NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1835622582|ref|XP_033782322|]
View 

formylglycine-generating enzyme isoform X4 [Geotrypetes seraphini]

Protein Classification

formylglycine-generating enzyme family protein( domain architecture ID 10510263)

formylglycine-generating enzyme family protein similar to human sulfatase-modifying factor 1 (SUMF1), which oxidizes a cysteine residue in the substrate sulfatase, to an active site 3-oxoalanine residue, also called C(alpha)-formylglycine

CATH:  3.90.1580.10
Gene Ontology:  GO:0046872
PubMed:  30824597|27862795|18625336
SCOP:  4000450

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
FGE-sulfatase pfam03781
Sulfatase-modifying factor enzyme 1; This domain is found in eukaryotic proteins required for ...
 66-298 2.12e-67

Sulfatase-modifying factor enzyme 1; This domain is found in eukaryotic proteins required for post-translational sulfatase modification (SUMF1). These proteins are associated with the rare disorder multiple sulfatase deficiency (MSD). The protein product of the SUMF1 gene is FGE, formylglycine (FGly),-generating enzyme, which is a sulfatase. Sulfatases are enzymes essential for degradation and remodelling of sulfate esters, and formylglycine (FGly), the key catalytic in the active site, is unique to sulfatases. FGE is localized to the endoplasmic reticulum (ER) and interacts with and modifies the unfolded form of newly synthesized sulfatases. FGE is a single-domain monomer with a surprising paucity of secondary structure that adopts a unique fold which is stabilized by two Ca2+ ions. The effect of all mutations found in MSD patients is explained by the FGE structure, providing a molecular basis for MSD. A redox-active disulfide bond is present in the active site of FGE. An oxidized cysteine residue, possibly cysteine sulfenic acid, has been detected that may allow formulation of a structure-based mechanism for FGly formation from cysteine residues in all sulfatases. In Mycobacteria and Treponema denticola this enzyme functions as an iron(II)-dependent oxidoreductase.


:

Pssm-ID: 397722 [Multi-domain]  Cd Length: 259  Bit Score: 210.82  E-value: 2.12e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835622582  66 QMAFISTGVFTMGTDEPaIPQDGEAPSRRVHIRHFYMDRYEVSNTEFEKFVTSTGYITEAerfgdsfvfegllsetvkrd 145
Cdd:pfam03781   4 DMVLIPGGSFEMGSAER-TGNDNEAPAHDVTVRPFAIDKYPVTNAQYAAFVEATGYTTEV-------------------- 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835622582 146 ihqavaAAPWWLPVKGANWKHPEGPGSEIHERMDHPVLHVSWRDAVEFCAWAGK------RLPTEAEWEYACRGGRENRL 219
Cdd:pfam03781  63 ------YPQWWAEVEGANWRHPSGGLSDIDDGADHPVTGVSWYDAVAYARWLGKrtgngyRLPTEAEWEYAARGGSKGRR 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835622582 220 FPWGNNLHPNGkhyaNIWQGT-FPSNDSGEDGYTG-TAPVTSFPPNGYGMYNMVGNVWEWTEDWWTVHHSAEETHNPTLF 297
Cdd:pfam03781 137 YPWGDELYPAG----NIWQGAdFPNEHAGADSFNGrTSPVGSFPPNALGLYDMAGNVWEWTSDWYKPHYSFAPYDELSRD 212


                  .
gi 1835622582 298 A 298
Cdd:pfam03781 213 N 213
 
Name Accession Description Interval E-value
FGE-sulfatase pfam03781
Sulfatase-modifying factor enzyme 1; This domain is found in eukaryotic proteins required for ...
 66-298 2.12e-67

Sulfatase-modifying factor enzyme 1; This domain is found in eukaryotic proteins required for post-translational sulfatase modification (SUMF1). These proteins are associated with the rare disorder multiple sulfatase deficiency (MSD). The protein product of the SUMF1 gene is FGE, formylglycine (FGly),-generating enzyme, which is a sulfatase. Sulfatases are enzymes essential for degradation and remodelling of sulfate esters, and formylglycine (FGly), the key catalytic in the active site, is unique to sulfatases. FGE is localized to the endoplasmic reticulum (ER) and interacts with and modifies the unfolded form of newly synthesized sulfatases. FGE is a single-domain monomer with a surprising paucity of secondary structure that adopts a unique fold which is stabilized by two Ca2+ ions. The effect of all mutations found in MSD patients is explained by the FGE structure, providing a molecular basis for MSD. A redox-active disulfide bond is present in the active site of FGE. An oxidized cysteine residue, possibly cysteine sulfenic acid, has been detected that may allow formulation of a structure-based mechanism for FGly formation from cysteine residues in all sulfatases. In Mycobacteria and Treponema denticola this enzyme functions as an iron(II)-dependent oxidoreductase.


Pssm-ID: 397722 [Multi-domain]  Cd Length: 259  Bit Score: 210.82  E-value: 2.12e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835622582  66 QMAFISTGVFTMGTDEPaIPQDGEAPSRRVHIRHFYMDRYEVSNTEFEKFVTSTGYITEAerfgdsfvfegllsetvkrd 145
Cdd:pfam03781   4 DMVLIPGGSFEMGSAER-TGNDNEAPAHDVTVRPFAIDKYPVTNAQYAAFVEATGYTTEV-------------------- 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835622582 146 ihqavaAAPWWLPVKGANWKHPEGPGSEIHERMDHPVLHVSWRDAVEFCAWAGK------RLPTEAEWEYACRGGRENRL 219
Cdd:pfam03781  63 ------YPQWWAEVEGANWRHPSGGLSDIDDGADHPVTGVSWYDAVAYARWLGKrtgngyRLPTEAEWEYAARGGSKGRR 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835622582 220 FPWGNNLHPNGkhyaNIWQGT-FPSNDSGEDGYTG-TAPVTSFPPNGYGMYNMVGNVWEWTEDWWTVHHSAEETHNPTLF 297
Cdd:pfam03781 137 YPWGDELYPAG----NIWQGAdFPNEHAGADSFNGrTSPVGSFPPNALGLYDMAGNVWEWTSDWYKPHYSFAPYDELSRD 212


                  .
gi 1835622582 298 A 298
Cdd:pfam03781 213 N 213
YfmG COG1262
Formylglycine-generating enzyme, required for sulfatase activity, contains SUMF1/FGE domain ...
 56-295 7.76e-59

Formylglycine-generating enzyme, required for sulfatase activity, contains SUMF1/FGE domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440874 [Multi-domain]  Cd Length: 238  Bit Score: 188.29  E-value: 7.76e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835622582  56 AGRPAHGPLQQMAFISTGVFTMGTDEPAIPQDGEAPSRRVHIRHFYMDRYEVSNTEFEKFVtstgyiteaerfgdsfvfe 135
Cdd:COG1262     2 ESFAGNAVGLEMVLIPGGTFLMGSPEGEGAFDNERPRHRVTVSPFYIDKYEVTNAEYRAFV------------------- 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835622582 136 gllsetvkrdihqavaaapWWLPvkgANWKHpeGPGSEIHERMDHPVLHVSWRDAVEFCAWAGK------RLPTEAEWEY 209
Cdd:COG1262    63 -------------------GWTL---ADGRN--NPLYSDFGGPDHPVVHVSWYDAQAYCRWLGKktgkgyRLPTEAEWEY 118

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835622582 210 ACRGGrENRLFPWGNNLHPngkHYANIwqgtfpsndSGEDGYTGTAPVTSFPPNGYGMYNMVGNVWEWTEDWWTVHHSAE 289
Cdd:COG1262   119 AARGG-DGRPYPWGDDLPP---ELANY---------AGNDGRGSTAPVGSFPPNPFGLYDMAGNVWEWTADWYDPPYPGA 185


                  ....*.
gi 1835622582 290 ETHNPT 295
Cdd:COG1262   186 PADGPV 191
GldK_short TIGR03529
gliding motility-associated lipoprotein GldK; Members of this protein family are exclusive to ...
 67-280 1.05e-30

gliding motility-associated lipoprotein GldK; Members of this protein family are exclusive to the Bacteroidetes phylum (previously Cytophaga-Flavobacteria-Bacteroides). GldK is a lipoprotein linked to a type of rapid surface gliding motility found in certain Bacteroidetes, such as Flavobacterium johnsoniae. Knockouts of GldK abolish the gliding phenotype. GldK is homologous to GldJ. This model represents a GldK homolog in Cytophaga hutchinsonii and several other species that has a different, shorter architecture than that found in Flavobacterium johnsoniae and related species (represented by (TIGR03525). Gliding motility appears closely linked to chitin utilization in the model species Flavobacterium johnsoniae. Bacteroidetes with members of this protein family appear to have all of the genes associated with gliding motility.


Pssm-ID: 274632 [Multi-domain]  Cd Length: 344  Bit Score: 117.72  E-value: 1.05e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835622582  67 MAFISTGVFTMGTDEPAIPQDGEAPSRRVHIRHFYMDRYEVSNTEFEKF--VTSTGYITEAERFGDSFVFEGLLSETVK- 143
Cdd:TIGR03529  54 MVVIPAGTFHMGQADEDVPATQINLNKQITISEFFMDKTEVTNNKYRQFleVVLEGQLATGTPLPPEYDMEELYPDTTVw 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835622582 144 -RDIHQAVAAapwwlPVKGANWKHPEGPgseihermDHPVLHVSWRDAVEFCAWAGK-----------------RLPTEA 205
Cdd:TIGR03529 134 sTSFSHHMGD-----PLMEYYFDHPAFD--------NYPVVGVDWNAAKQFCEWRTYhmnayrneesqydmprfRLPSEA 200

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1835622582 206 EWEYACRGGRENRLFPWGNNLHPN--GKHYANIWQGtfpSNDSGEDGYTGTAPVTSFPPNGYGMYNMVGNVWEWTED 280
Cdd:TIGR03529 201 EWEYAARGGRDMAKYPWGGPYLRNkrGCMLANFKPG---RGNYYDDGFPYTAPVAVYFPNDFGLYDMAGNVAEWVLD 274
SenA NF041186
selenoneine synthase SenA; Selenoneine is the selenium analog of ergothioneine, a ...
 56-226 1.37e-15

selenoneine synthase SenA; Selenoneine is the selenium analog of ergothioneine, a sulfur-containing derivative of a hercynine, which derives from histidine by trimethylation of its amino group. SenA, a homolog of ergothioneine biosynthesis protein EgtB, completes selenoneine biosynthesis in a pathway that also requires a SelD protein to prepare selenophosphate, EgtD to prepare hercynine, and the selenosugar-producing glycosyltransferase SenB (TIGR04348). SenA catalyzes selenium-carbon bond formation between hercynine and selenosugar to produce selenoneine. Other enzymes that create carbon-selenium bonds include SelA, involved in selenocysteine biosynthesis, SelU, involved in selenouridine biosynthesis, and SbtM, a radical SAM enzyme involved in post-translational modification of the RiPP precursor SbtA (see PMID:34730336).


Pssm-ID: 469092 [Multi-domain]  Cd Length: 384  Bit Score: 75.99  E-value: 1.37e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835622582  56 AGRPAHGPLQQMAFISTGVFTMGTD-EPAIPQDGEAPSRRVHIRHFYMDRYEVSNTEFEKFVTSTGYITEAerfgdsfvf 134
Cdd:NF041186  159 AAAPAPAPAAGDLAVPGGTFRLGSDpGPGFAFDNEKWAHPVEVAPFEIDAAPVTNAEFLAFVEAGGYRDPR--------- 229

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835622582 135 egLLSETVKRDIHQAVAAAP-WWLPVKGANWkhpegpgseiHER---------MDHPVLHVSWRDAVEFCAWAGKRLPTE 204
Cdd:NF041186  230 --LWSAAGWAWLAAQGLAAPrYWRRGADGAW----------QERrfgrwqpldPDAPVVHVSAHEAEAYCRWAGRRLPTE 297

                         170       180
                  ....*....|....*....|..
gi 1835622582 205 AEWEYACRGGREnrlFPWGNNL 226
Cdd:NF041186  298 AEWEYAAAGAPG---FPWGDSV 316
 
Name Accession Description Interval E-value
FGE-sulfatase pfam03781
Sulfatase-modifying factor enzyme 1; This domain is found in eukaryotic proteins required for ...
 66-298 2.12e-67

Sulfatase-modifying factor enzyme 1; This domain is found in eukaryotic proteins required for post-translational sulfatase modification (SUMF1). These proteins are associated with the rare disorder multiple sulfatase deficiency (MSD). The protein product of the SUMF1 gene is FGE, formylglycine (FGly),-generating enzyme, which is a sulfatase. Sulfatases are enzymes essential for degradation and remodelling of sulfate esters, and formylglycine (FGly), the key catalytic in the active site, is unique to sulfatases. FGE is localized to the endoplasmic reticulum (ER) and interacts with and modifies the unfolded form of newly synthesized sulfatases. FGE is a single-domain monomer with a surprising paucity of secondary structure that adopts a unique fold which is stabilized by two Ca2+ ions. The effect of all mutations found in MSD patients is explained by the FGE structure, providing a molecular basis for MSD. A redox-active disulfide bond is present in the active site of FGE. An oxidized cysteine residue, possibly cysteine sulfenic acid, has been detected that may allow formulation of a structure-based mechanism for FGly formation from cysteine residues in all sulfatases. In Mycobacteria and Treponema denticola this enzyme functions as an iron(II)-dependent oxidoreductase.


Pssm-ID: 397722 [Multi-domain]  Cd Length: 259  Bit Score: 210.82  E-value: 2.12e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835622582  66 QMAFISTGVFTMGTDEPaIPQDGEAPSRRVHIRHFYMDRYEVSNTEFEKFVTSTGYITEAerfgdsfvfegllsetvkrd 145
Cdd:pfam03781   4 DMVLIPGGSFEMGSAER-TGNDNEAPAHDVTVRPFAIDKYPVTNAQYAAFVEATGYTTEV-------------------- 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835622582 146 ihqavaAAPWWLPVKGANWKHPEGPGSEIHERMDHPVLHVSWRDAVEFCAWAGK------RLPTEAEWEYACRGGRENRL 219
Cdd:pfam03781  63 ------YPQWWAEVEGANWRHPSGGLSDIDDGADHPVTGVSWYDAVAYARWLGKrtgngyRLPTEAEWEYAARGGSKGRR 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835622582 220 FPWGNNLHPNGkhyaNIWQGT-FPSNDSGEDGYTG-TAPVTSFPPNGYGMYNMVGNVWEWTEDWWTVHHSAEETHNPTLF 297
Cdd:pfam03781 137 YPWGDELYPAG----NIWQGAdFPNEHAGADSFNGrTSPVGSFPPNALGLYDMAGNVWEWTSDWYKPHYSFAPYDELSRD 212


                  .
gi 1835622582 298 A 298
Cdd:pfam03781 213 N 213
YfmG COG1262
Formylglycine-generating enzyme, required for sulfatase activity, contains SUMF1/FGE domain ...
 56-295 7.76e-59

Formylglycine-generating enzyme, required for sulfatase activity, contains SUMF1/FGE domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440874 [Multi-domain]  Cd Length: 238  Bit Score: 188.29  E-value: 7.76e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835622582  56 AGRPAHGPLQQMAFISTGVFTMGTDEPAIPQDGEAPSRRVHIRHFYMDRYEVSNTEFEKFVtstgyiteaerfgdsfvfe 135
Cdd:COG1262     2 ESFAGNAVGLEMVLIPGGTFLMGSPEGEGAFDNERPRHRVTVSPFYIDKYEVTNAEYRAFV------------------- 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835622582 136 gllsetvkrdihqavaaapWWLPvkgANWKHpeGPGSEIHERMDHPVLHVSWRDAVEFCAWAGK------RLPTEAEWEY 209
Cdd:COG1262    63 -------------------GWTL---ADGRN--NPLYSDFGGPDHPVVHVSWYDAQAYCRWLGKktgkgyRLPTEAEWEY 118

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835622582 210 ACRGGrENRLFPWGNNLHPngkHYANIwqgtfpsndSGEDGYTGTAPVTSFPPNGYGMYNMVGNVWEWTEDWWTVHHSAE 289
Cdd:COG1262   119 AARGG-DGRPYPWGDDLPP---ELANY---------AGNDGRGSTAPVGSFPPNPFGLYDMAGNVWEWTADWYDPPYPGA 185


                  ....*.
gi 1835622582 290 ETHNPT 295
Cdd:COG1262   186 PADGPV 191
GldK_short TIGR03529
gliding motility-associated lipoprotein GldK; Members of this protein family are exclusive to ...
 67-280 1.05e-30

gliding motility-associated lipoprotein GldK; Members of this protein family are exclusive to the Bacteroidetes phylum (previously Cytophaga-Flavobacteria-Bacteroides). GldK is a lipoprotein linked to a type of rapid surface gliding motility found in certain Bacteroidetes, such as Flavobacterium johnsoniae. Knockouts of GldK abolish the gliding phenotype. GldK is homologous to GldJ. This model represents a GldK homolog in Cytophaga hutchinsonii and several other species that has a different, shorter architecture than that found in Flavobacterium johnsoniae and related species (represented by (TIGR03525). Gliding motility appears closely linked to chitin utilization in the model species Flavobacterium johnsoniae. Bacteroidetes with members of this protein family appear to have all of the genes associated with gliding motility.


Pssm-ID: 274632 [Multi-domain]  Cd Length: 344  Bit Score: 117.72  E-value: 1.05e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835622582  67 MAFISTGVFTMGTDEPAIPQDGEAPSRRVHIRHFYMDRYEVSNTEFEKF--VTSTGYITEAERFGDSFVFEGLLSETVK- 143
Cdd:TIGR03529  54 MVVIPAGTFHMGQADEDVPATQINLNKQITISEFFMDKTEVTNNKYRQFleVVLEGQLATGTPLPPEYDMEELYPDTTVw 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835622582 144 -RDIHQAVAAapwwlPVKGANWKHPEGPgseihermDHPVLHVSWRDAVEFCAWAGK-----------------RLPTEA 205
Cdd:TIGR03529 134 sTSFSHHMGD-----PLMEYYFDHPAFD--------NYPVVGVDWNAAKQFCEWRTYhmnayrneesqydmprfRLPSEA 200

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1835622582 206 EWEYACRGGRENRLFPWGNNLHPN--GKHYANIWQGtfpSNDSGEDGYTGTAPVTSFPPNGYGMYNMVGNVWEWTED 280
Cdd:TIGR03529 201 EWEYAARGGRDMAKYPWGGPYLRNkrGCMLANFKPG---RGNYYDDGFPYTAPVAVYFPNDFGLYDMAGNVAEWVLD 274
egtB_TIGR03440 TIGR03440
ergothioneine biosynthesis protein EgtB; Members of this family include EgtB, and enzyme of ...
 38-283 4.22e-25

ergothioneine biosynthesis protein EgtB; Members of this family include EgtB, and enzyme of the ergothioneine biosynthesis, as found in numerous Actinobacteria. Characterized homologs to this family include a formylglycine-generating enzyme that serves as a maturase for an aerobic sulfatase (cf. the radical SAM enzymes that serve as anaerobic sulfatase maturases). [Biosynthesis of cofactors, prosthetic groups, and carriers, Glutathione and analogs]


Pssm-ID: 274581 [Multi-domain]  Cd Length: 406  Bit Score: 103.56  E-value: 4.22e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835622582  38 SGNPLAEnlrfRYSREANAGRPAhGPLQQMAFIStGVFTMGTDEPAIPQDGEAPSRRVHIRHFYMDRYEVSNTEFEKFVT 117
Cdd:TIGR03440 147 SQNPLRP----AYQPPVPAPASA-PPLRWVAFPG-GEFEIGSDADGFAFDNERPRHRVLVPPFEIDARPVTNGEYLEFIE 220

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835622582 118 STGYITEAerfgdsfvfegllsetvkrdihqavaaapWWLP-----VKGANWKHPEG--PGSEIHERM----------DH 180
Cdd:TIGR03440 221 DGGYRRPE-----------------------------LWLSdgwawVQAEGWQAPLYwrRDDGTWWVFtlgglrpldpDA 271

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835622582 181 PVLHVSWRDAVEFCAWAGKRLPTEAEWEYACRGGRENRLFPWGNNLHPNGkhyaniwqgtfpsndsgedgytgtapvtSF 260
Cdd:TIGR03440 272 PVCHVSYYEADAYARWAGARLPTEAEWEKAARWGDAPPNFAEANLGAPVG----------------------------AY 323

                         250       260
                  ....*....|....*....|...
gi 1835622582 261 PPNGYGMYNMVGNVWEWTEDWWT 283
Cdd:TIGR03440 324 PAGAQGLGQLFGDVWEWTASPYE 346
GldK TIGR03525
gliding motility-associated lipoprotein GldK; Members of this protein family are exclusive to ...
 179-278 3.56e-22

gliding motility-associated lipoprotein GldK; Members of this protein family are exclusive to the Bacteroidetes phylum (previously Cytophaga-Flavobacteria-Bacteroides). GldK is a lipoprotein linked to a type of rapid surface gliding motility found in certain Bacteroidetes, such as Flavobacterium johnsoniae. Knockouts of GldK abolish the gliding phenotype. GldK is homologous to GldJ. There is a GldK homolog in Cytophaga hutchinsonii and several other species that has a different, shorter architecture and is represented by a separate model. Gliding motility appears closely linked to chitin utilization in the model species Flavobacterium johnsoniae. Bacteroidetes with members of this protein family appear to have all of the genes associated with gliding motility.


Pssm-ID: 274629  Cd Length: 450  Bit Score: 95.70  E-value: 3.56e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835622582 179 DHPVLHVSWRDAVEFCAWAGK-----------------RLPTEAEWEYACRGGRENRLFPWGNNlhpngkhYANIWQGTF 241
Cdd:TIGR03525 263 DYPVVGVTWKQARAFCNWRTKykndfrkkkgpanvntfRLPTEAEWEYAARGGLEGATYPWGGP-------YTKNDRGCF 335

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1835622582 242 PSN------DSGEDGYTGTAPVTSFPPNGYGMYNMVGNVWEWT 278
Cdd:TIGR03525 336 MANfkpvrgDYAADEALYTVEAKSYEPNDYGLYNMAGNVSEWT 378
SenA NF041186
selenoneine synthase SenA; Selenoneine is the selenium analog of ergothioneine, a ...
 56-226 1.37e-15

selenoneine synthase SenA; Selenoneine is the selenium analog of ergothioneine, a sulfur-containing derivative of a hercynine, which derives from histidine by trimethylation of its amino group. SenA, a homolog of ergothioneine biosynthesis protein EgtB, completes selenoneine biosynthesis in a pathway that also requires a SelD protein to prepare selenophosphate, EgtD to prepare hercynine, and the selenosugar-producing glycosyltransferase SenB (TIGR04348). SenA catalyzes selenium-carbon bond formation between hercynine and selenosugar to produce selenoneine. Other enzymes that create carbon-selenium bonds include SelA, involved in selenocysteine biosynthesis, SelU, involved in selenouridine biosynthesis, and SbtM, a radical SAM enzyme involved in post-translational modification of the RiPP precursor SbtA (see PMID:34730336).


Pssm-ID: 469092 [Multi-domain]  Cd Length: 384  Bit Score: 75.99  E-value: 1.37e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835622582  56 AGRPAHGPLQQMAFISTGVFTMGTD-EPAIPQDGEAPSRRVHIRHFYMDRYEVSNTEFEKFVTSTGYITEAerfgdsfvf 134
Cdd:NF041186  159 AAAPAPAPAAGDLAVPGGTFRLGSDpGPGFAFDNEKWAHPVEVAPFEIDAAPVTNAEFLAFVEAGGYRDPR--------- 229

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835622582 135 egLLSETVKRDIHQAVAAAP-WWLPVKGANWkhpegpgseiHER---------MDHPVLHVSWRDAVEFCAWAGKRLPTE 204
Cdd:NF041186  230 --LWSAAGWAWLAAQGLAAPrYWRRGADGAW----------QERrfgrwqpldPDAPVVHVSAHEAEAYCRWAGRRLPTE 297

                         170       180
                  ....*....|....*....|..
gi 1835622582 205 AEWEYACRGGREnrlFPWGNNL 226
Cdd:NF041186  298 AEWEYAAAGAPG---FPWGDSV 316
 
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