NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|498240852|ref|WP_010555008|]
View 

MULTISPECIES: adenylyl-sulfate kinase [Pseudoalteromonas]

Protein Classification

adenylyl-sulfate kinase( domain architecture ID 10792327)

adenylylsulfate kinase catalyzes the ATP-dependent phosphorylation of adenosine 5'-phosphosulfate (APS) to 3'-phosphoadenosine-5'-phosphosulfate (PAPS); it is often found as a fusion protein with sulphate adenylyltransferase. Both enzymes are required for PAPS (phosphoadenosine-phosphosulfate) synthesis from inorganic sulfate

CATH:  3.40.50.300
EC:  2.7.1.25
Gene Ontology:  GO:0004020|GO:0005524|GO:0000103
SCOP:  4003930

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PRK03846 PRK03846
adenylylsulfate kinase; Provisional
2-197 7.02e-148

adenylylsulfate kinase; Provisional


:

Pssm-ID: 179661  Cd Length: 198  Bit Score: 408.17  E-value: 7.02e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498240852   2 DENIVWHNYATTKAQRSEQKKHKPAILWFTGFSGSGKSTVANALEAALNQQGTHTYLLDGDNVRHGLCKDLGFSDEDRIE 81
Cdd:PRK03846   1 DENIVWHQHPVTKAQREQLHGHKGVVLWFTGLSGSGKSTVAGALEEALHELGVSTYLLDGDNVRHGLCSDLGFSDADRKE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498240852  82 NIRRVGETAKLMTDAGLLVLTAFISPFRAERDMVRSLVDDGEFIEVFIDTPLDVCESRDPKGLYKKARAGEIKHFTGIDS 161
Cdd:PRK03846  81 NIRRVGEVAKLMVDAGLVVLTAFISPHRAERQMVRERLGEGEFIEVFVDTPLAICEARDPKGLYKKARAGEIRNFTGIDS 160
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 498240852 162 SYEVPNNPEIILDTSKNTLDQSVTQLITYLKQKHII 197
Cdd:PRK03846 161 VYEAPESPEIHLDTGEQLVTNLVEQLLDYLRQRDII 196
 
Name Accession Description Interval E-value
PRK03846 PRK03846
adenylylsulfate kinase; Provisional
2-197 7.02e-148

adenylylsulfate kinase; Provisional


Pssm-ID: 179661  Cd Length: 198  Bit Score: 408.17  E-value: 7.02e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498240852   2 DENIVWHNYATTKAQRSEQKKHKPAILWFTGFSGSGKSTVANALEAALNQQGTHTYLLDGDNVRHGLCKDLGFSDEDRIE 81
Cdd:PRK03846   1 DENIVWHQHPVTKAQREQLHGHKGVVLWFTGLSGSGKSTVAGALEEALHELGVSTYLLDGDNVRHGLCSDLGFSDADRKE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498240852  82 NIRRVGETAKLMTDAGLLVLTAFISPFRAERDMVRSLVDDGEFIEVFIDTPLDVCESRDPKGLYKKARAGEIKHFTGIDS 161
Cdd:PRK03846  81 NIRRVGEVAKLMVDAGLVVLTAFISPHRAERQMVRERLGEGEFIEVFVDTPLAICEARDPKGLYKKARAGEIRNFTGIDS 160
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 498240852 162 SYEVPNNPEIILDTSKNTLDQSVTQLITYLKQKHII 197
Cdd:PRK03846 161 VYEAPESPEIHLDTGEQLVTNLVEQLLDYLRQRDII 196
CysC COG0529
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ...
10-197 1.86e-131

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: 366.34  E-value: 1.86e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498240852  10 YATTKAQRSEQKKHKPAILWFTGFSGSGKSTVANALEAALNQQGTHTYLLDGDNVRHGLCKDLGFSDEDRIENIRRVGET 89
Cdd:COG0529    1 SAVTREERAALKGQKGFVVWFTGLSGSGKSTLANALERRLFERGRHVYLLDGDNVRHGLNKDLGFSKEDRDENIRRIGEV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498240852  90 AKLMTDAGLLVLTAFISPFRAERDMVRSLVDDGEFIEVFIDTPLDVCESRDPKGLYKKARAGEIKHFTGIDSSYEVPNNP 169
Cdd:COG0529   81 AKLLADAGLIVLVAFISPYRADREEARELIGEGEFIEVYVDTPLEVCEARDPKGLYAKARAGEIKNFTGIDDPYEAPENP 160
                        170       180
                 ....*....|....*....|....*...
gi 498240852 170 EIILDTSKNTLDQSVTQLITYLKQKHII 197
Cdd:COG0529  161 ELVLDTDKESVEESVEKILAYLEERGYI 188
APSK cd02027
Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5 ...
27-175 8.43e-107

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: 302.47  E-value: 8.43e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498240852  27 ILWFTGFSGSGKSTVANALEAALNQQGTHTYLLDGDNVRHGLCKDLGFSDEDRIENIRRVGETAKLMTDAGLLVLTAFIS 106
Cdd:cd02027    1 VIWLTGLSGSGKSTIARALEEKLFQRGRPVYVLDGDNVRHGLNKDLGFSREDREENIRRIAEVAKLLADAGLIVIAAFIS 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498240852 107 PFRAERDMVRSLVDDGEFIEVFIDTPLDVCESRDPKGLYKKARAGEIKHFTGIDSSYEVPNNPEIILDT 175
Cdd:cd02027   81 PYREDREAARKIIGGGDFLEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDDPYEAPENPDLVLDT 149
APS_kinase pfam01583
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3 ...
24-177 9.16e-107

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: 302.70  E-value: 9.16e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498240852   24 KPAILWFTGFSGSGKSTVANALEAALNQQGTHTYLLDGDNVRHGLCKDLGFSDEDRIENIRRVGETAKLMTDAGLLVLTA 103
Cdd:pfam01583   1 RGCTIWLTGLSGAGKSTIANALERKLFEQGRSVYVLDGDNVRHGLNKDLGFSEEDRTENIRRIGEVAKLFADAGLIVITA 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498240852  104 FISPFRAERDMVRSLVDDGEFIEVFIDTPLDVCESRDPKGLYKKARAGEIKHFTGIDSSYEVPNNPEIILDTSK 177
Cdd:pfam01583  81 FISPYREDREQARELHEEGKFIEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDSPYEAPENPELVLDTDK 154
apsK TIGR00455
adenylyl-sulfate kinase; This protein, adenylylsulfate kinase, is often found as a fusion ...
7-191 1.45e-105

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: 300.92  E-value: 1.45e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498240852    7 WHNyATTKAQRSEQKKHKPAILWFTGFSGSGKSTVANALEAALNQQGTHTYLLDGDNVRHGLCKDLGFSDEDRIENIRRV 86
Cdd:TIGR00455   1 WHP-AITKDERQALNGHRGVVIWLTGLSGSGKSTIANALEKKLESKGYRVYVLDGDNVRHGLNKDLGFSEEDRKENIRRI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498240852   87 GETAKLMTDAGLLVLTAFISPFRAERDMVRSLVDDGEFIEVFIDTPLDVCESRDPKGLYKKARAGEIKHFTGIDSSYEVP 166
Cdd:TIGR00455  80 GEVAKLFVRNGIIVITSFISPYRADRQMVRELIEKGEFIEVFVDCPLEVCEQRDPKGLYKKARNGEIKGFTGIDSPYEAP 159
                         170       180
                  ....*....|....*....|....*
gi 498240852  167 NNPEIILDTSKNTLDQSVTQLITYL 191
Cdd:TIGR00455 160 ENPEVVLDTDQNDREECVGQIIEKL 184
 
Name Accession Description Interval E-value
PRK03846 PRK03846
adenylylsulfate kinase; Provisional
2-197 7.02e-148

adenylylsulfate kinase; Provisional


Pssm-ID: 179661  Cd Length: 198  Bit Score: 408.17  E-value: 7.02e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498240852   2 DENIVWHNYATTKAQRSEQKKHKPAILWFTGFSGSGKSTVANALEAALNQQGTHTYLLDGDNVRHGLCKDLGFSDEDRIE 81
Cdd:PRK03846   1 DENIVWHQHPVTKAQREQLHGHKGVVLWFTGLSGSGKSTVAGALEEALHELGVSTYLLDGDNVRHGLCSDLGFSDADRKE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498240852  82 NIRRVGETAKLMTDAGLLVLTAFISPFRAERDMVRSLVDDGEFIEVFIDTPLDVCESRDPKGLYKKARAGEIKHFTGIDS 161
Cdd:PRK03846  81 NIRRVGEVAKLMVDAGLVVLTAFISPHRAERQMVRERLGEGEFIEVFVDTPLAICEARDPKGLYKKARAGEIRNFTGIDS 160
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 498240852 162 SYEVPNNPEIILDTSKNTLDQSVTQLITYLKQKHII 197
Cdd:PRK03846 161 VYEAPESPEIHLDTGEQLVTNLVEQLLDYLRQRDII 196
CysC COG0529
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ...
10-197 1.86e-131

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: 366.34  E-value: 1.86e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498240852  10 YATTKAQRSEQKKHKPAILWFTGFSGSGKSTVANALEAALNQQGTHTYLLDGDNVRHGLCKDLGFSDEDRIENIRRVGET 89
Cdd:COG0529    1 SAVTREERAALKGQKGFVVWFTGLSGSGKSTLANALERRLFERGRHVYLLDGDNVRHGLNKDLGFSKEDRDENIRRIGEV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498240852  90 AKLMTDAGLLVLTAFISPFRAERDMVRSLVDDGEFIEVFIDTPLDVCESRDPKGLYKKARAGEIKHFTGIDSSYEVPNNP 169
Cdd:COG0529   81 AKLLADAGLIVLVAFISPYRADREEARELIGEGEFIEVYVDTPLEVCEARDPKGLYAKARAGEIKNFTGIDDPYEAPENP 160
                        170       180
                 ....*....|....*....|....*...
gi 498240852 170 EIILDTSKNTLDQSVTQLITYLKQKHII 197
Cdd:COG0529  161 ELVLDTDKESVEESVEKILAYLEERGYI 188
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
4-197 1.10e-109

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 326.50  E-value: 1.10e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498240852   4 NIVWHNYATTKAQRSEQKKHKPAILWFTGFSGSGKSTVANALEAALNQQGTHTYLLDGDNVRHGLCKDLGFSDEDRIENI 83
Cdd:PRK05506 439 NVHWQASDVSREARAARKGQKPATVWFTGLSGSGKSTIANLVERRLHALGRHTYLLDGDNVRHGLNRDLGFSDADRVENI 518
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498240852  84 RRVGETAKLMTDAGLLVLTAFISPFRAERDMVRSLVDDGEFIEVFIDTPLDVCESRDPKGLYKKARAGEIKHFTGIDSSY 163
Cdd:PRK05506 519 RRVAEVARLMADAGLIVLVSFISPFREERELARALHGEGEFVEVFVDTPLEVCEARDPKGLYAKARAGEIKNFTGIDSPY 598
                        170       180       190
                 ....*....|....*....|....*....|....
gi 498240852 164 EVPNNPEIILDTSKNTLDQSVTQLITYLKQKHII 197
Cdd:PRK05506 599 EAPENPELRLDTTGRSPEELAEQVLELLRRRGAI 632
APSK cd02027
Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5 ...
27-175 8.43e-107

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: 302.47  E-value: 8.43e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498240852  27 ILWFTGFSGSGKSTVANALEAALNQQGTHTYLLDGDNVRHGLCKDLGFSDEDRIENIRRVGETAKLMTDAGLLVLTAFIS 106
Cdd:cd02027    1 VIWLTGLSGSGKSTIARALEEKLFQRGRPVYVLDGDNVRHGLNKDLGFSREDREENIRRIAEVAKLLADAGLIVIAAFIS 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498240852 107 PFRAERDMVRSLVDDGEFIEVFIDTPLDVCESRDPKGLYKKARAGEIKHFTGIDSSYEVPNNPEIILDT 175
Cdd:cd02027   81 PYREDREAARKIIGGGDFLEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDDPYEAPENPDLVLDT 149
APS_kinase pfam01583
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3 ...
24-177 9.16e-107

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: 302.70  E-value: 9.16e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498240852   24 KPAILWFTGFSGSGKSTVANALEAALNQQGTHTYLLDGDNVRHGLCKDLGFSDEDRIENIRRVGETAKLMTDAGLLVLTA 103
Cdd:pfam01583   1 RGCTIWLTGLSGAGKSTIANALERKLFEQGRSVYVLDGDNVRHGLNKDLGFSEEDRTENIRRIGEVAKLFADAGLIVITA 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498240852  104 FISPFRAERDMVRSLVDDGEFIEVFIDTPLDVCESRDPKGLYKKARAGEIKHFTGIDSSYEVPNNPEIILDTSK 177
Cdd:pfam01583  81 FISPYREDREQARELHEEGKFIEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDSPYEAPENPELVLDTDK 154
apsK TIGR00455
adenylyl-sulfate kinase; This protein, adenylylsulfate kinase, is often found as a fusion ...
7-191 1.45e-105

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: 300.92  E-value: 1.45e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498240852    7 WHNyATTKAQRSEQKKHKPAILWFTGFSGSGKSTVANALEAALNQQGTHTYLLDGDNVRHGLCKDLGFSDEDRIENIRRV 86
Cdd:TIGR00455   1 WHP-AITKDERQALNGHRGVVIWLTGLSGSGKSTIANALEKKLESKGYRVYVLDGDNVRHGLNKDLGFSEEDRKENIRRI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498240852   87 GETAKLMTDAGLLVLTAFISPFRAERDMVRSLVDDGEFIEVFIDTPLDVCESRDPKGLYKKARAGEIKHFTGIDSSYEVP 166
Cdd:TIGR00455  80 GEVAKLFVRNGIIVITSFISPYRADRQMVRELIEKGEFIEVFVDCPLEVCEQRDPKGLYKKARNGEIKGFTGIDSPYEAP 159
                         170       180
                  ....*....|....*....|....*
gi 498240852  167 NNPEIILDTSKNTLDQSVTQLITYL 191
Cdd:TIGR00455 160 ENPEVVLDTDQNDREECVGQIIEKL 184
PRK00889 PRK00889
adenylylsulfate kinase; Provisional
22-193 5.44e-77

adenylylsulfate kinase; Provisional


Pssm-ID: 179157  Cd Length: 175  Bit Score: 228.37  E-value: 5.44e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498240852  22 KHKPAILWFTGFSGSGKSTVANALEAALNQQGTHTYLLDGDNVRHGLCKDLGFSDEDRIENIRRVGETAKLMTDAGLLVL 101
Cdd:PRK00889   1 KQRGVTVWFTGLSGAGKTTIARALAEKLREAGYPVEVLDGDAVRTNLSKGLGFSKEDRDTNIRRIGFVANLLTRHGVIVL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498240852 102 TAFISPFRAERDMVRSlvDDGEFIEVFIDTPLDVCESRDPKGLYKKARAGEIKHFTGIDSSYEVPNNPEIILDTSKNTLD 181
Cdd:PRK00889  81 VSAISPYRETREEVRA--NIGNFLEVFVDAPLEVCEQRDVKGLYAKARAGEIKHFTGIDDPYEPPLNPEVECRTDLESLE 158
                        170
                 ....*....|..
gi 498240852 182 QSVTQLITYLKQ 193
Cdd:PRK00889 159 ESVDKVLQKLEE 170
PRK05537 PRK05537
bifunctional sulfate adenylyltransferase/adenylylsulfate kinase;
22-194 6.63e-68

bifunctional sulfate adenylyltransferase/adenylylsulfate kinase;


Pssm-ID: 180124 [Multi-domain]  Cd Length: 568  Bit Score: 216.85  E-value: 6.63e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498240852  22 KHKPAI-LWFTGFSGSGKSTVANALEAALNQQGTHTY-LLDGDNVRHGLCKDLGFSDEDRIENIRRVGETAKLMTDAGLL 99
Cdd:PRK05537 388 RHKQGFtVFFTGLSGAGKSTIAKALMVKLMEMRGRPVtLLDGDVVRKHLSSELGFSKEDRDLNILRIGFVASEITKNGGI 467
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498240852 100 VLTAFISPFRAERDMVRSLVDD-GEFIEVFIDTPLDVCESRDPKGLYKKARAGEIKHFTGIDSSYEVPNNPEIILDTSKN 178
Cdd:PRK05537 468 AICAPIAPYRATRREVREMIEAyGGFIEVHVATPLEVCEQRDRKGLYAKAREGKIKGFTGISDPYEPPANPELVIDTTNV 547
                        170
                 ....*....|....*.
gi 498240852 179 TLDQSVTQLITYLKQK 194
Cdd:PRK05537 548 TPDECAHKILLYLEEK 563
PRK05541 PRK05541
adenylylsulfate kinase; Provisional
19-196 1.05e-31

adenylylsulfate kinase; Provisional


Pssm-ID: 235498  Cd Length: 176  Bit Score: 112.84  E-value: 1.05e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498240852  19 EQKKHKPAILWFTGFSGSGKSTVANALEAALNQQGTHTYLLDGDNVRHgLCKDLGFSDEDRIENIRRVGETAKLMTDAGL 98
Cdd:PRK05541   1 MQMKPNGYVIWITGLAGSGKTTIAKALYERLKLKYSNVIYLDGDELRE-ILGHYGYDKQSRIEMALKRAKLAKFLADQGM 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498240852  99 LVLTAFISPFRAERDMVRSLvdDGEFIEVFIDTPLDVCESRDPKGLYKKARAGEIKHFTGIDSSYEVPNNPEIILDTSKN 178
Cdd:PRK05541  80 IVIVTTISMFDEIYAYNRKH--LPNYFEVYLKCDMEELIRRDQKGLYTKALKGEIKNVVGVDIPFDEPKADLVIDNSCRT 157
                        170
                 ....*....|....*...
gi 498240852 179 TLDQSVTQLITYLKQKHI 196
Cdd:PRK05541 158 SLDEKVDLILNKLKLRLI 175
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
27-187 2.11e-11

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


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 59.54  E-value: 2.11e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498240852  27 ILWFTGFSGSGKSTVANALEAALNqqgthTYLLDGDNVRHGLCKDLGFSDEDRIENIRRVGEtakLMTDAGLLVLTAFIS 106
Cdd:COG0645    1 LILVCGLPGSGKSTLARALAERLG-----AVRLRSDVVRKRLFGAGLAPLERSPEATARTYA---RLLALARELLAAGRS 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498240852 107 -----PF--RAERDMVRSLVDD--GEFIEVFIDTPLDVC----ESRDPKGLYKKARAGEIKHFTGIDSSYEVPNNPEIIL 173
Cdd:COG0645   73 vildaTFlrRAQREAFRALAEEagAPFVLIWLDAPEEVLrerlEARNAEGGDSDATWEVLERQLAFEEPLTEDEGFLLVV 152
                        170
                 ....*....|....
gi 498240852 174 DTSKntLDQSVTQL 187
Cdd:COG0645  153 DTSG--LEEALAAL 164
GntK cd02021
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting ...
31-175 9.05e-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: 9.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498240852  31 TGFSGSGKSTVANALEAALnqQGTHtylLDGDNVRHGLCKDL-----GFSDEDRIENIRRVGE--TAKLMTDAGLLVLTA 103
Cdd:cd02021    5 MGVSGSGKSTVGKALAERL--GAPF---IDGDDLHPPANIAKmaagiPLNDEDRWPWLQALTDalLAKLASAGEGVVVAC 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498240852 104 -FISpfRAERDMVRSLVDDGEFIEVFIDTPLDVCESRDpkglykKARAGeikHFTG---IDS---SYEVPNNPE---IIL 173
Cdd:cd02021   80 sALK--RIYRDILRGGAANPRVRFVHLDGPREVLAERL------AARKG---HFMPadlLDSqfeTLEPPGEDEedvIVI 148

                 ..
gi 498240852 174 DT 175
Cdd:cd02021  149 DV 150
AAA_33 pfam13671
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ...
28-152 1.31e-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: 1.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498240852   28 LWFT-GFSGSGKSTVANALEAALnqqgtHTYLLDGDNVRHGLCKDLGFSDEDRIENI----RRVGETAKLMTDAGLLVL- 101
Cdd:pfam13671   1 LILLvGLPGSGKSTLARRLLEEL-----GAVRLSSDDERKRLFGEGRPSISYYTDATdrtyERLHELARIALRAGRPVIl 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 498240852  102 -TAFISpfRAERDMVRSLV-DDG-EFIEVFIDTPLDVCESRdpkgLYKKARAGE 152
Cdd:pfam13671  76 dATNLR--RDERARLLALArEYGvPVRIVVFEAPEEVLRER----LAARARAGG 123
GntK COG3265
Gluconate kinase [Carbohydrate transport and metabolism]; Gluconate kinase is part of the ...
32-192 2.61e-07

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: 48.20  E-value: 2.61e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498240852  32 GFSGSGKSTVANALEAALnqqgtHTYLLDGD------NV---RHGlckdLGFSDEDRIENIRRVGETAKLMTDAGL-LVL 101
Cdd:COG3265    8 GVSGSGKSTVGQALAERL-----GWPFIDGDdfhppaNIakmAAG----IPLTDEDRAPWLEALADAIAAHLAAGEgAVL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498240852 102 T--AFIspfRAERDMVRSLVDDGEFieVFIDTPLDVCESRdpkgLykKARAGeikHF---TGIDS---SYEVPNNPE--I 171
Cdd:COG3265   79 AcsALK---RSYRDRLREGNPDVRF--VYLDGSRELIAER----L--AARKG---HFmpaSLLDSqfaTLEPPGPDEdaI 144
                        170       180
                 ....*....|....*....|.
gi 498240852 172 ILDTSKnTLDQSVTQLITYLK 192
Cdd:COG3265  145 VVDIDQ-PPEEIVAQILAALG 164
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
34-132 5.07e-06

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: 45.56  E-value: 5.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498240852  34 SGSGKSTVANALEAALNQQGTHTYLLDGDNVRHGLCKDLGFSDE----DRIENIRRVGETAKLMTDAGLLVLTA-FISPF 108
Cdd:COG0489  102 GGEGKSTVAANLALALAQSGKRVLLIDADLRGPSLHRMLGLENRpglsDVLAGEASLEDVIQPTEVEGLDVLPAgPLPPN 181
                         90       100
                 ....*....|....*....|....*....
gi 498240852 109 RAE---RDMVRSLVDD--GEFIEVFIDTP 132
Cdd:COG0489  182 PSEllaSKRLKQLLEElrGRYDYVIIDTP 210
CmkB COG1102
Cytidylate kinase [Nucleotide transport and metabolism];
32-194 2.02e-05

Cytidylate kinase [Nucleotide transport and metabolism];


Pssm-ID: 440719 [Multi-domain]  Cd Length: 188  Bit Score: 43.28  E-value: 2.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498240852  32 GFSGSGKSTVANALEAALNqqgthtY-LLDGDNVRHgLCKDLGFSDEDrienIRRVGETAKLMTDAGLLVLTAFispFRA 110
Cdd:COG1102    7 REPGSGGTTIAKRLAEKLG------LpLYDGEILRE-AAKERGLSEEE----FEKLDEKAPSLLYRDTAEEDEI---DRA 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498240852 111 ERDMVRSLVDDGEFI-----------------EVFIDTPLDVCESR-------DPKGLYK------KARAGEIKHFTGID 160
Cdd:COG1102   73 LDKVIRELARKGNCVivgrladwilrdrpnvlKVFLTAPLEVRVKRiaeregiSEEEAEKeikkrdKSRAKYYKYYYGID 152
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 498240852 161 ssyevPNNPEI---ILDTSKNTLDQSVTQLITYLKQK 194
Cdd:COG1102  153 -----WGDPSNydlVINTSRLGIEEAVDLILAAIEAR 184
COG4639 COG4639
Predicted kinase [General function prediction only];
32-140 1.85e-04

Predicted kinase [General function prediction only];


Pssm-ID: 443677 [Multi-domain]  Cd Length: 145  Bit Score: 39.81  E-value: 1.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498240852  32 GFSGSGKSTVANALEAAlnqqgthTYLLDGDNVRHGLCKDLG-FSDEDRIENIRRvgETAKLMTDAGLLVL---TAfisp 107
Cdd:COG4639    9 GLPGSGKSTFARRLFAP-------TEVVSSDDIRALLGGDENdQSAWGDVFQLAH--EIARARLRAGRLTVvdaTN---- 75
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 498240852 108 frAERDMVRSLVD-----DGEFIEVFIDTPLDVCESRD 140
Cdd:COG4639   76 --LQREARRRLLAlarayGALVVAVVLDVPLEVCLARN 111
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
35-132 2.25e-04

bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on a C-terminal tyrosine cluster and also phosphorylate endogenous protein substrates by using ATP as phosphoryl donor. Besides their capacity to function as tyrosine kinase, most of these proteins are also involved in the production and transport of exopolysaccharides. BY-kinases are involved in a number of physiological processes ranging from stress resistance to pathogenicity.


Pssm-ID: 349772 [Multi-domain]  Cd Length: 190  Bit Score: 40.25  E-value: 2.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498240852  35 GSGKSTVANALEAALNQQGTHTYLLDGDNVRHGLCKDLGFSDEDRIENI----RRVGETAKLMTDAGLLVLTA-FISPFR 109
Cdd:cd05387   30 GEGKSTVAANLAVALAQSGKRVLLIDADLRRPSLHRLLGLPNEPGLSEVlsgqASLEDVIQSTNIPNLDVLPAgTVPPNP 109
                         90       100       110
                 ....*....|....*....|....*....|
gi 498240852 110 AE-------RDMVRSLVDDGEFIevFIDTP 132
Cdd:cd05387  110 SEllssprfAELLEELKEQYDYV--IIDTP 137
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
27-64 1.18e-03

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: 37.03  E-value: 1.18e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 498240852  27 ILWFTGF-SGSGKSTVANALEAALNQQGTHTYLLDGDNV 64
Cdd:cd01983    2 VIAVTGGkGGVGKTTLAAALAVALAAKGYKVLLIDLDDY 40
AAA_22 pfam13401
AAA domain;
31-73 1.62e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 36.94  E-value: 1.62e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 498240852   31 TGFSGSGKSTVANALEAALNQQGTHTYLLD------GDNVRHGLCKDLG 73
Cdd:pfam13401  11 TGESGTGKTTLLRRLLEQLPEVRDSVVFVDlpsgtsPKDLLRALLRALG 59
gntK PRK11545
gluconokinase;
32-156 2.39e-03

gluconokinase;


Pssm-ID: 236926  Cd Length: 163  Bit Score: 37.00  E-value: 2.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498240852  32 GFSGSGKSTVANALEAALnqqgtHTYLLDGD------NVR-----HGLckdlgfSDEDRIENIRRVGETAKLM---TDAG 97
Cdd:PRK11545   2 GVSGSGKSAVASEVAHQL-----HAAFLDGDflhprrNIEkmasgEPL------NDDDRKPWLQALNDAAFAMqrtNKVS 70
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 498240852  98 LLVLTAFISPFraeRDMVRSLVDDGEFIevFIDTPLDVCESRdpkglyKKARAGeikHF 156
Cdd:PRK11545  71 LIVCSALKKHY---RDLLREGNPNLSFI--YLKGDFDVIESR------LKARKG---HF 115
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
21-139 3.57e-03

Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway/BioSystem: Pyrimidine salvage


Pssm-ID: 440337 [Multi-domain]  Cd Length: 206  Bit Score: 36.74  E-value: 3.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498240852  21 KKHKPAILWFTGFSGSGKSTVANALEAALNQQGTHT-----YLLDGDNVRHGLCKDLGFSDED------RIENI------ 83
Cdd:COG0572    3 RSGKPRIIGIAGPSGSGKTTFARRLAEQLGADKVVVislddYYKDREHLPLDERGKPNFDHPEafdldlLNEHLeplkag 82
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498240852  84 -------------RRVGETAKLMTDA-----GLLVLTafispfraeRDMVRSLVDdgefIEVFIDTPLDVCESR 139
Cdd:COG0572   83 esvelpvydfatgTRSGETVKVEPADviiveGIHALN---------DELLRDLLD----LKIYVDADTDVRLIR 143
Bac_Flav_CT_G TIGR03783
Bacteroides conjugation system ATPase, TraG family; Members of this family include the ...
32-70 5.60e-03

Bacteroides conjugation system ATPase, TraG family; Members of this family include the predicted ATPase, TraG, encoded by transfer region genes of conjugative transposons of Bacteroides, such as CTnDOT, found on the main chromosome. Members also include TraG homologs borne on plasmids in Bacteroides. The protein family is related to the conjugative transfer system ATPase VirB4. [Cellular processes, DNA transformation]


Pssm-ID: 163495 [Multi-domain]  Cd Length: 829  Bit Score: 37.12  E-value: 5.60e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 498240852   32 GFSGSGKSTVANALEAALNQQGTHTYLLDGDNVRHGLCK 70
Cdd:TIGR03783 445 GPSGSGKSFFTNHLVRQYYEQGTHILLVDTGNSYQGLCE 483
HolB COG0470
DNA polymerase III, delta prime subunit [Replication, recombination and repair];
19-94 6.02e-03

DNA polymerase III, delta prime subunit [Replication, recombination and repair];


Pssm-ID: 440238 [Multi-domain]  Cd Length: 289  Bit Score: 36.49  E-value: 6.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498240852  19 EQKKHKPAILwFTGFSGSGKSTVANALEAALNQQGTHTYLLDGDNVRH----GLCKDL------GFSDEDRIENIRRVGE 88
Cdd:COG0470   13 ESGRLPHALL-LHGPPGIGKTTLALALARDLLCENPEGGKACGQCHSRlmaaGNHPDLlelnpeEKSDQIGIDQIRELGE 91

                 ....*.
gi 498240852  89 TAKLMT 94
Cdd:COG0470   92 FLSLTP 97
AAA_18 pfam13238
AAA domain;
29-113 8.26e-03

AAA domain;


Pssm-ID: 433052 [Multi-domain]  Cd Length: 128  Bit Score: 35.10  E-value: 8.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498240852   29 WFTGFSGSGKSTVANALEAALNQQGTHT------YLLDGDNVRHGLCKDLgfsDEDRIENIRRVGETAKLMTDAGLLVLT 102
Cdd:pfam13238   2 LITGTPGVGKTTLAKELSKRLGFGDNVRdlalenGLVLGDDPETRESKRL---DEDKLDRLLDLLEENAALEEGGNLIID 78
                          90
                  ....*....|.
gi 498240852  103 AFISPFRAERD 113
Cdd:pfam13238  79 GHLAELEPERA 89
PRK09270 PRK09270
nucleoside triphosphate hydrolase domain-containing protein; Reviewed
26-86 8.60e-03

nucleoside triphosphate hydrolase domain-containing protein; Reviewed


Pssm-ID: 236442  Cd Length: 229  Bit Score: 36.06  E-value: 8.60e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498240852  26 AILWFTGFSGSGKSTVANALEAALNQQGTHTYL---LDG---DNV---RHGLCKDLG----FSDEDRIENIRRV 86
Cdd:PRK09270  34 TIVGIAGPPGAGKSTLAEFLEALLQQDGELPAIqvpMDGfhlDNAvldAHGLRPRKGapetFDVAGLAALLRRL 107
PRK05416 PRK05416
RNase adapter RapZ;
31-46 9.59e-03

RNase adapter RapZ;


Pssm-ID: 235450  Cd Length: 288  Bit Score: 35.84  E-value: 9.59e-03
                         10
                 ....*....|....*.
gi 498240852  31 TGFSGSGKSTVANALE 46
Cdd:PRK05416  12 TGLSGAGKSVALRALE 27
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH
HHS Vulnerability Disclosure