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Conserved domains on  [gi|505384611|ref|WP_015571713|]
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MULTISPECIES: adenylyl-sulfate kinase [Enterobacter]

Protein Classification

adenylyl-sulfate kinase( domain architecture ID 10792327)

adenylylsulfate kinase catalyzes the ATP-dependent phosphorylation of adenosine 5'-phosphosulfate (APS) to 3'-phosphoadenosine-5'-phosphosulfate (PAPS); it is often found as a fusion protein with sulphate adenylyltransferase. Both enzymes are required for PAPS (phosphoadenosine-phosphosulfate) synthesis from inorganic sulfate

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
PRK03846 PRK03846
adenylylsulfate kinase; Provisional
 5-201 7.59e-152

adenylylsulfate kinase; Provisional


:

Pssm-ID: 179661  Cd Length: 198  Bit Score: 418.58  E-value: 7.59e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384611   5 DENVVWHPHPVTVAQREQLHGHRGVVLWFTGLSGSGKSTVAGALEEALHQQGVSTYLLDGDNVRHGLCSDLGFSDEDRKE 84
Cdd:PRK03846   1 DENIVWHQHPVTKAQREQLHGHKGVVLWFTGLSGSGKSTVAGALEEALHELGVSTYLLDGDNVRHGLCSDLGFSDADRKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384611  85 NIRRVGEVASLMADAGLVVLTAFISPHRAERQMVRERVGQNRFIEVFVDTPLAICEARDPKGLYKKARAGELRNFTGIDS 164
Cdd:PRK03846  81 NIRRVGEVAKLMVDAGLVVLTAFISPHRAERQMVRERLGEGEFIEVFVDTPLAICEARDPKGLYKKARAGEIRNFTGIDS 160

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 505384611 165 VYEAPESPEIHLE-GQQLVTNLVSQLLDLLRRDDIIRS 201
Cdd:PRK03846 161 VYEAPESPEIHLDtGEQLVTNLVEQLLDYLRQRDIIRS 198
 
Name Accession Description Interval E-value
PRK03846 PRK03846
adenylylsulfate kinase; Provisional
 5-201 7.59e-152

adenylylsulfate kinase; Provisional


Pssm-ID: 179661  Cd Length: 198  Bit Score: 418.58  E-value: 7.59e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384611   5 DENVVWHPHPVTVAQREQLHGHRGVVLWFTGLSGSGKSTVAGALEEALHQQGVSTYLLDGDNVRHGLCSDLGFSDEDRKE 84
Cdd:PRK03846   1 DENIVWHQHPVTKAQREQLHGHKGVVLWFTGLSGSGKSTVAGALEEALHELGVSTYLLDGDNVRHGLCSDLGFSDADRKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384611  85 NIRRVGEVASLMADAGLVVLTAFISPHRAERQMVRERVGQNRFIEVFVDTPLAICEARDPKGLYKKARAGELRNFTGIDS 164
Cdd:PRK03846  81 NIRRVGEVAKLMVDAGLVVLTAFISPHRAERQMVRERLGEGEFIEVFVDTPLAICEARDPKGLYKKARAGEIRNFTGIDS 160

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 505384611 165 VYEAPESPEIHLE-GQQLVTNLVSQLLDLLRRDDIIRS 201
Cdd:PRK03846 161 VYEAPESPEIHLDtGEQLVTNLVEQLLDYLRQRDIIRS 198
CysC COG0529
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ...
 13-200 7.87e-126

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: 352.47  E-value: 7.87e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384611  13 HPVTVAQREQLHGHRGVVLWFTGLSGSGKSTVAGALEEALHQQGVSTYLLDGDNVRHGLCSDLGFSDEDRKENIRRVGEV 92
Cdd:COG0529    1 SAVTREERAALKGQKGFVVWFTGLSGSGKSTLANALERRLFERGRHVYLLDGDNVRHGLNKDLGFSKEDRDENIRRIGEV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384611  93 ASLMADAGLVVLTAFISPHRAERQMVRERVGQNRFIEVFVDTPLAICEARDPKGLYKKARAGELRNFTGIDSVYEAPESP 172
Cdd:COG0529   81 AKLLADAGLIVLVAFISPYRADREEARELIGEGEFIEVYVDTPLEVCEARDPKGLYAKARAGEIKNFTGIDDPYEAPENP 160

                        170       180
                 ....*....|....*....|....*....
gi 505384611 173 EIHLEGQQL-VTNLVSQLLDLLRRDDIIR 200
Cdd:COG0529  161 ELVLDTDKEsVEESVEKILAYLEERGYIS 189
apsK TIGR00455
adenylyl-sulfate kinase; This protein, adenylylsulfate kinase, is often found as a fusion ...
 10-193 2.80e-113

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: 320.57  E-value: 2.80e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384611   10 WHPHpVTVAQREQLHGHRGVVLWFTGLSGSGKSTVAGALEEALHQQGVSTYLLDGDNVRHGLCSDLGFSDEDRKENIRRV 89
Cdd:TIGR00455   1 WHPA-ITKDERQALNGHRGVVIWLTGLSGSGKSTIANALEKKLESKGYRVYVLDGDNVRHGLNKDLGFSEEDRKENIRRI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384611   90 GEVASLMADAGLVVLTAFISPHRAERQMVRERVGQNRFIEVFVDTPLAICEARDPKGLYKKARAGELRNFTGIDSVYEAP 169
Cdd:TIGR00455  80 GEVAKLFVRNGIIVITSFISPYRADRQMVRELIEKGEFIEVFVDCPLEVCEQRDPKGLYKKARNGEIKGFTGIDSPYEAP 159

                         170       180
                  ....*....|....*....|....*
gi 505384611  170 ESPEIHLE-GQQLVTNLVSQLLDLL 193
Cdd:TIGR00455 160 ENPEVVLDtDQNDREECVGQIIEKL 184
APSK cd02027
Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5 ...
 30-177 9.36e-104

Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5'-phosphosulfate to form 3'-phosphoadenosine 5'-phosphosulfate (PAPS). The end-product PAPS is a biologically "activated" sulfate form important for the assimilation of inorganic sulfate.


Pssm-ID: 238985 [Multi-domain]  Cd Length: 149  Bit Score: 295.16  E-value: 9.36e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384611  30 VLWFTGLSGSGKSTVAGALEEALHQQGVSTYLLDGDNVRHGLCSDLGFSDEDRKENIRRVGEVASLMADAGLVVLTAFIS 109
Cdd:cd02027    1 VIWLTGLSGSGKSTIARALEEKLFQRGRPVYVLDGDNVRHGLNKDLGFSREDREENIRRIAEVAKLLADAGLIVIAAFIS 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505384611 110 PHRAERQMVRERVGQNRFIEVFVDTPLAICEARDPKGLYKKARAGELRNFTGIDSVYEAPESPEIHLE 177
Cdd:cd02027   81 PYREDREAARKIIGGGDFLEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDDPYEAPENPDLVLD 148
APS_kinase pfam01583
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3 ...
 27-180 3.96e-103

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: 293.84  E-value: 3.96e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384611   27 RGVVLWFTGLSGSGKSTVAGALEEALHQQGVSTYLLDGDNVRHGLCSDLGFSDEDRKENIRRVGEVASLMADAGLVVLTA 106
Cdd:pfam01583   1 RGCTIWLTGLSGAGKSTIANALERKLFEQGRSVYVLDGDNVRHGLNKDLGFSEEDRTENIRRIGEVAKLFADAGLIVITA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505384611  107 FISPHRAERQMVRERVGQNRFIEVFVDTPLAICEARDPKGLYKKARAGELRNFTGIDSVYEAPESPEIHLEGQQ 180
Cdd:pfam01583  81 FISPYREDREQARELHEEGKFIEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDSPYEAPENPELVLDTDK 154
 
Name Accession Description Interval E-value
PRK03846 PRK03846
adenylylsulfate kinase; Provisional
 5-201 7.59e-152

adenylylsulfate kinase; Provisional


Pssm-ID: 179661  Cd Length: 198  Bit Score: 418.58  E-value: 7.59e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384611   5 DENVVWHPHPVTVAQREQLHGHRGVVLWFTGLSGSGKSTVAGALEEALHQQGVSTYLLDGDNVRHGLCSDLGFSDEDRKE 84
Cdd:PRK03846   1 DENIVWHQHPVTKAQREQLHGHKGVVLWFTGLSGSGKSTVAGALEEALHELGVSTYLLDGDNVRHGLCSDLGFSDADRKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384611  85 NIRRVGEVASLMADAGLVVLTAFISPHRAERQMVRERVGQNRFIEVFVDTPLAICEARDPKGLYKKARAGELRNFTGIDS 164
Cdd:PRK03846  81 NIRRVGEVAKLMVDAGLVVLTAFISPHRAERQMVRERLGEGEFIEVFVDTPLAICEARDPKGLYKKARAGEIRNFTGIDS 160

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 505384611 165 VYEAPESPEIHLE-GQQLVTNLVSQLLDLLRRDDIIRS 201
Cdd:PRK03846 161 VYEAPESPEIHLDtGEQLVTNLVEQLLDYLRQRDIIRS 198
CysC COG0529
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ...
 13-200 7.87e-126

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: 352.47  E-value: 7.87e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384611  13 HPVTVAQREQLHGHRGVVLWFTGLSGSGKSTVAGALEEALHQQGVSTYLLDGDNVRHGLCSDLGFSDEDRKENIRRVGEV 92
Cdd:COG0529    1 SAVTREERAALKGQKGFVVWFTGLSGSGKSTLANALERRLFERGRHVYLLDGDNVRHGLNKDLGFSKEDRDENIRRIGEV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384611  93 ASLMADAGLVVLTAFISPHRAERQMVRERVGQNRFIEVFVDTPLAICEARDPKGLYKKARAGELRNFTGIDSVYEAPESP 172
Cdd:COG0529   81 AKLLADAGLIVLVAFISPYRADREEARELIGEGEFIEVYVDTPLEVCEARDPKGLYAKARAGEIKNFTGIDDPYEAPENP 160

                        170       180
                 ....*....|....*....|....*....
gi 505384611 173 EIHLEGQQL-VTNLVSQLLDLLRRDDIIR 200
Cdd:COG0529  161 ELVLDTDKEsVEESVEKILAYLEERGYIS 189
apsK TIGR00455
adenylyl-sulfate kinase; This protein, adenylylsulfate kinase, is often found as a fusion ...
 10-193 2.80e-113

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: 320.57  E-value: 2.80e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384611   10 WHPHpVTVAQREQLHGHRGVVLWFTGLSGSGKSTVAGALEEALHQQGVSTYLLDGDNVRHGLCSDLGFSDEDRKENIRRV 89
Cdd:TIGR00455   1 WHPA-ITKDERQALNGHRGVVIWLTGLSGSGKSTIANALEKKLESKGYRVYVLDGDNVRHGLNKDLGFSEEDRKENIRRI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384611   90 GEVASLMADAGLVVLTAFISPHRAERQMVRERVGQNRFIEVFVDTPLAICEARDPKGLYKKARAGELRNFTGIDSVYEAP 169
Cdd:TIGR00455  80 GEVAKLFVRNGIIVITSFISPYRADRQMVRELIEKGEFIEVFVDCPLEVCEQRDPKGLYKKARNGEIKGFTGIDSPYEAP 159

                         170       180
                  ....*....|....*....|....*
gi 505384611  170 ESPEIHLE-GQQLVTNLVSQLLDLL 193
Cdd:TIGR00455 160 ENPEVVLDtDQNDREECVGQIIEKL 184
APSK cd02027
Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5 ...
 30-177 9.36e-104

Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5'-phosphosulfate to form 3'-phosphoadenosine 5'-phosphosulfate (PAPS). The end-product PAPS is a biologically "activated" sulfate form important for the assimilation of inorganic sulfate.


Pssm-ID: 238985 [Multi-domain]  Cd Length: 149  Bit Score: 295.16  E-value: 9.36e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384611  30 VLWFTGLSGSGKSTVAGALEEALHQQGVSTYLLDGDNVRHGLCSDLGFSDEDRKENIRRVGEVASLMADAGLVVLTAFIS 109
Cdd:cd02027    1 VIWLTGLSGSGKSTIARALEEKLFQRGRPVYVLDGDNVRHGLNKDLGFSREDREENIRRIAEVAKLLADAGLIVIAAFIS 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505384611 110 PHRAERQMVRERVGQNRFIEVFVDTPLAICEARDPKGLYKKARAGELRNFTGIDSVYEAPESPEIHLE 177
Cdd:cd02027   81 PYREDREAARKIIGGGDFLEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDDPYEAPENPDLVLD 148
APS_kinase pfam01583
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3 ...
 27-180 3.96e-103

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: 293.84  E-value: 3.96e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384611   27 RGVVLWFTGLSGSGKSTVAGALEEALHQQGVSTYLLDGDNVRHGLCSDLGFSDEDRKENIRRVGEVASLMADAGLVVLTA 106
Cdd:pfam01583   1 RGCTIWLTGLSGAGKSTIANALERKLFEQGRSVYVLDGDNVRHGLNKDLGFSEEDRTENIRRIGEVAKLFADAGLIVITA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505384611  107 FISPHRAERQMVRERVGQNRFIEVFVDTPLAICEARDPKGLYKKARAGELRNFTGIDSVYEAPESPEIHLEGQQ 180
Cdd:pfam01583  81 FISPYREDREQARELHEEGKFIEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDSPYEAPENPELVLDTDK 154
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
 7-199 1.41e-101

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 306.09  E-value: 1.41e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384611   7 NVVWHPHPVTVAQREQLHGHRGVVLWFTGLSGSGKSTVAGALEEALHQQGVSTYLLDGDNVRHGLCSDLGFSDEDRKENI 86
Cdd:PRK05506 439 NVHWQASDVSREARAARKGQKPATVWFTGLSGSGKSTIANLVERRLHALGRHTYLLDGDNVRHGLNRDLGFSDADRVENI 518

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384611  87 RRVGEVASLMADAGLVVLTAFISPHRAERQMVRERVGQNRFIEVFVDTPLAICEARDPKGLYKKARAGELRNFTGIDSVY 166
Cdd:PRK05506 519 RRVAEVARLMADAGLIVLVSFISPFREERELARALHGEGEFVEVFVDTPLEVCEARDPKGLYAKARAGEIKNFTGIDSPY 598

                        170       180       190
                 ....*....|....*....|....*....|....
gi 505384611 167 EAPESPEIHLEGQQL-VTNLVSQLLDLLRRDDII 199
Cdd:PRK05506 599 EAPENPELRLDTTGRsPEELAEQVLELLRRRGAI 632
PRK00889 PRK00889
adenylylsulfate kinase; Provisional
 26-200 4.07e-76

adenylylsulfate kinase; Provisional


Pssm-ID: 179157  Cd Length: 175  Bit Score: 226.06  E-value: 4.07e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384611  26 HRGVVLWFTGLSGSGKSTVAGALEEALHQQGVSTYLLDGDNVRHGLCSDLGFSDEDRKENIRRVGEVASLMADAGLVVLT 105
Cdd:PRK00889   2 QRGVTVWFTGLSGAGKTTIARALAEKLREAGYPVEVLDGDAVRTNLSKGLGFSKEDRDTNIRRIGFVANLLTRHGVIVLV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384611 106 AFISPHRAERQMVRERVGqnRFIEVFVDTPLAICEARDPKGLYKKARAGELRNFTGIDSVYEAPESPEIHLE-GQQLVTN 184
Cdd:PRK00889  82 SAISPYRETREEVRANIG--NFLEVFVDAPLEVCEQRDVKGLYAKARAGEIKHFTGIDDPYEPPLNPEVECRtDLESLEE 159

                        170
                 ....*....|....*.
gi 505384611 185 LVSQLLDLLRRDDIIR 200
Cdd:PRK00889 160 SVDKVLQKLEELGYLV 175
PRK05537 PRK05537
bifunctional sulfate adenylyltransferase/adenylylsulfate kinase;
10-200 9.08e-61

bifunctional sulfate adenylyltransferase/adenylylsulfate kinase;


Pssm-ID: 180124 [Multi-domain]  Cd Length: 568  Bit Score: 198.36  E-value: 9.08e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384611  10 WHPHPVTVAQREQLHGHR---GVVLWFTGLSGSGKSTVAGALEEALHQQ-GVSTYLLDGDNVRHGLCSDLGFSDEDRKEN 85
Cdd:PRK05537 371 WFSFPEVVAELRRTYPPRhkqGFTVFFTGLSGAGKSTIAKALMVKLMEMrGRPVTLLDGDVVRKHLSSELGFSKEDRDLN 450

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384611  86 IRRVGEVASLMADAGLVVLTAFISPHRAERQMVRERVGQ-NRFIEVFVDTPLAICEARDPKGLYKKARAGELRNFTGIDS 164
Cdd:PRK05537 451 ILRIGFVASEITKNGGIAICAPIAPYRATRREVREMIEAyGGFIEVHVATPLEVCEQRDRKGLYAKAREGKIKGFTGISD 530

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 505384611 165 VYEAPESPEIHLEGQQL-VTNLVSQLLDLLRRDDIIR 200
Cdd:PRK05537 531 PYEPPANPELVIDTTNVtPDECAHKILLYLEEKGYLR 567
PRK05541 PRK05541
adenylylsulfate kinase; Provisional
 28-171 6.50e-29

adenylylsulfate kinase; Provisional


Pssm-ID: 235498  Cd Length: 176  Bit Score: 105.91  E-value: 6.50e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384611  28 GVVLWFTGLSGSGKSTVAGALEEALHQQGVSTYLLDGDNVRHGLCSDlGFSDEDRKENIRRVGEVASLMADAGLVVLTAF 107
Cdd:PRK05541   7 GYVIWITGLAGSGKTTIAKALYERLKLKYSNVIYLDGDELREILGHY-GYDKQSRIEMALKRAKLAKFLADQGMIVIVTT 85

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505384611 108 ISphraerqMVRERVGQNR-----FIEVFVDTPLAICEARDPKGLYKKARAGELRNFTGIDSVYEAPES 171
Cdd:PRK05541  86 IS-------MFDEIYAYNRkhlpnYFEVYLKCDMEELIRRDQKGLYTKALKGEIKNVVGVDIPFDEPKA 147
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
30-142 8.07e-10

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


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 55.30  E-value: 8.07e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384611  30 VLWFTGLSGSGKSTVAGALEEALHqqgvsTYLLDGDNVRHGLCSDLGFSDEDRKENIRRV----GEVASLMADAGL-VVL 104
Cdd:COG0645    1 LILVCGLPGSGKSTLARALAERLG-----AVRLRSDVVRKRLFGAGLAPLERSPEATARTyarlLALARELLAAGRsVIL 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 505384611 105 TA-FISphRAERQMVRERVGQN--RFIEVFVDTPLAICEAR 142
Cdd:COG0645   76 DAtFLR--RAQREAFRALAEEAgaPFVLIWLDAPEEVLRER 114
GntK cd02021
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting ...
 34-173 2.06e-09

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: 53.80  E-value: 2.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384611  34 TGLSGSGKSTVAGALEEALHqqgvSTYlLDGDNVRHGLC-----SDLGFSDEDRKENIRRVGE--VASLMADAGLVVLTA 106
Cdd:cd02021    5 MGVSGSGKSTVGKALAERLG----APF-IDGDDLHPPANiakmaAGIPLNDEDRWPWLQALTDalLAKLASAGEGVVVAC 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505384611 107 -FISphRAERQMVRERVGQNRFIEVFVDTPLAICEARDpkglykKARAGELRNFTGIDSVYEAPESPE 173
Cdd:cd02021   80 sALK--RIYRDILRGGAANPRVRFVHLDGPREVLAERL------AARKGHFMPADLLDSQFETLEPPG 139
AAA_33 pfam13671
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ...
 30-142 1.17e-08

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: 51.54  E-value: 1.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384611   30 VLWFTGLSGSGKSTVAGALEEALHqqgvsTYLLDGDNVRHGLCSDLGFSDEDRKENI----RRVGEVASLMADAGL-VVL 104
Cdd:pfam13671   1 LILLVGLPGSGKSTLARRLLEELG-----AVRLSSDDERKRLFGEGRPSISYYTDATdrtyERLHELARIALRAGRpVIL 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 505384611  105 TA-FISP-HRAERQMVRERVGQNRFIeVFVDTPLAICEAR 142
Cdd:pfam13671  76 DAtNLRRdERARLLALAREYGVPVRI-VVFEAPEEVLRER 114
GntK COG3265
Gluconate kinase [Carbohydrate transport and metabolism]; Gluconate kinase is part of the ...
 35-194 1.79e-05

Gluconate kinase [Carbohydrate transport and metabolism]; Gluconate kinase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 442496 [Multi-domain]  Cd Length: 164  Bit Score: 43.19  E-value: 1.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384611  35 GLSGSGKSTVAGALEEALHqqgvsTYLLDGD------NV---RHGlcsdLGFSDEDRKENIRRVGEVASLMADAGLVVLT 105
Cdd:COG3265    8 GVSGSGKSTVGQALAERLG-----WPFIDGDdfhppaNIakmAAG----IPLTDEDRAPWLEALADAIAAHLAAGEGAVL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384611 106 AFISPHRAERQMVRERVGQNRFieVFVDTPLAICEARdpkgLykKARAGELRNFTGIDS---VYEAPESPE--IHLEGQQ 180
Cdd:COG3265   79 ACSALKRSYRDRLREGNPDVRF--VYLDGSRELIAER----L--AARKGHFMPASLLDSqfaTLEPPGPDEdaIVVDIDQ 150

                        170
                 ....*....|....
gi 505384611 181 LVTNLVSQLLDLLR 194
Cdd:COG3265  151 PPEEIVAQILAALG 164
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 35-135 8.49e-05

Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440255 [Multi-domain]  Cd Length: 289  Bit Score: 42.10  E-value: 8.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384611  35 GLSGSGKSTVAGALEEALHQQGVSTYLLDGDNVRHGLCSDLGFSDE----DRKENIRRVGEVASLMADAGLVVLTA-FIS 109
Cdd:COG0489  100 GKGGEGKSTVAANLALALAQSGKRVLLIDADLRGPSLHRMLGLENRpglsDVLAGEASLEDVIQPTEVEGLDVLPAgPLP 179

                         90       100       110
                 ....*....|....*....|....*....|....
gi 505384611 110 PHRAERqMVRERVGQnrFIE--------VFVDTP 135
Cdd:COG0489  180 PNPSEL-LASKRLKQ--LLEelrgrydyVIIDTP 210
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 33-106 3.68e-04

SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal recognition particle, MinD, and BioD), consists of signal recognition particle (SRP) GTPases, the assemblage of MinD-like ATPases, which are involved in protein localization, chromosome partitioning, and membrane transport, and a group of metabolic enzymes with kinase or related phosphate transferase activity. Functionally, proteins in this superfamily use the energy from hydrolysis of NTP to transfer electron or ion.


Pssm-ID: 349751 [Multi-domain]  Cd Length: 107  Bit Score: 38.57  E-value: 3.68e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505384611  33 FTG-LSGSGKSTVAGALEEALHQQGVSTYLLDGDNVrhgLCSDLGFSDEDRKENIRRVGEVASLMADAGLVVLTA 106
Cdd:cd01983    5 VTGgKGGVGKTTLAAALAVALAAKGYKVLLIDLDDY---VLIDGGGGLETGLLLGTIVALLALKKADEVIVVVDP 76
COG4639 COG4639
Predicted kinase [General function prediction only];
35-143 6.26e-04

Predicted kinase [General function prediction only];


Pssm-ID: 443677 [Multi-domain]  Cd Length: 145  Bit Score: 38.66  E-value: 6.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384611  35 GLSGSGKSTVAGALEEAlhqqgvsTYLLDGDNVRHGLcsdlgFSDEDRKENIRRVGEVASLMADAGL-----VVL--TAF 107
Cdd:COG4639    9 GLPGSGKSTFARRLFAP-------TEVVSSDDIRALL-----GGDENDQSAWGDVFQLAHEIARARLragrlTVVdaTNL 76

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 505384611 108 ISPHRAE-RQMVRERvgQNRFIEVFVDTPLAICEARD 143
Cdd:COG4639   77 QREARRRlLALARAY--GALVVAVVLDVPLEVCLARN 111
ExeA COG3267
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ...
 23-104 9.40e-04

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: 39.00  E-value: 9.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384611  23 LHGHRGVVLwFTGLSGSGKSTVAGALEEALHQQGVSTYL----LDGDNVRHGLCSDLG--FSDEDRKENIRRVGEVASLM 96
Cdd:COG3267   39 LAQGGGFVV-LTGEVGTGKTTLLRRLLERLPDDVKVAYIpnpqLSPAELLRAIADELGlePKGASKADLLRQLQEFLLEL 117


                 ....*...
gi 505384611  97 ADAGLVVL 104
Cdd:COG3267  118 AAAGRRVV 125
AAA_22 pfam13401
AAA domain;
23-104 1.43e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 37.32  E-value: 1.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384611   23 LHGHRGVVLwFTGLSGSGKSTVAGALEEALHQQGVSTYLLD------GDNVRHGLCSDLG---FSDEDRKENIRRVGEVA 93
Cdd:pfam13401   1 IRFGAGILV-LTGESGTGKTTLLRRLLEQLPEVRDSVVFVDlpsgtsPKDLLRALLRALGlplSGRLSKEELLAALQQLL 79

                          90
                  ....*....|.
gi 505384611   94 SLMADAGLVVL 104
Cdd:pfam13401  80 LALAVAVVLII 90
AAA_18 pfam13238
AAA domain;
32-116 1.70e-03

AAA domain;


Pssm-ID: 433052 [Multi-domain]  Cd Length: 128  Bit Score: 37.02  E-value: 1.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384611   32 WFTGLSGSGKSTVAGALEEALHqqgvsTYLLDGDNVRHGLC--SDLGFSDEDRKENIRRVGEV------ASLMADAGLVV 103
Cdd:pfam13238   2 LITGTPGVGKTTLAKELSKRLG-----FGDNVRDLALENGLvlGDDPETRESKRLDEDKLDRLldlleeNAALEEGGNLI 76

                          90
                  ....*....|...
gi 505384611  104 LTAFISPHRAERQ 116
Cdd:pfam13238  77 IDGHLAELEPERA 89
PRK07667 PRK07667
uridine kinase; Provisional
 24-66 2.36e-03

uridine kinase; Provisional


Pssm-ID: 169051  Cd Length: 193  Bit Score: 37.40  E-value: 2.36e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 505384611  24 HGHRGVVLWFTGLSGSGKSTVAGALEEALHQQGVSTYLLDGDN 66
Cdd:PRK07667  13 HKENRFILGIDGLSRSGKTTFVANLKENMKQEGIPFHIFHIDD 55
 
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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