|
Name |
Accession |
Description |
Interval |
E-value |
| CysC |
COG0529 |
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ... |
14-197 |
7.40e-113 |
|
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: 319.73 E-value: 7.40e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032932144 14 MMTREDKEELLGQHSVMIWFTGLSGSGKSTIAIALERELHKRGLLCRILDGDNIRSGINNNLGFSETDRVENIRRIAEVS 93
Cdd:COG0529 2 AVTREERAALKGQKGFVVWFTGLSGSGKSTLANALERRLFERGRHVYLLDGDNVRHGLNKDLGFSKEDRDENIRRIGEVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032932144 94 KLFLDSGIITIAAFISPNNDIREMAANIIGKDDFLEVFVSTPLEECEKRDVKGLYAKARKGEIQNFTGISAPFEVPEHPA 173
Cdd:COG0529 82 KLLADAGLIVLVAFISPYRADREEARELIGEGEFIEVYVDTPLEVCEARDPKGLYAKARAGEIKNFTGIDDPYEAPENPE 161
|
170 180
....*....|....*....|....
gi 2032932144 174 LALDTSKLSLEESVNRLLEMVLPK 197
Cdd:COG0529 162 LVLDTDKESVEESVEKILAYLEER 185
|
|
| APSK |
cd02027 |
Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5 ... |
30-178 |
1.81e-97 |
|
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: 279.36 E-value: 1.81e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032932144 30 MIWFTGLSGSGKSTIAIALERELHKRGLLCRILDGDNIRSGINNNLGFSETDRVENIRRIAEVSKLFLDSGIITIAAFIS 109
Cdd:cd02027 1 VIWLTGLSGSGKSTIARALEEKLFQRGRPVYVLDGDNVRHGLNKDLGFSREDREENIRRIAEVAKLLADAGLIVIAAFIS 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2032932144 110 PNNDIREMAANIIGKDDFLEVFVSTPLEECEKRDVKGLYAKARKGEIQNFTGISAPFEVPEHPALALDT 178
Cdd:cd02027 81 PYREDREAARKIIGGGDFLEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDDPYEAPENPDLVLDT 149
|
|
| PRK03846 |
PRK03846 |
adenylylsulfate kinase; Provisional |
16-193 |
3.45e-96 |
|
adenylylsulfate kinase; Provisional
Pssm-ID: 179661 Cd Length: 198 Bit Score: 277.98 E-value: 3.45e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032932144 16 TREDKEELLGQHSVMIWFTGLSGSGKSTIAIALERELHKRGLLCRILDGDNIRSGINNNLGFSETDRVENIRRIAEVSKL 95
Cdd:PRK03846 12 TKAQREQLHGHKGVVLWFTGLSGSGKSTVAGALEEALHELGVSTYLLDGDNVRHGLCSDLGFSDADRKENIRRVGEVAKL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032932144 96 FLDSGIITIAAFISPNNDIREMAANIIGKDDFLEVFVSTPLEECEKRDVKGLYAKARKGEIQNFTGISAPFEVPEHPALA 175
Cdd:PRK03846 92 MVDAGLVVLTAFISPHRAERQMVRERLGEGEFIEVFVDTPLAICEARDPKGLYKKARAGEIRNFTGIDSVYEAPESPEIH 171
|
170
....*....|....*...
gi 2032932144 176 LDTSKLSLEESVNRLLEM 193
Cdd:PRK03846 172 LDTGEQLVTNLVEQLLDY 189
|
|
| APS_kinase |
pfam01583 |
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3 ... |
28-180 |
1.12e-87 |
|
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: 254.55 E-value: 1.12e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032932144 28 SVMIWFTGLSGSGKSTIAIALERELHKRGLLCRILDGDNIRSGINNNLGFSETDRVENIRRIAEVSKLFLDSGIITIAAF 107
Cdd:pfam01583 2 GCTIWLTGLSGAGKSTIANALERKLFEQGRSVYVLDGDNVRHGLNKDLGFSEEDRTENIRRIGEVAKLFADAGLIVITAF 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2032932144 108 ISPNNDIREMAANIIGKDDFLEVFVSTPLEECEKRDVKGLYAKARKGEIQNFTGISAPFEVPEHPALALDTSK 180
Cdd:pfam01583 82 ISPYREDREQARELHEEGKFIEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDSPYEAPENPELVLDTDK 154
|
|
| apsK |
TIGR00455 |
adenylyl-sulfate kinase; This protein, adenylylsulfate kinase, is often found as a fusion ... |
15-194 |
1.17e-82 |
|
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: 243.14 E-value: 1.17e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032932144 15 MTREDKEELLGQHSVMIWFTGLSGSGKSTIAIALERELHKRGLLCRILDGDNIRSGINNNLGFSETDRVENIRRIAEVSK 94
Cdd:TIGR00455 5 ITKDERQALNGHRGVVIWLTGLSGSGKSTIANALEKKLESKGYRVYVLDGDNVRHGLNKDLGFSEEDRKENIRRIGEVAK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032932144 95 LFLDSGIITIAAFISPNNDIREMAANIIGKDDFLEVFVSTPLEECEKRDVKGLYAKARKGEIQNFTGISAPFEVPEHPAL 174
Cdd:TIGR00455 85 LFVRNGIIVITSFISPYRADRQMVRELIEKGEFIEVFVDCPLEVCEQRDPKGLYKKARNGEIKGFTGIDSPYEAPENPEV 164
|
170 180
....*....|....*....|
gi 2032932144 175 ALDTSKLSLEESVNRLLEMV 194
Cdd:TIGR00455 165 VLDTDQNDREECVGQIIEKL 184
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
33-136 |
1.10e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 38.12 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032932144 33 FTGLSGSGKSTIAIALERELHKRGLLCRILDGDNIRSGI----------NNNLGFSETDRVENIRRIAEVSK---LFLDs 99
Cdd:smart00382 7 IVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVldqllliivgGKKASGSGELRLRLALALARKLKpdvLILD- 85
|
90 100 110
....*....|....*....|....*....|....*..
gi 2032932144 100 giiTIAAFISPNNDIREMAANIIGKDDFLEVFVSTPL 136
Cdd:smart00382 86 ---EITSLLDAEQEALLLLLEELRLLLLLKSEKNLTV 119
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CysC |
COG0529 |
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ... |
14-197 |
7.40e-113 |
|
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: 319.73 E-value: 7.40e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032932144 14 MMTREDKEELLGQHSVMIWFTGLSGSGKSTIAIALERELHKRGLLCRILDGDNIRSGINNNLGFSETDRVENIRRIAEVS 93
Cdd:COG0529 2 AVTREERAALKGQKGFVVWFTGLSGSGKSTLANALERRLFERGRHVYLLDGDNVRHGLNKDLGFSKEDRDENIRRIGEVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032932144 94 KLFLDSGIITIAAFISPNNDIREMAANIIGKDDFLEVFVSTPLEECEKRDVKGLYAKARKGEIQNFTGISAPFEVPEHPA 173
Cdd:COG0529 82 KLLADAGLIVLVAFISPYRADREEARELIGEGEFIEVYVDTPLEVCEARDPKGLYAKARAGEIKNFTGIDDPYEAPENPE 161
|
170 180
....*....|....*....|....
gi 2032932144 174 LALDTSKLSLEESVNRLLEMVLPK 197
Cdd:COG0529 162 LVLDTDKESVEESVEKILAYLEER 185
|
|
| APSK |
cd02027 |
Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5 ... |
30-178 |
1.81e-97 |
|
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: 279.36 E-value: 1.81e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032932144 30 MIWFTGLSGSGKSTIAIALERELHKRGLLCRILDGDNIRSGINNNLGFSETDRVENIRRIAEVSKLFLDSGIITIAAFIS 109
Cdd:cd02027 1 VIWLTGLSGSGKSTIARALEEKLFQRGRPVYVLDGDNVRHGLNKDLGFSREDREENIRRIAEVAKLLADAGLIVIAAFIS 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2032932144 110 PNNDIREMAANIIGKDDFLEVFVSTPLEECEKRDVKGLYAKARKGEIQNFTGISAPFEVPEHPALALDT 178
Cdd:cd02027 81 PYREDREAARKIIGGGDFLEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDDPYEAPENPDLVLDT 149
|
|
| PRK03846 |
PRK03846 |
adenylylsulfate kinase; Provisional |
16-193 |
3.45e-96 |
|
adenylylsulfate kinase; Provisional
Pssm-ID: 179661 Cd Length: 198 Bit Score: 277.98 E-value: 3.45e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032932144 16 TREDKEELLGQHSVMIWFTGLSGSGKSTIAIALERELHKRGLLCRILDGDNIRSGINNNLGFSETDRVENIRRIAEVSKL 95
Cdd:PRK03846 12 TKAQREQLHGHKGVVLWFTGLSGSGKSTVAGALEEALHELGVSTYLLDGDNVRHGLCSDLGFSDADRKENIRRVGEVAKL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032932144 96 FLDSGIITIAAFISPNNDIREMAANIIGKDDFLEVFVSTPLEECEKRDVKGLYAKARKGEIQNFTGISAPFEVPEHPALA 175
Cdd:PRK03846 92 MVDAGLVVLTAFISPHRAERQMVRERLGEGEFIEVFVDTPLAICEARDPKGLYKKARAGEIRNFTGIDSVYEAPESPEIH 171
|
170
....*....|....*...
gi 2032932144 176 LDTSKLSLEESVNRLLEM 193
Cdd:PRK03846 172 LDTGEQLVTNLVEQLLDY 189
|
|
| APS_kinase |
pfam01583 |
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3 ... |
28-180 |
1.12e-87 |
|
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: 254.55 E-value: 1.12e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032932144 28 SVMIWFTGLSGSGKSTIAIALERELHKRGLLCRILDGDNIRSGINNNLGFSETDRVENIRRIAEVSKLFLDSGIITIAAF 107
Cdd:pfam01583 2 GCTIWLTGLSGAGKSTIANALERKLFEQGRSVYVLDGDNVRHGLNKDLGFSEEDRTENIRRIGEVAKLFADAGLIVITAF 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2032932144 108 ISPNNDIREMAANIIGKDDFLEVFVSTPLEECEKRDVKGLYAKARKGEIQNFTGISAPFEVPEHPALALDTSK 180
Cdd:pfam01583 82 ISPYREDREQARELHEEGKFIEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDSPYEAPENPELVLDTDK 154
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
16-197 |
1.63e-85 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 264.48 E-value: 1.63e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032932144 16 TREDKEELLGQHSVMIWFTGLSGSGKSTIAIALERELHKRGLLCRILDGDNIRSGINNNLGFSETDRVENIRRIAEVSKL 95
Cdd:PRK05506 448 SREARAARKGQKPATVWFTGLSGSGKSTIANLVERRLHALGRHTYLLDGDNVRHGLNRDLGFSDADRVENIRRVAEVARL 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032932144 96 FLDSGIITIAAFISPNNDIREMAANIIGKDDFLEVFVSTPLEECEKRDVKGLYAKARKGEIQNFTGISAPFEVPEHPALA 175
Cdd:PRK05506 528 MADAGLIVLVSFISPFREERELARALHGEGEFVEVFVDTPLEVCEARDPKGLYAKARAGEIKNFTGIDSPYEAPENPELR 607
|
170 180
....*....|....*....|..
gi 2032932144 176 LDTSKLSLEESVNRLLEMVLPK 197
Cdd:PRK05506 608 LDTTGRSPEELAEQVLELLRRR 629
|
|
| apsK |
TIGR00455 |
adenylyl-sulfate kinase; This protein, adenylylsulfate kinase, is often found as a fusion ... |
15-194 |
1.17e-82 |
|
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: 243.14 E-value: 1.17e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032932144 15 MTREDKEELLGQHSVMIWFTGLSGSGKSTIAIALERELHKRGLLCRILDGDNIRSGINNNLGFSETDRVENIRRIAEVSK 94
Cdd:TIGR00455 5 ITKDERQALNGHRGVVIWLTGLSGSGKSTIANALEKKLESKGYRVYVLDGDNVRHGLNKDLGFSEEDRKENIRRIGEVAK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032932144 95 LFLDSGIITIAAFISPNNDIREMAANIIGKDDFLEVFVSTPLEECEKRDVKGLYAKARKGEIQNFTGISAPFEVPEHPAL 174
Cdd:TIGR00455 85 LFVRNGIIVITSFISPYRADRQMVRELIEKGEFIEVFVDCPLEVCEQRDPKGLYKKARNGEIKGFTGIDSPYEAPENPEV 164
|
170 180
....*....|....*....|
gi 2032932144 175 ALDTSKLSLEESVNRLLEMV 194
Cdd:TIGR00455 165 VLDTDQNDREECVGQIIEKL 184
|
|
| PRK00889 |
PRK00889 |
adenylylsulfate kinase; Provisional |
26-192 |
5.13e-71 |
|
adenylylsulfate kinase; Provisional
Pssm-ID: 179157 Cd Length: 175 Bit Score: 213.34 E-value: 5.13e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032932144 26 QHSVMIWFTGLSGSGKSTIAIALERELHKRGLLCRILDGDNIRSGINNNLGFSETDRVENIRRIAEVSKLFLDSGIITIA 105
Cdd:PRK00889 2 QRGVTVWFTGLSGAGKTTIARALAEKLREAGYPVEVLDGDAVRTNLSKGLGFSKEDRDTNIRRIGFVANLLTRHGVIVLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032932144 106 AFISPNNDIR-EMAANIIgkdDFLEVFVSTPLEECEKRDVKGLYAKARKGEIQNFTGISAPFEVPEHPALALDTSKLSLE 184
Cdd:PRK00889 82 SAISPYRETReEVRANIG---NFLEVFVDAPLEVCEQRDVKGLYAKARAGEIKHFTGIDDPYEPPLNPEVECRTDLESLE 158
|
....*...
gi 2032932144 185 ESVNRLLE 192
Cdd:PRK00889 159 ESVDKVLQ 166
|
|
| PRK05537 |
PRK05537 |
bifunctional sulfate adenylyltransferase/adenylylsulfate kinase; |
31-191 |
3.10e-56 |
|
bifunctional sulfate adenylyltransferase/adenylylsulfate kinase;
Pssm-ID: 180124 [Multi-domain] Cd Length: 568 Bit Score: 186.42 E-value: 3.10e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032932144 31 IWFTGLSGSGKSTIAIALE-RELHKRGLLCRILDGDNIRSGINNNLGFSETDRVENIRRIAEVSKLFLDSGIITIAAFIS 109
Cdd:PRK05537 395 VFFTGLSGAGKSTIAKALMvKLMEMRGRPVTLLDGDVVRKHLSSELGFSKEDRDLNILRIGFVASEITKNGGIAICAPIA 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032932144 110 PNNDIREMAANIIGKDD-FLEVFVSTPLEECEKRDVKGLYAKARKGEIQNFTGISAPFEVPEHPALALDTSKLSLEESVN 188
Cdd:PRK05537 475 PYRATRREVREMIEAYGgFIEVHVATPLEVCEQRDRKGLYAKAREGKIKGFTGISDPYEPPANPELVIDTTNVTPDECAH 554
|
...
gi 2032932144 189 RLL 191
Cdd:PRK05537 555 KIL 557
|
|
| PRK05541 |
PRK05541 |
adenylylsulfate kinase; Provisional |
31-197 |
1.43e-29 |
|
adenylylsulfate kinase; Provisional
Pssm-ID: 235498 Cd Length: 176 Bit Score: 107.45 E-value: 1.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032932144 31 IWFTGLSGSGKSTIAIALERELHKRGLLCRILDGDNIRSgINNNLGFSETDRVENIRRIAEVSKLFLDSGIITIAAFISP 110
Cdd:PRK05541 10 IWITGLAGSGKTTIAKALYERLKLKYSNVIYLDGDELRE-ILGHYGYDKQSRIEMALKRAKLAKFLADQGMIVIVTTISM 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032932144 111 NNDIREMAANIIGKddFLEVFVSTPLEECEKRDVKGLYAKARKGEIQNFTGISAPFEVPEhPALALDTSKL-SLEESVNR 189
Cdd:PRK05541 89 FDEIYAYNRKHLPN--YFEVYLKCDMEELIRRDQKGLYTKALKGEIKNVVGVDIPFDEPK-ADLVIDNSCRtSLDEKVDL 165
|
....*...
gi 2032932144 190 LLEMVLPK 197
Cdd:PRK05541 166 ILNKLKLR 173
|
|
| COG0645 |
COG0645 |
Predicted kinase, contains AAA domain [General function prediction only]; |
30-190 |
9.69e-12 |
|
Predicted kinase, contains AAA domain [General function prediction only];
Pssm-ID: 440410 [Multi-domain] Cd Length: 164 Bit Score: 60.70 E-value: 9.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032932144 30 MIWFTGLSGSGKSTIAIALERELHkrgllCRILDGDNIR-----SGINNNLGFSE-TDRVEniRRIAEVSKLFLDSGIIT 103
Cdd:COG0645 1 LILVCGLPGSGKSTLARALAERLG-----AVRLRSDVVRkrlfgAGLAPLERSPEaTARTY--ARLLALARELLAAGRSV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032932144 104 I--AAFISPnnDIREMAANIIGK--DDFLEVFVSTPLEEC----EKRDVKGLYAKARKGEIQNFTGISAPFEVPEHPALA 175
Cdd:COG0645 74 IldATFLRR--AQREAFRALAEEagAPFVLIWLDAPEEVLrerlEARNAEGGDSDATWEVLERQLAFEEPLTEDEGFLLV 151
|
170
....*....|....*
gi 2032932144 176 LDTSKlsLEESVNRL 190
Cdd:COG0645 152 VDTSG--LEEALAAL 164
|
|
| AAA_33 |
pfam13671 |
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ... |
30-185 |
1.54e-08 |
|
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the AAA superfamily. Many of the proteins in this family are just short fragments so there is no Walker B motif.
Pssm-ID: 463952 [Multi-domain] Cd Length: 143 Bit Score: 51.54 E-value: 1.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032932144 30 MIWFTGLSGSGKSTIAIALERELHkrgllCRILDGDNIRSGINNNLGFSETDRVENI----RRIAEVSKLFLDSGIITIA 105
Cdd:pfam13671 1 LILLVGLPGSGKSTLARRLLEELG-----AVRLSSDDERKRLFGEGRPSISYYTDATdrtyERLHELARIALRAGRPVIL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032932144 106 AFisPNNDIREMAA--NIIGKDDFLE--VFVSTPLEECEKRDVkglyAKARKGEiqnftgisAPFEVPEHpalALDTSKL 181
Cdd:pfam13671 76 DA--TNLRRDERARllALAREYGVPVriVVFEAPEEVLRERLA----ARARAGG--------DPSDVPEE---VLDRQKA 138
|
....
gi 2032932144 182 SLEE 185
Cdd:pfam13671 139 RFEP 142
|
|
| GntK |
cd02021 |
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting ... |
34-154 |
1.31e-04 |
|
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: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032932144 34 TGLSGSGKSTIAIALERELHkrgllCRILDGDNIRSGIN-----NNLGFSETDRVENIRRIAE--VSKLFLDSGIITIAA 106
Cdd:cd02021 5 MGVSGSGKSTVGKALAERLG-----APFIDGDDLHPPANiakmaAGIPLNDEDRWPWLQALTDalLAKLASAGEGVVVAC 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2032932144 107 fiSPNNDI-REMAANIIGKDDFLEVFVSTPLEECEKRDvkglyaKARKG 154
Cdd:cd02021 80 --SALKRIyRDILRGGAANPRVRFVHLDGPREVLAERL------AARKG 120
|
|
| GntK |
COG3265 |
Gluconate kinase [Carbohydrate transport and metabolism]; Gluconate kinase is part of the ... |
29-91 |
1.68e-04 |
|
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: 40.50 E-value: 1.68e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2032932144 29 VMiwftGLSGSGKSTIAIALERELHkrgllCRILDGD------NI---RSGInnnlGFSETDRVENIRRIAE 91
Cdd:COG3265 6 VM----GVSGSGKSTVGQALAERLG-----WPFIDGDdfhppaNIakmAAGI----PLTDEDRAPWLEALAD 64
|
|
| Cytidylate_kin |
pfam02224 |
Cytidylate kinase; Cytidylate kinase EC:2.7.4.14 catalyzes the phosphorylation of cytidine 5 ... |
35-194 |
6.26e-04 |
|
Cytidylate kinase; Cytidylate kinase EC:2.7.4.14 catalyzes the phosphorylation of cytidine 5'-monophosphate (dCMP) to cytidine 5'-diphosphate (dCDP) in the presence of ATP or GTP.
Pssm-ID: 280401 [Multi-domain] Cd Length: 211 Bit Score: 39.21 E-value: 6.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032932144 35 GLSGSGKSTIAIALERELHKR----GLLCRILDGDNIRSGINNnlgFSETDRVENIRRI-------------AEVSKLFL 97
Cdd:pfam02224 5 GPSGSGKSTVARILARKLGYKyldtGAMYRALALAALRQKVDL---TDEDALAELASEVdisfghtevflngEDVSSEIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032932144 98 DSGIITIAAFISPNNDIREMA----------ANII--GKDDFLEVFVSTPL--------EECEKRDVKGLYAkarKGEIQ 157
Cdd:pfam02224 82 TDEVAQAASQVAAIPAVRARLnklqrqlaknGNIVmeGRDIGTVVFPDAEVkifltaspEERAKRRYKQLQA---KGLSV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2032932144 158 NFTGISA---------------PFEVPEHpALALDTSKLSLEESVNRLLEMV 194
Cdd:pfam02224 159 DFEELLAeikrrdkrdseravgPLKPAPD-ALIIDTSKLTIEEVVEKILELI 209
|
|
| COG4639 |
COG4639 |
Predicted kinase [General function prediction only]; |
29-143 |
7.75e-04 |
|
Predicted kinase [General function prediction only];
Pssm-ID: 443677 [Multi-domain] Cd Length: 145 Bit Score: 38.27 E-value: 7.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032932144 29 VMIwftGLSGSGKSTIAialeRELHKRGLlcrILDGDNIRSGINNNLG-FSETDRVEN-IRRIAEVsklFLDSGIITI-- 104
Cdd:COG4639 6 VLI---GLPGSGKSTFA----RRLFAPTE---VVSSDDIRALLGGDENdQSAWGDVFQlAHEIARA---RLRAGRLTVvd 72
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2032932144 105 AAFISPnnDIREMAANIIGKDDFL--EVFVSTPLEECEKRD 143
Cdd:COG4639 73 ATNLQR--EARRRLLALARAYGALvvAVVLDVPLEVCLARN 111
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
33-136 |
1.10e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 38.12 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032932144 33 FTGLSGSGKSTIAIALERELHKRGLLCRILDGDNIRSGI----------NNNLGFSETDRVENIRRIAEVSK---LFLDs 99
Cdd:smart00382 7 IVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVldqllliivgGKKASGSGELRLRLALALARKLKpdvLILD- 85
|
90 100 110
....*....|....*....|....*....|....*..
gi 2032932144 100 giiTIAAFISPNNDIREMAANIIGKDDFLEVFVSTPL 136
Cdd:smart00382 86 ---EITSLLDAEQEALLLLLEELRLLLLLKSEKNLTV 119
|
|
| pseT |
PHA02530 |
polynucleotide kinase; Provisional |
31-145 |
3.85e-03 |
|
polynucleotide kinase; Provisional
Pssm-ID: 222856 [Multi-domain] Cd Length: 300 Bit Score: 37.31 E-value: 3.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032932144 31 IWFT-GLSGSGKSTIAialeRELHKRGLLCRILDGDNIRSGINNNLGFSE-------TDRVENIRRIAEVSKLFLDSGII 102
Cdd:PHA02530 4 IILTvGVPGSGKSTWA----REFAAKNPKAVNVNRDDLRQSLFGHGEWGEykftkekEDLVTKAQEAAALAALKSGKSVI 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2032932144 103 TIAAFISPNNDI--REMAANIigKDDFLEVFVSTPLEECEKRDVK 145
Cdd:PHA02530 80 ISDTNLNPERRRkwKELAKEL--GAEFEEKVFDVPVEELVKRNRK 122
|
|
| |
