NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|446767126|ref|WP_000844382|]
View 

MULTISPECIES: FAD-binding oxidoreductase [Bacillus]

Protein Classification

NAD(P)/FAD-dependent oxidoreductase( domain architecture ID 11429741)

FAD/NAD(P)-binding oxidoreductase that catalyzes the transfer of electrons from one molecule, the electron donor or reductant, to another molecule, the electron acceptor or oxidant

CATH:  3.30.9.10
EC:  1.-.-.-
Gene Ontology:  GO:0016491|GO:0050660
SCOP:  3000055

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
1-367 5.87e-87

Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];


:

Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 267.16  E-value: 5.87e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767126   1 MKSYIVVGSGILGASTAYHLAKAGANVTIVDRQQLGQ-ATDAGAGIVCPWLSQRRNKAWYKIVKGGARYYssliQQLEED 79
Cdd:COG0665    2 TADVVVIGGGIAGLSTAYHLARRGLDVTVLERGRPGSgASGRNAGQLRPGLAALADRALVRLAREALDLW----RELAAE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767126  80 GETDTGYNRVGAISLHTDEKKLDQMEERAykrrEDAPEIG-EITRLSAEETKKLFPALSDE--YSSVHISGAARVNGRLL 156
Cdd:COG0665   78 LGIDCDFRRTGVLYLARTEAELAALRAEA----EALRALGlPVELLDAAELREREPGLGSPdyAGGLYDPDDGHVDPAKL 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767126 157 RNALISAAKKHGATFIKGDAI--LVREGNHITGVTVNDETILAEKVIVTAGAWANEILNPLGINFLVTFQKGQIVHLQIE 234
Cdd:COG0665  154 VRALARAARAAGVRIREGTPVtgLEREGGRVTGVRTERGTVRADAVVLAAGAWSARLLPMLGLRLPLRPVRGYVLVTEPL 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767126 235 nTATENMPVVMPPNDqYILTFDNGHVVIGATHEnDTGFDHRVTAGGLHEVFHKALAVAPGLENATMLETRVGFRPFTPGF 314
Cdd:COG0665  234 -PDLPLRPVLDDTGV-YLRPTADGRLLVGGTAE-PAGFDRAPTPERLEALLRRLRRLFPALADAEIVRAWAGLRPMTPDG 310

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446767126 315 LPVIGPLPNFEGILVANGLGASGLTAGPYLGAELAKLALGQPIELDLNDYDVA 367
Cdd:COG0665  311 LPIIGRLPGAPGLYVATGHGGHGVTLAPAAGRLLADLILGGEPPLDLAPFSPD 363
 
Name Accession Description Interval E-value
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
1-367 5.87e-87

Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 267.16  E-value: 5.87e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767126   1 MKSYIVVGSGILGASTAYHLAKAGANVTIVDRQQLGQ-ATDAGAGIVCPWLSQRRNKAWYKIVKGGARYYssliQQLEED 79
Cdd:COG0665    2 TADVVVIGGGIAGLSTAYHLARRGLDVTVLERGRPGSgASGRNAGQLRPGLAALADRALVRLAREALDLW----RELAAE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767126  80 GETDTGYNRVGAISLHTDEKKLDQMEERAykrrEDAPEIG-EITRLSAEETKKLFPALSDE--YSSVHISGAARVNGRLL 156
Cdd:COG0665   78 LGIDCDFRRTGVLYLARTEAELAALRAEA----EALRALGlPVELLDAAELREREPGLGSPdyAGGLYDPDDGHVDPAKL 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767126 157 RNALISAAKKHGATFIKGDAI--LVREGNHITGVTVNDETILAEKVIVTAGAWANEILNPLGINFLVTFQKGQIVHLQIE 234
Cdd:COG0665  154 VRALARAARAAGVRIREGTPVtgLEREGGRVTGVRTERGTVRADAVVLAAGAWSARLLPMLGLRLPLRPVRGYVLVTEPL 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767126 235 nTATENMPVVMPPNDqYILTFDNGHVVIGATHEnDTGFDHRVTAGGLHEVFHKALAVAPGLENATMLETRVGFRPFTPGF 314
Cdd:COG0665  234 -PDLPLRPVLDDTGV-YLRPTADGRLLVGGTAE-PAGFDRAPTPERLEALLRRLRRLFPALADAEIVRAWAGLRPMTPDG 310

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446767126 315 LPVIGPLPNFEGILVANGLGASGLTAGPYLGAELAKLALGQPIELDLNDYDVA 367
Cdd:COG0665  311 LPIIGRLPGAPGLYVATGHGGHGVTLAPAAGRLLADLILGGEPPLDLAPFSPD 363
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
 5-351 7.58e-60

FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: Glycerol-3-phosphate dehydrogenase EC:1.1.99.5, Sarcosine oxidase beta subunit EC:1.5.3.1, D-alanine oxidase EC:1.4.99.1, D-aspartate oxidase EC:1.4.3.1.


Pssm-ID: 426168 [Multi-domain]  Cd Length: 339  Bit Score: 196.46  E-value: 7.58e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767126    5 IVVGSGILGASTAYHLAKAGANVTIVDRQQL--GQATDAGAGIVCPWLSQRRNKAWYKIVKGGARyyssLIQQLEEDGET 82
Cdd:pfam01266   3 VVIGGGIVGLSTAYELARRGLSVTLLERGDDpgSGASGRNAGLIHPGLRYLEPSELARLALEALD----LWEELEEELGI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767126   83 DTGYNRVGAISLHTDEKKLDQMEERAYKRREDAPEigeiTRLSAEETKKLFPALSDEYSSVHISGAARVNGRLLRNALIS 162
Cdd:pfam01266  79 DCGFRRCGVLVLARDEEEEALEKLLAALRRLGVPA----ELLDAEELRELEPLLPGLRGGLFYPDGGHVDPARLLRALAR 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767126  163 AAKKHGATFIKGDAIL-VREGNHITGVtvnDETILAEKVIVTAGAWANEILNPlGINFLVTFQKGQIVHLQIENTATENM 241
Cdd:pfam01266 155 AAEALGVRIIEGTEVTgIEEEGGVWGV---VTTGEADAVVNAAGAWADLLALP-GLRLPVRPVRGQVLVLEPLPEALLIL 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767126  242 PVVMPPNDQ---YILTFDNGHVVIGATHENDTGFDHRVTAGGLHEVFHKALAVAPGLenATMLETRVGFRPfTPGFLPVI 318
Cdd:pfam01266 231 PVPITVDPGrgvYLRPRADGRLLLGGTDEEDGFDDPTPDPEEIEELLEAARRLFPAL--ADIERAWAGLRP-LPDGLPII 307

                         330       340       350
                  ....*....|....*....|....*....|...
gi 446767126  319 GPlPNFEGILVANGLGASGLTAGPYLGAELAKL 351
Cdd:pfam01266 308 GR-PGSPGLYLATGHGGHGLTLAPGIGKLLAEL 339
PRK00711 PRK00711
D-amino acid dehydrogenase;
5-367 1.42e-20

D-amino acid dehydrogenase;


Pssm-ID: 234819 [Multi-domain]  Cd Length: 416  Bit Score: 92.17  E-value: 1.42e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767126   5 IVVGSGILGASTAYHLAKAGANVTIVDRQQlGQATD---AGAGIVCP-----------------WLSQRR---------- 54
Cdd:PRK00711   4 VVLGSGVIGVTSAWYLAQAGHEVTVIDRQP-GPALEtsfANAGQISPgyaapwaapgvplkaikWLFQRHaplairpdgd 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767126  55 --------------NKAWYKIVKggAR-----YYS-SLIQQLEEdgETDTGYN--RVGAISLHTDEKKLDQMEER-AYKR 111
Cdd:PRK00711  83 pfqlrwmwqmlrncTASRYAVNK--SRmvrlaEYSrDCLKALRA--ETGIQYEgrQGGTLQLFRTQQQLDAAAKDiAVLE 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767126 112 REDAP-EIgeitrLSAEETKKLFPALSDeySSVHISGAARVNG------RLLRNALISAAKKHGATFIKGDAI--LVREG 182
Cdd:PRK00711 159 EAGVPyEL-----LDRDELAAVEPALAG--VRHKLVGGLRLPNdetgdcQLFTQRLAAMAEQLGVKFRFNTPVdgLLVEG 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767126 183 NHITGVTVNDETILAEKVIVTAGAWANEILNPLGINFLVTFQKGQIVHLQIENTATEnmPV--VMppnDQyilTFdngHV 260
Cdd:PRK00711 232 GRITGVQTGGGVITADAYVVALGSYSTALLKPLGVDIPVYPLKGYSLTVPITDEDRA--PVstVL---DE---TY---KI 300

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767126 261 VIgathendTGFDHRVTAGGLHEV--FHKAL-------------AVAPGLENATMLETRVGFRPFTPGFLPVIGPLPnFE 325
Cdd:PRK00711 301 AI-------TRFDDRIRVGGMAEIvgFDLRLdparretlemvvrDLFPGGGDLSQATFWTGLRPMTPDGTPIVGATR-YK 372

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|..
gi 446767126 326 GILVANGLGASGLTAGPYLGAELAKLALGQPIELDLNDYDVA 367
Cdd:PRK00711 373 NLWLNTGHGTLGWTMACGSGQLLADLISGRKPAIDADDLSVA 414
MnmC_Cterm TIGR03197
tRNA U-34 5-methylaminomethyl-2-thiouridine biosynthesis protein MnmC, C-terminal domain; In ...
 16-362 3.86e-17

tRNA U-34 5-methylaminomethyl-2-thiouridine biosynthesis protein MnmC, C-terminal domain; In Escherichia coli, the protein previously designated YfcK is now identified as the bifunctional enzyme MnmC. It acts, following the action of the heterotetramer of GidA and MnmE, in the modification of U-34 of certain tRNA to 5-methylaminomethyl-2-thiouridine (mnm5s2U). In other bacterial, the corresponding proteins are usually but always found as a single polypeptide chain, but occasionally as the product of tandem genes. This model represents the C-terminal region of the multifunctional protein. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 274478 [Multi-domain]  Cd Length: 381  Bit Score: 81.93  E-value: 3.86e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767126   16 TAYHLAKAGANVTIVDRQ-QLGQATDAG-AGIVCPWLSQRRNkAWYKIVKGGARYYSSLIQQLEEDGETdTGYNRVGAIS 93
Cdd:TIGR03197   1 TAYSLARRGWQVTLYEQDeAPAQGASGNpQGALYPLLSADDN-PLSRFFLAAFLYARRFYRQLAEAGFP-FDHEWCGVLQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767126   94 LHTDEKKLDQMEERAykRREDAPEigEITR-LSAEETKKLFpALSDEYSSVHISGAARVNGRLLRNALISAAKKHGATFI 172
Cdd:TIGR03197  79 LAYDEKEAERLQKLL--EQLGFPE--ELARwVDAEQASQLA-GIPLPYGGLFFPQGGWLSPPQLCRALLAHAGIRLTLHF 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767126  173 KGDAI-LVREGNHITGVTVNDETILAEKVIVTAGAWANEiLNPLGiNFLVTFQKGQIVHLQiENTATENMPVVMPpNDQY 251
Cdd:TIGR03197 154 NTEITsLERDGEGWQLLDANGEVIAASVVVLANGAQAPQ-LAQTA-HLPLRPVRGQVSHLP-ATEALSALKTVLC-YDGY 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767126  252 ILTFDNGHVVIGATHE---NDTGF---DHRVTAGGLHEVF---HKALAVAPGLENAtmletRVGFRPFTPGFLPVIGPLP 322
Cdd:TIGR03197 230 LTPANNGEHCIGASYDrndDDLALreaDHAENLERLAECLpalAWASEVDISALQG-----RVGVRCASPDHLPLVGAVP 304

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446767126  323 NFE-------------------------GILVANGLGASGLTAGPyLGAE-LAKLALGQPIELDLN 362
Cdd:TIGR03197 305 DFEaikeayaelakdknrpiaepapyypGLYVLGGLGSRGLTSAP-LAAEiLAAQICGEPLPLERD 369
 
Name Accession Description Interval E-value
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
1-367 5.87e-87

Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 267.16  E-value: 5.87e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767126   1 MKSYIVVGSGILGASTAYHLAKAGANVTIVDRQQLGQ-ATDAGAGIVCPWLSQRRNKAWYKIVKGGARYYssliQQLEED 79
Cdd:COG0665    2 TADVVVIGGGIAGLSTAYHLARRGLDVTVLERGRPGSgASGRNAGQLRPGLAALADRALVRLAREALDLW----RELAAE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767126  80 GETDTGYNRVGAISLHTDEKKLDQMEERAykrrEDAPEIG-EITRLSAEETKKLFPALSDE--YSSVHISGAARVNGRLL 156
Cdd:COG0665   78 LGIDCDFRRTGVLYLARTEAELAALRAEA----EALRALGlPVELLDAAELREREPGLGSPdyAGGLYDPDDGHVDPAKL 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767126 157 RNALISAAKKHGATFIKGDAI--LVREGNHITGVTVNDETILAEKVIVTAGAWANEILNPLGINFLVTFQKGQIVHLQIE 234
Cdd:COG0665  154 VRALARAARAAGVRIREGTPVtgLEREGGRVTGVRTERGTVRADAVVLAAGAWSARLLPMLGLRLPLRPVRGYVLVTEPL 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767126 235 nTATENMPVVMPPNDqYILTFDNGHVVIGATHEnDTGFDHRVTAGGLHEVFHKALAVAPGLENATMLETRVGFRPFTPGF 314
Cdd:COG0665  234 -PDLPLRPVLDDTGV-YLRPTADGRLLVGGTAE-PAGFDRAPTPERLEALLRRLRRLFPALADAEIVRAWAGLRPMTPDG 310

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446767126 315 LPVIGPLPNFEGILVANGLGASGLTAGPYLGAELAKLALGQPIELDLNDYDVA 367
Cdd:COG0665  311 LPIIGRLPGAPGLYVATGHGGHGVTLAPAAGRLLADLILGGEPPLDLAPFSPD 363
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
 5-351 7.58e-60

FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: Glycerol-3-phosphate dehydrogenase EC:1.1.99.5, Sarcosine oxidase beta subunit EC:1.5.3.1, D-alanine oxidase EC:1.4.99.1, D-aspartate oxidase EC:1.4.3.1.


Pssm-ID: 426168 [Multi-domain]  Cd Length: 339  Bit Score: 196.46  E-value: 7.58e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767126    5 IVVGSGILGASTAYHLAKAGANVTIVDRQQL--GQATDAGAGIVCPWLSQRRNKAWYKIVKGGARyyssLIQQLEEDGET 82
Cdd:pfam01266   3 VVIGGGIVGLSTAYELARRGLSVTLLERGDDpgSGASGRNAGLIHPGLRYLEPSELARLALEALD----LWEELEEELGI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767126   83 DTGYNRVGAISLHTDEKKLDQMEERAYKRREDAPEigeiTRLSAEETKKLFPALSDEYSSVHISGAARVNGRLLRNALIS 162
Cdd:pfam01266  79 DCGFRRCGVLVLARDEEEEALEKLLAALRRLGVPA----ELLDAEELRELEPLLPGLRGGLFYPDGGHVDPARLLRALAR 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767126  163 AAKKHGATFIKGDAIL-VREGNHITGVtvnDETILAEKVIVTAGAWANEILNPlGINFLVTFQKGQIVHLQIENTATENM 241
Cdd:pfam01266 155 AAEALGVRIIEGTEVTgIEEEGGVWGV---VTTGEADAVVNAAGAWADLLALP-GLRLPVRPVRGQVLVLEPLPEALLIL 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767126  242 PVVMPPNDQ---YILTFDNGHVVIGATHENDTGFDHRVTAGGLHEVFHKALAVAPGLenATMLETRVGFRPfTPGFLPVI 318
Cdd:pfam01266 231 PVPITVDPGrgvYLRPRADGRLLLGGTDEEDGFDDPTPDPEEIEELLEAARRLFPAL--ADIERAWAGLRP-LPDGLPII 307

                         330       340       350
                  ....*....|....*....|....*....|...
gi 446767126  319 GPlPNFEGILVANGLGASGLTAGPYLGAELAKL 351
Cdd:pfam01266 308 GR-PGSPGLYLATGHGGHGLTLAPGIGKLLAEL 339
PRK00711 PRK00711
D-amino acid dehydrogenase;
5-367 1.42e-20

D-amino acid dehydrogenase;


Pssm-ID: 234819 [Multi-domain]  Cd Length: 416  Bit Score: 92.17  E-value: 1.42e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767126   5 IVVGSGILGASTAYHLAKAGANVTIVDRQQlGQATD---AGAGIVCP-----------------WLSQRR---------- 54
Cdd:PRK00711   4 VVLGSGVIGVTSAWYLAQAGHEVTVIDRQP-GPALEtsfANAGQISPgyaapwaapgvplkaikWLFQRHaplairpdgd 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767126  55 --------------NKAWYKIVKggAR-----YYS-SLIQQLEEdgETDTGYN--RVGAISLHTDEKKLDQMEER-AYKR 111
Cdd:PRK00711  83 pfqlrwmwqmlrncTASRYAVNK--SRmvrlaEYSrDCLKALRA--ETGIQYEgrQGGTLQLFRTQQQLDAAAKDiAVLE 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767126 112 REDAP-EIgeitrLSAEETKKLFPALSDeySSVHISGAARVNG------RLLRNALISAAKKHGATFIKGDAI--LVREG 182
Cdd:PRK00711 159 EAGVPyEL-----LDRDELAAVEPALAG--VRHKLVGGLRLPNdetgdcQLFTQRLAAMAEQLGVKFRFNTPVdgLLVEG 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767126 183 NHITGVTVNDETILAEKVIVTAGAWANEILNPLGINFLVTFQKGQIVHLQIENTATEnmPV--VMppnDQyilTFdngHV 260
Cdd:PRK00711 232 GRITGVQTGGGVITADAYVVALGSYSTALLKPLGVDIPVYPLKGYSLTVPITDEDRA--PVstVL---DE---TY---KI 300

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767126 261 VIgathendTGFDHRVTAGGLHEV--FHKAL-------------AVAPGLENATMLETRVGFRPFTPGFLPVIGPLPnFE 325
Cdd:PRK00711 301 AI-------TRFDDRIRVGGMAEIvgFDLRLdparretlemvvrDLFPGGGDLSQATFWTGLRPMTPDGTPIVGATR-YK 372

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|..
gi 446767126 326 GILVANGLGASGLTAGPYLGAELAKLALGQPIELDLNDYDVA 367
Cdd:PRK00711 373 NLWLNTGHGTLGWTMACGSGQLLADLISGRKPAIDADDLSVA 414
MnmC_Cterm TIGR03197
tRNA U-34 5-methylaminomethyl-2-thiouridine biosynthesis protein MnmC, C-terminal domain; In ...
 16-362 3.86e-17

tRNA U-34 5-methylaminomethyl-2-thiouridine biosynthesis protein MnmC, C-terminal domain; In Escherichia coli, the protein previously designated YfcK is now identified as the bifunctional enzyme MnmC. It acts, following the action of the heterotetramer of GidA and MnmE, in the modification of U-34 of certain tRNA to 5-methylaminomethyl-2-thiouridine (mnm5s2U). In other bacterial, the corresponding proteins are usually but always found as a single polypeptide chain, but occasionally as the product of tandem genes. This model represents the C-terminal region of the multifunctional protein. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 274478 [Multi-domain]  Cd Length: 381  Bit Score: 81.93  E-value: 3.86e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767126   16 TAYHLAKAGANVTIVDRQ-QLGQATDAG-AGIVCPWLSQRRNkAWYKIVKGGARYYSSLIQQLEEDGETdTGYNRVGAIS 93
Cdd:TIGR03197   1 TAYSLARRGWQVTLYEQDeAPAQGASGNpQGALYPLLSADDN-PLSRFFLAAFLYARRFYRQLAEAGFP-FDHEWCGVLQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767126   94 LHTDEKKLDQMEERAykRREDAPEigEITR-LSAEETKKLFpALSDEYSSVHISGAARVNGRLLRNALISAAKKHGATFI 172
Cdd:TIGR03197  79 LAYDEKEAERLQKLL--EQLGFPE--ELARwVDAEQASQLA-GIPLPYGGLFFPQGGWLSPPQLCRALLAHAGIRLTLHF 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767126  173 KGDAI-LVREGNHITGVTVNDETILAEKVIVTAGAWANEiLNPLGiNFLVTFQKGQIVHLQiENTATENMPVVMPpNDQY 251
Cdd:TIGR03197 154 NTEITsLERDGEGWQLLDANGEVIAASVVVLANGAQAPQ-LAQTA-HLPLRPVRGQVSHLP-ATEALSALKTVLC-YDGY 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767126  252 ILTFDNGHVVIGATHE---NDTGF---DHRVTAGGLHEVF---HKALAVAPGLENAtmletRVGFRPFTPGFLPVIGPLP 322
Cdd:TIGR03197 230 LTPANNGEHCIGASYDrndDDLALreaDHAENLERLAECLpalAWASEVDISALQG-----RVGVRCASPDHLPLVGAVP 304

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446767126  323 NFE-------------------------GILVANGLGASGLTAGPyLGAE-LAKLALGQPIELDLN 362
Cdd:TIGR03197 305 DFEaikeayaelakdknrpiaepapyypGLYVLGGLGSRGLTSAP-LAAEiLAAQICGEPLPLERD 369
mnmC PRK01747
bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent ...
 5-360 1.60e-16

bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent 5-carboxymethylaminomethyl-2-thiouridine(34) oxidoreductase MnmC;


Pssm-ID: 234978 [Multi-domain]  Cd Length: 662  Bit Score: 81.05  E-value: 1.60e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767126   5 IVVGSGILGASTAYHLAKAGANVTIVDRQQlGQATDAG---AGIVCPWLSQRRNKAwYKIVKGGARYYSSLIQQLEEDGE 81
Cdd:PRK01747 264 AIIGGGIAGAALALALARRGWQVTLYEADE-APAQGASgnrQGALYPLLSKDDNAL-SRFFRAAFLFARRFYDALPAAGV 341

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767126  82 TdTGYNRVGAISLHTDEK---KLDQMEERaykrrEDAPEIgeITRLSAEETKKLFpALSDEYSSVHISGAARVNGRLLRN 158
Cdd:PRK01747 342 A-FDHDWCGVLQLAWDEKsaeKIAKMLAL-----GLPAEL--ARALDAEEAEELA-GLPVPCGGIFYPQGGWLCPAELCR 412

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767126 159 ALISAAKKhGATFIKGDAI--LVREGNHITgVTVNDETILAEKVIVTAGAwaNEILNPLGINFLVTFQ-KGQIVHLQien 235
Cdd:PRK01747 413 ALLALAGQ-QLTIHFGHEVarLEREDDGWQ-LDFAGGTLASAPVVVLANG--HDAARFAQTAHLPLYSvRGQVSHLP--- 485

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767126 236 tATENMPVVMPP--NDQYIL-TFDNGHVVIGATHE---NDTGF---DHRVTAGGLHEVFHKALAVApgLENATMLETRVG 306
Cdd:PRK01747 486 -TTPALSALKQVlcYDGYLTpQPANGTHCIGASYDrddTDTAFreaDHQENLERLAECLPQALWAK--EVDVSALQGRVG 562

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446767126 307 FRPFTPGFLPVIGPLPNFE----------------------GILVANGLGASGLTAGPyLGAE-LAKLALGQPIELD 360
Cdd:PRK01747 563 FRCASRDRLPMVGNVPDEAatlaeyaalanqqpardaprlpGLYVAGALGSRGLCSAP-LGAElLASQIEGEPLPLE 638
solA PRK11259
N-methyl-L-tryptophan oxidase;
5-361 1.62e-16

N-methyl-L-tryptophan oxidase;


Pssm-ID: 236887 [Multi-domain]  Cd Length: 376  Bit Score: 79.88  E-value: 1.62e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767126   5 IVVGSGILGASTAYHLAKAGANVTIVDRQQLGQATDAGAG---IVcpwlsqRRnkAWYKivkgGARYYSSLI--QQLEED 79
Cdd:PRK11259   7 IVIGLGSMGSAAGYYLARRGLRVLGLDRFMPPHQQGSSHGdtrII------RH--AYGE----GPAYVPLVLraQELWRE 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767126  80 GETDTG---YNRVGAISLHTDEKKLDQMEERAYKRREDAPEIgeitrLSAEETKKLFP--ALSDEYSSVHISGAARVNGR 154
Cdd:PRK11259  75 LERESGeplFVRTGVLNLGPADSDFLANSIRSARQHGLPHEV-----LDAAEIRRRFPqfRLPDGYIALFEPDGGFLRPE 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767126 155 LLRNALISAAKKHGATFIKGDAILV--REGNHITgVTVNDETILAEKVIVTAGAWANEILNPLGINFLVTFQKGQIVHLQ 232
Cdd:PRK11259 150 LAIKAHLRLAREAGAELLFNEPVTAieADGDGVT-VTTADGTYEAKKLVVSAGAWVKDLLPPLELPLTPVRQVLAWFQAD 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767126 233 IENTATENMPVvmppndqYILTFDNGHVVIGATHENDTGFdhRVtagGLHEVFHKALAVAPGLENATMLETRVGFRPFTP 312
Cdd:PRK11259 229 GRYSEPNRFPA-------FIWEVPDGDQYYGFPAENGPGL--KI---GKHNGGQEITSPDERDRFVTVAEDGAELRPFLR 296

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767126 313 GFLPVIGP---------------------LPNFEGILVANGLGASGLTAGPYLGAELAKLALGQPIELDL 361
Cdd:PRK11259 297 NYLPGVGPclrgaactytntpdehfiidtLPGHPNVLVASGCSGHGFKFASVLGEILADLAQDGTSDFDL 366
soxA_mon TIGR01377
sarcosine oxidase, monomeric form; Sarcosine oxidase catalyzes the oxidative demethylation of ...
 5-361 5.78e-12

sarcosine oxidase, monomeric form; Sarcosine oxidase catalyzes the oxidative demethylation of sarcosine to glycine. The reaction converts tetrahydrofolate to 5,10-methylene-tetrahydrofolate. The enzyme is known in monomeric and heterotetrameric (alpha,beta,gamma,delta) forms [Energy metabolism, Amino acids and amines]


Pssm-ID: 130444 [Multi-domain]  Cd Length: 380  Bit Score: 66.39  E-value: 5.78e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767126    5 IVVGSGILGASTAYHLAKAGANVTIVDRQQLGQATDAGAGivcpwlSQRRNKAWYkivkgGARYYSSLI---QQLEEDGE 81
Cdd:TIGR01377   4 IVVGAGIMGCFAAYHLAKHGKKTLLLEQFDLPHSRGSSHG------QSRIIRKAY-----PEDFYTPMMlecYQLWAQLE 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767126   82 TDTGYNrvgaisLHTDEKKLD--QMEERAYKRREDAPEIGEITR--LSAEETKKLFP---------ALSDEYSSVHISGA 148
Cdd:TIGR01377  73 KEAGTK------LHRQTGLLLlgPKENQFLKTIQATLSRHGLEHelLSSKQLKQRFPnirvprnevGLLDPNGGVLYAEK 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767126  149 ArvngrlLRnALISAAKKHGATFIKGDAI--LVREGNHITgVTVNDETILAEKVIVTAGAWANEILNPLGINFLVTFQKG 226
Cdd:TIGR01377 147 A------LR-ALQELAEAHGATVRDGTKVveIEPTELLVT-VKTTKGSYQANKLVVTAGAWTSKLLSPLGIEIPLQPLRI 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767126  227 QIVHLQIENTATEN--------MPVVMPPNDQYILTFDNGHVVIGATH--------ENDTGFDHRVtaGGLHEVFHKALA 290
Cdd:TIGR01377 219 NVCYWREKEPGSYGvsqafpcfLVLGLNPHIYGLPSFEYPGLMKVYYHhgqqidpdERDCPFGADI--EDVQILRKFVRD 296

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446767126  291 VAPGLeNATMLETRVGFRPFTPGFLPVIGPLPNFEGILVANGLGASGLTAGPYLGAELAKLALGQPIELDL 361
Cdd:TIGR01377 297 HLPGL-NGEPKKGEVCMYTNTPDEHFVIDLHPKYDNVVIGAGFSGHGFKLAPVVGKILAELAMKLKPSYDL 366
PRK10015 PRK10015
oxidoreductase; Provisional
 5-205 2.68e-06

oxidoreductase; Provisional


Pssm-ID: 182194 [Multi-domain]  Cd Length: 429  Bit Score: 48.82  E-value: 2.68e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767126   5 IVVGSGILGASTAYHLAKAGANVTIVDRQqlgqatdagagivcpwlsqrrNKAWYKIVKGGaRYYSsliqqleedgetdt 84
Cdd:PRK10015   9 IVVGAGVAGSVAALVMARAGLDVLVIERG---------------------DSAGCKNMTGG-RLYA-------------- 52

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767126  85 gynrvgaislHTDEKKLDQMEERAYKRREDAPEigEITRLSAEEtkklfpALSDEYSSVHISGAARVNGRLLRNA----L 160
Cdd:PRK10015  53 ----------HTLEAIIPGFAASAPVERKVTRE--KISFLTEES------AVTLDFHREQPDVPQHASYTVLRNRldpwL 114

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 446767126 161 ISAAKKHGATFIKG---DAiLVREGNHITGVTVNDETILAEKVIVTAG 205
Cdd:PRK10015 115 MEQAEQAGAQFIPGvrvDA-LVREGNKVTGVQAGDDILEANVVILADG 161
PRK12409 PRK12409
D-amino acid dehydrogenase small subunit; Provisional
 1-33 9.93e-06

D-amino acid dehydrogenase small subunit; Provisional


Pssm-ID: 237093 [Multi-domain]  Cd Length: 410  Bit Score: 47.33  E-value: 9.93e-06
                         10        20        30
                 ....*....|....*....|....*....|...
gi 446767126   1 MKSYIVVGSGILGASTAYHLAKAGANVTIVDRQ 33
Cdd:PRK12409   1 MSHIAVIGAGITGVTTAYALAQRGYQVTVFDRH 33
COG1233 COG1233
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ...
 1-208 5.27e-05

Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440846 [Multi-domain]  Cd Length: 491  Bit Score: 44.84  E-value: 5.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767126   1 MKSYIVVGSGILGASTAYHLAKAGANVTIVDRQ-QLGQAT----------DAGAGIVCP---------------WLSQRR 54
Cdd:COG1233    3 MYDVVVIGAGIGGLAAAALLARAGYRVTVLEKNdTPGGRArtferpgfrfDVGPSVLTMpgvlerlfrelgledYLELVP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767126  55 NKAWYKIVKGG---ARYYSSL---IQQLE----EDGEtdtGYNRVGAISLHTDEKKLDQMEE------RAYKRREDAPEI 118
Cdd:COG1233   83 LDPAYRVPFPDgraLDLPRDLertAAELErlfpGDAE---AYRRFLAELRRLYDALLEDLLYrpllslRDLLRPLALARL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767126 119 GEITRLSA----------EETKKLFPALSDEYSS---------------VHISGAARVNG--RLLRNALISAAKKHGATF 171
Cdd:COG1233  160 LRLLLRSLrdllrryfkdPRLRALLAGQALYLGLspdrtpalyaliaylEYAGGVWYPKGgmGALADALARLAEELGGEI 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 446767126 172 IKG---DAILVrEGNHITGVTVND-ETILAEKVIVTAGAWA 208
Cdd:COG1233  240 RTGaevERILV-EGGRATGVRLADgEEIRADAVVSNADPAH 279
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
6-33 8.51e-05

NAD(P)-binding Rossmann-like domain;


Pssm-ID: 433218 [Multi-domain]  Cd Length: 67  Bit Score: 40.21  E-value: 8.51e-05
                          10        20
                  ....*....|....*....|....*...
gi 446767126    6 VVGSGILGASTAYHLAKAGANVTIVDRQ 33
Cdd:pfam13450   1 IVGAGLAGLVAAALLAKRGFRVLVLEKR 28
HemY COG1232
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ...
 1-36 1.29e-04

Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen oxidase HemY/PPOX is part of the Pathway/BioSystem: Heme biosynthesis


Pssm-ID: 440845 [Multi-domain]  Cd Length: 443  Bit Score: 43.67  E-value: 1.29e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 446767126   1 MKSYIVVGSGILGASTAYHLAKAGANVTIVDRQ-QLG 36
Cdd:COG1232    1 MKRVAVIGGGIAGLTAAYRLAKAGHEVTVLEASdRVG 37
PRK07233 PRK07233
hypothetical protein; Provisional
 6-204 3.92e-04

hypothetical protein; Provisional


Pssm-ID: 235977 [Multi-domain]  Cd Length: 434  Bit Score: 42.18  E-value: 3.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767126   6 VVGSGILGASTAYHLAKAGANVTIVDR-QQLGqatdaGagivcpwLSQRRNKAWYKIvkggARYY-------SSLIQQLE 77
Cdd:PRK07233   4 IVGGGIAGLAAAYRLAKRGHEVTVFEAdDQLG-----G-------LAASFEFGGLPI----ERFYhhifksdEALLELLD 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767126  78 EDG--------ETDTGYN--------------------------RVGAISLH----TDEKKLDQMEERAYkrredapeig 119
Cdd:PRK07233  68 ELGledklrwrETKTGYYvdgklyplgtplellrfphlslidkfRLGLLTLLarriKDWRALDKVPAEEW---------- 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767126 120 eITRLSAEET-----KKLFPALSDEY----------SSVHISGAARVN-------------GRLLrNALISAAKKHGATF 171
Cdd:PRK07233 138 -LRRWSGEGVyevfwEPLLESKFGDYaddvsaawlwSRIKRRGNRRYSlfgeklgyleggfATLI-DALAEAIEARGGEI 215

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 446767126 172 IKGDAI--LVREGNHITGVTVNDETILAEKVIVTA 204
Cdd:PRK07233 216 RLGTPVtsVVIDGGGVTGVEVDGEEEDFDAVISTA 250
GG-red-SF TIGR02032
geranylgeranyl reductase family; This model represents a subfamily which includes ...
 5-36 8.57e-04

geranylgeranyl reductase family; This model represents a subfamily which includes geranylgeranyl reductases involved in chlorophyll and bacteriochlorophyll biosynthesis as well as other related enzymes which may also act on geranylgeranyl groups or related substrates. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]


Pssm-ID: 273936 [Multi-domain]  Cd Length: 295  Bit Score: 40.77  E-value: 8.57e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 446767126    5 IVVGSGILGASTAYHLAKAGANVTIVDRQQLG 36
Cdd:TIGR02032   4 VVVGAGPAGASAAYRLADKGLRVLLLEKKSFP 35
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
 8-34 1.57e-03

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 39.88  E-value: 1.57e-03
                         10        20
                 ....*....|....*....|....*..
gi 446767126   8 GSGILGASTAYHLAKAGANVTIVDRQQ 34
Cdd:PRK08277  18 GGGVLGGAMAKELARAGAKVAILDRNQ 44
FadB COG1250
3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]; 3-hydroxyacyl-CoA ...
 6-34 2.20e-03

3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]; 3-hydroxyacyl-CoA dehydrogenase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440862 [Multi-domain]  Cd Length: 281  Bit Score: 39.32  E-value: 2.20e-03
                         10        20
                 ....*....|....*....|....*....
gi 446767126   6 VVGSGILGASTAYHLAKAGANVTIVDRQQ 34
Cdd:COG1250    7 VIGAGTMGAGIAAVFANAGYEVVLLDISP 35
FAD_binding_2 pfam00890
FAD binding domain; This family includes members that bind FAD. This family includes the ...
 5-226 2.98e-03

FAD binding domain; This family includes members that bind FAD. This family includes the flavoprotein subunits from succinate and fumarate dehydrogenase, aspartate oxidase and the alpha subunit of adenylylsulphate reductase.


Pssm-ID: 395718 [Multi-domain]  Cd Length: 398  Bit Score: 39.19  E-value: 2.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767126    5 IVVGSGILGASTAYHLAKAGANVTIVDR-QQLGQATD-AGAGIvcpWLSQRRNKAwykivkGG-----ARYYssLIQQLE 77
Cdd:pfam00890   3 LVIGGGLAGLAAALAAAEAGLKVAVVEKgQPFGGATAwSSGGI---DALGNPPQG------GIdspelHPTD--TLKGLD 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767126   78 EDGETDtgynrVGAISLHTDEKKLDQMEERA--YKRREDAPeIGeITRLSAEETKKLFPAlsdeysSVHISGAARVNGRL 155
Cdd:pfam00890  72 ELADHP-----YVEAFVEAAPEAVDWLEALGvpFSRTEDGH-LD-LRPLGGLSATWRTPH------DAADRRRGLGTGHA 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446767126  156 LRNALISAAKKHGATFIKGDAI--LVREGNHITGVTV------NDETILAEK-VIVTAGAWAN--EILNPLGINFLVTFQ 224
Cdd:pfam00890 139 LLARLLEGLRKAGVDFQPRTAAddLIVEDGRVTGAVVenrrngREVRIRAIAaVLLATGGFGRlaELLLPAAGYADTTNP 218


                  ..
gi 446767126  225 KG 226
Cdd:pfam00890 219 PA 220
COG3573 COG3573
Predicted oxidoreductase [General function prediction only];
5-38 5.26e-03

Predicted oxidoreductase [General function prediction only];


Pssm-ID: 442794 [Multi-domain]  Cd Length: 551  Bit Score: 38.62  E-value: 5.26e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 446767126   5 IVVGSGILGASTAYHLAKAGANVTIVDR---QQLG-QA 38
Cdd:COG3573    9 IVVGAGLAGLVAAAELADAGRRVLLLDQepeANLGgQA 46
PRK06847 PRK06847
hypothetical protein; Provisional
 1-45 6.81e-03

hypothetical protein; Provisional


Pssm-ID: 235874 [Multi-domain]  Cd Length: 375  Bit Score: 38.32  E-value: 6.81e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 446767126   1 MKSYIVVGSGILGASTAYHLAKAGANVTIVDRQQLGQATdaGAGI 45
Cdd:PRK06847   4 VKKVLIVGGGIGGLSAAIALRRAGIAVDLVEIDPEWRVY--GAGI 46
NadB COG0029
Aspartate oxidase [Coenzyme transport and metabolism]; Aspartate oxidase is part of the ...
 4-38 9.09e-03

Aspartate oxidase [Coenzyme transport and metabolism]; Aspartate oxidase is part of the Pathway/BioSystem: NAD biosynthesis


Pssm-ID: 439800 [Multi-domain]  Cd Length: 521  Bit Score: 37.78  E-value: 9.09e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 446767126   4 YIVVGSGILGASTAYHLAKAGaNVTIVDRQQLGQA 38
Cdd:COG0029    7 VLVIGSGIAGLSAALKLAERG-RVTLLTKGELGES 40
 
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