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Conserved domains on  [gi|2324101857|emb|CAI4036155|]
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hypothetical protein SMKI_14G3740 [Saccharomyces mikatae IFO 1815]

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

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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 ...
13-184 8.49e-69

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: 208.75  E-value: 8.49e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324101857  13 FVTGTDTDVGKTFVSTLLVHKWK-----ASYWKPVQTGIESDQGDSETLKKFEAAASTWQpriFTPTYELQKPLSPLQAM 87
Cdd:TIGR00347   1 FVTGTDTGVGKTVASSALAAKLKkagysVGYYKPVQTGIEKTNSDALLLQNISGTALDWD---EVNPYAFALPLSPHIAA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324101857  88 EYEPE-VDIKLLDFVAPEEWGAEDPLVVEGAGGVCVPITrKLEITTDLIKHLietsshPVYVVVVARSGLGTLNHTLLTW 166
Cdd:TIGR00347  78 DQEGRpIDLEELSKHLRTLEQKYDFVLVEGAGGLCVPIT-EEYTTADLIKLL------QLPVILVVRVKLGTINHTLLTV 150
                         170
                  ....*....|....*...
gi 2324101857 167 NHLCDNGLRghLFGVILN 184
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 ...
13-184 8.49e-69

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: 208.75  E-value: 8.49e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324101857  13 FVTGTDTDVGKTFVSTLLVHKWK-----ASYWKPVQTGIESDQGDSETLKKFEAAASTWQpriFTPTYELQKPLSPLQAM 87
Cdd:TIGR00347   1 FVTGTDTGVGKTVASSALAAKLKkagysVGYYKPVQTGIEKTNSDALLLQNISGTALDWD---EVNPYAFALPLSPHIAA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324101857  88 EYEPE-VDIKLLDFVAPEEWGAEDPLVVEGAGGVCVPITrKLEITTDLIKHLietsshPVYVVVVARSGLGTLNHTLLTW 166
Cdd:TIGR00347  78 DQEGRpIDLEELSKHLRTLEQKYDFVLVEGAGGLCVPIT-EEYTTADLIKLL------QLPVILVVRVKLGTINHTLLTV 150
                         170
                  ....*....|....*...
gi 2324101857 167 NHLCDNGLRghLFGVILN 184
Cdd:TIGR00347 151 EHARQTGLT--LAGVILN 166
DTBS cd03109
dethiobiotin synthetase; Dethiobiotin synthetase (DTBS) is the penultimate enzyme in the ...
10-198 9.95e-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: 166.21  E-value: 9.95e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324101857  10 PIVFVTGTDTDVGKTFVSTLLVHKW-----KASYWKPVQTG-IESDQGDSETLKKFeaaASTWQPRIFTPTYELQKPLSP 83
Cdd:cd03109     1 KTLFVTGTDTDVGKTVVSAGLARALrkkgiKVGYLKPVQTGcPGLEDSDAELLRKL---AGLLLDLELINPYRFEAPLSP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324101857  84 LQAMEYEpEVDIKLLDFVAPEEWGAE--DPLVVEGAGGVCVPITRKlEITTDLIKHLietsSHPvyVVVVARSGLGTLNH 161
Cdd:cd03109    78 HLAAELE-GRDIDLEEIVRALEELAKsyDVVLVEGAGGLLVPLTEG-YLNADLARAL----GLP--VILVARGGLGTINH 149
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2324101857 162 TLLTWNHLCDNGLRghLFGVILNGEPNEG-----NVQALEKF 198
Cdd:cd03109   150 TLLTLEALKSRGLD--VAGVVLNGIPPEPeaeadNAETLKEL 189
BioD COG0132
Dethiobiotin synthetase [Coenzyme transport and metabolism]; Dethiobiotin synthetase is part ...
12-199 2.25e-51

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: 166.10  E-value: 2.25e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324101857  12 VFVTGTDTDVGKTFVSTLLVHKW-----KASYWKPVQTGIESDQG-----DSETLKkfeAAASTWQPRIFTPTYELQKPL 81
Cdd:COG0132     4 LFVTGTDTDVGKTVVTAALAAALraaglRVGYYKPVQTGCEETDGglrngDAELLR---RLSGLPLSYELVNPYRFEEPL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324101857  82 SPLQAMEYEpEVDIKLLDFVAPEEWGAE--DPLVVEGAGGVCVPITRKLEItTDLIKHLietsSHPvyVVVVARSGLGTL 159
Cdd:COG0132    81 SPHLAARLE-GVPIDLDKILAALRALAAryDLVLVEGAGGLLVPLTEDLTL-ADLAKAL----GLP--VILVVRARLGTI 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2324101857 160 NHTLLTWNHLCDNGLRghLFGVILNGEPNEG-----NVQALEKFG 199
Cdd:COG0132   153 NHTLLTVEALRARGLP--LAGIVLNGVPPPDlaerdNLETLERLT 195
AAA_26 pfam13500
AAA domain; This domain is found in a number of proteins involved in cofactor biosynthesis ...
12-206 1.29e-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: 140.47  E-value: 1.29e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324101857  12 VFVTGTDTDVGKTFVSTLLVHKW-----KASYWKPVQTGIESDqGDSETLKKFeaaASTWQPRIFTPTYELQKPLSPLQA 86
Cdd:pfam13500   3 LFVTGTDTGVGKTVVSLGLARALkrrgvKVGYWKPVQTGLVED-GDSELVKRL---LGLDQSYEDPEPFRLSAPLSPHLA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324101857  87 MEYEP-EVDIKLLDFVAPEEwgaEDPLVVEGAGGVCVPITRKLeITTDLIKHL-IEtsshpvyVVVVARSGLGTLNHTLL 164
Cdd:pfam13500  79 ARQEGvTIDLEKIIYELPAD---ADPVVVEGAGGLLVPINEDL-LNADIAANLgLP-------VILVARGGLGTINHTLL 147
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2324101857 165 TWNHLCDNGLRghLFGVILNGEPNEGNVQALEKF-GVNIMAQV 206
Cdd:pfam13500 148 TLEALRQRGIP--VLGVILNGVPNPENVRTIFAFgGVPVLGAV 188
PLN02974 PLN02974
adenosylmethionine-8-amino-7-oxononanoate transaminase
10-71 5.97e-06

adenosylmethionine-8-amino-7-oxononanoate transaminase


Pssm-ID: 215526 [Multi-domain]  Cd Length: 817  Bit Score: 46.63  E-value: 5.97e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2324101857  10 PIVFVTGTDTDVGKTFVSTLLV-----HKWKASYWKPVQTGIESDQgDSETLKKFEAAASTWQPRIF 71
Cdd:PLN02974   28 PAFAVWGANTAVGKTLVSAGLAaaaasRRSPVLYVKPVQTGFPDDS-DARFVFRKADSLSRRSESLF 93
 
Name Accession Description Interval E-value
bioD TIGR00347
dethiobiotin synthase; Dethiobiotin synthase is involved in biotin biosynthesis and catalyses ...
13-184 8.49e-69

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: 208.75  E-value: 8.49e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324101857  13 FVTGTDTDVGKTFVSTLLVHKWK-----ASYWKPVQTGIESDQGDSETLKKFEAAASTWQpriFTPTYELQKPLSPLQAM 87
Cdd:TIGR00347   1 FVTGTDTGVGKTVASSALAAKLKkagysVGYYKPVQTGIEKTNSDALLLQNISGTALDWD---EVNPYAFALPLSPHIAA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324101857  88 EYEPE-VDIKLLDFVAPEEWGAEDPLVVEGAGGVCVPITrKLEITTDLIKHLietsshPVYVVVVARSGLGTLNHTLLTW 166
Cdd:TIGR00347  78 DQEGRpIDLEELSKHLRTLEQKYDFVLVEGAGGLCVPIT-EEYTTADLIKLL------QLPVILVVRVKLGTINHTLLTV 150
                         170
                  ....*....|....*...
gi 2324101857 167 NHLCDNGLRghLFGVILN 184
Cdd:TIGR00347 151 EHARQTGLT--LAGVILN 166
DTBS cd03109
dethiobiotin synthetase; Dethiobiotin synthetase (DTBS) is the penultimate enzyme in the ...
10-198 9.95e-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: 166.21  E-value: 9.95e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324101857  10 PIVFVTGTDTDVGKTFVSTLLVHKW-----KASYWKPVQTG-IESDQGDSETLKKFeaaASTWQPRIFTPTYELQKPLSP 83
Cdd:cd03109     1 KTLFVTGTDTDVGKTVVSAGLARALrkkgiKVGYLKPVQTGcPGLEDSDAELLRKL---AGLLLDLELINPYRFEAPLSP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324101857  84 LQAMEYEpEVDIKLLDFVAPEEWGAE--DPLVVEGAGGVCVPITRKlEITTDLIKHLietsSHPvyVVVVARSGLGTLNH 161
Cdd:cd03109    78 HLAAELE-GRDIDLEEIVRALEELAKsyDVVLVEGAGGLLVPLTEG-YLNADLARAL----GLP--VILVARGGLGTINH 149
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2324101857 162 TLLTWNHLCDNGLRghLFGVILNGEPNEG-----NVQALEKF 198
Cdd:cd03109   150 TLLTLEALKSRGLD--VAGVVLNGIPPEPeaeadNAETLKEL 189
BioD COG0132
Dethiobiotin synthetase [Coenzyme transport and metabolism]; Dethiobiotin synthetase is part ...
12-199 2.25e-51

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: 166.10  E-value: 2.25e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324101857  12 VFVTGTDTDVGKTFVSTLLVHKW-----KASYWKPVQTGIESDQG-----DSETLKkfeAAASTWQPRIFTPTYELQKPL 81
Cdd:COG0132     4 LFVTGTDTDVGKTVVTAALAAALraaglRVGYYKPVQTGCEETDGglrngDAELLR---RLSGLPLSYELVNPYRFEEPL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324101857  82 SPLQAMEYEpEVDIKLLDFVAPEEWGAE--DPLVVEGAGGVCVPITRKLEItTDLIKHLietsSHPvyVVVVARSGLGTL 159
Cdd:COG0132    81 SPHLAARLE-GVPIDLDKILAALRALAAryDLVLVEGAGGLLVPLTEDLTL-ADLAKAL----GLP--VILVVRARLGTI 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2324101857 160 NHTLLTWNHLCDNGLRghLFGVILNGEPNEG-----NVQALEKFG 199
Cdd:COG0132   153 NHTLLTVEALRARGLP--LAGIVLNGVPPPDlaerdNLETLERLT 195
AAA_26 pfam13500
AAA domain; This domain is found in a number of proteins involved in cofactor biosynthesis ...
12-206 1.29e-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: 140.47  E-value: 1.29e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324101857  12 VFVTGTDTDVGKTFVSTLLVHKW-----KASYWKPVQTGIESDqGDSETLKKFeaaASTWQPRIFTPTYELQKPLSPLQA 86
Cdd:pfam13500   3 LFVTGTDTGVGKTVVSLGLARALkrrgvKVGYWKPVQTGLVED-GDSELVKRL---LGLDQSYEDPEPFRLSAPLSPHLA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2324101857  87 MEYEP-EVDIKLLDFVAPEEwgaEDPLVVEGAGGVCVPITRKLeITTDLIKHL-IEtsshpvyVVVVARSGLGTLNHTLL 164
Cdd:pfam13500  79 ARQEGvTIDLEKIIYELPAD---ADPVVVEGAGGLLVPINEDL-LNADIAANLgLP-------VILVARGGLGTINHTLL 147
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2324101857 165 TWNHLCDNGLRghLFGVILNGEPNEGNVQALEKF-GVNIMAQV 206
Cdd:pfam13500 148 TLEALRQRGIP--VLGVILNGVPNPENVRTIFAFgGVPVLGAV 188
PLN02974 PLN02974
adenosylmethionine-8-amino-7-oxononanoate transaminase
10-71 5.97e-06

adenosylmethionine-8-amino-7-oxononanoate transaminase


Pssm-ID: 215526 [Multi-domain]  Cd Length: 817  Bit Score: 46.63  E-value: 5.97e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2324101857  10 PIVFVTGTDTDVGKTFVSTLLV-----HKWKASYWKPVQTGIESDQgDSETLKKFEAAASTWQPRIF 71
Cdd:PLN02974   28 PAFAVWGANTAVGKTLVSAGLAaaaasRRSPVLYVKPVQTGFPDDS-DARFVFRKADSLSRRSESLF 93
 
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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