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Conserved domains on  [gi|1063709285|ref|NP_001319463|]
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adenosine-5'-phosphosulfate (APS) kinase 3 [Arabidopsis thaliana]

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]; ...
 15-205 1.36e-110

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: 314.33  E-value: 1.36e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063709285  15 SPIGKTERQKLLNQKGCVVWITGLSGSGKSTLACSLSRELNNRGKLSYILDGDNLRHGLNKDLGFKAEDRVENIRRVGEV 94
Cdd:COG0529     1 SAVTREERAALKGQKGFVVWFTGLSGSGKSTLANALERRLFERGRHVYLLDGDNVRHGLNKDLGFSKEDRDENIRRIGEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063709285  95 AKLFADAGLICIASLISPYRKDRDACREMIQNSSFIEVFMNMSLQLCEARDPKGLYKLARAGKIKGFTGIDDPYESPLNC 174
Cdd:COG0529    81 AKLLADAGLIVLVAFISPYRADREEARELIGEGEFIEVYVDTPLEVCEARDPKGLYAKARAGEIKNFTGIDDPYEAPENP 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1063709285 175 EIELkekEGECPSPVAMAEEVISYLEDKGFL 205
Cdd:COG0529   161 ELVL---DTDKESVEESVEKILAYLEERGYI 188
 
Name Accession Description Interval E-value
CysC COG0529
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ...
 15-205 1.36e-110

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: 314.33  E-value: 1.36e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063709285  15 SPIGKTERQKLLNQKGCVVWITGLSGSGKSTLACSLSRELNNRGKLSYILDGDNLRHGLNKDLGFKAEDRVENIRRVGEV 94
Cdd:COG0529     1 SAVTREERAALKGQKGFVVWFTGLSGSGKSTLANALERRLFERGRHVYLLDGDNVRHGLNKDLGFSKEDRDENIRRIGEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063709285  95 AKLFADAGLICIASLISPYRKDRDACREMIQNSSFIEVFMNMSLQLCEARDPKGLYKLARAGKIKGFTGIDDPYESPLNC 174
Cdd:COG0529    81 AKLLADAGLIVLVAFISPYRADREEARELIGEGEFIEVYVDTPLEVCEARDPKGLYAKARAGEIKNFTGIDDPYEAPENP 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1063709285 175 EIELkekEGECPSPVAMAEEVISYLEDKGFL 205
Cdd:COG0529   161 ELVL---DTDKESVEESVEKILAYLEERGYI 188
PRK03846 PRK03846
adenylylsulfate kinase; Provisional
 7-206 4.73e-100

adenylylsulfate kinase; Provisional


Pssm-ID: 179661  Cd Length: 198  Bit Score: 287.99  E-value: 4.73e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063709285   7 STNIFWQESPIGKTERQKLLNQKGCVVWITGLSGSGKSTLACSLSRELNNRGKLSYILDGDNLRHGLNKDLGFKAEDRVE 86
Cdd:PRK03846    1 DENIVWHQHPVTKAQREQLHGHKGVVLWFTGLSGSGKSTVAGALEEALHELGVSTYLLDGDNVRHGLCSDLGFSDADRKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063709285  87 NIRRVGEVAKLFADAGLICIASLISPYRKDRDACREMIQNSSFIEVFMNMSLQLCEARDPKGLYKLARAGKIKGFTGIDD 166
Cdd:PRK03846   81 NIRRVGEVAKLMVDAGLVVLTAFISPHRAERQMVRERLGEGEFIEVFVDTPLAICEARDPKGLYKKARAGEIRNFTGIDS 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1063709285 167 PYESPLNCEIELKEKEGECPSPVamaEEVISYLEDKGFLQ 206
Cdd:PRK03846  161 VYEAPESPEIHLDTGEQLVTNLV---EQLLDYLRQRDIIR 197
APSK cd02027
Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5 ...
 32-179 1.55e-99

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: 284.76  E-value: 1.55e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063709285  32 VVWITGLSGSGKSTLACSLSRELNNRGKLSYILDGDNLRHGLNKDLGFKAEDRVENIRRVGEVAKLFADAGLICIASLIS 111
Cdd:cd02027     1 VIWLTGLSGSGKSTIARALEEKLFQRGRPVYVLDGDNVRHGLNKDLGFSREDREENIRRIAEVAKLLADAGLIVIAAFIS 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063709285 112 PYRKDRDACREMIQNSSFIEVFMNMSLQLCEARDPKGLYKLARAGKIKGFTGIDDPYESPLNCEIELK 179
Cdd:cd02027    81 PYREDREAARKIIGGGDFLEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDDPYEAPENPDLVLD 148
APS_kinase pfam01583
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3 ...
 29-179 1.18e-98

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: 282.67  E-value: 1.18e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063709285  29 KGCVVWITGLSGSGKSTLACSLSRELNNRGKLSYILDGDNLRHGLNKDLGFKAEDRVENIRRVGEVAKLFADAGLICIAS 108
Cdd:pfam01583   1 RGCTIWLTGLSGAGKSTIANALERKLFEQGRSVYVLDGDNVRHGLNKDLGFSEEDRTENIRRIGEVAKLFADAGLIVITA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063709285 109 LISPYRKDRDACREMIQNSSFIEVFMNMSLQLCEARDPKGLYKLARAGKIKGFTGIDDPYESPLNCEIELK 179
Cdd:pfam01583  81 FISPYREDREQARELHEEGKFIEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDSPYEAPENPELVLD 151
apsK TIGR00455
adenylyl-sulfate kinase; This protein, adenylylsulfate kinase, is often found as a fusion ...
 12-179 1.31e-83

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: 245.84  E-value: 1.31e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063709285  12 WQESpIGKTERQKLLNQKGCVVWITGLSGSGKSTLACSLSRELNNRGKLSYILDGDNLRHGLNKDLGFKAEDRVENIRRV 91
Cdd:TIGR00455   1 WHPA-ITKDERQALNGHRGVVIWLTGLSGSGKSTIANALEKKLESKGYRVYVLDGDNVRHGLNKDLGFSEEDRKENIRRI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063709285  92 GEVAKLFADAGLICIASLISPYRKDRDACREMIQNSSFIEVFMNMSLQLCEARDPKGLYKLARAGKIKGFTGIDDPYESP 171
Cdd:TIGR00455  80 GEVAKLFVRNGIIVITSFISPYRADRQMVRELIEKGEFIEVFVDCPLEVCEQRDPKGLYKKARNGEIKGFTGIDSPYEAP 159


                  ....*...
gi 1063709285 172 LNCEIELK 179
Cdd:TIGR00455 160 ENPEVVLD 167
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 35-101 2.53e-05

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: 42.75  E-value: 2.53e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063709285   35 ITGLSGSGKSTLACSLSRELNNRGKLSYILDGDNLRHG-LNKDLGFKAEDRVENIRRVGEVAKLFADA 101
Cdd:smart00382   7 IVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEvLDQLLLIIVGGKKASGSGELRLRLALALA 74
 
Name Accession Description Interval E-value
CysC COG0529
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ...
 15-205 1.36e-110

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: 314.33  E-value: 1.36e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063709285  15 SPIGKTERQKLLNQKGCVVWITGLSGSGKSTLACSLSRELNNRGKLSYILDGDNLRHGLNKDLGFKAEDRVENIRRVGEV 94
Cdd:COG0529     1 SAVTREERAALKGQKGFVVWFTGLSGSGKSTLANALERRLFERGRHVYLLDGDNVRHGLNKDLGFSKEDRDENIRRIGEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063709285  95 AKLFADAGLICIASLISPYRKDRDACREMIQNSSFIEVFMNMSLQLCEARDPKGLYKLARAGKIKGFTGIDDPYESPLNC 174
Cdd:COG0529    81 AKLLADAGLIVLVAFISPYRADREEARELIGEGEFIEVYVDTPLEVCEARDPKGLYAKARAGEIKNFTGIDDPYEAPENP 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1063709285 175 EIELkekEGECPSPVAMAEEVISYLEDKGFL 205
Cdd:COG0529   161 ELVL---DTDKESVEESVEKILAYLEERGYI 188
PRK03846 PRK03846
adenylylsulfate kinase; Provisional
 7-206 4.73e-100

adenylylsulfate kinase; Provisional


Pssm-ID: 179661  Cd Length: 198  Bit Score: 287.99  E-value: 4.73e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063709285   7 STNIFWQESPIGKTERQKLLNQKGCVVWITGLSGSGKSTLACSLSRELNNRGKLSYILDGDNLRHGLNKDLGFKAEDRVE 86
Cdd:PRK03846    1 DENIVWHQHPVTKAQREQLHGHKGVVLWFTGLSGSGKSTVAGALEEALHELGVSTYLLDGDNVRHGLCSDLGFSDADRKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063709285  87 NIRRVGEVAKLFADAGLICIASLISPYRKDRDACREMIQNSSFIEVFMNMSLQLCEARDPKGLYKLARAGKIKGFTGIDD 166
Cdd:PRK03846   81 NIRRVGEVAKLMVDAGLVVLTAFISPHRAERQMVRERLGEGEFIEVFVDTPLAICEARDPKGLYKKARAGEIRNFTGIDS 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1063709285 167 PYESPLNCEIELKEKEGECPSPVamaEEVISYLEDKGFLQ 206
Cdd:PRK03846  161 VYEAPESPEIHLDTGEQLVTNLV---EQLLDYLRQRDIIR 197
APSK cd02027
Adenosine 5'-phosphosulfate kinase (APSK) catalyzes the phosphorylation of adenosine 5 ...
 32-179 1.55e-99

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: 284.76  E-value: 1.55e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063709285  32 VVWITGLSGSGKSTLACSLSRELNNRGKLSYILDGDNLRHGLNKDLGFKAEDRVENIRRVGEVAKLFADAGLICIASLIS 111
Cdd:cd02027     1 VIWLTGLSGSGKSTIARALEEKLFQRGRPVYVLDGDNVRHGLNKDLGFSREDREENIRRIAEVAKLLADAGLIVIAAFIS 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063709285 112 PYRKDRDACREMIQNSSFIEVFMNMSLQLCEARDPKGLYKLARAGKIKGFTGIDDPYESPLNCEIELK 179
Cdd:cd02027    81 PYREDREAARKIIGGGDFLEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDDPYEAPENPDLVLD 148
APS_kinase pfam01583
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3 ...
 29-179 1.18e-98

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: 282.67  E-value: 1.18e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063709285  29 KGCVVWITGLSGSGKSTLACSLSRELNNRGKLSYILDGDNLRHGLNKDLGFKAEDRVENIRRVGEVAKLFADAGLICIAS 108
Cdd:pfam01583   1 RGCTIWLTGLSGAGKSTIANALERKLFEQGRSVYVLDGDNVRHGLNKDLGFSEEDRTENIRRIGEVAKLFADAGLIVITA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063709285 109 LISPYRKDRDACREMIQNSSFIEVFMNMSLQLCEARDPKGLYKLARAGKIKGFTGIDDPYESPLNCEIELK 179
Cdd:pfam01583  81 FISPYREDREQARELHEEGKFIEVFVDTPLEVCEQRDPKGLYKKARAGEIKGFTGIDSPYEAPENPELVLD 151
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
 7-205 1.00e-94

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 288.75  E-value: 1.00e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063709285   7 STNIFWQESPIGKTERQKLLNQKGCVVWITGLSGSGKSTLACSLSRELNNRGKLSYILDGDNLRHGLNKDLGFKAEDRVE 86
Cdd:PRK05506  437 ATNVHWQASDVSREARAARKGQKPATVWFTGLSGSGKSTIANLVERRLHALGRHTYLLDGDNVRHGLNRDLGFSDADRVE 516

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063709285  87 NIRRVGEVAKLFADAGLICIASLISPYRKDRDACREMIQNSSFIEVFMNMSLQLCEARDPKGLYKLARAGKIKGFTGIDD 166
Cdd:PRK05506  517 NIRRVAEVARLMADAGLIVLVSFISPFREERELARALHGEGEFVEVFVDTPLEVCEARDPKGLYAKARAGEIKNFTGIDS 596

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1063709285 167 PYESPLNCEIELKEKEGecpSPVAMAEEVISYLEDKGFL 205
Cdd:PRK05506  597 PYEAPENPELRLDTTGR---SPEELAEQVLELLRRRGAI 632
apsK TIGR00455
adenylyl-sulfate kinase; This protein, adenylylsulfate kinase, is often found as a fusion ...
 12-179 1.31e-83

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: 245.84  E-value: 1.31e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063709285  12 WQESpIGKTERQKLLNQKGCVVWITGLSGSGKSTLACSLSRELNNRGKLSYILDGDNLRHGLNKDLGFKAEDRVENIRRV 91
Cdd:TIGR00455   1 WHPA-ITKDERQALNGHRGVVIWLTGLSGSGKSTIANALEKKLESKGYRVYVLDGDNVRHGLNKDLGFSEEDRKENIRRI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063709285  92 GEVAKLFADAGLICIASLISPYRKDRDACREMIQNSSFIEVFMNMSLQLCEARDPKGLYKLARAGKIKGFTGIDDPYESP 171
Cdd:TIGR00455  80 GEVAKLFVRNGIIVITSFISPYRADRQMVRELIEKGEFIEVFVDCPLEVCEQRDPKGLYKKARNGEIKGFTGIDSPYEAP 159


                  ....*...
gi 1063709285 172 LNCEIELK 179
Cdd:TIGR00455 160 ENPEVVLD 167
PRK00889 PRK00889
adenylylsulfate kinase; Provisional
 27-206 2.13e-69

adenylylsulfate kinase; Provisional


Pssm-ID: 179157  Cd Length: 175  Bit Score: 209.49  E-value: 2.13e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063709285  27 NQKGCVVWITGLSGSGKSTLACSLSRELNNRGKLSYILDGDNLRHGLNKDLGFKAEDRVENIRRVGEVAKLFADAGLICI 106
Cdd:PRK00889    1 KQRGVTVWFTGLSGAGKTTIARALAEKLREAGYPVEVLDGDAVRTNLSKGLGFSKEDRDTNIRRIGFVANLLTRHGVIVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063709285 107 ASLISPYRKDRDACREMIQNssFIEVFMNMSLQLCEARDPKGLYKLARAGKIKGFTGIDDPYESPLNCEIELKEKEGECP 186
Cdd:PRK00889   81 VSAISPYRETREEVRANIGN--FLEVFVDAPLEVCEQRDVKGLYAKARAGEIKHFTGIDDPYEPPLNPEVECRTDLESLE 158

                         170       180
                  ....*....|....*....|
gi 1063709285 187 SPVAmaeEVISYLEDKGFLQ 206
Cdd:PRK00889  159 ESVD---KVLQKLEELGYLV 175
PRK05537 PRK05537
bifunctional sulfate adenylyltransferase/adenylylsulfate kinase;
27-205 1.97e-62

bifunctional sulfate adenylyltransferase/adenylylsulfate kinase;


Pssm-ID: 180124 [Multi-domain]  Cd Length: 568  Bit Score: 202.98  E-value: 1.97e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063709285  27 NQKGCVVWITGLSGSGKSTLACSL-SRELNNRGKLSYILDGDNLRHGLNKDLGFKAEDRVENIRRVGEVAKLFADAGLIC 105
Cdd:PRK05537  389 HKQGFTVFFTGLSGAGKSTIAKALmVKLMEMRGRPVTLLDGDVVRKHLSSELGFSKEDRDLNILRIGFVASEITKNGGIA 468

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063709285 106 IASLISPYRKDRDACREMIQNS-SFIEVFMNMSLQLCEARDPKGLYKLARAGKIKGFTGIDDPYESPLNCEIELKEKEge 184
Cdd:PRK05537  469 ICAPIAPYRATRREVREMIEAYgGFIEVHVATPLEVCEQRDRKGLYAKAREGKIKGFTGISDPYEPPANPELVIDTTN-- 546

                         170       180
                  ....*....|....*....|.
gi 1063709285 185 cPSPVAMAEEVISYLEDKGFL 205
Cdd:PRK05537  547 -VTPDECAHKILLYLEEKGYL 566
PRK05541 PRK05541
adenylylsulfate kinase; Provisional
 28-171 5.68e-28

adenylylsulfate kinase; Provisional


Pssm-ID: 235498  Cd Length: 176  Bit Score: 103.60  E-value: 5.68e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063709285  28 QKGCVVWITGLSGSGKSTLACSLSRELNNRGKLSYILDGDNLRHGLNKDlGFKAEDRVENIRRVGEVAKLFADAGLICIA 107
Cdd:PRK05541    5 PNGYVIWITGLAGSGKTTIAKALYERLKLKYSNVIYLDGDELREILGHY-GYDKQSRIEMALKRAKLAKFLADQGMIVIV 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063709285 108 SLISPYRKDRDACREMIQNssFIEVFMNMSLQLCEARDPKGLYKLARAGKIKGFTGIDDPYESP 171
Cdd:PRK05541   84 TTISMFDEIYAYNRKHLPN--YFEVYLKCDMEELIRRDQKGLYTKALKGEIKNVVGVDIPFDEP 145
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
32-144 3.24e-06

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


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 45.29  E-value: 3.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063709285  32 VVWITGLSGSGKSTLACSLSRELNNRgklsyILDGDNLRHGLNKDLGFKAEDRVENIRRV----GEVAKLFADAGLICIA 107
Cdd:COG0645     1 LILVCGLPGSGKSTLARALAERLGAV-----RLRSDVVRKRLFGAGLAPLERSPEATARTyarlLALARELLAAGRSVIL 75

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1063709285 108 SLISPYRKDRDACREMIQ--NSSFIEVFMNMSLQLCEAR 144
Cdd:COG0645    76 DATFLRRAQREAFRALAEeaGAPFVLIWLDAPEEVLRER 114
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 35-101 2.53e-05

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: 42.75  E-value: 2.53e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063709285   35 ITGLSGSGKSTLACSLSRELNNRGKLSYILDGDNLRHG-LNKDLGFKAEDRVENIRRVGEVAKLFADA 101
Cdd:smart00382   7 IVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEvLDQLLLIIVGGKKASGSGELRLRLALALA 74
COG4639 COG4639
Predicted kinase [General function prediction only];
37-145 1.14e-04

Predicted kinase [General function prediction only];


Pssm-ID: 443677 [Multi-domain]  Cd Length: 145  Bit Score: 40.58  E-value: 1.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063709285  37 GLSGSGKSTLAcslsRELNnrgKLSYILDGDNLRHGLNKDLG-FKAEDRVENIRRvgEVAKLFADAGLICI--ASLISP- 112
Cdd:COG4639     9 GLPGSGKSTFA----RRLF---APTEVVSSDDIRALLGGDENdQSAWGDVFQLAH--EIARARLRAGRLTVvdATNLQRe 79

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1063709285 113 YRKD-RDACREmiQNSSFIEVFMNMSLQLCEARD 145
Cdd:COG4639    80 ARRRlLALARA--YGALVVAVVLDVPLEVCLARN 111
AAA_33 pfam13671
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ...
 32-107 5.20e-04

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: 38.83  E-value: 5.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063709285  32 VVWITGLSGSGKSTLACSLSRELNnrgklSYILDGDNLRHGLNKDLGFKAEDRVENI----RRVGEVAKLFADAGLICIA 107
Cdd:pfam13671   1 LILLVGLPGSGKSTLARRLLEELG-----AVRLSSDDERKRLFGEGRPSISYYTDATdrtyERLHELARIALRAGRPVIL 75
ExeA COG3267
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ...
 26-106 8.31e-04

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: 39.39  E-value: 8.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063709285  26 LNQKGCVVWITGLSGSGKSTLACSLSRELNNRGKLSYI----LDGDNLRHGLNKDLG--FKAEDRVENIRRVGEVAKLFA 99
Cdd:COG3267    39 LAQGGGFVVLTGEVGTGKTTLLRRLLERLPDDVKVAYIpnpqLSPAELLRAIADELGlePKGASKADLLRQLQEFLLELA 118

                          90
                  ....*....|
gi 1063709285 100 DAG---LICI 106
Cdd:COG3267   119 AAGrrvVLII 128
AAA_18 pfam13238
AAA domain;
33-98 9.03e-04

AAA domain;


Pssm-ID: 433052 [Multi-domain]  Cd Length: 128  Bit Score: 37.79  E-value: 9.03e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063709285  33 VWITGLSGSGKSTLACSLSRELNNRGKLSYILDGDNLRHGlnkDLGFKAEDRVENIRRVGEVAKLF 98
Cdd:pfam13238   1 ILITGTPGVGKTTLAKELSKRLGFGDNVRDLALENGLVLG---DDPETRESKRLDEDKLDRLLDLL 63
GntK cd02021
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting ...
 35-156 9.35e-04

Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting product gluconate-6-phoshate is an important precursor of gluconate metabolism. GntK acts as a dimmer composed of two identical subunits.


Pssm-ID: 238979 [Multi-domain]  Cd Length: 150  Bit Score: 38.39  E-value: 9.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063709285  35 ITGLSGSGKSTLACSLSRELNNRgklsYIlDGDNLRHGLNKDlgfKA--------EDR---VENIRRVGEVAKLFADAGL 103
Cdd:cd02021     4 VMGVSGSGKSTVGKALAERLGAP----FI-DGDDLHPPANIA---KMaagiplndEDRwpwLQALTDALLAKLASAGEGV 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1063709285 104 ICIASLISpyRKDRDACREMIQNSSFIEVFMNMSLQLCEARDpkglykLARAG 156
Cdd:cd02021    76 VVACSALK--RIYRDILRGGAANPRVRFVHLDGPREVLAERL------AARKG 120
UvrA COG0178
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
32-47 1.19e-03

Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];


Pssm-ID: 439948 [Multi-domain]  Cd Length: 941  Bit Score: 39.24  E-value: 1.19e-03
                          10
                  ....*....|....*.
gi 1063709285  32 VVwITGLSGSGKSTLA 47
Cdd:COG0178    29 VV-ITGLSGSGKSSLA 43
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
 28-71 1.24e-03

ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213195 [Multi-domain]  Cd Length: 171  Bit Score: 38.13  E-value: 1.24e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1063709285  28 QKGCVVWITGLSGSGKSTLACSLSREL-NNRGKLSyiLDGDNLRH 71
Cdd:cd03228    26 KPGEKVAIVGPSGSGKSTLLKLLLRLYdPTSGEIL--IDGVDLRD 68
gntK PRK11545
gluconokinase;
37-144 1.86e-03

gluconokinase;


Pssm-ID: 236926  Cd Length: 163  Bit Score: 37.39  E-value: 1.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063709285  37 GLSGSGKSTLACSLSRELNnrgklSYILDGDNLR-----------HGLNKDlgfkaeDRVENIRRVGEVAklFA-----D 100
Cdd:PRK11545    2 GVSGSGKSAVASEVAHQLH-----AAFLDGDFLHprrniekmasgEPLNDD------DRKPWLQALNDAA--FAmqrtnK 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1063709285 101 AGLICIASLISPYrkdRDACREMIQNSSFIevFMNMSLQLCEAR 144
Cdd:PRK11545   69 VSLIVCSALKKHY---RDLLREGNPNLSFI--YLKGDFDVIESR 107
uvrA PRK00349
excinuclease ABC subunit UvrA;
32-47 2.66e-03

excinuclease ABC subunit UvrA;


Pssm-ID: 234734 [Multi-domain]  Cd Length: 943  Bit Score: 38.13  E-value: 2.66e-03
                          10
                  ....*....|....*.
gi 1063709285  32 VVwITGLSGSGKSTLA 47
Cdd:PRK00349   29 VV-FTGLSGSGKSSLA 43
PRK09270 PRK09270
nucleoside triphosphate hydrolase domain-containing protein; Reviewed
 32-91 3.37e-03

nucleoside triphosphate hydrolase domain-containing protein; Reviewed


Pssm-ID: 236442  Cd Length: 229  Bit Score: 37.22  E-value: 3.37e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063709285  32 VVWITGLSGSGKSTLACSLSRELNNRGKLSYI---LDG---DN---LRHGLNKDLG----FKAEDRVENIRRV 91
Cdd:PRK09270   35 IVGIAGPPGAGKSTLAEFLEALLQQDGELPAIqvpMDGfhlDNavlDAHGLRPRKGapetFDVAGLAALLRRL 107
NK cd02019
Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of ...
 32-58 3.49e-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: 35.00  E-value: 3.49e-03
                          10        20
                  ....*....|....*....|....*..
gi 1063709285  32 VVWITGLSGSGKSTLACSLSRELNNRG 58
Cdd:cd02019     1 IIAITGGSGSGKSTVAKKLAEQLGGRS 27
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
 28-70 3.65e-03

ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440740 [Multi-domain]  Cd Length: 514  Bit Score: 37.58  E-value: 3.65e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1063709285  28 QKGCVVWITGLSGSGKSTLACSLSRELNNRGKL--SYILDGDNLR 70
Cdd:COG1123    30 APGETVALVGESGSGKSTLALALMGLLPHGGRIsgEVLLDGRDLL 74
MobB cd03116
molybdopterin-guanine dinucleotide biosynthesis protein B; Molybdenum is an essential trace ...
 31-58 4.20e-03

molybdopterin-guanine dinucleotide biosynthesis protein B; Molybdenum is an essential trace element in the form of molybdenum cofactor (Moco) which is associated with the metabolism of nitrogen, carbon and sulfur by redox active enzymes. In Escherichia coli, the synthesis of Moco involves genes from several loci: moa, mob, mod, moe and mog. The mob locus contains mobA and mobB genes. MobB catalyzes the attachment of the guanine dinucleotide to molybdopterin.


Pssm-ID: 349770 [Multi-domain]  Cd Length: 157  Bit Score: 36.46  E-value: 4.20e-03
                          10        20
                  ....*....|....*....|....*...
gi 1063709285  31 CVVWITGLSGSGKSTLACSLSRELNNRG 58
Cdd:cd03116     1 KIVGVVGKSGSGKTTLIEKLIPELKARG 28
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 37-69 4.30e-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: 35.48  E-value: 4.30e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1063709285  37 GLSGSGKSTLACSLSRELNNRGKLSYILDGDNL 69
Cdd:cd01983     8 GKGGVGKTTLAAALAVALAAKGYKVLLIDLDDY 40
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
 28-71 5.42e-03

ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444012 [Multi-domain]  Cd Length: 563  Bit Score: 37.04  E-value: 5.42e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1063709285  28 QKGCVVWITGLSGSGKSTLACSLSREL-NNRGKLSyiLDGDNLRH 71
Cdd:COG4988   361 PPGERVALVGPSGAGKSTLLNLLLGFLpPYSGSIL--INGVDLSD 403
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 27-67 5.97e-03

partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved family of bacterial proteins implicated in chromosome segregation. ParB binds to DNA sequences adjacent to the origin of replication and localizes to opposite cell poles shortly following the initiation of DNA replication. ParB regulates the ParA ATPase activity by promoting nucleotide exchange in a fashion reminiscent of the exchange factors of eukaryotic G proteins. ADP-bound ParA binds single-stranded DNA, whereas the ATP-bound form dissociates ParB from its DNA binding sites. Increasing the fraction of ParA-ADP in the cell inhibits cell division, suggesting that this simple nucleotide switch may regulate cytokinesis. ParA shares sequence similarity to a conserved and widespread family of ATPases which includes the repA protein of the repABC operon in Rhizobium etli symbiotic plasmid. This operon is involved in the plasmid replication and partition.


Pssm-ID: 349760 [Multi-domain]  Cd Length: 130  Bit Score: 35.59  E-value: 5.97e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1063709285  27 NQKGcvvwitglsGSGKSTLACSLSRELNNRGKLSYILDGD 67
Cdd:cd02042     7 NQKG---------GVGKTTLAVNLAAALALRGKRVLLIDLD 38
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
29-131 6.16e-03

lipid A ABC transporter ATP-binding protein/permease MsbA;


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 36.92  E-value: 6.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063709285  29 KGCVVWITGLSGSGKSTLACSLSRELN-NRGKLsyILDGDNLRhglnkdlgfkaEDRVENIRR----VGEVAKLFADAgl 103
Cdd:PRK11176  368 AGKTVALVGRSGSGKSTIANLLTRFYDiDEGEI--LLDGHDLR-----------DYTLASLRNqvalVSQNVHLFNDT-- 432

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1063709285 104 icIASLISPYRKDRDAcREMIQNSS-------FIE 131
Cdd:PRK11176  433 --IANNIAYARTEQYS-REQIEEAArmayamdFIN 464
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
 29-77 6.50e-03

ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213179 [Multi-domain]  Cd Length: 157  Bit Score: 35.68  E-value: 6.50e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1063709285  29 KGCVVWITGLSGSGKSTLACSLSRELN-NRGKLsyILDGDNLRHGLNKDL 77
Cdd:cd00267    24 AGEIVALVGPNGSGKSTLLRAIAGLLKpTSGEI--LIDGKDIAKLPLEEL 71
MobB pfam03205
Molybdopterin guanine dinucleotide synthesis protein B; This protein contains a P-loop.
 32-63 6.59e-03

Molybdopterin guanine dinucleotide synthesis protein B; This protein contains a P-loop.


Pssm-ID: 427196 [Multi-domain]  Cd Length: 133  Bit Score: 35.60  E-value: 6.59e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1063709285  32 VVWITGLSGSGKSTLACSLSRELNNRG-KLSYI 63
Cdd:pfam03205   1 ILGIVGWSGSGKTTLLEKLIPELKARGlRVGTI 33
MobB COG1763
Molybdopterin-guanine dinucleotide biosynthesis protein [Coenzyme transport and metabolism]; ...
 32-63 6.70e-03

Molybdopterin-guanine dinucleotide biosynthesis protein [Coenzyme transport and metabolism]; Molybdopterin-guanine dinucleotide biosynthesis protein is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 441369 [Multi-domain]  Cd Length: 162  Bit Score: 35.93  E-value: 6.70e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1063709285  32 VVWITGLSGSGKSTLACSLSRELNNRG-KLSYI 63
Cdd:COG1763     3 VLGIVGYSGSGKTTLLEKLIPELKARGlRVGTI 35
pseT PHA02530
polynucleotide kinase; Provisional
 33-147 6.72e-03

polynucleotide kinase; Provisional


Pssm-ID: 222856 [Multi-domain]  Cd Length: 300  Bit Score: 36.54  E-value: 6.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063709285  33 VWIT-GLSGSGKSTLAcslsRELNNRGKLSYILDGDNLR---HGLNKDLGFK----AEDRVENIRRVGEVAKLFADAGLI 104
Cdd:PHA02530    4 IILTvGVPGSGKSTWA----REFAAKNPKAVNVNRDDLRqslFGHGEWGEYKftkeKEDLVTKAQEAAALAALKSGKSVI 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1063709285 105 CIASLISPyrKDRDACREMIQ--NSSFIEVFMNMSLQLCEARDPK 147
Cdd:PHA02530   80 ISDTNLNP--ERRRKWKELAKelGAEFEEKVFDVPVEELVKRNRK 122
uvrA PRK00349
excinuclease ABC subunit UvrA;
30-56 8.84e-03

excinuclease ABC subunit UvrA;


Pssm-ID: 234734 [Multi-domain]  Cd Length: 943  Bit Score: 36.59  E-value: 8.84e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1063709285  30 GCVVWITGLSGSGKST-----LACSLSRELNN 56
Cdd:PRK00349  635 GKFTCVTGVSGSGKSTlinetLYKALARKLNG 666
 
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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