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Conserved domains on  [gi|1477141595|ref|WP_119052872|]
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adenylyl-sulfate kinase [Paraflavitalea soli]

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

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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]; ...
4-172 1.73e-61

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: 188.37  E-value: 1.73e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477141595   4 IQLTGLSGAGKTSIAFRVQQMLLQREIAAEIIDGDMYRKSICKDLGFSPADRRENIRRLGAIAQALVLKNTIAIIAAINP 83
Cdd:COG0529    19 VWFTGLSGSGKSTLANALERRLFERGRHVYLLDGDNVRHGLNKDLGFSKEDRDENIRRIGEVAKLLADAGLIVLVAFISP 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477141595  84 FDDVRKELKEKYDAR---TVWIHCALDILVERDTKGLYRKALLpgdhpDKIRNLTGLNDIYEIPIGADLVIYTHTEDLET 160
Cdd:COG0529    99 YRADREEARELIGEGefiEVYVDTPLEVCEARDPKGLYAKARA-----GEIKNFTGIDDPYEAPENPELVLDTDKESVEE 173
                         170
                  ....*....|..
gi 1477141595 161 SAVRLFSFILDN 172
Cdd:COG0529   174 SVEKILAYLEER 185
 
Name Accession Description Interval E-value
CysC COG0529
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ...
4-172 1.73e-61

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: 188.37  E-value: 1.73e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477141595   4 IQLTGLSGAGKTSIAFRVQQMLLQREIAAEIIDGDMYRKSICKDLGFSPADRRENIRRLGAIAQALVLKNTIAIIAAINP 83
Cdd:COG0529    19 VWFTGLSGSGKSTLANALERRLFERGRHVYLLDGDNVRHGLNKDLGFSKEDRDENIRRIGEVAKLLADAGLIVLVAFISP 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477141595  84 FDDVRKELKEKYDAR---TVWIHCALDILVERDTKGLYRKALLpgdhpDKIRNLTGLNDIYEIPIGADLVIYTHTEDLET 160
Cdd:COG0529    99 YRADREEARELIGEGefiEVYVDTPLEVCEARDPKGLYAKARA-----GEIKNFTGIDDPYEAPENPELVLDTDKESVEE 173
                         170
                  ....*....|..
gi 1477141595 161 SAVRLFSFILDN 172
Cdd:COG0529   174 SVEKILAYLEER 185
PRK00889 PRK00889
adenylylsulfate kinase; Provisional
4-165 2.24e-48

adenylylsulfate kinase; Provisional


Pssm-ID: 179157  Cd Length: 175  Bit Score: 154.79  E-value: 2.24e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477141595   4 IQLTGLSGAGKTSIAFRVQQMLLQREIAAEIIDGDMYRKSICKDLGFSPADRRENIRRLGAIAQALVLKNTIAIIAAINP 83
Cdd:PRK00889    7 VWFTGLSGAGKTTIARALAEKLREAGYPVEVLDGDAVRTNLSKGLGFSKEDRDTNIRRIGFVANLLTRHGVIVLVSAISP 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477141595  84 FDDVRKELKEKY-DARTVWIHCALDILVERDTKGLYRKALlpgdhPDKIRNLTGLNDIYEIPIGADLVIYTHTEDLETSA 162
Cdd:PRK00889   87 YRETREEVRANIgNFLEVFVDAPLEVCEQRDVKGLYAKAR-----AGEIKHFTGIDDPYEPPLNPEVECRTDLESLEESV 161

                  ...
gi 1477141595 163 VRL 165
Cdd:PRK00889  162 DKV 164
APSK cd02027
Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5 ...
4-153 4.37e-45

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: 145.70  E-value: 4.37e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477141595   4 IQLTGLSGAGKTSIAFRVQQMLLQREIAAEIIDGDMYRKSICKDLGFSPADRRENIRRLGAIAQALVLKNTIAIIAAINP 83
Cdd:cd02027     2 IWLTGLSGSGKSTIARALEEKLFQRGRPVYVLDGDNVRHGLNKDLGFSREDREENIRRIAEVAKLLADAGLIVIAAFISP 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1477141595  84 FDDVR---KELKEKYDARTVWIHCALDILVERDTKGLYRKALLpgdhpDKIRNLTGLNDIYEIPIGADLVIYT 153
Cdd:cd02027    82 YREDReaaRKIIGGGDFLEVFVDTPLEVCEQRDPKGLYKKARA-----GEIKGFTGIDDPYEAPENPDLVLDT 149
APS_kinase pfam01583
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3 ...
4-154 5.54e-45

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: 145.54  E-value: 5.54e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477141595   4 IQLTGLSGAGKTSIAFRVQQMLLQREIAAEIIDGDMYRKSICKDLGFSPADRRENIRRLGAIAQALVLKNTIAIIAAINP 83
Cdd:pfam01583   5 IWLTGLSGAGKSTIANALERKLFEQGRSVYVLDGDNVRHGLNKDLGFSEEDRTENIRRIGEVAKLFADAGLIVITAFISP 84
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1477141595  84 FDDVR---KELKEKYDARTVWIHCALDILVERDTKGLYRKALlpgdhPDKIRNLTGLNDIYEIPIGADLVIYTH 154
Cdd:pfam01583  85 YREDReqaRELHEEGKFIEVFVDTPLEVCEQRDPKGLYKKAR-----AGEIKGFTGIDSPYEAPENPELVLDTD 153
apsK TIGR00455
adenylyl-sulfate kinase; This protein, adenylylsulfate kinase, is often found as a fusion ...
4-169 1.39e-42

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: 140.30  E-value: 1.39e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477141595   4 IQLTGLSGAGKTSIAFRVQQMLLQREIAAEIIDGDMYRKSICKDLGFSPADRRENIRRLGAIAQALVLKNTIAIIAAINP 83
Cdd:TIGR00455  21 IWLTGLSGSGKSTIANALEKKLESKGYRVYVLDGDNVRHGLNKDLGFSEEDRKENIRRIGEVAKLFVRNGIIVITSFISP 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477141595  84 FDDVR---KELKEKYDARTVWIHCALDILVERDTKGLYRKALlpgdhPDKIRNLTGLNDIYEIPIGADLVIYTHTEDLET 160
Cdd:TIGR00455 101 YRADRqmvRELIEKGEFIEVFVDCPLEVCEQRDPKGLYKKAR-----NGEIKGFTGIDSPYEAPENPEVVLDTDQNDREE 175

                  ....*....
gi 1477141595 161 SAVRLFSFI 169
Cdd:TIGR00455 176 CVGQIIEKL 184
 
Name Accession Description Interval E-value
CysC COG0529
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ...
4-172 1.73e-61

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: 188.37  E-value: 1.73e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477141595   4 IQLTGLSGAGKTSIAFRVQQMLLQREIAAEIIDGDMYRKSICKDLGFSPADRRENIRRLGAIAQALVLKNTIAIIAAINP 83
Cdd:COG0529    19 VWFTGLSGSGKSTLANALERRLFERGRHVYLLDGDNVRHGLNKDLGFSKEDRDENIRRIGEVAKLLADAGLIVLVAFISP 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477141595  84 FDDVRKELKEKYDAR---TVWIHCALDILVERDTKGLYRKALLpgdhpDKIRNLTGLNDIYEIPIGADLVIYTHTEDLET 160
Cdd:COG0529    99 YRADREEARELIGEGefiEVYVDTPLEVCEARDPKGLYAKARA-----GEIKNFTGIDDPYEAPENPELVLDTDKESVEE 173
                         170
                  ....*....|..
gi 1477141595 161 SAVRLFSFILDN 172
Cdd:COG0529   174 SVEKILAYLEER 185
PRK00889 PRK00889
adenylylsulfate kinase; Provisional
4-165 2.24e-48

adenylylsulfate kinase; Provisional


Pssm-ID: 179157  Cd Length: 175  Bit Score: 154.79  E-value: 2.24e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477141595   4 IQLTGLSGAGKTSIAFRVQQMLLQREIAAEIIDGDMYRKSICKDLGFSPADRRENIRRLGAIAQALVLKNTIAIIAAINP 83
Cdd:PRK00889    7 VWFTGLSGAGKTTIARALAEKLREAGYPVEVLDGDAVRTNLSKGLGFSKEDRDTNIRRIGFVANLLTRHGVIVLVSAISP 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477141595  84 FDDVRKELKEKY-DARTVWIHCALDILVERDTKGLYRKALlpgdhPDKIRNLTGLNDIYEIPIGADLVIYTHTEDLETSA 162
Cdd:PRK00889   87 YRETREEVRANIgNFLEVFVDAPLEVCEQRDVKGLYAKAR-----AGEIKHFTGIDDPYEPPLNPEVECRTDLESLEESV 161

                  ...
gi 1477141595 163 VRL 165
Cdd:PRK00889  162 DKV 164
APSK cd02027
Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5 ...
4-153 4.37e-45

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: 145.70  E-value: 4.37e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477141595   4 IQLTGLSGAGKTSIAFRVQQMLLQREIAAEIIDGDMYRKSICKDLGFSPADRRENIRRLGAIAQALVLKNTIAIIAAINP 83
Cdd:cd02027     2 IWLTGLSGSGKSTIARALEEKLFQRGRPVYVLDGDNVRHGLNKDLGFSREDREENIRRIAEVAKLLADAGLIVIAAFISP 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1477141595  84 FDDVR---KELKEKYDARTVWIHCALDILVERDTKGLYRKALLpgdhpDKIRNLTGLNDIYEIPIGADLVIYT 153
Cdd:cd02027    82 YREDReaaRKIIGGGDFLEVFVDTPLEVCEQRDPKGLYKKARA-----GEIKGFTGIDDPYEAPENPDLVLDT 149
APS_kinase pfam01583
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3 ...
4-154 5.54e-45

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: 145.54  E-value: 5.54e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477141595   4 IQLTGLSGAGKTSIAFRVQQMLLQREIAAEIIDGDMYRKSICKDLGFSPADRRENIRRLGAIAQALVLKNTIAIIAAINP 83
Cdd:pfam01583   5 IWLTGLSGAGKSTIANALERKLFEQGRSVYVLDGDNVRHGLNKDLGFSEEDRTENIRRIGEVAKLFADAGLIVITAFISP 84
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1477141595  84 FDDVR---KELKEKYDARTVWIHCALDILVERDTKGLYRKALlpgdhPDKIRNLTGLNDIYEIPIGADLVIYTH 154
Cdd:pfam01583  85 YREDReqaRELHEEGKFIEVFVDTPLEVCEQRDPKGLYKKAR-----AGEIKGFTGIDSPYEAPENPELVLDTD 153
apsK TIGR00455
adenylyl-sulfate kinase; This protein, adenylylsulfate kinase, is often found as a fusion ...
4-169 1.39e-42

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: 140.30  E-value: 1.39e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477141595   4 IQLTGLSGAGKTSIAFRVQQMLLQREIAAEIIDGDMYRKSICKDLGFSPADRRENIRRLGAIAQALVLKNTIAIIAAINP 83
Cdd:TIGR00455  21 IWLTGLSGSGKSTIANALEKKLESKGYRVYVLDGDNVRHGLNKDLGFSEEDRKENIRRIGEVAKLFVRNGIIVITSFISP 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477141595  84 FDDVR---KELKEKYDARTVWIHCALDILVERDTKGLYRKALlpgdhPDKIRNLTGLNDIYEIPIGADLVIYTHTEDLET 160
Cdd:TIGR00455 101 YRADRqmvRELIEKGEFIEVFVDCPLEVCEQRDPKGLYKKAR-----NGEIKGFTGIDSPYEAPENPEVVLDTDQNDREE 175

                  ....*....
gi 1477141595 161 SAVRLFSFI 169
Cdd:TIGR00455 176 CVGQIIEKL 184
PRK03846 PRK03846
adenylylsulfate kinase; Provisional
3-165 5.30e-38

adenylylsulfate kinase; Provisional


Pssm-ID: 179661  Cd Length: 198  Bit Score: 128.91  E-value: 5.30e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477141595   3 LIQLTGLSGAGKTSIAFRVQQMLLQREIAAEIIDGDMYRKSICKDLGFSPADRRENIRRLGAIAQALVLKNTIAIIAAIN 82
Cdd:PRK03846   26 VLWFTGLSGSGKSTVAGALEEALHELGVSTYLLDGDNVRHGLCSDLGFSDADRKENIRRVGEVAKLMVDAGLVVLTAFIS 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477141595  83 PF----DDVRKELKEKyDARTVWIHCALDILVERDTKGLYRKAllpgdHPDKIRNLTGLNDIYEIPIGADLVIYTHTEDL 158
Cdd:PRK03846  106 PHraerQMVRERLGEG-EFIEVFVDTPLAICEARDPKGLYKKA-----RAGEIRNFTGIDSVYEAPESPEIHLDTGEQLV 179

                  ....*..
gi 1477141595 159 ETSAVRL 165
Cdd:PRK03846  180 TNLVEQL 186
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
6-171 5.88e-35

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 128.89  E-value: 5.88e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477141595   6 LTGLSGAGKTSIAFRVQQMLLQREIAAEIIDGDMYRKSICKDLGFSPADRRENIRRLGAIAQALVLKNTIAIIAAINPFD 85
Cdd:PRK05506  465 FTGLSGSGKSTIANLVERRLHALGRHTYLLDGDNVRHGLNRDLGFSDADRVENIRRVAEVARLMADAGLIVLVSFISPFR 544
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477141595  86 DVR---KELKEKYDARTVWIHCALDILVERDTKGLYRKALlpgdhPDKIRNLTGLNDIYEIPIGADLVIYTHTEDLETSA 162
Cdd:PRK05506  545 EERelaRALHGEGEFVEVFVDTPLEVCEARDPKGLYAKAR-----AGEIKNFTGIDSPYEAPENPELRLDTTGRSPEELA 619

                  ....*....
gi 1477141595 163 VRLFSFILD 171
Cdd:PRK05506  620 EQVLELLRR 628
PRK05537 PRK05537
bifunctional sulfate adenylyltransferase/adenylylsulfate kinase;
6-162 1.99e-30

bifunctional sulfate adenylyltransferase/adenylylsulfate kinase;


Pssm-ID: 180124 [Multi-domain]  Cd Length: 568  Bit Score: 115.92  E-value: 1.99e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477141595   6 LTGLSGAGKTSIAFRVQQMLLQ-REIAAEIIDGDMYRKSICKDLGFSPADRRENIRRLGAIAQALVLKNTIAIIAAINPF 84
Cdd:PRK05537  397 FTGLSGAGKSTIAKALMVKLMEmRGRPVTLLDGDVVRKHLSSELGFSKEDRDLNILRIGFVASEITKNGGIAICAPIAPY 476
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477141595  85 DDVRKELKEKYDA--RTVWIHCALDILV--ERDTKGLYRKAllpgdHPDKIRNLTGLNDIYEIPIGADLVIYTHTEDLET 160
Cdd:PRK05537  477 RATRREVREMIEAygGFIEVHVATPLEVceQRDRKGLYAKA-----REGKIKGFTGISDPYEPPANPELVIDTTNVTPDE 551

                  ..
gi 1477141595 161 SA 162
Cdd:PRK05537  552 CA 553
PRK05541 PRK05541
adenylylsulfate kinase; Provisional
2-151 1.58e-17

adenylylsulfate kinase; Provisional


Pssm-ID: 235498  Cd Length: 176  Bit Score: 75.48  E-value: 1.58e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477141595   2 LLIQLTGLSGAGKTSIAFRVQQMLLQREIAAEIIDGDMYRKsICKDLGFSPADRRENIRRLGAIAQALVLKNTIAIIAAI 81
Cdd:PRK05541    8 YVIWITGLAGSGKTTIAKALYERLKLKYSNVIYLDGDELRE-ILGHYGYDKQSRIEMALKRAKLAKFLADQGMIVIVTTI 86
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1477141595  82 NPFDDV----RKELKEKYDartVWIHCALDILVERDTKGLYRKALLpgdhpDKIRNLTGLNDIYEIPiGADLVI 151
Cdd:PRK05541   87 SMFDEIyaynRKHLPNYFE---VYLKCDMEELIRRDQKGLYTKALK-----GEIKNVVGVDIPFDEP-KADLVI 151
Kti12 COG4088
tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) ...
1-112 9.23e-09

tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) [Translation, ribosomal structure and biogenesis, Defense mechanisms];


Pssm-ID: 443264 [Multi-domain]  Cd Length: 179  Bit Score: 52.04  E-value: 9.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477141595   1 MLLIqLTGLSGAGKTSIAFRVQQMLLQREIAAEIIDGDMYRKSICKDLGFSPAdRRENIRRLGAIAQALVLKNTIAIIA- 79
Cdd:COG4088     5 MLLI-LTGPPGSGKTTFAKALAQRLYAEGIAVALLHSDDFRRFLVNESFPKET-YEEVVEDVRTTTADNALDNGYSVIVd 82
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1477141595  80 AINPFDDVRKEL----KEKYDARTVWIHCALDILVER 112
Cdd:COG4088    83 GTFYYRSWQRDFrnlaKHKAPIHIIYLKAPLETALRR 119
GntK cd02021
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting ...
3-123 7.99e-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: 40.70  E-value: 7.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477141595   3 LIQLTGLSGAGKTSIAfrvqqMLLQREIAAEIIDGDMYRK--SICKDLGFSP---ADRRENIRRL-GAIAQALVLKNTIA 76
Cdd:cd02021     1 IIVVMGVSGSGKSTVG-----KALAERLGAPFIDGDDLHPpaNIAKMAAGIPlndEDRWPWLQALtDALLAKLASAGEGV 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1477141595  77 IIAAINPFDDVRKEL-KEKYDARTVWIHCAL--DILVERDT--KGLYRKALL 123
Cdd:cd02021    76 VVACSALKRIYRDILrGGAANPRVRFVHLDGprEVLAERLAarKGHFMPADL 127
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
3-112 2.77e-04

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


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 39.51  E-value: 2.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477141595   3 LIQLTGLSGAGKTSIAfrvqqMLLQREIAAEIIDGDMYRKSICKDlGFSPADRRENIR-----RLGAIAQALVLKNTIAI 77
Cdd:COG0645     1 LILVCGLPGSGKSTLA-----RALAERLGAVRLRSDVVRKRLFGA-GLAPLERSPEATartyaRLLALARELLAAGRSVI 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1477141595  78 IAAINPFDDVRKELKE-----KYDARTVWIHCALDILVER 112
Cdd:COG0645    75 LDATFLRRAQREAFRAlaeeaGAPFVLIWLDAPEEVLRER 114
SK cd00464
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic ...
4-134 7.90e-04

Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic pathway which converts erythrose-4-phosphate to chorismic acid, found in bacteria, fungi and plants. Chorismic acid is a important intermediate in the synthesis of aromatic compounds, such as aromatic amino acids, p-aminobenzoic acid, folate and ubiquinone. Shikimate kinase catalyses the phosphorylation of the 3-hydroxyl group of shikimic acid using ATP.


Pssm-ID: 238260 [Multi-domain]  Cd Length: 154  Bit Score: 37.92  E-value: 7.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477141595   4 IQLTGLSGAGKTSIAFRVQQMLlqreiAAEIIDGDMYrksICKDLGFSPAD-----RRENIRRLGAIAQALVLKNTIAII 78
Cdd:cd00464     2 IVLIGMMGAGKTTVGRLLAKAL-----GLPFVDLDEL---IEQRAGMSIPEifaeeGEEGFRELEREVLLLLLTKENAVI 73
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1477141595  79 AA-----INPfdDVRKELKEKydARTVWIHCALDILVERDTKGLYRkALLPGDHPDKIRNL 134
Cdd:cd00464    74 ATgggavLRE--ENRRLLLEN--GIVVWLDASPEELLERLARDKTR-PLLQDEDPERLREL 129
COG4639 COG4639
Predicted kinase [General function prediction only];
3-113 8.42e-04

Predicted kinase [General function prediction only];


Pssm-ID: 443677 [Multi-domain]  Cd Length: 145  Bit Score: 37.89  E-value: 8.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477141595   3 LIQLTGLSGAGKTSIAFRVQQmllqreiAAEIIDGDMYRksicKDLGFSPADRREN---IRRLGAIAQALVLKNTIAIIA 79
Cdd:COG4639     4 LVVLIGLPGSGKSTFARRLFA-------PTEVVSSDDIR----ALLGGDENDQSAWgdvFQLAHEIARARLRAGRLTVVD 72
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1477141595  80 AINPFDDVRKELKE---KYDART--VWIHCALDILVERD 113
Cdd:COG4639    73 ATNLQREARRRLLAlarAYGALVvaVVLDVPLEVCLARN 111
AAA_33 pfam13671
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ...
3-112 1.07e-03

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: 37.67  E-value: 1.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477141595   3 LIQLTGLSGAGKTSIAFRvqqmlLQREIAAEIIDGDMYRKSICKDLGFSPADRRENI----RRLGAIAQALVLKNTIAII 78
Cdd:pfam13671   1 LILLVGLPGSGKSTLARR-----LLEELGAVRLSSDDERKRLFGEGRPSISYYTDATdrtyERLHELARIALRAGRPVIL 75
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1477141595  79 AAINPFDDVRK---ELKEKYDART--VWIHCALDILVER 112
Cdd:pfam13671  76 DATNLRRDERArllALAREYGVPVriVVFEAPEEVLRER 114
KTI12 pfam08433
Chromatin associated protein KTI12; This is a family of chromatin associated proteins which ...
3-123 2.72e-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: 37.28  E-value: 2.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477141595   3 LIQLTGLSGAGKTSIAFRVQQMLLQREIAAEIIDGDMYRKSiCKDLGFSPADR--RENIRRlgAIAQALVlKNTIAIIAA 80
Cdd:pfam08433   1 LVLLTGLPSSGKSTRAKQLAKYLEESNYDVIVISDESLGIE-KDDYKDSAKEKflRGSLRS--AVKRDLS-KNTIVIVDS 76
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1477141595  81 INPFDDVRKEL----KEkYDARTVWIHCA--LDILV----ERDTKGLYRKALL 123
Cdd:pfam08433  77 LNYIKGFRYELyciaKA-ARTTYCVIHCKapLDLCRkwneERGQKSRYPDELL 128
 
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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