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Conserved domains on  [gi|931474955|gb|KPK56380|]
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MAG: adenylylsulfate kinase [Thiotrichales bacterium SG8_50]

Protein Classification

adenylyl-sulfate kinase( domain architecture ID 10785573)

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

CATH:  3.40.50.300
EC:  2.7.1.25
Gene Ontology:  GO:0004020|GO:0005524|GO:0000103
SCOP:  4003930

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
CysC COG0529
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ...
 18-206 2.79e-121

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: 341.30  E-value: 2.79e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474955  18 ATVTRARREALNRHKGAVVWFTGLSGSGKSTLAHTVEEKLYQMGCRTFVFDGDNVRHGLCGDLTFSPEDRRENIRRIGEM 97
Cdd:COG0529    1 SAVTREERAALKGQKGFVVWFTGLSGSGKSTLANALERRLFERGRHVYLLDGDNVRHGLNKDLGFSKEDRDENIRRIGEV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474955  98 TKLFLDAGVIAMTAFISPYRDDRERVRAIVGPTDFIEIHCDCPVEICEQRDVKGMYKKAREGLIKEFTGISAPYETPVAP 177
Cdd:COG0529   81 AKLLADAGLIVLVAFISPYRADREEARELIGEGEFIEVYVDTPLEVCEARDPKGLYAKARAGEIKNFTGIDDPYEAPENP 160

                        170       180
                 ....*....|....*....|....*....
gi 931474955 178 ELRLNTGSDPLDDCADRVLTVLADRGVIS 206
Cdd:COG0529  161 ELVLDTDKESVEESVEKILAYLEERGYIS 189
 
Name Accession Description Interval E-value
CysC COG0529
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ...
 18-206 2.79e-121

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: 341.30  E-value: 2.79e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474955  18 ATVTRARREALNRHKGAVVWFTGLSGSGKSTLAHTVEEKLYQMGCRTFVFDGDNVRHGLCGDLTFSPEDRRENIRRIGEM 97
Cdd:COG0529    1 SAVTREERAALKGQKGFVVWFTGLSGSGKSTLANALERRLFERGRHVYLLDGDNVRHGLNKDLGFSKEDRDENIRRIGEV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474955  98 TKLFLDAGVIAMTAFISPYRDDRERVRAIVGPTDFIEIHCDCPVEICEQRDVKGMYKKAREGLIKEFTGISAPYETPVAP 177
Cdd:COG0529   81 AKLLADAGLIVLVAFISPYRADREEARELIGEGEFIEVYVDTPLEVCEARDPKGLYAKARAGEIKNFTGIDDPYEAPENP 160

                        170       180
                 ....*....|....*....|....*....
gi 931474955 178 ELRLNTGSDPLDDCADRVLTVLADRGVIS 206
Cdd:COG0529  161 ELVLDTDKESVEESVEKILAYLEERGYIS 189
PRK03846 PRK03846
adenylylsulfate kinase; Provisional
 12-207 8.34e-120

adenylylsulfate kinase; Provisional


Pssm-ID: 179661  Cd Length: 198  Bit Score: 338.07  E-value: 8.34e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474955  12 NVVWHHATVTRARREALNRHKGAVVWFTGLSGSGKSTLAHTVEEKLYQMGCRTFVFDGDNVRHGLCGDLTFSPEDRRENI 91
Cdd:PRK03846   3 NIVWHQHPVTKAQREQLHGHKGVVLWFTGLSGSGKSTVAGALEEALHELGVSTYLLDGDNVRHGLCSDLGFSDADRKENI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474955  92 RRIGEMTKLFLDAGVIAMTAFISPYRDDRERVRAIVGPTDFIEIHCDCPVEICEQRDVKGMYKKAREGLIKEFTGISAPY 171
Cdd:PRK03846  83 RRVGEVAKLMVDAGLVVLTAFISPHRAERQMVRERLGEGEFIEVFVDTPLAICEARDPKGLYKKARAGEIRNFTGIDSVY 162

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 931474955 172 ETPVAPELRLNTGSDPLDDCADRVLTVLADRGVISP 207
Cdd:PRK03846 163 EAPESPEIHLDTGEQLVTNLVEQLLDYLRQRDIIRS 198
APSK cd02027
Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5 ...
 35-183 3.34e-97

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: 278.98  E-value: 3.34e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474955  35 VVWFTGLSGSGKSTLAHTVEEKLYQMGCRTFVFDGDNVRHGLCGDLTFSPEDRRENIRRIGEMTKLFLDAGVIAMTAFIS 114
Cdd:cd02027    1 VIWLTGLSGSGKSTIARALEEKLFQRGRPVYVLDGDNVRHGLNKDLGFSREDREENIRRIAEVAKLLADAGLIVIAAFIS 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 931474955 115 PYRDDRERVRAIVGPTDFIEIHCDCPVEICEQRDVKGMYKKAREGLIKEFTGISAPYETPVAPELRLNT 183
Cdd:cd02027   81 PYREDREAARKIIGGGDFLEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDDPYEAPENPDLVLDT 149
apsK TIGR00455
adenylyl-sulfate kinase; This protein, adenylylsulfate kinase, is often found as a fusion ...
 15-199 1.62e-94

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: 273.57  E-value: 1.62e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474955   15 WHHAtVTRARREALNRHKGAVVWFTGLSGSGKSTLAHTVEEKLYQMGCRTFVFDGDNVRHGLCGDLTFSPEDRRENIRRI 94
Cdd:TIGR00455   1 WHPA-ITKDERQALNGHRGVVIWLTGLSGSGKSTIANALEKKLESKGYRVYVLDGDNVRHGLNKDLGFSEEDRKENIRRI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474955   95 GEMTKLFLDAGVIAMTAFISPYRDDRERVRAIVGPTDFIEIHCDCPVEICEQRDVKGMYKKAREGLIKEFTGISAPYETP 174
Cdd:TIGR00455  80 GEVAKLFVRNGIIVITSFISPYRADRQMVRELIEKGEFIEVFVDCPLEVCEQRDPKGLYKKARNGEIKGFTGIDSPYEAP 159

                         170       180
                  ....*....|....*....|....*
gi 931474955  175 VAPELRLNTGSDPLDDCADRVLTVL 199
Cdd:TIGR00455 160 ENPEVVLDTDQNDREECVGQIIEKL 184
APS_kinase pfam01583
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3 ...
 32-184 1.36e-93

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: 269.96  E-value: 1.36e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474955   32 KGAVVWFTGLSGSGKSTLAHTVEEKLYQMGCRTFVFDGDNVRHGLCGDLTFSPEDRRENIRRIGEMTKLFLDAGVIAMTA 111
Cdd:pfam01583   1 RGCTIWLTGLSGAGKSTIANALERKLFEQGRSVYVLDGDNVRHGLNKDLGFSEEDRTENIRRIGEVAKLFADAGLIVITA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 931474955  112 FISPYRDDRERVRAIVGPTDFIEIHCDCPVEICEQRDVKGMYKKAREGLIKEFTGISAPYETPVAPELRLNTG 184
Cdd:pfam01583  81 FISPYREDREQARELHEEGKFIEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDSPYEAPENPELVLDTD 153
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 32-76 6.61e-03

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 35.81  E-value: 6.61e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 931474955    32 KGAVVWFTGLSGSGKSTLAHTVEEKLYQMGCRTFVFDGDNVRHGL 76
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEV 45
 
Name Accession Description Interval E-value
CysC COG0529
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ...
 18-206 2.79e-121

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: 341.30  E-value: 2.79e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474955  18 ATVTRARREALNRHKGAVVWFTGLSGSGKSTLAHTVEEKLYQMGCRTFVFDGDNVRHGLCGDLTFSPEDRRENIRRIGEM 97
Cdd:COG0529    1 SAVTREERAALKGQKGFVVWFTGLSGSGKSTLANALERRLFERGRHVYLLDGDNVRHGLNKDLGFSKEDRDENIRRIGEV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474955  98 TKLFLDAGVIAMTAFISPYRDDRERVRAIVGPTDFIEIHCDCPVEICEQRDVKGMYKKAREGLIKEFTGISAPYETPVAP 177
Cdd:COG0529   81 AKLLADAGLIVLVAFISPYRADREEARELIGEGEFIEVYVDTPLEVCEARDPKGLYAKARAGEIKNFTGIDDPYEAPENP 160

                        170       180
                 ....*....|....*....|....*....
gi 931474955 178 ELRLNTGSDPLDDCADRVLTVLADRGVIS 206
Cdd:COG0529  161 ELVLDTDKESVEESVEKILAYLEERGYIS 189
PRK03846 PRK03846
adenylylsulfate kinase; Provisional
 12-207 8.34e-120

adenylylsulfate kinase; Provisional


Pssm-ID: 179661  Cd Length: 198  Bit Score: 338.07  E-value: 8.34e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474955  12 NVVWHHATVTRARREALNRHKGAVVWFTGLSGSGKSTLAHTVEEKLYQMGCRTFVFDGDNVRHGLCGDLTFSPEDRRENI 91
Cdd:PRK03846   3 NIVWHQHPVTKAQREQLHGHKGVVLWFTGLSGSGKSTVAGALEEALHELGVSTYLLDGDNVRHGLCSDLGFSDADRKENI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474955  92 RRIGEMTKLFLDAGVIAMTAFISPYRDDRERVRAIVGPTDFIEIHCDCPVEICEQRDVKGMYKKAREGLIKEFTGISAPY 171
Cdd:PRK03846  83 RRVGEVAKLMVDAGLVVLTAFISPHRAERQMVRERLGEGEFIEVFVDTPLAICEARDPKGLYKKARAGEIRNFTGIDSVY 162

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 931474955 172 ETPVAPELRLNTGSDPLDDCADRVLTVLADRGVISP 207
Cdd:PRK03846 163 EAPESPEIHLDTGEQLVTNLVEQLLDYLRQRDIIRS 198
APSK cd02027
Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5 ...
 35-183 3.34e-97

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: 278.98  E-value: 3.34e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474955  35 VVWFTGLSGSGKSTLAHTVEEKLYQMGCRTFVFDGDNVRHGLCGDLTFSPEDRRENIRRIGEMTKLFLDAGVIAMTAFIS 114
Cdd:cd02027    1 VIWLTGLSGSGKSTIARALEEKLFQRGRPVYVLDGDNVRHGLNKDLGFSREDREENIRRIAEVAKLLADAGLIVIAAFIS 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 931474955 115 PYRDDRERVRAIVGPTDFIEIHCDCPVEICEQRDVKGMYKKAREGLIKEFTGISAPYETPVAPELRLNT 183
Cdd:cd02027   81 PYREDREAARKIIGGGDFLEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDDPYEAPENPDLVLDT 149
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
 10-205 7.62e-95

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 289.14  E-value: 7.62e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474955  10 TPNVVWHHATVTRARREALNRHKGAVVWFTGLSGSGKSTLAHTVEEKLYQMGCRTFVFDGDNVRHGLCGDLTFSPEDRRE 89
Cdd:PRK05506 437 ATNVHWQASDVSREARAARKGQKPATVWFTGLSGSGKSTIANLVERRLHALGRHTYLLDGDNVRHGLNRDLGFSDADRVE 516

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474955  90 NIRRIGEMTKLFLDAGVIAMTAFISPYRDDRERVRAIVGPTDFIEIHCDCPVEICEQRDVKGMYKKAREGLIKEFTGISA 169
Cdd:PRK05506 517 NIRRVAEVARLMADAGLIVLVSFISPFREERELARALHGEGEFVEVFVDTPLEVCEARDPKGLYAKARAGEIKNFTGIDS 596

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 931474955 170 PYETPVAPELRLNTGSDPLDDCADRVLTVLADRGVI 205
Cdd:PRK05506 597 PYEAPENPELRLDTTGRSPEELAEQVLELLRRRGAI 632
apsK TIGR00455
adenylyl-sulfate kinase; This protein, adenylylsulfate kinase, is often found as a fusion ...
 15-199 1.62e-94

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: 273.57  E-value: 1.62e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474955   15 WHHAtVTRARREALNRHKGAVVWFTGLSGSGKSTLAHTVEEKLYQMGCRTFVFDGDNVRHGLCGDLTFSPEDRRENIRRI 94
Cdd:TIGR00455   1 WHPA-ITKDERQALNGHRGVVIWLTGLSGSGKSTIANALEKKLESKGYRVYVLDGDNVRHGLNKDLGFSEEDRKENIRRI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474955   95 GEMTKLFLDAGVIAMTAFISPYRDDRERVRAIVGPTDFIEIHCDCPVEICEQRDVKGMYKKAREGLIKEFTGISAPYETP 174
Cdd:TIGR00455  80 GEVAKLFVRNGIIVITSFISPYRADRQMVRELIEKGEFIEVFVDCPLEVCEQRDPKGLYKKARNGEIKGFTGIDSPYEAP 159

                         170       180
                  ....*....|....*....|....*
gi 931474955  175 VAPELRLNTGSDPLDDCADRVLTVL 199
Cdd:TIGR00455 160 ENPEVVLDTDQNDREECVGQIIEKL 184
APS_kinase pfam01583
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3 ...
 32-184 1.36e-93

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: 269.96  E-value: 1.36e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474955   32 KGAVVWFTGLSGSGKSTLAHTVEEKLYQMGCRTFVFDGDNVRHGLCGDLTFSPEDRRENIRRIGEMTKLFLDAGVIAMTA 111
Cdd:pfam01583   1 RGCTIWLTGLSGAGKSTIANALERKLFEQGRSVYVLDGDNVRHGLNKDLGFSEEDRTENIRRIGEVAKLFADAGLIVITA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 931474955  112 FISPYRDDRERVRAIVGPTDFIEIHCDCPVEICEQRDVKGMYKKAREGLIKEFTGISAPYETPVAPELRLNTG 184
Cdd:pfam01583  81 FISPYREDREQARELHEEGKFIEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDSPYEAPENPELVLDTD 153
PRK00889 PRK00889
adenylylsulfate kinase; Provisional
 31-205 2.17e-77

adenylylsulfate kinase; Provisional


Pssm-ID: 179157  Cd Length: 175  Bit Score: 229.91  E-value: 2.17e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474955  31 HKGAVVWFTGLSGSGKSTLAHTVEEKLYQMGCRTFVFDGDNVRHGLCGDLTFSPEDRRENIRRIGEMTKLFLDAGVIAMT 110
Cdd:PRK00889   2 QRGVTVWFTGLSGAGKTTIARALAEKLREAGYPVEVLDGDAVRTNLSKGLGFSKEDRDTNIRRIGFVANLLTRHGVIVLV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474955 111 AFISPYRDDRERVRAIVGptDFIEIHCDCPVEICEQRDVKGMYKKAREGLIKEFTGISAPYETPVAPELRLNTGSDPLDD 190
Cdd:PRK00889  82 SAISPYRETREEVRANIG--NFLEVFVDAPLEVCEQRDVKGLYAKARAGEIKHFTGIDDPYEPPLNPEVECRTDLESLEE 159

                        170
                 ....*....|....*
gi 931474955 191 CADRVLTVLADRGVI 205
Cdd:PRK00889 160 SVDKVLQKLEELGYL 174
PRK05537 PRK05537
bifunctional sulfate adenylyltransferase/adenylylsulfate kinase;
19-207 8.36e-67

bifunctional sulfate adenylyltransferase/adenylylsulfate kinase;


Pssm-ID: 180124 [Multi-domain]  Cd Length: 568  Bit Score: 214.92  E-value: 8.36e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474955  19 TVTRARREALNRHK-GAVVWFTGLSGSGKSTLAHTVEEKLYQMGCRTFVF-DGDNVRHGLCGDLTFSPEDRRENIRRIG- 95
Cdd:PRK05537 377 VVAELRRTYPPRHKqGFTVFFTGLSGAGKSTIAKALMVKLMEMRGRPVTLlDGDVVRKHLSSELGFSKEDRDLNILRIGf 456

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474955  96 ---EMTKlfldAGVIAMTAFISPYRDDRERVRAIVGPTD-FIEIHCDCPVEICEQRDVKGMYKKAREGLIKEFTGISAPY 171
Cdd:PRK05537 457 vasEITK----NGGIAICAPIAPYRATRREVREMIEAYGgFIEVHVATPLEVCEQRDRKGLYAKAREGKIKGFTGISDPY 532

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 931474955 172 ETPVAPELRLNTGSDPLDDCADRVLTVLADRGVISP 207
Cdd:PRK05537 533 EPPANPELVIDTTNVTPDECAHKILLYLEEKGYLRG 568
PRK05541 PRK05541
adenylylsulfate kinase; Provisional
 32-204 1.11e-28

adenylylsulfate kinase; Provisional


Pssm-ID: 235498  Cd Length: 176  Bit Score: 105.52  E-value: 1.11e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474955  32 KGAVVWFTGLSGSGKSTLAHTVEEKLYQMGCRTFVFDGDNVRHgLCGDLTFSPEDRRENIRRIGEMTKLFLDAGVIAMTA 111
Cdd:PRK05541   6 NGYVIWITGLAGSGKTTIAKALYERLKLKYSNVIYLDGDELRE-ILGHYGYDKQSRIEMALKRAKLAKFLADQGMIVIVT 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474955 112 FISPYRDDRERVRAIVgpTDFIEIHCDCPVEICEQRDVKGMYKKAREGLIKEFTGISAPYETPVAPELRLNTGSDPLDDC 191
Cdd:PRK05541  85 TISMFDEIYAYNRKHL--PNYFEVYLKCDMEELIRRDQKGLYTKALKGEIKNVVGVDIPFDEPKADLVIDNSCRTSLDEK 162

                        170
                 ....*....|...
gi 931474955 192 ADRVLTVLADRGV 204
Cdd:PRK05541 163 VDLILNKLKLRLI 175
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
35-195 2.41e-13

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


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 64.93  E-value: 2.41e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474955  35 VVWFTGLSGSGKSTLAHTVEEKLyqmgcRTFVFDGDNVRHGLCGDLtFSPEDRRENIR-----RIGEMTKLFLDAG--VI 107
Cdd:COG0645    1 LILVCGLPGSGKSTLARALAERL-----GAVRLRSDVVRKRLFGAG-LAPLERSPEATartyaRLLALARELLAAGrsVI 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474955 108 AMTAFISpyRDDRERVRAIVGPT--DFIEIHCDCPVEIC----EQRDVKGMYKKAREGLIKEFTGISAPYETPVAPELRL 181
Cdd:COG0645   75 LDATFLR--RAQREAFRALAEEAgaPFVLIWLDAPEEVLrerlEARNAEGGDSDATWEVLERQLAFEEPLTEDEGFLLVV 152

                        170
                 ....*....|....
gi 931474955 182 NTgsDPLDDCADRV 195
Cdd:COG0645  153 DT--SGLEEALAAL 164
AAA_33 pfam13671
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ...
 35-150 5.52e-10

AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the AAA superfamily. Many of the proteins in this family are just short fragments so there is no Walker B motif.


Pssm-ID: 463952 [Multi-domain]  Cd Length: 143  Bit Score: 55.39  E-value: 5.52e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474955   35 VVWFTGLSGSGKSTLAHTVEEKLyqmgcRTFVFDGDNVRHGLCGDLTFSPEDRRENI----RRIGEMTKLFLDAG--VIA 108
Cdd:pfam13671   1 LILLVGLPGSGKSTLARRLLEEL-----GAVRLSSDDERKRLFGEGRPSISYYTDATdrtyERLHELARIALRAGrpVIL 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 931474955  109 MTAFISpyRDDRERVRAIVGPTDFIE--IHCDCPVEICEQRDVK 150
Cdd:pfam13671  76 DATNLR--RDERARLLALAREYGVPVriVVFEAPEEVLRERLAA 117
GntK cd02021
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting ...
 39-159 2.76e-05

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: 42.62  E-value: 2.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474955  39 TGLSGSGKSTLAHTVEEKLyqmGCRtfVFDGDNVRHGLCGDLTFS--P---EDRRENIRRIGE-MTKLFLDAG---VIAM 109
Cdd:cd02021    5 MGVSGSGKSTVGKALAERL---GAP--FIDGDDLHPPANIAKMAAgiPlndEDRWPWLQALTDaLLAKLASAGegvVVAC 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 931474955 110 TAFISPYRDdreRVRAIVGPTDFIEIHCDCPVEICEQRDvkgmykKAREG 159
Cdd:cd02021   80 SALKRIYRD---ILRGGAANPRVRFVHLDGPREVLAERL------AARKG 120
uvrA PRK00349
excinuclease ABC subunit UvrA;
35-50 1.91e-03

excinuclease ABC subunit UvrA;


Pssm-ID: 234734 [Multi-domain]  Cd Length: 943  Bit Score: 38.52  E-value: 1.91e-03
                         10
                 ....*....|....*.
gi 931474955  35 VVwFTGLSGSGKSTLA 50
Cdd:PRK00349  29 VV-FTGLSGSGKSSLA 43
UvrA COG0178
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
35-50 3.10e-03

Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];


Pssm-ID: 439948 [Multi-domain]  Cd Length: 941  Bit Score: 38.08  E-value: 3.10e-03
                         10
                 ....*....|....*.
gi 931474955  35 VVwFTGLSGSGKSTLA 50
Cdd:COG0178   29 VV-ITGLSGSGKSSLA 43
HerA COG0433
Archaeal DNA helicase HerA or a related bacterial ATPase, contains HAS-barrel and ATPase ...
 28-94 4.34e-03

Archaeal DNA helicase HerA or a related bacterial ATPase, contains HAS-barrel and ATPase domains [Replication, recombination and repair];


Pssm-ID: 440202 [Multi-domain]  Cd Length: 388  Bit Score: 37.28  E-value: 4.34e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 931474955  28 LNRHkGAVVwftGLSGSGKSTLAHTVEEKLYQMGCRTFVFDgdnvRHglcGDLT--FSPEDRRENIRRI 94
Cdd:COG0433   46 LNRH-ILIL---GATGSGKSNTLQVLLEELSRAGVPVLVFD----PH---GEYSglAEPGAERADVGVF 103
VirB4 COG3451
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and ...
 28-111 5.57e-03

Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 442674 [Multi-domain]  Cd Length: 546  Bit Score: 37.23  E-value: 5.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474955  28 LNRHKGAVVW---FTGLSGSGKSTLAHTVEEKLYQMGCRTFVFD-------------GDNVRHGLCGDLTFSP---EDRR 88
Cdd:COG3451  196 FDFHDGLDNGntlILGPSGSGKSFLLKLLLLQLLRYGARIVIFDpggsyeilvralgGTYIDLSPGSPTGLNPfdlEDTE 275

                         90       100
                 ....*....|....*....|...
gi 931474955  89 ENIRRIGEMTKLFLDAGVIAMTA 111
Cdd:COG3451  276 EKRDFLLELLELLLGREGEPLTP 298
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 32-76 6.61e-03

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 35.81  E-value: 6.61e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 931474955    32 KGAVVWFTGLSGSGKSTLAHTVEEKLYQMGCRTFVFDGDNVRHGL 76
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEV 45
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
 32-66 6.93e-03

excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273184 [Multi-domain]  Cd Length: 925  Bit Score: 36.91  E-value: 6.93e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 931474955   32 KGAVVWFTGLSGSGKSTLAHtveEKLYQMGCRTFV 66
Cdd:TIGR00630  21 RDKLVVITGLSGSGKSSLAF---DTIYAEGQRRYV 52
ExeA COG3267
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ...
 21-86 7.26e-03

Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 442498 [Multi-domain]  Cd Length: 261  Bit Score: 36.30  E-value: 7.26e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 931474955  21 TRARREALNR-------HKGAVVwFTGLSGSGKSTLAHTVEEKLyqmgcrtfvfdGDNVRHGLCGDLTFSPED 86
Cdd:COG3267   25 SPSHREALARleyalaqGGGFVV-LTGEVGTGKTTLLRRLLERL-----------PDDVKVAYIPNPQLSPAE 85
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
 31-91 7.52e-03

ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213195 [Multi-domain]  Cd Length: 171  Bit Score: 35.82  E-value: 7.52e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 931474955  31 HKGAVVWFTGLSGSGKSTLAHTVeEKLYQMGCRTFVFDGDNVRHglcgdltFSPEDRRENI 91
Cdd:cd03228   26 KPGEKVAIVGPSGSGKSTLLKLL-LRLYDPTSGEILIDGVDLRD-------LDLESLRKNI 78
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 20-103 7.98e-03

The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 35.58  E-value: 7.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474955  20 VTRARREALNRHKGAVVWFTGLSGSGKSTLAHTVEEKLYQMGCRTFVFDGdnvrHGLCGDLTFSPEDRRENIRRIGEMTK 99
Cdd:cd00009    6 AIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNA----SDLLEGLVVAELFGHFLVRLLFELAE 81

                         90
                 ....*....|
gi 931474955 100 ------LFLD 103
Cdd:cd00009   82 kakpgvLFID 91
 
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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