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Conserved domains on  [gi|257780908|gb|ACV64802|]
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adenylylsulfate kinase [Desulfofarcimen acetoxidans DSM 771]

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]; ...
3-175 6.29e-95

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: 273.50  E-value: 6.29e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257780908   3 QGFTVWFTGMSGAGKTTLGEKLVKELRFRGFKADGLDGDVVRQGLCRDLGFSVEDREKNIRCMAFAAQILNRNGICAIAS 82
Cdd:COG0529   15 KGFVVWFTGLSGSGKSTLANALERRLFERGRHVYLLDGDNVRHGLNKDLGFSKEDRDENIRRIGEVAKLLADAGLIVLVA 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257780908  83 FITPYNSMRRFCREQIS--RYVEIYVRCPLETLIRRDVKGLYKKALSGELPAFTGISDPFEEPETPDLVVDTSCETPEKS 160
Cdd:COG0529   95 FISPYRADREEARELIGegEFIEVYVDTPLEVCEARDPKGLYAKARAGEIKNFTGIDDPYEAPENPELVLDTDKESVEES 174
                        170
                 ....*....|....*
gi 257780908 161 LAKVIYMLEMKGFLE 175
Cdd:COG0529  175 VEKILAYLEERGYIS 189
 
Name Accession Description Interval E-value
CysC COG0529
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ...
3-175 6.29e-95

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: 273.50  E-value: 6.29e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257780908   3 QGFTVWFTGMSGAGKTTLGEKLVKELRFRGFKADGLDGDVVRQGLCRDLGFSVEDREKNIRCMAFAAQILNRNGICAIAS 82
Cdd:COG0529   15 KGFVVWFTGLSGSGKSTLANALERRLFERGRHVYLLDGDNVRHGLNKDLGFSKEDRDENIRRIGEVAKLLADAGLIVLVA 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257780908  83 FITPYNSMRRFCREQIS--RYVEIYVRCPLETLIRRDVKGLYKKALSGELPAFTGISDPFEEPETPDLVVDTSCETPEKS 160
Cdd:COG0529   95 FISPYRADREEARELIGegEFIEVYVDTPLEVCEARDPKGLYAKARAGEIKNFTGIDDPYEAPENPELVLDTDKESVEES 174
                        170
                 ....*....|....*
gi 257780908 161 LAKVIYMLEMKGFLE 175
Cdd:COG0529  175 VEKILAYLEERGYIS 189
PRK00889 PRK00889
adenylylsulfate kinase; Provisional
1-175 5.93e-80

adenylylsulfate kinase; Provisional


Pssm-ID: 179157  Cd Length: 175  Bit Score: 234.92  E-value: 5.93e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257780908   1 MYQGFTVWFTGMSGAGKTTLGEKLVKELRFRGFKADGLDGDVVRQGLCRDLGFSVEDREKNIRCMAFAAQILNRNGICAI 80
Cdd:PRK00889   1 KQRGVTVWFTGLSGAGKTTIARALAEKLREAGYPVEVLDGDAVRTNLSKGLGFSKEDRDTNIRRIGFVANLLTRHGVIVL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257780908  81 ASFITPYNSMRRFCREQISRYVEIYVRCPLETLIRRDVKGLYKKALSGELPAFTGISDPFEEPETPDLVVDTSCETPEKS 160
Cdd:PRK00889  81 VSAISPYRETREEVRANIGNFLEVFVDAPLEVCEQRDVKGLYAKARAGEIKHFTGIDDPYEPPLNPEVECRTDLESLEES 160
                        170
                 ....*....|....*
gi 257780908 161 LAKVIYMLEMKGFLE 175
Cdd:PRK00889 161 VDKVLQKLEELGYLV 175
APSK cd02027
Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5 ...
6-152 1.15e-73

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: 218.12  E-value: 1.15e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257780908   6 TVWFTGMSGAGKTTLGEKLVKELRFRGFKADGLDGDVVRQGLCRDLGFSVEDREKNIRCMAFAAQILNRNGICAIASFIT 85
Cdd:cd02027    1 VIWLTGLSGSGKSTIARALEEKLFQRGRPVYVLDGDNVRHGLNKDLGFSREDREENIRRIAEVAKLLADAGLIVIAAFIS 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 257780908  86 PYNSMRRFCREQIS--RYVEIYVRCPLETLIRRDVKGLYKKALSGELPAFTGISDPFEEPETPDLVVDT 152
Cdd:cd02027   81 PYREDREAARKIIGggDFLEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDDPYEAPENPDLVLDT 149
APS_kinase pfam01583
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3 ...
3-153 9.18e-70

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: 208.33  E-value: 9.18e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257780908    3 QGFTVWFTGMSGAGKTTLGEKLVKELRFRGFKADGLDGDVVRQGLCRDLGFSVEDREKNIRCMAFAAQILNRNGICAIAS 82
Cdd:pfam01583   1 RGCTIWLTGLSGAGKSTIANALERKLFEQGRSVYVLDGDNVRHGLNKDLGFSEEDRTENIRRIGEVAKLFADAGLIVITA 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 257780908   83 FITPYNSMRRFCREQI--SRYVEIYVRCPLETLIRRDVKGLYKKALSGELPAFTGISDPFEEPETPDLVVDTS 153
Cdd:pfam01583  81 FISPYREDREQARELHeeGKFIEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDSPYEAPENPELVLDTD 153
apsK TIGR00455
adenylyl-sulfate kinase; This protein, adenylylsulfate kinase, is often found as a fusion ...
4-168 1.79e-64

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: 196.15  E-value: 1.79e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257780908    4 GFTVWFTGMSGAGKTTLGEKLVKELRFRGFKADGLDGDVVRQGLCRDLGFSVEDREKNIRCMAFAAQILNRNGICAIASF 83
Cdd:TIGR00455  18 GVVIWLTGLSGSGKSTIANALEKKLESKGYRVYVLDGDNVRHGLNKDLGFSEEDRKENIRRIGEVAKLFVRNGIIVITSF 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257780908   84 ITPYNSMRRFCREQIS--RYVEIYVRCPLETLIRRDVKGLYKKALSGELPAFTGISDPFEEPETPDLVVDTSCETPEKSL 161
Cdd:TIGR00455  98 ISPYRADRQMVRELIEkgEFIEVFVDCPLEVCEQRDPKGLYKKARNGEIKGFTGIDSPYEAPENPEVVLDTDQNDREECV 177

                  ....*..
gi 257780908  162 AKVIYML 168
Cdd:TIGR00455 178 GQIIEKL 184
 
Name Accession Description Interval E-value
CysC COG0529
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ...
3-175 6.29e-95

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: 273.50  E-value: 6.29e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257780908   3 QGFTVWFTGMSGAGKTTLGEKLVKELRFRGFKADGLDGDVVRQGLCRDLGFSVEDREKNIRCMAFAAQILNRNGICAIAS 82
Cdd:COG0529   15 KGFVVWFTGLSGSGKSTLANALERRLFERGRHVYLLDGDNVRHGLNKDLGFSKEDRDENIRRIGEVAKLLADAGLIVLVA 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257780908  83 FITPYNSMRRFCREQIS--RYVEIYVRCPLETLIRRDVKGLYKKALSGELPAFTGISDPFEEPETPDLVVDTSCETPEKS 160
Cdd:COG0529   95 FISPYRADREEARELIGegEFIEVYVDTPLEVCEARDPKGLYAKARAGEIKNFTGIDDPYEAPENPELVLDTDKESVEES 174
                        170
                 ....*....|....*
gi 257780908 161 LAKVIYMLEMKGFLE 175
Cdd:COG0529  175 VEKILAYLEERGYIS 189
PRK00889 PRK00889
adenylylsulfate kinase; Provisional
1-175 5.93e-80

adenylylsulfate kinase; Provisional


Pssm-ID: 179157  Cd Length: 175  Bit Score: 234.92  E-value: 5.93e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257780908   1 MYQGFTVWFTGMSGAGKTTLGEKLVKELRFRGFKADGLDGDVVRQGLCRDLGFSVEDREKNIRCMAFAAQILNRNGICAI 80
Cdd:PRK00889   1 KQRGVTVWFTGLSGAGKTTIARALAEKLREAGYPVEVLDGDAVRTNLSKGLGFSKEDRDTNIRRIGFVANLLTRHGVIVL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257780908  81 ASFITPYNSMRRFCREQISRYVEIYVRCPLETLIRRDVKGLYKKALSGELPAFTGISDPFEEPETPDLVVDTSCETPEKS 160
Cdd:PRK00889  81 VSAISPYRETREEVRANIGNFLEVFVDAPLEVCEQRDVKGLYAKARAGEIKHFTGIDDPYEPPLNPEVECRTDLESLEES 160
                        170
                 ....*....|....*
gi 257780908 161 LAKVIYMLEMKGFLE 175
Cdd:PRK00889 161 VDKVLQKLEELGYLV 175
APSK cd02027
Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5 ...
6-152 1.15e-73

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: 218.12  E-value: 1.15e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257780908   6 TVWFTGMSGAGKTTLGEKLVKELRFRGFKADGLDGDVVRQGLCRDLGFSVEDREKNIRCMAFAAQILNRNGICAIASFIT 85
Cdd:cd02027    1 VIWLTGLSGSGKSTIARALEEKLFQRGRPVYVLDGDNVRHGLNKDLGFSREDREENIRRIAEVAKLLADAGLIVIAAFIS 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 257780908  86 PYNSMRRFCREQIS--RYVEIYVRCPLETLIRRDVKGLYKKALSGELPAFTGISDPFEEPETPDLVVDT 152
Cdd:cd02027   81 PYREDREAARKIIGggDFLEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDDPYEAPENPDLVLDT 149
APS_kinase pfam01583
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3 ...
3-153 9.18e-70

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: 208.33  E-value: 9.18e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257780908    3 QGFTVWFTGMSGAGKTTLGEKLVKELRFRGFKADGLDGDVVRQGLCRDLGFSVEDREKNIRCMAFAAQILNRNGICAIAS 82
Cdd:pfam01583   1 RGCTIWLTGLSGAGKSTIANALERKLFEQGRSVYVLDGDNVRHGLNKDLGFSEEDRTENIRRIGEVAKLFADAGLIVITA 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 257780908   83 FITPYNSMRRFCREQI--SRYVEIYVRCPLETLIRRDVKGLYKKALSGELPAFTGISDPFEEPETPDLVVDTS 153
Cdd:pfam01583  81 FISPYREDREQARELHeeGKFIEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDSPYEAPENPELVLDTD 153
PRK05537 PRK05537
bifunctional sulfate adenylyltransferase/adenylylsulfate kinase;
3-175 3.43e-65

bifunctional sulfate adenylyltransferase/adenylylsulfate kinase;


Pssm-ID: 180124 [Multi-domain]  Cd Length: 568  Bit Score: 209.14  E-value: 3.43e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257780908   3 QGFTVWFTGMSGAGKTTLGEKL-VKELRFRGFKADGLDGDVVRQGLCRDLGFSVEDREKNIRCMAFAAQILNRNGICAIA 81
Cdd:PRK05537 391 QGFTVFFTGLSGAGKSTIAKALmVKLMEMRGRPVTLLDGDVVRKHLSSELGFSKEDRDLNILRIGFVASEITKNGGIAIC 470
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257780908  82 SFITPYNSMRRFCREQIS---RYVEIYVRCPLETLIRRDVKGLYKKALSGELPAFTGISDPFEEPETPDLVVDTSCETPE 158
Cdd:PRK05537 471 APIAPYRATRREVREMIEaygGFIEVHVATPLEVCEQRDRKGLYAKAREGKIKGFTGISDPYEPPANPELVIDTTNVTPD 550
                        170
                 ....*....|....*..
gi 257780908 159 KSLAKVIYMLEMKGFLE 175
Cdd:PRK05537 551 ECAHKILLYLEEKGYLR 567
apsK TIGR00455
adenylyl-sulfate kinase; This protein, adenylylsulfate kinase, is often found as a fusion ...
4-168 1.79e-64

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: 196.15  E-value: 1.79e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257780908    4 GFTVWFTGMSGAGKTTLGEKLVKELRFRGFKADGLDGDVVRQGLCRDLGFSVEDREKNIRCMAFAAQILNRNGICAIASF 83
Cdd:TIGR00455  18 GVVIWLTGLSGSGKSTIANALEKKLESKGYRVYVLDGDNVRHGLNKDLGFSEEDRKENIRRIGEVAKLFVRNGIIVITSF 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257780908   84 ITPYNSMRRFCREQIS--RYVEIYVRCPLETLIRRDVKGLYKKALSGELPAFTGISDPFEEPETPDLVVDTSCETPEKSL 161
Cdd:TIGR00455  98 ISPYRADRQMVRELIEkgEFIEVFVDCPLEVCEQRDPKGLYKKARNGEIKGFTGIDSPYEAPENPEVVLDTDQNDREECV 177

                  ....*..
gi 257780908  162 AKVIYML 168
Cdd:TIGR00455 178 GQIIEKL 184
PRK03846 PRK03846
adenylylsulfate kinase; Provisional
3-174 9.52e-60

adenylylsulfate kinase; Provisional


Pssm-ID: 179661  Cd Length: 198  Bit Score: 184.76  E-value: 9.52e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257780908   3 QGFTVWFTGMSGAGKTTLGEKLVKELRFRGFKADGLDGDVVRQGLCRDLGFSVEDREKNIRCMAFAAQILNRNGICAIAS 82
Cdd:PRK03846  23 KGVVLWFTGLSGSGKSTVAGALEEALHELGVSTYLLDGDNVRHGLCSDLGFSDADRKENIRRVGEVAKLMVDAGLVVLTA 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257780908  83 FITPYNSMRRFCREQI--SRYVEIYVRCPLETLIRRDVKGLYKKALSGELPAFTGISDPFEEPETPDLVVDTSCETPEKS 160
Cdd:PRK03846 103 FISPHRAERQMVRERLgeGEFIEVFVDTPLAICEARDPKGLYKKARAGEIRNFTGIDSVYEAPESPEIHLDTGEQLVTNL 182
                        170
                 ....*....|....
gi 257780908 161 LAKVIYMLEMKGFL 174
Cdd:PRK03846 183 VEQLLDYLRQRDII 196
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
3-174 1.62e-56

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 187.44  E-value: 1.62e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257780908   3 QGFTVWFTGMSGAGKTTLGEKLVKELRFRGFKADGLDGDVVRQGLCRDLGFSVEDREKNIRCMAFAAQILNRNGICAIAS 82
Cdd:PRK05506 459 KPATVWFTGLSGSGKSTIANLVERRLHALGRHTYLLDGDNVRHGLNRDLGFSDADRVENIRRVAEVARLMADAGLIVLVS 538
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257780908  83 FITPYNSMRRFCREQI--SRYVEIYVRCPLETLIRRDVKGLYKKALSGELPAFTGISDPFEEPETPDLVVDTSCETPEKS 160
Cdd:PRK05506 539 FISPFREERELARALHgeGEFVEVFVDTPLEVCEARDPKGLYAKARAGEIKNFTGIDSPYEAPENPELRLDTTGRSPEEL 618
                        170
                 ....*....|....
gi 257780908 161 LAKVIYMLEMKGFL 174
Cdd:PRK05506 619 AEQVLELLRRRGAI 632
PRK05541 PRK05541
adenylylsulfate kinase; Provisional
1-166 9.52e-38

adenylylsulfate kinase; Provisional


Pssm-ID: 235498  Cd Length: 176  Bit Score: 127.86  E-value: 9.52e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257780908   1 MYQGFTVWFTGMSGAGKTTLGEKLVKELRFRGFKADGLDGDVVRQGLCRDlGFSVEDREKNIRCMAFAAQILNRNGICAI 80
Cdd:PRK05541   4 KPNGYVIWITGLAGSGKTTIAKALYERLKLKYSNVIYLDGDELREILGHY-GYDKQSRIEMALKRAKLAKFLADQGMIVI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257780908  81 ASFITPYNSMRRFCREQISRYVEIYVRCPLETLIRRDVKGLYKKALSGELPAFTGISDPFEEPETpDLVVDTSCETPEKS 160
Cdd:PRK05541  83 VTTISMFDEIYAYNRKHLPNYFEVYLKCDMEELIRRDQKGLYTKALKGEIKNVVGVDIPFDEPKA-DLVIDNSCRTSLDE 161

                 ....*.
gi 257780908 161 LAKVIY 166
Cdd:PRK05541 162 KVDLIL 167
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
7-164 2.39e-13

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


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 64.16  E-value: 2.39e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257780908   7 VWFTGMSGAGKTTLGEKLVKELRFRgfkadGLDGDVVRQGLCRD----LGFSVEDREKNIRCMAFAAQILNRNGICAI-- 80
Cdd:COG0645    2 ILVCGLPGSGKSTLARALAERLGAV-----RLRSDVVRKRLFGAglapLERSPEATARTYARLLALARELLAAGRSVIld 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257780908  81 ASFITP--YNSMRRFCREQISRYVEIYVRCPLETLIRRdvkgLYKKALSGELPAFT--------GISDPFEEPETPDLVV 150
Cdd:COG0645   77 ATFLRRaqREAFRALAEEAGAPFVLIWLDAPEEVLRER----LEARNAEGGDSDATwevlerqlAFEEPLTEDEGFLLVV 152
                        170
                 ....*....|....
gi 257780908 151 DTSceTPEKSLAKV 164
Cdd:COG0645  153 DTS--GLEEALAAL 164
AAA_18 pfam13238
AAA domain;
7-116 6.61e-08

AAA domain;


Pssm-ID: 433052 [Multi-domain]  Cd Length: 128  Bit Score: 48.96  E-value: 6.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257780908    7 VWFTGMSGAGKTTLGEKLVKELRFRGFkadglDGDVVRQGLCRDLGFSV--EDREKNIRCMAFAAQILNRN------GIC 78
Cdd:pfam13238   1 ILITGTPGVGKTTLAKELSKRLGFGDN-----VRDLALENGLVLGDDPEtrESKRLDEDKLDRLLDLLEENaaleegGNL 75
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 257780908   79 AIASFITPYNSMRRFcreqisRYVEIYVRCPLETLIRR 116
Cdd:pfam13238  76 IIDGHLAELEPERAK------DLVGIVLRASPEELLER 107
KTI12 pfam08433
Chromatin associated protein KTI12; This is a family of chromatin associated proteins which ...
7-157 2.23e-07

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: 49.22  E-value: 2.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257780908    7 VWFTGMSGAGKTTLGEKLVKElrfrgFKADGLDGDVVRQGLCRDLGFSVED--REKNIR--CMAFAAQILNRNGIcAIAS 82
Cdd:pfam08433   2 VLLTGLPSSGKSTRAKQLAKY-----LEESNYDVIVISDESLGIEKDDYKDsaKEKFLRgsLRSAVKRDLSKNTI-VIVD 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257780908   83 FITPYNSMRR--FC--REQISRYVEIYVRCPLETLIRRDVKGLYKKALSGELpaFTGISDPFEEPET------PDLVVDT 152
Cdd:pfam08433  76 SLNYIKGFRYelYCiaKAARTTYCVIHCKAPLDLCRKWNEERGQKSRYPDEL--LDALIQRYEEPNSknrwdsPLFTVLS 153

                  ....*
gi 257780908  153 SCETP 157
Cdd:pfam08433 154 DDETL 158
MobB COG1763
Molybdopterin-guanine dinucleotide biosynthesis protein [Coenzyme transport and metabolism]; ...
9-34 8.85e-07

Molybdopterin-guanine dinucleotide biosynthesis protein [Coenzyme transport and metabolism]; Molybdopterin-guanine dinucleotide biosynthesis protein is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 441369 [Multi-domain]  Cd Length: 162  Bit Score: 46.33  E-value: 8.85e-07
                         10        20
                 ....*....|....*....|....*.
gi 257780908   9 FTGMSGAGKTTLGEKLVKELRFRGFK 34
Cdd:COG1763    6 IVGYSGSGKTTLLEKLIPELKARGLR 31
AAA_33 pfam13671
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ...
7-119 2.62e-06

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: 44.99  E-value: 2.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257780908    7 VWFTGMSGAGKTTLGEKLVKELrfrgfKADGLDGDVVRQGLCRDLGFSVEDREKNI----RCMAFAAQILNRNGICAI-- 80
Cdd:pfam13671   2 ILLVGLPGSGKSTLARRLLEEL-----GAVRLSSDDERKRLFGEGRPSISYYTDATdrtyERLHELARIALRAGRPVIld 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 257780908   81 ASFITPyNSMRRFC---REQISRYVEIYVRCPLETLIRRDVK 119
Cdd:pfam13671  77 ATNLRR-DERARLLalaREYGVPVRIVVFEAPEEVLRERLAA 117
MobB pfam03205
Molybdopterin guanine dinucleotide synthesis protein B; This protein contains a P-loop.
9-34 2.83e-06

Molybdopterin guanine dinucleotide synthesis protein B; This protein contains a P-loop.


Pssm-ID: 427196 [Multi-domain]  Cd Length: 133  Bit Score: 44.46  E-value: 2.83e-06
                          10        20
                  ....*....|....*....|....*.
gi 257780908    9 FTGMSGAGKTTLGEKLVKELRFRGFK 34
Cdd:pfam03205   4 IVGWSGSGKTTLLEKLIPELKARGLR 29
MobB cd03116
molybdopterin-guanine dinucleotide biosynthesis protein B; Molybdenum is an essential trace ...
9-46 1.01e-05

molybdopterin-guanine dinucleotide biosynthesis protein B; Molybdenum is an essential trace element in the form of molybdenum cofactor (Moco) which is associated with the metabolism of nitrogen, carbon and sulfur by redox active enzymes. In Escherichia coli, the synthesis of Moco involves genes from several loci: moa, mob, mod, moe and mog. The mob locus contains mobA and mobB genes. MobB catalyzes the attachment of the guanine dinucleotide to molybdopterin.


Pssm-ID: 349770 [Multi-domain]  Cd Length: 157  Bit Score: 43.40  E-value: 1.01e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 257780908   9 FTGMSGAGKTTLGEKLVKELRFRGF-----KADGLDGDVVRQG 46
Cdd:cd03116    5 VVGKSGSGKTTLIEKLIPELKARGLrvaviKHTHHGFDIDTPG 47
NTPase_1 pfam03266
NTPase; This domain is found across all species from bacteria to human, and the function was ...
10-57 1.74e-04

NTPase; This domain is found across all species from bacteria to human, and the function was determined first in a hyperthermophilic bacterium to be an NTPase. The structure of one member-sequence represents a variation of the RecA fold, and implies that the function might be that of a DNA/RNA modifying enzyme. The sequence carries both a Walker A and Walker B motif which together are characteriztic of ATPases or GTPases. The protein exhibits an increased expression profile in human liver cholangiocarcinoma when compared to normal tissue.


Pssm-ID: 460869  Cd Length: 168  Bit Score: 40.30  E-value: 1.74e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 257780908   10 TGMSGAGKTTLGEKLVKELRFRGFKADGLDGDVVRQGLCRdLGFSVED 57
Cdd:pfam03266   5 TGPPGVGKTTLVLKVAELLKSSGVKVGGFYTPEVREGGRR-IGFKIVD 51
RecA-like_Thep1 cd19482
RecA-like domain of the nucleoside-triphosphatase THEP1 family; This family represents the ...
10-57 3.62e-04

RecA-like domain of the nucleoside-triphosphatase THEP1 family; This family represents the THEP1 family ATPase domain. It includes nucleoside-triphosphatase THEP 1 from Aquifex aeolicus (aaTHEP1) a nucleoside-phosphatase, with activity towards ATP, GTP, CTP, TTP and UTP; and which may hydrolyze nucleoside diphosphates with lower efficiency. The catalytic function of aaTHEP1 remains unclear, it may be a DNA/RNA modifying enzyme. Human THEP1 (hsTHEP1) may have a general function in many human tissues, as it is widely expressed in most examined tissues (such as in brain, heart, lymph node, skin, pancreas); it is especially highly expressed in embryonic and various tumor tissues. This family belongs to the RecA-like NTPase superfamily which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410890 [Multi-domain]  Cd Length: 164  Bit Score: 39.12  E-value: 3.62e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 257780908  10 TGMSGAGKTTLGEKLVKELRFRGFKADGLDGDVVRQGLCRdLGFSVED 57
Cdd:cd19482    4 TGPPGVGKTTLVLKVAELLKESGLKVGGFYTPEVREGGKR-IGFKIVD 50
PRK13695 PRK13695
NTPase;
10-57 4.38e-04

NTPase;


Pssm-ID: 237475  Cd Length: 174  Bit Score: 39.13  E-value: 4.38e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 257780908  10 TGMSGAGKTTLGEKLVKELRFRGFKADGLDGDVVRQGLCRdLGFSVED 57
Cdd:PRK13695   6 TGPPGVGKTTLVLKIAELLKEEGYKVGGFYTEEVREGGKR-IGFKIID 52
PRK14489 PRK14489
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobA/MobB; ...
9-35 4.87e-04

putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobA/MobB; Provisional


Pssm-ID: 237727 [Multi-domain]  Cd Length: 366  Bit Score: 39.74  E-value: 4.87e-04
                         10        20
                 ....*....|....*....|....*..
gi 257780908   9 FTGMSGAGKTTLGEKLVKELRFRGFKA 35
Cdd:PRK14489 210 VVGYSGTGKTTLLEKLIPELIARGYRI 236
aroK PRK00131
shikimate kinase; Reviewed
1-170 6.55e-04

shikimate kinase; Reviewed


Pssm-ID: 234654 [Multi-domain]  Cd Length: 175  Bit Score: 38.63  E-value: 6.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257780908   1 MYQGFTVWFTGMSGAGKTTLGEKLVKELRfRGFkadgLDGDVV---RQGL-CRDLgFSVE------DREKNIrcmafAAQ 70
Cdd:PRK00131   1 MLKGPNIVLIGFMGAGKSTIGRLLAKRLG-YDF----IDTDHLieaRAGKsIPEI-FEEEgeaafrELEEEV-----LAE 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257780908  71 ILNRNGICaIA----SFITPYNsmRRFCREQ--IsryveIYVRCPLETLIRR---DVK-GLYKKALSGELpaftgISDPF 140
Cdd:PRK00131  70 LLARHNLV-IStgggAVLREEN--RALLRERgtV-----VYLDASFEELLRRlrrDRNrPLLQTNDPKEK-----LRDLY 136
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 257780908 141 EE--P---ETPDLVVDTSCETPEKSLAKVIYMLEM 170
Cdd:PRK00131 137 EErdPlyeEVADITVETDGRSPEEVVNEILEKLEA 171
PRK14491 PRK14491
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; ...
9-34 6.21e-03

putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; Provisional


Pssm-ID: 237729 [Multi-domain]  Cd Length: 597  Bit Score: 36.52  E-value: 6.21e-03
                         10        20
                 ....*....|....*....|....*.
gi 257780908   9 FTGMSGAGKTTLGEKLVKELRFRGFK 34
Cdd:PRK14491  15 FCAYSGTGKTTLLEQLIPELNQRGLR 40
AAA_17 pfam13207
AAA domain;
10-45 6.22e-03

AAA domain;


Pssm-ID: 463810 [Multi-domain]  Cd Length: 136  Bit Score: 35.29  E-value: 6.22e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 257780908   10 TGMSGAGKTTLGEKLVKELRFRGFKAdgldGDVVRQ 45
Cdd:pfam13207   1 TGVPGSGKTTQLKKLAEKLGFPHISA----GDLLRE 32
NK cd02019
Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of ...
6-63 6.27e-03

Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of enzymes that share structural similarity and are functionally related to the catalysis of the reversible phosphate group transfer from nucleoside triphosphates to nucleosides/nucleotides, nucleoside monophosphates, or sugars. Members of this family play a wide variety of essential roles in nucleotide metabolism, the biosynthesis of coenzymes and aromatic compounds, as well as the metabolism of sugar and sulfate.


Pssm-ID: 238977 [Multi-domain]  Cd Length: 69  Bit Score: 33.85  E-value: 6.27e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 257780908   6 TVWFTGMSGAGKTTLGEKLVKELRFRGFKAdgLDGDVVrqgLCRdLGFSVEDREKNIR 63
Cdd:cd02019    1 IIAITGGSGSGKSTVAKKLAEQLGGRSVVV--LDEIVI---LEG-LYASYKSRDARIR 52
 
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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