|
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
|
| 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
|
|
|