149 91 DAASLKEGDEVALVYKGEPYGVLEVEEIYTYDKKKEAEKVYKTTDEKHPGVKKLYEQGDVYLAGPVTLLNRKF-HEPFPR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319918850 385 YRLTPLELKQKCKDMNADAVFAFQLRNPVHNGHALLMqdtrrrllergyKHPV-----LLLHPLGGWTKDDDVPLEWRMK 459
Cdd:PRK04149 170 FWLTPAETRELFEEKGWKTVVAFQTRNPPHRAHEYLQ------------KCALeivdgLLLNPLVGETKSGDIPAEVRME 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319918850 460 QHAAVLeERVLDPKSTIVAIFPSPMLYAGPTEVQWHCRCRMIAGANFYIVGRDPAGMphpetkKDLYEPTHGGKVLSM-- 537
Cdd:PRK04149 238 AYEALL-KNYYPKDRVLLSVTPAAMRYAGPREAIFHAIVRKNYGCTHFIVGRDHAGV------GDYYGPYDAQEIFDEft 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 319918850 538 APGLtSVEIIPFRVAAYNKIKKAMDF-----YDPARHEEFdfiSGTRMRKLAREGEDPPDGFMAPKAWKVLTDYYRSLE 611
Cdd:PRK04149 311 EEEL-GITPLKFEEAFYCPKCGGMASektcpHGKEDRVHL---SGTKVREMLREGEKPPPEFSRPEVAEVLIKGLKKYG 385
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ATPS |
cd00517 |
ATP-sulfurylase; ATP-sulfurylase (ATPS), also known as sulfate adenylate transferase, ... |
243-606 |
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: 516.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319918850 243 LPSLPITKLDLQWVQILSEGWATPLKGFMREKEYLQTLHFDTLLDDgvINMSIPIVLPVSADDKARLEGCSKFALMYEGR 322
Cdd:cd00517 1 LPSVELSERDLCDLEMLAEGGFSPLTGFMTEADYLSVLEEMRLLDG--TLWPIPIVLDVSEEDAKRLKEGERVALRYPGQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319918850 323 RVALLQDPEFYEHRKEERCSRVWGTATAKHPHIKMVMESGDWLVGGDLQVLERIRWDDgLDQYRLTPLELKQKCKDMNAD 402
Cdd:cd00517 79 PLAILTVEEIYEPDKEEEAARVFGTTDPHHPGVKKVMEQGDWLVGGPIEVLELPPFPD-FDQYRLTPAELRALFKERGWR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319918850 403 AVFAFQLRNPVHNGHALLMQDTRRRLLErgykhPVLLLHPLGGWTKDDDVPLEWRMKQHAAVLEERVLdPKSTIVAIFPS 482
Cdd:cd00517 158 RVVAFQTRNPMHRAHEELMKRAAEKLLN-----DGLLLHPLVGWTKPGDVPDEVRMRAYEALLEEYYL-PERTVLAILPL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319918850 483 PMLYAGPTEVQWHCRCRMIAGANFYIVGRDPAGMPHPETKKDLYEPTHGGKVLSMApglTSVEIIPFRVAAYNKIKKAMD 562
Cdd:cd00517 232 PMRYAGPREALWHAIIRKNYGATHFIVGRDHAGVGHPGDYYGPYDAQEIFKKLAPE---LGIEPVPFREAAYCPKCDGMA 308
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 319918850 563 FYDPARH-EEFDFISGTRMRKLAREGEDPPDGFMAPKAWKVLTDY 606
Cdd:cd00517 309 SEDTCPHgEDFLNISGTKLRKMLREGEKPPEWFMRPEVAKVLREY 353
|
|
| sopT |
TIGR00339 |
ATP sulphurylase; This enzyme forms adenosine 5'-phosphosulfate (APS) from ATP and free ... |
234-605 |
2.55e-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: 407.93 E-value: 2.55e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319918850 234 DQIRAEAETLPSLPITKLDLQWVQILSEGWATPLKGFMREKEYLQTLHfDTLLDDGViNMSIPIVLPVSADDKARLEGCS 313
Cdd:TIGR00339 18 HKLLAEAESLPSITLSDRQLCDLELLGNGAFSPLEGFMNEADYDSVVE-SMRLSDGV-LFSVPITLDIDDEDADDIKLGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319918850 314 KFALMYE-GRRVALLQDPEFYEHRKEERCSRVWGTATAKHPHIKMVMESGDWLVGGDLQVLERIRWDDgLDQYRLTPLEL 392
Cdd:TIGR00339 96 RIALTDPkGQPLAILTIEEVYKPNKEKEAKKVFGTTDPEHPGVVYLNTAGNYYIGGPIEVINLPKFYD-FPRFRFTPAEL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319918850 393 KQKCKDMNADAVFAFQLRNPVHNGHALLMQDTRRRLlergyKHPVLLLHPLGGWTKDDDVPLEWRMKQHAaVLEERVLDP 472
Cdd:TIGR00339 175 REEFKERGWDTVVAFQTRNPMHRAHEELTKRAAERL-----PNAGVLVHPLVGLTKPGDIPAEVRMRAYE-VLKEGYPNP 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319918850 473 KSTIVAIFPSPMLYAGPTEVQWHCRCRMIAGANFYIVGRDPAGMPHPETKKDLYEPTHGGKVLSMAPGLTSVEIIPFRVA 552
Cdd:TIGR00339 249 ERTVVSFLPLAMRYAGPREAIWHAIIRKNYGATHFIVGRDHAGPGSNSKGQDFYGPYDAQELFEKYKAELGIKIVPFRHV 328
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 319918850 553 AYNKIKKAMDFYDPARHEEFDF--ISGTRMRKLAREGEDPPDGFMAPKAWKVLTD 605
Cdd:TIGR00339 329 AYCPDEDEYAPADQAGHTNLRTlnISGTKLRGMLRNGVFPPEWFSRPEVVKILRE 383
|
|
| CysC |
COG0529 |
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ... |
22-216 |
7.10e-104 |
|
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: 312.02 E-value: 7.10e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319918850 22 HHVSRNKRGQvvgtRGGFRGCTVWLTGLSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRHGLNKNLGFSAGDREENIRR 101
Cdd:COG0529 1 SAVTREERAA----LKGQKGFVVWFTGLSGSGKSTLANALERRLFERGRHVYLLDGDNVRHGLNKDLGFSKEDRDENIRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319918850 102 IAEVARLFADAGLVCITSFISPFAKDRENARKIHESAglPFFEIFVDAPLNICESRDVKGLYKRARAGEIKGFTGIDSDY 181
Cdd:COG0529 77 IGEVAKLLADAGLIVLVAFISPYRADREEARELIGEG--EFIEVYVDTPLEVCEARDPKGLYAKARAGEIKNFTGIDDPY 154
|
170 180 190
....*....|....*....|....*....|....*
gi 319918850 182 EKPETPECVLKTNLSSVSDCVQQVVELLQEQNIVP 216
Cdd:COG0529 155 EAPENPELVLDTDKESVEESVEKILAYLEERGYIS 189
|
|
| APSK |
cd02027 |
Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5 ... |
43-193 |
5.03e-100 |
|
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: 300.55 E-value: 5.03e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319918850 43 TVWLTGLSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRHGLNKNLGFSAGDREENIRRIAEVARLFADAGLVCITSFIS 122
Cdd:cd02027 1 VIWLTGLSGSGKSTIARALEEKLFQRGRPVYVLDGDNVRHGLNKDLGFSREDREENIRRIAEVAKLLADAGLIVIAAFIS 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 319918850 123 PFAKDRENARKIHEsaGLPFFEIFVDAPLNICESRDVKGLYKRARAGEIKGFTGIDSDYEKPETPECVLKT 193
Cdd:cd02027 81 PYREDREAARKIIG--GGDFLEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDDPYEAPENPDLVLDT 149
|
|
| APS_kinase |
pfam01583 |
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3 ... |
40-193 |
7.75e-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: 289.99 E-value: 7.75e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319918850 40 RGCTVWLTGLSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRHGLNKNLGFSAGDREENIRRIAEVARLFADAGLVCITS 119
Cdd:pfam01583 1 RGCTIWLTGLSGAGKSTIANALERKLFEQGRSVYVLDGDNVRHGLNKDLGFSEEDRTENIRRIGEVAKLFADAGLIVITA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 319918850 120 FISPFAKDRENARKIHESAglPFFEIFVDAPLNICESRDVKGLYKRARAGEIKGFTGIDSDYEKPETPECVLKT 193
Cdd:pfam01583 81 FISPYREDREQARELHEEG--KFIEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDSPYEAPENPELVLDT 152
|
|
| ATP-sulfurylase |
pfam01747 |
ATP-sulfurylase; This domain is the catalytic domain of ATP-sulfurylase or sulfate ... |
383-606 |
5.64e-93 |
|
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: 285.20 E-value: 5.64e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319918850 383 DQYRLTPLELKQKCKDMNADAVFAFQLRNPVHNGHALLMQDTRRRLlERGYkhpvLLLHPLGGWTKDDDVPLEWRMKQHA 462
Cdd:pfam01747 1 DEYRLTPAETRALFKEKGWRTVVAFQTRNPLHRAHEELMKRALEEL-EADG----LLLHPLVGPTKPGDVPAEVRVRCYE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319918850 463 AVLEErVLDPKSTIVAIFPSPMLYAGPTEVQWHCRCRMIAGANFYIVGRDPAGMPHpetkkdLYEPTHGGKVLSMAPGLT 542
Cdd:pfam01747 76 ALLEN-YLPPDRVVLALLPLAMRYAGPREALLHAIIRKNYGCTHFIVGRDHAGVGD------FYGPYDAQEIFDEYPGEL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 319918850 543 SVEIIPFRVAAYNKIKKAM-DFYDPARHEEFDFISGTRMRKLAREGEDPPDGFMAPKAWKVLTDY 606
Cdd:pfam01747 149 GIEPVPFREAVYCKKCGEMaSTKCPHGGEDRLFISGTKVRELLREGEEPPEWFSRPEVAKVLREY 213
|
|
| PRK03846 |
PRK03846 |
adenylylsulfate kinase; Provisional |
14-215 |
7.53e-89 |
|
adenylylsulfate kinase; Provisional
Pssm-ID: 179661 Cd Length: 198 Bit Score: 273.74 E-value: 7.53e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319918850 14 STNVVYQAHHVSRNKRGQvvgtRGGFRGCTVWLTGLSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRHGLNKNLGFSAG 93
Cdd:PRK03846 1 DENIVWHQHPVTKAQREQ----LHGHKGVVLWFTGLSGSGKSTVAGALEEALHELGVSTYLLDGDNVRHGLCSDLGFSDA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319918850 94 DREENIRRIAEVARLFADAGLVCITSFISPFAKDRENARKIhesagLP---FFEIFVDAPLNICESRDVKGLYKRARAGE 170
Cdd:PRK03846 77 DRKENIRRVGEVAKLMVDAGLVVLTAFISPHRAERQMVRER-----LGegeFIEVFVDTPLAICEARDPKGLYKKARAGE 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 319918850 171 IKGFTGIDSDYEKPETPECVLKTNLSSVSDCVQQVVELLQEQNIV 215
Cdd:PRK03846 152 IRNFTGIDSVYEAPESPEIHLDTGEQLVTNLVEQLLDYLRQRDII 196
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
12-212 |
8.60e-87 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 282.97 E-value: 8.60e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319918850 12 QKSTNVVYQAHHVSRNKRGqvvgTRGGFRGCTVWLTGLSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRHGLNKNLGFS 91
Cdd:PRK05506 435 RRATNVHWQASDVSREARA----ARKGQKPATVWFTGLSGSGKSTIANLVERRLHALGRHTYLLDGDNVRHGLNRDLGFS 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319918850 92 AGDREENIRRIAEVARLFADAGLVCITSFISPFAKDRENARKIHESAglPFFEIFVDAPLNICESRDVKGLYKRARAGEI 171
Cdd:PRK05506 511 DADRVENIRRVAEVARLMADAGLIVLVSFISPFREERELARALHGEG--EFVEVFVDTPLEVCEARDPKGLYAKARAGEI 588
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 319918850 172 KGFTGIDSDYEKPETPECVLKTNLSSVSDCVQQVVELLQEQ 212
Cdd:PRK05506 589 KNFTGIDSPYEAPENPELRLDTTGRSPEELAEQVLELLRRR 629
|
|
| apsK |
TIGR00455 |
adenylyl-sulfate kinase; This protein, adenylylsulfate kinase, is often found as a fusion ... |
23-209 |
5.68e-82 |
|
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: 255.47 E-value: 5.68e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319918850 23 HVSRNKRGQVVGTRGgfrgCTVWLTGLSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRHGLNKNLGFSAGDREENIRRI 102
Cdd:TIGR00455 4 AITKDERQALNGHRG----VVIWLTGLSGSGKSTIANALEKKLESKGYRVYVLDGDNVRHGLNKDLGFSEEDRKENIRRI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319918850 103 AEVARLFADAGLVCITSFISPFAKDRENARKIHESAglPFFEIFVDAPLNICESRDVKGLYKRARAGEIKGFTGIDSDYE 182
Cdd:TIGR00455 80 GEVAKLFVRNGIIVITSFISPYRADRQMVRELIEKG--EFIEVFVDCPLEVCEQRDPKGLYKKARNGEIKGFTGIDSPYE 157
|
170 180
....*....|....*....|....*..
gi 319918850 183 KPETPECVLKTNLSSVSDCVQQVVELL 209
Cdd:TIGR00455 158 APENPEVVLDTDQNDREECVGQIIEKL 184
|
|
| MET3 |
COG2046 |
ATP sulfurylase (sulfate adenylyltransferase) [Inorganic ion transport and metabolism]; ATP ... |
225-612 |
3.41e-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: 242.35 E-value: 3.41e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319918850 225 ELFVPENKVDQIRAEAETLPSLPITKLDLQWVQILSEGWATPLKGFMREKEYLQTLHfDTLLDDGVInMSIPIVLPVSAD 304
Cdd:COG2046 14 NRVVPGEEREALLEEAKGLPSIELSSRALSDLEMIAIGGFSPLTGFMNKADYESVVE-NMRLADGLL-WPIPITLDVSEE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319918850 305 DKARLEGCSKFALM-YEGRRVALLQDPEFYEHRKEERCSRVWGTATAKHPHIKMVMESGDWLVGGDLQVLERIRWDDgLD 383
Cdd:COG2046 92 DAAGLKEGDEVALRdEEGEPLAVLEVEEIYEYDKEEEAEKVYGTTDPAHPGVAKLYERGDVYLGGPITLLNRPKHPD-FP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319918850 384 QYRLTPLELKQKCKDMNADAVFAFQLRNPVHNGHALLMqdtrRRLLERGYkhpVLLLHPLGGWTKDDDVPLEWRMKQHAA 463
Cdd:COG2046 171 DYRLTPAETRALFEEKGWKTVVAFQTRNPMHRAHEYLQ----KRALETVD---GLLIHPLVGETKPGDIPAEVRVRCYEA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319918850 464 VLEERVlDPKSTIVAIFPSPMLYAGPTEVQWHCRCRMIAGANFYIVGRDPAGMPhpetkkDLYEP--------THGGKVL 535
Cdd:COG2046 244 LLENYY-PKDRVLLSGLPLAMRYAGPREALLHAIIRKNYGCTHFIVGRDHAGVG------DYYGPydaqeifdEFPPGEL 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 319918850 536 SMapgltsvEIIPFRVAAYNKIKKAMDFYD--PARHEEFDFISGTRMRKLAREGEDPPDGFMAPKAWKVLTDYYRSLEK 612
Cdd:COG2046 317 GI-------EPLKFEEAFYCKKCGGMATSKtcPHDKEDRVSLSGTKVREMLREGEEPPPEFSRPEVAEILRKYYQPFGE 388
|
|
| PRK00889 |
PRK00889 |
adenylylsulfate kinase; Provisional |
40-216 |
8.86e-72 |
|
adenylylsulfate kinase; Provisional
Pssm-ID: 179157 Cd Length: 175 Bit Score: 228.75 E-value: 8.86e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319918850 40 RGCTVWLTGLSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRHGLNKNLGFSAGDREENIRRIAEVARLFADAGLVCITS 119
Cdd:PRK00889 3 RGVTVWFTGLSGAGKTTIARALAEKLREAGYPVEVLDGDAVRTNLSKGLGFSKEDRDTNIRRIGFVANLLTRHGVIVLVS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319918850 120 FISPFAKDRENARkihesAGLP-FFEIFVDAPLNICESRDVKGLYKRARAGEIKGFTGIDSDYEKPETPECVLKTNLSSV 198
Cdd:PRK00889 83 AISPYRETREEVR-----ANIGnFLEVFVDAPLEVCEQRDVKGLYAKARAGEIKHFTGIDDPYEPPLNPEVECRTDLESL 157
|
170
....*....|....*...
gi 319918850 199 SDCVQQVVELLQEQNIVP 216
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. |
214-375 |
1.52e-63 |
|
PUA-like domain; This PUA like domain is found at the N-terminus of ATP-sulfurylase enzymes.
Pssm-ID: 464131 [Multi-domain] Cd Length: 159 Bit Score: 206.22 E-value: 1.52e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319918850 214 IVPHTtiKGIHELFVPENKVDQIRAEAETLPSLPITKLDLQWVQILSEGWATPLKGFMREKEYLQTLHFDTlLDDGVInM 293
Cdd:pfam14306 1 IKPHG--GKLVDLVVRDAEREELLAEAAELPSIELSKRELCDLELIAIGGFSPLTGFMGEADYLSVLEFMR-LADGLL-W 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319918850 294 SIPIVLPVSADDKARLEGCSKFALMY-EGRRVALLQDPEFYEHRKEERCSRVWGTATAKHPHIKMVMESGDWLVGGDLQV 372
Cdd:pfam14306 77 SIPITLDVSEEDAASLKEGDRVALRDpEGEPLAILTVEEIYEPDKEEEAEKVFGTTDPAHPGVKKLYEQGDFYVGGDIEV 156
|
...
gi 319918850 373 LER 375
Cdd:pfam14306 157 LNR 159
|
|
| sat |
PRK04149 |
sulfate adenylyltransferase; Reviewed |
225-611 |
2.12e-63 |
|
sulfate adenylyltransferase; Reviewed
Pssm-ID: 235227 Cd Length: 391 Bit Score: 213.95 E-value: 2.12e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319918850 225 ELFVPENKVDQIRAEAETLPSLPITKLDLQWVQILSEGWATPLKGFMREKEYLQTLHFDTLLDDGVinMSIPIVLPVSAD 304
Cdd:PRK04149 13 NRVVEGRDREEILEEAESLPRIELDERAASDLEMIAIGGFSPLTGFMGREDYDSVVEEMRLANGLV--WSIPITLDVSEE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319918850 305 DKARLEGCSKFALMYEGRRVALLQDPEFYEHRKEERCSRVWGTATAKHPHIKMVMESGDWLVGGDLQVLERIRwDDGLDQ 384
Cdd:PRK04149 91 DAASLKEGDEVALVYKGEPYGVLEVEEIYTYDKKKEAEKVYKTTDEKHPGVKKLYEQGDVYLAGPVTLLNRKF-HEPFPR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319918850 385 YRLTPLELKQKCKDMNADAVFAFQLRNPVHNGHALLMqdtrrrllergyKHPV-----LLLHPLGGWTKDDDVPLEWRMK 459
Cdd:PRK04149 170 FWLTPAETRELFEEKGWKTVVAFQTRNPPHRAHEYLQ------------KCALeivdgLLLNPLVGETKSGDIPAEVRME 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319918850 460 QHAAVLeERVLDPKSTIVAIFPSPMLYAGPTEVQWHCRCRMIAGANFYIVGRDPAGMphpetkKDLYEPTHGGKVLSM-- 537
Cdd:PRK04149 238 AYEALL-KNYYPKDRVLLSVTPAAMRYAGPREAIFHAIVRKNYGCTHFIVGRDHAGV------GDYYGPYDAQEIFDEft 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 319918850 538 APGLtSVEIIPFRVAAYNKIKKAMDF-----YDPARHEEFdfiSGTRMRKLAREGEDPPDGFMAPKAWKVLTDYYRSLE 611
Cdd:PRK04149 311 EEEL-GITPLKFEEAFYCPKCGGMASektcpHGKEDRVHL---SGTKVREMLREGEKPPPEFSRPEVAEVLIKGLKKYG 385
|
|
| PRK05537 |
PRK05537 |
bifunctional sulfate adenylyltransferase/adenylylsulfate kinase; |
41-212 |
2.12e-53 |
|
bifunctional sulfate adenylyltransferase/adenylylsulfate kinase;
Pssm-ID: 180124 [Multi-domain] Cd Length: 568 Bit Score: 191.81 E-value: 2.12e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319918850 41 GCTVWLTGLSGAGKTTISFALEEYLVSHAIPCYS-LDGDNVRHGLNKNLGFSAGDREENIRRIAEVARLFADAGLVCITS 119
Cdd:PRK05537 392 GFTVFFTGLSGAGKSTIAKALMVKLMEMRGRPVTlLDGDVVRKHLSSELGFSKEDRDLNILRIGFVASEITKNGGIAICA 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319918850 120 FISPFAKDRENARKIHESAGlPFFEIFVDAPLNICESRDVKGLYKRARAGEIKGFTGIDSDYEKPETPECVLKTNLSSVS 199
Cdd:PRK05537 472 PIAPYRATRREVREMIEAYG-GFIEVHVATPLEVCEQRDRKGLYAKAREGKIKGFTGISDPYEPPANPELVIDTTNVTPD 550
|
170
....*....|...
gi 319918850 200 DCVQQVVELLQEQ 212
Cdd:PRK05537 551 ECAHKILLYLEEK 563
|
|
| PRK05537 |
PRK05537 |
bifunctional sulfate adenylyltransferase/adenylylsulfate kinase; |
221-603 |
4.71e-49 |
|
bifunctional sulfate adenylyltransferase/adenylylsulfate kinase;
Pssm-ID: 180124 [Multi-domain] Cd Length: 568 Bit Score: 179.87 E-value: 4.71e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319918850 221 KGIHELFVPENKVDQIRAEAETLPSLpitklDLQWVQI-----LSEGWATPLKGFMREKEYLQTLHfDTLLDDGVInMSI 295
Cdd:PRK05537 7 GPLPNLYVSPESREKLKAEALSLPSL-----DLSPRQIcdlelLMNGGFSPLKGFMGRADYECVLE-NMRLADGTL-WPI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319918850 296 PIVLPVSADDKARLEGCSKFALM-YEGRRVALLQDPEFYEHRKEERCSRVWGTATAKHPHI-KMVMESGDWLVGGDLQVL 373
Cdd:PRK05537 80 PITLDVSEKFAAGLEIGERIALRdQEGVLLAILTVSDIWEPDKEREAEAVFGTTDPAHPGVnYLHRWAGKFYLGGPLTGI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319918850 374 ERIRWDDgLDQYRLTPLELKQKCKDMNADAVFAFQLRNPVHNGHALLmqdTRRRLLERGYKhpvLLLHPLGGWTKDDDVP 453
Cdd:PRK05537 160 QLPVHYD-FVQLRLTPAELRARFRKLGWRRVVAFQTRNPLHRAHEEL---TKRAAREVGAN---LLIHPVVGMTKPGDID 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319918850 454 LEWRMKQHAAVLEErvLDPKSTIVAIFPSPMLYAGPTEVQWHCRCRMIAGANFYIVGRDPAGMPHPETKKDLYEPTHGGK 533
Cdd:PRK05537 233 HFTRVRCYEALLDK--YPPATTLLSLLPLAMRMAGPREALWHAIIRRNYGCTHFIVGRDHAGPGKDSRGKPFYGPYDAQE 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 319918850 534 VLSMAPGLTSVEIIPFRVAAYNKIKKAMDFYDPARH-EEFDFISGTRMRKLAREGEDPPDGFMAPKAWKVL 603
Cdd:PRK05537 311 LFAKYADEIGITMVPFKEMVYVQDKAQYVPVDEVPQgATVLTISGTELRRRLREGLEIPEWFSFPEVVAEL 381
|
|
| PRK05541 |
PRK05541 |
adenylylsulfate kinase; Provisional |
41-214 |
1.21e-25 |
|
adenylylsulfate kinase; Provisional
Pssm-ID: 235498 Cd Length: 176 Bit Score: 103.98 E-value: 1.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319918850 41 GCTVWLTGLSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRhglnKNLGFSAGDREENI---RRIAEVARLFADAGLVCI 117
Cdd:PRK05541 7 GYVIWITGLAGSGKTTIAKALYERLKLKYSNVIYLDGDELR----EILGHYGYDKQSRIemaLKRAKLAKFLADQGMIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319918850 118 TSFISPFakdRENARkiHESAGLP-FFEIFVDAPLNICESRDVKGLYKRARAGEIKGFTGIDSDYEKPETPECVLKTNLS 196
Cdd:PRK05541 83 VTTISMF---DEIYA--YNRKHLPnYFEVYLKCDMEELIRRDQKGLYTKALKGEIKNVVGVDIPFDEPKADLVIDNSCRT 157
|
170
....*....|....*...
gi 319918850 197 SVSDCVQQVVELLQEQNI 214
Cdd:PRK05541 158 SLDEKVDLILNKLKLRLI 175
|
|
| COG0645 |
COG0645 |
Predicted kinase, contains AAA domain [General function prediction only]; |
44-175 |
1.42e-08 |
|
Predicted kinase, contains AAA domain [General function prediction only];
Pssm-ID: 440410 [Multi-domain] Cd Length: 164 Bit Score: 54.53 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319918850 44 VWLTGLSGAGKTTISFALEEYLvsHAIPcysLDGDNVRHGLNKNLGFSAGDREENIRR----IAEVARLFADAGLVCIts 119
Cdd:COG0645 2 ILVCGLPGSGKSTLARALAERL--GAVR---LRSDVVRKRLFGAGLAPLERSPEATARtyarLLALARELLAAGRSVI-- 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 319918850 120 FISPFAK--DRENARKIHESAGLPFFEIFVDAPLNICESRdvkgLYKRARAGEIKGFT 175
Cdd:COG0645 75 LDATFLRraQREAFRALAEEAGAPFVLIWLDAPEEVLRER----LEARNAEGGDSDAT 128
|
|
| Kti12 |
COG4088 |
tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) ... |
46-211 |
8.04e-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: 49.73 E-value: 8.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319918850 46 LTGLSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRHGLnKNLGFSAGDREENIRRIAE-VARLFADAGLVCITSFISPF 124
Cdd:COG4088 9 LTGPPGSGKTTFAKALAQRLYAEGIAVALLHSDDFRRFL-VNESFPKETYEEVVEDVRTtTADNALDNGYSVIVDGTFYY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319918850 125 AKDRENARKIHESAGlPFFEIFVDAPLNICESRDvkglykRARAGEI--KGFTGIDSDYEKPET---PECVLKTNLSSVS 199
Cdd:COG4088 88 RSWQRDFRNLAKHKA-PIHIIYLKAPLETALRRN------RERGEPIpeRVIARMYRKFDKPGTkdrPDLVIDTTEDSVS 160
|
170
....*....|..
gi 319918850 200 DCVQQVVELLQE 211
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 ... |
44-170 |
1.10e-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: 48.46 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319918850 44 VWLTGLSGAGKTTISFALEEylvshAIPCYSLDGDNVRHGLNKNLGFSAGDREENI----RRIAEVARLFADAGLVCITS 119
Cdd:pfam13671 2 ILLVGLPGSGKSTLARRLLE-----ELGAVRLSSDDERKRLFGEGRPSISYYTDATdrtyERLHELARIALRAGRPVILD 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 319918850 120 FisPFAKDRENARKIH--ESAGLPFFEIFVDAPLNICESRDVkglyKRARAGE 170
Cdd:pfam13671 77 A--TNLRRDERARLLAlaREYGVPVRIVVFEAPEEVLRERLA----ARARAGG 123
|
|
| GntK |
cd02021 |
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting ... |
46-189 |
1.00e-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: 39.93 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319918850 46 LTGLSGAGKTTISFALeeylvSHAIPCYSLDGDNVRHGLNKNLgFSAG------DRE---ENIRRIAEVARLFADAGLVC 116
Cdd:cd02021 4 VMGVSGSGKSTVGKAL-----AERLGAPFIDGDDLHPPANIAK-MAAGiplndeDRWpwlQALTDALLAKLASAGEGVVV 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 319918850 117 ITSFIspfaKD--RENARKIHESAGLPFfeIFVDAPLNICESRDvkglykRARAGEIKGFTGIDSDYEKPETPEC 189
Cdd:cd02021 78 ACSAL----KRiyRDILRGGAANPRVRF--VHLDGPREVLAERL------AARKGHFMPADLLDSQFETLEPPGE 140
|
|
| KTI12 |
pfam08433 |
Chromatin associated protein KTI12; This is a family of chromatin associated proteins which ... |
44-188 |
9.03e-03 |
|
Chromatin associated protein KTI12; This is a family of chromatin associated proteins which interact with the Elongator complex, a component of the elongating form of RNA polymerase II. The Elongator complex has histone acetyltransferase activity.
Pssm-ID: 400643 Cd Length: 269 Bit Score: 38.43 E-value: 9.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319918850 44 VWLTGLSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRHGlNKNLGFSAGdrEENIRR--IAEVARLFADAGLVCI--TS 119
Cdd:pfam08433 2 VLLTGLPSSGKSTRAKQLAKYLEESNYDVIVISDESLGIE-KDDYKDSAK--EKFLRGslRSAVKRDLSKNTIVIVdsLN 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 319918850 120 FISPFAKDRENARKiheSAGLPFFEIFVDAPLNIC----ESRDVKGLYKRARageikgftgIDSDYEKPETPE 188
Cdd:pfam08433 79 YIKGFRYELYCIAK---AARTTYCVIHCKAPLDLCrkwnEERGQKSRYPDEL---------LDALIQRYEEPN 139
|
|
| |
