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Conserved domains on  [gi|1338686330|ref|NP_001347332|]
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bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 2 isoform 3 [Mus musculus]

Protein Classification

adenylyl-sulfate kinase( domain architecture ID 10785574)

adenylylsulfate kinase catalyzes the ATP-dependent phosphorylation of adenosine 5'-phosphosulfate (APS) to 3'-phosphoadenosine-5'-phosphosulfate (PAPS)

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, ...
 245-608 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: 515.65  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686330 245 LPSLPITKLDLQWVQILSEGWATPLKGFMREKEYLQTLHFDTLLDDgvINMSIPIVLPVSADDKARLEGCSKFALMYEGR 324
Cdd:cd00517     1 LPSVELSERDLCDLEMLAEGGFSPLTGFMTEADYLSVLEEMRLLDG--TLWPIPIVLDVSEEDAKRLKEGERVALRYPGQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686330 325 RVALLQDPEFYEHRKEERCSRVWGTATAKHPHIKMVMESGDWLVGGDLQVLERIRWDDgLDQYRLTPLELKQKCKDMNAD 404
Cdd:cd00517    79 PLAILTVEEIYEPDKEEEAARVFGTTDPHHPGVKKVMEQGDWLVGGPIEVLELPPFPD-FDQYRLTPAELRALFKERGWR 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686330 405 AVFAFQLRNPVHNGHALLMQDTRRRLLErgykhPVLLLHPLGGWTKDDDVPLEWRMKQHAAVLEERVLdPKSTIVAIFPS 484
Cdd:cd00517   158 RVVAFQTRNPMHRAHEELMKRAAEKLLN-----DGLLLHPLVGWTKPGDVPDEVRMRAYEALLEEYYL-PERTVLAILPL 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686330 485 PMLYAGPTEVQWHCRCRMIAGANFYIVGRDPAGMPHPETKKDLYEPTHGGKVLSMApglTSVEIIPFRVAAYNKIKKAMD 564
Cdd:cd00517   232 PMRYAGPREALWHAIIRKNYGATHFIVGRDHAGVGHPGDYYGPYDAQEIFKKLAPE---LGIEPVPFREAAYCPKCDGMA 308

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1338686330 565 FYDPARH-EEFDFISGTRMRKLAREGEDPPDGFMAPKAWKVLTDY 608
Cdd:cd00517   309 SEDTCPHgEDFLNISGTKLRKMLREGEKPPEWFMRPEVAKVLREY 353
CysC COG0529
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ...
 24-218 7.19e-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: 7.19e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686330  24 HHVSRNKRGQvvgtRGGFRGCTVWLTGLSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRHGLNKNLGFSAGDREENIRR 103
Cdd:COG0529     1 SAVTREERAA----LKGQKGFVVWFTGLSGSGKSTLANALERRLFERGRHVYLLDGDNVRHGLNKDLGFSKEDRDENIRR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686330 104 IAEVARLFADAGLVCITSFISPFAKDRENARKIHESAglPFFEIFVDAPLNICESRDVKGLYKRARAGEIKGFTGIDSDY 183
Cdd:COG0529    77 IGEVAKLLADAGLIVLVAFISPYRADREEARELIGEG--EFIEVYVDTPLEVCEARDPKGLYAKARAGEIKNFTGIDDPY 154

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1338686330 184 EKPETPECVLKTNLSSVSDCVQQVVELLQEQNIVP 218
Cdd:COG0529   155 EAPENPELVLDTDKESVEESVEKILAYLEERGYIS 189
 
Name Accession Description Interval E-value
ATPS cd00517
ATP-sulfurylase; ATP-sulfurylase (ATPS), also known as sulfate adenylate transferase, ...
 245-608 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: 515.65  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686330 245 LPSLPITKLDLQWVQILSEGWATPLKGFMREKEYLQTLHFDTLLDDgvINMSIPIVLPVSADDKARLEGCSKFALMYEGR 324
Cdd:cd00517     1 LPSVELSERDLCDLEMLAEGGFSPLTGFMTEADYLSVLEEMRLLDG--TLWPIPIVLDVSEEDAKRLKEGERVALRYPGQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686330 325 RVALLQDPEFYEHRKEERCSRVWGTATAKHPHIKMVMESGDWLVGGDLQVLERIRWDDgLDQYRLTPLELKQKCKDMNAD 404
Cdd:cd00517    79 PLAILTVEEIYEPDKEEEAARVFGTTDPHHPGVKKVMEQGDWLVGGPIEVLELPPFPD-FDQYRLTPAELRALFKERGWR 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686330 405 AVFAFQLRNPVHNGHALLMQDTRRRLLErgykhPVLLLHPLGGWTKDDDVPLEWRMKQHAAVLEERVLdPKSTIVAIFPS 484
Cdd:cd00517   158 RVVAFQTRNPMHRAHEELMKRAAEKLLN-----DGLLLHPLVGWTKPGDVPDEVRMRAYEALLEEYYL-PERTVLAILPL 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686330 485 PMLYAGPTEVQWHCRCRMIAGANFYIVGRDPAGMPHPETKKDLYEPTHGGKVLSMApglTSVEIIPFRVAAYNKIKKAMD 564
Cdd:cd00517   232 PMRYAGPREALWHAIIRKNYGATHFIVGRDHAGVGHPGDYYGPYDAQEIFKKLAPE---LGIEPVPFREAAYCPKCDGMA 308

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1338686330 565 FYDPARH-EEFDFISGTRMRKLAREGEDPPDGFMAPKAWKVLTDY 608
Cdd:cd00517   309 SEDTCPHgEDFLNISGTKLRKMLREGEKPPEWFMRPEVAKVLREY 353
sopT TIGR00339
ATP sulphurylase; This enzyme forms adenosine 5'-phosphosulfate (APS) from ATP and free ...
 236-607 3.17e-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: 3.17e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686330 236 DQIRAEAETLPSLPITKLDLQWVQILSEGWATPLKGFMREKEYLQTLHfDTLLDDGViNMSIPIVLPVSADDKARLEGCS 315
Cdd:TIGR00339  18 HKLLAEAESLPSITLSDRQLCDLELLGNGAFSPLEGFMNEADYDSVVE-SMRLSDGV-LFSVPITLDIDDEDADDIKLGD 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686330 316 KFALMYE-GRRVALLQDPEFYEHRKEERCSRVWGTATAKHPHIKMVMESGDWLVGGDLQVLERIRWDDgLDQYRLTPLEL 394
Cdd:TIGR00339  96 RIALTDPkGQPLAILTIEEVYKPNKEKEAKKVFGTTDPEHPGVVYLNTAGNYYIGGPIEVINLPKFYD-FPRFRFTPAEL 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686330 395 KQKCKDMNADAVFAFQLRNPVHNGHALLMQDTRRRLlergyKHPVLLLHPLGGWTKDDDVPLEWRMKQHAaVLEERVLDP 474
Cdd:TIGR00339 175 REEFKERGWDTVVAFQTRNPMHRAHEELTKRAAERL-----PNAGVLVHPLVGLTKPGDIPAEVRMRAYE-VLKEGYPNP 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686330 475 KSTIVAIFPSPMLYAGPTEVQWHCRCRMIAGANFYIVGRDPAGMPHPETKKDLYEPTHGGKVLSMAPGLTSVEIIPFRVA 554
Cdd:TIGR00339 249 ERTVVSFLPLAMRYAGPREAIWHAIIRKNYGATHFIVGRDHAGPGSNSKGQDFYGPYDAQELFEKYKAELGIKIVPFRHV 328

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1338686330 555 AYNKIKKAMDFYDPARHEEFDF--ISGTRMRKLAREGEDPPDGFMAPKAWKVLTD 607
Cdd:TIGR00339 329 AYCPDEDEYAPADQAGHTNLRTlnISGTKLRGMLRNGVFPPEWFSRPEVVKILRE 383
CysC COG0529
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ...
 24-218 7.19e-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: 7.19e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686330  24 HHVSRNKRGQvvgtRGGFRGCTVWLTGLSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRHGLNKNLGFSAGDREENIRR 103
Cdd:COG0529     1 SAVTREERAA----LKGQKGFVVWFTGLSGSGKSTLANALERRLFERGRHVYLLDGDNVRHGLNKDLGFSKEDRDENIRR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686330 104 IAEVARLFADAGLVCITSFISPFAKDRENARKIHESAglPFFEIFVDAPLNICESRDVKGLYKRARAGEIKGFTGIDSDY 183
Cdd:COG0529    77 IGEVAKLLADAGLIVLVAFISPYRADREEARELIGEG--EFIEVYVDTPLEVCEARDPKGLYAKARAGEIKNFTGIDDPY 154

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1338686330 184 EKPETPECVLKTNLSSVSDCVQQVVELLQEQNIVP 218
Cdd:COG0529   155 EAPENPELVLDTDKESVEESVEKILAYLEERGYIS 189
APSK cd02027
Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5 ...
 45-195 5.08e-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: 300.93  E-value: 5.08e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686330  45 TVWLTGLSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRHGLNKNLGFSAGDREENIRRIAEVARLFADAGLVCITSFIS 124
Cdd:cd02027     1 VIWLTGLSGSGKSTIARALEEKLFQRGRPVYVLDGDNVRHGLNKDLGFSREDREENIRRIAEVAKLLADAGLIVIAAFIS 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1338686330 125 PFAKDRENARKIHEsaGLPFFEIFVDAPLNICESRDVKGLYKRARAGEIKGFTGIDSDYEKPETPECVLKT 195
Cdd:cd02027    81 PYREDREAARKIIG--GGDFLEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDDPYEAPENPDLVLDT 149
APS_kinase pfam01583
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3 ...
 42-195 8.17e-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: 8.17e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686330  42 RGCTVWLTGLSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRHGLNKNLGFSAGDREENIRRIAEVARLFADAGLVCITS 121
Cdd:pfam01583   1 RGCTIWLTGLSGAGKSTIANALERKLFEQGRSVYVLDGDNVRHGLNKDLGFSEEDRTENIRRIGEVAKLFADAGLIVITA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1338686330 122 FISPFAKDRENARKIHESAglPFFEIFVDAPLNICESRDVKGLYKRARAGEIKGFTGIDSDYEKPETPECVLKT 195
Cdd:pfam01583  81 FISPYREDREQARELHEEG--KFIEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDSPYEAPENPELVLDT 152
ATP-sulfurylase pfam01747
ATP-sulfurylase; This domain is the catalytic domain of ATP-sulfurylase or sulfate ...
 385-608 1.13e-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: 284.43  E-value: 1.13e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686330 385 DQYRLTPLELKQKCKDMNADAVFAFQLRNPVHNGHALLMQDTRRRLlERGYkhpvLLLHPLGGWTKDDDVPLEWRMKQHA 464
Cdd:pfam01747   1 DEYRLTPAETRALFKEKGWRTVVAFQTRNPLHRAHEELMKRALEEL-EADG----LLLHPLVGPTKPGDVPAEVRVRCYE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686330 465 AVLEErVLDPKSTIVAIFPSPMLYAGPTEVQWHCRCRMIAGANFYIVGRDPAGMPHpetkkdLYEPTHGGKVLSMAPGLT 544
Cdd:pfam01747  76 ALLEN-YLPPDRVVLALLPLAMRYAGPREALLHAIIRKNYGCTHFIVGRDHAGVGD------FYGPYDAQEIFDEYPGEL 148

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1338686330 545 SVEIIPFRVAAYNKIKKAM-DFYDPARHEEFDFISGTRMRKLAREGEDPPDGFMAPKAWKVLTDY 608
Cdd:pfam01747 149 GIEPVPFREAVYCKKCGEMaSTKCPHGGEDRLFISGTKVRELLREGEEPPEWFSRPEVAKVLREY 213
PRK03846 PRK03846
adenylylsulfate kinase; Provisional
 16-217 7.75e-89

adenylylsulfate kinase; Provisional


Pssm-ID: 179661  Cd Length: 198  Bit Score: 273.74  E-value: 7.75e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686330  16 STNVVYQAHHVSRNKRGQvvgtRGGFRGCTVWLTGLSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRHGLNKNLGFSAG 95
Cdd:PRK03846    1 DENIVWHQHPVTKAQREQ----LHGHKGVVLWFTGLSGSGKSTVAGALEEALHELGVSTYLLDGDNVRHGLCSDLGFSDA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686330  96 DREENIRRIAEVARLFADAGLVCITSFISPFAKDRENARKIhesagLP---FFEIFVDAPLNICESRDVKGLYKRARAGE 172
Cdd:PRK03846   77 DRKENIRRVGEVAKLMVDAGLVVLTAFISPHRAERQMVRER-----LGegeFIEVFVDTPLAICEARDPKGLYKKARAGE 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1338686330 173 IKGFTGIDSDYEKPETPECVLKTNLSSVSDCVQQVVELLQEQNIV 217
Cdd:PRK03846  152 IRNFTGIDSVYEAPESPEIHLDTGEQLVTNLVEQLLDYLRQRDII 196
apsK TIGR00455
adenylyl-sulfate kinase; This protein, adenylylsulfate kinase, is often found as a fusion ...
 25-211 4.91e-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: 255.86  E-value: 4.91e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686330  25 HVSRNKRGQVVGTRGgfrgCTVWLTGLSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRHGLNKNLGFSAGDREENIRRI 104
Cdd:TIGR00455   4 AITKDERQALNGHRG----VVIWLTGLSGSGKSTIANALEKKLESKGYRVYVLDGDNVRHGLNKDLGFSEEDRKENIRRI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686330 105 AEVARLFADAGLVCITSFISPFAKDRENARKIHESAglPFFEIFVDAPLNICESRDVKGLYKRARAGEIKGFTGIDSDYE 184
Cdd:TIGR00455  80 GEVAKLFVRNGIIVITSFISPYRADRQMVRELIEKG--EFIEVFVDCPLEVCEQRDPKGLYKKARNGEIKGFTGIDSPYE 157

                         170       180
                  ....*....|....*....|....*..
gi 1338686330 185 KPETPECVLKTNLSSVSDCVQQVVELL 211
Cdd:TIGR00455 158 APENPEVVLDTDQNDREECVGQIIEKL 184
MET3 COG2046
ATP sulfurylase (sulfate adenylyltransferase) [Inorganic ion transport and metabolism]; ATP ...
 227-614 4.60e-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: 4.60e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686330 227 ELFVPENKVDQIRAEAETLPSLPITKLDLQWVQILSEGWATPLKGFMREKEYLQTLHfDTLLDDGVInMSIPIVLPVSAD 306
Cdd:COG2046    14 NRVVPGEEREALLEEAKGLPSIELSSRALSDLEMIAIGGFSPLTGFMNKADYESVVE-NMRLADGLL-WPIPITLDVSEE 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686330 307 DKARLEGCSKFALM-YEGRRVALLQDPEFYEHRKEERCSRVWGTATAKHPHIKMVMESGDWLVGGDLQVLERIRWDDgLD 385
Cdd:COG2046    92 DAAGLKEGDEVALRdEEGEPLAVLEVEEIYEYDKEEEAEKVYGTTDPAHPGVAKLYERGDVYLGGPITLLNRPKHPD-FP 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686330 386 QYRLTPLELKQKCKDMNADAVFAFQLRNPVHNGHALLMqdtrRRLLERGYkhpVLLLHPLGGWTKDDDVPLEWRMKQHAA 465
Cdd:COG2046   171 DYRLTPAETRALFEEKGWKTVVAFQTRNPMHRAHEYLQ----KRALETVD---GLLIHPLVGETKPGDIPAEVRVRCYEA 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686330 466 VLEERVlDPKSTIVAIFPSPMLYAGPTEVQWHCRCRMIAGANFYIVGRDPAGMPhpetkkDLYEP--------THGGKVL 537
Cdd:COG2046   244 LLENYY-PKDRVLLSGLPLAMRYAGPREALLHAIIRKNYGCTHFIVGRDHAGVG------DYYGPydaqeifdEFPPGEL 316

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1338686330 538 SMapgltsvEIIPFRVAAYNKIKKAMDFYD--PARHEEFDFISGTRMRKLAREGEDPPDGFMAPKAWKVLTDYYRSLEK 614
Cdd:COG2046   317 GI-------EPLKFEEAFYCKKCGGMATSKtcPHDKEDRVSLSGTKVREMLREGEEPPPEFSRPEVAEILRKYYQPFGE 388
sat PRK04149
sulfate adenylyltransferase; Reviewed
 227-613 2.58e-63

sulfate adenylyltransferase; Reviewed


Pssm-ID: 235227  Cd Length: 391  Bit Score: 213.95  E-value: 2.58e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686330 227 ELFVPENKVDQIRAEAETLPSLPITKLDLQWVQILSEGWATPLKGFMREKEYLQTLHFDTLLDDGVinMSIPIVLPVSAD 306
Cdd:PRK04149   13 NRVVEGRDREEILEEAESLPRIELDERAASDLEMIAIGGFSPLTGFMGREDYDSVVEEMRLANGLV--WSIPITLDVSEE 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686330 307 DKARLEGCSKFALMYEGRRVALLQDPEFYEHRKEERCSRVWGTATAKHPHIKMVMESGDWLVGGDLQVLERIRwDDGLDQ 386
Cdd:PRK04149   91 DAASLKEGDEVALVYKGEPYGVLEVEEIYTYDKKKEAEKVYKTTDEKHPGVKKLYEQGDVYLAGPVTLLNRKF-HEPFPR 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686330 387 YRLTPLELKQKCKDMNADAVFAFQLRNPVHNGHALLMqdtrrrllergyKHPV-----LLLHPLGGWTKDDDVPLEWRMK 461
Cdd:PRK04149  170 FWLTPAETRELFEEKGWKTVVAFQTRNPPHRAHEYLQ------------KCALeivdgLLLNPLVGETKSGDIPAEVRME 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686330 462 QHAAVLeERVLDPKSTIVAIFPSPMLYAGPTEVQWHCRCRMIAGANFYIVGRDPAGMphpetkKDLYEPTHGGKVLSM-- 539
Cdd:PRK04149  238 AYEALL-KNYYPKDRVLLSVTPAAMRYAGPREAIFHAIVRKNYGCTHFIVGRDHAGV------GDYYGPYDAQEIFDEft 310

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1338686330 540 APGLtSVEIIPFRVAAYNKIKKAMDF-----YDPARHEEFdfiSGTRMRKLAREGEDPPDGFMAPKAWKVLTDYYRSLE 613
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, ...
 245-608 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: 515.65  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686330 245 LPSLPITKLDLQWVQILSEGWATPLKGFMREKEYLQTLHFDTLLDDgvINMSIPIVLPVSADDKARLEGCSKFALMYEGR 324
Cdd:cd00517     1 LPSVELSERDLCDLEMLAEGGFSPLTGFMTEADYLSVLEEMRLLDG--TLWPIPIVLDVSEEDAKRLKEGERVALRYPGQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686330 325 RVALLQDPEFYEHRKEERCSRVWGTATAKHPHIKMVMESGDWLVGGDLQVLERIRWDDgLDQYRLTPLELKQKCKDMNAD 404
Cdd:cd00517    79 PLAILTVEEIYEPDKEEEAARVFGTTDPHHPGVKKVMEQGDWLVGGPIEVLELPPFPD-FDQYRLTPAELRALFKERGWR 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686330 405 AVFAFQLRNPVHNGHALLMQDTRRRLLErgykhPVLLLHPLGGWTKDDDVPLEWRMKQHAAVLEERVLdPKSTIVAIFPS 484
Cdd:cd00517   158 RVVAFQTRNPMHRAHEELMKRAAEKLLN-----DGLLLHPLVGWTKPGDVPDEVRMRAYEALLEEYYL-PERTVLAILPL 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686330 485 PMLYAGPTEVQWHCRCRMIAGANFYIVGRDPAGMPHPETKKDLYEPTHGGKVLSMApglTSVEIIPFRVAAYNKIKKAMD 564
Cdd:cd00517   232 PMRYAGPREALWHAIIRKNYGATHFIVGRDHAGVGHPGDYYGPYDAQEIFKKLAPE---LGIEPVPFREAAYCPKCDGMA 308

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1338686330 565 FYDPARH-EEFDFISGTRMRKLAREGEDPPDGFMAPKAWKVLTDY 608
Cdd:cd00517   309 SEDTCPHgEDFLNISGTKLRKMLREGEKPPEWFMRPEVAKVLREY 353
sopT TIGR00339
ATP sulphurylase; This enzyme forms adenosine 5'-phosphosulfate (APS) from ATP and free ...
 236-607 3.17e-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: 3.17e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686330 236 DQIRAEAETLPSLPITKLDLQWVQILSEGWATPLKGFMREKEYLQTLHfDTLLDDGViNMSIPIVLPVSADDKARLEGCS 315
Cdd:TIGR00339  18 HKLLAEAESLPSITLSDRQLCDLELLGNGAFSPLEGFMNEADYDSVVE-SMRLSDGV-LFSVPITLDIDDEDADDIKLGD 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686330 316 KFALMYE-GRRVALLQDPEFYEHRKEERCSRVWGTATAKHPHIKMVMESGDWLVGGDLQVLERIRWDDgLDQYRLTPLEL 394
Cdd:TIGR00339  96 RIALTDPkGQPLAILTIEEVYKPNKEKEAKKVFGTTDPEHPGVVYLNTAGNYYIGGPIEVINLPKFYD-FPRFRFTPAEL 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686330 395 KQKCKDMNADAVFAFQLRNPVHNGHALLMQDTRRRLlergyKHPVLLLHPLGGWTKDDDVPLEWRMKQHAaVLEERVLDP 474
Cdd:TIGR00339 175 REEFKERGWDTVVAFQTRNPMHRAHEELTKRAAERL-----PNAGVLVHPLVGLTKPGDIPAEVRMRAYE-VLKEGYPNP 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686330 475 KSTIVAIFPSPMLYAGPTEVQWHCRCRMIAGANFYIVGRDPAGMPHPETKKDLYEPTHGGKVLSMAPGLTSVEIIPFRVA 554
Cdd:TIGR00339 249 ERTVVSFLPLAMRYAGPREAIWHAIIRKNYGATHFIVGRDHAGPGSNSKGQDFYGPYDAQELFEKYKAELGIKIVPFRHV 328

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1338686330 555 AYNKIKKAMDFYDPARHEEFDF--ISGTRMRKLAREGEDPPDGFMAPKAWKVLTD 607
Cdd:TIGR00339 329 AYCPDEDEYAPADQAGHTNLRTlnISGTKLRGMLRNGVFPPEWFSRPEVVKILRE 383
CysC COG0529
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ...
 24-218 7.19e-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: 7.19e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686330  24 HHVSRNKRGQvvgtRGGFRGCTVWLTGLSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRHGLNKNLGFSAGDREENIRR 103
Cdd:COG0529     1 SAVTREERAA----LKGQKGFVVWFTGLSGSGKSTLANALERRLFERGRHVYLLDGDNVRHGLNKDLGFSKEDRDENIRR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686330 104 IAEVARLFADAGLVCITSFISPFAKDRENARKIHESAglPFFEIFVDAPLNICESRDVKGLYKRARAGEIKGFTGIDSDY 183
Cdd:COG0529    77 IGEVAKLLADAGLIVLVAFISPYRADREEARELIGEG--EFIEVYVDTPLEVCEARDPKGLYAKARAGEIKNFTGIDDPY 154

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1338686330 184 EKPETPECVLKTNLSSVSDCVQQVVELLQEQNIVP 218
Cdd:COG0529   155 EAPENPELVLDTDKESVEESVEKILAYLEERGYIS 189
APSK cd02027
Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5 ...
 45-195 5.08e-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: 300.93  E-value: 5.08e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686330  45 TVWLTGLSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRHGLNKNLGFSAGDREENIRRIAEVARLFADAGLVCITSFIS 124
Cdd:cd02027     1 VIWLTGLSGSGKSTIARALEEKLFQRGRPVYVLDGDNVRHGLNKDLGFSREDREENIRRIAEVAKLLADAGLIVIAAFIS 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1338686330 125 PFAKDRENARKIHEsaGLPFFEIFVDAPLNICESRDVKGLYKRARAGEIKGFTGIDSDYEKPETPECVLKT 195
Cdd:cd02027    81 PYREDREAARKIIG--GGDFLEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDDPYEAPENPDLVLDT 149
APS_kinase pfam01583
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3 ...
 42-195 8.17e-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: 8.17e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686330  42 RGCTVWLTGLSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRHGLNKNLGFSAGDREENIRRIAEVARLFADAGLVCITS 121
Cdd:pfam01583   1 RGCTIWLTGLSGAGKSTIANALERKLFEQGRSVYVLDGDNVRHGLNKDLGFSEEDRTENIRRIGEVAKLFADAGLIVITA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1338686330 122 FISPFAKDRENARKIHESAglPFFEIFVDAPLNICESRDVKGLYKRARAGEIKGFTGIDSDYEKPETPECVLKT 195
Cdd:pfam01583  81 FISPYREDREQARELHEEG--KFIEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDSPYEAPENPELVLDT 152
ATP-sulfurylase pfam01747
ATP-sulfurylase; This domain is the catalytic domain of ATP-sulfurylase or sulfate ...
 385-608 1.13e-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: 284.43  E-value: 1.13e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686330 385 DQYRLTPLELKQKCKDMNADAVFAFQLRNPVHNGHALLMQDTRRRLlERGYkhpvLLLHPLGGWTKDDDVPLEWRMKQHA 464
Cdd:pfam01747   1 DEYRLTPAETRALFKEKGWRTVVAFQTRNPLHRAHEELMKRALEEL-EADG----LLLHPLVGPTKPGDVPAEVRVRCYE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686330 465 AVLEErVLDPKSTIVAIFPSPMLYAGPTEVQWHCRCRMIAGANFYIVGRDPAGMPHpetkkdLYEPTHGGKVLSMAPGLT 544
Cdd:pfam01747  76 ALLEN-YLPPDRVVLALLPLAMRYAGPREALLHAIIRKNYGCTHFIVGRDHAGVGD------FYGPYDAQEIFDEYPGEL 148

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1338686330 545 SVEIIPFRVAAYNKIKKAM-DFYDPARHEEFDFISGTRMRKLAREGEDPPDGFMAPKAWKVLTDY 608
Cdd:pfam01747 149 GIEPVPFREAVYCKKCGEMaSTKCPHGGEDRLFISGTKVRELLREGEEPPEWFSRPEVAKVLREY 213
PRK03846 PRK03846
adenylylsulfate kinase; Provisional
 16-217 7.75e-89

adenylylsulfate kinase; Provisional


Pssm-ID: 179661  Cd Length: 198  Bit Score: 273.74  E-value: 7.75e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686330  16 STNVVYQAHHVSRNKRGQvvgtRGGFRGCTVWLTGLSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRHGLNKNLGFSAG 95
Cdd:PRK03846    1 DENIVWHQHPVTKAQREQ----LHGHKGVVLWFTGLSGSGKSTVAGALEEALHELGVSTYLLDGDNVRHGLCSDLGFSDA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686330  96 DREENIRRIAEVARLFADAGLVCITSFISPFAKDRENARKIhesagLP---FFEIFVDAPLNICESRDVKGLYKRARAGE 172
Cdd:PRK03846   77 DRKENIRRVGEVAKLMVDAGLVVLTAFISPHRAERQMVRER-----LGegeFIEVFVDTPLAICEARDPKGLYKKARAGE 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1338686330 173 IKGFTGIDSDYEKPETPECVLKTNLSSVSDCVQQVVELLQEQNIV 217
Cdd:PRK03846  152 IRNFTGIDSVYEAPESPEIHLDTGEQLVTNLVEQLLDYLRQRDII 196
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
 14-214 9.25e-87

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 282.97  E-value: 9.25e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686330  14 QKSTNVVYQAHHVSRNKRGqvvgTRGGFRGCTVWLTGLSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRHGLNKNLGFS 93
Cdd:PRK05506  435 RRATNVHWQASDVSREARA----ARKGQKPATVWFTGLSGSGKSTIANLVERRLHALGRHTYLLDGDNVRHGLNRDLGFS 510

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686330  94 AGDREENIRRIAEVARLFADAGLVCITSFISPFAKDRENARKIHESAglPFFEIFVDAPLNICESRDVKGLYKRARAGEI 173
Cdd:PRK05506  511 DADRVENIRRVAEVARLMADAGLIVLVSFISPFREERELARALHGEG--EFVEVFVDTPLEVCEARDPKGLYAKARAGEI 588

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1338686330 174 KGFTGIDSDYEKPETPECVLKTNLSSVSDCVQQVVELLQEQ 214
Cdd:PRK05506  589 KNFTGIDSPYEAPENPELRLDTTGRSPEELAEQVLELLRRR 629
apsK TIGR00455
adenylyl-sulfate kinase; This protein, adenylylsulfate kinase, is often found as a fusion ...
 25-211 4.91e-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: 255.86  E-value: 4.91e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686330  25 HVSRNKRGQVVGTRGgfrgCTVWLTGLSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRHGLNKNLGFSAGDREENIRRI 104
Cdd:TIGR00455   4 AITKDERQALNGHRG----VVIWLTGLSGSGKSTIANALEKKLESKGYRVYVLDGDNVRHGLNKDLGFSEEDRKENIRRI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686330 105 AEVARLFADAGLVCITSFISPFAKDRENARKIHESAglPFFEIFVDAPLNICESRDVKGLYKRARAGEIKGFTGIDSDYE 184
Cdd:TIGR00455  80 GEVAKLFVRNGIIVITSFISPYRADRQMVRELIEKG--EFIEVFVDCPLEVCEQRDPKGLYKKARNGEIKGFTGIDSPYE 157

                         170       180
                  ....*....|....*....|....*..
gi 1338686330 185 KPETPECVLKTNLSSVSDCVQQVVELL 211
Cdd:TIGR00455 158 APENPEVVLDTDQNDREECVGQIIEKL 184
MET3 COG2046
ATP sulfurylase (sulfate adenylyltransferase) [Inorganic ion transport and metabolism]; ATP ...
 227-614 4.60e-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: 4.60e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686330 227 ELFVPENKVDQIRAEAETLPSLPITKLDLQWVQILSEGWATPLKGFMREKEYLQTLHfDTLLDDGVInMSIPIVLPVSAD 306
Cdd:COG2046    14 NRVVPGEEREALLEEAKGLPSIELSSRALSDLEMIAIGGFSPLTGFMNKADYESVVE-NMRLADGLL-WPIPITLDVSEE 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686330 307 DKARLEGCSKFALM-YEGRRVALLQDPEFYEHRKEERCSRVWGTATAKHPHIKMVMESGDWLVGGDLQVLERIRWDDgLD 385
Cdd:COG2046    92 DAAGLKEGDEVALRdEEGEPLAVLEVEEIYEYDKEEEAEKVYGTTDPAHPGVAKLYERGDVYLGGPITLLNRPKHPD-FP 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686330 386 QYRLTPLELKQKCKDMNADAVFAFQLRNPVHNGHALLMqdtrRRLLERGYkhpVLLLHPLGGWTKDDDVPLEWRMKQHAA 465
Cdd:COG2046   171 DYRLTPAETRALFEEKGWKTVVAFQTRNPMHRAHEYLQ----KRALETVD---GLLIHPLVGETKPGDIPAEVRVRCYEA 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686330 466 VLEERVlDPKSTIVAIFPSPMLYAGPTEVQWHCRCRMIAGANFYIVGRDPAGMPhpetkkDLYEP--------THGGKVL 537
Cdd:COG2046   244 LLENYY-PKDRVLLSGLPLAMRYAGPREALLHAIIRKNYGCTHFIVGRDHAGVG------DYYGPydaqeifdEFPPGEL 316

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1338686330 538 SMapgltsvEIIPFRVAAYNKIKKAMDFYD--PARHEEFDFISGTRMRKLAREGEDPPDGFMAPKAWKVLTDYYRSLEK 614
Cdd:COG2046   317 GI-------EPLKFEEAFYCKKCGGMATSKtcPHDKEDRVSLSGTKVREMLREGEEPPPEFSRPEVAEILRKYYQPFGE 388
PRK00889 PRK00889
adenylylsulfate kinase; Provisional
 42-218 9.25e-72

adenylylsulfate kinase; Provisional


Pssm-ID: 179157  Cd Length: 175  Bit Score: 228.75  E-value: 9.25e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686330  42 RGCTVWLTGLSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRHGLNKNLGFSAGDREENIRRIAEVARLFADAGLVCITS 121
Cdd:PRK00889    3 RGVTVWFTGLSGAGKTTIARALAEKLREAGYPVEVLDGDAVRTNLSKGLGFSKEDRDTNIRRIGFVANLLTRHGVIVLVS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686330 122 FISPFAKDRENARkihesAGLP-FFEIFVDAPLNICESRDVKGLYKRARAGEIKGFTGIDSDYEKPETPECVLKTNLSSV 200
Cdd:PRK00889   83 AISPYRETREEVR-----ANIGnFLEVFVDAPLEVCEQRDVKGLYAKARAGEIKHFTGIDDPYEPPLNPEVECRTDLESL 157

                         170
                  ....*....|....*...
gi 1338686330 201 SDCVQQVVELLQEQNIVP 218
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.
 216-377 1.16e-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: 206.60  E-value: 1.16e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686330 216 IVPHTtiKGIHELFVPENKVDQIRAEAETLPSLPITKLDLQWVQILSEGWATPLKGFMREKEYLQTLHFDTlLDDGVInM 295
Cdd:pfam14306   1 IKPHG--GKLVDLVVRDAEREELLAEAAELPSIELSKRELCDLELIAIGGFSPLTGFMGEADYLSVLEFMR-LADGLL-W 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686330 296 SIPIVLPVSADDKARLEGCSKFALMY-EGRRVALLQDPEFYEHRKEERCSRVWGTATAKHPHIKMVMESGDWLVGGDLQV 374
Cdd:pfam14306  77 SIPITLDVSEEDAASLKEGDRVALRDpEGEPLAILTVEEIYEPDKEEEAEKVFGTTDPAHPGVKKLYEQGDFYVGGDIEV 156


                  ...
gi 1338686330 375 LER 377
Cdd:pfam14306 157 LNR 159
sat PRK04149
sulfate adenylyltransferase; Reviewed
 227-613 2.58e-63

sulfate adenylyltransferase; Reviewed


Pssm-ID: 235227  Cd Length: 391  Bit Score: 213.95  E-value: 2.58e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686330 227 ELFVPENKVDQIRAEAETLPSLPITKLDLQWVQILSEGWATPLKGFMREKEYLQTLHFDTLLDDGVinMSIPIVLPVSAD 306
Cdd:PRK04149   13 NRVVEGRDREEILEEAESLPRIELDERAASDLEMIAIGGFSPLTGFMGREDYDSVVEEMRLANGLV--WSIPITLDVSEE 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686330 307 DKARLEGCSKFALMYEGRRVALLQDPEFYEHRKEERCSRVWGTATAKHPHIKMVMESGDWLVGGDLQVLERIRwDDGLDQ 386
Cdd:PRK04149   91 DAASLKEGDEVALVYKGEPYGVLEVEEIYTYDKKKEAEKVYKTTDEKHPGVKKLYEQGDVYLAGPVTLLNRKF-HEPFPR 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686330 387 YRLTPLELKQKCKDMNADAVFAFQLRNPVHNGHALLMqdtrrrllergyKHPV-----LLLHPLGGWTKDDDVPLEWRMK 461
Cdd:PRK04149  170 FWLTPAETRELFEEKGWKTVVAFQTRNPPHRAHEYLQ------------KCALeivdgLLLNPLVGETKSGDIPAEVRME 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686330 462 QHAAVLeERVLDPKSTIVAIFPSPMLYAGPTEVQWHCRCRMIAGANFYIVGRDPAGMphpetkKDLYEPTHGGKVLSM-- 539
Cdd:PRK04149  238 AYEALL-KNYYPKDRVLLSVTPAAMRYAGPREAIFHAIVRKNYGCTHFIVGRDHAGV------GDYYGPYDAQEIFDEft 310

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1338686330 540 APGLtSVEIIPFRVAAYNKIKKAMDF-----YDPARHEEFdfiSGTRMRKLAREGEDPPDGFMAPKAWKVLTDYYRSLE 613
Cdd:PRK04149  311 EEEL-GITPLKFEEAFYCPKCGGMASektcpHGKEDRVHL---SGTKVREMLREGEKPPPEFSRPEVAEVLIKGLKKYG 385
PRK05537 PRK05537
bifunctional sulfate adenylyltransferase/adenylylsulfate kinase;
43-214 2.17e-53

bifunctional sulfate adenylyltransferase/adenylylsulfate kinase;


Pssm-ID: 180124 [Multi-domain]  Cd Length: 568  Bit Score: 191.81  E-value: 2.17e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686330  43 GCTVWLTGLSGAGKTTISFALEEYLVSHAIPCYS-LDGDNVRHGLNKNLGFSAGDREENIRRIAEVARLFADAGLVCITS 121
Cdd:PRK05537  392 GFTVFFTGLSGAGKSTIAKALMVKLMEMRGRPVTlLDGDVVRKHLSSELGFSKEDRDLNILRIGFVASEITKNGGIAICA 471

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686330 122 FISPFAKDRENARKIHESAGlPFFEIFVDAPLNICESRDVKGLYKRARAGEIKGFTGIDSDYEKPETPECVLKTNLSSVS 201
Cdd:PRK05537  472 PIAPYRATRREVREMIEAYG-GFIEVHVATPLEVCEQRDRKGLYAKAREGKIKGFTGISDPYEPPANPELVIDTTNVTPD 550

                         170
                  ....*....|...
gi 1338686330 202 DCVQQVVELLQEQ 214
Cdd:PRK05537  551 ECAHKILLYLEEK 563
PRK05537 PRK05537
bifunctional sulfate adenylyltransferase/adenylylsulfate kinase;
223-605 4.67e-49

bifunctional sulfate adenylyltransferase/adenylylsulfate kinase;


Pssm-ID: 180124 [Multi-domain]  Cd Length: 568  Bit Score: 179.87  E-value: 4.67e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686330 223 KGIHELFVPENKVDQIRAEAETLPSLpitklDLQWVQI-----LSEGWATPLKGFMREKEYLQTLHfDTLLDDGVInMSI 297
Cdd:PRK05537    7 GPLPNLYVSPESREKLKAEALSLPSL-----DLSPRQIcdlelLMNGGFSPLKGFMGRADYECVLE-NMRLADGTL-WPI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686330 298 PIVLPVSADDKARLEGCSKFALM-YEGRRVALLQDPEFYEHRKEERCSRVWGTATAKHPHI-KMVMESGDWLVGGDLQVL 375
Cdd:PRK05537   80 PITLDVSEKFAAGLEIGERIALRdQEGVLLAILTVSDIWEPDKEREAEAVFGTTDPAHPGVnYLHRWAGKFYLGGPLTGI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686330 376 ERIRWDDgLDQYRLTPLELKQKCKDMNADAVFAFQLRNPVHNGHALLmqdTRRRLLERGYKhpvLLLHPLGGWTKDDDVP 455
Cdd:PRK05537  160 QLPVHYD-FVQLRLTPAELRARFRKLGWRRVVAFQTRNPLHRAHEEL---TKRAAREVGAN---LLIHPVVGMTKPGDID 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686330 456 LEWRMKQHAAVLEErvLDPKSTIVAIFPSPMLYAGPTEVQWHCRCRMIAGANFYIVGRDPAGMPHPETKKDLYEPTHGGK 535
Cdd:PRK05537  233 HFTRVRCYEALLDK--YPPATTLLSLLPLAMRMAGPREALWHAIIRRNYGCTHFIVGRDHAGPGKDSRGKPFYGPYDAQE 310

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1338686330 536 VLSMAPGLTSVEIIPFRVAAYNKIKKAMDFYDPARH-EEFDFISGTRMRKLAREGEDPPDGFMAPKAWKVL 605
Cdd:PRK05537  311 LFAKYADEIGITMVPFKEMVYVQDKAQYVPVDEVPQgATVLTISGTELRRRLREGLEIPEWFSFPEVVAEL 381
PRK05541 PRK05541
adenylylsulfate kinase; Provisional
 43-216 1.14e-25

adenylylsulfate kinase; Provisional


Pssm-ID: 235498  Cd Length: 176  Bit Score: 103.98  E-value: 1.14e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686330  43 GCTVWLTGLSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRhglnKNLGFSAGDREENI---RRIAEVARLFADAGLVCI 119
Cdd:PRK05541    7 GYVIWITGLAGSGKTTIAKALYERLKLKYSNVIYLDGDELR----EILGHYGYDKQSRIemaLKRAKLAKFLADQGMIVI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686330 120 TSFISPFakdRENARkiHESAGLP-FFEIFVDAPLNICESRDVKGLYKRARAGEIKGFTGIDSDYEKPETPECVLKTNLS 198
Cdd:PRK05541   83 VTTISMF---DEIYA--YNRKHLPnYFEVYLKCDMEELIRRDQKGLYTKALKGEIKNVVGVDIPFDEPKADLVIDNSCRT 157

                         170
                  ....*....|....*...
gi 1338686330 199 SVSDCVQQVVELLQEQNI 216
Cdd:PRK05541  158 SLDEKVDLILNKLKLRLI 175
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
46-177 1.40e-08

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


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 54.53  E-value: 1.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686330  46 VWLTGLSGAGKTTISFALEEYLvsHAIPcysLDGDNVRHGLNKNLGFSAGDREENIRR----IAEVARLFADAGLVCIts 121
Cdd:COG0645     2 ILVCGLPGSGKSTLARALAERL--GAVR---LRSDVVRKRLFGAGLAPLERSPEATARtyarLLALARELLAAGRSVI-- 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1338686330 122 FISPFAK--DRENARKIHESAGLPFFEIFVDAPLNICESRdvkgLYKRARAGEIKGFT 177
Cdd:COG0645    75 LDATFLRraQREAFRALAEEAGAPFVLIWLDAPEEVLRER----LEARNAEGGDSDAT 128
Kti12 COG4088
tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) ...
 48-213 8.00e-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: 8.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686330  48 LTGLSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRHGLnKNLGFSAGDREENIRRIAE-VARLFADAGLVCITSFISPF 126
Cdd:COG4088     9 LTGPPGSGKTTFAKALAQRLYAEGIAVALLHSDDFRRFL-VNESFPKETYEEVVEDVRTtTADNALDNGYSVIVDGTFYY 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686330 127 AKDRENARKIHESAGlPFFEIFVDAPLNICESRDvkglykRARAGEI--KGFTGIDSDYEKPET---PECVLKTNLSSVS 201
Cdd:COG4088    88 RSWQRDFRNLAKHKA-PIHIIYLKAPLETALRRN------RERGEPIpeRVIARMYRKFDKPGTkdrPDLVIDTTEDSVS 160

                         170
                  ....*....|..
gi 1338686330 202 DCVQQVVELLQE 213
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 ...
 46-172 1.21e-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: 1.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686330  46 VWLTGLSGAGKTTISFALEEylvshAIPCYSLDGDNVRHGLNKNLGFSAGDREENI----RRIAEVARLFADAGLVCITS 121
Cdd:pfam13671   2 ILLVGLPGSGKSTLARRLLE-----ELGAVRLSSDDERKRLFGEGRPSISYYTDATdrtyERLHELARIALRAGRPVILD 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1338686330 122 FisPFAKDRENARKIH--ESAGLPFFEIFVDAPLNICESRDVkglyKRARAGE 172
Cdd:pfam13671  77 A--TNLRRDERARLLAlaREYGVPVRIVVFEAPEEVLRERLA----ARARAGG 123
GntK cd02021
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting ...
 48-191 1.03e-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: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686330  48 LTGLSGAGKTTISFALeeylvSHAIPCYSLDGDNVRHGLNKNLgFSAG------DRE---ENIRRIAEVARLFADAGLVC 118
Cdd:cd02021     4 VMGVSGSGKSTVGKAL-----AERLGAPFIDGDDLHPPANIAK-MAAGiplndeDRWpwlQALTDALLAKLASAGEGVVV 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1338686330 119 ITSFIspfaKD--RENARKIHESAGLPFfeIFVDAPLNICESRDvkglykRARAGEIKGFTGIDSDYEKPETPEC 191
Cdd:cd02021    78 ACSAL----KRiyRDILRGGAANPRVRF--VHLDGPREVLAERL------AARKGHFMPADLLDSQFETLEPPGE 140
KTI12 pfam08433
Chromatin associated protein KTI12; This is a family of chromatin associated proteins which ...
 46-190 9.06e-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: 9.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1338686330  46 VWLTGLSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRHGlNKNLGFSAGdrEENIRR--IAEVARLFADAGLVCI--TS 121
Cdd:pfam08433   2 VLLTGLPSSGKSTRAKQLAKYLEESNYDVIVISDESLGIE-KDDYKDSAK--EKFLRGslRSAVKRDLSKNTIVIVdsLN 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1338686330 122 FISPFAKDRENARKiheSAGLPFFEIFVDAPLNIC----ESRDVKGLYKRARageikgftgIDSDYEKPETPE 190
Cdd:pfam08433  79 YIKGFRYELYCIAK---AARTTYCVIHCKAPLDLCrkwnEERGQKSRYPDEL---------LDALIQRYEEPN 139
 
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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