NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|767243132|gb|AJT21666|]
View 

Bio4p [Saccharomyces cerevisiae YJM1341]

Protein Classification

P-loop NTPase family protein( domain architecture ID 1562424)

P-loop NTPase (nucleoside triphosphate hydrolase) family protein contains two conserved sequence signatures, the Walker A motif (the P-loop proper) and Walker B motif which bind, respectively, the beta and gamma phosphate moieties of the bound nucleotide (typically ATP or GTP), and a Mg(2+) cation

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
P-loop_NTPase super family cl38936
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...
15-186 2.20e-73

P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.


The actual alignment was detected with superfamily member TIGR00347:

Pssm-ID: 476819 [Multi-domain]  Cd Length: 166  Bit Score: 220.31  E-value: 2.20e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243132   15 FVTGTDTDVGKTFVSTLLVHKWK-----AAYWKPVQTGIESDQGDSETLKNFKIAASTWQppiFTPTYALQKPLSPLQAM 89
Cdd:TIGR00347   1 FVTGTDTGVGKTVASSALAAKLKkagysVGYYKPVQTGIEKTNSDALLLQNISGTALDWD---EVNPYAFALPLSPHIAA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243132   90 EYEPN-VDIRLLDFVVPEEWSAENPLVVEGAGGVCVPITrKLEITTDLIKHLietsghPVYVVVVARSGLGTLNHTLLTW 168
Cdd:TIGR00347  78 DQEGRpIDLEELSKHLRTLEQKYDFVLVEGAGGLCVPIT-EEYTTADLIKLL------QLPVILVVRVKLGTINHTLLTV 150
                         170
                  ....*....|....*...
gi 767243132  169 NHLCDNGLRshLFGVILN 186
Cdd:TIGR00347 151 EHARQTGLT--LAGVILN 166
 
Name Accession Description Interval E-value
bioD TIGR00347
dethiobiotin synthase; Dethiobiotin synthase is involved in biotin biosynthesis and catalyses ...
15-186 2.20e-73

dethiobiotin synthase; Dethiobiotin synthase is involved in biotin biosynthesis and catalyses the reaction (CO2 + 7,8-diaminononanoate + ATP = dethiobiotin + phosphate + ADP). The enzyme binds ATP (see motif in first 12 residues of the SEED alignment) and requires magnesium as a co-factor. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]


Pssm-ID: 129447 [Multi-domain]  Cd Length: 166  Bit Score: 220.31  E-value: 2.20e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243132   15 FVTGTDTDVGKTFVSTLLVHKWK-----AAYWKPVQTGIESDQGDSETLKNFKIAASTWQppiFTPTYALQKPLSPLQAM 89
Cdd:TIGR00347   1 FVTGTDTGVGKTVASSALAAKLKkagysVGYYKPVQTGIEKTNSDALLLQNISGTALDWD---EVNPYAFALPLSPHIAA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243132   90 EYEPN-VDIRLLDFVVPEEWSAENPLVVEGAGGVCVPITrKLEITTDLIKHLietsghPVYVVVVARSGLGTLNHTLLTW 168
Cdd:TIGR00347  78 DQEGRpIDLEELSKHLRTLEQKYDFVLVEGAGGLCVPIT-EEYTTADLIKLL------QLPVILVVRVKLGTINHTLLTV 150
                         170
                  ....*....|....*...
gi 767243132  169 NHLCDNGLRshLFGVILN 186
Cdd:TIGR00347 151 EHARQTGLT--LAGVILN 166
BioD COG0132
Dethiobiotin synthetase [Coenzyme transport and metabolism]; Dethiobiotin synthetase is part ...
14-201 1.09e-53

Dethiobiotin synthetase [Coenzyme transport and metabolism]; Dethiobiotin synthetase is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 439902 [Multi-domain]  Cd Length: 222  Bit Score: 172.26  E-value: 1.09e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243132  14 VFVTGTDTDVGKTFVSTLLVHKW-----KAAYWKPVQTGIESDQG-----DSETLKNfkiAASTWQPPIFTPTYALQKPL 83
Cdd:COG0132    4 LFVTGTDTDVGKTVVTAALAAALraaglRVGYYKPVQTGCEETDGglrngDAELLRR---LSGLPLSYELVNPYRFEEPL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243132  84 SPLQAMEYEpNVDI---RLLDFVvpEEWSAE-NPLVVEGAGGVCVPITRKLEItTDLIKHLietsGHPvyVVVVARSGLG 159
Cdd:COG0132   81 SPHLAARLE-GVPIdldKILAAL--RALAARyDLVLVEGAGGLLVPLTEDLTL-ADLAKAL----GLP--VILVVRARLG 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 767243132 160 TLNHTLLTWNHLCDNGLRshLFGVILNGEPNEG-----NVQALKKFG 201
Cdd:COG0132  151 TINHTLLTVEALRARGLP--LAGIVLNGVPPPDlaerdNLETLERLT 195
DTBS cd03109
dethiobiotin synthetase; Dethiobiotin synthetase (DTBS) is the penultimate enzyme in the ...
12-200 1.29e-52

dethiobiotin synthetase; Dethiobiotin synthetase (DTBS) is the penultimate enzyme in the biotin biosynthesis pathway in Escherichia coli and other microorganisms. The enzyme catalyzes formation of the ureido ring of dethiobiotin from (7R,8S)-7,8-diaminononanoic acid (DAPA) and carbon dioxide. The enzyme utilizes carbon dioxide instead of hydrogen carbonate as substrate and is dependent on ATP and divalent metal ions as cofactors.


Pssm-ID: 349763 [Multi-domain]  Cd Length: 189  Bit Score: 168.52  E-value: 1.29e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243132  12 PIVFVTGTDTDVGKTFVSTLLVHKW-----KAAYWKPVQTG-IESDQGDSETLKNFkiaASTWQPPIFTPTYALQKPLSP 85
Cdd:cd03109    1 KTLFVTGTDTDVGKTVVSAGLARALrkkgiKVGYLKPVQTGcPGLEDSDAELLRKL---AGLLLDLELINPYRFEAPLSP 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243132  86 LQAMEYEpNVDI---RLLDFVvpEEWSAE-NPLVVEGAGGVCVPITRKlEITTDLIKHLietsGHPvyVVVVARSGLGTL 161
Cdd:cd03109   78 HLAAELE-GRDIdleEIVRAL--EELAKSyDVVLVEGAGGLLVPLTEG-YLNADLARAL----GLP--VILVARGGLGTI 147
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 767243132 162 NHTLLTWNHLCDNGLRshLFGVILNGEPNEG-----NVQALKKF 200
Cdd:cd03109  148 NHTLLTLEALKSRGLD--VAGVVLNGIPPEPeaeadNAETLKEL 189
AAA_26 pfam13500
AAA domain; This domain is found in a number of proteins involved in cofactor biosynthesis ...
14-208 2.12e-41

AAA domain; This domain is found in a number of proteins involved in cofactor biosynthesis such as dethiobiotin synthase and cobyric acid synthase. This domain contains a P-loop motif.


Pssm-ID: 433259 [Multi-domain]  Cd Length: 198  Bit Score: 140.09  E-value: 2.12e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243132   14 VFVTGTDTDVGKTFVSTLLVHKW-----KAAYWKPVQTGIESDqGDSETLKNFkiaASTWQPPIFTPTYALQKPLSPLQA 88
Cdd:pfam13500   3 LFVTGTDTGVGKTVVSLGLARALkrrgvKVGYWKPVQTGLVED-GDSELVKRL---LGLDQSYEDPEPFRLSAPLSPHLA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243132   89 MEYEpNVDIRLLDFVVPEEWSAEnPLVVEGAGGVCVPITRKLeITTDLIKHLietsGHPvyVVVVARSGLGTLNHTLLTW 168
Cdd:pfam13500  79 ARQE-GVTIDLEKIIYELPADAD-PVVVEGAGGLLVPINEDL-LNADIAANL----GLP--VILVARGGLGTINHTLLTL 149
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 767243132  169 NHLCDNGLRshLFGVILNGEPNEGNVQALKKF-GVNIMAQV 208
Cdd:pfam13500 150 EALRQRGIP--VLGVILNGVPNPENVRTIFAFgGVPVLGAV 188
PLN02974 PLN02974
adenosylmethionine-8-amino-7-oxononanoate transaminase
12-51 1.14e-05

adenosylmethionine-8-amino-7-oxononanoate transaminase


Pssm-ID: 215526 [Multi-domain]  Cd Length: 817  Bit Score: 45.86  E-value: 1.14e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 767243132  12 PIVFVTGTDTDVGKTFVSTLLV-----HKWKAAYWKPVQTGIESD 51
Cdd:PLN02974  28 PAFAVWGANTAVGKTLVSAGLAaaaasRRSPVLYVKPVQTGFPDD 72
 
Name Accession Description Interval E-value
bioD TIGR00347
dethiobiotin synthase; Dethiobiotin synthase is involved in biotin biosynthesis and catalyses ...
15-186 2.20e-73

dethiobiotin synthase; Dethiobiotin synthase is involved in biotin biosynthesis and catalyses the reaction (CO2 + 7,8-diaminononanoate + ATP = dethiobiotin + phosphate + ADP). The enzyme binds ATP (see motif in first 12 residues of the SEED alignment) and requires magnesium as a co-factor. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]


Pssm-ID: 129447 [Multi-domain]  Cd Length: 166  Bit Score: 220.31  E-value: 2.20e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243132   15 FVTGTDTDVGKTFVSTLLVHKWK-----AAYWKPVQTGIESDQGDSETLKNFKIAASTWQppiFTPTYALQKPLSPLQAM 89
Cdd:TIGR00347   1 FVTGTDTGVGKTVASSALAAKLKkagysVGYYKPVQTGIEKTNSDALLLQNISGTALDWD---EVNPYAFALPLSPHIAA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243132   90 EYEPN-VDIRLLDFVVPEEWSAENPLVVEGAGGVCVPITrKLEITTDLIKHLietsghPVYVVVVARSGLGTLNHTLLTW 168
Cdd:TIGR00347  78 DQEGRpIDLEELSKHLRTLEQKYDFVLVEGAGGLCVPIT-EEYTTADLIKLL------QLPVILVVRVKLGTINHTLLTV 150
                         170
                  ....*....|....*...
gi 767243132  169 NHLCDNGLRshLFGVILN 186
Cdd:TIGR00347 151 EHARQTGLT--LAGVILN 166
BioD COG0132
Dethiobiotin synthetase [Coenzyme transport and metabolism]; Dethiobiotin synthetase is part ...
14-201 1.09e-53

Dethiobiotin synthetase [Coenzyme transport and metabolism]; Dethiobiotin synthetase is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 439902 [Multi-domain]  Cd Length: 222  Bit Score: 172.26  E-value: 1.09e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243132  14 VFVTGTDTDVGKTFVSTLLVHKW-----KAAYWKPVQTGIESDQG-----DSETLKNfkiAASTWQPPIFTPTYALQKPL 83
Cdd:COG0132    4 LFVTGTDTDVGKTVVTAALAAALraaglRVGYYKPVQTGCEETDGglrngDAELLRR---LSGLPLSYELVNPYRFEEPL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243132  84 SPLQAMEYEpNVDI---RLLDFVvpEEWSAE-NPLVVEGAGGVCVPITRKLEItTDLIKHLietsGHPvyVVVVARSGLG 159
Cdd:COG0132   81 SPHLAARLE-GVPIdldKILAAL--RALAARyDLVLVEGAGGLLVPLTEDLTL-ADLAKAL----GLP--VILVVRARLG 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 767243132 160 TLNHTLLTWNHLCDNGLRshLFGVILNGEPNEG-----NVQALKKFG 201
Cdd:COG0132  151 TINHTLLTVEALRARGLP--LAGIVLNGVPPPDlaerdNLETLERLT 195
DTBS cd03109
dethiobiotin synthetase; Dethiobiotin synthetase (DTBS) is the penultimate enzyme in the ...
12-200 1.29e-52

dethiobiotin synthetase; Dethiobiotin synthetase (DTBS) is the penultimate enzyme in the biotin biosynthesis pathway in Escherichia coli and other microorganisms. The enzyme catalyzes formation of the ureido ring of dethiobiotin from (7R,8S)-7,8-diaminononanoic acid (DAPA) and carbon dioxide. The enzyme utilizes carbon dioxide instead of hydrogen carbonate as substrate and is dependent on ATP and divalent metal ions as cofactors.


Pssm-ID: 349763 [Multi-domain]  Cd Length: 189  Bit Score: 168.52  E-value: 1.29e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243132  12 PIVFVTGTDTDVGKTFVSTLLVHKW-----KAAYWKPVQTG-IESDQGDSETLKNFkiaASTWQPPIFTPTYALQKPLSP 85
Cdd:cd03109    1 KTLFVTGTDTDVGKTVVSAGLARALrkkgiKVGYLKPVQTGcPGLEDSDAELLRKL---AGLLLDLELINPYRFEAPLSP 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243132  86 LQAMEYEpNVDI---RLLDFVvpEEWSAE-NPLVVEGAGGVCVPITRKlEITTDLIKHLietsGHPvyVVVVARSGLGTL 161
Cdd:cd03109   78 HLAAELE-GRDIdleEIVRAL--EELAKSyDVVLVEGAGGLLVPLTEG-YLNADLARAL----GLP--VILVARGGLGTI 147
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 767243132 162 NHTLLTWNHLCDNGLRshLFGVILNGEPNEG-----NVQALKKF 200
Cdd:cd03109  148 NHTLLTLEALKSRGLD--VAGVVLNGIPPEPeaeadNAETLKEL 189
AAA_26 pfam13500
AAA domain; This domain is found in a number of proteins involved in cofactor biosynthesis ...
14-208 2.12e-41

AAA domain; This domain is found in a number of proteins involved in cofactor biosynthesis such as dethiobiotin synthase and cobyric acid synthase. This domain contains a P-loop motif.


Pssm-ID: 433259 [Multi-domain]  Cd Length: 198  Bit Score: 140.09  E-value: 2.12e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243132   14 VFVTGTDTDVGKTFVSTLLVHKW-----KAAYWKPVQTGIESDqGDSETLKNFkiaASTWQPPIFTPTYALQKPLSPLQA 88
Cdd:pfam13500   3 LFVTGTDTGVGKTVVSLGLARALkrrgvKVGYWKPVQTGLVED-GDSELVKRL---LGLDQSYEDPEPFRLSAPLSPHLA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767243132   89 MEYEpNVDIRLLDFVVPEEWSAEnPLVVEGAGGVCVPITRKLeITTDLIKHLietsGHPvyVVVVARSGLGTLNHTLLTW 168
Cdd:pfam13500  79 ARQE-GVTIDLEKIIYELPADAD-PVVVEGAGGLLVPINEDL-LNADIAANL----GLP--VILVARGGLGTINHTLLTL 149
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 767243132  169 NHLCDNGLRshLFGVILNGEPNEGNVQALKKF-GVNIMAQV 208
Cdd:pfam13500 150 EALRQRGIP--VLGVILNGVPNPENVRTIFAFgGVPVLGAV 188
PLN02974 PLN02974
adenosylmethionine-8-amino-7-oxononanoate transaminase
12-51 1.14e-05

adenosylmethionine-8-amino-7-oxononanoate transaminase


Pssm-ID: 215526 [Multi-domain]  Cd Length: 817  Bit Score: 45.86  E-value: 1.14e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 767243132  12 PIVFVTGTDTDVGKTFVSTLLV-----HKWKAAYWKPVQTGIESD 51
Cdd:PLN02974  28 PAFAVWGANTAVGKTLVSAGLAaaaasRRSPVLYVKPVQTGFPDD 72
 
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