|
Name |
Accession |
Description |
Interval |
E-value |
| PRK03846 |
PRK03846 |
adenylylsulfate kinase; Provisional |
5-201 |
1.78e-152 |
|
adenylylsulfate kinase; Provisional
Pssm-ID: 179661 Cd Length: 198 Bit Score: 420.12 E-value: 1.78e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004547 5 DENVVWHAHPVTQQQREQHHGHRGVVLWFTGLSGSGKSTVAGALEEALHERGVSTYLLDGDNVRHGLCSDLGFSDEDRKE 84
Cdd:PRK03846 1 DENIVWHQHPVTKAQREQLHGHKGVVLWFTGLSGSGKSTVAGALEEALHELGVSTYLLDGDNVRHGLCSDLGFSDADRKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004547 85 NIRRVGEVARLMVDAGLVVLTAFISPHRAERQMVRERLGEGRFIEVFVDTPLAICEARDPKGLYKKARAGELRNFTGIDS 164
Cdd:PRK03846 81 NIRRVGEVAKLMVDAGLVVLTAFISPHRAERQMVRERLGEGEFIEVFVDTPLAICEARDPKGLYKKARAGEIRNFTGIDS 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 489004547 165 VYEAPEKAEIHLD-GEQLVTNLVHQLLDLLQQSDIIRS 201
Cdd:PRK03846 161 VYEAPESPEIHLDtGEQLVTNLVEQLLDYLRQRDIIRS 198
|
|
| CysC |
COG0529 |
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ... |
13-200 |
4.07e-127 |
|
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: 355.55 E-value: 4.07e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004547 13 HPVTQQQREQHHGHRGVVLWFTGLSGSGKSTVAGALEEALHERGVSTYLLDGDNVRHGLCSDLGFSDEDRKENIRRVGEV 92
Cdd:COG0529 1 SAVTREERAALKGQKGFVVWFTGLSGSGKSTLANALERRLFERGRHVYLLDGDNVRHGLNKDLGFSKEDRDENIRRIGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004547 93 ARLMVDAGLVVLTAFISPHRAERQMVRERLGEGRFIEVFVDTPLAICEARDPKGLYKKARAGELRNFTGIDSVYEAPEKA 172
Cdd:COG0529 81 AKLLADAGLIVLVAFISPYRADREEARELIGEGEFIEVYVDTPLEVCEARDPKGLYAKARAGEIKNFTGIDDPYEAPENP 160
|
170 180
....*....|....*....|....*....
gi 489004547 173 EIHLDGEQL-VTNLVHQLLDLLQQSDIIR 200
Cdd:COG0529 161 ELVLDTDKEsVEESVEKILAYLEERGYIS 189
|
|
| apsK |
TIGR00455 |
adenylyl-sulfate kinase; This protein, adenylylsulfate kinase, is often found as a fusion ... |
10-193 |
2.59e-111 |
|
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: 315.56 E-value: 2.59e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004547 10 WHAHpVTQQQREQHHGHRGVVLWFTGLSGSGKSTVAGALEEALHERGVSTYLLDGDNVRHGLCSDLGFSDEDRKENIRRV 89
Cdd:TIGR00455 1 WHPA-ITKDERQALNGHRGVVIWLTGLSGSGKSTIANALEKKLESKGYRVYVLDGDNVRHGLNKDLGFSEEDRKENIRRI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004547 90 GEVARLMVDAGLVVLTAFISPHRAERQMVRERLGEGRFIEVFVDTPLAICEARDPKGLYKKARAGELRNFTGIDSVYEAP 169
Cdd:TIGR00455 80 GEVAKLFVRNGIIVITSFISPYRADRQMVRELIEKGEFIEVFVDCPLEVCEQRDPKGLYKKARNGEIKGFTGIDSPYEAP 159
|
170 180
....*....|....*....|....*
gi 489004547 170 EKAEIHLD-GEQLVTNLVHQLLDLL 193
Cdd:TIGR00455 160 ENPEVVLDtDQNDREECVGQIIEKL 184
|
|
| APSK |
cd02027 |
Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5 ... |
30-177 |
3.53e-105 |
|
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: 298.62 E-value: 3.53e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004547 30 VLWFTGLSGSGKSTVAGALEEALHERGVSTYLLDGDNVRHGLCSDLGFSDEDRKENIRRVGEVARLMVDAGLVVLTAFIS 109
Cdd:cd02027 1 VIWLTGLSGSGKSTIARALEEKLFQRGRPVYVLDGDNVRHGLNKDLGFSREDREENIRRIAEVAKLLADAGLIVIAAFIS 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489004547 110 PHRAERQMVRERLGEGRFIEVFVDTPLAICEARDPKGLYKKARAGELRNFTGIDSVYEAPEKAEIHLD 177
Cdd:cd02027 81 PYREDREAARKIIGGGDFLEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDDPYEAPENPDLVLD 148
|
|
| APS_kinase |
pfam01583 |
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3 ... |
27-177 |
2.12e-103 |
|
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: 294.61 E-value: 2.12e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004547 27 RGVVLWFTGLSGSGKSTVAGALEEALHERGVSTYLLDGDNVRHGLCSDLGFSDEDRKENIRRVGEVARLMVDAGLVVLTA 106
Cdd:pfam01583 1 RGCTIWLTGLSGAGKSTIANALERKLFEQGRSVYVLDGDNVRHGLNKDLGFSEEDRTENIRRIGEVAKLFADAGLIVITA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489004547 107 FISPHRAERQMVRERLGEGRFIEVFVDTPLAICEARDPKGLYKKARAGELRNFTGIDSVYEAPEKAEIHLD 177
Cdd:pfam01583 81 FISPYREDREQARELHEEGKFIEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDSPYEAPENPELVLD 151
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK03846 |
PRK03846 |
adenylylsulfate kinase; Provisional |
5-201 |
1.78e-152 |
|
adenylylsulfate kinase; Provisional
Pssm-ID: 179661 Cd Length: 198 Bit Score: 420.12 E-value: 1.78e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004547 5 DENVVWHAHPVTQQQREQHHGHRGVVLWFTGLSGSGKSTVAGALEEALHERGVSTYLLDGDNVRHGLCSDLGFSDEDRKE 84
Cdd:PRK03846 1 DENIVWHQHPVTKAQREQLHGHKGVVLWFTGLSGSGKSTVAGALEEALHELGVSTYLLDGDNVRHGLCSDLGFSDADRKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004547 85 NIRRVGEVARLMVDAGLVVLTAFISPHRAERQMVRERLGEGRFIEVFVDTPLAICEARDPKGLYKKARAGELRNFTGIDS 164
Cdd:PRK03846 81 NIRRVGEVAKLMVDAGLVVLTAFISPHRAERQMVRERLGEGEFIEVFVDTPLAICEARDPKGLYKKARAGEIRNFTGIDS 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 489004547 165 VYEAPEKAEIHLD-GEQLVTNLVHQLLDLLQQSDIIRS 201
Cdd:PRK03846 161 VYEAPESPEIHLDtGEQLVTNLVEQLLDYLRQRDIIRS 198
|
|
| CysC |
COG0529 |
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ... |
13-200 |
4.07e-127 |
|
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: 355.55 E-value: 4.07e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004547 13 HPVTQQQREQHHGHRGVVLWFTGLSGSGKSTVAGALEEALHERGVSTYLLDGDNVRHGLCSDLGFSDEDRKENIRRVGEV 92
Cdd:COG0529 1 SAVTREERAALKGQKGFVVWFTGLSGSGKSTLANALERRLFERGRHVYLLDGDNVRHGLNKDLGFSKEDRDENIRRIGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004547 93 ARLMVDAGLVVLTAFISPHRAERQMVRERLGEGRFIEVFVDTPLAICEARDPKGLYKKARAGELRNFTGIDSVYEAPEKA 172
Cdd:COG0529 81 AKLLADAGLIVLVAFISPYRADREEARELIGEGEFIEVYVDTPLEVCEARDPKGLYAKARAGEIKNFTGIDDPYEAPENP 160
|
170 180
....*....|....*....|....*....
gi 489004547 173 EIHLDGEQL-VTNLVHQLLDLLQQSDIIR 200
Cdd:COG0529 161 ELVLDTDKEsVEESVEKILAYLEERGYIS 189
|
|
| apsK |
TIGR00455 |
adenylyl-sulfate kinase; This protein, adenylylsulfate kinase, is often found as a fusion ... |
10-193 |
2.59e-111 |
|
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: 315.56 E-value: 2.59e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004547 10 WHAHpVTQQQREQHHGHRGVVLWFTGLSGSGKSTVAGALEEALHERGVSTYLLDGDNVRHGLCSDLGFSDEDRKENIRRV 89
Cdd:TIGR00455 1 WHPA-ITKDERQALNGHRGVVIWLTGLSGSGKSTIANALEKKLESKGYRVYVLDGDNVRHGLNKDLGFSEEDRKENIRRI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004547 90 GEVARLMVDAGLVVLTAFISPHRAERQMVRERLGEGRFIEVFVDTPLAICEARDPKGLYKKARAGELRNFTGIDSVYEAP 169
Cdd:TIGR00455 80 GEVAKLFVRNGIIVITSFISPYRADRQMVRELIEKGEFIEVFVDCPLEVCEQRDPKGLYKKARNGEIKGFTGIDSPYEAP 159
|
170 180
....*....|....*....|....*
gi 489004547 170 EKAEIHLD-GEQLVTNLVHQLLDLL 193
Cdd:TIGR00455 160 ENPEVVLDtDQNDREECVGQIIEKL 184
|
|
| APSK |
cd02027 |
Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5 ... |
30-177 |
3.53e-105 |
|
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: 298.62 E-value: 3.53e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004547 30 VLWFTGLSGSGKSTVAGALEEALHERGVSTYLLDGDNVRHGLCSDLGFSDEDRKENIRRVGEVARLMVDAGLVVLTAFIS 109
Cdd:cd02027 1 VIWLTGLSGSGKSTIARALEEKLFQRGRPVYVLDGDNVRHGLNKDLGFSREDREENIRRIAEVAKLLADAGLIVIAAFIS 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489004547 110 PHRAERQMVRERLGEGRFIEVFVDTPLAICEARDPKGLYKKARAGELRNFTGIDSVYEAPEKAEIHLD 177
Cdd:cd02027 81 PYREDREAARKIIGGGDFLEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDDPYEAPENPDLVLD 148
|
|
| APS_kinase |
pfam01583 |
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3 ... |
27-177 |
2.12e-103 |
|
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: 294.61 E-value: 2.12e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004547 27 RGVVLWFTGLSGSGKSTVAGALEEALHERGVSTYLLDGDNVRHGLCSDLGFSDEDRKENIRRVGEVARLMVDAGLVVLTA 106
Cdd:pfam01583 1 RGCTIWLTGLSGAGKSTIANALERKLFEQGRSVYVLDGDNVRHGLNKDLGFSEEDRTENIRRIGEVAKLFADAGLIVITA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489004547 107 FISPHRAERQMVRERLGEGRFIEVFVDTPLAICEARDPKGLYKKARAGELRNFTGIDSVYEAPEKAEIHLD 177
Cdd:pfam01583 81 FISPYREDREQARELHEEGKFIEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDSPYEAPENPELVLD 151
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
3-199 |
4.01e-103 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 309.94 E-value: 4.01e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004547 3 QHDENVVWHAHPVTQQQREQHHGHRGVVLWFTGLSGSGKSTVAGALEEALHERGVSTYLLDGDNVRHGLCSDLGFSDEDR 82
Cdd:PRK05506 435 RRATNVHWQASDVSREARAARKGQKPATVWFTGLSGSGKSTIANLVERRLHALGRHTYLLDGDNVRHGLNRDLGFSDADR 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004547 83 KENIRRVGEVARLMVDAGLVVLTAFISPHRAERQMVRERLGEGRFIEVFVDTPLAICEARDPKGLYKKARAGELRNFTGI 162
Cdd:PRK05506 515 VENIRRVAEVARLMADAGLIVLVSFISPFREERELARALHGEGEFVEVFVDTPLEVCEARDPKGLYAKARAGEIKNFTGI 594
|
170 180 190
....*....|....*....|....*....|....*...
gi 489004547 163 DSVYEAPEKAEIHLDGEQL-VTNLVHQLLDLLQQSDII 199
Cdd:PRK05506 595 DSPYEAPENPELRLDTTGRsPEELAEQVLELLRRRGAI 632
|
|
| PRK00889 |
PRK00889 |
adenylylsulfate kinase; Provisional |
26-192 |
2.51e-74 |
|
adenylylsulfate kinase; Provisional
Pssm-ID: 179157 Cd Length: 175 Bit Score: 221.82 E-value: 2.51e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004547 26 HRGVVLWFTGLSGSGKSTVAGALEEALHERGVSTYLLDGDNVRHGLCSDLGFSDEDRKENIRRVGEVARLMVDAGLVVLT 105
Cdd:PRK00889 2 QRGVTVWFTGLSGAGKTTIARALAEKLREAGYPVEVLDGDAVRTNLSKGLGFSKEDRDTNIRRIGFVANLLTRHGVIVLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004547 106 AFISPHRAERQMVRERLgeGRFIEVFVDTPLAICEARDPKGLYKKARAGELRNFTGIDSVYEAPEKAEIHL--DGEQL-- 181
Cdd:PRK00889 82 SAISPYRETREEVRANI--GNFLEVFVDAPLEVCEQRDVKGLYAKARAGEIKHFTGIDDPYEPPLNPEVECrtDLESLee 159
|
170
....*....|..
gi 489004547 182 -VTNLVHQLLDL 192
Cdd:PRK00889 160 sVDKVLQKLEEL 171
|
|
| PRK05537 |
PRK05537 |
bifunctional sulfate adenylyltransferase/adenylylsulfate kinase; |
10-200 |
1.02e-62 |
|
bifunctional sulfate adenylyltransferase/adenylylsulfate kinase;
Pssm-ID: 180124 [Multi-domain] Cd Length: 568 Bit Score: 203.75 E-value: 1.02e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004547 10 WHAHP-VTQQQREQH---HGhRGVVLWFTGLSGSGKSTVAGALEEALHE-RGVSTYLLDGDNVRHGLCSDLGFSDEDRKE 84
Cdd:PRK05537 371 WFSFPeVVAELRRTYpprHK-QGFTVFFTGLSGAGKSTIAKALMVKLMEmRGRPVTLLDGDVVRKHLSSELGFSKEDRDL 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004547 85 NIRRVGEVARLMVDAGLVVLTAFISPHRAERQMVRERLGE-GRFIEVFVDTPLAICEARDPKGLYKKARAGELRNFTGID 163
Cdd:PRK05537 450 NILRIGFVASEITKNGGIAICAPIAPYRATRREVREMIEAyGGFIEVHVATPLEVCEQRDRKGLYAKAREGKIKGFTGIS 529
|
170 180 190
....*....|....*....|....*....|....*...
gi 489004547 164 SVYEAPEKAEIHLDGEQL-VTNLVHQLLDLLQQSDIIR 200
Cdd:PRK05537 530 DPYEPPANPELVIDTTNVtPDECAHKILLYLEEKGYLR 567
|
|
| PRK05541 |
PRK05541 |
adenylylsulfate kinase; Provisional |
28-195 |
1.79e-29 |
|
adenylylsulfate kinase; Provisional
Pssm-ID: 235498 Cd Length: 176 Bit Score: 107.45 E-value: 1.79e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004547 28 GVVLWFTGLSGSGKSTVAGALEEALHERGVSTYLLDGDNVRHGLCSDlGFSDEDRKENIRRVGEVARLMVDAGLVVLTAF 107
Cdd:PRK05541 7 GYVIWITGLAGSGKTTIAKALYERLKLKYSNVIYLDGDELREILGHY-GYDKQSRIEMALKRAKLAKFLADQGMIVIVTT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004547 108 ISPHRAERQMVRERLgeGRFIEVFVDTPLAICEARDPKGLYKKARAGELRNFTGIDSVYEAPeKAEIHLDGEqLVTNLVH 187
Cdd:PRK05541 86 ISMFDEIYAYNRKHL--PNYFEVYLKCDMEELIRRDQKGLYTKALKGEIKNVVGVDIPFDEP-KADLVIDNS-CRTSLDE 161
|
....*...
gi 489004547 188 QLLDLLQQ 195
Cdd:PRK05541 162 KVDLILNK 169
|
|
| COG0645 |
COG0645 |
Predicted kinase, contains AAA domain [General function prediction only]; |
30-142 |
1.54e-10 |
|
Predicted kinase, contains AAA domain [General function prediction only];
Pssm-ID: 440410 [Multi-domain] Cd Length: 164 Bit Score: 57.23 E-value: 1.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004547 30 VLWFTGLSGSGKSTVAGALEEALheRGVstyLLDGDNVRHGLCSDLGFSDEDRKENIRRV----GEVARLMVDAGL-VVL 104
Cdd:COG0645 1 LILVCGLPGSGKSTLARALAERL--GAV---RLRSDVVRKRLFGAGLAPLERSPEATARTyarlLALARELLAAGRsVIL 75
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 489004547 105 TA-FISphRAERQMVRERLGE--GRFIEVFVDTPLAICEAR 142
Cdd:COG0645 76 DAtFLR--RAQREAFRALAEEagAPFVLIWLDAPEEVLRER 114
|
|
| GntK |
cd02021 |
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting ... |
34-170 |
7.63e-09 |
|
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: 52.25 E-value: 7.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004547 34 TGLSGSGKSTVAGALEEALHergvSTYlLDGDNVRHGLC-----SDLGFSDEDRKENIRRVGE--VARLMVDAGLVVLTA 106
Cdd:cd02021 5 MGVSGSGKSTVGKALAERLG----APF-IDGDDLHPPANiakmaAGIPLNDEDRWPWLQALTDalLAKLASAGEGVVVAC 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489004547 107 -FISphRAERQMVRERLGEGRFIEVFVDTPLAICEARDpkglykKARAGELRNFTGIDSVYEAPE 170
Cdd:cd02021 80 sALK--RIYRDILRGGAANPRVRFVHLDGPREVLAERL------AARKGHFMPADLLDSQFETLE 136
|
|
| AAA_33 |
pfam13671 |
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ... |
30-142 |
9.74e-09 |
|
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: 51.93 E-value: 9.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004547 30 VLWFTGLSGSGKSTVAGALEEALHergvsTYLLDGDNVRHGLCSDLGFSDEDRKENI----RRVGEVARLMVDAGL-VVL 104
Cdd:pfam13671 1 LILLVGLPGSGKSTLARRLLEELG-----AVRLSSDDERKRLFGEGRPSISYYTDATdrtyERLHELARIALRAGRpVIL 75
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 489004547 105 TA-FISP-HRAERQMVRERLGEgRFIEVFVDTPLAICEAR 142
Cdd:pfam13671 76 DAtNLRRdERARLLALAREYGV-PVRIVVFEAPEEVLRER 114
|
|
| GntK |
COG3265 |
Gluconate kinase [Carbohydrate transport and metabolism]; Gluconate kinase is part of the ... |
35-194 |
4.50e-06 |
|
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: 44.73 E-value: 4.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004547 35 GLSGSGKSTVAGALEEALHergvsTYLLDGD------NV---RHGlcsdLGFSDEDRKENIRRVGEVARLMVDAGLVVLT 105
Cdd:COG3265 8 GVSGSGKSTVGQALAERLG-----WPFIDGDdfhppaNIakmAAG----IPLTDEDRAPWLEALADAIAAHLAAGEGAVL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004547 106 AFISPHRAERQMVRERLGEGRFieVFVDTPLAICEARdpkgLykKARAGELRNFTGIDS---VYEAPEKAE--IHLDGEQ 180
Cdd:COG3265 79 ACSALKRSYRDRLREGNPDVRF--VYLDGSRELIAER----L--AARKGHFMPASLLDSqfaTLEPPGPDEdaIVVDIDQ 150
|
170
....*....|....
gi 489004547 181 LVTNLVHQLLDLLQ 194
Cdd:COG3265 151 PPEEIVAQILAALG 164
|
|
| Mrp |
COG0489 |
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ... |
35-135 |
1.75e-05 |
|
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440255 [Multi-domain] Cd Length: 289 Bit Score: 44.02 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004547 35 GLSGSGKSTVAGALEEALHERGVSTYLLDGDNVRHGLCSDLGFSDE----DRKENIRRVGEVARLMVDAGLVVLTA-FIS 109
Cdd:COG0489 100 GKGGEGKSTVAANLALALAQSGKRVLLIDADLRGPSLHRMLGLENRpglsDVLAGEASLEDVIQPTEVEGLDVLPAgPLP 179
|
90 100 110
....*....|....*....|....*....|....
gi 489004547 110 PHRAERqMVRERLGEgrFIE--------VFVDTP 135
Cdd:COG0489 180 PNPSEL-LASKRLKQ--LLEelrgrydyVIIDTP 210
|
|
| COG4639 |
COG4639 |
Predicted kinase [General function prediction only]; |
35-143 |
1.63e-04 |
|
Predicted kinase [General function prediction only];
Pssm-ID: 443677 [Multi-domain] Cd Length: 145 Bit Score: 40.20 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004547 35 GLSGSGKSTVAGALEEAlhergvsTYLLDGDNVRHGLcsdlgFSDEDRKENIRRVGEVARLMVDAGL-----VVLTAfIS 109
Cdd:COG4639 9 GLPGSGKSTFARRLFAP-------TEVVSSDDIRALL-----GGDENDQSAWGDVFQLAHEIARARLragrlTVVDA-TN 75
|
90 100 110
....*....|....*....|....*....|....*.
gi 489004547 110 PHRAERQMVRERLGE--GRFIEVFVDTPLAICEARD 143
Cdd:COG4639 76 LQREARRRLLALARAygALVVAVVLDVPLEVCLARN 111
|
|
| SIMIBI |
cd01983 |
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ... |
33-106 |
4.53e-04 |
|
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal recognition particle, MinD, and BioD), consists of signal recognition particle (SRP) GTPases, the assemblage of MinD-like ATPases, which are involved in protein localization, chromosome partitioning, and membrane transport, and a group of metabolic enzymes with kinase or related phosphate transferase activity. Functionally, proteins in this superfamily use the energy from hydrolysis of NTP to transfer electron or ion.
Pssm-ID: 349751 [Multi-domain] Cd Length: 107 Bit Score: 38.18 E-value: 4.53e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489004547 33 FTG-LSGSGKSTVAGALEEALHERGVSTYLLDGDNVrhgLCSDLGFSDEDRKENIRRVGEVARLMVDAGLVVLTA 106
Cdd:cd01983 5 VTGgKGGVGKTTLAAALAVALAAKGYKVLLIDLDDY---VLIDGGGGLETGLLLGTIVALLALKKADEVIVVVDP 76
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
23-104 |
1.52e-03 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 37.32 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004547 23 HHGHRGVVLwFTGLSGSGKSTVAGALEEALHERGVSTYLLD------GDNVRHGLCSDLGFSDEDRKENIRRVGEVARLM 96
Cdd:pfam13401 1 IRFGAGILV-LTGESGTGKTTLLRRLLEQLPEVRDSVVFVDlpsgtsPKDLLRALLRALGLPLSGRLSKEELLAALQQLL 79
|
....*...
gi 489004547 97 VDAGLVVL 104
Cdd:pfam13401 80 LALAVAVV 87
|
|
| AAA_18 |
pfam13238 |
AAA domain; |
32-116 |
2.01e-03 |
|
AAA domain;
Pssm-ID: 433052 [Multi-domain] Cd Length: 128 Bit Score: 37.02 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004547 32 WFTGLSGSGKSTVAGALEEALHERGVStylldGDNVRHGLC--SDLGFSDEDRKENIRRVGEVARL------MVDAGLVV 103
Cdd:pfam13238 2 LITGTPGVGKTTLAKELSKRLGFGDNV-----RDLALENGLvlGDDPETRESKRLDEDKLDRLLDLleenaaLEEGGNLI 76
|
90
....*....|...
gi 489004547 104 LTAFISPHRAERQ 116
Cdd:pfam13238 77 IDGHLAELEPERA 89
|
|
| KTI12 |
pfam08433 |
Chromatin associated protein KTI12; This is a family of chromatin associated proteins which ... |
33-69 |
2.81e-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: 37.66 E-value: 2.81e-03
10 20 30
....*....|....*....|....*....|....*..
gi 489004547 33 FTGLSGSGKSTVAGALEEALHERGVSTYLLDGDNVRH 69
Cdd:pfam08433 4 LTGLPSSGKSTRAKQLAKYLEESNYDVIVISDESLGI 40
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
26-82 |
3.06e-03 |
|
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442498 [Multi-domain] Cd Length: 261 Bit Score: 37.46 E-value: 3.06e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489004547 26 HRGVVLwFTGLSGSGKSTVAGALEEALHERGVSTYL----LDGDNVRHGLCSDLGFSDEDR 82
Cdd:COG3267 42 GGGFVV-LTGEVGTGKTTLLRRLLERLPDDVKVAYIpnpqLSPAELLRAIADELGLEPKGA 101
|
|
| ParA |
COG1192 |
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ... |
38-135 |
6.09e-03 |
|
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein BcsQ [Cell cycle control, cell division, chromosome partitioning, Cell motility];
Pssm-ID: 440805 [Multi-domain] Cd Length: 253 Bit Score: 36.37 E-value: 6.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489004547 38 GSGKSTVAGALEEALHERGVSTYLLDGD---NVRHGlcsdLGFSDEDRKENI-------RRVGEVARLMVDAGLVVLTAF 107
Cdd:COG1192 12 GVGKTTTAVNLAAALARRGKRVLLIDLDpqgNLTSG----LGLDPDDLDPTLydlllddAPLEDAIVPTEIPGLDLIPAN 87
|
90 100 110
....*....|....*....|....*....|....*....
gi 489004547 108 ISPHRAERQMVRERLGEGRFIE-----------VFVDTP 135
Cdd:COG1192 88 IDLAGAEIELVSRPGRELRLKRalapladdydyILIDCP 126
|
|
| PRK07667 |
PRK07667 |
uridine kinase; Provisional |
24-66 |
9.48e-03 |
|
uridine kinase; Provisional
Pssm-ID: 169051 Cd Length: 193 Bit Score: 35.48 E-value: 9.48e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 489004547 24 HGHRGVVLWFTGLSGSGKSTVAGALEEALHERGVSTYLLDGDN 66
Cdd:PRK07667 13 HKENRFILGIDGLSRSGKTTFVANLKENMKQEGIPFHIFHIDD 55
|
|
|