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Conserved domains on  [gi|489004547|ref|WP_002915158|]
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MULTISPECIES: adenylyl-sulfate kinase [Klebsiella]

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 1.78e-152

adenylylsulfate kinase; Provisional


:

Pssm-ID: 179661  Cd Length: 198  Bit Score: 420.12  E-value: 1.78e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004547   5 DENVVWHAHPVTQQQREQHHGHRGVVLWFTGLSGSGKSTVAGALEEALHERGVSTYLLDGDNVRHGLCSDLGFSDEDRKE 84
Cdd:PRK03846   1 DENIVWHQHPVTKAQREQLHGHKGVVLWFTGLSGSGKSTVAGALEEALHELGVSTYLLDGDNVRHGLCSDLGFSDADRKE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004547  85 NIRRVGEVARLMVDAGLVVLTAFISPHRAERQMVRERLGEGRFIEVFVDTPLAICEARDPKGLYKKARAGELRNFTGIDS 164
Cdd:PRK03846  81 NIRRVGEVAKLMVDAGLVVLTAFISPHRAERQMVRERLGEGEFIEVFVDTPLAICEARDPKGLYKKARAGEIRNFTGIDS 160
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 489004547 165 VYEAPEKAEIHLD-GEQLVTNLVHQLLDLLQQSDIIRS 201
Cdd:PRK03846 161 VYEAPESPEIHLDtGEQLVTNLVEQLLDYLRQRDIIRS 198
 
Name Accession Description Interval E-value
PRK03846 PRK03846
adenylylsulfate kinase; Provisional
5-201 1.78e-152

adenylylsulfate kinase; Provisional


Pssm-ID: 179661  Cd Length: 198  Bit Score: 420.12  E-value: 1.78e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004547   5 DENVVWHAHPVTQQQREQHHGHRGVVLWFTGLSGSGKSTVAGALEEALHERGVSTYLLDGDNVRHGLCSDLGFSDEDRKE 84
Cdd:PRK03846   1 DENIVWHQHPVTKAQREQLHGHKGVVLWFTGLSGSGKSTVAGALEEALHELGVSTYLLDGDNVRHGLCSDLGFSDADRKE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004547  85 NIRRVGEVARLMVDAGLVVLTAFISPHRAERQMVRERLGEGRFIEVFVDTPLAICEARDPKGLYKKARAGELRNFTGIDS 164
Cdd:PRK03846  81 NIRRVGEVAKLMVDAGLVVLTAFISPHRAERQMVRERLGEGEFIEVFVDTPLAICEARDPKGLYKKARAGEIRNFTGIDS 160
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 489004547 165 VYEAPEKAEIHLD-GEQLVTNLVHQLLDLLQQSDIIRS 201
Cdd:PRK03846 161 VYEAPESPEIHLDtGEQLVTNLVEQLLDYLRQRDIIRS 198
CysC COG0529
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ...
13-200 4.07e-127

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: 355.55  E-value: 4.07e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004547  13 HPVTQQQREQHHGHRGVVLWFTGLSGSGKSTVAGALEEALHERGVSTYLLDGDNVRHGLCSDLGFSDEDRKENIRRVGEV 92
Cdd:COG0529    1 SAVTREERAALKGQKGFVVWFTGLSGSGKSTLANALERRLFERGRHVYLLDGDNVRHGLNKDLGFSKEDRDENIRRIGEV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004547  93 ARLMVDAGLVVLTAFISPHRAERQMVRERLGEGRFIEVFVDTPLAICEARDPKGLYKKARAGELRNFTGIDSVYEAPEKA 172
Cdd:COG0529   81 AKLLADAGLIVLVAFISPYRADREEARELIGEGEFIEVYVDTPLEVCEARDPKGLYAKARAGEIKNFTGIDDPYEAPENP 160
                        170       180
                 ....*....|....*....|....*....
gi 489004547 173 EIHLDGEQL-VTNLVHQLLDLLQQSDIIR 200
Cdd:COG0529  161 ELVLDTDKEsVEESVEKILAYLEERGYIS 189
apsK TIGR00455
adenylyl-sulfate kinase; This protein, adenylylsulfate kinase, is often found as a fusion ...
10-193 2.59e-111

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: 315.56  E-value: 2.59e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004547   10 WHAHpVTQQQREQHHGHRGVVLWFTGLSGSGKSTVAGALEEALHERGVSTYLLDGDNVRHGLCSDLGFSDEDRKENIRRV 89
Cdd:TIGR00455   1 WHPA-ITKDERQALNGHRGVVIWLTGLSGSGKSTIANALEKKLESKGYRVYVLDGDNVRHGLNKDLGFSEEDRKENIRRI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004547   90 GEVARLMVDAGLVVLTAFISPHRAERQMVRERLGEGRFIEVFVDTPLAICEARDPKGLYKKARAGELRNFTGIDSVYEAP 169
Cdd:TIGR00455  80 GEVAKLFVRNGIIVITSFISPYRADRQMVRELIEKGEFIEVFVDCPLEVCEQRDPKGLYKKARNGEIKGFTGIDSPYEAP 159
                         170       180
                  ....*....|....*....|....*
gi 489004547  170 EKAEIHLD-GEQLVTNLVHQLLDLL 193
Cdd:TIGR00455 160 ENPEVVLDtDQNDREECVGQIIEKL 184
APSK cd02027
Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5 ...
30-177 3.53e-105

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: 298.62  E-value: 3.53e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004547  30 VLWFTGLSGSGKSTVAGALEEALHERGVSTYLLDGDNVRHGLCSDLGFSDEDRKENIRRVGEVARLMVDAGLVVLTAFIS 109
Cdd:cd02027    1 VIWLTGLSGSGKSTIARALEEKLFQRGRPVYVLDGDNVRHGLNKDLGFSREDREENIRRIAEVAKLLADAGLIVIAAFIS 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489004547 110 PHRAERQMVRERLGEGRFIEVFVDTPLAICEARDPKGLYKKARAGELRNFTGIDSVYEAPEKAEIHLD 177
Cdd:cd02027   81 PYREDREAARKIIGGGDFLEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDDPYEAPENPDLVLD 148
APS_kinase pfam01583
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3 ...
27-177 2.12e-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: 294.61  E-value: 2.12e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004547   27 RGVVLWFTGLSGSGKSTVAGALEEALHERGVSTYLLDGDNVRHGLCSDLGFSDEDRKENIRRVGEVARLMVDAGLVVLTA 106
Cdd:pfam01583   1 RGCTIWLTGLSGAGKSTIANALERKLFEQGRSVYVLDGDNVRHGLNKDLGFSEEDRTENIRRIGEVAKLFADAGLIVITA 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489004547  107 FISPHRAERQMVRERLGEGRFIEVFVDTPLAICEARDPKGLYKKARAGELRNFTGIDSVYEAPEKAEIHLD 177
Cdd:pfam01583  81 FISPYREDREQARELHEEGKFIEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDSPYEAPENPELVLD 151
 
Name Accession Description Interval E-value
PRK03846 PRK03846
adenylylsulfate kinase; Provisional
5-201 1.78e-152

adenylylsulfate kinase; Provisional


Pssm-ID: 179661  Cd Length: 198  Bit Score: 420.12  E-value: 1.78e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004547   5 DENVVWHAHPVTQQQREQHHGHRGVVLWFTGLSGSGKSTVAGALEEALHERGVSTYLLDGDNVRHGLCSDLGFSDEDRKE 84
Cdd:PRK03846   1 DENIVWHQHPVTKAQREQLHGHKGVVLWFTGLSGSGKSTVAGALEEALHELGVSTYLLDGDNVRHGLCSDLGFSDADRKE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004547  85 NIRRVGEVARLMVDAGLVVLTAFISPHRAERQMVRERLGEGRFIEVFVDTPLAICEARDPKGLYKKARAGELRNFTGIDS 164
Cdd:PRK03846  81 NIRRVGEVAKLMVDAGLVVLTAFISPHRAERQMVRERLGEGEFIEVFVDTPLAICEARDPKGLYKKARAGEIRNFTGIDS 160
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 489004547 165 VYEAPEKAEIHLD-GEQLVTNLVHQLLDLLQQSDIIRS 201
Cdd:PRK03846 161 VYEAPESPEIHLDtGEQLVTNLVEQLLDYLRQRDIIRS 198
CysC COG0529
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ...
13-200 4.07e-127

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: 355.55  E-value: 4.07e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004547  13 HPVTQQQREQHHGHRGVVLWFTGLSGSGKSTVAGALEEALHERGVSTYLLDGDNVRHGLCSDLGFSDEDRKENIRRVGEV 92
Cdd:COG0529    1 SAVTREERAALKGQKGFVVWFTGLSGSGKSTLANALERRLFERGRHVYLLDGDNVRHGLNKDLGFSKEDRDENIRRIGEV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004547  93 ARLMVDAGLVVLTAFISPHRAERQMVRERLGEGRFIEVFVDTPLAICEARDPKGLYKKARAGELRNFTGIDSVYEAPEKA 172
Cdd:COG0529   81 AKLLADAGLIVLVAFISPYRADREEARELIGEGEFIEVYVDTPLEVCEARDPKGLYAKARAGEIKNFTGIDDPYEAPENP 160
                        170       180
                 ....*....|....*....|....*....
gi 489004547 173 EIHLDGEQL-VTNLVHQLLDLLQQSDIIR 200
Cdd:COG0529  161 ELVLDTDKEsVEESVEKILAYLEERGYIS 189
apsK TIGR00455
adenylyl-sulfate kinase; This protein, adenylylsulfate kinase, is often found as a fusion ...
10-193 2.59e-111

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: 315.56  E-value: 2.59e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004547   10 WHAHpVTQQQREQHHGHRGVVLWFTGLSGSGKSTVAGALEEALHERGVSTYLLDGDNVRHGLCSDLGFSDEDRKENIRRV 89
Cdd:TIGR00455   1 WHPA-ITKDERQALNGHRGVVIWLTGLSGSGKSTIANALEKKLESKGYRVYVLDGDNVRHGLNKDLGFSEEDRKENIRRI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004547   90 GEVARLMVDAGLVVLTAFISPHRAERQMVRERLGEGRFIEVFVDTPLAICEARDPKGLYKKARAGELRNFTGIDSVYEAP 169
Cdd:TIGR00455  80 GEVAKLFVRNGIIVITSFISPYRADRQMVRELIEKGEFIEVFVDCPLEVCEQRDPKGLYKKARNGEIKGFTGIDSPYEAP 159
                         170       180
                  ....*....|....*....|....*
gi 489004547  170 EKAEIHLD-GEQLVTNLVHQLLDLL 193
Cdd:TIGR00455 160 ENPEVVLDtDQNDREECVGQIIEKL 184
APSK cd02027
Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5 ...
30-177 3.53e-105

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: 298.62  E-value: 3.53e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004547  30 VLWFTGLSGSGKSTVAGALEEALHERGVSTYLLDGDNVRHGLCSDLGFSDEDRKENIRRVGEVARLMVDAGLVVLTAFIS 109
Cdd:cd02027    1 VIWLTGLSGSGKSTIARALEEKLFQRGRPVYVLDGDNVRHGLNKDLGFSREDREENIRRIAEVAKLLADAGLIVIAAFIS 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489004547 110 PHRAERQMVRERLGEGRFIEVFVDTPLAICEARDPKGLYKKARAGELRNFTGIDSVYEAPEKAEIHLD 177
Cdd:cd02027   81 PYREDREAARKIIGGGDFLEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDDPYEAPENPDLVLD 148
APS_kinase pfam01583
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3 ...
27-177 2.12e-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: 294.61  E-value: 2.12e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004547   27 RGVVLWFTGLSGSGKSTVAGALEEALHERGVSTYLLDGDNVRHGLCSDLGFSDEDRKENIRRVGEVARLMVDAGLVVLTA 106
Cdd:pfam01583   1 RGCTIWLTGLSGAGKSTIANALERKLFEQGRSVYVLDGDNVRHGLNKDLGFSEEDRTENIRRIGEVAKLFADAGLIVITA 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489004547  107 FISPHRAERQMVRERLGEGRFIEVFVDTPLAICEARDPKGLYKKARAGELRNFTGIDSVYEAPEKAEIHLD 177
Cdd:pfam01583  81 FISPYREDREQARELHEEGKFIEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDSPYEAPENPELVLD 151
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
3-199 4.01e-103

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 309.94  E-value: 4.01e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004547   3 QHDENVVWHAHPVTQQQREQHHGHRGVVLWFTGLSGSGKSTVAGALEEALHERGVSTYLLDGDNVRHGLCSDLGFSDEDR 82
Cdd:PRK05506 435 RRATNVHWQASDVSREARAARKGQKPATVWFTGLSGSGKSTIANLVERRLHALGRHTYLLDGDNVRHGLNRDLGFSDADR 514
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004547  83 KENIRRVGEVARLMVDAGLVVLTAFISPHRAERQMVRERLGEGRFIEVFVDTPLAICEARDPKGLYKKARAGELRNFTGI 162
Cdd:PRK05506 515 VENIRRVAEVARLMADAGLIVLVSFISPFREERELARALHGEGEFVEVFVDTPLEVCEARDPKGLYAKARAGEIKNFTGI 594
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 489004547 163 DSVYEAPEKAEIHLDGEQL-VTNLVHQLLDLLQQSDII 199
Cdd:PRK05506 595 DSPYEAPENPELRLDTTGRsPEELAEQVLELLRRRGAI 632
PRK00889 PRK00889
adenylylsulfate kinase; Provisional
26-192 2.51e-74

adenylylsulfate kinase; Provisional


Pssm-ID: 179157  Cd Length: 175  Bit Score: 221.82  E-value: 2.51e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004547  26 HRGVVLWFTGLSGSGKSTVAGALEEALHERGVSTYLLDGDNVRHGLCSDLGFSDEDRKENIRRVGEVARLMVDAGLVVLT 105
Cdd:PRK00889   2 QRGVTVWFTGLSGAGKTTIARALAEKLREAGYPVEVLDGDAVRTNLSKGLGFSKEDRDTNIRRIGFVANLLTRHGVIVLV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004547 106 AFISPHRAERQMVRERLgeGRFIEVFVDTPLAICEARDPKGLYKKARAGELRNFTGIDSVYEAPEKAEIHL--DGEQL-- 181
Cdd:PRK00889  82 SAISPYRETREEVRANI--GNFLEVFVDAPLEVCEQRDVKGLYAKARAGEIKHFTGIDDPYEPPLNPEVECrtDLESLee 159
                        170
                 ....*....|..
gi 489004547 182 -VTNLVHQLLDL 192
Cdd:PRK00889 160 sVDKVLQKLEEL 171
PRK05537 PRK05537
bifunctional sulfate adenylyltransferase/adenylylsulfate kinase;
10-200 1.02e-62

bifunctional sulfate adenylyltransferase/adenylylsulfate kinase;


Pssm-ID: 180124 [Multi-domain]  Cd Length: 568  Bit Score: 203.75  E-value: 1.02e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004547  10 WHAHP-VTQQQREQH---HGhRGVVLWFTGLSGSGKSTVAGALEEALHE-RGVSTYLLDGDNVRHGLCSDLGFSDEDRKE 84
Cdd:PRK05537 371 WFSFPeVVAELRRTYpprHK-QGFTVFFTGLSGAGKSTIAKALMVKLMEmRGRPVTLLDGDVVRKHLSSELGFSKEDRDL 449
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004547  85 NIRRVGEVARLMVDAGLVVLTAFISPHRAERQMVRERLGE-GRFIEVFVDTPLAICEARDPKGLYKKARAGELRNFTGID 163
Cdd:PRK05537 450 NILRIGFVASEITKNGGIAICAPIAPYRATRREVREMIEAyGGFIEVHVATPLEVCEQRDRKGLYAKAREGKIKGFTGIS 529
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 489004547 164 SVYEAPEKAEIHLDGEQL-VTNLVHQLLDLLQQSDIIR 200
Cdd:PRK05537 530 DPYEPPANPELVIDTTNVtPDECAHKILLYLEEKGYLR 567
PRK05541 PRK05541
adenylylsulfate kinase; Provisional
28-195 1.79e-29

adenylylsulfate kinase; Provisional


Pssm-ID: 235498  Cd Length: 176  Bit Score: 107.45  E-value: 1.79e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004547  28 GVVLWFTGLSGSGKSTVAGALEEALHERGVSTYLLDGDNVRHGLCSDlGFSDEDRKENIRRVGEVARLMVDAGLVVLTAF 107
Cdd:PRK05541   7 GYVIWITGLAGSGKTTIAKALYERLKLKYSNVIYLDGDELREILGHY-GYDKQSRIEMALKRAKLAKFLADQGMIVIVTT 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004547 108 ISPHRAERQMVRERLgeGRFIEVFVDTPLAICEARDPKGLYKKARAGELRNFTGIDSVYEAPeKAEIHLDGEqLVTNLVH 187
Cdd:PRK05541  86 ISMFDEIYAYNRKHL--PNYFEVYLKCDMEELIRRDQKGLYTKALKGEIKNVVGVDIPFDEP-KADLVIDNS-CRTSLDE 161

                 ....*...
gi 489004547 188 QLLDLLQQ 195
Cdd:PRK05541 162 KVDLILNK 169
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
30-142 1.54e-10

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


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 57.23  E-value: 1.54e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004547  30 VLWFTGLSGSGKSTVAGALEEALheRGVstyLLDGDNVRHGLCSDLGFSDEDRKENIRRV----GEVARLMVDAGL-VVL 104
Cdd:COG0645    1 LILVCGLPGSGKSTLARALAERL--GAV---RLRSDVVRKRLFGAGLAPLERSPEATARTyarlLALARELLAAGRsVIL 75
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 489004547 105 TA-FISphRAERQMVRERLGE--GRFIEVFVDTPLAICEAR 142
Cdd:COG0645   76 DAtFLR--RAQREAFRALAEEagAPFVLIWLDAPEEVLRER 114
GntK cd02021
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting ...
34-170 7.63e-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: 52.25  E-value: 7.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004547  34 TGLSGSGKSTVAGALEEALHergvSTYlLDGDNVRHGLC-----SDLGFSDEDRKENIRRVGE--VARLMVDAGLVVLTA 106
Cdd:cd02021    5 MGVSGSGKSTVGKALAERLG----APF-IDGDDLHPPANiakmaAGIPLNDEDRWPWLQALTDalLAKLASAGEGVVVAC 79
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489004547 107 -FISphRAERQMVRERLGEGRFIEVFVDTPLAICEARDpkglykKARAGELRNFTGIDSVYEAPE 170
Cdd:cd02021   80 sALK--RIYRDILRGGAANPRVRFVHLDGPREVLAERL------AARKGHFMPADLLDSQFETLE 136
AAA_33 pfam13671
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ...
30-142 9.74e-09

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: 51.93  E-value: 9.74e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004547   30 VLWFTGLSGSGKSTVAGALEEALHergvsTYLLDGDNVRHGLCSDLGFSDEDRKENI----RRVGEVARLMVDAGL-VVL 104
Cdd:pfam13671   1 LILLVGLPGSGKSTLARRLLEELG-----AVRLSSDDERKRLFGEGRPSISYYTDATdrtyERLHELARIALRAGRpVIL 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 489004547  105 TA-FISP-HRAERQMVRERLGEgRFIEVFVDTPLAICEAR 142
Cdd:pfam13671  76 DAtNLRRdERARLLALAREYGV-PVRIVVFEAPEEVLRER 114
GntK COG3265
Gluconate kinase [Carbohydrate transport and metabolism]; Gluconate kinase is part of the ...
35-194 4.50e-06

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: 44.73  E-value: 4.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004547  35 GLSGSGKSTVAGALEEALHergvsTYLLDGD------NV---RHGlcsdLGFSDEDRKENIRRVGEVARLMVDAGLVVLT 105
Cdd:COG3265    8 GVSGSGKSTVGQALAERLG-----WPFIDGDdfhppaNIakmAAG----IPLTDEDRAPWLEALADAIAAHLAAGEGAVL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004547 106 AFISPHRAERQMVRERLGEGRFieVFVDTPLAICEARdpkgLykKARAGELRNFTGIDS---VYEAPEKAE--IHLDGEQ 180
Cdd:COG3265   79 ACSALKRSYRDRLREGNPDVRF--VYLDGSRELIAER----L--AARKGHFMPASLLDSqfaTLEPPGPDEdaIVVDIDQ 150
                        170
                 ....*....|....
gi 489004547 181 LVTNLVHQLLDLLQ 194
Cdd:COG3265  151 PPEEIVAQILAALG 164
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
35-135 1.75e-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: 44.02  E-value: 1.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004547  35 GLSGSGKSTVAGALEEALHERGVSTYLLDGDNVRHGLCSDLGFSDE----DRKENIRRVGEVARLMVDAGLVVLTA-FIS 109
Cdd:COG0489  100 GKGGEGKSTVAANLALALAQSGKRVLLIDADLRGPSLHRMLGLENRpglsDVLAGEASLEDVIQPTEVEGLDVLPAgPLP 179
                         90       100       110
                 ....*....|....*....|....*....|....
gi 489004547 110 PHRAERqMVRERLGEgrFIE--------VFVDTP 135
Cdd:COG0489  180 PNPSEL-LASKRLKQ--LLEelrgrydyVIIDTP 210
COG4639 COG4639
Predicted kinase [General function prediction only];
35-143 1.63e-04

Predicted kinase [General function prediction only];


Pssm-ID: 443677 [Multi-domain]  Cd Length: 145  Bit Score: 40.20  E-value: 1.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004547  35 GLSGSGKSTVAGALEEAlhergvsTYLLDGDNVRHGLcsdlgFSDEDRKENIRRVGEVARLMVDAGL-----VVLTAfIS 109
Cdd:COG4639    9 GLPGSGKSTFARRLFAP-------TEVVSSDDIRALL-----GGDENDQSAWGDVFQLAHEIARARLragrlTVVDA-TN 75
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 489004547 110 PHRAERQMVRERLGE--GRFIEVFVDTPLAICEARD 143
Cdd:COG4639   76 LQREARRRLLALARAygALVVAVVLDVPLEVCLARN 111
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
33-106 4.53e-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: 38.18  E-value: 4.53e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489004547  33 FTG-LSGSGKSTVAGALEEALHERGVSTYLLDGDNVrhgLCSDLGFSDEDRKENIRRVGEVARLMVDAGLVVLTA 106
Cdd:cd01983    5 VTGgKGGVGKTTLAAALAVALAAKGYKVLLIDLDDY---VLIDGGGGLETGLLLGTIVALLALKKADEVIVVVDP 76
AAA_22 pfam13401
AAA domain;
23-104 1.52e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 37.32  E-value: 1.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004547   23 HHGHRGVVLwFTGLSGSGKSTVAGALEEALHERGVSTYLLD------GDNVRHGLCSDLGFSDEDRKENIRRVGEVARLM 96
Cdd:pfam13401   1 IRFGAGILV-LTGESGTGKTTLLRRLLEQLPEVRDSVVFVDlpsgtsPKDLLRALLRALGLPLSGRLSKEELLAALQQLL 79

                  ....*...
gi 489004547   97 VDAGLVVL 104
Cdd:pfam13401  80 LALAVAVV 87
AAA_18 pfam13238
AAA domain;
32-116 2.01e-03

AAA domain;


Pssm-ID: 433052 [Multi-domain]  Cd Length: 128  Bit Score: 37.02  E-value: 2.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004547   32 WFTGLSGSGKSTVAGALEEALHERGVStylldGDNVRHGLC--SDLGFSDEDRKENIRRVGEVARL------MVDAGLVV 103
Cdd:pfam13238   2 LITGTPGVGKTTLAKELSKRLGFGDNV-----RDLALENGLvlGDDPETRESKRLDEDKLDRLLDLleenaaLEEGGNLI 76
                          90
                  ....*....|...
gi 489004547  104 LTAFISPHRAERQ 116
Cdd:pfam13238  77 IDGHLAELEPERA 89
KTI12 pfam08433
Chromatin associated protein KTI12; This is a family of chromatin associated proteins which ...
33-69 2.81e-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: 37.66  E-value: 2.81e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 489004547   33 FTGLSGSGKSTVAGALEEALHERGVSTYLLDGDNVRH 69
Cdd:pfam08433   4 LTGLPSSGKSTRAKQLAKYLEESNYDVIVISDESLGI 40
ExeA COG3267
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ...
26-82 3.06e-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: 37.46  E-value: 3.06e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489004547  26 HRGVVLwFTGLSGSGKSTVAGALEEALHERGVSTYL----LDGDNVRHGLCSDLGFSDEDR 82
Cdd:COG3267   42 GGGFVV-LTGEVGTGKTTLLRRLLERLPDDVKVAYIpnpqLSPAELLRAIADELGLEPKGA 101
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
38-135 6.09e-03

ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein BcsQ [Cell cycle control, cell division, chromosome partitioning, Cell motility];


Pssm-ID: 440805 [Multi-domain]  Cd Length: 253  Bit Score: 36.37  E-value: 6.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004547  38 GSGKSTVAGALEEALHERGVSTYLLDGD---NVRHGlcsdLGFSDEDRKENI-------RRVGEVARLMVDAGLVVLTAF 107
Cdd:COG1192   12 GVGKTTTAVNLAAALARRGKRVLLIDLDpqgNLTSG----LGLDPDDLDPTLydlllddAPLEDAIVPTEIPGLDLIPAN 87
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 489004547 108 ISPHRAERQMVRERLGEGRFIE-----------VFVDTP 135
Cdd:COG1192   88 IDLAGAEIELVSRPGRELRLKRalapladdydyILIDCP 126
PRK07667 PRK07667
uridine kinase; Provisional
24-66 9.48e-03

uridine kinase; Provisional


Pssm-ID: 169051  Cd Length: 193  Bit Score: 35.48  E-value: 9.48e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 489004547  24 HGHRGVVLWFTGLSGSGKSTVAGALEEALHERGVSTYLLDGDN 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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