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Conserved domains on  [gi|505182879|ref|WP_015369981|]
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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 7.11e-152

adenylylsulfate kinase; Provisional


:

Pssm-ID: 179661  Cd Length: 198  Bit Score: 418.58  E-value: 7.11e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505182879   5 DENVVWHAHPVTREQREQHHGHRGVVLWFTGLSGSGKSTVAGALEEALHELGVSTYLLDGDNVRHGLCSDLGFSDDDRKE 84
Cdd:PRK03846   1 DENIVWHQHPVTKAQREQLHGHKGVVLWFTGLSGSGKSTVAGALEEALHELGVSTYLLDGDNVRHGLCSDLGFSDADRKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505182879  85 NIRRVGEVAKLMVDAGLVVLTAFISPHRAERQMVRERLGEGRFIEVFVDTPLAICETRDPKGLYKKARAGELRNFTGIDS 164
Cdd:PRK03846  81 NIRRVGEVAKLMVDAGLVVLTAFISPHRAERQMVRERLGEGEFIEVFVDTPLAICEARDPKGLYKKARAGEIRNFTGIDS 160

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 505182879 165 VYESPENAEIHLD-GEQLVTNLVHQLLDLLRQSDIIRS 201
Cdd:PRK03846 161 VYEAPESPEIHLDtGEQLVTNLVEQLLDYLRQRDIIRS 198
 
Name Accession Description Interval E-value
PRK03846 PRK03846
adenylylsulfate kinase; Provisional
 5-201 7.11e-152

adenylylsulfate kinase; Provisional


Pssm-ID: 179661  Cd Length: 198  Bit Score: 418.58  E-value: 7.11e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505182879   5 DENVVWHAHPVTREQREQHHGHRGVVLWFTGLSGSGKSTVAGALEEALHELGVSTYLLDGDNVRHGLCSDLGFSDDDRKE 84
Cdd:PRK03846   1 DENIVWHQHPVTKAQREQLHGHKGVVLWFTGLSGSGKSTVAGALEEALHELGVSTYLLDGDNVRHGLCSDLGFSDADRKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505182879  85 NIRRVGEVAKLMVDAGLVVLTAFISPHRAERQMVRERLGEGRFIEVFVDTPLAICETRDPKGLYKKARAGELRNFTGIDS 164
Cdd:PRK03846  81 NIRRVGEVAKLMVDAGLVVLTAFISPHRAERQMVRERLGEGEFIEVFVDTPLAICEARDPKGLYKKARAGEIRNFTGIDS 160

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 505182879 165 VYESPENAEIHLD-GEQLVTNLVHQLLDLLRQSDIIRS 201
Cdd:PRK03846 161 VYEAPESPEIHLDtGEQLVTNLVEQLLDYLRQRDIIRS 198
CysC COG0529
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ...
 13-200 8.88e-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: 352.08  E-value: 8.88e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505182879  13 HPVTREQREQHHGHRGVVLWFTGLSGSGKSTVAGALEEALHELGVSTYLLDGDNVRHGLCSDLGFSDDDRKENIRRVGEV 92
Cdd:COG0529    1 SAVTREERAALKGQKGFVVWFTGLSGSGKSTLANALERRLFERGRHVYLLDGDNVRHGLNKDLGFSKEDRDENIRRIGEV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505182879  93 AKLMVDAGLVVLTAFISPHRAERQMVRERLGEGRFIEVFVDTPLAICETRDPKGLYKKARAGELRNFTGIDSVYESPENA 172
Cdd:COG0529   81 AKLLADAGLIVLVAFISPYRADREEARELIGEGEFIEVYVDTPLEVCEARDPKGLYAKARAGEIKNFTGIDDPYEAPENP 160

                        170       180
                 ....*....|....*....|....*....
gi 505182879 173 EIHLDGEQL-VTNLVHQLLDLLRQSDIIR 200
Cdd:COG0529  161 ELVLDTDKEsVEESVEKILAYLEERGYIS 189
apsK TIGR00455
adenylyl-sulfate kinase; This protein, adenylylsulfate kinase, is often found as a fusion ...
 10-193 1.80e-110

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: 313.64  E-value: 1.80e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505182879   10 WHAHpVTREQREQHHGHRGVVLWFTGLSGSGKSTVAGALEEALHELGVSTYLLDGDNVRHGLCSDLGFSDDDRKENIRRV 89
Cdd:TIGR00455   1 WHPA-ITKDERQALNGHRGVVIWLTGLSGSGKSTIANALEKKLESKGYRVYVLDGDNVRHGLNKDLGFSEEDRKENIRRI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505182879   90 GEVAKLMVDAGLVVLTAFISPHRAERQMVRERLGEGRFIEVFVDTPLAICETRDPKGLYKKARAGELRNFTGIDSVYESP 169
Cdd:TIGR00455  80 GEVAKLFVRNGIIVITSFISPYRADRQMVRELIEKGEFIEVFVDCPLEVCEQRDPKGLYKKARNGEIKGFTGIDSPYEAP 159

                         170       180
                  ....*....|....*....|....*
gi 505182879  170 ENAEIHLD-GEQLVTNLVHQLLDLL 193
Cdd:TIGR00455 160 ENPEVVLDtDQNDREECVGQIIEKL 184
APSK cd02027
Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5 ...
 30-177 8.30e-103

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: 292.84  E-value: 8.30e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505182879  30 VLWFTGLSGSGKSTVAGALEEALHELGVSTYLLDGDNVRHGLCSDLGFSDDDRKENIRRVGEVAKLMVDAGLVVLTAFIS 109
Cdd:cd02027    1 VIWLTGLSGSGKSTIARALEEKLFQRGRPVYVLDGDNVRHGLNKDLGFSREDREENIRRIAEVAKLLADAGLIVIAAFIS 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505182879 110 PHRAERQMVRERLGEGRFIEVFVDTPLAICETRDPKGLYKKARAGELRNFTGIDSVYESPENAEIHLD 177
Cdd:cd02027   81 PYREDREAARKIIGGGDFLEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDDPYEAPENPDLVLD 148
APS_kinase pfam01583
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3 ...
 27-177 1.90e-102

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: 291.91  E-value: 1.90e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505182879   27 RGVVLWFTGLSGSGKSTVAGALEEALHELGVSTYLLDGDNVRHGLCSDLGFSDDDRKENIRRVGEVAKLMVDAGLVVLTA 106
Cdd:pfam01583   1 RGCTIWLTGLSGAGKSTIANALERKLFEQGRSVYVLDGDNVRHGLNKDLGFSEEDRTENIRRIGEVAKLFADAGLIVITA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505182879  107 FISPHRAERQMVRERLGEGRFIEVFVDTPLAICETRDPKGLYKKARAGELRNFTGIDSVYESPENAEIHLD 177
Cdd:pfam01583  81 FISPYREDREQARELHEEGKFIEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDSPYEAPENPELVLD 151
 
Name Accession Description Interval E-value
PRK03846 PRK03846
adenylylsulfate kinase; Provisional
 5-201 7.11e-152

adenylylsulfate kinase; Provisional


Pssm-ID: 179661  Cd Length: 198  Bit Score: 418.58  E-value: 7.11e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505182879   5 DENVVWHAHPVTREQREQHHGHRGVVLWFTGLSGSGKSTVAGALEEALHELGVSTYLLDGDNVRHGLCSDLGFSDDDRKE 84
Cdd:PRK03846   1 DENIVWHQHPVTKAQREQLHGHKGVVLWFTGLSGSGKSTVAGALEEALHELGVSTYLLDGDNVRHGLCSDLGFSDADRKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505182879  85 NIRRVGEVAKLMVDAGLVVLTAFISPHRAERQMVRERLGEGRFIEVFVDTPLAICETRDPKGLYKKARAGELRNFTGIDS 164
Cdd:PRK03846  81 NIRRVGEVAKLMVDAGLVVLTAFISPHRAERQMVRERLGEGEFIEVFVDTPLAICEARDPKGLYKKARAGEIRNFTGIDS 160

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 505182879 165 VYESPENAEIHLD-GEQLVTNLVHQLLDLLRQSDIIRS 201
Cdd:PRK03846 161 VYEAPESPEIHLDtGEQLVTNLVEQLLDYLRQRDIIRS 198
CysC COG0529
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ...
 13-200 8.88e-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: 352.08  E-value: 8.88e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505182879  13 HPVTREQREQHHGHRGVVLWFTGLSGSGKSTVAGALEEALHELGVSTYLLDGDNVRHGLCSDLGFSDDDRKENIRRVGEV 92
Cdd:COG0529    1 SAVTREERAALKGQKGFVVWFTGLSGSGKSTLANALERRLFERGRHVYLLDGDNVRHGLNKDLGFSKEDRDENIRRIGEV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505182879  93 AKLMVDAGLVVLTAFISPHRAERQMVRERLGEGRFIEVFVDTPLAICETRDPKGLYKKARAGELRNFTGIDSVYESPENA 172
Cdd:COG0529   81 AKLLADAGLIVLVAFISPYRADREEARELIGEGEFIEVYVDTPLEVCEARDPKGLYAKARAGEIKNFTGIDDPYEAPENP 160

                        170       180
                 ....*....|....*....|....*....
gi 505182879 173 EIHLDGEQL-VTNLVHQLLDLLRQSDIIR 200
Cdd:COG0529  161 ELVLDTDKEsVEESVEKILAYLEERGYIS 189
apsK TIGR00455
adenylyl-sulfate kinase; This protein, adenylylsulfate kinase, is often found as a fusion ...
 10-193 1.80e-110

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: 313.64  E-value: 1.80e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505182879   10 WHAHpVTREQREQHHGHRGVVLWFTGLSGSGKSTVAGALEEALHELGVSTYLLDGDNVRHGLCSDLGFSDDDRKENIRRV 89
Cdd:TIGR00455   1 WHPA-ITKDERQALNGHRGVVIWLTGLSGSGKSTIANALEKKLESKGYRVYVLDGDNVRHGLNKDLGFSEEDRKENIRRI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505182879   90 GEVAKLMVDAGLVVLTAFISPHRAERQMVRERLGEGRFIEVFVDTPLAICETRDPKGLYKKARAGELRNFTGIDSVYESP 169
Cdd:TIGR00455  80 GEVAKLFVRNGIIVITSFISPYRADRQMVRELIEKGEFIEVFVDCPLEVCEQRDPKGLYKKARNGEIKGFTGIDSPYEAP 159

                         170       180
                  ....*....|....*....|....*
gi 505182879  170 ENAEIHLD-GEQLVTNLVHQLLDLL 193
Cdd:TIGR00455 160 ENPEVVLDtDQNDREECVGQIIEKL 184
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
 3-199 1.25e-104

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 313.79  E-value: 1.25e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505182879   3 RHDENVVWHAHPVTREQREQHHGHRGVVLWFTGLSGSGKSTVAGALEEALHELGVSTYLLDGDNVRHGLCSDLGFSDDDR 82
Cdd:PRK05506 435 RRATNVHWQASDVSREARAARKGQKPATVWFTGLSGSGKSTIANLVERRLHALGRHTYLLDGDNVRHGLNRDLGFSDADR 514

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505182879  83 KENIRRVGEVAKLMVDAGLVVLTAFISPHRAERQMVRERLGEGRFIEVFVDTPLAICETRDPKGLYKKARAGELRNFTGI 162
Cdd:PRK05506 515 VENIRRVAEVARLMADAGLIVLVSFISPFREERELARALHGEGEFVEVFVDTPLEVCEARDPKGLYAKARAGEIKNFTGI 594

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 505182879 163 DSVYESPENAEIHLDGEQL-VTNLVHQLLDLLRQSDII 199
Cdd:PRK05506 595 DSPYEAPENPELRLDTTGRsPEELAEQVLELLRRRGAI 632
APSK cd02027
Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5 ...
 30-177 8.30e-103

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: 292.84  E-value: 8.30e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505182879  30 VLWFTGLSGSGKSTVAGALEEALHELGVSTYLLDGDNVRHGLCSDLGFSDDDRKENIRRVGEVAKLMVDAGLVVLTAFIS 109
Cdd:cd02027    1 VIWLTGLSGSGKSTIARALEEKLFQRGRPVYVLDGDNVRHGLNKDLGFSREDREENIRRIAEVAKLLADAGLIVIAAFIS 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505182879 110 PHRAERQMVRERLGEGRFIEVFVDTPLAICETRDPKGLYKKARAGELRNFTGIDSVYESPENAEIHLD 177
Cdd:cd02027   81 PYREDREAARKIIGGGDFLEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDDPYEAPENPDLVLD 148
APS_kinase pfam01583
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3 ...
 27-177 1.90e-102

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: 291.91  E-value: 1.90e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505182879   27 RGVVLWFTGLSGSGKSTVAGALEEALHELGVSTYLLDGDNVRHGLCSDLGFSDDDRKENIRRVGEVAKLMVDAGLVVLTA 106
Cdd:pfam01583   1 RGCTIWLTGLSGAGKSTIANALERKLFEQGRSVYVLDGDNVRHGLNKDLGFSEEDRTENIRRIGEVAKLFADAGLIVITA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505182879  107 FISPHRAERQMVRERLGEGRFIEVFVDTPLAICETRDPKGLYKKARAGELRNFTGIDSVYESPENAEIHLD 177
Cdd:pfam01583  81 FISPYREDREQARELHEEGKFIEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDSPYEAPENPELVLD 151
PRK00889 PRK00889
adenylylsulfate kinase; Provisional
 26-192 8.23e-73

adenylylsulfate kinase; Provisional


Pssm-ID: 179157  Cd Length: 175  Bit Score: 217.97  E-value: 8.23e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505182879  26 HRGVVLWFTGLSGSGKSTVAGALEEALHELGVSTYLLDGDNVRHGLCSDLGFSDDDRKENIRRVGEVAKLMVDAGLVVLT 105
Cdd:PRK00889   2 QRGVTVWFTGLSGAGKTTIARALAEKLREAGYPVEVLDGDAVRTNLSKGLGFSKEDRDTNIRRIGFVANLLTRHGVIVLV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505182879 106 AFISPHRAERQMVRERLgeGRFIEVFVDTPLAICETRDPKGLYKKARAGELRNFTGIDSVYESPENAEIHL--DGEQL-- 181
Cdd:PRK00889  82 SAISPYRETREEVRANI--GNFLEVFVDAPLEVCEQRDVKGLYAKARAGEIKHFTGIDDPYEPPLNPEVECrtDLESLee 159

                        170
                 ....*....|..
gi 505182879 182 -VTNLVHQLLDL 192
Cdd:PRK00889 160 sVDKVLQKLEEL 171
PRK05537 PRK05537
bifunctional sulfate adenylyltransferase/adenylylsulfate kinase;
10-200 3.26e-62

bifunctional sulfate adenylyltransferase/adenylylsulfate kinase;


Pssm-ID: 180124 [Multi-domain]  Cd Length: 568  Bit Score: 202.21  E-value: 3.26e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505182879  10 WHAHP-VTREQREQH---HGhRGVVLWFTGLSGSGKSTVAGALEEALHEL-GVSTYLLDGDNVRHGLCSDLGFSDDDRKE 84
Cdd:PRK05537 371 WFSFPeVVAELRRTYpprHK-QGFTVFFTGLSGAGKSTIAKALMVKLMEMrGRPVTLLDGDVVRKHLSSELGFSKEDRDL 449

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505182879  85 NIRRVGEVAKLMVDAGLVVLTAFISPHRAERQMVRERLGE-GRFIEVFVDTPLAICETRDPKGLYKKARAGELRNFTGID 163
Cdd:PRK05537 450 NILRIGFVASEITKNGGIAICAPIAPYRATRREVREMIEAyGGFIEVHVATPLEVCEQRDRKGLYAKAREGKIKGFTGIS 529

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 505182879 164 SVYESPENAEIHLDGEQL-VTNLVHQLLDLLRQSDIIR 200
Cdd:PRK05537 530 DPYEPPANPELVIDTTNVtPDECAHKILLYLEEKGYLR 567
PRK05541 PRK05541
adenylylsulfate kinase; Provisional
 28-195 3.99e-28

adenylylsulfate kinase; Provisional


Pssm-ID: 235498  Cd Length: 176  Bit Score: 103.98  E-value: 3.99e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505182879  28 GVVLWFTGLSGSGKSTVAGALEEALHELGVSTYLLDGDNVRHGLCSDlGFSDDDRKENIRRVGEVAKLMVDAGLVVLTAF 107
Cdd:PRK05541   7 GYVIWITGLAGSGKTTIAKALYERLKLKYSNVIYLDGDELREILGHY-GYDKQSRIEMALKRAKLAKFLADQGMIVIVTT 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505182879 108 ISPHRAERQMVRERLgeGRFIEVFVDTPLAICETRDPKGLYKKARAGELRNFTGIDSVYESPeNAEIHLDGEqLVTNLVH 187
Cdd:PRK05541  86 ISMFDEIYAYNRKHL--PNYFEVYLKCDMEELIRRDQKGLYTKALKGEIKNVVGVDIPFDEP-KADLVIDNS-CRTSLDE 161


                 ....*...
gi 505182879 188 QLLDLLRQ 195
Cdd:PRK05541 162 KVDLILNK 169
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
30-142 1.45e-09

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


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 54.53  E-value: 1.45e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505182879  30 VLWFTGLSGSGKSTVAGALEEALHelgvsTYLLDGDNVRHGLCSDLGFSDDDRKENIRRV----GEVAKLMVDAGL-VVL 104
Cdd:COG0645    1 LILVCGLPGSGKSTLARALAERLG-----AVRLRSDVVRKRLFGAGLAPLERSPEATARTyarlLALARELLAAGRsVIL 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 505182879 105 TA-FISphRAERQMVRERLGE--GRFIEVFVDTPLAICETR 142
Cdd:COG0645   76 DAtFLR--RAQREAFRALAEEagAPFVLIWLDAPEEVLRER 114
GntK cd02021
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting ...
 34-170 2.54e-08

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: 51.10  E-value: 2.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505182879  34 TGLSGSGKSTVAGALEEALHelgvSTYlLDGDNVRHGLC-----SDLGFSDDDRKENIRRVGE--VAKLMVDAGLVVLTA 106
Cdd:cd02021    5 MGVSGSGKSTVGKALAERLG----APF-IDGDDLHPPANiakmaAGIPLNDEDRWPWLQALTDalLAKLASAGEGVVVAC 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505182879 107 -FISphRAERQMVRERLGEGRFIEVFVDTPLAICETRDpkglykKARAGELRNFTGIDSVYESPE 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 4.53e-07

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: 47.30  E-value: 4.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505182879   30 VLWFTGLSGSGKSTVAGALEEALHelgvsTYLLDGDNVRHGLCSDLGFSDDDRKENI----RRVGEVAKLMVDAGL-VVL 104
Cdd:pfam13671   1 LILLVGLPGSGKSTLARRLLEELG-----AVRLSSDDERKRLFGEGRPSISYYTDATdrtyERLHELARIALRAGRpVIL 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 505182879  105 TA-FISP-HRAERQMVRERLGEgRFIEVFVDTPLAICETR 142
Cdd:pfam13671  76 DAtNLRRdERARLLALAREYGV-PVRIVVFEAPEEVLRER 114
GntK COG3265
Gluconate kinase [Carbohydrate transport and metabolism]; Gluconate kinase is part of the ...
 35-194 2.24e-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: 42.81  E-value: 2.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505182879  35 GLSGSGKSTVAGALEEALHelgvsTYLLDGD------NV---RHGlcsdLGFSDDDRKENIRRVGEVAKLMVDAGLVVLT 105
Cdd:COG3265    8 GVSGSGKSTVGQALAERLG-----WPFIDGDdfhppaNIakmAAG----IPLTDEDRAPWLEALADAIAAHLAAGEGAVL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505182879 106 AFISPHRAERQMVRERLGEGRFieVFVDTPLAICETRdpkgLykKARAGELRNFTGIDS---VYESPENAE--IHLDGEQ 180
Cdd:COG3265   79 ACSALKRSYRDRLREGNPDVRF--VYLDGSRELIAER----L--AARKGHFMPASLLDSqfaTLEPPGPDEdaIVVDIDQ 150

                        170
                 ....*....|....
gi 505182879 181 LVTNLVHQLLDLLR 194
Cdd:COG3265  151 PPEEIVAQILAALG 164
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 35-135 2.48e-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: 43.64  E-value: 2.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505182879  35 GLSGSGKSTVAGALEEALHELGVSTYLLDGDNVRHGLCSDLGFSDD----DRKENIRRVGEVAKLMVDAGLVVLTA-FIS 109
Cdd:COG0489  100 GKGGEGKSTVAANLALALAQSGKRVLLIDADLRGPSLHRMLGLENRpglsDVLAGEASLEDVIQPTEVEGLDVLPAgPLP 179

                         90       100       110
                 ....*....|....*....|....*....|....
gi 505182879 110 PHRAERqMVRERLGEgrFIE--------VFVDTP 135
Cdd:COG0489  180 PNPSEL-LASKRLKQ--LLEelrgrydyVIIDTP 210
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 33-67 1.15e-03

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: 37.03  E-value: 1.15e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 505182879  33 FTG-LSGSGKSTVAGALEEALHELGVSTYLLDGDNV 67
Cdd:cd01983    5 VTGgKGGVGKTTLAAALAVALAAKGYKVLLIDLDDY 40
COG4639 COG4639
Predicted kinase [General function prediction only];
35-143 4.38e-03

Predicted kinase [General function prediction only];


Pssm-ID: 443677 [Multi-domain]  Cd Length: 145  Bit Score: 35.96  E-value: 4.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505182879  35 GLSGSGKSTVAGALEEAlhelgvsTYLLDGDNVRHGLCSDlgfsDDDRKENiRRVGEVAKLMVDAGL-----VVLTAfIS 109
Cdd:COG4639    9 GLPGSGKSTFARRLFAP-------TEVVSSDDIRALLGGD----ENDQSAW-GDVFQLAHEIARARLragrlTVVDA-TN 75

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 505182879 110 PHRAERQMVRERLGE--GRFIEVFVDTPLAICETRD 143
Cdd:COG4639   76 LQREARRRLLALARAygALVVAVVLDVPLEVCLARN 111
AAA_22 pfam13401
AAA domain;
23-104 6.11e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 35.40  E-value: 6.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505182879   23 HHGHRGVVLwFTGLSGSGKSTVAGALEEALHELGVSTYLLD------GDNVRHGLCSDLG---FSDDDRKENIRRVGEVA 93
Cdd:pfam13401   1 IRFGAGILV-LTGESGTGKTTLLRRLLEQLPEVRDSVVFVDlpsgtsPKDLLRALLRALGlplSGRLSKEELLAALQQLL 79

                          90
                  ....*....|.
gi 505182879   94 KLMVDAGLVVL 104
Cdd:pfam13401  80 LALAVAVVLII 90
KTI12 pfam08433
Chromatin associated protein KTI12; This is a family of chromatin associated proteins which ...
 33-69 9.88e-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: 35.73  E-value: 9.88e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 505182879   33 FTGLSGSGKSTVAGALEEALHELGVSTYLLDGDNVRH 69
Cdd:pfam08433   4 LTGLPSSGKSTRAKQLAKYLEESNYDVIVISDESLGI 40
 
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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