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Conserved domains on  [gi|24584727|ref|NP_609812|]
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uncharacterized protein Dmel_CG13280, isoform A [Drosophila melanogaster]

Protein Classification

Gfo/Idh/MocA family protein( domain architecture ID 11430574)

Gfo/Idh/MocA family protein belonging to the NAD(P)(+)-binding Rossmann-fold superfamily, may function as an oxidoreductase that catalyzes the transfer of electrons from one molecule, the electron donor or reductant, to another molecule, the electron acceptor or oxidant

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MviM COG0673
Predicted dehydrogenase [General function prediction only];
91-331 1.70e-43

Predicted dehydrogenase [General function prediction only];


:

Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 155.08  E-value: 1.70e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584727  91 TLRWGIAPVSLMADDFAAALSVLPEqhHRIVSCVAAYQSHALAFAERHQVEnVYTSFEDLAKCPNVDVVYISPLNPQHSE 170
Cdd:COG0673   3 KLRVGIIGAGGIGRAHAPALAALPG--VELVAVADRDPERAEAFAEEYGVR-VYTDYEELLADPDIDAVVIATPNHLHAE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584727 171 LCHLMLNHDKHVLCEKPLCMTEEQVTKLLEKARARGLFLMEGMWPRCVPAYHYLRHQILRNRLGEIKQVHCTLGLPVSQG 250
Cdd:COG0673  80 LAIAALEAGKHVLCEKPLALTLEEARELVAAAEEAGVVLMVGFNRRFDPAVRAARELIDSGAIGEIRSVRARFGHPRPAG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584727 251 RLG-------LYGGVTNDFGVYGMQLALWVFREVPRCLKVSGRV---NSEHVDVSADIELCFTRGKRALIEVS---SEKK 317
Cdd:COG0673 160 PADwrfdpelAGGGALLDLGIHDIDLARWLLGSEPESVSATGGRlvpDRVEVDDTAAATLRFANGAVATLEASwvaPGGE 239
                       250
                ....*....|....
gi 24584727 318 LSNQAVIQGKDGSI 331
Cdd:COG0673 240 RDERLEVYGTKGTL 253
 
Name Accession Description Interval E-value
MviM COG0673
Predicted dehydrogenase [General function prediction only];
91-331 1.70e-43

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 155.08  E-value: 1.70e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584727  91 TLRWGIAPVSLMADDFAAALSVLPEqhHRIVSCVAAYQSHALAFAERHQVEnVYTSFEDLAKCPNVDVVYISPLNPQHSE 170
Cdd:COG0673   3 KLRVGIIGAGGIGRAHAPALAALPG--VELVAVADRDPERAEAFAEEYGVR-VYTDYEELLADPDIDAVVIATPNHLHAE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584727 171 LCHLMLNHDKHVLCEKPLCMTEEQVTKLLEKARARGLFLMEGMWPRCVPAYHYLRHQILRNRLGEIKQVHCTLGLPVSQG 250
Cdd:COG0673  80 LAIAALEAGKHVLCEKPLALTLEEARELVAAAEEAGVVLMVGFNRRFDPAVRAARELIDSGAIGEIRSVRARFGHPRPAG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584727 251 RLG-------LYGGVTNDFGVYGMQLALWVFREVPRCLKVSGRV---NSEHVDVSADIELCFTRGKRALIEVS---SEKK 317
Cdd:COG0673 160 PADwrfdpelAGGGALLDLGIHDIDLARWLLGSEPESVSATGGRlvpDRVEVDDTAAATLRFANGAVATLEASwvaPGGE 239
                       250
                ....*....|....
gi 24584727 318 LSNQAVIQGKDGSI 331
Cdd:COG0673 240 RDERLEVYGTKGTL 253
GFO_IDH_MocA pfam01408
Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. ...
92-212 9.66e-18

Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. This family is called the GFO/IDH/MOCA family in swiss-prot.


Pssm-ID: 426248 [Multi-domain]  Cd Length: 120  Bit Score: 78.79  E-value: 9.66e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584727    92 LRWGIAPVSLMADDFAAALsVLPEQHHRIVSCVAAYQSHALAFAERHQVEnVYTSFEDLAKCPNVDVVYISPLNPQHSEL 171
Cdd:pfam01408   1 IRVGIIGAGKIGSKHARAL-NASQPGAELVAILDPNSERAEAVAESFGVE-VYSDLEELLNDPEIDAVIVATPNGLHYDL 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 24584727   172 CHLMLNHDKHVLCEKPLCMTEEQVTKLLEKARARGLFLMEG 212
Cdd:pfam01408  79 AIAALEAGKHVLCEKPLATTVEEAKELVELAKKKGVRVSVG 119
thiaz-red TIGR01761
thiazolinyl imide reductase; This reductase is found associated with gene clusters for the ...
106-283 3.93e-04

thiazolinyl imide reductase; This reductase is found associated with gene clusters for the biosynthesis of various non-ribosomal peptide derived natural products in which cysteine is cyclized to a thiazoline ring containing an imide double bond. Examples include yersiniabactin (irp3/YbtU, GP|21959262) and pyochelin (PchG, GP|4325022).


Pssm-ID: 273791  Cd Length: 344  Bit Score: 42.51  E-value: 3.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584727   106 FAAALSVLPEQHhRIVSCVAAYQSHALAFAERHQVEnVYTSFEDLAKCPNVDVVYI--SPLNPQHSELCHLMLNHDKHVL 183
Cdd:TIGR01761  17 YLAAFMQAPEGL-ELAGLLAQGSERSRALAHALGVP-LYTSPEELPDDIDIACVVVrsTIVGGQGSQLARALLARGIHVL 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584727   184 CEKPLCMTEeqVTKLLEKARARGL-FLMEGMWPRcVPA----YHYLRHQILRNRlgeIKQVHCTLGLPVSQGRLG----L 254
Cdd:TIGR01761  95 QEHPLHPDD--ISSLLRLAQRQGCrYWVNTFYPH-LPAgrrfIRYARQLCLRKT---PPFVEATTSVQLLYSTLDillrL 168
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 24584727   255 YGGV--------TNDFGVYGMQLALWVFREVPRCLKV 283
Cdd:TIGR01761 169 LGGVgpaalecpGGDFSPFPCRRLQGVIAEVPLSLNL 205
PRK11579 PRK11579
putative oxidoreductase; Provisional
143-237 4.90e-04

putative oxidoreductase; Provisional


Pssm-ID: 183212 [Multi-domain]  Cd Length: 346  Bit Score: 42.01  E-value: 4.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584727  143 VYTSFEDLAKCPNVDVVYISPLNPQHSELCHLMLNHDKHVLCEKPLCMTEEQVTKLLEKARARGLFLMEGMWPRCVPAYH 222
Cdd:PRK11579  52 VVSEPQHLFNDPNIDLIVIPTPNDTHFPLAKAALEAGKHVVVDKPFTVTLSQARELDALAKSAGRVLSVFHNRRWDSDFL 131
                         90
                 ....*....|....*
gi 24584727  223 YLRHQILRNRLGEIK 237
Cdd:PRK11579 132 TLKALLAEGVLGEVA 146
XylDh_Gfo6_Halo NF041392
D-xylose 1-dehydrogenase Gfo6;
144-291 1.29e-03

D-xylose 1-dehydrogenase Gfo6;


Pssm-ID: 469283 [Multi-domain]  Cd Length: 350  Bit Score: 41.06  E-value: 1.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584727  144 YTSFEDLAKCPNVDVVYISPLNPQHSELCHLMLNHDKHVLCEKPLCMTEEQVTKLLEKARARGLFLMEGMWPRCVPAYHY 223
Cdd:NF041392  71 YDEFHDGAAADAYDAVYVCTPNALHLEYVETAAELGKAVLCEKPMEATVERAERMVEACEDADVPLMVAYRMHTEPAVRR 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584727  224 LRHQILRNRLGEIKQVHCTLGLPV-------SQGRL-----GlYGGVTNDFGVYGMQLALWVFREVPRclKVSGRVNSEH 291
Cdd:NF041392 151 ARELIRDGFIGDPVQVHGNNSQPLlemipdpDQWRLdpdlsG-YGTSVMDLGIYPLNTARFLLDADPV--AVQASMRSEH 227
 
Name Accession Description Interval E-value
MviM COG0673
Predicted dehydrogenase [General function prediction only];
91-331 1.70e-43

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 155.08  E-value: 1.70e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584727  91 TLRWGIAPVSLMADDFAAALSVLPEqhHRIVSCVAAYQSHALAFAERHQVEnVYTSFEDLAKCPNVDVVYISPLNPQHSE 170
Cdd:COG0673   3 KLRVGIIGAGGIGRAHAPALAALPG--VELVAVADRDPERAEAFAEEYGVR-VYTDYEELLADPDIDAVVIATPNHLHAE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584727 171 LCHLMLNHDKHVLCEKPLCMTEEQVTKLLEKARARGLFLMEGMWPRCVPAYHYLRHQILRNRLGEIKQVHCTLGLPVSQG 250
Cdd:COG0673  80 LAIAALEAGKHVLCEKPLALTLEEARELVAAAEEAGVVLMVGFNRRFDPAVRAARELIDSGAIGEIRSVRARFGHPRPAG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584727 251 RLG-------LYGGVTNDFGVYGMQLALWVFREVPRCLKVSGRV---NSEHVDVSADIELCFTRGKRALIEVS---SEKK 317
Cdd:COG0673 160 PADwrfdpelAGGGALLDLGIHDIDLARWLLGSEPESVSATGGRlvpDRVEVDDTAAATLRFANGAVATLEASwvaPGGE 239
                       250
                ....*....|....
gi 24584727 318 LSNQAVIQGKDGSI 331
Cdd:COG0673 240 RDERLEVYGTKGTL 253
GFO_IDH_MocA pfam01408
Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. ...
92-212 9.66e-18

Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. This family is called the GFO/IDH/MOCA family in swiss-prot.


Pssm-ID: 426248 [Multi-domain]  Cd Length: 120  Bit Score: 78.79  E-value: 9.66e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584727    92 LRWGIAPVSLMADDFAAALsVLPEQHHRIVSCVAAYQSHALAFAERHQVEnVYTSFEDLAKCPNVDVVYISPLNPQHSEL 171
Cdd:pfam01408   1 IRVGIIGAGKIGSKHARAL-NASQPGAELVAILDPNSERAEAVAESFGVE-VYSDLEELLNDPEIDAVIVATPNGLHYDL 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 24584727   172 CHLMLNHDKHVLCEKPLCMTEEQVTKLLEKARARGLFLMEG 212
Cdd:pfam01408  79 AIAALEAGKHVLCEKPLATTVEEAKELVELAKKKGVRVSVG 119
thiaz-red TIGR01761
thiazolinyl imide reductase; This reductase is found associated with gene clusters for the ...
106-283 3.93e-04

thiazolinyl imide reductase; This reductase is found associated with gene clusters for the biosynthesis of various non-ribosomal peptide derived natural products in which cysteine is cyclized to a thiazoline ring containing an imide double bond. Examples include yersiniabactin (irp3/YbtU, GP|21959262) and pyochelin (PchG, GP|4325022).


Pssm-ID: 273791  Cd Length: 344  Bit Score: 42.51  E-value: 3.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584727   106 FAAALSVLPEQHhRIVSCVAAYQSHALAFAERHQVEnVYTSFEDLAKCPNVDVVYI--SPLNPQHSELCHLMLNHDKHVL 183
Cdd:TIGR01761  17 YLAAFMQAPEGL-ELAGLLAQGSERSRALAHALGVP-LYTSPEELPDDIDIACVVVrsTIVGGQGSQLARALLARGIHVL 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584727   184 CEKPLCMTEeqVTKLLEKARARGL-FLMEGMWPRcVPA----YHYLRHQILRNRlgeIKQVHCTLGLPVSQGRLG----L 254
Cdd:TIGR01761  95 QEHPLHPDD--ISSLLRLAQRQGCrYWVNTFYPH-LPAgrrfIRYARQLCLRKT---PPFVEATTSVQLLYSTLDillrL 168
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 24584727   255 YGGV--------TNDFGVYGMQLALWVFREVPRCLKV 283
Cdd:TIGR01761 169 LGGVgpaalecpGGDFSPFPCRRLQGVIAEVPLSLNL 205
PRK11579 PRK11579
putative oxidoreductase; Provisional
143-237 4.90e-04

putative oxidoreductase; Provisional


Pssm-ID: 183212 [Multi-domain]  Cd Length: 346  Bit Score: 42.01  E-value: 4.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584727  143 VYTSFEDLAKCPNVDVVYISPLNPQHSELCHLMLNHDKHVLCEKPLCMTEEQVTKLLEKARARGLFLMEGMWPRCVPAYH 222
Cdd:PRK11579  52 VVSEPQHLFNDPNIDLIVIPTPNDTHFPLAKAALEAGKHVVVDKPFTVTLSQARELDALAKSAGRVLSVFHNRRWDSDFL 131
                         90
                 ....*....|....*
gi 24584727  223 YLRHQILRNRLGEIK 237
Cdd:PRK11579 132 TLKALLAEGVLGEVA 146
XylDh_Gfo6_Halo NF041392
D-xylose 1-dehydrogenase Gfo6;
144-291 1.29e-03

D-xylose 1-dehydrogenase Gfo6;


Pssm-ID: 469283 [Multi-domain]  Cd Length: 350  Bit Score: 41.06  E-value: 1.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584727  144 YTSFEDLAKCPNVDVVYISPLNPQHSELCHLMLNHDKHVLCEKPLCMTEEQVTKLLEKARARGLFLMEGMWPRCVPAYHY 223
Cdd:NF041392  71 YDEFHDGAAADAYDAVYVCTPNALHLEYVETAAELGKAVLCEKPMEATVERAERMVEACEDADVPLMVAYRMHTEPAVRR 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584727  224 LRHQILRNRLGEIKQVHCTLGLPV-------SQGRL-----GlYGGVTNDFGVYGMQLALWVFREVPRclKVSGRVNSEH 291
Cdd:NF041392 151 ARELIRDGFIGDPVQVHGNNSQPLlemipdpDQWRLdpdlsG-YGTSVMDLGIYPLNTARFLLDADPV--AVQASMRSEH 227
 
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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