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Conserved domains on  [gi|1079396235|ref|XP_018513399|]
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adenylyl-sulfate kinase 2, chloroplastic isoform X2 [Brassica rapa]

Protein Classification

adenylyl-sulfate kinase( domain architecture ID 10785573)

adenylylsulfate kinase catalyzes the ATP-dependent phosphorylation of adenosine 5'-phosphosulfate (APS) to 3'-phosphoadenosine-5'-phosphosulfate (PAPS)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CysC COG0529
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ...
 90-282 8.40e-116

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: 330.51  E-value: 8.40e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079396235  90 SSICRCDRQQLLQQKGCVIWITGLSGSGKSTVACALSKALFERGKLTYTLDGDNVRHGLNRDLTFKAEDRTENIRRIGEV 169
Cdd:COG0529     1 SAVTREERAALKGQKGFVVWFTGLSGSGKSTLANALERRLFERGRHVYLLDGDNVRHGLNKDLGFSKEDRDENIRRIGEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079396235 170 AKLFADVGVICIASLISPYRRDRDECRSLLPEGDFVEVFMDVPLSVCESRDPKGLYKLARAGKIKGFTGIDDPYEAPLNC 249
Cdd:COG0529    81 AKLLADAGLIVLVAFISPYRADREEARELIGEGEFIEVYVDTPLEVCEARDPKGLYAKARAGEIKNFTGIDDPYEAPENP 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1079396235 250 EVVLkhtgDDDSCSPRQMAEHIISYLQNKGYLE 282
Cdd:COG0529   161 ELVL----DTDKESVEESVEKILAYLEERGYIS 189
 
Name Accession Description Interval E-value
CysC COG0529
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ...
 90-282 8.40e-116

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: 330.51  E-value: 8.40e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079396235  90 SSICRCDRQQLLQQKGCVIWITGLSGSGKSTVACALSKALFERGKLTYTLDGDNVRHGLNRDLTFKAEDRTENIRRIGEV 169
Cdd:COG0529     1 SAVTREERAALKGQKGFVVWFTGLSGSGKSTLANALERRLFERGRHVYLLDGDNVRHGLNKDLGFSKEDRDENIRRIGEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079396235 170 AKLFADVGVICIASLISPYRRDRDECRSLLPEGDFVEVFMDVPLSVCESRDPKGLYKLARAGKIKGFTGIDDPYEAPLNC 249
Cdd:COG0529    81 AKLLADAGLIVLVAFISPYRADREEARELIGEGEFIEVYVDTPLEVCEARDPKGLYAKARAGEIKNFTGIDDPYEAPENP 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1079396235 250 EVVLkhtgDDDSCSPRQMAEHIISYLQNKGYLE 282
Cdd:COG0529   161 ELVL----DTDKESVEESVEKILAYLEERGYIS 189
PRK03846 PRK03846
adenylylsulfate kinase; Provisional
 82-281 6.02e-108

adenylylsulfate kinase; Provisional


Pssm-ID: 179661  Cd Length: 198  Bit Score: 311.10  E-value: 6.02e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079396235  82 PENIVWHESSICRCDRQQLLQQKGCVIWITGLSGSGKSTVACALSKALFERGKLTYTLDGDNVRHGLNRDLTFKAEDRTE 161
Cdd:PRK03846    1 DENIVWHQHPVTKAQREQLHGHKGVVLWFTGLSGSGKSTVAGALEEALHELGVSTYLLDGDNVRHGLCSDLGFSDADRKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079396235 162 NIRRIGEVAKLFADVGVICIASLISPYRRDRDECRSLLPEGDFVEVFMDVPLSVCESRDPKGLYKLARAGKIKGFTGIDD 241
Cdd:PRK03846   81 NIRRVGEVAKLMVDAGLVVLTAFISPHRAERQMVRERLGEGEFIEVFVDTPLAICEARDPKGLYKKARAGEIRNFTGIDS 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1079396235 242 PYEAPLNCEVVLkHTGDDDScspRQMAEHIISYLQNKGYL 281
Cdd:PRK03846  161 VYEAPESPEIHL-DTGEQLV---TNLVEQLLDYLRQRDII 196
APS_kinase pfam01583
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3 ...
 104-257 1.12e-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: 298.46  E-value: 1.12e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079396235 104 KGCVIWITGLSGSGKSTVACALSKALFERGKLTYTLDGDNVRHGLNRDLTFKAEDRTENIRRIGEVAKLFADVGVICIAS 183
Cdd:pfam01583   1 RGCTIWLTGLSGAGKSTIANALERKLFEQGRSVYVLDGDNVRHGLNKDLGFSEEDRTENIRRIGEVAKLFADAGLIVITA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1079396235 184 LISPYRRDRDECRSLLPEGDFVEVFMDVPLSVCESRDPKGLYKLARAGKIKGFTGIDDPYEAPLNCEVVLKHTG 257
Cdd:pfam01583  81 FISPYREDREQARELHEEGKFIEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDSPYEAPENPELVLDTDK 154
APSK cd02027
Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5 ...
 107-254 2.52e-100

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: 289.76  E-value: 2.52e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079396235 107 VIWITGLSGSGKSTVACALSKALFERGKLTYTLDGDNVRHGLNRDLTFKAEDRTENIRRIGEVAKLFADVGVICIASLIS 186
Cdd:cd02027     1 VIWLTGLSGSGKSTIARALEEKLFQRGRPVYVLDGDNVRHGLNKDLGFSREDREENIRRIAEVAKLLADAGLIVIAAFIS 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1079396235 187 PYRRDRDECRSLLPEGDFVEVFMDVPLSVCESRDPKGLYKLARAGKIKGFTGIDDPYEAPLNCEVVLK 254
Cdd:cd02027    81 PYREDREAARKIIGGGDFLEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDDPYEAPENPDLVLD 148
apsK TIGR00455
adenylyl-sulfate kinase; This protein, adenylylsulfate kinase, is often found as a fusion ...
 87-275 2.09e-90

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: 266.26  E-value: 2.09e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079396235  87 WHESsICRCDRQQLLQQKGCVIWITGLSGSGKSTVACALSKALFERGKLTYTLDGDNVRHGLNRDLTFKAEDRTENIRRI 166
Cdd:TIGR00455   1 WHPA-ITKDERQALNGHRGVVIWLTGLSGSGKSTIANALEKKLESKGYRVYVLDGDNVRHGLNKDLGFSEEDRKENIRRI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079396235 167 GEVAKLFADVGVICIASLISPYRRDRDECRSLLPEGDFVEVFMDVPLSVCESRDPKGLYKLARAGKIKGFTGIDDPYEAP 246
Cdd:TIGR00455  80 GEVAKLFVRNGIIVITSFISPYRADRQMVRELIEKGEFIEVFVDCPLEVCEQRDPKGLYKKARNGEIKGFTGIDSPYEAP 159

                         170       180
                  ....*....|....*....|....*....
gi 1079396235 247 LNCEVVLkhtgDDDSCSPRQMAEHIISYL 275
Cdd:TIGR00455 160 ENPEVVL----DTDQNDREECVGQIIEKL 184
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 110-176 3.78e-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: 36.97  E-value: 3.78e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1079396235  110 ITGLSGSGKSTVACALSKALFERGKLTYTLDGDNVRHGLNRDLTFKAEDRTE-NIRRIGEVAKLFADV 176
Cdd:smart00382   7 IVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKaSGSGELRLRLALALA 74
 
Name Accession Description Interval E-value
CysC COG0529
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ...
 90-282 8.40e-116

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: 330.51  E-value: 8.40e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079396235  90 SSICRCDRQQLLQQKGCVIWITGLSGSGKSTVACALSKALFERGKLTYTLDGDNVRHGLNRDLTFKAEDRTENIRRIGEV 169
Cdd:COG0529     1 SAVTREERAALKGQKGFVVWFTGLSGSGKSTLANALERRLFERGRHVYLLDGDNVRHGLNKDLGFSKEDRDENIRRIGEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079396235 170 AKLFADVGVICIASLISPYRRDRDECRSLLPEGDFVEVFMDVPLSVCESRDPKGLYKLARAGKIKGFTGIDDPYEAPLNC 249
Cdd:COG0529    81 AKLLADAGLIVLVAFISPYRADREEARELIGEGEFIEVYVDTPLEVCEARDPKGLYAKARAGEIKNFTGIDDPYEAPENP 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1079396235 250 EVVLkhtgDDDSCSPRQMAEHIISYLQNKGYLE 282
Cdd:COG0529   161 ELVL----DTDKESVEESVEKILAYLEERGYIS 189
PRK03846 PRK03846
adenylylsulfate kinase; Provisional
 82-281 6.02e-108

adenylylsulfate kinase; Provisional


Pssm-ID: 179661  Cd Length: 198  Bit Score: 311.10  E-value: 6.02e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079396235  82 PENIVWHESSICRCDRQQLLQQKGCVIWITGLSGSGKSTVACALSKALFERGKLTYTLDGDNVRHGLNRDLTFKAEDRTE 161
Cdd:PRK03846    1 DENIVWHQHPVTKAQREQLHGHKGVVLWFTGLSGSGKSTVAGALEEALHELGVSTYLLDGDNVRHGLCSDLGFSDADRKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079396235 162 NIRRIGEVAKLFADVGVICIASLISPYRRDRDECRSLLPEGDFVEVFMDVPLSVCESRDPKGLYKLARAGKIKGFTGIDD 241
Cdd:PRK03846   81 NIRRVGEVAKLMVDAGLVVLTAFISPHRAERQMVRERLGEGEFIEVFVDTPLAICEARDPKGLYKKARAGEIRNFTGIDS 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1079396235 242 PYEAPLNCEVVLkHTGDDDScspRQMAEHIISYLQNKGYL 281
Cdd:PRK03846  161 VYEAPESPEIHL-DTGEQLV---TNLVEQLLDYLRQRDII 196
APS_kinase pfam01583
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3 ...
 104-257 1.12e-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: 298.46  E-value: 1.12e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079396235 104 KGCVIWITGLSGSGKSTVACALSKALFERGKLTYTLDGDNVRHGLNRDLTFKAEDRTENIRRIGEVAKLFADVGVICIAS 183
Cdd:pfam01583   1 RGCTIWLTGLSGAGKSTIANALERKLFEQGRSVYVLDGDNVRHGLNKDLGFSEEDRTENIRRIGEVAKLFADAGLIVITA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1079396235 184 LISPYRRDRDECRSLLPEGDFVEVFMDVPLSVCESRDPKGLYKLARAGKIKGFTGIDDPYEAPLNCEVVLKHTG 257
Cdd:pfam01583  81 FISPYREDREQARELHEEGKFIEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDSPYEAPENPELVLDTDK 154
APSK cd02027
Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5 ...
 107-254 2.52e-100

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: 289.76  E-value: 2.52e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079396235 107 VIWITGLSGSGKSTVACALSKALFERGKLTYTLDGDNVRHGLNRDLTFKAEDRTENIRRIGEVAKLFADVGVICIASLIS 186
Cdd:cd02027     1 VIWLTGLSGSGKSTIARALEEKLFQRGRPVYVLDGDNVRHGLNKDLGFSREDREENIRRIAEVAKLLADAGLIVIAAFIS 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1079396235 187 PYRRDRDECRSLLPEGDFVEVFMDVPLSVCESRDPKGLYKLARAGKIKGFTGIDDPYEAPLNCEVVLK 254
Cdd:cd02027    81 PYREDREAARKIIGGGDFLEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDDPYEAPENPDLVLD 148
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
 75-281 2.42e-94

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 290.68  E-value: 2.42e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079396235  75 INGDKNKPENIVWHESSICRCDRQQLLQQKGCVIWITGLSGSGKSTVACALSKALFERGKLTYTLDGDNVRHGLNRDLTF 154
Cdd:PRK05506  430 IDFALRRATNVHWQASDVSREARAARKGQKPATVWFTGLSGSGKSTIANLVERRLHALGRHTYLLDGDNVRHGLNRDLGF 509

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079396235 155 KAEDRTENIRRIGEVAKLFADVGVICIASLISPYRRDRDECRSLLPEGDFVEVFMDVPLSVCESRDPKGLYKLARAGKIK 234
Cdd:PRK05506  510 SDADRVENIRRVAEVARLMADAGLIVLVSFISPFREERELARALHGEGEFVEVFVDTPLEVCEARDPKGLYAKARAGEIK 589

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1079396235 235 GFTGIDDPYEAPLNCEVVLKHTGDddscSPRQMAEHIISYLQNKGYL 281
Cdd:PRK05506  590 NFTGIDSPYEAPENPELRLDTTGR----SPEELAEQVLELLRRRGAI 632
apsK TIGR00455
adenylyl-sulfate kinase; This protein, adenylylsulfate kinase, is often found as a fusion ...
 87-275 2.09e-90

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: 266.26  E-value: 2.09e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079396235  87 WHESsICRCDRQQLLQQKGCVIWITGLSGSGKSTVACALSKALFERGKLTYTLDGDNVRHGLNRDLTFKAEDRTENIRRI 166
Cdd:TIGR00455   1 WHPA-ITKDERQALNGHRGVVIWLTGLSGSGKSTIANALEKKLESKGYRVYVLDGDNVRHGLNKDLGFSEEDRKENIRRI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079396235 167 GEVAKLFADVGVICIASLISPYRRDRDECRSLLPEGDFVEVFMDVPLSVCESRDPKGLYKLARAGKIKGFTGIDDPYEAP 246
Cdd:TIGR00455  80 GEVAKLFVRNGIIVITSFISPYRADRQMVRELIEKGEFIEVFVDCPLEVCEQRDPKGLYKKARNGEIKGFTGIDSPYEAP 159

                         170       180
                  ....*....|....*....|....*....
gi 1079396235 247 LNCEVVLkhtgDDDSCSPRQMAEHIISYL 275
Cdd:TIGR00455 160 ENPEVVL----DTDQNDREECVGQIIEKL 184
PRK00889 PRK00889
adenylylsulfate kinase; Provisional
 102-282 1.24e-73

adenylylsulfate kinase; Provisional


Pssm-ID: 179157  Cd Length: 175  Bit Score: 222.97  E-value: 1.24e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079396235 102 QQKGCVIWITGLSGSGKSTVACALSKALFERGKLTYTLDGDNVRHGLNRDLTFKAEDRTENIRRIGEVAKLFADVGVICI 181
Cdd:PRK00889    1 KQRGVTVWFTGLSGAGKTTIARALAEKLREAGYPVEVLDGDAVRTNLSKGLGFSKEDRDTNIRRIGFVANLLTRHGVIVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079396235 182 ASLISPYRRDRDECRSLLPegDFVEVFMDVPLSVCESRDPKGLYKLARAGKIKGFTGIDDPYEAPLNCEVVLKhtgdDDS 261
Cdd:PRK00889   81 VSAISPYRETREEVRANIG--NFLEVFVDAPLEVCEQRDVKGLYAKARAGEIKHFTGIDDPYEPPLNPEVECR----TDL 154

                         170       180
                  ....*....|....*....|.
gi 1079396235 262 CSPRQMAEHIISYLQNKGYLE 282
Cdd:PRK00889  155 ESLEESVDKVLQKLEELGYLV 175
PRK05537 PRK05537
bifunctional sulfate adenylyltransferase/adenylylsulfate kinase;
103-283 3.71e-63

bifunctional sulfate adenylyltransferase/adenylylsulfate kinase;


Pssm-ID: 180124 [Multi-domain]  Cd Length: 568  Bit Score: 207.99  E-value: 3.71e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079396235 103 QKGCVIWITGLSGSGKSTVACALSKALFE-RGKLTYTLDGDNVRHGLNRDLTFKAEDRTENIRRIGEVAKLFADVGVICI 181
Cdd:PRK05537  390 KQGFTVFFTGLSGAGKSTIAKALMVKLMEmRGRPVTLLDGDVVRKHLSSELGFSKEDRDLNILRIGFVASEITKNGGIAI 469

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079396235 182 ASLISPYRRDRDECRSLLPE-GDFVEVFMDVPLSVCESRDPKGLYKLARAGKIKGFTGIDDPYEAPLNCEVVLkhtgDDD 260
Cdd:PRK05537  470 CAPIAPYRATRREVREMIEAyGGFIEVHVATPLEVCEQRDRKGLYAKAREGKIKGFTGISDPYEPPANPELVI----DTT 545

                         170       180
                  ....*....|....*....|...
gi 1079396235 261 SCSPRQMAEHIISYLQNKGYLEG 283
Cdd:PRK05537  546 NVTPDECAHKILLYLEEKGYLRG 568
PRK05541 PRK05541
adenylylsulfate kinase; Provisional
 103-257 2.54e-29

adenylylsulfate kinase; Provisional


Pssm-ID: 235498  Cd Length: 176  Bit Score: 109.37  E-value: 2.54e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079396235 103 QKGCVIWITGLSGSGKSTVACALSKALFERGKLTYTLDGDNVRHGLNRDlTFKAEDRTENIRRIGEVAKLFADVGVICIA 182
Cdd:PRK05541    5 PNGYVIWITGLAGSGKTTIAKALYERLKLKYSNVIYLDGDELREILGHY-GYDKQSRIEMALKRAKLAKFLADQGMIVIV 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1079396235 183 SLISPYRRDRDECRSLLPegDFVEVFMDVPLSVCESRDPKGLYKLARAGKIKGFTGIDDPYEAPlNCEVVLKHTG 257
Cdd:PRK05541   84 TTISMFDEIYAYNRKHLP--NYFEVYLKCDMEELIRRDQKGLYTKALKGEIKNVVGVDIPFDEP-KADLVIDNSC 155
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
107-219 2.73e-08

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


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 52.22  E-value: 2.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079396235 107 VIWITGLSGSGKSTVACALSKAL-FERgkltytLDGDNVRHGLnRDLTFKAEDRTENIR-----RIGEVAKLFADVG--V 178
Cdd:COG0645     1 LILVCGLPGSGKSTLARALAERLgAVR------LRSDVVRKRL-FGAGLAPLERSPEATartyaRLLALARELLAAGrsV 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1079396235 179 ICIASLISPYRRD--RDECRSLlpEGDFVEVFMDVPLSVCESR 219
Cdd:COG0645    74 ILDATFLRRAQREafRALAEEA--GAPFVLIWLDAPEEVLRER 114
GntK cd02021
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting ...
 107-231 1.04e-07

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: 50.33  E-value: 1.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079396235 107 VIWITGLSGSGKSTVAcalsKALFERGKLTYtLDGDNVRHGLNRD-------LTfkAEDR---TENIRRIGEVAKLFADV 176
Cdd:cd02021     1 IIVVMGVSGSGKSTVG----KALAERLGAPF-IDGDDLHPPANIAkmaagipLN--DEDRwpwLQALTDALLAKLASAGE 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1079396235 177 GVICIASLISpyRRDRDECRSLLPEGDFVEVFMDVPLSVCESRDpkglykLARAG 231
Cdd:cd02021    74 GVVVACSALK--RIYRDILRGGAANPRVRFVHLDGPREVLAERL------AARKG 120
AAA_33 pfam13671
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ...
 107-219 9.19e-05

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: 41.53  E-value: 9.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079396235 107 VIWITGLSGSGKSTVAcalsKALFERGKlTYTLDGDNVRHGLNRDLTFKAEDRTENIRRIGEVAKLFADVG------VIC 180
Cdd:pfam13671   1 LILLVGLPGSGKSTLA----RRLLEELG-AVRLSSDDERKRLFGEGRPSISYYTDATDRTYERLHELARIAlragrpVIL 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1079396235 181 IASLISpyRRDRDECRSLLPEGDFVE--VFMDVPLSVCESR 219
Cdd:pfam13671  76 DATNLR--RDERARLLALAREYGVPVriVVFEAPEEVLRER 114
COG4639 COG4639
Predicted kinase [General function prediction only];
112-220 1.90e-04

Predicted kinase [General function prediction only];


Pssm-ID: 443677 [Multi-domain]  Cd Length: 145  Bit Score: 40.58  E-value: 1.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079396235 112 GLSGSGKSTVAcalsKALFERgklTYTLDGDNVRHGLNRDLT-FKAEDRTENIRRigEVAK--LFADVGVICIASLISpy 188
Cdd:COG4639     9 GLPGSGKSTFA----RRLFAP---TEVVSSDDIRALLGGDENdQSAWGDVFQLAH--EIARarLRAGRLTVVDATNLQ-- 77

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1079396235 189 RRDRDECRSLLPE--GDFVEVFMDVPLSVCESRD 220
Cdd:COG4639    78 REARRRLLALARAygALVVAVVLDVPLEVCLARN 111
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 107-144 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: 38.95  E-value: 4.53e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1079396235 107 VIWITG-LSGSGKSTVACALSKALFERGKLTYTLDGDNV 144
Cdd:cd01983     2 VIAVTGgKGGVGKTTLAAALAVALAAKGYKVLLIDLDDY 40
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
110-173 9.24e-04

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 440188 [Multi-domain]  Cd Length: 204  Bit Score: 39.61  E-value: 9.24e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1079396235 110 ITGLSGSGKSTVACALSKALFERGKLTYTLDGDNVRHGLNR---DLTFKAEDRTENI-RRIGEVAKLF 173
Cdd:COG0419    28 IVGPNGAGKSTILEAIRYALYGKARSRSKLRSDLINVGSEEasvELEFEHGGKRYRIeRRQGEFAEFL 95
NK cd02019
Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of ...
 107-133 3.07e-03

Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of enzymes that share structural similarity and are functionally related to the catalysis of the reversible phosphate group transfer from nucleoside triphosphates to nucleosides/nucleotides, nucleoside monophosphates, or sugars. Members of this family play a wide variety of essential roles in nucleotide metabolism, the biosynthesis of coenzymes and aromatic compounds, as well as the metabolism of sugar and sulfate.


Pssm-ID: 238977 [Multi-domain]  Cd Length: 69  Bit Score: 35.39  E-value: 3.07e-03
                          10        20
                  ....*....|....*....|....*..
gi 1079396235 107 VIWITGLSGSGKSTVACALSKALFERG 133
Cdd:cd02019     1 IIAITGGSGSGKSTVAKKLAEQLGGRS 27
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 110-176 3.78e-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: 36.97  E-value: 3.78e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1079396235  110 ITGLSGSGKSTVACALSKALFERGKLTYTLDGDNVRHGLNRDLTFKAEDRTE-NIRRIGEVAKLFADV 176
Cdd:smart00382   7 IVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKaSGSGELRLRLALALA 74
archRadB cd01394
archaeal RadB; The archaeal protein RadB shares similarity RadA, the archaeal functional ...
 103-201 4.58e-03

archaeal RadB; The archaeal protein RadB shares similarity RadA, the archaeal functional homologue to the bacterial RecA. The precise function of RadB is unclear.


Pssm-ID: 410882 [Multi-domain]  Cd Length: 216  Bit Score: 37.68  E-value: 4.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079396235 103 QKGCVIWITGLSGSGKSTVACALSKALFERGKLTYTLD-------------GDNVRHGLNRDLTFKAEDRTENIRRIGEV 169
Cdd:cd01394    17 ERGTITQIYGPPGSGKTNICLQLAVEAAKQGKKVVYIDteglsperfqqiaGERFESIASNIIVFEPYSFDEQGVAIQEA 96

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1079396235 170 AKLF--ADVGVICIASLISPYRRDRDECRSLLPE 201
Cdd:cd01394    97 EKLLksDKVDLVVVDSATALYRLELGDDSEANRE 130
pseT PHA02530
polynucleotide kinase; Provisional
 108-222 4.73e-03

polynucleotide kinase; Provisional


Pssm-ID: 222856 [Multi-domain]  Cd Length: 300  Bit Score: 37.69  E-value: 4.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1079396235 108 IWIT-GLSGSGKSTVAcalsKALFERGKLTYTLDGDNVR-----HGLNRDLTFKA--EDRTENIRRIGEVAKLFADVGVI 179
Cdd:PHA02530    4 IILTvGVPGSGKSTWA----REFAAKNPKAVNVNRDDLRqslfgHGEWGEYKFTKekEDLVTKAQEAAALAALKSGKSVI 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1079396235 180 CIASLISPYRrdRDECRSLLPE--GDFVEVFMDVPLSVCESRDPK 222
Cdd:PHA02530   80 ISDTNLNPER--RRKWKELAKElgAEFEEKVFDVPVEELVKRNRK 122
GntK COG3265
Gluconate kinase [Carbohydrate transport and metabolism]; Gluconate kinase is part of the ...
 105-142 7.44e-03

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: 36.26  E-value: 7.44e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1079396235 105 GCVIWITGLSGSGKSTVACALSKALfergKLTYtLDGD 142
Cdd:COG3265     1 PMVIVVMGVSGSGKSTVGQALAERL----GWPF-IDGD 33
AAA_18 pfam13238
AAA domain;
108-129 9.12e-03

AAA domain;


Pssm-ID: 433052 [Multi-domain]  Cd Length: 128  Bit Score: 35.48  E-value: 9.12e-03
                          10        20
                  ....*....|....*....|..
gi 1079396235 108 IWITGLSGSGKSTVACALSKAL 129
Cdd:pfam13238   1 ILITGTPGVGKTTLAKELSKRL 22
 
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.
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