|
Name |
Accession |
Description |
Interval |
E-value |
| CysC |
COG0529 |
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ... |
10-207 |
1.16e-109 |
|
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: 312.02 E-value: 1.16e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7387810 10 SALTRSERTELRNQRGLTIWLTGLSASGKSTLAVELEHQLvRDRRVHAYRLDGDNIRFGLNKDLGFSEADRNENIRRIAE 89
Cdd:COG0529 1 SAVTREERAALKGQKGFVVWFTGLSGSGKSTLANALERRL-FERGRHVYLLDGDNVRHGLNKDLGFSKEDRDENIRRIGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7387810 90 VAKLFADSNSIAITSFISPYRKDRDTARQLHEvatPGEetglpFVEVYVDVPVEVAEQRDPKGLYKKAREGVIKEFTGIS 169
Cdd:COG0529 80 VAKLLADAGLIVLVAFISPYRADREEARELIG---EGE-----FIEVYVDTPLEVCEARDPKGLYAKARAGEIKNFTGID 151
|
170 180 190
....*....|....*....|....*....|....*...
gi 7387810 170 APYEAPANPEVHVKNYELPVQDAVKQIIDYLDTKGYLP 207
Cdd:COG0529 152 DPYEAPENPELVLDTDKESVEESVEKILAYLEERGYIS 189
|
|
| PRK03846 |
PRK03846 |
adenylylsulfate kinase; Provisional |
2-208 |
2.15e-97 |
|
adenylylsulfate kinase; Provisional
Pssm-ID: 179661 Cd Length: 198 Bit Score: 281.44 E-value: 2.15e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7387810 2 STNITFHASALTRSERTELRNQRGLTIWLTGLSASGKSTLAVELEHQLVrDRRVHAYRLDGDNIRFGLNKDLGFSEADRN 81
Cdd:PRK03846 1 DENIVWHQHPVTKAQREQLHGHKGVVLWFTGLSGSGKSTVAGALEEALH-ELGVSTYLLDGDNVRHGLCSDLGFSDADRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7387810 82 ENIRRIAEVAKLFADSNSIAITSFISPYRKDRDTARQLHEvatPGEetglpFVEVYVDVPVEVAEQRDPKGLYKKAREGV 161
Cdd:PRK03846 80 ENIRRVGEVAKLMVDAGLVVLTAFISPHRAERQMVRERLG---EGE-----FIEVFVDTPLAICEARDPKGLYKKARAGE 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 7387810 162 IKEFTGISAPYEAPANPEVHVKNYELPVQDAVKQIIDYLDTKGYLPA 208
Cdd:PRK03846 152 IRNFTGIDSVYEAPESPEIHLDTGEQLVTNLVEQLLDYLRQRDIIRS 198
|
|
| APS_kinase |
pfam01583 |
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3 ... |
24-186 |
5.52e-97 |
|
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: 278.82 E-value: 5.52e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7387810 24 RGLTIWLTGLSASGKSTLAVELEHQLVrDRRVHAYRLDGDNIRFGLNKDLGFSEADRNENIRRIAEVAKLFADSNSIAIT 103
Cdd:pfam01583 1 RGCTIWLTGLSGAGKSTIANALERKLF-EQGRSVYVLDGDNVRHGLNKDLGFSEEDRTENIRRIGEVAKLFADAGLIVIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7387810 104 SFISPYRKDRDTARQLHEVAtpgeetglPFVEVYVDVPVEVAEQRDPKGLYKKAREGVIKEFTGISAPYEAPANPEVHVK 183
Cdd:pfam01583 80 AFISPYREDREQARELHEEG--------KFIEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDSPYEAPENPELVLD 151
|
...
gi 7387810 184 NYE 186
Cdd:pfam01583 152 TDK 154
|
|
| APSK |
cd02027 |
Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5 ... |
27-183 |
2.35e-92 |
|
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: 266.65 E-value: 2.35e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7387810 27 TIWLTGLSASGKSTLAVELEHQLvRDRRVHAYRLDGDNIRFGLNKDLGFSEADRNENIRRIAEVAKLFADSNSIAITSFI 106
Cdd:cd02027 1 VIWLTGLSGSGKSTIARALEEKL-FQRGRPVYVLDGDNVRHGLNKDLGFSREDREENIRRIAEVAKLLADAGLIVIAAFI 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7387810 107 SPYRKDRDTARQLHEvatpgeetGLPFVEVYVDVPVEVAEQRDPKGLYKKAREGVIKEFTGISAPYEAPANPEVHVK 183
Cdd:cd02027 80 SPYREDREAARKIIG--------GGDFLEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDDPYEAPENPDLVLD 148
|
|
| apsK |
TIGR00455 |
adenylyl-sulfate kinase; This protein, adenylylsulfate kinase, is often found as a fusion ... |
10-200 |
1.35e-88 |
|
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: 258.55 E-value: 1.35e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7387810 10 SALTRSERTELRNQRGLTIWLTGLSASGKSTLAVELEHQLvRDRRVHAYRLDGDNIRFGLNKDLGFSEADRNENIRRIAE 89
Cdd:TIGR00455 3 PAITKDERQALNGHRGVVIWLTGLSGSGKSTIANALEKKL-ESKGYRVYVLDGDNVRHGLNKDLGFSEEDRKENIRRIGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7387810 90 VAKLFADSNSIAITSFISPYRKDRDTARQLHEVATpgeetglpFVEVYVDVPVEVAEQRDPKGLYKKAREGVIKEFTGIS 169
Cdd:TIGR00455 82 VAKLFVRNGIIVITSFISPYRADRQMVRELIEKGE--------FIEVFVDCPLEVCEQRDPKGLYKKARNGEIKGFTGID 153
|
170 180 190
....*....|....*....|....*....|.
gi 7387810 170 APYEAPANPEVHVKNYELPVQDAVKQIIDYL 200
Cdd:TIGR00455 154 SPYEAPENPEVVLDTDQNDREECVGQIIEKL 184
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| CysC |
COG0529 |
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ... |
10-207 |
1.16e-109 |
|
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: 312.02 E-value: 1.16e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7387810 10 SALTRSERTELRNQRGLTIWLTGLSASGKSTLAVELEHQLvRDRRVHAYRLDGDNIRFGLNKDLGFSEADRNENIRRIAE 89
Cdd:COG0529 1 SAVTREERAALKGQKGFVVWFTGLSGSGKSTLANALERRL-FERGRHVYLLDGDNVRHGLNKDLGFSKEDRDENIRRIGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7387810 90 VAKLFADSNSIAITSFISPYRKDRDTARQLHEvatPGEetglpFVEVYVDVPVEVAEQRDPKGLYKKAREGVIKEFTGIS 169
Cdd:COG0529 80 VAKLLADAGLIVLVAFISPYRADREEARELIG---EGE-----FIEVYVDTPLEVCEARDPKGLYAKARAGEIKNFTGID 151
|
170 180 190
....*....|....*....|....*....|....*...
gi 7387810 170 APYEAPANPEVHVKNYELPVQDAVKQIIDYLDTKGYLP 207
Cdd:COG0529 152 DPYEAPENPELVLDTDKESVEESVEKILAYLEERGYIS 189
|
|
| PRK03846 |
PRK03846 |
adenylylsulfate kinase; Provisional |
2-208 |
2.15e-97 |
|
adenylylsulfate kinase; Provisional
Pssm-ID: 179661 Cd Length: 198 Bit Score: 281.44 E-value: 2.15e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7387810 2 STNITFHASALTRSERTELRNQRGLTIWLTGLSASGKSTLAVELEHQLVrDRRVHAYRLDGDNIRFGLNKDLGFSEADRN 81
Cdd:PRK03846 1 DENIVWHQHPVTKAQREQLHGHKGVVLWFTGLSGSGKSTVAGALEEALH-ELGVSTYLLDGDNVRHGLCSDLGFSDADRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7387810 82 ENIRRIAEVAKLFADSNSIAITSFISPYRKDRDTARQLHEvatPGEetglpFVEVYVDVPVEVAEQRDPKGLYKKAREGV 161
Cdd:PRK03846 80 ENIRRVGEVAKLMVDAGLVVLTAFISPHRAERQMVRERLG---EGE-----FIEVFVDTPLAICEARDPKGLYKKARAGE 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 7387810 162 IKEFTGISAPYEAPANPEVHVKNYELPVQDAVKQIIDYLDTKGYLPA 208
Cdd:PRK03846 152 IRNFTGIDSVYEAPESPEIHLDTGEQLVTNLVEQLLDYLRQRDIIRS 198
|
|
| APS_kinase |
pfam01583 |
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3 ... |
24-186 |
5.52e-97 |
|
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: 278.82 E-value: 5.52e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7387810 24 RGLTIWLTGLSASGKSTLAVELEHQLVrDRRVHAYRLDGDNIRFGLNKDLGFSEADRNENIRRIAEVAKLFADSNSIAIT 103
Cdd:pfam01583 1 RGCTIWLTGLSGAGKSTIANALERKLF-EQGRSVYVLDGDNVRHGLNKDLGFSEEDRTENIRRIGEVAKLFADAGLIVIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7387810 104 SFISPYRKDRDTARQLHEVAtpgeetglPFVEVYVDVPVEVAEQRDPKGLYKKAREGVIKEFTGISAPYEAPANPEVHVK 183
Cdd:pfam01583 80 AFISPYREDREQARELHEEG--------KFIEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDSPYEAPENPELVLD 151
|
...
gi 7387810 184 NYE 186
Cdd:pfam01583 152 TDK 154
|
|
| APSK |
cd02027 |
Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5 ... |
27-183 |
2.35e-92 |
|
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: 266.65 E-value: 2.35e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7387810 27 TIWLTGLSASGKSTLAVELEHQLvRDRRVHAYRLDGDNIRFGLNKDLGFSEADRNENIRRIAEVAKLFADSNSIAITSFI 106
Cdd:cd02027 1 VIWLTGLSGSGKSTIARALEEKL-FQRGRPVYVLDGDNVRHGLNKDLGFSREDREENIRRIAEVAKLLADAGLIVIAAFI 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7387810 107 SPYRKDRDTARQLHEvatpgeetGLPFVEVYVDVPVEVAEQRDPKGLYKKAREGVIKEFTGISAPYEAPANPEVHVK 183
Cdd:cd02027 80 SPYREDREAARKIIG--------GGDFLEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDDPYEAPENPDLVLD 148
|
|
| PRK05506 |
PRK05506 |
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional |
2-206 |
2.68e-90 |
|
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
Pssm-ID: 180120 [Multi-domain] Cd Length: 632 Bit Score: 277.20 E-value: 2.68e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7387810 2 STNITFHASALTRSERTELRNQRGLTIWLTGLSASGKSTLAVELEHQLVrDRRVHAYRLDGDNIRFGLNKDLGFSEADRN 81
Cdd:PRK05506 437 ATNVHWQASDVSREARAARKGQKPATVWFTGLSGSGKSTIANLVERRLH-ALGRHTYLLDGDNVRHGLNRDLGFSDADRV 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7387810 82 ENIRRIAEVAKLFADSNSIAITSFISPYRKDRDTARQLHEVAtpgeetglPFVEVYVDVPVEVAEQRDPKGLYKKAREGV 161
Cdd:PRK05506 516 ENIRRVAEVARLMADAGLIVLVSFISPFREERELARALHGEG--------EFVEVFVDTPLEVCEARDPKGLYAKARAGE 587
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 7387810 162 IKEFTGISAPYEAPANPEVHVKNYELPVQDAVKQIIDYLDTKGYL 206
Cdd:PRK05506 588 IKNFTGIDSPYEAPENPELRLDTTGRSPEELAEQVLELLRRRGAI 632
|
|
| apsK |
TIGR00455 |
adenylyl-sulfate kinase; This protein, adenylylsulfate kinase, is often found as a fusion ... |
10-200 |
1.35e-88 |
|
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: 258.55 E-value: 1.35e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7387810 10 SALTRSERTELRNQRGLTIWLTGLSASGKSTLAVELEHQLvRDRRVHAYRLDGDNIRFGLNKDLGFSEADRNENIRRIAE 89
Cdd:TIGR00455 3 PAITKDERQALNGHRGVVIWLTGLSGSGKSTIANALEKKL-ESKGYRVYVLDGDNVRHGLNKDLGFSEEDRKENIRRIGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7387810 90 VAKLFADSNSIAITSFISPYRKDRDTARQLHEVATpgeetglpFVEVYVDVPVEVAEQRDPKGLYKKAREGVIKEFTGIS 169
Cdd:TIGR00455 82 VAKLFVRNGIIVITSFISPYRADRQMVRELIEKGE--------FIEVFVDCPLEVCEQRDPKGLYKKARNGEIKGFTGID 153
|
170 180 190
....*....|....*....|....*....|.
gi 7387810 170 APYEAPANPEVHVKNYELPVQDAVKQIIDYL 200
Cdd:TIGR00455 154 SPYEAPENPEVVLDTDQNDREECVGQIIEKL 184
|
|
| PRK00889 |
PRK00889 |
adenylylsulfate kinase; Provisional |
22-207 |
2.87e-68 |
|
adenylylsulfate kinase; Provisional
Pssm-ID: 179157 Cd Length: 175 Bit Score: 206.80 E-value: 2.87e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7387810 22 NQRGLTIWLTGLSASGKSTLAVELEHQL-VRDRRVHAyrLDGDNIRFGLNKDLGFSEADRNENIRRIAEVAKLFADSNSI 100
Cdd:PRK00889 1 KQRGVTVWFTGLSGAGKTTIARALAEKLrEAGYPVEV--LDGDAVRTNLSKGLGFSKEDRDTNIRRIGFVANLLTRHGVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7387810 101 AITSFISPYRKDRDTARQlhevATPGeetglpFVEVYVDVPVEVAEQRDPKGLYKKAREGVIKEFTGISAPYEAPANPEV 180
Cdd:PRK00889 79 VLVSAISPYRETREEVRA----NIGN------FLEVFVDAPLEVCEQRDVKGLYAKARAGEIKHFTGIDDPYEPPLNPEV 148
|
170 180
....*....|....*....|....*..
gi 7387810 181 HVKNYELPVQDAVKQIIDYLDTKGYLP 207
Cdd:PRK00889 149 ECRTDLESLEESVDKVLQKLEELGYLV 175
|
|
| PRK05537 |
PRK05537 |
bifunctional sulfate adenylyltransferase/adenylylsulfate kinase; |
21-206 |
6.01e-63 |
|
bifunctional sulfate adenylyltransferase/adenylylsulfate kinase;
Pssm-ID: 180124 [Multi-domain] Cd Length: 568 Bit Score: 204.52 E-value: 6.01e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7387810 21 RNQRGLTIWLTGLSASGKSTLAVELEHQL--VRDRRVHAyrLDGDNIRFGLNKDLGFSEADRNENIRRIAEVAKLFADSN 98
Cdd:PRK05537 388 RHKQGFTVFFTGLSGAGKSTIAKALMVKLmeMRGRPVTL--LDGDVVRKHLSSELGFSKEDRDLNILRIGFVASEITKNG 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7387810 99 SIAITSFISPYRKDRDTARQLHEvatpgeETGlPFVEVYVDVPVEVAEQRDPKGLYKKAREGVIKEFTGISAPYEAPANP 178
Cdd:PRK05537 466 GIAICAPIAPYRATRREVREMIE------AYG-GFIEVHVATPLEVCEQRDRKGLYAKAREGKIKGFTGISDPYEPPANP 538
|
170 180
....*....|....*....|....*...
gi 7387810 179 EVHVKNYELPVQDAVKQIIDYLDTKGYL 206
Cdd:PRK05537 539 ELVIDTTNVTPDECAHKILLYLEEKGYL 566
|
|
| PRK05541 |
PRK05541 |
adenylylsulfate kinase; Provisional |
23-204 |
6.14e-24 |
|
adenylylsulfate kinase; Provisional
Pssm-ID: 235498 Cd Length: 176 Bit Score: 93.20 E-value: 6.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7387810 23 QRGLTIWLTGLSASGKSTLAVELEHQLvRDRRVHAYRLDGDNIR--FGLNkdlGFSEADRNENIRRIAEVAKLFADSNSI 100
Cdd:PRK05541 5 PNGYVIWITGLAGSGKTTIAKALYERL-KLKYSNVIYLDGDELReiLGHY---GYDKQSRIEMALKRAKLAKFLADQGMI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7387810 101 AITSFISPYRKDRDTARQLhevatpgeetgLP-FVEVYVDVPVEVAEQRDPKGLYKKAREGVIKEFTGISAPYEAPANPE 179
Cdd:PRK05541 81 VIVTTISMFDEIYAYNRKH-----------LPnYFEVYLKCDMEELIRRDQKGLYTKALKGEIKNVVGVDIPFDEPKADL 149
|
170 180
....*....|....*....|....*
gi 7387810 180 VHVKNYELPVQDAVKQIIDYLDTKG 204
Cdd:PRK05541 150 VIDNSCRTSLDEKVDLILNKLKLRL 174
|
|
| COG0645 |
COG0645 |
Predicted kinase, contains AAA domain [General function prediction only]; |
28-196 |
8.32e-10 |
|
Predicted kinase, contains AAA domain [General function prediction only];
Pssm-ID: 440410 [Multi-domain] Cd Length: 164 Bit Score: 55.30 E-value: 8.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7387810 28 IWLTGLSASGKSTLAVELEhqlvrdRRVHAYRLDGDNIRFGLnKDLGFSEADRNENIR-----RIAEVAKLFADSNSIAI 102
Cdd:COG0645 2 ILVCGLPGSGKSTLARALA------ERLGAVRLRSDVVRKRL-FGAGLAPLERSPEATartyaRLLALARELLAAGRSVI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7387810 103 TSFISPYRKDRDTARQLhevatpGEETGLPFVEVYVDVPVEVA----EQRDPKGLYKKAREGVIKEFTGISAPYEAPANP 178
Cdd:COG0645 75 LDATFLRRAQREAFRAL------AEEAGAPFVLIWLDAPEEVLrerlEARNAEGGDSDATWEVLERQLAFEEPLTEDEGF 148
|
170
....*....|....*...
gi 7387810 179 EVHVKNYELPvqDAVKQI 196
Cdd:COG0645 149 LLVVDTSGLE--EALAAL 164
|
|
| AAA_33 |
pfam13671 |
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ... |
28-148 |
8.33e-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: 52.31 E-value: 8.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7387810 28 IWLTGLSASGKSTLAVELEhqlvrdRRVHAYRLDGDNIRFGLNKDLGFSEADRNENIRRIAEVAKLFADS------NSIA 101
Cdd:pfam13671 2 ILLVGLPGSGKSTLARRLL------EELGAVRLSSDDERKRLFGEGRPSISYYTDATDRTYERLHELARIalragrPVIL 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 7387810 102 ITSFISpyRKDRDTARQLhevatpGEETGLPFVEVYVDVPVEVAEQR 148
Cdd:pfam13671 76 DATNLR--RDERARLLAL------AREYGVPVRIVVFEAPEEVLRER 114
|
|
| COG4639 |
COG4639 |
Predicted kinase [General function prediction only]; |
30-164 |
4.72e-07 |
|
Predicted kinase [General function prediction only];
Pssm-ID: 443677 [Multi-domain] Cd Length: 145 Bit Score: 47.52 E-value: 4.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7387810 30 LTGLSASGKSTLAveleHQLVRDRRVhayrLDGDNIRfglnKDLGFSEADRNENiRRIAEVAKLFADSNSIAITSFI--- 106
Cdd:COG4639 7 LIGLPGSGKSTFA----RRLFAPTEV----VSSDDIR----ALLGGDENDQSAW-GDVFQLAHEIARARLRAGRLTVvda 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 7387810 107 -SPYRKDRdtaRQLHEVATpgeETGLPFVEVYVDVPVEVAEQRDpkglykKAREGVIKE 164
Cdd:COG4639 74 tNLQREAR---RRLLALAR---AYGALVVAVVLDVPLEVCLARN------AARDRQVPE 120
|
|
| Kti12 |
COG4088 |
tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) ... |
24-204 |
1.24e-06 |
|
tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) [Translation, ribosomal structure and biogenesis, Defense mechanisms];
Pssm-ID: 443264 [Multi-domain] Cd Length: 179 Bit Score: 47.03 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7387810 24 RGLTIWLTGLSASGKSTLAVEL--EHQLVRDRRVHayrLDGDNIRFGLNKDLGFSEADRnENIRRIAE-VAKLFADSNSI 100
Cdd:COG4088 3 SPMLLILTGPPGSGKTTFAKALaqRLYAEGIAVAL---LHSDDFRRFLVNESFPKETYE-EVVEDVRTtTADNALDNGYS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7387810 101 AITSFISPYRKDRDTARQLHEVATpgeetglPFVEVYVDVPVEVAEQRDPKGLYKKAREGVIKEFTGISAPYEaPANPEV 180
Cdd:COG4088 79 VIVDGTFYYRSWQRDFRNLAKHKA-------PIHIIYLKAPLETALRRNRERGEPIPERVIARMYRKFDKPGT-KDRPDL 150
|
170 180
....*....|....*....|....
gi 7387810 181 HVKNYELPVQDAVKQIIDYLDTKG 204
Cdd:COG4088 151 VIDTTEDSVSETLDAILKAIETWG 174
|
|
| GntK |
cd02021 |
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting ... |
30-160 |
1.42e-05 |
|
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting product gluconate-6-phoshate is an important precursor of gluconate metabolism. GntK acts as a dimmer composed of two identical subunits.
Pssm-ID: 238979 [Multi-domain] Cd Length: 150 Bit Score: 43.40 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7387810 30 LTGLSASGKSTLAVELEHQLvrdrrvHAYRLDGDNIRFGLNKDL-----GFSEADRN---ENIRRIAEVAKLFADSNSIA 101
Cdd:cd02021 4 VMGVSGSGKSTVGKALAERL------GAPFIDGDDLHPPANIAKmaagiPLNDEDRWpwlQALTDALLAKLASAGEGVVV 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 7387810 102 ITSFISpyRKDRDTARQLHevatpgeeTGLPFVEVYVDVPVEVAEQRDpkglykKAREG 160
Cdd:cd02021 78 ACSALK--RIYRDILRGGA--------ANPRVRFVHLDGPREVLAERL------AARKG 120
|
|
| NK |
cd02019 |
Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of ... |
27-62 |
7.01e-05 |
|
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: 39.63 E-value: 7.01e-05
10 20 30
....*....|....*....|....*....|....*.
gi 7387810 27 TIWLTGLSASGKSTLAVELEHQLvrdRRVHAYRLDG 62
Cdd:cd02019 1 IIAITGGSGSGKSTVAKKLAEQL---GGRSVVVLDE 33
|
|
| pseT |
PHA02530 |
polynucleotide kinase; Provisional |
28-164 |
6.44e-03 |
|
polynucleotide kinase; Provisional
Pssm-ID: 222856 [Multi-domain] Cd Length: 300 Bit Score: 36.54 E-value: 6.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7387810 28 IWLT-GLSASGKSTLAVELEHQLVRdrrvhAYRLDGDNIR---FGLNKDLGFSEADRNENIRRIAE----VAKLFADSNS 99
Cdd:PHA02530 4 IILTvGVPGSGKSTWAREFAAKNPK-----AVNVNRDDLRqslFGHGEWGEYKFTKEKEDLVTKAQeaaaLAALKSGKSV 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7387810 100 IAITSFISPYRKdrdtaRQLHEVATpgeETGLPFVEVYVDVPVEVAEQRDPKGLYKKAREGVIKE 164
Cdd:PHA02530 79 IISDTNLNPERR-----RKWKELAK---ELGAEFEEKVFDVPVEELVKRNRKRGERAVPEDVLRS 135
|
|
|